data_9D84
# 
_entry.id   9D84 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9D84         pdb_00009d84 10.2210/pdb9d84/pdb 
WWPDB D_1000287478 ?            ?                   
EMDB  EMD-46628    ?            ?                   
# 
_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       2025-01-15 
# 
_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             ? 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9D84 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-18 
_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_database_related.db_name        EMDB 
_pdbx_database_related.details        'Shigella flexneri bacteriophage B2 Gp48 and Gp49' 
_pdbx_database_related.db_id          EMD-46628 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              kparent@msu.edu 
_pdbx_contact_author.name_first         Kristin 
_pdbx_contact_author.name_last          Parent 
_pdbx_contact_author.name_mi            N. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6095-0628 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Subramanian, S.'        1 0000-0002-8684-6984 
'Bergland Drarvik, S.M.' 2 0000-0003-2248-2293 
'Parent, K.N.'           3 0000-0002-6095-0628 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                eadt0022 
_citation.page_last                 eadt0022 
_citation.title                     
'Moo19 and B2: Structures of Schitoviridae podophages with T = 9 geometry and tailspikes with esterase activity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adt0022 
_citation.pdbx_database_id_PubMed   39693418 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Subramanian, S.'        1 0000-0002-8684-6984 
primary 'Bergland Drarvik, S.M.' 2 ?                   
primary 'Tinney, K.R.'           3 ?                   
primary 'Doore, S.M.'            4 0000-0002-7672-2355 
primary 'Parent, K.N.'           5 0000-0002-6095-0628 
# 
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 Gp48 83297.094 1 ? ? ? ? 
2 polymer man Gp49 44471.602 1 ? ? ? ? 
# 
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 
;MNQLFSQGGKGSAGILTNKQAVARHFGVKQSEVVYFSVGVDISGYKVIYDKTTQRAYSLPIGIPAGTTAISLSTAAVLVH
SQGSVDLGAVAVLRKEYVTIPGDFTSGATIQVKNEILTHSNGAQYRWAGAVPKVVPAGSTPASSGGISASAWIEVTGEEL
RDELATTGGASQIGTSDGKTVQQWIIANDSANYRARNIQKLAWVDKQVHSRGSIKVLFQGDSMTAGYDTTSTDRVPANNG
DWATHASMTYPQRFMAYLPEQSGCSVTGVYRAISGHTAIQSYNEPSWQSNPNCDVVILMLGLNDAGGVAGTTEDIYMEYM
EKLIRRFIDWGMGVVVQTCSTGGQGSGGVVANLWAKRMRMMADTYGCAHFNADEVQYYRHNGAVQSDGGHFNSMGYAIHG
QMLASMFMAGGLLPTYRPLTNEINTWCGRLDDSIGYCDATGNINLGRSDGAYTRTKVVGGMLANVASIATFSFYLDAEAA
HIFVHGSGAGPINVLVDAPSWWNNGAQDYYDFANNQSINFSNSPQAANNAIVDLSTTYSADRKFVGRILGRGWKTLTFFT
NLQGTGGDFYLNSLTVQPVPVGMSVQARNWARFDKGHRAVYSKKIPQAYNQATLPTATALVNFQVPMPQSMLPTTPSISG
DLGTNFYNCGHSVLKISNSSGDYLEVLLIKTTGGGYVFTGKILKTTYATGNQPTAITATAAHYSMKDLKVAGANGPNMPL
ETIRDIDMASYVTIGVGAGNGGLVLDINITWPSTPPTSYWNIELEAWDMFGNSEASI
;
;MNQLFSQGGKGSAGILTNKQAVARHFGVKQSEVVYFSVGVDISGYKVIYDKTTQRAYSLPIGIPAGTTAISLSTAAVLVH
SQGSVDLGAVAVLRKEYVTIPGDFTSGATIQVKNEILTHSNGAQYRWAGAVPKVVPAGSTPASSGGISASAWIEVTGEEL
RDELATTGGASQIGTSDGKTVQQWIIANDSANYRARNIQKLAWVDKQVHSRGSIKVLFQGDSMTAGYDTTSTDRVPANNG
DWATHASMTYPQRFMAYLPEQSGCSVTGVYRAISGHTAIQSYNEPSWQSNPNCDVVILMLGLNDAGGVAGTTEDIYMEYM
EKLIRRFIDWGMGVVVQTCSTGGQGSGGVVANLWAKRMRMMADTYGCAHFNADEVQYYRHNGAVQSDGGHFNSMGYAIHG
QMLASMFMAGGLLPTYRPLTNEINTWCGRLDDSIGYCDATGNINLGRSDGAYTRTKVVGGMLANVASIATFSFYLDAEAA
HIFVHGSGAGPINVLVDAPSWWNNGAQDYYDFANNQSINFSNSPQAANNAIVDLSTTYSADRKFVGRILGRGWKTLTFFT
NLQGTGGDFYLNSLTVQPVPVGMSVQARNWARFDKGHRAVYSKKIPQAYNQATLPTATALVNFQVPMPQSMLPTTPSISG
DLGTNFYNCGHSVLKISNSSGDYLEVLLIKTTGGGYVFTGKILKTTYATGNQPTAITATAAHYSMKDLKVAGANGPNMPL
ETIRDIDMASYVTIGVGAGNGGLVLDINITWPSTPPTSYWNIELEAWDMFGNSEASI
;
A ? 
2 'polypeptide(L)' no no 
;MIRTTNTCCGNQAGMVEKFIGTAYDVVKTVYDNLGEIQFIYNFLNDYGVLITVDSVTELQELPTTAKYTRVYSSTPTGVR
IYTDYLYVEGDRTGVLPSDPTATGSWVVVGSSNSGAATGTGAYIPFVFNNGSAAGGETTIVVPDYTIGVPEIYVEGFRQQ
VGRGFTFNSVNLTVTLAQPLEQGDEVVLMLSGNPAVPDNPNIDSWTVINWIYNNGAAVGGEQVIVIPYTFQTVPAIFKNG
LRYQGGLSTQSYTVDQDNKRILLTEPLSTNDRLVVQLGGELVTLESPDRSLYEIARATNMKDSEVIKSDNTVETLNGKRI
LYDIVSQVYYWIPSSVPNNVYIQSVVNGQLTYLPGNIVVTLTPIVTLGLSGTTAQRPIGVLTGTQHFDTTLGKPIWFNGT
AWVDSTGAVV
;
;MIRTTNTCCGNQAGMVEKFIGTAYDVVKTVYDNLGEIQFIYNFLNDYGVLITVDSVTELQELPTTAKYTRVYSSTPTGVR
IYTDYLYVEGDRTGVLPSDPTATGSWVVVGSSNSGAATGTGAYIPFVFNNGSAAGGETTIVVPDYTIGVPEIYVEGFRQQ
VGRGFTFNSVNLTVTLAQPLEQGDEVVLMLSGNPAVPDNPNIDSWTVINWIYNNGAAVGGEQVIVIPYTFQTVPAIFKNG
LRYQGGLSTQSYTVDQDNKRILLTEPLSTNDRLVVQLGGELVTLESPDRSLYEIARATNMKDSEVIKSDNTVETLNGKRI
LYDIVSQVYYWIPSSVPNNVYIQSVVNGQLTYLPGNIVVTLTPIVTLGLSGTTAQRPIGVLTGTQHFDTTLGKPIWFNGT
AWVDSTGAVV
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   GLN n 
1 4   LEU n 
1 5   PHE n 
1 6   SER n 
1 7   GLN n 
1 8   GLY n 
1 9   GLY n 
1 10  LYS n 
1 11  GLY n 
1 12  SER n 
1 13  ALA n 
1 14  GLY n 
1 15  ILE n 
1 16  LEU n 
1 17  THR n 
1 18  ASN n 
1 19  LYS n 
1 20  GLN n 
1 21  ALA n 
1 22  VAL n 
1 23  ALA n 
1 24  ARG n 
1 25  HIS n 
1 26  PHE n 
1 27  GLY n 
1 28  VAL n 
1 29  LYS n 
1 30  GLN n 
1 31  SER n 
1 32  GLU n 
1 33  VAL n 
1 34  VAL n 
1 35  TYR n 
1 36  PHE n 
1 37  SER n 
1 38  VAL n 
1 39  GLY n 
1 40  VAL n 
1 41  ASP n 
1 42  ILE n 
1 43  SER n 
1 44  GLY n 
1 45  TYR n 
1 46  LYS n 
1 47  VAL n 
1 48  ILE n 
1 49  TYR n 
1 50  ASP n 
1 51  LYS n 
1 52  THR n 
1 53  THR n 
1 54  GLN n 
1 55  ARG n 
1 56  ALA n 
1 57  TYR n 
1 58  SER n 
1 59  LEU n 
1 60  PRO n 
1 61  ILE n 
1 62  GLY n 
1 63  ILE n 
1 64  PRO n 
1 65  ALA n 
1 66  GLY n 
1 67  THR n 
1 68  THR n 
1 69  ALA n 
1 70  ILE n 
1 71  SER n 
1 72  LEU n 
1 73  SER n 
1 74  THR n 
1 75  ALA n 
1 76  ALA n 
1 77  VAL n 
1 78  LEU n 
1 79  VAL n 
1 80  HIS n 
1 81  SER n 
1 82  GLN n 
1 83  GLY n 
1 84  SER n 
1 85  VAL n 
1 86  ASP n 
1 87  LEU n 
1 88  GLY n 
1 89  ALA n 
1 90  VAL n 
1 91  ALA n 
1 92  VAL n 
1 93  LEU n 
1 94  ARG n 
1 95  LYS n 
1 96  GLU n 
1 97  TYR n 
1 98  VAL n 
1 99  THR n 
1 100 ILE n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 PHE n 
1 105 THR n 
1 106 SER n 
1 107 GLY n 
1 108 ALA n 
1 109 THR n 
1 110 ILE n 
1 111 GLN n 
1 112 VAL n 
1 113 LYS n 
1 114 ASN n 
1 115 GLU n 
1 116 ILE n 
1 117 LEU n 
1 118 THR n 
1 119 HIS n 
1 120 SER n 
1 121 ASN n 
1 122 GLY n 
1 123 ALA n 
1 124 GLN n 
1 125 TYR n 
1 126 ARG n 
1 127 TRP n 
1 128 ALA n 
1 129 GLY n 
1 130 ALA n 
1 131 VAL n 
1 132 PRO n 
1 133 LYS n 
1 134 VAL n 
1 135 VAL n 
1 136 PRO n 
1 137 ALA n 
1 138 GLY n 
1 139 SER n 
1 140 THR n 
1 141 PRO n 
1 142 ALA n 
1 143 SER n 
1 144 SER n 
1 145 GLY n 
1 146 GLY n 
1 147 ILE n 
1 148 SER n 
1 149 ALA n 
1 150 SER n 
1 151 ALA n 
1 152 TRP n 
1 153 ILE n 
1 154 GLU n 
1 155 VAL n 
1 156 THR n 
1 157 GLY n 
1 158 GLU n 
1 159 GLU n 
1 160 LEU n 
1 161 ARG n 
1 162 ASP n 
1 163 GLU n 
1 164 LEU n 
1 165 ALA n 
1 166 THR n 
1 167 THR n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 SER n 
1 172 GLN n 
1 173 ILE n 
1 174 GLY n 
1 175 THR n 
1 176 SER n 
1 177 ASP n 
1 178 GLY n 
1 179 LYS n 
1 180 THR n 
1 181 VAL n 
1 182 GLN n 
1 183 GLN n 
1 184 TRP n 
1 185 ILE n 
1 186 ILE n 
1 187 ALA n 
1 188 ASN n 
1 189 ASP n 
1 190 SER n 
1 191 ALA n 
1 192 ASN n 
1 193 TYR n 
1 194 ARG n 
1 195 ALA n 
1 196 ARG n 
1 197 ASN n 
1 198 ILE n 
1 199 GLN n 
1 200 LYS n 
1 201 LEU n 
1 202 ALA n 
1 203 TRP n 
1 204 VAL n 
1 205 ASP n 
1 206 LYS n 
1 207 GLN n 
1 208 VAL n 
1 209 HIS n 
1 210 SER n 
1 211 ARG n 
1 212 GLY n 
1 213 SER n 
1 214 ILE n 
1 215 LYS n 
1 216 VAL n 
1 217 LEU n 
1 218 PHE n 
1 219 GLN n 
1 220 GLY n 
1 221 ASP n 
1 222 SER n 
1 223 MET n 
1 224 THR n 
1 225 ALA n 
1 226 GLY n 
1 227 TYR n 
1 228 ASP n 
1 229 THR n 
1 230 THR n 
1 231 SER n 
1 232 THR n 
1 233 ASP n 
1 234 ARG n 
1 235 VAL n 
1 236 PRO n 
1 237 ALA n 
1 238 ASN n 
1 239 ASN n 
1 240 GLY n 
1 241 ASP n 
1 242 TRP n 
1 243 ALA n 
1 244 THR n 
1 245 HIS n 
1 246 ALA n 
1 247 SER n 
1 248 MET n 
1 249 THR n 
1 250 TYR n 
1 251 PRO n 
1 252 GLN n 
1 253 ARG n 
1 254 PHE n 
1 255 MET n 
1 256 ALA n 
1 257 TYR n 
1 258 LEU n 
1 259 PRO n 
1 260 GLU n 
1 261 GLN n 
1 262 SER n 
1 263 GLY n 
1 264 CYS n 
1 265 SER n 
1 266 VAL n 
1 267 THR n 
1 268 GLY n 
1 269 VAL n 
1 270 TYR n 
1 271 ARG n 
1 272 ALA n 
1 273 ILE n 
1 274 SER n 
1 275 GLY n 
1 276 HIS n 
1 277 THR n 
1 278 ALA n 
1 279 ILE n 
1 280 GLN n 
1 281 SER n 
1 282 TYR n 
1 283 ASN n 
1 284 GLU n 
1 285 PRO n 
1 286 SER n 
1 287 TRP n 
1 288 GLN n 
1 289 SER n 
1 290 ASN n 
1 291 PRO n 
1 292 ASN n 
1 293 CYS n 
1 294 ASP n 
1 295 VAL n 
1 296 VAL n 
1 297 ILE n 
1 298 LEU n 
1 299 MET n 
1 300 LEU n 
1 301 GLY n 
1 302 LEU n 
1 303 ASN n 
1 304 ASP n 
1 305 ALA n 
1 306 GLY n 
1 307 GLY n 
1 308 VAL n 
1 309 ALA n 
1 310 GLY n 
1 311 THR n 
1 312 THR n 
1 313 GLU n 
1 314 ASP n 
1 315 ILE n 
1 316 TYR n 
1 317 MET n 
1 318 GLU n 
1 319 TYR n 
1 320 MET n 
1 321 GLU n 
1 322 LYS n 
1 323 LEU n 
1 324 ILE n 
1 325 ARG n 
1 326 ARG n 
1 327 PHE n 
1 328 ILE n 
1 329 ASP n 
1 330 TRP n 
1 331 GLY n 
1 332 MET n 
1 333 GLY n 
1 334 VAL n 
1 335 VAL n 
1 336 VAL n 
1 337 GLN n 
1 338 THR n 
1 339 CYS n 
1 340 SER n 
1 341 THR n 
1 342 GLY n 
1 343 GLY n 
1 344 GLN n 
1 345 GLY n 
1 346 SER n 
1 347 GLY n 
1 348 GLY n 
1 349 VAL n 
1 350 VAL n 
1 351 ALA n 
1 352 ASN n 
1 353 LEU n 
1 354 TRP n 
1 355 ALA n 
1 356 LYS n 
1 357 ARG n 
1 358 MET n 
1 359 ARG n 
1 360 MET n 
1 361 MET n 
1 362 ALA n 
1 363 ASP n 
1 364 THR n 
1 365 TYR n 
1 366 GLY n 
1 367 CYS n 
1 368 ALA n 
1 369 HIS n 
1 370 PHE n 
1 371 ASN n 
1 372 ALA n 
1 373 ASP n 
1 374 GLU n 
1 375 VAL n 
1 376 GLN n 
1 377 TYR n 
1 378 TYR n 
1 379 ARG n 
1 380 HIS n 
1 381 ASN n 
1 382 GLY n 
1 383 ALA n 
1 384 VAL n 
1 385 GLN n 
1 386 SER n 
1 387 ASP n 
1 388 GLY n 
1 389 GLY n 
1 390 HIS n 
1 391 PHE n 
1 392 ASN n 
1 393 SER n 
1 394 MET n 
1 395 GLY n 
1 396 TYR n 
1 397 ALA n 
1 398 ILE n 
1 399 HIS n 
1 400 GLY n 
1 401 GLN n 
1 402 MET n 
1 403 LEU n 
1 404 ALA n 
1 405 SER n 
1 406 MET n 
1 407 PHE n 
1 408 MET n 
1 409 ALA n 
1 410 GLY n 
1 411 GLY n 
1 412 LEU n 
1 413 LEU n 
1 414 PRO n 
1 415 THR n 
1 416 TYR n 
1 417 ARG n 
1 418 PRO n 
1 419 LEU n 
1 420 THR n 
1 421 ASN n 
1 422 GLU n 
1 423 ILE n 
1 424 ASN n 
1 425 THR n 
1 426 TRP n 
1 427 CYS n 
1 428 GLY n 
1 429 ARG n 
1 430 LEU n 
1 431 ASP n 
1 432 ASP n 
1 433 SER n 
1 434 ILE n 
1 435 GLY n 
1 436 TYR n 
1 437 CYS n 
1 438 ASP n 
1 439 ALA n 
1 440 THR n 
1 441 GLY n 
1 442 ASN n 
1 443 ILE n 
1 444 ASN n 
1 445 LEU n 
1 446 GLY n 
1 447 ARG n 
1 448 SER n 
1 449 ASP n 
1 450 GLY n 
1 451 ALA n 
1 452 TYR n 
1 453 THR n 
1 454 ARG n 
1 455 THR n 
1 456 LYS n 
1 457 VAL n 
1 458 VAL n 
1 459 GLY n 
1 460 GLY n 
1 461 MET n 
1 462 LEU n 
1 463 ALA n 
1 464 ASN n 
1 465 VAL n 
1 466 ALA n 
1 467 SER n 
1 468 ILE n 
1 469 ALA n 
1 470 THR n 
1 471 PHE n 
1 472 SER n 
1 473 PHE n 
1 474 TYR n 
1 475 LEU n 
1 476 ASP n 
1 477 ALA n 
1 478 GLU n 
1 479 ALA n 
1 480 ALA n 
1 481 HIS n 
1 482 ILE n 
1 483 PHE n 
1 484 VAL n 
1 485 HIS n 
1 486 GLY n 
1 487 SER n 
1 488 GLY n 
1 489 ALA n 
1 490 GLY n 
1 491 PRO n 
1 492 ILE n 
1 493 ASN n 
1 494 VAL n 
1 495 LEU n 
1 496 VAL n 
1 497 ASP n 
1 498 ALA n 
1 499 PRO n 
1 500 SER n 
1 501 TRP n 
1 502 TRP n 
1 503 ASN n 
1 504 ASN n 
1 505 GLY n 
1 506 ALA n 
1 507 GLN n 
1 508 ASP n 
1 509 TYR n 
1 510 TYR n 
1 511 ASP n 
1 512 PHE n 
1 513 ALA n 
1 514 ASN n 
1 515 ASN n 
1 516 GLN n 
1 517 SER n 
1 518 ILE n 
1 519 ASN n 
1 520 PHE n 
1 521 SER n 
1 522 ASN n 
1 523 SER n 
1 524 PRO n 
1 525 GLN n 
1 526 ALA n 
1 527 ALA n 
1 528 ASN n 
1 529 ASN n 
1 530 ALA n 
1 531 ILE n 
1 532 VAL n 
1 533 ASP n 
1 534 LEU n 
1 535 SER n 
1 536 THR n 
1 537 THR n 
1 538 TYR n 
1 539 SER n 
1 540 ALA n 
1 541 ASP n 
1 542 ARG n 
1 543 LYS n 
1 544 PHE n 
1 545 VAL n 
1 546 GLY n 
1 547 ARG n 
1 548 ILE n 
1 549 LEU n 
1 550 GLY n 
1 551 ARG n 
1 552 GLY n 
1 553 TRP n 
1 554 LYS n 
1 555 THR n 
1 556 LEU n 
1 557 THR n 
1 558 PHE n 
1 559 PHE n 
1 560 THR n 
1 561 ASN n 
1 562 LEU n 
1 563 GLN n 
1 564 GLY n 
1 565 THR n 
1 566 GLY n 
1 567 GLY n 
1 568 ASP n 
1 569 PHE n 
1 570 TYR n 
1 571 LEU n 
1 572 ASN n 
1 573 SER n 
1 574 LEU n 
1 575 THR n 
1 576 VAL n 
1 577 GLN n 
1 578 PRO n 
1 579 VAL n 
1 580 PRO n 
1 581 VAL n 
1 582 GLY n 
1 583 MET n 
1 584 SER n 
1 585 VAL n 
1 586 GLN n 
1 587 ALA n 
1 588 ARG n 
1 589 ASN n 
1 590 TRP n 
1 591 ALA n 
1 592 ARG n 
1 593 PHE n 
1 594 ASP n 
1 595 LYS n 
1 596 GLY n 
1 597 HIS n 
1 598 ARG n 
1 599 ALA n 
1 600 VAL n 
1 601 TYR n 
1 602 SER n 
1 603 LYS n 
1 604 LYS n 
1 605 ILE n 
1 606 PRO n 
1 607 GLN n 
1 608 ALA n 
1 609 TYR n 
1 610 ASN n 
1 611 GLN n 
1 612 ALA n 
1 613 THR n 
1 614 LEU n 
1 615 PRO n 
1 616 THR n 
1 617 ALA n 
1 618 THR n 
1 619 ALA n 
1 620 LEU n 
1 621 VAL n 
1 622 ASN n 
1 623 PHE n 
1 624 GLN n 
1 625 VAL n 
1 626 PRO n 
1 627 MET n 
1 628 PRO n 
1 629 GLN n 
1 630 SER n 
1 631 MET n 
1 632 LEU n 
1 633 PRO n 
1 634 THR n 
1 635 THR n 
1 636 PRO n 
1 637 SER n 
1 638 ILE n 
1 639 SER n 
1 640 GLY n 
1 641 ASP n 
1 642 LEU n 
1 643 GLY n 
1 644 THR n 
1 645 ASN n 
1 646 PHE n 
1 647 TYR n 
1 648 ASN n 
1 649 CYS n 
1 650 GLY n 
1 651 HIS n 
1 652 SER n 
1 653 VAL n 
1 654 LEU n 
1 655 LYS n 
1 656 ILE n 
1 657 SER n 
1 658 ASN n 
1 659 SER n 
1 660 SER n 
1 661 GLY n 
1 662 ASP n 
1 663 TYR n 
1 664 LEU n 
1 665 GLU n 
1 666 VAL n 
1 667 LEU n 
1 668 LEU n 
1 669 ILE n 
1 670 LYS n 
1 671 THR n 
1 672 THR n 
1 673 GLY n 
1 674 GLY n 
1 675 GLY n 
1 676 TYR n 
1 677 VAL n 
1 678 PHE n 
1 679 THR n 
1 680 GLY n 
1 681 LYS n 
1 682 ILE n 
1 683 LEU n 
1 684 LYS n 
1 685 THR n 
1 686 THR n 
1 687 TYR n 
1 688 ALA n 
1 689 THR n 
1 690 GLY n 
1 691 ASN n 
1 692 GLN n 
1 693 PRO n 
1 694 THR n 
1 695 ALA n 
1 696 ILE n 
1 697 THR n 
1 698 ALA n 
1 699 THR n 
1 700 ALA n 
1 701 ALA n 
1 702 HIS n 
1 703 TYR n 
1 704 SER n 
1 705 MET n 
1 706 LYS n 
1 707 ASP n 
1 708 LEU n 
1 709 LYS n 
1 710 VAL n 
1 711 ALA n 
1 712 GLY n 
1 713 ALA n 
1 714 ASN n 
1 715 GLY n 
1 716 PRO n 
1 717 ASN n 
1 718 MET n 
1 719 PRO n 
1 720 LEU n 
1 721 GLU n 
1 722 THR n 
1 723 ILE n 
1 724 ARG n 
1 725 ASP n 
1 726 ILE n 
1 727 ASP n 
1 728 MET n 
1 729 ALA n 
1 730 SER n 
1 731 TYR n 
1 732 VAL n 
1 733 THR n 
1 734 ILE n 
1 735 GLY n 
1 736 VAL n 
1 737 GLY n 
1 738 ALA n 
1 739 GLY n 
1 740 ASN n 
1 741 GLY n 
1 742 GLY n 
1 743 LEU n 
1 744 VAL n 
1 745 LEU n 
1 746 ASP n 
1 747 ILE n 
1 748 ASN n 
1 749 ILE n 
1 750 THR n 
1 751 TRP n 
1 752 PRO n 
1 753 SER n 
1 754 THR n 
1 755 PRO n 
1 756 PRO n 
1 757 THR n 
1 758 SER n 
1 759 TYR n 
1 760 TRP n 
1 761 ASN n 
1 762 ILE n 
1 763 GLU n 
1 764 LEU n 
1 765 GLU n 
1 766 ALA n 
1 767 TRP n 
1 768 ASP n 
1 769 MET n 
1 770 PHE n 
1 771 GLY n 
1 772 ASN n 
1 773 SER n 
1 774 GLU n 
1 775 ALA n 
1 776 SER n 
1 777 ILE n 
2 1   MET n 
2 2   ILE n 
2 3   ARG n 
2 4   THR n 
2 5   THR n 
2 6   ASN n 
2 7   THR n 
2 8   CYS n 
2 9   CYS n 
2 10  GLY n 
2 11  ASN n 
2 12  GLN n 
2 13  ALA n 
2 14  GLY n 
2 15  MET n 
2 16  VAL n 
2 17  GLU n 
2 18  LYS n 
2 19  PHE n 
2 20  ILE n 
2 21  GLY n 
2 22  THR n 
2 23  ALA n 
2 24  TYR n 
2 25  ASP n 
2 26  VAL n 
2 27  VAL n 
2 28  LYS n 
2 29  THR n 
2 30  VAL n 
2 31  TYR n 
2 32  ASP n 
2 33  ASN n 
2 34  LEU n 
2 35  GLY n 
2 36  GLU n 
2 37  ILE n 
2 38  GLN n 
2 39  PHE n 
2 40  ILE n 
2 41  TYR n 
2 42  ASN n 
2 43  PHE n 
2 44  LEU n 
2 45  ASN n 
2 46  ASP n 
2 47  TYR n 
2 48  GLY n 
2 49  VAL n 
2 50  LEU n 
2 51  ILE n 
2 52  THR n 
2 53  VAL n 
2 54  ASP n 
2 55  SER n 
2 56  VAL n 
2 57  THR n 
2 58  GLU n 
2 59  LEU n 
2 60  GLN n 
2 61  GLU n 
2 62  LEU n 
2 63  PRO n 
2 64  THR n 
2 65  THR n 
2 66  ALA n 
2 67  LYS n 
2 68  TYR n 
2 69  THR n 
2 70  ARG n 
2 71  VAL n 
2 72  TYR n 
2 73  SER n 
2 74  SER n 
2 75  THR n 
2 76  PRO n 
2 77  THR n 
2 78  GLY n 
2 79  VAL n 
2 80  ARG n 
2 81  ILE n 
2 82  TYR n 
2 83  THR n 
2 84  ASP n 
2 85  TYR n 
2 86  LEU n 
2 87  TYR n 
2 88  VAL n 
2 89  GLU n 
2 90  GLY n 
2 91  ASP n 
2 92  ARG n 
2 93  THR n 
2 94  GLY n 
2 95  VAL n 
2 96  LEU n 
2 97  PRO n 
2 98  SER n 
2 99  ASP n 
2 100 PRO n 
2 101 THR n 
2 102 ALA n 
2 103 THR n 
2 104 GLY n 
2 105 SER n 
2 106 TRP n 
2 107 VAL n 
2 108 VAL n 
2 109 VAL n 
2 110 GLY n 
2 111 SER n 
2 112 SER n 
2 113 ASN n 
2 114 SER n 
2 115 GLY n 
2 116 ALA n 
2 117 ALA n 
2 118 THR n 
2 119 GLY n 
2 120 THR n 
2 121 GLY n 
2 122 ALA n 
2 123 TYR n 
2 124 ILE n 
2 125 PRO n 
2 126 PHE n 
2 127 VAL n 
2 128 PHE n 
2 129 ASN n 
2 130 ASN n 
2 131 GLY n 
2 132 SER n 
2 133 ALA n 
2 134 ALA n 
2 135 GLY n 
2 136 GLY n 
2 137 GLU n 
2 138 THR n 
2 139 THR n 
2 140 ILE n 
2 141 VAL n 
2 142 VAL n 
2 143 PRO n 
2 144 ASP n 
2 145 TYR n 
2 146 THR n 
2 147 ILE n 
2 148 GLY n 
2 149 VAL n 
2 150 PRO n 
2 151 GLU n 
2 152 ILE n 
2 153 TYR n 
2 154 VAL n 
2 155 GLU n 
2 156 GLY n 
2 157 PHE n 
2 158 ARG n 
2 159 GLN n 
2 160 GLN n 
2 161 VAL n 
2 162 GLY n 
2 163 ARG n 
2 164 GLY n 
2 165 PHE n 
2 166 THR n 
2 167 PHE n 
2 168 ASN n 
2 169 SER n 
2 170 VAL n 
2 171 ASN n 
2 172 LEU n 
2 173 THR n 
2 174 VAL n 
2 175 THR n 
2 176 LEU n 
2 177 ALA n 
2 178 GLN n 
2 179 PRO n 
2 180 LEU n 
2 181 GLU n 
2 182 GLN n 
2 183 GLY n 
2 184 ASP n 
2 185 GLU n 
2 186 VAL n 
2 187 VAL n 
2 188 LEU n 
2 189 MET n 
2 190 LEU n 
2 191 SER n 
2 192 GLY n 
2 193 ASN n 
2 194 PRO n 
2 195 ALA n 
2 196 VAL n 
2 197 PRO n 
2 198 ASP n 
2 199 ASN n 
2 200 PRO n 
2 201 ASN n 
2 202 ILE n 
2 203 ASP n 
2 204 SER n 
2 205 TRP n 
2 206 THR n 
2 207 VAL n 
2 208 ILE n 
2 209 ASN n 
2 210 TRP n 
2 211 ILE n 
2 212 TYR n 
2 213 ASN n 
2 214 ASN n 
2 215 GLY n 
2 216 ALA n 
2 217 ALA n 
2 218 VAL n 
2 219 GLY n 
2 220 GLY n 
2 221 GLU n 
2 222 GLN n 
2 223 VAL n 
2 224 ILE n 
2 225 VAL n 
2 226 ILE n 
2 227 PRO n 
2 228 TYR n 
2 229 THR n 
2 230 PHE n 
2 231 GLN n 
2 232 THR n 
2 233 VAL n 
2 234 PRO n 
2 235 ALA n 
2 236 ILE n 
2 237 PHE n 
2 238 LYS n 
2 239 ASN n 
2 240 GLY n 
2 241 LEU n 
2 242 ARG n 
2 243 TYR n 
2 244 GLN n 
2 245 GLY n 
2 246 GLY n 
2 247 LEU n 
2 248 SER n 
2 249 THR n 
2 250 GLN n 
2 251 SER n 
2 252 TYR n 
2 253 THR n 
2 254 VAL n 
2 255 ASP n 
2 256 GLN n 
2 257 ASP n 
2 258 ASN n 
2 259 LYS n 
2 260 ARG n 
2 261 ILE n 
2 262 LEU n 
2 263 LEU n 
2 264 THR n 
2 265 GLU n 
2 266 PRO n 
2 267 LEU n 
2 268 SER n 
2 269 THR n 
2 270 ASN n 
2 271 ASP n 
2 272 ARG n 
2 273 LEU n 
2 274 VAL n 
2 275 VAL n 
2 276 GLN n 
2 277 LEU n 
2 278 GLY n 
2 279 GLY n 
2 280 GLU n 
2 281 LEU n 
2 282 VAL n 
2 283 THR n 
2 284 LEU n 
2 285 GLU n 
2 286 SER n 
2 287 PRO n 
2 288 ASP n 
2 289 ARG n 
2 290 SER n 
2 291 LEU n 
2 292 TYR n 
2 293 GLU n 
2 294 ILE n 
2 295 ALA n 
2 296 ARG n 
2 297 ALA n 
2 298 THR n 
2 299 ASN n 
2 300 MET n 
2 301 LYS n 
2 302 ASP n 
2 303 SER n 
2 304 GLU n 
2 305 VAL n 
2 306 ILE n 
2 307 LYS n 
2 308 SER n 
2 309 ASP n 
2 310 ASN n 
2 311 THR n 
2 312 VAL n 
2 313 GLU n 
2 314 THR n 
2 315 LEU n 
2 316 ASN n 
2 317 GLY n 
2 318 LYS n 
2 319 ARG n 
2 320 ILE n 
2 321 LEU n 
2 322 TYR n 
2 323 ASP n 
2 324 ILE n 
2 325 VAL n 
2 326 SER n 
2 327 GLN n 
2 328 VAL n 
2 329 TYR n 
2 330 TYR n 
2 331 TRP n 
2 332 ILE n 
2 333 PRO n 
2 334 SER n 
2 335 SER n 
2 336 VAL n 
2 337 PRO n 
2 338 ASN n 
2 339 ASN n 
2 340 VAL n 
2 341 TYR n 
2 342 ILE n 
2 343 GLN n 
2 344 SER n 
2 345 VAL n 
2 346 VAL n 
2 347 ASN n 
2 348 GLY n 
2 349 GLN n 
2 350 LEU n 
2 351 THR n 
2 352 TYR n 
2 353 LEU n 
2 354 PRO n 
2 355 GLY n 
2 356 ASN n 
2 357 ILE n 
2 358 VAL n 
2 359 VAL n 
2 360 THR n 
2 361 LEU n 
2 362 THR n 
2 363 PRO n 
2 364 ILE n 
2 365 VAL n 
2 366 THR n 
2 367 LEU n 
2 368 GLY n 
2 369 LEU n 
2 370 SER n 
2 371 GLY n 
2 372 THR n 
2 373 THR n 
2 374 ALA n 
2 375 GLN n 
2 376 ARG n 
2 377 PRO n 
2 378 ILE n 
2 379 GLY n 
2 380 VAL n 
2 381 LEU n 
2 382 THR n 
2 383 GLY n 
2 384 THR n 
2 385 GLN n 
2 386 HIS n 
2 387 PHE n 
2 388 ASP n 
2 389 THR n 
2 390 THR n 
2 391 LEU n 
2 392 GLY n 
2 393 LYS n 
2 394 PRO n 
2 395 ILE n 
2 396 TRP n 
2 397 PHE n 
2 398 ASN n 
2 399 GLY n 
2 400 THR n 
2 401 ALA n 
2 402 TRP n 
2 403 VAL n 
2 404 ASP n 
2 405 SER n 
2 406 THR n 
2 407 GLY n 
2 408 ALA n 
2 409 VAL n 
2 410 VAL 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' 1 777 ? ? ? ? ? ? ? ? ? 'Shigella phage B2' 2968270 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 410 ? ? ? ? ? ? ? ? ? 'Shigella phage B2' 2968270 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  HIS 25  25  25  HIS HIS A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 TRP 127 127 127 TRP TRP A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 VAL 131 131 131 VAL ALA A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 TRP 152 152 152 TRP TRP A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 GLN 183 183 183 GLN GLN A . n 
A 1 184 TRP 184 184 184 TRP TRP A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 MET 223 223 223 MET MET A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 TRP 242 242 242 TRP TRP A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 THR 244 244 244 THR THR A . n 
A 1 245 HIS 245 245 245 HIS HIS A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 MET 248 248 248 MET MET A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 PRO 251 251 251 PRO PRO A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 GLN 261 261 261 GLN GLN A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 CYS 264 264 264 CYS CYS A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 HIS 276 276 276 HIS HIS A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 GLN 280 280 280 GLN GLN A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 TRP 287 287 287 TRP TRP A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 ASN 290 290 290 ASN ASN A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 ASN 292 292 292 ASN ASN A . n 
A 1 293 CYS 293 293 293 CYS CYS A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 ASN 303 303 303 ASN ASN A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 MET 317 317 317 MET MET A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 MET 320 320 320 MET MET A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ILE 324 324 324 ILE ILE A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 ARG 326 326 326 ARG ARG A . n 
A 1 327 PHE 327 327 327 PHE PHE A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 TRP 330 330 330 TRP TRP A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 MET 332 332 332 MET MET A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 GLN 337 337 337 GLN GLN A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 CYS 339 339 339 CYS CYS A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 THR 341 341 341 THR THR A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 ARG 357 357 357 ARG ARG A . n 
A 1 358 MET 358 358 358 MET MET A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 MET 360 360 360 MET MET A . n 
A 1 361 MET 361 361 361 MET MET A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 THR 364 364 364 THR THR A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 CYS 367 367 367 CYS CYS A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 HIS 369 369 369 HIS HIS A . n 
A 1 370 PHE 370 370 370 PHE PHE A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 ASP 373 373 373 ASP ASP A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 GLN 376 376 376 GLN GLN A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 TYR 378 378 378 TYR TYR A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 HIS 380 380 380 HIS HIS A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 VAL 384 384 384 VAL VAL A . n 
A 1 385 GLN 385 385 385 GLN GLN A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 ASP 387 387 387 ASP ASP A . n 
A 1 388 GLY 388 388 388 GLY GLY A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 HIS 390 390 390 HIS HIS A . n 
A 1 391 PHE 391 391 391 PHE PHE A . n 
A 1 392 ASN 392 392 392 ASN ASN A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 MET 394 394 394 MET MET A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 TYR 396 396 396 TYR TYR A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ILE 398 398 398 ILE ILE A . n 
A 1 399 HIS 399 399 399 HIS HIS A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 MET 402 402 402 MET MET A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 MET 406 406 406 MET MET A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 MET 408 408 408 MET MET A . n 
A 1 409 ALA 409 409 409 ALA ALA A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 THR 415 415 415 THR THR A . n 
A 1 416 TYR 416 416 416 TYR TYR A . n 
A 1 417 ARG 417 417 417 ARG ARG A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 THR 420 420 420 THR THR A . n 
A 1 421 ASN 421 421 421 ASN ASN A . n 
A 1 422 GLU 422 422 422 GLU GLU A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 ASN 424 424 424 ASN ASN A . n 
A 1 425 THR 425 425 425 THR THR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 CYS 427 427 427 CYS CYS A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 TYR 436 436 436 TYR TYR A . n 
A 1 437 CYS 437 437 437 CYS CYS A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 ILE 443 443 443 ILE ILE A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 ARG 447 447 447 ARG ARG A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ASP 449 449 449 ASP ASP A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 ALA 451 451 451 ALA ALA A . n 
A 1 452 TYR 452 452 452 TYR TYR A . n 
A 1 453 THR 453 453 453 THR THR A . n 
A 1 454 ARG 454 454 454 ARG ARG A . n 
A 1 455 THR 455 455 455 THR THR A . n 
A 1 456 LYS 456 456 456 LYS LYS A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 VAL 458 458 458 VAL VAL A . n 
A 1 459 GLY 459 459 459 GLY GLY A . n 
A 1 460 GLY 460 460 460 GLY GLY A . n 
A 1 461 MET 461 461 461 MET MET A . n 
A 1 462 LEU 462 462 462 LEU LEU A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 VAL 465 465 465 VAL VAL A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 SER 467 467 467 SER SER A . n 
A 1 468 ILE 468 468 468 ILE ILE A . n 
A 1 469 ALA 469 469 469 ALA ALA A . n 
A 1 470 THR 470 470 470 THR THR A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 SER 472 472 472 SER SER A . n 
A 1 473 PHE 473 473 473 PHE PHE A . n 
A 1 474 TYR 474 474 474 TYR TYR A . n 
A 1 475 LEU 475 475 475 LEU LEU A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 ALA 477 477 477 ALA ALA A . n 
A 1 478 GLU 478 478 478 GLU GLU A . n 
A 1 479 ALA 479 479 479 ALA ALA A . n 
A 1 480 ALA 480 480 480 ALA ALA A . n 
A 1 481 HIS 481 481 481 HIS HIS A . n 
A 1 482 ILE 482 482 482 ILE ILE A . n 
A 1 483 PHE 483 483 483 PHE PHE A . n 
A 1 484 VAL 484 484 484 VAL VAL A . n 
A 1 485 HIS 485 485 485 HIS HIS A . n 
A 1 486 GLY 486 486 486 GLY GLY A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 GLY 488 488 488 GLY GLY A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 GLY 490 490 490 GLY GLY A . n 
A 1 491 PRO 491 491 491 PRO PRO A . n 
A 1 492 ILE 492 492 492 ILE ILE A . n 
A 1 493 ASN 493 493 493 ASN ASN A . n 
A 1 494 VAL 494 494 494 VAL VAL A . n 
A 1 495 LEU 495 495 495 LEU LEU A . n 
A 1 496 VAL 496 496 496 VAL VAL A . n 
A 1 497 ASP 497 497 497 ASP ASP A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 PRO 499 499 499 PRO PRO A . n 
A 1 500 SER 500 500 500 SER SER A . n 
A 1 501 TRP 501 501 501 TRP TRP A . n 
A 1 502 TRP 502 502 502 TRP TRP A . n 
A 1 503 ASN 503 503 503 ASN ASN A . n 
A 1 504 ASN 504 504 504 ASN ASN A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 GLN 507 507 507 GLN GLN A . n 
A 1 508 ASP 508 508 508 ASP ALA A . n 
A 1 509 TYR 509 509 509 TYR TYR A . n 
A 1 510 TYR 510 510 510 TYR TYR A . n 
A 1 511 ASP 511 511 511 ASP ASP A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 ALA 513 513 513 ALA ALA A . n 
A 1 514 ASN 514 514 514 ASN ASN A . n 
A 1 515 ASN 515 515 515 ASN ASN A . n 
A 1 516 GLN 516 516 516 GLN GLN A . n 
A 1 517 SER 517 517 517 SER SER A . n 
A 1 518 ILE 518 518 518 ILE ILE A . n 
A 1 519 ASN 519 519 519 ASN ASN A . n 
A 1 520 PHE 520 520 520 PHE PHE A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 ASN 522 522 522 ASN ASN A . n 
A 1 523 SER 523 523 523 SER SER A . n 
A 1 524 PRO 524 524 524 PRO PRO A . n 
A 1 525 GLN 525 525 525 GLN GLN A . n 
A 1 526 ALA 526 526 526 ALA ALA A . n 
A 1 527 ALA 527 527 527 ALA ALA A . n 
A 1 528 ASN 528 528 528 ASN ASN A . n 
A 1 529 ASN 529 529 529 ASN ASN A . n 
A 1 530 ALA 530 530 530 ALA ALA A . n 
A 1 531 ILE 531 531 531 ILE ILE A . n 
A 1 532 VAL 532 532 532 VAL VAL A . n 
A 1 533 ASP 533 533 533 ASP ASP A . n 
A 1 534 LEU 534 534 534 LEU LEU A . n 
A 1 535 SER 535 535 535 SER SER A . n 
A 1 536 THR 536 536 536 THR THR A . n 
A 1 537 THR 537 537 537 THR THR A . n 
A 1 538 TYR 538 538 538 TYR TYR A . n 
A 1 539 SER 539 539 539 SER SER A . n 
A 1 540 ALA 540 540 540 ALA ALA A . n 
A 1 541 ASP 541 541 541 ASP ASP A . n 
A 1 542 ARG 542 542 542 ARG ARG A . n 
A 1 543 LYS 543 543 543 LYS LYS A . n 
A 1 544 PHE 544 544 544 PHE PHE A . n 
A 1 545 VAL 545 545 545 VAL VAL A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 ARG 547 547 547 ARG ARG A . n 
A 1 548 ILE 548 548 548 ILE ILE A . n 
A 1 549 LEU 549 549 549 LEU LEU A . n 
A 1 550 GLY 550 550 550 GLY GLY A . n 
A 1 551 ARG 551 551 551 ARG ARG A . n 
A 1 552 GLY 552 552 552 GLY GLY A . n 
A 1 553 TRP 553 553 553 TRP TRP A . n 
A 1 554 LYS 554 554 554 LYS LYS A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 LEU 556 556 556 LEU LEU A . n 
A 1 557 THR 557 557 557 THR THR A . n 
A 1 558 PHE 558 558 558 PHE PHE A . n 
A 1 559 PHE 559 559 559 PHE PHE A . n 
A 1 560 THR 560 560 560 THR THR A . n 
A 1 561 ASN 561 561 561 ASN ASN A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 GLN 563 563 563 GLN GLN A . n 
A 1 564 GLY 564 564 564 GLY GLY A . n 
A 1 565 THR 565 565 565 THR THR A . n 
A 1 566 GLY 566 566 566 GLY GLY A . n 
A 1 567 GLY 567 567 567 GLY GLY A . n 
A 1 568 ASP 568 568 568 ASP ASP A . n 
A 1 569 PHE 569 569 569 PHE PHE A . n 
A 1 570 TYR 570 570 570 TYR TYR A . n 
A 1 571 LEU 571 571 571 LEU LEU A . n 
A 1 572 ASN 572 572 572 ASN ASN A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 LEU 574 574 574 LEU LEU A . n 
A 1 575 THR 575 575 575 THR THR A . n 
A 1 576 VAL 576 576 576 VAL VAL A . n 
A 1 577 GLN 577 577 577 GLN GLN A . n 
A 1 578 PRO 578 578 578 PRO PRO A . n 
A 1 579 VAL 579 579 579 VAL VAL A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 VAL 581 581 581 VAL VAL A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 MET 583 583 583 MET MET A . n 
A 1 584 SER 584 584 584 SER SER A . n 
A 1 585 VAL 585 585 585 VAL VAL A . n 
A 1 586 GLN 586 586 586 GLN GLN A . n 
A 1 587 ALA 587 587 587 ALA ALA A . n 
A 1 588 ARG 588 588 588 ARG ARG A . n 
A 1 589 ASN 589 589 589 ASN ASN A . n 
A 1 590 TRP 590 590 590 TRP TRP A . n 
A 1 591 ALA 591 591 591 ALA ALA A . n 
A 1 592 ARG 592 592 592 ARG ARG A . n 
A 1 593 PHE 593 593 593 PHE PHE A . n 
A 1 594 ASP 594 594 594 ASP ASP A . n 
A 1 595 LYS 595 595 595 LYS LYS A . n 
A 1 596 GLY 596 596 596 GLY GLY A . n 
A 1 597 HIS 597 597 597 HIS HIS A . n 
A 1 598 ARG 598 598 598 ARG ARG A . n 
A 1 599 ALA 599 599 599 ALA ALA A . n 
A 1 600 VAL 600 600 600 VAL VAL A . n 
A 1 601 TYR 601 601 601 TYR TYR A . n 
A 1 602 SER 602 602 602 SER SER A . n 
A 1 603 LYS 603 603 603 LYS LYS A . n 
A 1 604 LYS 604 604 604 LYS LYS A . n 
A 1 605 ILE 605 605 605 ILE ILE A . n 
A 1 606 PRO 606 606 606 PRO PRO A . n 
A 1 607 GLN 607 607 607 GLN GLN A . n 
A 1 608 ALA 608 608 608 ALA ALA A . n 
A 1 609 TYR 609 609 609 TYR TYR A . n 
A 1 610 ASN 610 610 610 ASN ASN A . n 
A 1 611 GLN 611 611 611 GLN GLN A . n 
A 1 612 ALA 612 612 612 ALA ALA A . n 
A 1 613 THR 613 613 613 THR THR A . n 
A 1 614 LEU 614 614 614 LEU LEU A . n 
A 1 615 PRO 615 615 615 PRO PRO A . n 
A 1 616 THR 616 616 616 THR THR A . n 
A 1 617 ALA 617 617 617 ALA ALA A . n 
A 1 618 THR 618 618 618 THR THR A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 LEU 620 620 620 LEU LEU A . n 
A 1 621 VAL 621 621 621 VAL VAL A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 PHE 623 623 623 PHE PHE A . n 
A 1 624 GLN 624 624 624 GLN GLN A . n 
A 1 625 VAL 625 625 625 VAL VAL A . n 
A 1 626 PRO 626 626 626 PRO PRO A . n 
A 1 627 MET 627 627 627 MET MET A . n 
A 1 628 PRO 628 628 628 PRO PRO A . n 
A 1 629 GLN 629 629 629 GLN GLN A . n 
A 1 630 SER 630 630 630 SER SER A . n 
A 1 631 MET 631 631 631 MET MET A . n 
A 1 632 LEU 632 632 632 LEU LEU A . n 
A 1 633 PRO 633 633 633 PRO PRO A . n 
A 1 634 THR 634 634 634 THR THR A . n 
A 1 635 THR 635 635 635 THR THR A . n 
A 1 636 PRO 636 636 636 PRO PRO A . n 
A 1 637 SER 637 637 637 SER SER A . n 
A 1 638 ILE 638 638 638 ILE ILE A . n 
A 1 639 SER 639 639 639 SER SER A . n 
A 1 640 GLY 640 640 640 GLY GLY A . n 
A 1 641 ASP 641 641 641 ASP ASP A . n 
A 1 642 LEU 642 642 642 LEU LEU A . n 
A 1 643 GLY 643 643 643 GLY GLY A . n 
A 1 644 THR 644 644 644 THR THR A . n 
A 1 645 ASN 645 645 645 ASN ASN A . n 
A 1 646 PHE 646 646 646 PHE PHE A . n 
A 1 647 TYR 647 647 647 TYR TYR A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 CYS 649 649 649 CYS CYS A . n 
A 1 650 GLY 650 650 650 GLY GLY A . n 
A 1 651 HIS 651 651 651 HIS HIS A . n 
A 1 652 SER 652 652 652 SER SER A . n 
A 1 653 VAL 653 653 653 VAL VAL A . n 
A 1 654 LEU 654 654 654 LEU LEU A . n 
A 1 655 LYS 655 655 655 LYS LYS A . n 
A 1 656 ILE 656 656 656 ILE ILE A . n 
A 1 657 SER 657 657 657 SER SER A . n 
A 1 658 ASN 658 658 658 ASN ASN A . n 
A 1 659 SER 659 659 659 SER SER A . n 
A 1 660 SER 660 660 660 SER SER A . n 
A 1 661 GLY 661 661 661 GLY GLY A . n 
A 1 662 ASP 662 662 662 ASP ASP A . n 
A 1 663 TYR 663 663 663 TYR TYR A . n 
A 1 664 LEU 664 664 664 LEU LEU A . n 
A 1 665 GLU 665 665 665 GLU GLU A . n 
A 1 666 VAL 666 666 666 VAL VAL A . n 
A 1 667 LEU 667 667 667 LEU LEU A . n 
A 1 668 LEU 668 668 668 LEU LEU A . n 
A 1 669 ILE 669 669 669 ILE ILE A . n 
A 1 670 LYS 670 670 670 LYS LYS A . n 
A 1 671 THR 671 671 671 THR THR A . n 
A 1 672 THR 672 672 672 THR THR A . n 
A 1 673 GLY 673 673 673 GLY GLY A . n 
A 1 674 GLY 674 674 674 GLY GLY A . n 
A 1 675 GLY 675 675 675 GLY GLY A . n 
A 1 676 TYR 676 676 676 TYR TYR A . n 
A 1 677 VAL 677 677 677 VAL VAL A . n 
A 1 678 PHE 678 678 678 PHE PHE A . n 
A 1 679 THR 679 679 679 THR THR A . n 
A 1 680 GLY 680 680 680 GLY GLY A . n 
A 1 681 LYS 681 681 681 LYS LYS A . n 
A 1 682 ILE 682 682 682 ILE ILE A . n 
A 1 683 LEU 683 683 683 LEU LEU A . n 
A 1 684 LYS 684 684 684 LYS LYS A . n 
A 1 685 THR 685 685 685 THR THR A . n 
A 1 686 THR 686 686 686 THR THR A . n 
A 1 687 TYR 687 687 687 TYR TYR A . n 
A 1 688 ALA 688 688 688 ALA ALA A . n 
A 1 689 THR 689 689 689 THR THR A . n 
A 1 690 GLY 690 690 690 GLY GLY A . n 
A 1 691 ASN 691 691 691 ASN ASN A . n 
A 1 692 GLN 692 692 692 GLN GLN A . n 
A 1 693 PRO 693 693 693 PRO PRO A . n 
A 1 694 THR 694 694 694 THR THR A . n 
A 1 695 ALA 695 695 695 ALA ALA A . n 
A 1 696 ILE 696 696 696 ILE ILE A . n 
A 1 697 THR 697 697 697 THR THR A . n 
A 1 698 ALA 698 698 698 ALA ALA A . n 
A 1 699 THR 699 699 699 THR THR A . n 
A 1 700 ALA 700 700 700 ALA ALA A . n 
A 1 701 ALA 701 701 701 ALA ALA A . n 
A 1 702 HIS 702 702 702 HIS HIS A . n 
A 1 703 TYR 703 703 703 TYR TYR A . n 
A 1 704 SER 704 704 704 SER SER A . n 
A 1 705 MET 705 705 705 MET MET A . n 
A 1 706 LYS 706 706 706 LYS LYS A . n 
A 1 707 ASP 707 707 707 ASP ASP A . n 
A 1 708 LEU 708 708 708 LEU LEU A . n 
A 1 709 LYS 709 709 709 LYS LYS A . n 
A 1 710 VAL 710 710 710 VAL VAL A . n 
A 1 711 ALA 711 711 711 ALA ALA A . n 
A 1 712 GLY 712 712 712 GLY GLY A . n 
A 1 713 ALA 713 713 713 ALA ALA A . n 
A 1 714 ASN 714 714 714 ASN ASN A . n 
A 1 715 GLY 715 715 715 GLY GLY A . n 
A 1 716 PRO 716 716 716 PRO PRO A . n 
A 1 717 ASN 717 717 717 ASN ASN A . n 
A 1 718 MET 718 718 718 MET MET A . n 
A 1 719 PRO 719 719 719 PRO PRO A . n 
A 1 720 LEU 720 720 720 LEU LEU A . n 
A 1 721 GLU 721 721 721 GLU GLU A . n 
A 1 722 THR 722 722 722 THR THR A . n 
A 1 723 ILE 723 723 723 ILE ILE A . n 
A 1 724 ARG 724 724 724 ARG ARG A . n 
A 1 725 ASP 725 725 725 ASP ASP A . n 
A 1 726 ILE 726 726 726 ILE ILE A . n 
A 1 727 ASP 727 727 727 ASP ASP A . n 
A 1 728 MET 728 728 728 MET MET A . n 
A 1 729 ALA 729 729 729 ALA ALA A . n 
A 1 730 SER 730 730 730 SER SER A . n 
A 1 731 TYR 731 731 731 TYR TYR A . n 
A 1 732 VAL 732 732 732 VAL VAL A . n 
A 1 733 THR 733 733 733 THR THR A . n 
A 1 734 ILE 734 734 734 ILE ILE A . n 
A 1 735 GLY 735 735 735 GLY GLY A . n 
A 1 736 VAL 736 736 736 VAL VAL A . n 
A 1 737 GLY 737 737 737 GLY GLY A . n 
A 1 738 ALA 738 738 738 ALA ALA A . n 
A 1 739 GLY 739 739 739 GLY GLY A . n 
A 1 740 ASN 740 740 740 ASN ASN A . n 
A 1 741 GLY 741 741 741 GLY GLY A . n 
A 1 742 GLY 742 742 742 GLY GLY A . n 
A 1 743 LEU 743 743 743 LEU LEU A . n 
A 1 744 VAL 744 744 744 VAL VAL A . n 
A 1 745 LEU 745 745 745 LEU LEU A . n 
A 1 746 ASP 746 746 746 ASP ASP A . n 
A 1 747 ILE 747 747 747 ILE ILE A . n 
A 1 748 ASN 748 748 748 ASN ASN A . n 
A 1 749 ILE 749 749 749 ILE ILE A . n 
A 1 750 THR 750 750 750 THR THR A . n 
A 1 751 TRP 751 751 751 TRP TRP A . n 
A 1 752 PRO 752 752 752 PRO PRO A . n 
A 1 753 SER 753 753 753 SER SER A . n 
A 1 754 THR 754 754 754 THR THR A . n 
A 1 755 PRO 755 755 755 PRO PRO A . n 
A 1 756 PRO 756 756 756 PRO PRO A . n 
A 1 757 THR 757 757 757 THR THR A . n 
A 1 758 SER 758 758 758 SER SER A . n 
A 1 759 TYR 759 759 759 TYR TYR A . n 
A 1 760 TRP 760 760 760 TRP TRP A . n 
A 1 761 ASN 761 761 761 ASN ASN A . n 
A 1 762 ILE 762 762 762 ILE ILE A . n 
A 1 763 GLU 763 763 763 GLU GLU A . n 
A 1 764 LEU 764 764 764 LEU LEU A . n 
A 1 765 GLU 765 765 765 GLU GLU A . n 
A 1 766 ALA 766 766 766 ALA ALA A . n 
A 1 767 TRP 767 767 767 TRP TRP A . n 
A 1 768 ASP 768 768 768 ASP ASP A . n 
A 1 769 MET 769 769 769 MET MET A . n 
A 1 770 PHE 770 770 770 PHE PHE A . n 
A 1 771 GLY 771 771 771 GLY GLY A . n 
A 1 772 ASN 772 772 772 ASN ASN A . n 
A 1 773 SER 773 773 773 SER SER A . n 
A 1 774 GLU 774 774 774 GLU GLU A . n 
A 1 775 ALA 775 775 775 ALA ALA A . n 
A 1 776 SER 776 776 776 SER SER A . n 
A 1 777 ILE 777 777 777 ILE ILE A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ILE 2   2   ?   ?   ?   B . n 
B 2 3   ARG 3   3   ?   ?   ?   B . n 
B 2 4   THR 4   4   ?   ?   ?   B . n 
B 2 5   THR 5   5   ?   ?   ?   B . n 
B 2 6   ASN 6   6   ?   ?   ?   B . n 
B 2 7   THR 7   7   ?   ?   ?   B . n 
B 2 8   CYS 8   8   ?   ?   ?   B . n 
B 2 9   CYS 9   9   ?   ?   ?   B . n 
B 2 10  GLY 10  10  ?   ?   ?   B . n 
B 2 11  ASN 11  11  ?   ?   ?   B . n 
B 2 12  GLN 12  12  ?   ?   ?   B . n 
B 2 13  ALA 13  13  ?   ?   ?   B . n 
B 2 14  GLY 14  14  ?   ?   ?   B . n 
B 2 15  MET 15  15  ?   ?   ?   B . n 
B 2 16  VAL 16  16  ?   ?   ?   B . n 
B 2 17  GLU 17  17  ?   ?   ?   B . n 
B 2 18  LYS 18  18  ?   ?   ?   B . n 
B 2 19  PHE 19  19  ?   ?   ?   B . n 
B 2 20  ILE 20  20  ?   ?   ?   B . n 
B 2 21  GLY 21  21  ?   ?   ?   B . n 
B 2 22  THR 22  22  ?   ?   ?   B . n 
B 2 23  ALA 23  23  ?   ?   ?   B . n 
B 2 24  TYR 24  24  ?   ?   ?   B . n 
B 2 25  ASP 25  25  ?   ?   ?   B . n 
B 2 26  VAL 26  26  ?   ?   ?   B . n 
B 2 27  VAL 27  27  ?   ?   ?   B . n 
B 2 28  LYS 28  28  ?   ?   ?   B . n 
B 2 29  THR 29  29  ?   ?   ?   B . n 
B 2 30  VAL 30  30  ?   ?   ?   B . n 
B 2 31  TYR 31  31  ?   ?   ?   B . n 
B 2 32  ASP 32  32  ?   ?   ?   B . n 
B 2 33  ASN 33  33  ?   ?   ?   B . n 
B 2 34  LEU 34  34  ?   ?   ?   B . n 
B 2 35  GLY 35  35  ?   ?   ?   B . n 
B 2 36  GLU 36  36  ?   ?   ?   B . n 
B 2 37  ILE 37  37  ?   ?   ?   B . n 
B 2 38  GLN 38  38  ?   ?   ?   B . n 
B 2 39  PHE 39  39  ?   ?   ?   B . n 
B 2 40  ILE 40  40  ?   ?   ?   B . n 
B 2 41  TYR 41  41  ?   ?   ?   B . n 
B 2 42  ASN 42  42  ?   ?   ?   B . n 
B 2 43  PHE 43  43  ?   ?   ?   B . n 
B 2 44  LEU 44  44  ?   ?   ?   B . n 
B 2 45  ASN 45  45  ?   ?   ?   B . n 
B 2 46  ASP 46  46  ?   ?   ?   B . n 
B 2 47  TYR 47  47  ?   ?   ?   B . n 
B 2 48  GLY 48  48  ?   ?   ?   B . n 
B 2 49  VAL 49  49  ?   ?   ?   B . n 
B 2 50  LEU 50  50  ?   ?   ?   B . n 
B 2 51  ILE 51  51  ?   ?   ?   B . n 
B 2 52  THR 52  52  ?   ?   ?   B . n 
B 2 53  VAL 53  53  ?   ?   ?   B . n 
B 2 54  ASP 54  54  ?   ?   ?   B . n 
B 2 55  SER 55  55  ?   ?   ?   B . n 
B 2 56  VAL 56  56  ?   ?   ?   B . n 
B 2 57  THR 57  57  ?   ?   ?   B . n 
B 2 58  GLU 58  58  ?   ?   ?   B . n 
B 2 59  LEU 59  59  ?   ?   ?   B . n 
B 2 60  GLN 60  60  ?   ?   ?   B . n 
B 2 61  GLU 61  61  ?   ?   ?   B . n 
B 2 62  LEU 62  62  ?   ?   ?   B . n 
B 2 63  PRO 63  63  ?   ?   ?   B . n 
B 2 64  THR 64  64  ?   ?   ?   B . n 
B 2 65  THR 65  65  ?   ?   ?   B . n 
B 2 66  ALA 66  66  ?   ?   ?   B . n 
B 2 67  LYS 67  67  ?   ?   ?   B . n 
B 2 68  TYR 68  68  ?   ?   ?   B . n 
B 2 69  THR 69  69  ?   ?   ?   B . n 
B 2 70  ARG 70  70  ?   ?   ?   B . n 
B 2 71  VAL 71  71  ?   ?   ?   B . n 
B 2 72  TYR 72  72  ?   ?   ?   B . n 
B 2 73  SER 73  73  ?   ?   ?   B . n 
B 2 74  SER 74  74  ?   ?   ?   B . n 
B 2 75  THR 75  75  ?   ?   ?   B . n 
B 2 76  PRO 76  76  ?   ?   ?   B . n 
B 2 77  THR 77  77  ?   ?   ?   B . n 
B 2 78  GLY 78  78  ?   ?   ?   B . n 
B 2 79  VAL 79  79  ?   ?   ?   B . n 
B 2 80  ARG 80  80  ?   ?   ?   B . n 
B 2 81  ILE 81  81  ?   ?   ?   B . n 
B 2 82  TYR 82  82  ?   ?   ?   B . n 
B 2 83  THR 83  83  ?   ?   ?   B . n 
B 2 84  ASP 84  84  ?   ?   ?   B . n 
B 2 85  TYR 85  85  ?   ?   ?   B . n 
B 2 86  LEU 86  86  ?   ?   ?   B . n 
B 2 87  TYR 87  87  ?   ?   ?   B . n 
B 2 88  VAL 88  88  ?   ?   ?   B . n 
B 2 89  GLU 89  89  ?   ?   ?   B . n 
B 2 90  GLY 90  90  ?   ?   ?   B . n 
B 2 91  ASP 91  91  ?   ?   ?   B . n 
B 2 92  ARG 92  92  ?   ?   ?   B . n 
B 2 93  THR 93  93  ?   ?   ?   B . n 
B 2 94  GLY 94  94  ?   ?   ?   B . n 
B 2 95  VAL 95  95  ?   ?   ?   B . n 
B 2 96  LEU 96  96  ?   ?   ?   B . n 
B 2 97  PRO 97  97  ?   ?   ?   B . n 
B 2 98  SER 98  98  ?   ?   ?   B . n 
B 2 99  ASP 99  99  ?   ?   ?   B . n 
B 2 100 PRO 100 100 ?   ?   ?   B . n 
B 2 101 THR 101 101 ?   ?   ?   B . n 
B 2 102 ALA 102 102 ?   ?   ?   B . n 
B 2 103 THR 103 103 ?   ?   ?   B . n 
B 2 104 GLY 104 104 ?   ?   ?   B . n 
B 2 105 SER 105 105 ?   ?   ?   B . n 
B 2 106 TRP 106 106 ?   ?   ?   B . n 
B 2 107 VAL 107 107 ?   ?   ?   B . n 
B 2 108 VAL 108 108 ?   ?   ?   B . n 
B 2 109 VAL 109 109 ?   ?   ?   B . n 
B 2 110 GLY 110 110 ?   ?   ?   B . n 
B 2 111 SER 111 111 ?   ?   ?   B . n 
B 2 112 SER 112 112 ?   ?   ?   B . n 
B 2 113 ASN 113 113 ?   ?   ?   B . n 
B 2 114 SER 114 114 ?   ?   ?   B . n 
B 2 115 GLY 115 115 ?   ?   ?   B . n 
B 2 116 ALA 116 116 ?   ?   ?   B . n 
B 2 117 ALA 117 117 ?   ?   ?   B . n 
B 2 118 THR 118 118 ?   ?   ?   B . n 
B 2 119 GLY 119 119 ?   ?   ?   B . n 
B 2 120 THR 120 120 ?   ?   ?   B . n 
B 2 121 GLY 121 121 ?   ?   ?   B . n 
B 2 122 ALA 122 122 ?   ?   ?   B . n 
B 2 123 TYR 123 123 123 TYR TYR B . n 
B 2 124 ILE 124 124 124 ILE ILE B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 PHE 126 126 126 PHE PHE B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ASN 130 130 130 ASN ASN B . n 
B 2 131 GLY 131 131 131 GLY GLY B . n 
B 2 132 SER 132 132 132 SER SER B . n 
B 2 133 ALA 133 133 133 ALA ALA B . n 
B 2 134 ALA 134 134 134 ALA ALA B . n 
B 2 135 GLY 135 135 135 GLY GLY B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 GLU 137 137 137 GLU GLU B . n 
B 2 138 THR 138 138 138 THR THR B . n 
B 2 139 THR 139 139 139 THR THR B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 VAL 141 141 141 VAL VAL B . n 
B 2 142 VAL 142 142 142 VAL VAL B . n 
B 2 143 PRO 143 143 143 PRO PRO B . n 
B 2 144 ASP 144 144 144 ASP ASP B . n 
B 2 145 TYR 145 145 145 TYR ALA B . n 
B 2 146 THR 146 146 146 THR ALA B . n 
B 2 147 ILE 147 147 147 ILE ALA B . n 
B 2 148 GLY 148 148 148 GLY GLY B . n 
B 2 149 VAL 149 149 149 VAL VAL B . n 
B 2 150 PRO 150 150 150 PRO PRO B . n 
B 2 151 GLU 151 151 151 GLU GLU B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 TYR 153 153 153 TYR TYR B . n 
B 2 154 VAL 154 154 154 VAL VAL B . n 
B 2 155 GLU 155 155 155 GLU GLU B . n 
B 2 156 GLY 156 156 156 GLY GLY B . n 
B 2 157 PHE 157 157 157 PHE PHE B . n 
B 2 158 ARG 158 158 158 ARG ARG B . n 
B 2 159 GLN 159 159 159 GLN GLN B . n 
B 2 160 GLN 160 160 160 GLN GLN B . n 
B 2 161 VAL 161 161 161 VAL VAL B . n 
B 2 162 GLY 162 162 162 GLY GLY B . n 
B 2 163 ARG 163 163 163 ARG ARG B . n 
B 2 164 GLY 164 164 164 GLY GLY B . n 
B 2 165 PHE 165 165 165 PHE PHE B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 PHE 167 167 167 PHE PHE B . n 
B 2 168 ASN 168 168 168 ASN ASN B . n 
B 2 169 SER 169 169 169 SER SER B . n 
B 2 170 VAL 170 170 170 VAL VAL B . n 
B 2 171 ASN 171 171 171 ASN ASN B . n 
B 2 172 LEU 172 172 172 LEU LEU B . n 
B 2 173 THR 173 173 173 THR THR B . n 
B 2 174 VAL 174 174 174 VAL VAL B . n 
B 2 175 THR 175 175 175 THR THR B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 ALA 177 177 177 ALA ALA B . n 
B 2 178 GLN 178 178 178 GLN GLN B . n 
B 2 179 PRO 179 179 179 PRO PRO B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 GLU 181 181 181 GLU GLU B . n 
B 2 182 GLN 182 182 182 GLN GLN B . n 
B 2 183 GLY 183 183 183 GLY GLY B . n 
B 2 184 ASP 184 184 184 ASP ASP B . n 
B 2 185 GLU 185 185 185 GLU GLU B . n 
B 2 186 VAL 186 186 186 VAL VAL B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 MET 189 189 189 MET MET B . n 
B 2 190 LEU 190 190 190 LEU LEU B . n 
B 2 191 SER 191 191 191 SER SER B . n 
B 2 192 GLY 192 192 ?   ?   ?   B . n 
B 2 193 ASN 193 193 ?   ?   ?   B . n 
B 2 194 PRO 194 194 ?   ?   ?   B . n 
B 2 195 ALA 195 195 ?   ?   ?   B . n 
B 2 196 VAL 196 196 ?   ?   ?   B . n 
B 2 197 PRO 197 197 ?   ?   ?   B . n 
B 2 198 ASP 198 198 ?   ?   ?   B . n 
B 2 199 ASN 199 199 ?   ?   ?   B . n 
B 2 200 PRO 200 200 ?   ?   ?   B . n 
B 2 201 ASN 201 201 ?   ?   ?   B . n 
B 2 202 ILE 202 202 ?   ?   ?   B . n 
B 2 203 ASP 203 203 ?   ?   ?   B . n 
B 2 204 SER 204 204 ?   ?   ?   B . n 
B 2 205 TRP 205 205 ?   ?   ?   B . n 
B 2 206 THR 206 206 ?   ?   ?   B . n 
B 2 207 VAL 207 207 ?   ?   ?   B . n 
B 2 208 ILE 208 208 ?   ?   ?   B . n 
B 2 209 ASN 209 209 ?   ?   ?   B . n 
B 2 210 TRP 210 210 ?   ?   ?   B . n 
B 2 211 ILE 211 211 ?   ?   ?   B . n 
B 2 212 TYR 212 212 ?   ?   ?   B . n 
B 2 213 ASN 213 213 ?   ?   ?   B . n 
B 2 214 ASN 214 214 ?   ?   ?   B . n 
B 2 215 GLY 215 215 ?   ?   ?   B . n 
B 2 216 ALA 216 216 ?   ?   ?   B . n 
B 2 217 ALA 217 217 ?   ?   ?   B . n 
B 2 218 VAL 218 218 ?   ?   ?   B . n 
B 2 219 GLY 219 219 ?   ?   ?   B . n 
B 2 220 GLY 220 220 ?   ?   ?   B . n 
B 2 221 GLU 221 221 ?   ?   ?   B . n 
B 2 222 GLN 222 222 ?   ?   ?   B . n 
B 2 223 VAL 223 223 ?   ?   ?   B . n 
B 2 224 ILE 224 224 ?   ?   ?   B . n 
B 2 225 VAL 225 225 ?   ?   ?   B . n 
B 2 226 ILE 226 226 ?   ?   ?   B . n 
B 2 227 PRO 227 227 ?   ?   ?   B . n 
B 2 228 TYR 228 228 ?   ?   ?   B . n 
B 2 229 THR 229 229 ?   ?   ?   B . n 
B 2 230 PHE 230 230 ?   ?   ?   B . n 
B 2 231 GLN 231 231 ?   ?   ?   B . n 
B 2 232 THR 232 232 ?   ?   ?   B . n 
B 2 233 VAL 233 233 ?   ?   ?   B . n 
B 2 234 PRO 234 234 ?   ?   ?   B . n 
B 2 235 ALA 235 235 ?   ?   ?   B . n 
B 2 236 ILE 236 236 ?   ?   ?   B . n 
B 2 237 PHE 237 237 ?   ?   ?   B . n 
B 2 238 LYS 238 238 ?   ?   ?   B . n 
B 2 239 ASN 239 239 ?   ?   ?   B . n 
B 2 240 GLY 240 240 ?   ?   ?   B . n 
B 2 241 LEU 241 241 ?   ?   ?   B . n 
B 2 242 ARG 242 242 ?   ?   ?   B . n 
B 2 243 TYR 243 243 ?   ?   ?   B . n 
B 2 244 GLN 244 244 ?   ?   ?   B . n 
B 2 245 GLY 245 245 ?   ?   ?   B . n 
B 2 246 GLY 246 246 ?   ?   ?   B . n 
B 2 247 LEU 247 247 ?   ?   ?   B . n 
B 2 248 SER 248 248 ?   ?   ?   B . n 
B 2 249 THR 249 249 ?   ?   ?   B . n 
B 2 250 GLN 250 250 ?   ?   ?   B . n 
B 2 251 SER 251 251 ?   ?   ?   B . n 
B 2 252 TYR 252 252 ?   ?   ?   B . n 
B 2 253 THR 253 253 ?   ?   ?   B . n 
B 2 254 VAL 254 254 ?   ?   ?   B . n 
B 2 255 ASP 255 255 ?   ?   ?   B . n 
B 2 256 GLN 256 256 ?   ?   ?   B . n 
B 2 257 ASP 257 257 ?   ?   ?   B . n 
B 2 258 ASN 258 258 ?   ?   ?   B . n 
B 2 259 LYS 259 259 ?   ?   ?   B . n 
B 2 260 ARG 260 260 ?   ?   ?   B . n 
B 2 261 ILE 261 261 ?   ?   ?   B . n 
B 2 262 LEU 262 262 ?   ?   ?   B . n 
B 2 263 LEU 263 263 ?   ?   ?   B . n 
B 2 264 THR 264 264 ?   ?   ?   B . n 
B 2 265 GLU 265 265 ?   ?   ?   B . n 
B 2 266 PRO 266 266 ?   ?   ?   B . n 
B 2 267 LEU 267 267 ?   ?   ?   B . n 
B 2 268 SER 268 268 ?   ?   ?   B . n 
B 2 269 THR 269 269 ?   ?   ?   B . n 
B 2 270 ASN 270 270 ?   ?   ?   B . n 
B 2 271 ASP 271 271 ?   ?   ?   B . n 
B 2 272 ARG 272 272 ?   ?   ?   B . n 
B 2 273 LEU 273 273 ?   ?   ?   B . n 
B 2 274 VAL 274 274 ?   ?   ?   B . n 
B 2 275 VAL 275 275 ?   ?   ?   B . n 
B 2 276 GLN 276 276 ?   ?   ?   B . n 
B 2 277 LEU 277 277 ?   ?   ?   B . n 
B 2 278 GLY 278 278 ?   ?   ?   B . n 
B 2 279 GLY 279 279 ?   ?   ?   B . n 
B 2 280 GLU 280 280 ?   ?   ?   B . n 
B 2 281 LEU 281 281 ?   ?   ?   B . n 
B 2 282 VAL 282 282 ?   ?   ?   B . n 
B 2 283 THR 283 283 ?   ?   ?   B . n 
B 2 284 LEU 284 284 ?   ?   ?   B . n 
B 2 285 GLU 285 285 ?   ?   ?   B . n 
B 2 286 SER 286 286 ?   ?   ?   B . n 
B 2 287 PRO 287 287 ?   ?   ?   B . n 
B 2 288 ASP 288 288 ?   ?   ?   B . n 
B 2 289 ARG 289 289 ?   ?   ?   B . n 
B 2 290 SER 290 290 ?   ?   ?   B . n 
B 2 291 LEU 291 291 ?   ?   ?   B . n 
B 2 292 TYR 292 292 ?   ?   ?   B . n 
B 2 293 GLU 293 293 ?   ?   ?   B . n 
B 2 294 ILE 294 294 ?   ?   ?   B . n 
B 2 295 ALA 295 295 ?   ?   ?   B . n 
B 2 296 ARG 296 296 ?   ?   ?   B . n 
B 2 297 ALA 297 297 ?   ?   ?   B . n 
B 2 298 THR 298 298 ?   ?   ?   B . n 
B 2 299 ASN 299 299 ?   ?   ?   B . n 
B 2 300 MET 300 300 ?   ?   ?   B . n 
B 2 301 LYS 301 301 ?   ?   ?   B . n 
B 2 302 ASP 302 302 ?   ?   ?   B . n 
B 2 303 SER 303 303 ?   ?   ?   B . n 
B 2 304 GLU 304 304 ?   ?   ?   B . n 
B 2 305 VAL 305 305 ?   ?   ?   B . n 
B 2 306 ILE 306 306 ?   ?   ?   B . n 
B 2 307 LYS 307 307 ?   ?   ?   B . n 
B 2 308 SER 308 308 ?   ?   ?   B . n 
B 2 309 ASP 309 309 ?   ?   ?   B . n 
B 2 310 ASN 310 310 ?   ?   ?   B . n 
B 2 311 THR 311 311 ?   ?   ?   B . n 
B 2 312 VAL 312 312 ?   ?   ?   B . n 
B 2 313 GLU 313 313 ?   ?   ?   B . n 
B 2 314 THR 314 314 ?   ?   ?   B . n 
B 2 315 LEU 315 315 ?   ?   ?   B . n 
B 2 316 ASN 316 316 ?   ?   ?   B . n 
B 2 317 GLY 317 317 ?   ?   ?   B . n 
B 2 318 LYS 318 318 ?   ?   ?   B . n 
B 2 319 ARG 319 319 ?   ?   ?   B . n 
B 2 320 ILE 320 320 ?   ?   ?   B . n 
B 2 321 LEU 321 321 ?   ?   ?   B . n 
B 2 322 TYR 322 322 ?   ?   ?   B . n 
B 2 323 ASP 323 323 ?   ?   ?   B . n 
B 2 324 ILE 324 324 ?   ?   ?   B . n 
B 2 325 VAL 325 325 ?   ?   ?   B . n 
B 2 326 SER 326 326 ?   ?   ?   B . n 
B 2 327 GLN 327 327 ?   ?   ?   B . n 
B 2 328 VAL 328 328 ?   ?   ?   B . n 
B 2 329 TYR 329 329 ?   ?   ?   B . n 
B 2 330 TYR 330 330 ?   ?   ?   B . n 
B 2 331 TRP 331 331 ?   ?   ?   B . n 
B 2 332 ILE 332 332 ?   ?   ?   B . n 
B 2 333 PRO 333 333 ?   ?   ?   B . n 
B 2 334 SER 334 334 ?   ?   ?   B . n 
B 2 335 SER 335 335 ?   ?   ?   B . n 
B 2 336 VAL 336 336 ?   ?   ?   B . n 
B 2 337 PRO 337 337 ?   ?   ?   B . n 
B 2 338 ASN 338 338 ?   ?   ?   B . n 
B 2 339 ASN 339 339 ?   ?   ?   B . n 
B 2 340 VAL 340 340 ?   ?   ?   B . n 
B 2 341 TYR 341 341 ?   ?   ?   B . n 
B 2 342 ILE 342 342 ?   ?   ?   B . n 
B 2 343 GLN 343 343 ?   ?   ?   B . n 
B 2 344 SER 344 344 ?   ?   ?   B . n 
B 2 345 VAL 345 345 ?   ?   ?   B . n 
B 2 346 VAL 346 346 ?   ?   ?   B . n 
B 2 347 ASN 347 347 ?   ?   ?   B . n 
B 2 348 GLY 348 348 ?   ?   ?   B . n 
B 2 349 GLN 349 349 ?   ?   ?   B . n 
B 2 350 LEU 350 350 ?   ?   ?   B . n 
B 2 351 THR 351 351 ?   ?   ?   B . n 
B 2 352 TYR 352 352 ?   ?   ?   B . n 
B 2 353 LEU 353 353 ?   ?   ?   B . n 
B 2 354 PRO 354 354 ?   ?   ?   B . n 
B 2 355 GLY 355 355 ?   ?   ?   B . n 
B 2 356 ASN 356 356 ?   ?   ?   B . n 
B 2 357 ILE 357 357 ?   ?   ?   B . n 
B 2 358 VAL 358 358 ?   ?   ?   B . n 
B 2 359 VAL 359 359 ?   ?   ?   B . n 
B 2 360 THR 360 360 ?   ?   ?   B . n 
B 2 361 LEU 361 361 ?   ?   ?   B . n 
B 2 362 THR 362 362 ?   ?   ?   B . n 
B 2 363 PRO 363 363 ?   ?   ?   B . n 
B 2 364 ILE 364 364 ?   ?   ?   B . n 
B 2 365 VAL 365 365 ?   ?   ?   B . n 
B 2 366 THR 366 366 ?   ?   ?   B . n 
B 2 367 LEU 367 367 ?   ?   ?   B . n 
B 2 368 GLY 368 368 ?   ?   ?   B . n 
B 2 369 LEU 369 369 ?   ?   ?   B . n 
B 2 370 SER 370 370 ?   ?   ?   B . n 
B 2 371 GLY 371 371 ?   ?   ?   B . n 
B 2 372 THR 372 372 ?   ?   ?   B . n 
B 2 373 THR 373 373 ?   ?   ?   B . n 
B 2 374 ALA 374 374 ?   ?   ?   B . n 
B 2 375 GLN 375 375 ?   ?   ?   B . n 
B 2 376 ARG 376 376 ?   ?   ?   B . n 
B 2 377 PRO 377 377 ?   ?   ?   B . n 
B 2 378 ILE 378 378 ?   ?   ?   B . n 
B 2 379 GLY 379 379 ?   ?   ?   B . n 
B 2 380 VAL 380 380 ?   ?   ?   B . n 
B 2 381 LEU 381 381 ?   ?   ?   B . n 
B 2 382 THR 382 382 ?   ?   ?   B . n 
B 2 383 GLY 383 383 ?   ?   ?   B . n 
B 2 384 THR 384 384 ?   ?   ?   B . n 
B 2 385 GLN 385 385 ?   ?   ?   B . n 
B 2 386 HIS 386 386 ?   ?   ?   B . n 
B 2 387 PHE 387 387 ?   ?   ?   B . n 
B 2 388 ASP 388 388 ?   ?   ?   B . n 
B 2 389 THR 389 389 ?   ?   ?   B . n 
B 2 390 THR 390 390 ?   ?   ?   B . n 
B 2 391 LEU 391 391 ?   ?   ?   B . n 
B 2 392 GLY 392 392 ?   ?   ?   B . n 
B 2 393 LYS 393 393 ?   ?   ?   B . n 
B 2 394 PRO 394 394 ?   ?   ?   B . n 
B 2 395 ILE 395 395 ?   ?   ?   B . n 
B 2 396 TRP 396 396 ?   ?   ?   B . n 
B 2 397 PHE 397 397 ?   ?   ?   B . n 
B 2 398 ASN 398 398 ?   ?   ?   B . n 
B 2 399 GLY 399 399 ?   ?   ?   B . n 
B 2 400 THR 400 400 ?   ?   ?   B . n 
B 2 401 ALA 401 401 ?   ?   ?   B . n 
B 2 402 TRP 402 402 ?   ?   ?   B . n 
B 2 403 VAL 403 403 ?   ?   ?   B . n 
B 2 404 ASP 404 404 ?   ?   ?   B . n 
B 2 405 SER 405 405 ?   ?   ?   B . n 
B 2 406 THR 406 406 ?   ?   ?   B . n 
B 2 407 GLY 407 407 ?   ?   ?   B . n 
B 2 408 ALA 408 408 ?   ?   ?   B . n 
B 2 409 VAL 409 409 ?   ?   ?   B . n 
B 2 410 VAL 410 410 ?   ?   ?   B . n 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A VAL 131 ? CG1 ? A VAL 131 CG1 
2  1 Y 1 A VAL 131 ? CG2 ? A VAL 131 CG2 
3  1 Y 1 A ASP 508 ? CG  ? A ASP 508 CG  
4  1 Y 1 A ASP 508 ? OD1 ? A ASP 508 OD1 
5  1 Y 1 A ASP 508 ? OD2 ? A ASP 508 OD2 
6  1 Y 1 B TYR 145 ? CG  ? B TYR 145 CG  
7  1 Y 1 B TYR 145 ? CD1 ? B TYR 145 CD1 
8  1 Y 1 B TYR 145 ? CD2 ? B TYR 145 CD2 
9  1 Y 1 B TYR 145 ? CE1 ? B TYR 145 CE1 
10 1 Y 1 B TYR 145 ? CE2 ? B TYR 145 CE2 
11 1 Y 1 B TYR 145 ? CZ  ? B TYR 145 CZ  
12 1 Y 1 B TYR 145 ? OH  ? B TYR 145 OH  
13 1 Y 1 B THR 146 ? OG1 ? B THR 146 OG1 
14 1 Y 1 B THR 146 ? CG2 ? B THR 146 CG2 
15 1 Y 1 B ILE 147 ? CG1 ? B ILE 147 CG1 
16 1 Y 1 B ILE 147 ? CG2 ? B ILE 147 CG2 
17 1 Y 1 B ILE 147 ? CD1 ? B ILE 147 CD1 
# 
_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                     9D84 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9D84 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9D84 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9D84 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.003 ? 19494 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.584 ? 26542 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.580 ? 2717  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.043 ? 2953  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 3456  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9D84 
_struct.title                        'Shigella flexneri bacteriophage B2 Gp48 and Gp49' 
_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        9D84 
_struct_keywords.text            'B2, Gp48 & Gp49, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
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 PDB 9D84 9D84 ? 1 ? 1 
2 PDB 9D84 9D84 ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9D84 A 1 ? 777 ? 9D84 1 ? 777 ? 1 777 
2 2 9D84 B 1 ? 410 ? 9D84 1 ? 410 ? 1 410 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0  0.0       0.0 0.0 0.0       1.0  0.0 0.0 0.0 0.0 1.0 0.0 
2 'point symmetry operation' ?     ?     -0.5 -0.866025 0.0 0.0 0.866025  -0.5 0.0 0.0 0.0 0.0 1.0 0.0 
3 'point symmetry operation' ?     ?     -0.5 0.866025  0.0 0.0 -0.866025 -0.5 0.0 0.0 0.0 0.0 1.0 0.0 
# 
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 LYS A 10  ? ALA A 13  ? LYS A 10  ALA A 13  5 ? 4  
HELX_P HELX_P2  AA2 GLY A 14  ? GLY A 27  ? GLY A 14  GLY A 27  1 ? 14 
HELX_P HELX_P3  AA3 LYS A 29  ? SER A 31  ? LYS A 29  SER A 31  5 ? 3  
HELX_P HELX_P4  AA4 LEU A 87  ? ARG A 94  ? LEU A 87  ARG A 94  1 ? 8  
HELX_P HELX_P5  AA5 GLY A 157 ? ALA A 165 ? GLY A 157 ALA A 165 1 ? 9  
HELX_P HELX_P6  AA6 GLY A 168 ? ILE A 173 ? GLY A 168 ILE A 173 5 ? 6  
HELX_P HELX_P7  AA7 THR A 180 ? HIS A 209 ? THR A 180 HIS A 209 1 ? 30 
HELX_P HELX_P8  AA8 ASP A 221 ? GLY A 226 ? ASP A 221 GLY A 226 1 ? 6  
HELX_P HELX_P9  AA9 THR A 249 ? GLY A 263 ? THR A 249 GLY A 263 1 ? 15 
HELX_P HELX_P10 AB1 THR A 277 ? ASN A 283 ? THR A 277 ASN A 283 1 ? 7  
HELX_P HELX_P11 AB2 GLU A 284 ? GLN A 288 ? GLU A 284 GLN A 288 5 ? 5  
HELX_P HELX_P12 AB3 GLY A 301 ? GLY A 306 ? GLY A 301 GLY A 306 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 307 ? THR A 311 ? GLY A 307 THR A 311 5 ? 5  
HELX_P HELX_P14 AB5 THR A 312 ? TRP A 330 ? THR A 312 TRP A 330 1 ? 19 
HELX_P HELX_P15 AB6 GLY A 348 ? TYR A 365 ? GLY A 348 TYR A 365 1 ? 18 
HELX_P HELX_P16 AB7 ASN A 371 ? VAL A 375 ? ASN A 371 VAL A 375 5 ? 5  
HELX_P HELX_P17 AB8 HIS A 380 ? GLN A 385 ? HIS A 380 GLN A 385 1 ? 6  
HELX_P HELX_P18 AB9 ASN A 392 ? GLY A 410 ? ASN A 392 GLY A 410 1 ? 19 
HELX_P HELX_P19 AC1 ASP A 497 ? TRP A 502 ? ASP A 497 TRP A 502 1 ? 6  
HELX_P HELX_P20 AC2 GLN A 507 ? ALA A 513 ? GLN A 507 ALA A 513 5 ? 7  
HELX_P HELX_P21 AC3 SER A 535 ? SER A 539 ? SER A 535 SER A 539 5 ? 5  
HELX_P HELX_P22 AC4 PRO A 580 ? SER A 584 ? PRO A 580 SER A 584 5 ? 5  
HELX_P HELX_P23 AC5 PRO A 628 ? LEU A 632 ? PRO A 628 LEU A 632 5 ? 5  
HELX_P HELX_P24 AC6 THR A 635 ? GLY A 640 ? THR A 635 GLY A 640 1 ? 6  
HELX_P HELX_P25 AC7 ASN B 129 ? SER B 132 ? ASN B 129 SER B 132 5 ? 4  
# 
_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 ILE 605 A . ? ILE 605 A PRO 606 A ? PRO 606 A 1 1.28  
2 MET 718 A . ? MET 718 A PRO 719 A ? PRO 719 A 1 -0.37 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 8 ? 
AB1 ? 7 ? 
AB2 ? 2 ? 
AB3 ? 4 ? 
AB4 ? 3 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AA9 7 8 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? 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 VAL A 33  ? TYR A 35  ? VAL A 33  TYR A 35  
AA1 2 VAL A 47  ? ASP A 50  ? VAL A 47  ASP A 50  
AA1 3 ARG A 55  ? SER A 58  ? ARG A 55  SER A 58  
AA2 1 ALA A 69  ? LEU A 72  ? ALA A 69  LEU A 72  
AA2 2 VAL A 77  ? HIS A 80  ? VAL A 77  HIS A 80  
AA2 3 GLY A 83  ? ASP A 86  ? GLY A 83  ASP A 86  
AA3 1 VAL A 98  ? ASP A 103 ? VAL A 98  ASP A 103 
AA3 2 GLU A 115 ? THR A 118 ? GLU A 115 THR A 118 
AA3 3 GLN A 124 ? ARG A 126 ? GLN A 124 ARG A 126 
AA3 4 ILE A 153 ? GLU A 154 ? ILE A 153 GLU A 154 
AA4 1 SER A 265 ? ALA A 272 ? SER A 265 ALA A 272 
AA4 2 SER A 213 ? GLY A 220 ? SER A 213 GLY A 220 
AA4 3 VAL A 295 ? MET A 299 ? VAL A 295 MET A 299 
AA4 4 GLY A 333 ? GLN A 337 ? GLY A 333 GLN A 337 
AA4 5 ALA A 368 ? PHE A 370 ? ALA A 368 PHE A 370 
AA5 1 ARG A 234 ? VAL A 235 ? ARG A 234 VAL A 235 
AA5 2 HIS A 245 ? ALA A 246 ? HIS A 245 ALA A 246 
AA6 1 ILE A 423 ? THR A 425 ? ILE A 423 THR A 425 
AA6 2 PHE A 569 ? VAL A 579 ? PHE A 569 VAL A 579 
AA6 3 GLY A 460 ? MET A 461 ? GLY A 460 MET A 461 
AA7 1 ILE A 423 ? THR A 425 ? ILE A 423 THR A 425 
AA7 2 PHE A 569 ? VAL A 579 ? PHE A 569 VAL A 579 
AA7 3 ALA A 479 ? GLY A 488 ? ALA A 479 GLY A 488 
AA7 4 LYS A 543 ? LEU A 549 ? LYS A 543 LEU A 549 
AA8 1 ILE A 434 ? ASP A 438 ? ILE A 434 ASP A 438 
AA8 2 ILE A 468 ? LEU A 475 ? ILE A 468 LEU A 475 
AA8 3 GLY A 552 ? PHE A 559 ? GLY A 552 PHE A 559 
AA8 4 ASN A 493 ? LEU A 495 ? ASN A 493 LEU A 495 
AA9 1 HIS A 597 ? ILE A 605 ? HIS A 597 ILE A 605 
AA9 2 TRP A 760 ? ASP A 768 ? TRP A 760 ASP A 768 
AA9 3 SER A 652 ? ASN A 658 ? SER A 652 ASN A 658 
AA9 4 TYR A 663 ? ILE A 669 ? TYR A 663 ILE A 669 
AA9 5 VAL A 677 ? THR A 685 ? VAL A 677 THR A 685 
AA9 6 ALA A 695 ? LYS A 709 ? ALA A 695 LYS A 709 
AA9 7 LEU A 743 ? THR A 750 ? LEU A 743 THR A 750 
AA9 8 ASN A 622 ? PRO A 626 ? ASN A 622 PRO A 626 
AB1 1 HIS A 597 ? ILE A 605 ? HIS A 597 ILE A 605 
AB1 2 TRP A 760 ? ASP A 768 ? TRP A 760 ASP A 768 
AB1 3 SER A 652 ? ASN A 658 ? SER A 652 ASN A 658 
AB1 4 TYR A 663 ? ILE A 669 ? TYR A 663 ILE A 669 
AB1 5 VAL A 677 ? THR A 685 ? VAL A 677 THR A 685 
AB1 6 ALA A 695 ? LYS A 709 ? ALA A 695 LYS A 709 
AB1 7 ILE A 723 ? THR A 733 ? ILE A 723 THR A 733 
AB2 1 THR A 618 ? ALA A 619 ? THR A 618 ALA A 619 
AB2 2 THR A 757 ? SER A 758 ? THR A 757 SER A 758 
AB3 1 ILE B 124 ? VAL B 127 ? ILE B 124 VAL B 127 
AB3 2 VAL B 186 ? LEU B 190 ? VAL B 186 LEU B 190 
AB3 3 GLU B 151 ? VAL B 154 ? GLU B 151 VAL B 154 
AB3 4 PHE B 157 ? GLN B 160 ? PHE B 157 GLN B 160 
AB4 1 ALA B 134 ? VAL B 141 ? ALA B 134 VAL B 141 
AB4 2 THR B 173 ? GLN B 182 ? THR B 173 GLN B 182 
AB4 3 PHE B 165 ? ASN B 168 ? PHE B 165 ASN B 168 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 34  ? N VAL A 34  O TYR A 49  ? O TYR A 49  
AA1 2 3 N ILE A 48  ? N ILE A 48  O TYR A 57  ? O TYR A 57  
AA2 1 2 N ILE A 70  ? N ILE A 70  O VAL A 79  ? O VAL A 79  
AA2 2 3 N LEU A 78  ? N LEU A 78  O VAL A 85  ? O VAL A 85  
AA3 1 2 N VAL A 98  ? N VAL A 98  O ILE A 116 ? O ILE A 116 
AA3 2 3 N LEU A 117 ? N LEU A 117 O TYR A 125 ? O TYR A 125 
AA3 3 4 N ARG A 126 ? N ARG A 126 O ILE A 153 ? O ILE A 153 
AA4 1 2 O THR A 267 ? O THR A 267 N VAL A 216 ? N VAL A 216 
AA4 2 3 N LEU A 217 ? N LEU A 217 O VAL A 295 ? O VAL A 295 
AA4 3 4 N VAL A 296 ? N VAL A 296 O GLY A 333 ? O GLY A 333 
AA4 4 5 N VAL A 336 ? N VAL A 336 O ALA A 368 ? O ALA A 368 
AA5 1 2 N VAL A 235 ? N VAL A 235 O HIS A 245 ? O HIS A 245 
AA6 1 2 N THR A 425 ? N THR A 425 O LEU A 574 ? O LEU A 574 
AA6 2 3 O PHE A 569 ? O PHE A 569 N MET A 461 ? N MET A 461 
AA7 1 2 N THR A 425 ? N THR A 425 O LEU A 574 ? O LEU A 574 
AA7 2 3 O THR A 575 ? O THR A 575 N PHE A 483 ? N PHE A 483 
AA7 3 4 N VAL A 484 ? N VAL A 484 O LYS A 543 ? O LYS A 543 
AA8 1 2 N GLY A 435 ? N GLY A 435 O SER A 472 ? O SER A 472 
AA8 2 3 N ALA A 469 ? N ALA A 469 O PHE A 558 ? O PHE A 558 
AA8 3 4 O PHE A 559 ? O PHE A 559 N ASN A 493 ? N ASN A 493 
AA9 1 2 N ILE A 605 ? N ILE A 605 O TRP A 760 ? O TRP A 760 
AA9 2 3 O ASN A 761 ? O ASN A 761 N SER A 657 ? N SER A 657 
AA9 3 4 N LEU A 654 ? N LEU A 654 O VAL A 666 ? O VAL A 666 
AA9 4 5 N LEU A 667 ? N LEU A 667 O LYS A 681 ? O LYS A 681 
AA9 5 6 N PHE A 678 ? N PHE A 678 O ALA A 698 ? O ALA A 698 
AA9 6 7 N ALA A 701 ? N ALA A 701 O VAL A 744 ? O VAL A 744 
AA9 7 8 O LEU A 745 ? O LEU A 745 N VAL A 625 ? N VAL A 625 
AB1 1 2 N ILE A 605 ? N ILE A 605 O TRP A 760 ? O TRP A 760 
AB1 2 3 O ASN A 761 ? O ASN A 761 N SER A 657 ? N SER A 657 
AB1 3 4 N LEU A 654 ? N LEU A 654 O VAL A 666 ? O VAL A 666 
AB1 4 5 N LEU A 667 ? N LEU A 667 O LYS A 681 ? O LYS A 681 
AB1 5 6 N PHE A 678 ? N PHE A 678 O ALA A 698 ? O ALA A 698 
AB1 6 7 N SER A 704 ? N SER A 704 O ASP A 727 ? O ASP A 727 
AB2 1 2 N THR A 618 ? N THR A 618 O SER A 758 ? O SER A 758 
AB3 1 2 N PHE B 126 ? N PHE B 126 O LEU B 188 ? O LEU B 188 
AB3 2 3 O VAL B 187 ? O VAL B 187 N TYR B 153 ? N TYR B 153 
AB3 3 4 N ILE B 152 ? N ILE B 152 O GLN B 159 ? O GLN B 159 
AB4 1 2 N ILE B 140 ? N ILE B 140 O VAL B 174 ? O VAL B 174 
AB4 2 3 O THR B 175 ? O THR B 175 N THR B 166 ? N THR B 166 
# 
_pdbx_entry_details.entry_id                   9D84 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   THR 
_pdbx_validate_close_contact.auth_seq_id_1    634 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    639 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CA 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_1             776 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_2             776 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.433 
_pdbx_validate_rmsd_bond.bond_target_value         1.525 
_pdbx_validate_rmsd_bond.bond_deviation            -0.092 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.015 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 132 ? ? -102.24 59.38   
2 1 ALA A 151 ? ? -126.02 -165.93 
3 1 ASP A 387 ? ? -126.24 -167.65 
4 1 ASN A 503 ? ? -161.83 114.67  
5 1 LEU A 534 ? ? -95.38  56.90   
6 1 ASN A 648 ? ? -66.71  0.03    
7 1 SER A 753 ? ? -125.03 -166.32 
8 1 SER A 758 ? ? -160.83 -169.52 
9 1 ASN B 130 ? ? 54.33   12.62   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    129 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    130 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -135.87 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9D84 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9D84 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.4 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               2078531 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 VIRUS 
_em_entity_assembly.name                 'Shigella phage B2' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9D84 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             2100 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_virus_entity.id                    1 
_em_virus_entity.virus_host_category   ? 
_em_virus_entity.virus_type            VIRION 
_em_virus_entity.virus_isolate         OTHER 
_em_virus_entity.entity_assembly_id    1 
_em_virus_entity.enveloped             NO 
_em_virus_entity.empty                 NO 
_em_virus_entity.details               ? 
# 
_em_vitrification.entry_id              9D84 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9D84 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9D84 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C3 
# 
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 MET 1   ? A MET 1   
2   1 Y 1 A ASN 2   ? A ASN 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 B MET 1   ? B MET 1   
5   1 Y 1 B ILE 2   ? B ILE 2   
6   1 Y 1 B ARG 3   ? B ARG 3   
7   1 Y 1 B THR 4   ? B THR 4   
8   1 Y 1 B THR 5   ? B THR 5   
9   1 Y 1 B ASN 6   ? B ASN 6   
10  1 Y 1 B THR 7   ? B THR 7   
11  1 Y 1 B CYS 8   ? B CYS 8   
12  1 Y 1 B CYS 9   ? B CYS 9   
13  1 Y 1 B GLY 10  ? B GLY 10  
14  1 Y 1 B ASN 11  ? B ASN 11  
15  1 Y 1 B GLN 12  ? B GLN 12  
16  1 Y 1 B ALA 13  ? B ALA 13  
17  1 Y 1 B GLY 14  ? B GLY 14  
18  1 Y 1 B MET 15  ? B MET 15  
19  1 Y 1 B VAL 16  ? B VAL 16  
20  1 Y 1 B GLU 17  ? B GLU 17  
21  1 Y 1 B LYS 18  ? B LYS 18  
22  1 Y 1 B PHE 19  ? B PHE 19  
23  1 Y 1 B ILE 20  ? B ILE 20  
24  1 Y 1 B GLY 21  ? B GLY 21  
25  1 Y 1 B THR 22  ? B THR 22  
26  1 Y 1 B ALA 23  ? B ALA 23  
27  1 Y 1 B TYR 24  ? B TYR 24  
28  1 Y 1 B ASP 25  ? B ASP 25  
29  1 Y 1 B VAL 26  ? B VAL 26  
30  1 Y 1 B VAL 27  ? B VAL 27  
31  1 Y 1 B LYS 28  ? B LYS 28  
32  1 Y 1 B THR 29  ? B THR 29  
33  1 Y 1 B VAL 30  ? B VAL 30  
34  1 Y 1 B TYR 31  ? B TYR 31  
35  1 Y 1 B ASP 32  ? B ASP 32  
36  1 Y 1 B ASN 33  ? B ASN 33  
37  1 Y 1 B LEU 34  ? B LEU 34  
38  1 Y 1 B GLY 35  ? B GLY 35  
39  1 Y 1 B GLU 36  ? B GLU 36  
40  1 Y 1 B ILE 37  ? B ILE 37  
41  1 Y 1 B GLN 38  ? B GLN 38  
42  1 Y 1 B PHE 39  ? B PHE 39  
43  1 Y 1 B ILE 40  ? B ILE 40  
44  1 Y 1 B TYR 41  ? B TYR 41  
45  1 Y 1 B ASN 42  ? B ASN 42  
46  1 Y 1 B PHE 43  ? B PHE 43  
47  1 Y 1 B LEU 44  ? B LEU 44  
48  1 Y 1 B ASN 45  ? B ASN 45  
49  1 Y 1 B ASP 46  ? B ASP 46  
50  1 Y 1 B TYR 47  ? B TYR 47  
51  1 Y 1 B GLY 48  ? B GLY 48  
52  1 Y 1 B VAL 49  ? B VAL 49  
53  1 Y 1 B LEU 50  ? B LEU 50  
54  1 Y 1 B ILE 51  ? B ILE 51  
55  1 Y 1 B THR 52  ? B THR 52  
56  1 Y 1 B VAL 53  ? B VAL 53  
57  1 Y 1 B ASP 54  ? B ASP 54  
58  1 Y 1 B SER 55  ? B SER 55  
59  1 Y 1 B VAL 56  ? B VAL 56  
60  1 Y 1 B THR 57  ? B THR 57  
61  1 Y 1 B GLU 58  ? B GLU 58  
62  1 Y 1 B LEU 59  ? B LEU 59  
63  1 Y 1 B GLN 60  ? B GLN 60  
64  1 Y 1 B GLU 61  ? B GLU 61  
65  1 Y 1 B LEU 62  ? B LEU 62  
66  1 Y 1 B PRO 63  ? B PRO 63  
67  1 Y 1 B THR 64  ? B THR 64  
68  1 Y 1 B THR 65  ? B THR 65  
69  1 Y 1 B ALA 66  ? B ALA 66  
70  1 Y 1 B LYS 67  ? B LYS 67  
71  1 Y 1 B TYR 68  ? B TYR 68  
72  1 Y 1 B THR 69  ? B THR 69  
73  1 Y 1 B ARG 70  ? B ARG 70  
74  1 Y 1 B VAL 71  ? B VAL 71  
75  1 Y 1 B TYR 72  ? B TYR 72  
76  1 Y 1 B SER 73  ? B SER 73  
77  1 Y 1 B SER 74  ? B SER 74  
78  1 Y 1 B THR 75  ? B THR 75  
79  1 Y 1 B PRO 76  ? B PRO 76  
80  1 Y 1 B THR 77  ? B THR 77  
81  1 Y 1 B GLY 78  ? B GLY 78  
82  1 Y 1 B VAL 79  ? B VAL 79  
83  1 Y 1 B ARG 80  ? B ARG 80  
84  1 Y 1 B ILE 81  ? B ILE 81  
85  1 Y 1 B TYR 82  ? B TYR 82  
86  1 Y 1 B THR 83  ? B THR 83  
87  1 Y 1 B ASP 84  ? B ASP 84  
88  1 Y 1 B TYR 85  ? B TYR 85  
89  1 Y 1 B LEU 86  ? B LEU 86  
90  1 Y 1 B TYR 87  ? B TYR 87  
91  1 Y 1 B VAL 88  ? B VAL 88  
92  1 Y 1 B GLU 89  ? B GLU 89  
93  1 Y 1 B GLY 90  ? B GLY 90  
94  1 Y 1 B ASP 91  ? B ASP 91  
95  1 Y 1 B ARG 92  ? B ARG 92  
96  1 Y 1 B THR 93  ? B THR 93  
97  1 Y 1 B GLY 94  ? B GLY 94  
98  1 Y 1 B VAL 95  ? B VAL 95  
99  1 Y 1 B LEU 96  ? B LEU 96  
100 1 Y 1 B PRO 97  ? B PRO 97  
101 1 Y 1 B SER 98  ? B SER 98  
102 1 Y 1 B ASP 99  ? B ASP 99  
103 1 Y 1 B PRO 100 ? B PRO 100 
104 1 Y 1 B THR 101 ? B THR 101 
105 1 Y 1 B ALA 102 ? B ALA 102 
106 1 Y 1 B THR 103 ? B THR 103 
107 1 Y 1 B GLY 104 ? B GLY 104 
108 1 Y 1 B SER 105 ? B SER 105 
109 1 Y 1 B TRP 106 ? B TRP 106 
110 1 Y 1 B VAL 107 ? B VAL 107 
111 1 Y 1 B VAL 108 ? B VAL 108 
112 1 Y 1 B VAL 109 ? B VAL 109 
113 1 Y 1 B GLY 110 ? B GLY 110 
114 1 Y 1 B SER 111 ? B SER 111 
115 1 Y 1 B SER 112 ? B SER 112 
116 1 Y 1 B ASN 113 ? B ASN 113 
117 1 Y 1 B SER 114 ? B SER 114 
118 1 Y 1 B GLY 115 ? B GLY 115 
119 1 Y 1 B ALA 116 ? B ALA 116 
120 1 Y 1 B ALA 117 ? B ALA 117 
121 1 Y 1 B THR 118 ? B THR 118 
122 1 Y 1 B GLY 119 ? B GLY 119 
123 1 Y 1 B THR 120 ? B THR 120 
124 1 Y 1 B GLY 121 ? B GLY 121 
125 1 Y 1 B ALA 122 ? B ALA 122 
126 1 Y 1 B GLY 192 ? B GLY 192 
127 1 Y 1 B ASN 193 ? B ASN 193 
128 1 Y 1 B PRO 194 ? B PRO 194 
129 1 Y 1 B ALA 195 ? B ALA 195 
130 1 Y 1 B VAL 196 ? B VAL 196 
131 1 Y 1 B PRO 197 ? B PRO 197 
132 1 Y 1 B ASP 198 ? B ASP 198 
133 1 Y 1 B ASN 199 ? B ASN 199 
134 1 Y 1 B PRO 200 ? B PRO 200 
135 1 Y 1 B ASN 201 ? B ASN 201 
136 1 Y 1 B ILE 202 ? B ILE 202 
137 1 Y 1 B ASP 203 ? B ASP 203 
138 1 Y 1 B SER 204 ? B SER 204 
139 1 Y 1 B TRP 205 ? B TRP 205 
140 1 Y 1 B THR 206 ? B THR 206 
141 1 Y 1 B VAL 207 ? B VAL 207 
142 1 Y 1 B ILE 208 ? B ILE 208 
143 1 Y 1 B ASN 209 ? B ASN 209 
144 1 Y 1 B TRP 210 ? B TRP 210 
145 1 Y 1 B ILE 211 ? B ILE 211 
146 1 Y 1 B TYR 212 ? B TYR 212 
147 1 Y 1 B ASN 213 ? B ASN 213 
148 1 Y 1 B ASN 214 ? B ASN 214 
149 1 Y 1 B GLY 215 ? B GLY 215 
150 1 Y 1 B ALA 216 ? B ALA 216 
151 1 Y 1 B ALA 217 ? B ALA 217 
152 1 Y 1 B VAL 218 ? B VAL 218 
153 1 Y 1 B GLY 219 ? B GLY 219 
154 1 Y 1 B GLY 220 ? B GLY 220 
155 1 Y 1 B GLU 221 ? B GLU 221 
156 1 Y 1 B GLN 222 ? B GLN 222 
157 1 Y 1 B VAL 223 ? B VAL 223 
158 1 Y 1 B ILE 224 ? B ILE 224 
159 1 Y 1 B VAL 225 ? B VAL 225 
160 1 Y 1 B ILE 226 ? B ILE 226 
161 1 Y 1 B PRO 227 ? B PRO 227 
162 1 Y 1 B TYR 228 ? B TYR 228 
163 1 Y 1 B THR 229 ? B THR 229 
164 1 Y 1 B PHE 230 ? B PHE 230 
165 1 Y 1 B GLN 231 ? B GLN 231 
166 1 Y 1 B THR 232 ? B THR 232 
167 1 Y 1 B VAL 233 ? B VAL 233 
168 1 Y 1 B PRO 234 ? B PRO 234 
169 1 Y 1 B ALA 235 ? B ALA 235 
170 1 Y 1 B ILE 236 ? B ILE 236 
171 1 Y 1 B PHE 237 ? B PHE 237 
172 1 Y 1 B LYS 238 ? B LYS 238 
173 1 Y 1 B ASN 239 ? B ASN 239 
174 1 Y 1 B GLY 240 ? B GLY 240 
175 1 Y 1 B LEU 241 ? B LEU 241 
176 1 Y 1 B ARG 242 ? B ARG 242 
177 1 Y 1 B TYR 243 ? B TYR 243 
178 1 Y 1 B GLN 244 ? B GLN 244 
179 1 Y 1 B GLY 245 ? B GLY 245 
180 1 Y 1 B GLY 246 ? B GLY 246 
181 1 Y 1 B LEU 247 ? B LEU 247 
182 1 Y 1 B SER 248 ? B SER 248 
183 1 Y 1 B THR 249 ? B THR 249 
184 1 Y 1 B GLN 250 ? B GLN 250 
185 1 Y 1 B SER 251 ? B SER 251 
186 1 Y 1 B TYR 252 ? B TYR 252 
187 1 Y 1 B THR 253 ? B THR 253 
188 1 Y 1 B VAL 254 ? B VAL 254 
189 1 Y 1 B ASP 255 ? B ASP 255 
190 1 Y 1 B GLN 256 ? B GLN 256 
191 1 Y 1 B ASP 257 ? B ASP 257 
192 1 Y 1 B ASN 258 ? B ASN 258 
193 1 Y 1 B LYS 259 ? B LYS 259 
194 1 Y 1 B ARG 260 ? B ARG 260 
195 1 Y 1 B ILE 261 ? B ILE 261 
196 1 Y 1 B LEU 262 ? B LEU 262 
197 1 Y 1 B LEU 263 ? B LEU 263 
198 1 Y 1 B THR 264 ? B THR 264 
199 1 Y 1 B GLU 265 ? B GLU 265 
200 1 Y 1 B PRO 266 ? B PRO 266 
201 1 Y 1 B LEU 267 ? B LEU 267 
202 1 Y 1 B SER 268 ? B SER 268 
203 1 Y 1 B THR 269 ? B THR 269 
204 1 Y 1 B ASN 270 ? B ASN 270 
205 1 Y 1 B ASP 271 ? B ASP 271 
206 1 Y 1 B ARG 272 ? B ARG 272 
207 1 Y 1 B LEU 273 ? B LEU 273 
208 1 Y 1 B VAL 274 ? B VAL 274 
209 1 Y 1 B VAL 275 ? B VAL 275 
210 1 Y 1 B GLN 276 ? B GLN 276 
211 1 Y 1 B LEU 277 ? B LEU 277 
212 1 Y 1 B GLY 278 ? B GLY 278 
213 1 Y 1 B GLY 279 ? B GLY 279 
214 1 Y 1 B GLU 280 ? B GLU 280 
215 1 Y 1 B LEU 281 ? B LEU 281 
216 1 Y 1 B VAL 282 ? B VAL 282 
217 1 Y 1 B THR 283 ? B THR 283 
218 1 Y 1 B LEU 284 ? B LEU 284 
219 1 Y 1 B GLU 285 ? B GLU 285 
220 1 Y 1 B SER 286 ? B SER 286 
221 1 Y 1 B PRO 287 ? B PRO 287 
222 1 Y 1 B ASP 288 ? B ASP 288 
223 1 Y 1 B ARG 289 ? B ARG 289 
224 1 Y 1 B SER 290 ? B SER 290 
225 1 Y 1 B LEU 291 ? B LEU 291 
226 1 Y 1 B TYR 292 ? B TYR 292 
227 1 Y 1 B GLU 293 ? B GLU 293 
228 1 Y 1 B ILE 294 ? B ILE 294 
229 1 Y 1 B ALA 295 ? B ALA 295 
230 1 Y 1 B ARG 296 ? B ARG 296 
231 1 Y 1 B ALA 297 ? B ALA 297 
232 1 Y 1 B THR 298 ? B THR 298 
233 1 Y 1 B ASN 299 ? B ASN 299 
234 1 Y 1 B MET 300 ? B MET 300 
235 1 Y 1 B LYS 301 ? B LYS 301 
236 1 Y 1 B ASP 302 ? B ASP 302 
237 1 Y 1 B SER 303 ? B SER 303 
238 1 Y 1 B GLU 304 ? B GLU 304 
239 1 Y 1 B VAL 305 ? B VAL 305 
240 1 Y 1 B ILE 306 ? B ILE 306 
241 1 Y 1 B LYS 307 ? B LYS 307 
242 1 Y 1 B SER 308 ? B SER 308 
243 1 Y 1 B ASP 309 ? B ASP 309 
244 1 Y 1 B ASN 310 ? B ASN 310 
245 1 Y 1 B THR 311 ? B THR 311 
246 1 Y 1 B VAL 312 ? B VAL 312 
247 1 Y 1 B GLU 313 ? B GLU 313 
248 1 Y 1 B THR 314 ? B THR 314 
249 1 Y 1 B LEU 315 ? B LEU 315 
250 1 Y 1 B ASN 316 ? B ASN 316 
251 1 Y 1 B GLY 317 ? B GLY 317 
252 1 Y 1 B LYS 318 ? B LYS 318 
253 1 Y 1 B ARG 319 ? B ARG 319 
254 1 Y 1 B ILE 320 ? B ILE 320 
255 1 Y 1 B LEU 321 ? B LEU 321 
256 1 Y 1 B TYR 322 ? B TYR 322 
257 1 Y 1 B ASP 323 ? B ASP 323 
258 1 Y 1 B ILE 324 ? B ILE 324 
259 1 Y 1 B VAL 325 ? B VAL 325 
260 1 Y 1 B SER 326 ? B SER 326 
261 1 Y 1 B GLN 327 ? B GLN 327 
262 1 Y 1 B VAL 328 ? B VAL 328 
263 1 Y 1 B TYR 329 ? B TYR 329 
264 1 Y 1 B TYR 330 ? B TYR 330 
265 1 Y 1 B TRP 331 ? B TRP 331 
266 1 Y 1 B ILE 332 ? B ILE 332 
267 1 Y 1 B PRO 333 ? B PRO 333 
268 1 Y 1 B SER 334 ? B SER 334 
269 1 Y 1 B SER 335 ? B SER 335 
270 1 Y 1 B VAL 336 ? B VAL 336 
271 1 Y 1 B PRO 337 ? B PRO 337 
272 1 Y 1 B ASN 338 ? B ASN 338 
273 1 Y 1 B ASN 339 ? B ASN 339 
274 1 Y 1 B VAL 340 ? B VAL 340 
275 1 Y 1 B TYR 341 ? B TYR 341 
276 1 Y 1 B ILE 342 ? B ILE 342 
277 1 Y 1 B GLN 343 ? B GLN 343 
278 1 Y 1 B SER 344 ? B SER 344 
279 1 Y 1 B VAL 345 ? B VAL 345 
280 1 Y 1 B VAL 346 ? B VAL 346 
281 1 Y 1 B ASN 347 ? B ASN 347 
282 1 Y 1 B GLY 348 ? B GLY 348 
283 1 Y 1 B GLN 349 ? B GLN 349 
284 1 Y 1 B LEU 350 ? B LEU 350 
285 1 Y 1 B THR 351 ? B THR 351 
286 1 Y 1 B TYR 352 ? B TYR 352 
287 1 Y 1 B LEU 353 ? B LEU 353 
288 1 Y 1 B PRO 354 ? B PRO 354 
289 1 Y 1 B GLY 355 ? B GLY 355 
290 1 Y 1 B ASN 356 ? B ASN 356 
291 1 Y 1 B ILE 357 ? B ILE 357 
292 1 Y 1 B VAL 358 ? B VAL 358 
293 1 Y 1 B VAL 359 ? B VAL 359 
294 1 Y 1 B THR 360 ? B THR 360 
295 1 Y 1 B LEU 361 ? B LEU 361 
296 1 Y 1 B THR 362 ? B THR 362 
297 1 Y 1 B PRO 363 ? B PRO 363 
298 1 Y 1 B ILE 364 ? B ILE 364 
299 1 Y 1 B VAL 365 ? B VAL 365 
300 1 Y 1 B THR 366 ? B THR 366 
301 1 Y 1 B LEU 367 ? B LEU 367 
302 1 Y 1 B GLY 368 ? B GLY 368 
303 1 Y 1 B LEU 369 ? B LEU 369 
304 1 Y 1 B SER 370 ? B SER 370 
305 1 Y 1 B GLY 371 ? B GLY 371 
306 1 Y 1 B THR 372 ? B THR 372 
307 1 Y 1 B THR 373 ? B THR 373 
308 1 Y 1 B ALA 374 ? B ALA 374 
309 1 Y 1 B GLN 375 ? B GLN 375 
310 1 Y 1 B ARG 376 ? B ARG 376 
311 1 Y 1 B PRO 377 ? B PRO 377 
312 1 Y 1 B ILE 378 ? B ILE 378 
313 1 Y 1 B GLY 379 ? B GLY 379 
314 1 Y 1 B VAL 380 ? B VAL 380 
315 1 Y 1 B LEU 381 ? B LEU 381 
316 1 Y 1 B THR 382 ? B THR 382 
317 1 Y 1 B GLY 383 ? B GLY 383 
318 1 Y 1 B THR 384 ? B THR 384 
319 1 Y 1 B GLN 385 ? B GLN 385 
320 1 Y 1 B HIS 386 ? B HIS 386 
321 1 Y 1 B PHE 387 ? B PHE 387 
322 1 Y 1 B ASP 388 ? B ASP 388 
323 1 Y 1 B THR 389 ? B THR 389 
324 1 Y 1 B THR 390 ? B THR 390 
325 1 Y 1 B LEU 391 ? B LEU 391 
326 1 Y 1 B GLY 392 ? B GLY 392 
327 1 Y 1 B LYS 393 ? B LYS 393 
328 1 Y 1 B PRO 394 ? B PRO 394 
329 1 Y 1 B ILE 395 ? B ILE 395 
330 1 Y 1 B TRP 396 ? B TRP 396 
331 1 Y 1 B PHE 397 ? B PHE 397 
332 1 Y 1 B ASN 398 ? B ASN 398 
333 1 Y 1 B GLY 399 ? B GLY 399 
334 1 Y 1 B THR 400 ? B THR 400 
335 1 Y 1 B ALA 401 ? B ALA 401 
336 1 Y 1 B TRP 402 ? B TRP 402 
337 1 Y 1 B VAL 403 ? B VAL 403 
338 1 Y 1 B ASP 404 ? B ASP 404 
339 1 Y 1 B SER 405 ? B SER 405 
340 1 Y 1 B THR 406 ? B THR 406 
341 1 Y 1 B GLY 407 ? B GLY 407 
342 1 Y 1 B ALA 408 ? B ALA 408 
343 1 Y 1 B VAL 409 ? B VAL 409 
344 1 Y 1 B VAL 410 ? B VAL 410 
# 
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 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-18 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9D84 
_em_admin.last_update        2025-01-15 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'Shigella flexneri bacteriophage B2 Gp48 and Gp49' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 10 mM ?     1 'tris(hydroxymethyl)aminomethane' 
1 10 mM MgCl2 2 'magnesium chloride'              
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          2968270 
_em_entity_assembly_naturalsource.organism             'Shigella phage B2' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         43.14 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_em_virus_natural_host.entity_assembly_id   1 
_em_virus_natural_host.id                   1 
_em_virus_natural_host.ncbi_tax_id          198215 
_em_virus_natural_host.organism             'Shigella flexneri 2a str. 2457T' 
_em_virus_natural_host.strain               ? 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM110185 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM116789 2 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM140803 3 
'National Science Foundation (NSF, United States)'                                         'United States' 1750125  4 
# 
_atom_sites.entry_id                    9D84 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
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   . LEU A 1 4   ? 4.374   -13.995 -58.206 1.00 99.86  ? 4   LEU A N   1 
ATOM 2    C CA  . LEU A 1 4   ? 3.393   -12.999 -57.813 1.00 97.23  ? 4   LEU A CA  1 
ATOM 3    C C   . LEU A 1 4   ? 3.135   -12.048 -58.977 1.00 98.03  ? 4   LEU A C   1 
ATOM 4    O O   . LEU A 1 4   ? 3.953   -11.916 -59.890 1.00 98.00  ? 4   LEU A O   1 
ATOM 5    C CB  . LEU A 1 4   ? 3.887   -12.210 -56.596 1.00 94.72  ? 4   LEU A CB  1 
ATOM 6    C CG  . LEU A 1 4   ? 3.420   -12.601 -55.187 1.00 96.46  ? 4   LEU A CG  1 
ATOM 7    C CD1 . LEU A 1 4   ? 3.638   -11.454 -54.204 1.00 95.52  ? 4   LEU A CD1 1 
ATOM 8    C CD2 . LEU A 1 4   ? 1.994   -13.122 -55.134 1.00 95.50  ? 4   LEU A CD2 1 
ATOM 9    N N   . PHE A 1 5   ? 1.984   -11.382 -58.939 1.00 94.22  ? 5   PHE A N   1 
ATOM 10   C CA  . PHE A 1 5   ? 1.736   -10.302 -59.881 1.00 92.00  ? 5   PHE A CA  1 
ATOM 11   C C   . PHE A 1 5   ? 2.688   -9.143  -59.620 1.00 93.12  ? 5   PHE A C   1 
ATOM 12   O O   . PHE A 1 5   ? 3.196   -8.963  -58.510 1.00 96.82  ? 5   PHE A O   1 
ATOM 13   C CB  . PHE A 1 5   ? 0.294   -9.791  -59.801 1.00 91.69  ? 5   PHE A CB  1 
ATOM 14   C CG  . PHE A 1 5   ? -0.689  -10.598 -60.597 1.00 91.85  ? 5   PHE A CG  1 
ATOM 15   C CD1 . PHE A 1 5   ? -0.431  -10.923 -61.917 1.00 90.97  ? 5   PHE A CD1 1 
ATOM 16   C CD2 . PHE A 1 5   ? -1.900  -10.979 -60.047 1.00 91.13  ? 5   PHE A CD2 1 
ATOM 17   C CE1 . PHE A 1 5   ? -1.340  -11.650 -62.658 1.00 89.96  ? 5   PHE A CE1 1 
ATOM 18   C CE2 . PHE A 1 5   ? -2.816  -11.701 -60.785 1.00 90.19  ? 5   PHE A CE2 1 
ATOM 19   C CZ  . PHE A 1 5   ? -2.535  -12.038 -62.091 1.00 89.59  ? 5   PHE A CZ  1 
ATOM 20   N N   . SER A 1 6   ? 2.929   -8.359  -60.665 1.00 88.70  ? 6   SER A N   1 
ATOM 21   C CA  . SER A 1 6   ? 3.777   -7.181  -60.566 1.00 90.36  ? 6   SER A CA  1 
ATOM 22   C C   . SER A 1 6   ? 2.977   -6.001  -60.025 1.00 93.15  ? 6   SER A C   1 
ATOM 23   O O   . SER A 1 6   ? 2.439   -5.205  -60.800 1.00 96.81  ? 6   SER A O   1 
ATOM 24   C CB  . SER A 1 6   ? 4.382   -6.864  -61.933 1.00 87.07  ? 6   SER A CB  1 
ATOM 25   O OG  . SER A 1 6   ? 4.733   -5.503  -62.039 1.00 92.02  ? 6   SER A OG  1 
ATOM 26   N N   . GLN A 1 7   ? 2.894   -5.879  -58.698 1.00 87.49  ? 7   GLN A N   1 
ATOM 27   C CA  . GLN A 1 7   ? 1.983   -4.928  -58.070 1.00 83.20  ? 7   GLN A CA  1 
ATOM 28   C C   . GLN A 1 7   ? 2.674   -3.698  -57.498 1.00 88.54  ? 7   GLN A C   1 
ATOM 29   O O   . GLN A 1 7   ? 2.076   -2.974  -56.695 1.00 91.30  ? 7   GLN A O   1 
ATOM 30   C CB  . GLN A 1 7   ? 1.198   -5.601  -56.947 1.00 85.15  ? 7   GLN A CB  1 
ATOM 31   C CG  . GLN A 1 7   ? 1.024   -7.087  -57.089 1.00 84.61  ? 7   GLN A CG  1 
ATOM 32   C CD  . GLN A 1 7   ? 0.428   -7.692  -55.844 1.00 90.76  ? 7   GLN A CD  1 
ATOM 33   O OE1 . GLN A 1 7   ? 0.562   -7.145  -54.751 1.00 93.87  ? 7   GLN A OE1 1 
ATOM 34   N NE2 . GLN A 1 7   ? -0.253  -8.813  -56.002 1.00 91.69  ? 7   GLN A NE2 1 
ATOM 35   N N   . GLY A 1 8   ? 3.925   -3.462  -57.869 1.00 90.16  ? 8   GLY A N   1 
ATOM 36   C CA  . GLY A 1 8   ? 4.604   -2.254  -57.449 1.00 89.91  ? 8   GLY A CA  1 
ATOM 37   C C   . GLY A 1 8   ? 4.740   -2.080  -55.951 1.00 91.50  ? 8   GLY A C   1 
ATOM 38   O O   . GLY A 1 8   ? 4.681   -0.957  -55.442 1.00 96.93  ? 8   GLY A O   1 
ATOM 39   N N   . GLY A 1 9   ? 4.919   -3.182  -55.231 1.00 79.14  ? 9   GLY A N   1 
ATOM 40   C CA  . GLY A 1 9   ? 5.181   -3.112  -53.809 1.00 77.86  ? 9   GLY A CA  1 
ATOM 41   C C   . GLY A 1 9   ? 6.622   -3.463  -53.515 1.00 86.02  ? 9   GLY A C   1 
ATOM 42   O O   . GLY A 1 9   ? 7.062   -3.451  -52.363 1.00 85.11  ? 9   GLY A O   1 
ATOM 43   N N   . LYS A 1 10  ? 7.365   -3.783  -54.571 1.00 95.24  ? 10  LYS A N   1 
ATOM 44   C CA  . LYS A 1 10  ? 8.741   -4.230  -54.446 1.00 91.99  ? 10  LYS A CA  1 
ATOM 45   C C   . LYS A 1 10  ? 9.714   -3.114  -54.812 1.00 92.46  ? 10  LYS A C   1 
ATOM 46   O O   . LYS A 1 10  ? 9.502   -2.347  -55.756 1.00 92.08  ? 10  LYS A O   1 
ATOM 47   C CB  . LYS A 1 10  ? 8.992   -5.441  -55.345 1.00 90.22  ? 10  LYS A CB  1 
ATOM 48   C CG  . LYS A 1 10  ? 8.783   -6.786  -54.669 1.00 91.66  ? 10  LYS A CG  1 
ATOM 49   C CD  . LYS A 1 10  ? 8.892   -7.950  -55.656 1.00 93.13  ? 10  LYS A CD  1 
ATOM 50   C CE  . LYS A 1 10  ? 9.935   -7.728  -56.751 1.00 91.79  ? 10  LYS A CE  1 
ATOM 51   N NZ  . LYS A 1 10  ? 11.280  -7.326  -56.239 1.00 94.25  ? 10  LYS A NZ  1 
ATOM 52   N N   . GLY A 1 11  ? 10.797  -3.037  -54.042 1.00 88.93  ? 11  GLY A N   1 
ATOM 53   C CA  . GLY A 1 11  ? 11.930  -2.190  -54.361 1.00 88.75  ? 11  GLY A CA  1 
ATOM 54   C C   . GLY A 1 11  ? 11.620  -0.730  -54.611 1.00 88.74  ? 11  GLY A C   1 
ATOM 55   O O   . GLY A 1 11  ? 10.942  -0.080  -53.811 1.00 88.79  ? 11  GLY A O   1 
ATOM 56   N N   . SER A 1 12  ? 12.115  -0.209  -55.734 1.00 85.17  ? 12  SER A N   1 
ATOM 57   C CA  . SER A 1 12  ? 12.019  1.210   -56.044 1.00 84.70  ? 12  SER A CA  1 
ATOM 58   C C   . SER A 1 12  ? 10.596  1.678   -56.307 1.00 88.94  ? 12  SER A C   1 
ATOM 59   O O   . SER A 1 12  ? 10.303  2.858   -56.093 1.00 92.16  ? 12  SER A O   1 
ATOM 60   C CB  . SER A 1 12  ? 12.888  1.542   -57.262 1.00 86.36  ? 12  SER A CB  1 
ATOM 61   O OG  . SER A 1 12  ? 12.588  0.684   -58.348 1.00 89.04  ? 12  SER A OG  1 
ATOM 62   N N   . ALA A 1 13  ? 9.712   0.794   -56.758 1.00 86.41  ? 13  ALA A N   1 
ATOM 63   C CA  . ALA A 1 13  ? 8.341   1.177   -57.058 1.00 83.87  ? 13  ALA A CA  1 
ATOM 64   C C   . ALA A 1 13  ? 7.421   1.101   -55.848 1.00 87.34  ? 13  ALA A C   1 
ATOM 65   O O   . ALA A 1 13  ? 6.241   1.449   -55.965 1.00 90.87  ? 13  ALA A O   1 
ATOM 66   C CB  . ALA A 1 13  ? 7.781   0.303   -58.181 1.00 82.28  ? 13  ALA A CB  1 
ATOM 67   N N   . GLY A 1 14  ? 7.920   0.648   -54.705 1.00 80.55  ? 14  GLY A N   1 
ATOM 68   C CA  . GLY A 1 14  ? 7.149   0.606   -53.484 1.00 79.09  ? 14  GLY A CA  1 
ATOM 69   C C   . GLY A 1 14  ? 7.469   1.690   -52.482 1.00 77.54  ? 14  GLY A C   1 
ATOM 70   O O   . GLY A 1 14  ? 7.042   1.588   -51.328 1.00 81.25  ? 14  GLY A O   1 
ATOM 71   N N   . ILE A 1 15  ? 8.208   2.728   -52.882 1.00 73.95  ? 15  ILE A N   1 
ATOM 72   C CA  . ILE A 1 15  ? 8.615   3.763   -51.935 1.00 74.59  ? 15  ILE A CA  1 
ATOM 73   C C   . ILE A 1 15  ? 7.403   4.526   -51.413 1.00 77.48  ? 15  ILE A C   1 
ATOM 74   O O   . ILE A 1 15  ? 7.286   4.772   -50.208 1.00 78.40  ? 15  ILE A O   1 
ATOM 75   C CB  . ILE A 1 15  ? 9.650   4.706   -52.579 1.00 75.63  ? 15  ILE A CB  1 
ATOM 76   C CG1 . ILE A 1 15  ? 11.074  4.244   -52.268 1.00 73.54  ? 15  ILE A CG1 1 
ATOM 77   C CG2 . ILE A 1 15  ? 9.463   6.138   -52.096 1.00 76.47  ? 15  ILE A CG2 1 
ATOM 78   C CD1 . ILE A 1 15  ? 11.436  2.907   -52.848 1.00 75.40  ? 15  ILE A CD1 1 
ATOM 79   N N   . LEU A 1 16  ? 6.480   4.906   -52.300 1.00 70.80  ? 16  LEU A N   1 
ATOM 80   C CA  . LEU A 1 16  ? 5.373   5.760   -51.883 1.00 66.19  ? 16  LEU A CA  1 
ATOM 81   C C   . LEU A 1 16  ? 4.355   5.006   -51.036 1.00 70.09  ? 16  LEU A C   1 
ATOM 82   O O   . LEU A 1 16  ? 3.859   5.542   -50.039 1.00 73.21  ? 16  LEU A O   1 
ATOM 83   C CB  . LEU A 1 16  ? 4.698   6.377   -53.107 1.00 69.17  ? 16  LEU A CB  1 
ATOM 84   C CG  . LEU A 1 16  ? 5.465   7.531   -53.755 1.00 69.16  ? 16  LEU A CG  1 
ATOM 85   C CD1 . LEU A 1 16  ? 4.682   8.110   -54.921 1.00 71.87  ? 16  LEU A CD1 1 
ATOM 86   C CD2 . LEU A 1 16  ? 5.781   8.604   -52.728 1.00 64.62  ? 16  LEU A CD2 1 
ATOM 87   N N   . THR A 1 17  ? 4.024   3.771   -51.412 1.00 72.14  ? 17  THR A N   1 
ATOM 88   C CA  . THR A 1 17  ? 3.090   2.988   -50.610 1.00 67.52  ? 17  THR A CA  1 
ATOM 89   C C   . THR A 1 17  ? 3.691   2.640   -49.253 1.00 64.69  ? 17  THR A C   1 
ATOM 90   O O   . THR A 1 17  ? 2.995   2.655   -48.231 1.00 69.52  ? 17  THR A O   1 
ATOM 91   C CB  . THR A 1 17  ? 2.684   1.723   -51.362 1.00 69.85  ? 17  THR A CB  1 
ATOM 92   O OG1 . THR A 1 17  ? 3.856   1.067   -51.861 1.00 79.41  ? 17  THR A OG1 1 
ATOM 93   C CG2 . THR A 1 17  ? 1.785   2.081   -52.530 1.00 67.30  ? 17  THR A CG2 1 
ATOM 94   N N   . ASN A 1 18  ? 4.987   2.324   -49.224 1.00 66.43  ? 18  ASN A N   1 
ATOM 95   C CA  . ASN A 1 18  ? 5.655   2.078   -47.953 1.00 67.08  ? 18  ASN A CA  1 
ATOM 96   C C   . ASN A 1 18  ? 5.684   3.336   -47.096 1.00 72.57  ? 18  ASN A C   1 
ATOM 97   O O   . ASN A 1 18  ? 5.541   3.263   -45.870 1.00 79.03  ? 18  ASN A O   1 
ATOM 98   C CB  . ASN A 1 18  ? 7.070   1.561   -48.191 1.00 66.28  ? 18  ASN A CB  1 
ATOM 99   C CG  . ASN A 1 18  ? 7.749   1.125   -46.917 1.00 69.59  ? 18  ASN A CG  1 
ATOM 100  O OD1 . ASN A 1 18  ? 7.094   0.742   -45.949 1.00 76.18  ? 18  ASN A OD1 1 
ATOM 101  N ND2 . ASN A 1 18  ? 9.072   1.188   -46.903 1.00 74.25  ? 18  ASN A ND2 1 
ATOM 102  N N   . LYS A 1 19  ? 5.880   4.498   -47.721 1.00 69.16  ? 19  LYS A N   1 
ATOM 103  C CA  . LYS A 1 19  ? 5.811   5.754   -46.982 1.00 67.48  ? 19  LYS A CA  1 
ATOM 104  C C   . LYS A 1 19  ? 4.417   5.989   -46.420 1.00 70.55  ? 19  LYS A C   1 
ATOM 105  O O   . LYS A 1 19  ? 4.284   6.466   -45.291 1.00 75.71  ? 19  LYS A O   1 
ATOM 106  C CB  . LYS A 1 19  ? 6.226   6.918   -47.881 1.00 67.31  ? 19  LYS A CB  1 
ATOM 107  C CG  . LYS A 1 19  ? 7.727   7.068   -48.041 1.00 69.45  ? 19  LYS A CG  1 
ATOM 108  C CD  . LYS A 1 19  ? 8.076   8.303   -48.849 1.00 68.91  ? 19  LYS A CD  1 
ATOM 109  C CE  . LYS A 1 19  ? 9.579   8.486   -48.945 1.00 69.01  ? 19  LYS A CE  1 
ATOM 110  N NZ  . LYS A 1 19  ? 9.937   9.766   -49.613 1.00 71.15  ? 19  LYS A NZ  1 
ATOM 111  N N   . GLN A 1 20  ? 3.376   5.666   -47.189 1.00 70.36  ? 20  GLN A N   1 
ATOM 112  C CA  . GLN A 1 20  ? 2.013   5.747   -46.673 1.00 65.89  ? 20  GLN A CA  1 
ATOM 113  C C   . GLN A 1 20  ? 1.836   4.850   -45.457 1.00 72.71  ? 20  GLN A C   1 
ATOM 114  O O   . GLN A 1 20  ? 1.264   5.262   -44.441 1.00 73.29  ? 20  GLN A O   1 
ATOM 115  C CB  . GLN A 1 20  ? 1.013   5.358   -47.762 1.00 60.95  ? 20  GLN A CB  1 
ATOM 116  C CG  . GLN A 1 20  ? 0.579   6.489   -48.665 1.00 71.48  ? 20  GLN A CG  1 
ATOM 117  C CD  . GLN A 1 20  ? -0.411  6.031   -49.715 1.00 76.51  ? 20  GLN A CD  1 
ATOM 118  O OE1 . GLN A 1 20  ? -0.672  4.837   -49.857 1.00 74.80  ? 20  GLN A OE1 1 
ATOM 119  N NE2 . GLN A 1 20  ? -0.974  6.979   -50.453 1.00 77.24  ? 20  GLN A NE2 1 
ATOM 120  N N   . ALA A 1 21  ? 2.319   3.609   -45.548 1.00 68.66  ? 21  ALA A N   1 
ATOM 121  C CA  . ALA A 1 21  ? 2.177   2.671   -44.439 1.00 60.42  ? 21  ALA A CA  1 
ATOM 122  C C   . ALA A 1 21  ? 2.915   3.166   -43.201 1.00 62.02  ? 21  ALA A C   1 
ATOM 123  O O   . ALA A 1 21  ? 2.386   3.117   -42.085 1.00 71.63  ? 21  ALA A O   1 
ATOM 124  C CB  . ALA A 1 21  ? 2.686   1.291   -44.855 1.00 57.52  ? 21  ALA A CB  1 
ATOM 125  N N   . VAL A 1 22  ? 4.141   3.659   -43.386 1.00 58.12  ? 22  VAL A N   1 
ATOM 126  C CA  . VAL A 1 22  ? 4.929   4.158   -42.262 1.00 62.28  ? 22  VAL A CA  1 
ATOM 127  C C   . VAL A 1 22  ? 4.266   5.382   -41.644 1.00 67.83  ? 22  VAL A C   1 
ATOM 128  O O   . VAL A 1 22  ? 4.194   5.514   -40.416 1.00 71.10  ? 22  VAL A O   1 
ATOM 129  C CB  . VAL A 1 22  ? 6.369   4.461   -42.716 1.00 61.75  ? 22  VAL A CB  1 
ATOM 130  C CG1 . VAL A 1 22  ? 7.110   5.242   -41.649 1.00 65.24  ? 22  VAL A CG1 1 
ATOM 131  C CG2 . VAL A 1 22  ? 7.103   3.172   -43.037 1.00 59.36  ? 22  VAL A CG2 1 
ATOM 132  N N   . ALA A 1 23  ? 3.773   6.295   -42.482 1.00 64.22  ? 23  ALA A N   1 
ATOM 133  C CA  . ALA A 1 23  ? 3.120   7.496   -41.976 1.00 62.28  ? 23  ALA A CA  1 
ATOM 134  C C   . ALA A 1 23  ? 1.861   7.154   -41.193 1.00 64.95  ? 23  ALA A C   1 
ATOM 135  O O   . ALA A 1 23  ? 1.601   7.741   -40.137 1.00 71.57  ? 23  ALA A O   1 
ATOM 136  C CB  . ALA A 1 23  ? 2.797   8.435   -43.136 1.00 58.05  ? 23  ALA A CB  1 
ATOM 137  N N   . ARG A 1 24  ? 1.067   6.207   -41.693 1.00 62.84  ? 24  ARG A N   1 
ATOM 138  C CA  . ARG A 1 24  ? -0.119  5.775   -40.968 1.00 63.96  ? 24  ARG A CA  1 
ATOM 139  C C   . ARG A 1 24  ? 0.224   5.068   -39.667 1.00 62.87  ? 24  ARG A C   1 
ATOM 140  O O   . ARG A 1 24  ? -0.497  5.231   -38.679 1.00 66.38  ? 24  ARG A O   1 
ATOM 141  C CB  . ARG A 1 24  ? -0.972  4.864   -41.851 1.00 60.28  ? 24  ARG A CB  1 
ATOM 142  C CG  . ARG A 1 24  ? -1.634  5.581   -43.015 1.00 57.90  ? 24  ARG A CG  1 
ATOM 143  C CD  . ARG A 1 24  ? -2.264  6.899   -42.583 1.00 60.67  ? 24  ARG A CD  1 
ATOM 144  N NE  . ARG A 1 24  ? -1.425  8.060   -42.868 1.00 65.64  ? 24  ARG A NE  1 
ATOM 145  C CZ  . ARG A 1 24  ? -1.057  8.458   -44.078 1.00 62.61  ? 24  ARG A CZ  1 
ATOM 146  N NH1 . ARG A 1 24  ? -1.464  7.831   -45.170 1.00 66.70  ? 24  ARG A NH1 1 
ATOM 147  N NH2 . ARG A 1 24  ? -0.269  9.522   -44.199 1.00 62.68  ? 24  ARG A NH2 1 
ATOM 148  N N   . HIS A 1 25  ? 1.307   4.290   -39.646 1.00 63.87  ? 25  HIS A N   1 
ATOM 149  C CA  . HIS A 1 25  ? 1.754   3.669   -38.406 1.00 63.73  ? 25  HIS A CA  1 
ATOM 150  C C   . HIS A 1 25  ? 2.215   4.701   -37.386 1.00 65.22  ? 25  HIS A C   1 
ATOM 151  O O   . HIS A 1 25  ? 1.954   4.542   -36.189 1.00 67.38  ? 25  HIS A O   1 
ATOM 152  C CB  . HIS A 1 25  ? 2.883   2.680   -38.694 1.00 58.15  ? 25  HIS A CB  1 
ATOM 153  C CG  . HIS A 1 25  ? 3.350   1.931   -37.487 1.00 64.14  ? 25  HIS A CG  1 
ATOM 154  N ND1 . HIS A 1 25  ? 2.572   0.992   -36.846 1.00 65.77  ? 25  HIS A ND1 1 
ATOM 155  C CD2 . HIS A 1 25  ? 4.516   1.983   -36.802 1.00 63.56  ? 25  HIS A CD2 1 
ATOM 156  C CE1 . HIS A 1 25  ? 3.238   0.497   -35.820 1.00 66.17  ? 25  HIS A CE1 1 
ATOM 157  N NE2 . HIS A 1 25  ? 4.421   1.082   -35.770 1.00 68.18  ? 25  HIS A NE2 1 
ATOM 158  N N   . PHE A 1 26  ? 2.899   5.753   -37.833 1.00 63.86  ? 26  PHE A N   1 
ATOM 159  C CA  . PHE A 1 26  ? 3.433   6.774   -36.944 1.00 62.93  ? 26  PHE A CA  1 
ATOM 160  C C   . PHE A 1 26  ? 2.515   7.975   -36.776 1.00 63.08  ? 26  PHE A C   1 
ATOM 161  O O   . PHE A 1 26  ? 2.820   8.855   -35.964 1.00 70.14  ? 26  PHE A O   1 
ATOM 162  C CB  . PHE A 1 26  ? 4.797   7.249   -37.455 1.00 61.12  ? 26  PHE A CB  1 
ATOM 163  C CG  . PHE A 1 26  ? 5.922   6.316   -37.124 1.00 63.53  ? 26  PHE A CG  1 
ATOM 164  C CD1 . PHE A 1 26  ? 6.489   6.315   -35.864 1.00 62.50  ? 26  PHE A CD1 1 
ATOM 165  C CD2 . PHE A 1 26  ? 6.397   5.425   -38.067 1.00 64.37  ? 26  PHE A CD2 1 
ATOM 166  C CE1 . PHE A 1 26  ? 7.521   5.455   -35.556 1.00 65.19  ? 26  PHE A CE1 1 
ATOM 167  C CE2 . PHE A 1 26  ? 7.426   4.561   -37.762 1.00 64.27  ? 26  PHE A CE2 1 
ATOM 168  C CZ  . PHE A 1 26  ? 7.988   4.576   -36.506 1.00 64.34  ? 26  PHE A CZ  1 
ATOM 169  N N   . GLY A 1 27  ? 1.406   8.037   -37.507 1.00 62.17  ? 27  GLY A N   1 
ATOM 170  C CA  . GLY A 1 27  ? 0.512   9.172   -37.396 1.00 61.61  ? 27  GLY A CA  1 
ATOM 171  C C   . GLY A 1 27  ? 1.052   10.455  -37.981 1.00 66.00  ? 27  GLY A C   1 
ATOM 172  O O   . GLY A 1 27  ? 0.619   11.540  -37.584 1.00 69.93  ? 27  GLY A O   1 
ATOM 173  N N   . VAL A 1 28  ? 1.990   10.363  -38.922 1.00 67.02  ? 28  VAL A N   1 
ATOM 174  C CA  . VAL A 1 28  ? 2.587   11.540  -39.541 1.00 65.86  ? 28  VAL A CA  1 
ATOM 175  C C   . VAL A 1 28  ? 2.142   11.609  -40.995 1.00 66.21  ? 28  VAL A C   1 
ATOM 176  O O   . VAL A 1 28  ? 1.430   10.723  -41.478 1.00 68.51  ? 28  VAL A O   1 
ATOM 177  C CB  . VAL A 1 28  ? 4.122   11.513  -39.431 1.00 65.94  ? 28  VAL A CB  1 
ATOM 178  C CG1 . VAL A 1 28  ? 4.551   11.621  -37.979 1.00 65.49  ? 28  VAL A CG1 1 
ATOM 179  C CG2 . VAL A 1 28  ? 4.676   10.249  -40.064 1.00 66.63  ? 28  VAL A CG2 1 
ATOM 180  N N   . LYS A 1 29  ? 2.532   12.670  -41.692 1.00 76.12  ? 29  LYS A N   1 
ATOM 181  C CA  . LYS A 1 29  ? 2.216   12.789  -43.103 1.00 74.02  ? 29  LYS A CA  1 
ATOM 182  C C   . LYS A 1 29  ? 3.147   11.913  -43.937 1.00 76.18  ? 29  LYS A C   1 
ATOM 183  O O   . LYS A 1 29  ? 4.274   11.604  -43.540 1.00 79.07  ? 29  LYS A O   1 
ATOM 184  C CB  . LYS A 1 29  ? 2.315   14.243  -43.561 1.00 73.46  ? 29  LYS A CB  1 
ATOM 185  C CG  . LYS A 1 29  ? 1.501   15.212  -42.727 1.00 75.55  ? 29  LYS A CG  1 
ATOM 186  C CD  . LYS A 1 29  ? 0.842   16.265  -43.597 1.00 77.26  ? 29  LYS A CD  1 
ATOM 187  C CE  . LYS A 1 29  ? -0.031  17.193  -42.771 1.00 78.02  ? 29  LYS A CE  1 
ATOM 188  N NZ  . LYS A 1 29  ? -0.810  18.126  -43.630 1.00 79.96  ? 29  LYS A NZ  1 
ATOM 189  N N   . GLN A 1 30  ? 2.656   11.510  -45.110 1.00 81.19  ? 30  GLN A N   1 
ATOM 190  C CA  . GLN A 1 30  ? 3.462   10.698  -46.014 1.00 78.52  ? 30  GLN A CA  1 
ATOM 191  C C   . GLN A 1 30  ? 4.705   11.438  -46.489 1.00 84.43  ? 30  GLN A C   1 
ATOM 192  O O   . GLN A 1 30  ? 5.761   10.817  -46.644 1.00 85.68  ? 30  GLN A O   1 
ATOM 193  C CB  . GLN A 1 30  ? 2.622   10.258  -47.214 1.00 76.67  ? 30  GLN A CB  1 
ATOM 194  C CG  . GLN A 1 30  ? 3.403   9.518   -48.285 1.00 77.34  ? 30  GLN A CG  1 
ATOM 195  C CD  . GLN A 1 30  ? 2.569   9.230   -49.514 1.00 82.80  ? 30  GLN A CD  1 
ATOM 196  O OE1 . GLN A 1 30  ? 1.391   9.578   -49.574 1.00 84.03  ? 30  GLN A OE1 1 
ATOM 197  N NE2 . GLN A 1 30  ? 3.175   8.586   -50.503 1.00 84.47  ? 30  GLN A NE2 1 
ATOM 198  N N   . SER A 1 31  ? 4.606   12.749  -46.705 1.00 89.05  ? 31  SER A N   1 
ATOM 199  C CA  . SER A 1 31  ? 5.754   13.556  -47.095 1.00 87.91  ? 31  SER A CA  1 
ATOM 200  C C   . SER A 1 31  ? 6.754   13.745  -45.964 1.00 88.69  ? 31  SER A C   1 
ATOM 201  O O   . SER A 1 31  ? 7.842   14.277  -46.206 1.00 88.13  ? 31  SER A O   1 
ATOM 202  C CB  . SER A 1 31  ? 5.287   14.924  -47.595 1.00 88.97  ? 31  SER A CB  1 
ATOM 203  O OG  . SER A 1 31  ? 4.582   15.617  -46.580 1.00 88.98  ? 31  SER A OG  1 
ATOM 204  N N   . GLU A 1 32  ? 6.414   13.333  -44.745 1.00 83.73  ? 32  GLU A N   1 
ATOM 205  C CA  . GLU A 1 32  ? 7.292   13.469  -43.592 1.00 79.35  ? 32  GLU A CA  1 
ATOM 206  C C   . GLU A 1 32  ? 8.088   12.205  -43.303 1.00 81.42  ? 32  GLU A C   1 
ATOM 207  O O   . GLU A 1 32  ? 8.755   12.131  -42.267 1.00 84.58  ? 32  GLU A O   1 
ATOM 208  C CB  . GLU A 1 32  ? 6.474   13.864  -42.360 1.00 78.77  ? 32  GLU A CB  1 
ATOM 209  C CG  . GLU A 1 32  ? 5.797   15.217  -42.494 1.00 81.92  ? 32  GLU A CG  1 
ATOM 210  C CD  . GLU A 1 32  ? 4.764   15.463  -41.416 1.00 87.24  ? 32  GLU A CD  1 
ATOM 211  O OE1 . GLU A 1 32  ? 4.455   14.520  -40.660 1.00 88.36  ? 32  GLU A OE1 1 
ATOM 212  O OE2 . GLU A 1 32  ? 4.259   16.602  -41.323 1.00 86.53  ? 32  GLU A OE2 1 
ATOM 213  N N   . VAL A 1 33  ? 8.033   11.213  -44.188 1.00 74.69  ? 33  VAL A N   1 
ATOM 214  C CA  . VAL A 1 33  ? 8.818   9.992   -44.067 1.00 72.85  ? 33  VAL A CA  1 
ATOM 215  C C   . VAL A 1 33  ? 9.902   10.021  -45.134 1.00 76.35  ? 33  VAL A C   1 
ATOM 216  O O   . VAL A 1 33  ? 9.625   10.317  -46.302 1.00 80.91  ? 33  VAL A O   1 
ATOM 217  C CB  . VAL A 1 33  ? 7.935   8.742   -44.212 1.00 74.82  ? 33  VAL A CB  1 
ATOM 218  C CG1 . VAL A 1 33  ? 8.778   7.481   -44.113 1.00 73.38  ? 33  VAL A CG1 1 
ATOM 219  C CG2 . VAL A 1 33  ? 6.841   8.740   -43.160 1.00 75.67  ? 33  VAL A CG2 1 
ATOM 220  N N   . VAL A 1 34  ? 11.136  9.722   -44.737 1.00 81.28  ? 34  VAL A N   1 
ATOM 221  C CA  . VAL A 1 34  ? 12.280  9.757   -45.640 1.00 81.67  ? 34  VAL A CA  1 
ATOM 222  C C   . VAL A 1 34  ? 12.950  8.390   -45.646 1.00 83.94  ? 34  VAL A C   1 
ATOM 223  O O   . VAL A 1 34  ? 13.084  7.748   -44.598 1.00 84.83  ? 34  VAL A O   1 
ATOM 224  C CB  . VAL A 1 34  ? 13.275  10.873  -45.257 1.00 81.15  ? 34  VAL A CB  1 
ATOM 225  C CG1 . VAL A 1 34  ? 14.071  10.514  -44.009 1.00 79.06  ? 34  VAL A CG1 1 
ATOM 226  C CG2 . VAL A 1 34  ? 14.212  11.162  -46.418 1.00 80.16  ? 34  VAL A CG2 1 
ATOM 227  N N   . TYR A 1 35  ? 13.319  7.927   -46.837 1.00 82.87  ? 35  TYR A N   1 
ATOM 228  C CA  . TYR A 1 35  ? 14.170  6.754   -46.959 1.00 78.51  ? 35  TYR A CA  1 
ATOM 229  C C   . TYR A 1 35  ? 15.616  7.144   -46.697 1.00 82.89  ? 35  TYR A C   1 
ATOM 230  O O   . TYR A 1 35  ? 16.061  8.231   -47.075 1.00 90.39  ? 35  TYR A O   1 
ATOM 231  C CB  . TYR A 1 35  ? 14.041  6.139   -48.350 1.00 79.30  ? 35  TYR A CB  1 
ATOM 232  C CG  . TYR A 1 35  ? 13.002  5.051   -48.463 1.00 80.19  ? 35  TYR A CG  1 
ATOM 233  C CD1 . TYR A 1 35  ? 11.670  5.298   -48.162 1.00 81.35  ? 35  TYR A CD1 1 
ATOM 234  C CD2 . TYR A 1 35  ? 13.353  3.777   -48.884 1.00 79.75  ? 35  TYR A CD2 1 
ATOM 235  C CE1 . TYR A 1 35  ? 10.720  4.304   -48.271 1.00 81.38  ? 35  TYR A CE1 1 
ATOM 236  C CE2 . TYR A 1 35  ? 12.412  2.778   -48.995 1.00 82.22  ? 35  TYR A CE2 1 
ATOM 237  C CZ  . TYR A 1 35  ? 11.097  3.046   -48.688 1.00 84.64  ? 35  TYR A CZ  1 
ATOM 238  O OH  . TYR A 1 35  ? 10.159  2.048   -48.800 1.00 86.39  ? 35  TYR A OH  1 
ATOM 239  N N   . PHE A 1 36  ? 16.357  6.254   -46.045 1.00 92.09  ? 36  PHE A N   1 
ATOM 240  C CA  . PHE A 1 36  ? 17.752  6.536   -45.737 1.00 92.08  ? 36  PHE A CA  1 
ATOM 241  C C   . PHE A 1 36  ? 18.647  5.968   -46.832 1.00 94.99  ? 36  PHE A C   1 
ATOM 242  O O   . PHE A 1 36  ? 18.524  4.796   -47.202 1.00 94.99  ? 36  PHE A O   1 
ATOM 243  C CB  . PHE A 1 36  ? 18.125  5.980   -44.360 1.00 91.32  ? 36  PHE A CB  1 
ATOM 244  C CG  . PHE A 1 36  ? 19.616  5.888   -44.108 1.00 95.97  ? 36  PHE A CG  1 
ATOM 245  C CD1 . PHE A 1 36  ? 20.395  4.902   -44.701 1.00 96.59  ? 36  PHE A CD1 1 
ATOM 246  C CD2 . PHE A 1 36  ? 20.243  6.829   -43.311 1.00 96.26  ? 36  PHE A CD2 1 
ATOM 247  C CE1 . PHE A 1 36  ? 21.751  4.842   -44.481 1.00 94.01  ? 36  PHE A CE1 1 
ATOM 248  C CE2 . PHE A 1 36  ? 21.602  6.771   -43.090 1.00 94.17  ? 36  PHE A CE2 1 
ATOM 249  C CZ  . PHE A 1 36  ? 22.355  5.778   -43.678 1.00 93.50  ? 36  PHE A CZ  1 
ATOM 250  N N   . SER A 1 37  ? 19.542  6.804   -47.344 1.00 101.16 ? 37  SER A N   1 
ATOM 251  C CA  . SER A 1 37  ? 20.716  6.377   -48.086 1.00 103.38 ? 37  SER A CA  1 
ATOM 252  C C   . SER A 1 37  ? 21.869  7.307   -47.733 1.00 106.35 ? 37  SER A C   1 
ATOM 253  O O   . SER A 1 37  ? 21.800  8.083   -46.777 1.00 107.01 ? 37  SER A O   1 
ATOM 254  C CB  . SER A 1 37  ? 20.464  6.360   -49.600 1.00 102.34 ? 37  SER A CB  1 
ATOM 255  O OG  . SER A 1 37  ? 20.198  7.654   -50.103 1.00 100.48 ? 37  SER A OG  1 
ATOM 256  N N   . VAL A 1 38  ? 22.942  7.229   -48.514 1.00 107.82 ? 38  VAL A N   1 
ATOM 257  C CA  . VAL A 1 38  ? 24.137  8.013   -48.225 1.00 103.95 ? 38  VAL A CA  1 
ATOM 258  C C   . VAL A 1 38  ? 24.033  9.393   -48.864 1.00 103.21 ? 38  VAL A C   1 
ATOM 259  O O   . VAL A 1 38  ? 24.497  9.610   -49.989 1.00 104.33 ? 38  VAL A O   1 
ATOM 260  C CB  . VAL A 1 38  ? 25.406  7.272   -48.687 1.00 105.57 ? 38  VAL A CB  1 
ATOM 261  C CG1 . VAL A 1 38  ? 25.793  6.217   -47.668 1.00 103.50 ? 38  VAL A CG1 1 
ATOM 262  C CG2 . VAL A 1 38  ? 25.180  6.616   -50.043 1.00 105.61 ? 38  VAL A CG2 1 
ATOM 263  N N   . GLY A 1 39  ? 23.423  10.338  -48.151 1.00 95.96  ? 39  GLY A N   1 
ATOM 264  C CA  . GLY A 1 39  ? 23.412  11.714  -48.606 1.00 96.81  ? 39  GLY A CA  1 
ATOM 265  C C   . GLY A 1 39  ? 22.058  12.395  -48.628 1.00 101.17 ? 39  GLY A C   1 
ATOM 266  O O   . GLY A 1 39  ? 21.949  13.533  -49.096 1.00 101.47 ? 39  GLY A O   1 
ATOM 267  N N   . VAL A 1 40  ? 21.023  11.729  -48.129 1.00 100.07 ? 40  VAL A N   1 
ATOM 268  C CA  . VAL A 1 40  ? 19.678  12.289  -48.128 1.00 96.72  ? 40  VAL A CA  1 
ATOM 269  C C   . VAL A 1 40  ? 19.592  13.405  -47.098 1.00 97.96  ? 40  VAL A C   1 
ATOM 270  O O   . VAL A 1 40  ? 20.251  13.367  -46.053 1.00 99.31  ? 40  VAL A O   1 
ATOM 271  C CB  . VAL A 1 40  ? 18.618  11.203  -47.858 1.00 95.63  ? 40  VAL A CB  1 
ATOM 272  C CG1 . VAL A 1 40  ? 18.816  10.039  -48.793 1.00 96.72  ? 40  VAL A CG1 1 
ATOM 273  C CG2 . VAL A 1 40  ? 18.680  10.731  -46.413 1.00 98.38  ? 40  VAL A CG2 1 
ATOM 274  N N   . ASP A 1 41  ? 18.788  14.418  -47.408 1.00 99.93  ? 41  ASP A N   1 
ATOM 275  C CA  . ASP A 1 41  ? 18.522  15.490  -46.459 1.00 101.52 ? 41  ASP A CA  1 
ATOM 276  C C   . ASP A 1 41  ? 17.431  15.045  -45.494 1.00 103.97 ? 41  ASP A C   1 
ATOM 277  O O   . ASP A 1 41  ? 16.274  14.874  -45.891 1.00 106.90 ? 41  ASP A O   1 
ATOM 278  C CB  . ASP A 1 41  ? 18.108  16.758  -47.202 1.00 102.12 ? 41  ASP A CB  1 
ATOM 279  C CG  . ASP A 1 41  ? 17.862  17.929  -46.270 1.00 105.62 ? 41  ASP A CG  1 
ATOM 280  O OD1 . ASP A 1 41  ? 18.300  17.873  -45.104 1.00 107.39 ? 41  ASP A OD1 1 
ATOM 281  O OD2 . ASP A 1 41  ? 17.226  18.911  -46.709 1.00 104.82 ? 41  ASP A OD2 1 
ATOM 282  N N   . ILE A 1 42  ? 17.795  14.854  -44.231 1.00 97.49  ? 42  ILE A N   1 
ATOM 283  C CA  . ILE A 1 42  ? 16.860  14.388  -43.219 1.00 97.00  ? 42  ILE A CA  1 
ATOM 284  C C   . ILE A 1 42  ? 16.202  15.557  -42.484 1.00 98.54  ? 42  ILE A C   1 
ATOM 285  O O   . ILE A 1 42  ? 15.454  15.345  -41.533 1.00 100.24 ? 42  ILE A O   1 
ATOM 286  C CB  . ILE A 1 42  ? 17.532  13.421  -42.235 1.00 98.29  ? 42  ILE A CB  1 
ATOM 287  C CG1 . ILE A 1 42  ? 18.683  14.114  -41.506 1.00 97.96  ? 42  ILE A CG1 1 
ATOM 288  C CG2 . ILE A 1 42  ? 18.034  12.186  -42.965 1.00 95.90  ? 42  ILE A CG2 1 
ATOM 289  C CD1 . ILE A 1 42  ? 19.342  13.252  -40.455 1.00 96.40  ? 42  ILE A CD1 1 
ATOM 290  N N   . SER A 1 43  ? 16.476  16.787  -42.908 1.00 97.11  ? 43  SER A N   1 
ATOM 291  C CA  . SER A 1 43  ? 15.853  17.946  -42.295 1.00 97.71  ? 43  SER A CA  1 
ATOM 292  C C   . SER A 1 43  ? 14.382  18.035  -42.696 1.00 99.55  ? 43  SER A C   1 
ATOM 293  O O   . SER A 1 43  ? 13.982  17.658  -43.801 1.00 99.55  ? 43  SER A O   1 
ATOM 294  C CB  . SER A 1 43  ? 16.590  19.222  -42.691 1.00 100.34 ? 43  SER A CB  1 
ATOM 295  O OG  . SER A 1 43  ? 16.354  19.545  -44.050 1.00 100.99 ? 43  SER A OG  1 
ATOM 296  N N   . GLY A 1 44  ? 13.568  18.542  -41.772 1.00 96.05  ? 44  GLY A N   1 
ATOM 297  C CA  . GLY A 1 44  ? 12.143  18.661  -41.985 1.00 96.44  ? 44  GLY A CA  1 
ATOM 298  C C   . GLY A 1 44  ? 11.376  17.359  -41.977 1.00 97.58  ? 44  GLY A C   1 
ATOM 299  O O   . GLY A 1 44  ? 10.142  17.390  -41.903 1.00 96.23  ? 44  GLY A O   1 
ATOM 300  N N   . TYR A 1 45  ? 12.055  16.220  -42.048 1.00 93.15  ? 45  TYR A N   1 
ATOM 301  C CA  . TYR A 1 45  ? 11.415  14.918  -41.989 1.00 87.64  ? 45  TYR A CA  1 
ATOM 302  C C   . TYR A 1 45  ? 11.243  14.495  -40.538 1.00 89.12  ? 45  TYR A C   1 
ATOM 303  O O   . TYR A 1 45  ? 12.054  14.832  -39.671 1.00 91.25  ? 45  TYR A O   1 
ATOM 304  C CB  . TYR A 1 45  ? 12.232  13.874  -42.750 1.00 84.06  ? 45  TYR A CB  1 
ATOM 305  C CG  . TYR A 1 45  ? 12.155  14.027  -44.250 1.00 87.18  ? 45  TYR A CG  1 
ATOM 306  C CD1 . TYR A 1 45  ? 13.248  14.472  -44.979 1.00 88.93  ? 45  TYR A CD1 1 
ATOM 307  C CD2 . TYR A 1 45  ? 10.988  13.729  -44.938 1.00 87.65  ? 45  TYR A CD2 1 
ATOM 308  C CE1 . TYR A 1 45  ? 13.181  14.615  -46.350 1.00 88.61  ? 45  TYR A CE1 1 
ATOM 309  C CE2 . TYR A 1 45  ? 10.913  13.869  -46.308 1.00 86.66  ? 45  TYR A CE2 1 
ATOM 310  C CZ  . TYR A 1 45  ? 12.012  14.311  -47.009 1.00 89.22  ? 45  TYR A CZ  1 
ATOM 311  O OH  . TYR A 1 45  ? 11.941  14.452  -48.375 1.00 94.82  ? 45  TYR A OH  1 
ATOM 312  N N   . LYS A 1 46  ? 10.171  13.751  -40.280 1.00 82.96  ? 46  LYS A N   1 
ATOM 313  C CA  . LYS A 1 46  ? 9.801   13.375  -38.923 1.00 80.77  ? 46  LYS A CA  1 
ATOM 314  C C   . LYS A 1 46  ? 9.972   11.895  -38.633 1.00 80.72  ? 46  LYS A C   1 
ATOM 315  O O   . LYS A 1 46  ? 10.138  11.523  -37.470 1.00 78.80  ? 46  LYS A O   1 
ATOM 316  C CB  . LYS A 1 46  ? 8.350   13.787  -38.652 1.00 76.88  ? 46  LYS A CB  1 
ATOM 317  C CG  . LYS A 1 46  ? 8.185   15.293  -38.544 1.00 81.03  ? 46  LYS A CG  1 
ATOM 318  C CD  . LYS A 1 46  ? 6.740   15.721  -38.690 1.00 80.97  ? 46  LYS A CD  1 
ATOM 319  C CE  . LYS A 1 46  ? 6.614   17.234  -38.731 1.00 83.07  ? 46  LYS A CE  1 
ATOM 320  N NZ  . LYS A 1 46  ? 7.937   17.906  -38.600 1.00 83.36  ? 46  LYS A NZ  1 
ATOM 321  N N   . VAL A 1 47  ? 9.938   11.046  -39.656 1.00 75.01  ? 47  VAL A N   1 
ATOM 322  C CA  . VAL A 1 47  ? 10.204  9.621   -39.518 1.00 74.94  ? 47  VAL A CA  1 
ATOM 323  C C   . VAL A 1 47  ? 11.179  9.216   -40.613 1.00 73.84  ? 47  VAL A C   1 
ATOM 324  O O   . VAL A 1 47  ? 11.018  9.608   -41.774 1.00 77.94  ? 47  VAL A O   1 
ATOM 325  C CB  . VAL A 1 47  ? 8.913   8.779   -39.599 1.00 72.38  ? 47  VAL A CB  1 
ATOM 326  C CG1 . VAL A 1 47  ? 9.234   7.301   -39.470 1.00 70.74  ? 47  VAL A CG1 1 
ATOM 327  C CG2 . VAL A 1 47  ? 7.926   9.203   -38.524 1.00 72.81  ? 47  VAL A CG2 1 
ATOM 328  N N   . ILE A 1 48  ? 12.193  8.440   -40.246 1.00 73.47  ? 48  ILE A N   1 
ATOM 329  C CA  . ILE A 1 48  ? 13.171  7.919   -41.193 1.00 72.57  ? 48  ILE A CA  1 
ATOM 330  C C   . ILE A 1 48  ? 12.991  6.411   -41.277 1.00 72.48  ? 48  ILE A C   1 
ATOM 331  O O   . ILE A 1 48  ? 12.790  5.744   -40.255 1.00 77.48  ? 48  ILE A O   1 
ATOM 332  C CB  . ILE A 1 48  ? 14.613  8.291   -40.795 1.00 76.70  ? 48  ILE A CB  1 
ATOM 333  C CG1 . ILE A 1 48  ? 15.603  7.819   -41.861 1.00 77.72  ? 48  ILE A CG1 1 
ATOM 334  C CG2 . ILE A 1 48  ? 14.969  7.720   -39.433 1.00 74.87  ? 48  ILE A CG2 1 
ATOM 335  C CD1 . ILE A 1 48  ? 16.972  8.447   -41.740 1.00 77.44  ? 48  ILE A CD1 1 
ATOM 336  N N   . TYR A 1 49  ? 13.031  5.881   -42.493 1.00 69.38  ? 49  TYR A N   1 
ATOM 337  C CA  . TYR A 1 49  ? 12.843  4.459   -42.729 1.00 71.33  ? 49  TYR A CA  1 
ATOM 338  C C   . TYR A 1 49  ? 14.142  3.850   -43.235 1.00 73.20  ? 49  TYR A C   1 
ATOM 339  O O   . TYR A 1 49  ? 14.743  4.359   -44.187 1.00 81.64  ? 49  TYR A O   1 
ATOM 340  C CB  . TYR A 1 49  ? 11.710  4.221   -43.731 1.00 72.14  ? 49  TYR A CB  1 
ATOM 341  C CG  . TYR A 1 49  ? 11.595  2.795   -44.217 1.00 69.96  ? 49  TYR A CG  1 
ATOM 342  C CD1 . TYR A 1 49  ? 10.854  1.860   -43.508 1.00 72.48  ? 49  TYR A CD1 1 
ATOM 343  C CD2 . TYR A 1 49  ? 12.201  2.390   -45.397 1.00 68.42  ? 49  TYR A CD2 1 
ATOM 344  C CE1 . TYR A 1 49  ? 10.739  0.559   -43.949 1.00 72.01  ? 49  TYR A CE1 1 
ATOM 345  C CE2 . TYR A 1 49  ? 12.090  1.092   -45.845 1.00 72.67  ? 49  TYR A CE2 1 
ATOM 346  C CZ  . TYR A 1 49  ? 11.358  0.180   -45.118 1.00 74.46  ? 49  TYR A CZ  1 
ATOM 347  O OH  . TYR A 1 49  ? 11.244  -1.115  -45.566 1.00 77.19  ? 49  TYR A OH  1 
ATOM 348  N N   . ASP A 1 50  ? 14.572  2.768   -42.595 1.00 79.75  ? 50  ASP A N   1 
ATOM 349  C CA  . ASP A 1 50  ? 15.764  2.038   -43.011 1.00 83.76  ? 50  ASP A CA  1 
ATOM 350  C C   . ASP A 1 50  ? 15.338  0.957   -43.995 1.00 81.88  ? 50  ASP A C   1 
ATOM 351  O O   . ASP A 1 50  ? 14.571  0.056   -43.643 1.00 82.35  ? 50  ASP A O   1 
ATOM 352  C CB  . ASP A 1 50  ? 16.478  1.436   -41.803 1.00 85.53  ? 50  ASP A CB  1 
ATOM 353  C CG  . ASP A 1 50  ? 17.826  0.837   -42.160 1.00 90.44  ? 50  ASP A CG  1 
ATOM 354  O OD1 . ASP A 1 50  ? 18.239  0.939   -43.333 1.00 90.65  ? 50  ASP A OD1 1 
ATOM 355  O OD2 . ASP A 1 50  ? 18.475  0.261   -41.261 1.00 91.29  ? 50  ASP A OD2 1 
ATOM 356  N N   . LYS A 1 51  ? 15.833  1.048   -45.229 1.00 83.99  ? 51  LYS A N   1 
ATOM 357  C CA  . LYS A 1 51  ? 15.468  0.067   -46.244 1.00 85.78  ? 51  LYS A CA  1 
ATOM 358  C C   . LYS A 1 51  ? 16.055  -1.306  -45.941 1.00 88.21  ? 51  LYS A C   1 
ATOM 359  O O   . LYS A 1 51  ? 15.408  -2.326  -46.202 1.00 88.93  ? 51  LYS A O   1 
ATOM 360  C CB  . LYS A 1 51  ? 15.917  0.559   -47.620 1.00 86.15  ? 51  LYS A CB  1 
ATOM 361  C CG  . LYS A 1 51  ? 16.155  -0.538  -48.643 1.00 88.65  ? 51  LYS A CG  1 
ATOM 362  C CD  . LYS A 1 51  ? 17.162  -0.105  -49.696 1.00 90.33  ? 51  LYS A CD  1 
ATOM 363  C CE  . LYS A 1 51  ? 17.034  1.377   -50.018 1.00 90.55  ? 51  LYS A CE  1 
ATOM 364  N NZ  . LYS A 1 51  ? 18.121  1.847   -50.920 1.00 89.45  ? 51  LYS A NZ  1 
ATOM 365  N N   . THR A 1 52  ? 17.267  -1.353  -45.384 1.00 88.87  ? 52  THR A N   1 
ATOM 366  C CA  . THR A 1 52  ? 17.926  -2.630  -45.134 1.00 90.04  ? 52  THR A CA  1 
ATOM 367  C C   . THR A 1 52  ? 17.218  -3.437  -44.052 1.00 90.29  ? 52  THR A C   1 
ATOM 368  O O   . THR A 1 52  ? 16.946  -4.627  -44.244 1.00 90.10  ? 52  THR A O   1 
ATOM 369  C CB  . THR A 1 52  ? 19.386  -2.399  -44.748 1.00 91.87  ? 52  THR A CB  1 
ATOM 370  O OG1 . THR A 1 52  ? 19.965  -1.426  -45.626 1.00 92.96  ? 52  THR A OG1 1 
ATOM 371  C CG2 . THR A 1 52  ? 20.174  -3.695  -44.845 1.00 89.83  ? 52  THR A CG2 1 
ATOM 372  N N   . THR A 1 53  ? 16.915  -2.814  -42.913 1.00 86.15  ? 53  THR A N   1 
ATOM 373  C CA  . THR A 1 53  ? 16.268  -3.544  -41.827 1.00 85.38  ? 53  THR A CA  1 
ATOM 374  C C   . THR A 1 53  ? 14.750  -3.475  -41.933 1.00 84.73  ? 53  THR A C   1 
ATOM 375  O O   . THR A 1 53  ? 14.044  -4.149  -41.173 1.00 86.94  ? 53  THR A O   1 
ATOM 376  C CB  . THR A 1 53  ? 16.726  -2.998  -40.475 1.00 84.63  ? 53  THR A CB  1 
ATOM 377  O OG1 . THR A 1 53  ? 16.722  -1.566  -40.511 1.00 85.68  ? 53  THR A OG1 1 
ATOM 378  C CG2 . THR A 1 53  ? 18.129  -3.485  -40.155 1.00 84.58  ? 53  THR A CG2 1 
ATOM 379  N N   . GLN A 1 54  ? 14.239  -2.674  -42.868 1.00 81.24  ? 54  GLN A N   1 
ATOM 380  C CA  . GLN A 1 54  ? 12.809  -2.444  -43.038 1.00 77.90  ? 54  GLN A CA  1 
ATOM 381  C C   . GLN A 1 54  ? 12.183  -1.975  -41.731 1.00 79.53  ? 54  GLN A C   1 
ATOM 382  O O   . GLN A 1 54  ? 11.059  -2.359  -41.394 1.00 82.33  ? 54  GLN A O   1 
ATOM 383  C CB  . GLN A 1 54  ? 12.111  -3.700  -43.563 1.00 76.49  ? 54  GLN A CB  1 
ATOM 384  C CG  . GLN A 1 54  ? 12.706  -4.221  -44.859 1.00 78.47  ? 54  GLN A CG  1 
ATOM 385  C CD  . GLN A 1 54  ? 11.701  -4.973  -45.705 1.00 84.12  ? 54  GLN A CD  1 
ATOM 386  O OE1 . GLN A 1 54  ? 10.532  -5.093  -45.342 1.00 83.09  ? 54  GLN A OE1 1 
ATOM 387  N NE2 . GLN A 1 54  ? 12.154  -5.490  -46.841 1.00 85.16  ? 54  GLN A NE2 1 
ATOM 388  N N   . ARG A 1 55  ? 12.911  -1.145  -40.992 1.00 70.86  ? 55  ARG A N   1 
ATOM 389  C CA  . ARG A 1 55  ? 12.436  -0.549  -39.755 1.00 69.55  ? 55  ARG A CA  1 
ATOM 390  C C   . ARG A 1 55  ? 12.394  0.965   -39.904 1.00 69.48  ? 55  ARG A C   1 
ATOM 391  O O   . ARG A 1 55  ? 13.291  1.564   -40.505 1.00 73.24  ? 55  ARG A O   1 
ATOM 392  C CB  . ARG A 1 55  ? 13.333  -0.930  -38.575 1.00 70.18  ? 55  ARG A CB  1 
ATOM 393  C CG  . ARG A 1 55  ? 13.330  -2.409  -38.245 1.00 74.13  ? 55  ARG A CG  1 
ATOM 394  C CD  . ARG A 1 55  ? 12.041  -2.810  -37.548 1.00 69.80  ? 55  ARG A CD  1 
ATOM 395  N NE  . ARG A 1 55  ? 12.085  -4.175  -37.037 1.00 71.38  ? 55  ARG A NE  1 
ATOM 396  C CZ  . ARG A 1 55  ? 12.840  -4.580  -36.024 1.00 72.43  ? 55  ARG A CZ  1 
ATOM 397  N NH1 . ARG A 1 55  ? 13.622  -3.741  -35.364 1.00 74.99  ? 55  ARG A NH1 1 
ATOM 398  N NH2 . ARG A 1 55  ? 12.806  -5.858  -35.661 1.00 72.86  ? 55  ARG A NH2 1 
ATOM 399  N N   . ALA A 1 56  ? 11.350  1.576   -39.357 1.00 69.32  ? 56  ALA A N   1 
ATOM 400  C CA  . ALA A 1 56  ? 11.156  3.016   -39.425 1.00 66.98  ? 56  ALA A CA  1 
ATOM 401  C C   . ALA A 1 56  ? 11.303  3.608   -38.032 1.00 66.43  ? 56  ALA A C   1 
ATOM 402  O O   . ALA A 1 56  ? 10.769  3.062   -37.062 1.00 70.26  ? 56  ALA A O   1 
ATOM 403  C CB  . ALA A 1 56  ? 9.785   3.357   -40.010 1.00 65.40  ? 56  ALA A CB  1 
ATOM 404  N N   . TYR A 1 57  ? 12.033  4.714   -37.938 1.00 68.27  ? 57  TYR A N   1 
ATOM 405  C CA  . TYR A 1 57  ? 12.323  5.362   -36.669 1.00 68.31  ? 57  TYR A CA  1 
ATOM 406  C C   . TYR A 1 57  ? 11.931  6.829   -36.745 1.00 71.25  ? 57  TYR A C   1 
ATOM 407  O O   . TYR A 1 57  ? 12.125  7.480   -37.776 1.00 78.42  ? 57  TYR A O   1 
ATOM 408  C CB  . TYR A 1 57  ? 13.807  5.234   -36.316 1.00 67.89  ? 57  TYR A CB  1 
ATOM 409  C CG  . TYR A 1 57  ? 14.282  3.804   -36.240 1.00 65.60  ? 57  TYR A CG  1 
ATOM 410  C CD1 . TYR A 1 57  ? 14.124  3.059   -35.082 1.00 68.36  ? 57  TYR A CD1 1 
ATOM 411  C CD2 . TYR A 1 57  ? 14.879  3.193   -37.335 1.00 66.27  ? 57  TYR A CD2 1 
ATOM 412  C CE1 . TYR A 1 57  ? 14.553  1.749   -35.012 1.00 73.22  ? 57  TYR A CE1 1 
ATOM 413  C CE2 . TYR A 1 57  ? 15.309  1.886   -37.276 1.00 70.01  ? 57  TYR A CE2 1 
ATOM 414  C CZ  . TYR A 1 57  ? 15.143  1.168   -36.113 1.00 72.67  ? 57  TYR A CZ  1 
ATOM 415  O OH  . TYR A 1 57  ? 15.574  -0.136  -36.050 1.00 73.63  ? 57  TYR A OH  1 
ATOM 416  N N   . SER A 1 58  ? 11.379  7.345   -35.652 1.00 73.82  ? 58  SER A N   1 
ATOM 417  C CA  . SER A 1 58  ? 11.013  8.753   -35.599 1.00 76.24  ? 58  SER A CA  1 
ATOM 418  C C   . SER A 1 58  ? 12.263  9.612   -35.479 1.00 80.58  ? 58  SER A C   1 
ATOM 419  O O   . SER A 1 58  ? 13.055  9.450   -34.546 1.00 84.16  ? 58  SER A O   1 
ATOM 420  C CB  . SER A 1 58  ? 10.075  9.017   -34.425 1.00 74.79  ? 58  SER A CB  1 
ATOM 421  O OG  . SER A 1 58  ? 8.728   8.768   -34.782 1.00 81.63  ? 58  SER A OG  1 
ATOM 422  N N   . LEU A 1 59  ? 12.442  10.519  -36.426 1.00 86.10  ? 59  LEU A N   1 
ATOM 423  C CA  . LEU A 1 59  ? 13.570  11.435  -36.367 1.00 81.35  ? 59  LEU A CA  1 
ATOM 424  C C   . LEU A 1 59  ? 13.349  12.469  -35.267 1.00 85.74  ? 59  LEU A C   1 
ATOM 425  O O   . LEU A 1 59  ? 12.257  13.032  -35.157 1.00 86.34  ? 59  LEU A O   1 
ATOM 426  C CB  . LEU A 1 59  ? 13.761  12.140  -37.705 1.00 76.98  ? 59  LEU A CB  1 
ATOM 427  C CG  . LEU A 1 59  ? 14.503  11.351  -38.780 1.00 83.97  ? 59  LEU A CG  1 
ATOM 428  C CD1 . LEU A 1 59  ? 14.498  12.107  -40.094 1.00 88.17  ? 59  LEU A CD1 1 
ATOM 429  C CD2 . LEU A 1 59  ? 15.924  11.065  -38.331 1.00 88.08  ? 59  LEU A CD2 1 
ATOM 430  N N   . PRO A 1 60  ? 14.355  12.725  -34.436 1.00 90.46  ? 60  PRO A N   1 
ATOM 431  C CA  . PRO A 1 60  ? 14.224  13.787  -33.435 1.00 89.03  ? 60  PRO A CA  1 
ATOM 432  C C   . PRO A 1 60  ? 14.036  15.140  -34.101 1.00 89.69  ? 60  PRO A C   1 
ATOM 433  O O   . PRO A 1 60  ? 14.629  15.447  -35.137 1.00 91.71  ? 60  PRO A O   1 
ATOM 434  C CB  . PRO A 1 60  ? 15.541  13.735  -32.652 1.00 88.37  ? 60  PRO A CB  1 
ATOM 435  C CG  . PRO A 1 60  ? 16.424  12.788  -33.359 1.00 87.63  ? 60  PRO A CG  1 
ATOM 436  C CD  . PRO A 1 60  ? 15.685  12.095  -34.449 1.00 86.70  ? 60  PRO A CD  1 
ATOM 437  N N   . ILE A 1 61  ? 13.190  15.951  -33.488 1.00 97.44  ? 61  ILE A N   1 
ATOM 438  C CA  . ILE A 1 61  ? 12.903  17.281  -34.008 1.00 100.20 ? 61  ILE A CA  1 
ATOM 439  C C   . ILE A 1 61  ? 14.086  18.195  -33.718 1.00 102.58 ? 61  ILE A C   1 
ATOM 440  O O   . ILE A 1 61  ? 14.931  17.906  -32.863 1.00 101.74 ? 61  ILE A O   1 
ATOM 441  C CB  . ILE A 1 61  ? 11.594  17.823  -33.403 1.00 98.97  ? 61  ILE A CB  1 
ATOM 442  C CG1 . ILE A 1 61  ? 11.035  18.971  -34.249 1.00 99.09  ? 61  ILE A CG1 1 
ATOM 443  C CG2 . ILE A 1 61  ? 11.822  18.265  -31.977 1.00 97.10  ? 61  ILE A CG2 1 
ATOM 444  C CD1 . ILE A 1 61  ? 9.527   19.000  -34.321 1.00 95.94  ? 61  ILE A CD1 1 
ATOM 445  N N   . GLY A 1 62  ? 14.153  19.310  -34.439 1.00 107.94 ? 62  GLY A N   1 
ATOM 446  C CA  . GLY A 1 62  ? 15.252  20.238  -34.289 1.00 109.02 ? 62  GLY A CA  1 
ATOM 447  C C   . GLY A 1 62  ? 16.458  19.947  -35.150 1.00 109.89 ? 62  GLY A C   1 
ATOM 448  O O   . GLY A 1 62  ? 17.489  20.608  -34.986 1.00 111.50 ? 62  GLY A O   1 
ATOM 449  N N   . ILE A 1 63  ? 16.369  18.978  -36.051 1.00 103.50 ? 63  ILE A N   1 
ATOM 450  C CA  . ILE A 1 63  ? 17.474  18.717  -36.979 1.00 103.91 ? 63  ILE A CA  1 
ATOM 451  C C   . ILE A 1 63  ? 17.640  19.922  -37.900 1.00 104.85 ? 63  ILE A C   1 
ATOM 452  O O   . ILE A 1 63  ? 16.663  20.346  -38.542 1.00 102.09 ? 63  ILE A O   1 
ATOM 453  C CB  . ILE A 1 63  ? 17.209  17.442  -37.778 1.00 102.94 ? 63  ILE A CB  1 
ATOM 454  C CG1 . ILE A 1 63  ? 17.297  16.216  -36.866 1.00 101.24 ? 63  ILE A CG1 1 
ATOM 455  C CG2 . ILE A 1 63  ? 18.188  17.316  -38.930 1.00 102.89 ? 63  ILE A CG2 1 
ATOM 456  C CD1 . ILE A 1 63  ? 17.053  14.906  -37.579 1.00 100.78 ? 63  ILE A CD1 1 
ATOM 457  N N   . PRO A 1 64  ? 18.832  20.506  -37.994 1.00 107.80 ? 64  PRO A N   1 
ATOM 458  C CA  . PRO A 1 64  ? 18.995  21.735  -38.780 1.00 105.32 ? 64  PRO A CA  1 
ATOM 459  C C   . PRO A 1 64  ? 18.767  21.493  -40.264 1.00 106.04 ? 64  PRO A C   1 
ATOM 460  O O   . PRO A 1 64  ? 19.007  20.408  -40.797 1.00 107.08 ? 64  PRO A O   1 
ATOM 461  C CB  . PRO A 1 64  ? 20.441  22.166  -38.507 1.00 104.76 ? 64  PRO A CB  1 
ATOM 462  C CG  . PRO A 1 64  ? 21.063  21.108  -37.684 1.00 103.72 ? 64  PRO A CG  1 
ATOM 463  C CD  . PRO A 1 64  ? 20.083  20.033  -37.379 1.00 104.73 ? 64  PRO A CD  1 
ATOM 464  N N   . ALA A 1 65  ? 18.295  22.545  -40.932 1.00 107.34 ? 65  ALA A N   1 
ATOM 465  C CA  . ALA A 1 65  ? 17.979  22.484  -42.353 1.00 107.26 ? 65  ALA A CA  1 
ATOM 466  C C   . ALA A 1 65  ? 19.230  22.240  -43.185 1.00 106.99 ? 65  ALA A C   1 
ATOM 467  O O   . ALA A 1 65  ? 20.192  23.013  -43.114 1.00 109.53 ? 65  ALA A O   1 
ATOM 468  C CB  . ALA A 1 65  ? 17.284  23.770  -42.803 1.00 104.60 ? 65  ALA A CB  1 
ATOM 469  N N   . GLY A 1 66  ? 19.229  21.168  -43.973 1.00 103.97 ? 66  GLY A N   1 
ATOM 470  C CA  . GLY A 1 66  ? 20.360  20.848  -44.819 1.00 102.50 ? 66  GLY A CA  1 
ATOM 471  C C   . GLY A 1 66  ? 21.209  19.716  -44.282 1.00 103.34 ? 66  GLY A C   1 
ATOM 472  O O   . GLY A 1 66  ? 22.267  19.405  -44.836 1.00 103.37 ? 66  GLY A O   1 
ATOM 473  N N   . THR A 1 67  ? 20.754  19.091  -43.200 1.00 104.80 ? 67  THR A N   1 
ATOM 474  C CA  . THR A 1 67  ? 21.508  18.002  -42.593 1.00 104.48 ? 67  THR A CA  1 
ATOM 475  C C   . THR A 1 67  ? 21.399  16.742  -43.441 1.00 103.22 ? 67  THR A C   1 
ATOM 476  O O   . THR A 1 67  ? 20.304  16.345  -43.848 1.00 105.48 ? 67  THR A O   1 
ATOM 477  C CB  . THR A 1 67  ? 20.996  17.733  -41.179 1.00 104.70 ? 67  THR A CB  1 
ATOM 478  O OG1 . THR A 1 67  ? 20.936  18.964  -40.449 1.00 104.59 ? 67  THR A OG1 1 
ATOM 479  C CG2 . THR A 1 67  ? 21.916  16.770  -40.456 1.00 103.76 ? 67  THR A CG2 1 
ATOM 480  N N   . THR A 1 68  ? 22.539  16.111  -43.704 1.00 103.77 ? 68  THR A N   1 
ATOM 481  C CA  . THR A 1 68  ? 22.602  14.901  -44.508 1.00 103.88 ? 68  THR A CA  1 
ATOM 482  C C   . THR A 1 68  ? 23.083  13.731  -43.660 1.00 103.13 ? 68  THR A C   1 
ATOM 483  O O   . THR A 1 68  ? 23.750  13.906  -42.637 1.00 105.67 ? 68  THR A O   1 
ATOM 484  C CB  . THR A 1 68  ? 23.529  15.087  -45.714 1.00 105.18 ? 68  THR A CB  1 
ATOM 485  O OG1 . THR A 1 68  ? 24.875  15.276  -45.262 1.00 108.30 ? 68  THR A OG1 1 
ATOM 486  C CG2 . THR A 1 68  ? 23.098  16.294  -46.533 1.00 103.82 ? 68  THR A CG2 1 
ATOM 487  N N   . ALA A 1 69  ? 22.734  12.526  -44.100 1.00 103.09 ? 69  ALA A N   1 
ATOM 488  C CA  . ALA A 1 69  ? 23.048  11.303  -43.376 1.00 106.48 ? 69  ALA A CA  1 
ATOM 489  C C   . ALA A 1 69  ? 24.205  10.568  -44.042 1.00 106.27 ? 69  ALA A C   1 
ATOM 490  O O   . ALA A 1 69  ? 24.284  10.496  -45.271 1.00 107.07 ? 69  ALA A O   1 
ATOM 491  C CB  . ALA A 1 69  ? 21.826  10.385  -43.303 1.00 106.61 ? 69  ALA A CB  1 
ATOM 492  N N   . ILE A 1 70  ? 25.100  10.025  -43.220 1.00 104.07 ? 70  ILE A N   1 
ATOM 493  C CA  . ILE A 1 70  ? 26.242  9.251   -43.689 1.00 105.22 ? 70  ILE A CA  1 
ATOM 494  C C   . ILE A 1 70  ? 25.997  7.754   -43.549 1.00 105.48 ? 70  ILE A C   1 
ATOM 495  O O   . ILE A 1 70  ? 26.099  7.008   -44.524 1.00 106.44 ? 70  ILE A O   1 
ATOM 496  C CB  . ILE A 1 70  ? 27.548  9.666   -42.969 1.00 105.39 ? 70  ILE A CB  1 
ATOM 497  C CG1 . ILE A 1 70  ? 27.792  11.180  -43.034 1.00 104.45 ? 70  ILE A CG1 1 
ATOM 498  C CG2 . ILE A 1 70  ? 28.736  8.909   -43.545 1.00 104.77 ? 70  ILE A CG2 1 
ATOM 499  C CD1 . ILE A 1 70  ? 27.079  11.999  -41.985 1.00 102.62 ? 70  ILE A CD1 1 
ATOM 500  N N   . SER A 1 71  ? 25.671  7.295   -42.343 1.00 104.17 ? 71  SER A N   1 
ATOM 501  C CA  . SER A 1 71  ? 25.462  5.872   -42.119 1.00 105.62 ? 71  SER A CA  1 
ATOM 502  C C   . SER A 1 71  ? 24.400  5.669   -41.049 1.00 107.26 ? 71  SER A C   1 
ATOM 503  O O   . SER A 1 71  ? 24.194  6.532   -40.193 1.00 106.75 ? 71  SER A O   1 
ATOM 504  C CB  . SER A 1 71  ? 26.761  5.169   -41.710 1.00 104.70 ? 71  SER A CB  1 
ATOM 505  O OG  . SER A 1 71  ? 26.957  5.231   -40.309 1.00 104.98 ? 71  SER A OG  1 
ATOM 506  N N   . LEU A 1 72  ? 23.730  4.522   -41.116 1.00 101.85 ? 72  LEU A N   1 
ATOM 507  C CA  . LEU A 1 72  ? 22.737  4.110   -40.132 1.00 99.84  ? 72  LEU A CA  1 
ATOM 508  C C   . LEU A 1 72  ? 23.038  2.674   -39.729 1.00 99.77  ? 72  LEU A C   1 
ATOM 509  O O   . LEU A 1 72  ? 22.860  1.751   -40.530 1.00 100.23 ? 72  LEU A O   1 
ATOM 510  C CB  . LEU A 1 72  ? 21.321  4.231   -40.694 1.00 99.99  ? 72  LEU A CB  1 
ATOM 511  C CG  . LEU A 1 72  ? 20.163  3.818   -39.784 1.00 100.03 ? 72  LEU A CG  1 
ATOM 512  C CD1 . LEU A 1 72  ? 20.074  4.723   -38.573 1.00 98.97  ? 72  LEU A CD1 1 
ATOM 513  C CD2 . LEU A 1 72  ? 18.860  3.844   -40.560 1.00 96.47  ? 72  LEU A CD2 1 
ATOM 514  N N   . SER A 1 73  ? 23.491  2.491   -38.493 1.00 95.07  ? 73  SER A N   1 
ATOM 515  C CA  . SER A 1 73  ? 23.912  1.181   -38.028 1.00 95.83  ? 73  SER A CA  1 
ATOM 516  C C   . SER A 1 73  ? 22.714  0.256   -37.850 1.00 96.26  ? 73  SER A C   1 
ATOM 517  O O   . SER A 1 73  ? 21.558  0.688   -37.812 1.00 96.29  ? 73  SER A O   1 
ATOM 518  C CB  . SER A 1 73  ? 24.681  1.302   -36.712 1.00 95.45  ? 73  SER A CB  1 
ATOM 519  O OG  . SER A 1 73  ? 23.823  1.103   -35.603 1.00 96.15  ? 73  SER A OG  1 
ATOM 520  N N   . THR A 1 74  ? 23.007  -1.043  -37.741 1.00 94.85  ? 74  THR A N   1 
ATOM 521  C CA  . THR A 1 74  ? 21.956  -2.022  -37.496 1.00 94.13  ? 74  THR A CA  1 
ATOM 522  C C   . THR A 1 74  ? 21.309  -1.832  -36.130 1.00 95.13  ? 74  THR A C   1 
ATOM 523  O O   . THR A 1 74  ? 20.227  -2.376  -35.887 1.00 96.72  ? 74  THR A O   1 
ATOM 524  C CB  . THR A 1 74  ? 22.514  -3.443  -37.626 1.00 94.93  ? 74  THR A CB  1 
ATOM 525  O OG1 . THR A 1 74  ? 21.462  -4.338  -38.008 1.00 93.35  ? 74  THR A OG1 1 
ATOM 526  C CG2 . THR A 1 74  ? 23.124  -3.911  -36.312 1.00 92.59  ? 74  THR A CG2 1 
ATOM 527  N N   . ALA A 1 75  ? 21.947  -1.075  -35.237 1.00 93.36  ? 75  ALA A N   1 
ATOM 528  C CA  . ALA A 1 75  ? 21.352  -0.673  -33.973 1.00 92.63  ? 75  ALA A CA  1 
ATOM 529  C C   . ALA A 1 75  ? 20.617  0.654   -34.084 1.00 94.12  ? 75  ALA A C   1 
ATOM 530  O O   . ALA A 1 75  ? 20.370  1.302   -33.062 1.00 94.18  ? 75  ALA A O   1 
ATOM 531  C CB  . ALA A 1 75  ? 22.425  -0.592  -32.886 1.00 92.12  ? 75  ALA A CB  1 
ATOM 532  N N   . ALA A 1 76  ? 20.285  1.075   -35.307 1.00 88.98  ? 76  ALA A N   1 
ATOM 533  C CA  . ALA A 1 76  ? 19.561  2.312   -35.575 1.00 89.86  ? 76  ALA A CA  1 
ATOM 534  C C   . ALA A 1 76  ? 20.333  3.535   -35.097 1.00 91.93  ? 76  ALA A C   1 
ATOM 535  O O   . ALA A 1 76  ? 19.735  4.571   -34.794 1.00 93.63  ? 76  ALA A O   1 
ATOM 536  C CB  . ALA A 1 76  ? 18.171  2.283   -34.937 1.00 88.97  ? 76  ALA A CB  1 
ATOM 537  N N   . VAL A 1 77  ? 21.654  3.429   -35.021 1.00 97.55  ? 77  VAL A N   1 
ATOM 538  C CA  . VAL A 1 77  ? 22.499  4.570   -34.696 1.00 97.63  ? 77  VAL A CA  1 
ATOM 539  C C   . VAL A 1 77  ? 22.695  5.382   -35.968 1.00 96.37  ? 77  VAL A C   1 
ATOM 540  O O   . VAL A 1 77  ? 23.356  4.930   -36.910 1.00 96.48  ? 77  VAL A O   1 
ATOM 541  C CB  . VAL A 1 77  ? 23.845  4.122   -34.111 1.00 98.28  ? 77  VAL A CB  1 
ATOM 542  C CG1 . VAL A 1 77  ? 24.762  5.318   -33.918 1.00 96.31  ? 77  VAL A CG1 1 
ATOM 543  C CG2 . VAL A 1 77  ? 23.630  3.389   -32.797 1.00 95.79  ? 77  VAL A CG2 1 
ATOM 544  N N   . LEU A 1 78  ? 22.118  6.580   -36.001 1.00 94.89  ? 78  LEU A N   1 
ATOM 545  C CA  . LEU A 1 78  ? 22.165  7.441   -37.174 1.00 96.99  ? 78  LEU A CA  1 
ATOM 546  C C   . LEU A 1 78  ? 23.210  8.526   -36.960 1.00 98.58  ? 78  LEU A C   1 
ATOM 547  O O   . LEU A 1 78  ? 23.115  9.303   -36.004 1.00 100.27 ? 78  LEU A O   1 
ATOM 548  C CB  . LEU A 1 78  ? 20.798  8.068   -37.448 1.00 96.33  ? 78  LEU A CB  1 
ATOM 549  C CG  . LEU A 1 78  ? 20.746  9.064   -38.607 1.00 94.53  ? 78  LEU A CG  1 
ATOM 550  C CD1 . LEU A 1 78  ? 20.734  8.338   -39.942 1.00 95.94  ? 78  LEU A CD1 1 
ATOM 551  C CD2 . LEU A 1 78  ? 19.539  9.979   -38.480 1.00 94.77  ? 78  LEU A CD2 1 
ATOM 552  N N   . VAL A 1 79  ? 24.195  8.580   -37.848 1.00 104.99 ? 79  VAL A N   1 
ATOM 553  C CA  . VAL A 1 79  ? 25.191  9.643   -37.849 1.00 105.54 ? 79  VAL A CA  1 
ATOM 554  C C   . VAL A 1 79  ? 24.860  10.575  -39.010 1.00 102.81 ? 79  VAL A C   1 
ATOM 555  O O   . VAL A 1 79  ? 24.828  10.160  -40.174 1.00 101.25 ? 79  VAL A O   1 
ATOM 556  C CB  . VAL A 1 79  ? 26.623  9.092   -37.935 1.00 104.53 ? 79  VAL A CB  1 
ATOM 557  C CG1 . VAL A 1 79  ? 26.959  8.319   -36.673 1.00 103.13 ? 79  VAL A CG1 1 
ATOM 558  C CG2 . VAL A 1 79  ? 26.799  8.187   -39.142 1.00 103.38 ? 79  VAL A CG2 1 
ATOM 559  N N   . HIS A 1 80  ? 24.568  11.827  -38.693 1.00 106.20 ? 80  HIS A N   1 
ATOM 560  C CA  . HIS A 1 80  ? 24.272  12.825  -39.702 1.00 107.56 ? 80  HIS A CA  1 
ATOM 561  C C   . HIS A 1 80  ? 25.406  13.848  -39.750 1.00 110.16 ? 80  HIS A C   1 
ATOM 562  O O   . HIS A 1 80  ? 26.400  13.743  -39.025 1.00 107.83 ? 80  HIS A O   1 
ATOM 563  C CB  . HIS A 1 80  ? 22.910  13.475  -39.442 1.00 104.57 ? 80  HIS A CB  1 
ATOM 564  C CG  . HIS A 1 80  ? 22.637  13.782  -38.002 1.00 106.10 ? 80  HIS A CG  1 
ATOM 565  N ND1 . HIS A 1 80  ? 22.428  15.065  -37.545 1.00 107.54 ? 80  HIS A ND1 1 
ATOM 566  C CD2 . HIS A 1 80  ? 22.499  12.973  -36.924 1.00 105.83 ? 80  HIS A CD2 1 
ATOM 567  C CE1 . HIS A 1 80  ? 22.199  15.035  -36.244 1.00 108.39 ? 80  HIS A CE1 1 
ATOM 568  N NE2 . HIS A 1 80  ? 22.237  13.778  -35.843 1.00 108.80 ? 80  HIS A NE2 1 
ATOM 569  N N   . SER A 1 81  ? 25.268  14.842  -40.628 1.00 112.14 ? 81  SER A N   1 
ATOM 570  C CA  . SER A 1 81  ? 26.345  15.805  -40.819 1.00 109.78 ? 81  SER A CA  1 
ATOM 571  C C   . SER A 1 81  ? 26.537  16.680  -39.586 1.00 111.15 ? 81  SER A C   1 
ATOM 572  O O   . SER A 1 81  ? 27.651  17.139  -39.309 1.00 111.26 ? 81  SER A O   1 
ATOM 573  C CB  . SER A 1 81  ? 26.070  16.659  -42.057 1.00 108.58 ? 81  SER A CB  1 
ATOM 574  O OG  . SER A 1 81  ? 24.915  17.459  -41.880 1.00 109.10 ? 81  SER A OG  1 
ATOM 575  N N   . GLN A 1 82  ? 25.467  16.922  -38.832 1.00 113.05 ? 82  GLN A N   1 
ATOM 576  C CA  . GLN A 1 82  ? 25.541  17.750  -37.636 1.00 112.88 ? 82  GLN A CA  1 
ATOM 577  C C   . GLN A 1 82  ? 25.718  16.952  -36.351 1.00 112.87 ? 82  GLN A C   1 
ATOM 578  O O   . GLN A 1 82  ? 25.755  17.552  -35.272 1.00 114.64 ? 82  GLN A O   1 
ATOM 579  C CB  . GLN A 1 82  ? 24.291  18.631  -37.521 1.00 110.75 ? 82  GLN A CB  1 
ATOM 580  C CG  . GLN A 1 82  ? 24.412  19.990  -38.202 1.00 112.03 ? 82  GLN A CG  1 
ATOM 581  C CD  . GLN A 1 82  ? 24.214  19.929  -39.705 1.00 114.59 ? 82  GLN A CD  1 
ATOM 582  O OE1 . GLN A 1 82  ? 24.443  18.899  -40.335 1.00 115.65 ? 82  GLN A OE1 1 
ATOM 583  N NE2 . GLN A 1 82  ? 23.782  21.041  -40.287 1.00 113.51 ? 82  GLN A NE2 1 
ATOM 584  N N   . GLY A 1 83  ? 25.827  15.631  -36.425 1.00 106.50 ? 83  GLY A N   1 
ATOM 585  C CA  . GLY A 1 83  ? 26.049  14.850  -35.227 1.00 106.96 ? 83  GLY A CA  1 
ATOM 586  C C   . GLY A 1 83  ? 25.608  13.413  -35.417 1.00 107.01 ? 83  GLY A C   1 
ATOM 587  O O   . GLY A 1 83  ? 25.475  12.924  -36.540 1.00 107.85 ? 83  GLY A O   1 
ATOM 588  N N   . SER A 1 84  ? 25.397  12.745  -34.285 1.00 103.22 ? 84  SER A N   1 
ATOM 589  C CA  . SER A 1 84  ? 24.956  11.359  -34.248 1.00 104.41 ? 84  SER A CA  1 
ATOM 590  C C   . SER A 1 84  ? 23.758  11.229  -33.318 1.00 104.84 ? 84  SER A C   1 
ATOM 591  O O   . SER A 1 84  ? 23.722  11.843  -32.247 1.00 103.34 ? 84  SER A O   1 
ATOM 592  C CB  . SER A 1 84  ? 26.081  10.431  -33.782 1.00 102.94 ? 84  SER A CB  1 
ATOM 593  O OG  . SER A 1 84  ? 25.663  9.077   -33.804 1.00 100.01 ? 84  SER A OG  1 
ATOM 594  N N   . VAL A 1 85  ? 22.780  10.428  -33.733 1.00 101.71 ? 85  VAL A N   1 
ATOM 595  C CA  . VAL A 1 85  ? 21.569  10.194  -32.957 1.00 96.05  ? 85  VAL A CA  1 
ATOM 596  C C   . VAL A 1 85  ? 21.323  8.696   -32.861 1.00 94.94  ? 85  VAL A C   1 
ATOM 597  O O   . VAL A 1 85  ? 21.348  7.987   -33.873 1.00 95.93  ? 85  VAL A O   1 
ATOM 598  C CB  . VAL A 1 85  ? 20.347  10.903  -33.576 1.00 94.20  ? 85  VAL A CB  1 
ATOM 599  C CG1 . VAL A 1 85  ? 19.066  10.397  -32.938 1.00 96.93  ? 85  VAL A CG1 1 
ATOM 600  C CG2 . VAL A 1 85  ? 20.465  12.406  -33.407 1.00 96.06  ? 85  VAL A CG2 1 
ATOM 601  N N   . ASP A 1 86  ? 21.088  8.217   -31.642 1.00 89.71  ? 86  ASP A N   1 
ATOM 602  C CA  . ASP A 1 86  ? 20.678  6.833   -31.417 1.00 90.68  ? 86  ASP A CA  1 
ATOM 603  C C   . ASP A 1 86  ? 19.166  6.769   -31.582 1.00 91.69  ? 86  ASP A C   1 
ATOM 604  O O   . ASP A 1 86  ? 18.415  7.058   -30.647 1.00 91.01  ? 86  ASP A O   1 
ATOM 605  C CB  . ASP A 1 86  ? 21.113  6.358   -30.036 1.00 89.89  ? 86  ASP A CB  1 
ATOM 606  C CG  . ASP A 1 86  ? 20.840  4.884   -29.811 1.00 93.64  ? 86  ASP A CG  1 
ATOM 607  O OD1 . ASP A 1 86  ? 20.456  4.189   -30.774 1.00 91.18  ? 86  ASP A OD1 1 
ATOM 608  O OD2 . ASP A 1 86  ? 21.010  4.416   -28.666 1.00 96.71  ? 86  ASP A OD2 1 
ATOM 609  N N   . LEU A 1 87  ? 18.714  6.397   -32.782 1.00 85.34  ? 87  LEU A N   1 
ATOM 610  C CA  . LEU A 1 87  ? 17.282  6.373   -33.058 1.00 81.24  ? 87  LEU A CA  1 
ATOM 611  C C   . LEU A 1 87  ? 16.559  5.338   -32.209 1.00 84.43  ? 87  LEU A C   1 
ATOM 612  O O   . LEU A 1 87  ? 15.367  5.494   -31.931 1.00 87.46  ? 87  LEU A O   1 
ATOM 613  C CB  . LEU A 1 87  ? 17.039  6.107   -34.542 1.00 82.49  ? 87  LEU A CB  1 
ATOM 614  C CG  . LEU A 1 87  ? 17.417  7.250   -35.481 1.00 82.98  ? 87  LEU A CG  1 
ATOM 615  C CD1 . LEU A 1 87  ? 17.352  6.788   -36.922 1.00 83.09  ? 87  LEU A CD1 1 
ATOM 616  C CD2 . LEU A 1 87  ? 16.514  8.452   -35.257 1.00 80.13  ? 87  LEU A CD2 1 
ATOM 617  N N   . GLY A 1 88  ? 17.256  4.280   -31.793 1.00 84.52  ? 88  GLY A N   1 
ATOM 618  C CA  . GLY A 1 88  ? 16.652  3.331   -30.874 1.00 83.50  ? 88  GLY A CA  1 
ATOM 619  C C   . GLY A 1 88  ? 16.318  3.957   -29.535 1.00 84.75  ? 88  GLY A C   1 
ATOM 620  O O   . GLY A 1 88  ? 15.253  3.706   -28.968 1.00 88.77  ? 88  GLY A O   1 
ATOM 621  N N   . ALA A 1 89  ? 17.223  4.788   -29.013 1.00 86.08  ? 89  ALA A N   1 
ATOM 622  C CA  . ALA A 1 89  ? 16.945  5.495   -27.767 1.00 85.80  ? 89  ALA A CA  1 
ATOM 623  C C   . ALA A 1 89  ? 15.784  6.465   -27.931 1.00 84.32  ? 89  ALA A C   1 
ATOM 624  O O   . ALA A 1 89  ? 14.951  6.606   -27.028 1.00 85.44  ? 89  ALA A O   1 
ATOM 625  C CB  . ALA A 1 89  ? 18.198  6.228   -27.289 1.00 84.74  ? 89  ALA A CB  1 
ATOM 626  N N   . VAL A 1 90  ? 15.711  7.145   -29.077 1.00 76.49  ? 90  VAL A N   1 
ATOM 627  C CA  . VAL A 1 90  ? 14.599  8.052   -29.337 1.00 78.36  ? 90  VAL A CA  1 
ATOM 628  C C   . VAL A 1 90  ? 13.283  7.284   -29.379 1.00 82.60  ? 90  VAL A C   1 
ATOM 629  O O   . VAL A 1 90  ? 12.273  7.725   -28.819 1.00 88.07  ? 90  VAL A O   1 
ATOM 630  C CB  . VAL A 1 90  ? 14.843  8.835   -30.640 1.00 80.05  ? 90  VAL A CB  1 
ATOM 631  C CG1 . VAL A 1 90  ? 13.620  9.656   -31.008 1.00 77.94  ? 90  VAL A CG1 1 
ATOM 632  C CG2 . VAL A 1 90  ? 16.067  9.722   -30.501 1.00 79.06  ? 90  VAL A CG2 1 
ATOM 633  N N   . ALA A 1 91  ? 13.276  6.124   -30.039 1.00 77.37  ? 91  ALA A N   1 
ATOM 634  C CA  . ALA A 1 91  ? 12.066  5.310   -30.100 1.00 74.96  ? 91  ALA A CA  1 
ATOM 635  C C   . ALA A 1 91  ? 11.671  4.800   -28.720 1.00 76.01  ? 91  ALA A C   1 
ATOM 636  O O   . ALA A 1 91  ? 10.480  4.738   -28.394 1.00 81.97  ? 91  ALA A O   1 
ATOM 637  C CB  . ALA A 1 91  ? 12.267  4.147   -31.069 1.00 72.36  ? 91  ALA A CB  1 
ATOM 638  N N   . VAL A 1 92  ? 12.653  4.420   -27.900 1.00 66.67  ? 92  VAL A N   1 
ATOM 639  C CA  . VAL A 1 92  ? 12.361  4.006   -26.531 1.00 64.78  ? 92  VAL A CA  1 
ATOM 640  C C   . VAL A 1 92  ? 11.745  5.156   -25.748 1.00 70.43  ? 92  VAL A C   1 
ATOM 641  O O   . VAL A 1 92  ? 10.780  4.969   -24.998 1.00 76.46  ? 92  VAL A O   1 
ATOM 642  C CB  . VAL A 1 92  ? 13.634  3.475   -25.849 1.00 70.23  ? 92  VAL A CB  1 
ATOM 643  C CG1 . VAL A 1 92  ? 13.429  3.365   -24.349 1.00 71.76  ? 92  VAL A CG1 1 
ATOM 644  C CG2 . VAL A 1 92  ? 14.015  2.130   -26.422 1.00 71.70  ? 92  VAL A CG2 1 
ATOM 645  N N   . LEU A 1 93  ? 12.290  6.363   -25.910 1.00 72.33  ? 93  LEU A N   1 
ATOM 646  C CA  . LEU A 1 93  ? 11.725  7.527   -25.239 1.00 75.13  ? 93  LEU A CA  1 
ATOM 647  C C   . LEU A 1 93  ? 10.297  7.792   -25.692 1.00 73.05  ? 93  LEU A C   1 
ATOM 648  O O   . LEU A 1 93  ? 9.437   8.128   -24.872 1.00 78.74  ? 93  LEU A O   1 
ATOM 649  C CB  . LEU A 1 93  ? 12.599  8.754   -25.490 1.00 78.45  ? 93  LEU A CB  1 
ATOM 650  C CG  . LEU A 1 93  ? 12.690  9.756   -24.339 1.00 80.02  ? 93  LEU A CG  1 
ATOM 651  C CD1 . LEU A 1 93  ? 13.701  9.288   -23.306 1.00 76.66  ? 93  LEU A CD1 1 
ATOM 652  C CD2 . LEU A 1 93  ? 13.050  11.137  -24.859 1.00 78.06  ? 93  LEU A CD2 1 
ATOM 653  N N   . ARG A 1 94  ? 10.024  7.641   -26.986 1.00 66.18  ? 94  ARG A N   1 
ATOM 654  C CA  . ARG A 1 94  ? 8.679   7.811   -27.514 1.00 66.50  ? 94  ARG A CA  1 
ATOM 655  C C   . ARG A 1 94  ? 7.835   6.549   -27.410 1.00 67.26  ? 94  ARG A C   1 
ATOM 656  O O   . ARG A 1 94  ? 6.685   6.557   -27.860 1.00 73.39  ? 94  ARG A O   1 
ATOM 657  C CB  . ARG A 1 94  ? 8.736   8.271   -28.974 1.00 69.38  ? 94  ARG A CB  1 
ATOM 658  C CG  . ARG A 1 94  ? 9.639   9.468   -29.208 1.00 67.50  ? 94  ARG A CG  1 
ATOM 659  C CD  . ARG A 1 94  ? 9.901   9.682   -30.689 1.00 68.38  ? 94  ARG A CD  1 
ATOM 660  N NE  . ARG A 1 94  ? 8.678   9.661   -31.483 1.00 71.51  ? 94  ARG A NE  1 
ATOM 661  C CZ  . ARG A 1 94  ? 7.733   10.590  -31.441 1.00 70.41  ? 94  ARG A CZ  1 
ATOM 662  N NH1 . ARG A 1 94  ? 7.842   11.656  -30.665 1.00 68.03  ? 94  ARG A NH1 1 
ATOM 663  N NH2 . ARG A 1 94  ? 6.652   10.451  -32.204 1.00 72.77  ? 94  ARG A NH2 1 
ATOM 664  N N   . LYS A 1 95  ? 8.380   5.474   -26.836 1.00 71.47  ? 95  LYS A N   1 
ATOM 665  C CA  . LYS A 1 95  ? 7.677   4.199   -26.681 1.00 67.02  ? 95  LYS A CA  1 
ATOM 666  C C   . LYS A 1 95  ? 7.202   3.643   -28.018 1.00 70.48  ? 95  LYS A C   1 
ATOM 667  O O   . LYS A 1 95  ? 6.150   3.005   -28.100 1.00 72.08  ? 95  LYS A O   1 
ATOM 668  C CB  . LYS A 1 95  ? 6.503   4.319   -25.707 1.00 63.85  ? 95  LYS A CB  1 
ATOM 669  C CG  . LYS A 1 95  ? 6.910   4.693   -24.299 1.00 66.66  ? 95  LYS A CG  1 
ATOM 670  C CD  . LYS A 1 95  ? 6.322   3.726   -23.293 1.00 70.90  ? 95  LYS A CD  1 
ATOM 671  C CE  . LYS A 1 95  ? 6.538   4.212   -21.877 1.00 70.94  ? 95  LYS A CE  1 
ATOM 672  N NZ  . LYS A 1 95  ? 7.978   4.451   -21.588 1.00 73.69  ? 95  LYS A NZ  1 
ATOM 673  N N   . GLU A 1 96  ? 7.974   3.884   -29.075 1.00 71.27  ? 96  GLU A N   1 
ATOM 674  C CA  . GLU A 1 96  ? 7.695   3.310   -30.389 1.00 68.43  ? 96  GLU A CA  1 
ATOM 675  C C   . GLU A 1 96  ? 8.447   1.986   -30.483 1.00 70.54  ? 96  GLU A C   1 
ATOM 676  O O   . GLU A 1 96  ? 9.465   1.849   -31.164 1.00 71.37  ? 96  GLU A O   1 
ATOM 677  C CB  . GLU A 1 96  ? 8.090   4.281   -31.491 1.00 71.52  ? 96  GLU A CB  1 
ATOM 678  C CG  . GLU A 1 96  ? 7.302   5.577   -31.463 1.00 67.64  ? 96  GLU A CG  1 
ATOM 679  C CD  . GLU A 1 96  ? 7.903   6.641   -32.351 1.00 77.53  ? 96  GLU A CD  1 
ATOM 680  O OE1 . GLU A 1 96  ? 8.997   6.402   -32.906 1.00 79.91  ? 96  GLU A OE1 1 
ATOM 681  O OE2 . GLU A 1 96  ? 7.283   7.714   -32.499 1.00 78.20  ? 96  GLU A OE2 1 
ATOM 682  N N   . TYR A 1 97  ? 7.923   0.995   -29.771 1.00 69.77  ? 97  TYR A N   1 
ATOM 683  C CA  . TYR A 1 97  ? 8.571   -0.297  -29.619 1.00 67.21  ? 97  TYR A CA  1 
ATOM 684  C C   . TYR A 1 97  ? 8.250   -1.203  -30.798 1.00 69.00  ? 97  TYR A C   1 
ATOM 685  O O   . TYR A 1 97  ? 7.187   -1.085  -31.415 1.00 74.74  ? 97  TYR A O   1 
ATOM 686  C CB  . TYR A 1 97  ? 8.133   -0.974  -28.320 1.00 64.90  ? 97  TYR A CB  1 
ATOM 687  C CG  . TYR A 1 97  ? 8.478   -0.199  -27.073 1.00 67.98  ? 97  TYR A CG  1 
ATOM 688  C CD1 . TYR A 1 97  ? 9.793   0.140   -26.783 1.00 70.71  ? 97  TYR A CD1 1 
ATOM 689  C CD2 . TYR A 1 97  ? 7.491   0.191   -26.182 1.00 67.59  ? 97  TYR A CD2 1 
ATOM 690  C CE1 . TYR A 1 97  ? 10.111  0.845   -25.643 1.00 70.62  ? 97  TYR A CE1 1 
ATOM 691  C CE2 . TYR A 1 97  ? 7.800   0.898   -25.039 1.00 69.18  ? 97  TYR A CE2 1 
ATOM 692  C CZ  . TYR A 1 97  ? 9.111   1.223   -24.774 1.00 72.03  ? 97  TYR A CZ  1 
ATOM 693  O OH  . TYR A 1 97  ? 9.423   1.926   -23.635 1.00 77.09  ? 97  TYR A OH  1 
ATOM 694  N N   . VAL A 1 98  ? 9.175   -2.104  -31.104 1.00 64.83  ? 98  VAL A N   1 
ATOM 695  C CA  . VAL A 1 98  ? 8.965   -3.158  -32.087 1.00 61.35  ? 98  VAL A CA  1 
ATOM 696  C C   . VAL A 1 98  ? 8.999   -4.480  -31.337 1.00 65.95  ? 98  VAL A C   1 
ATOM 697  O O   . VAL A 1 98  ? 10.044  -4.876  -30.808 1.00 73.24  ? 98  VAL A O   1 
ATOM 698  C CB  . VAL A 1 98  ? 10.020  -3.123  -33.201 1.00 61.80  ? 98  VAL A CB  1 
ATOM 699  C CG1 . VAL A 1 98  ? 9.834   -4.305  -34.135 1.00 62.78  ? 98  VAL A CG1 1 
ATOM 700  C CG2 . VAL A 1 98  ? 9.936   -1.816  -33.967 1.00 68.38  ? 98  VAL A CG2 1 
ATOM 701  N N   . THR A 1 99  ? 7.861   -5.164  -31.283 1.00 70.11  ? 99  THR A N   1 
ATOM 702  C CA  . THR A 1 99  ? 7.794   -6.459  -30.614 1.00 68.80  ? 99  THR A CA  1 
ATOM 703  C C   . THR A 1 99  ? 8.406   -7.515  -31.524 1.00 75.17  ? 99  THR A C   1 
ATOM 704  O O   . THR A 1 99  ? 7.744   -8.014  -32.440 1.00 74.37  ? 99  THR A O   1 
ATOM 705  C CB  . THR A 1 99  ? 6.351   -6.806  -30.264 1.00 68.61  ? 99  THR A CB  1 
ATOM 706  O OG1 . THR A 1 99  ? 5.749   -5.705  -29.572 1.00 72.54  ? 99  THR A OG1 1 
ATOM 707  C CG2 . THR A 1 99  ? 6.304   -8.032  -29.370 1.00 67.29  ? 99  THR A CG2 1 
ATOM 708  N N   . ILE A 1 100 ? 9.669   -7.850  -31.278 1.00 79.81  ? 100 ILE A N   1 
ATOM 709  C CA  . ILE A 1 100 ? 10.410  -8.774  -32.131 1.00 72.53  ? 100 ILE A CA  1 
ATOM 710  C C   . ILE A 1 100 ? 9.742   -10.142 -32.086 1.00 75.14  ? 100 ILE A C   1 
ATOM 711  O O   . ILE A 1 100 ? 9.245   -10.556 -31.029 1.00 77.74  ? 100 ILE A O   1 
ATOM 712  C CB  . ILE A 1 100 ? 11.885  -8.866  -31.712 1.00 72.83  ? 100 ILE A CB  1 
ATOM 713  C CG1 . ILE A 1 100 ? 12.010  -8.906  -30.189 1.00 74.41  ? 100 ILE A CG1 1 
ATOM 714  C CG2 . ILE A 1 100 ? 12.667  -7.701  -32.283 1.00 73.68  ? 100 ILE A CG2 1 
ATOM 715  C CD1 . ILE A 1 100 ? 13.405  -9.219  -29.703 1.00 75.04  ? 100 ILE A CD1 1 
ATOM 716  N N   . PRO A 1 101 ? 9.695   -10.866 -33.200 1.00 79.24  ? 101 PRO A N   1 
ATOM 717  C CA  . PRO A 1 101 ? 9.043   -12.184 -33.222 1.00 81.54  ? 101 PRO A CA  1 
ATOM 718  C C   . PRO A 1 101 ? 9.814   -13.184 -32.376 1.00 81.52  ? 101 PRO A C   1 
ATOM 719  O O   . PRO A 1 101 ? 11.047  -13.235 -32.411 1.00 81.72  ? 101 PRO A O   1 
ATOM 720  C CB  . PRO A 1 101 ? 9.055   -12.559 -34.712 1.00 77.30  ? 101 PRO A CB  1 
ATOM 721  C CG  . PRO A 1 101 ? 9.725   -11.460 -35.434 1.00 75.30  ? 101 PRO A CG  1 
ATOM 722  C CD  . PRO A 1 101 ? 10.305  -10.497 -34.485 1.00 74.54  ? 101 PRO A CD  1 
ATOM 723  N N   . GLY A 1 102 ? 9.084   -13.979 -31.605 1.00 86.22  ? 102 GLY A N   1 
ATOM 724  C CA  . GLY A 1 102 ? 9.655   -14.946 -30.700 1.00 86.95  ? 102 GLY A CA  1 
ATOM 725  C C   . GLY A 1 102 ? 9.393   -14.546 -29.271 1.00 89.37  ? 102 GLY A C   1 
ATOM 726  O O   . GLY A 1 102 ? 8.660   -13.593 -28.988 1.00 91.80  ? 102 GLY A O   1 
ATOM 727  N N   . ASP A 1 103 ? 10.000  -15.282 -28.349 1.00 92.46  ? 103 ASP A N   1 
ATOM 728  C CA  . ASP A 1 103 ? 9.880   -15.006 -26.927 1.00 90.89  ? 103 ASP A CA  1 
ATOM 729  C C   . ASP A 1 103 ? 11.190  -15.363 -26.238 1.00 92.13  ? 103 ASP A C   1 
ATOM 730  O O   . ASP A 1 103 ? 12.169  -15.758 -26.879 1.00 95.42  ? 103 ASP A O   1 
ATOM 731  C CB  . ASP A 1 103 ? 8.703   -15.773 -26.311 1.00 92.30  ? 103 ASP A CB  1 
ATOM 732  C CG  . ASP A 1 103 ? 8.528   -17.153 -26.910 1.00 97.41  ? 103 ASP A CG  1 
ATOM 733  O OD1 . ASP A 1 103 ? 7.387   -17.505 -27.273 1.00 96.18  ? 103 ASP A OD1 1 
ATOM 734  O OD2 . ASP A 1 103 ? 9.532   -17.888 -27.016 1.00 98.98  ? 103 ASP A OD2 1 
ATOM 735  N N   . PHE A 1 104 ? 11.208  -15.209 -24.914 1.00 92.18  ? 104 PHE A N   1 
ATOM 736  C CA  . PHE A 1 104 ? 12.376  -15.584 -24.132 1.00 92.29  ? 104 PHE A CA  1 
ATOM 737  C C   . PHE A 1 104 ? 12.637  -17.083 -24.155 1.00 94.79  ? 104 PHE A C   1 
ATOM 738  O O   . PHE A 1 104 ? 13.801  -17.494 -24.196 1.00 96.19  ? 104 PHE A O   1 
ATOM 739  C CB  . PHE A 1 104 ? 12.215  -15.113 -22.685 1.00 89.65  ? 104 PHE A CB  1 
ATOM 740  C CG  . PHE A 1 104 ? 12.601  -13.679 -22.466 1.00 88.92  ? 104 PHE A CG  1 
ATOM 741  C CD1 . PHE A 1 104 ? 13.899  -13.340 -22.128 1.00 90.56  ? 104 PHE A CD1 1 
ATOM 742  C CD2 . PHE A 1 104 ? 11.661  -12.669 -22.587 1.00 88.55  ? 104 PHE A CD2 1 
ATOM 743  C CE1 . PHE A 1 104 ? 14.256  -12.023 -21.923 1.00 91.07  ? 104 PHE A CE1 1 
ATOM 744  C CE2 . PHE A 1 104 ? 12.012  -11.350 -22.383 1.00 88.58  ? 104 PHE A CE2 1 
ATOM 745  C CZ  . PHE A 1 104 ? 13.311  -11.026 -22.051 1.00 90.35  ? 104 PHE A CZ  1 
ATOM 746  N N   . THR A 1 105 ? 11.585  -17.904 -24.131 1.00 95.45  ? 105 THR A N   1 
ATOM 747  C CA  . THR A 1 105 ? 11.761  -19.352 -24.115 1.00 95.46  ? 105 THR A CA  1 
ATOM 748  C C   . THR A 1 105 ? 12.335  -19.887 -25.419 1.00 95.14  ? 105 THR A C   1 
ATOM 749  O O   . THR A 1 105 ? 12.847  -21.011 -25.440 1.00 96.15  ? 105 THR A O   1 
ATOM 750  C CB  . THR A 1 105 ? 10.429  -20.044 -23.823 1.00 95.91  ? 105 THR A CB  1 
ATOM 751  O OG1 . THR A 1 105 ? 9.442   -19.594 -24.759 1.00 96.10  ? 105 THR A OG1 1 
ATOM 752  C CG2 . THR A 1 105 ? 9.963   -19.727 -22.412 1.00 93.96  ? 105 THR A CG2 1 
ATOM 753  N N   . SER A 1 106 ? 12.258  -19.117 -26.504 1.00 94.37  ? 106 SER A N   1 
ATOM 754  C CA  . SER A 1 106 ? 12.780  -19.546 -27.795 1.00 96.93  ? 106 SER A CA  1 
ATOM 755  C C   . SER A 1 106 ? 14.100  -18.872 -28.140 1.00 96.46  ? 106 SER A C   1 
ATOM 756  O O   . SER A 1 106 ? 14.886  -19.431 -28.913 1.00 97.82  ? 106 SER A O   1 
ATOM 757  C CB  . SER A 1 106 ? 11.756  -19.276 -28.899 1.00 92.33  ? 106 SER A CB  1 
ATOM 758  O OG  . SER A 1 106 ? 11.546  -17.885 -29.062 1.00 91.69  ? 106 SER A OG  1 
ATOM 759  N N   . GLY A 1 107 ? 14.359  -17.686 -27.600 1.00 91.46  ? 107 GLY A N   1 
ATOM 760  C CA  . GLY A 1 107 ? 15.620  -17.015 -27.839 1.00 93.60  ? 107 GLY A CA  1 
ATOM 761  C C   . GLY A 1 107 ? 15.578  -16.072 -29.022 1.00 94.09  ? 107 GLY A C   1 
ATOM 762  O O   . GLY A 1 107 ? 15.390  -16.504 -30.163 1.00 99.15  ? 107 GLY A O   1 
ATOM 763  N N   . ALA A 1 108 ? 15.748  -14.780 -28.764 1.00 87.75  ? 108 ALA A N   1 
ATOM 764  C CA  . ALA A 1 108 ? 15.804  -13.778 -29.814 1.00 89.99  ? 108 ALA A CA  1 
ATOM 765  C C   . ALA A 1 108 ? 16.937  -12.807 -29.517 1.00 91.14  ? 108 ALA A C   1 
ATOM 766  O O   . ALA A 1 108 ? 17.296  -12.572 -28.362 1.00 93.26  ? 108 ALA A O   1 
ATOM 767  C CB  . ALA A 1 108 ? 14.478  -13.020 -29.947 1.00 94.63  ? 108 ALA A CB  1 
ATOM 768  N N   . THR A 1 109 ? 17.501  -12.242 -30.578 1.00 92.82  ? 109 THR A N   1 
ATOM 769  C CA  . THR A 1 109 ? 18.610  -11.309 -30.448 1.00 94.23  ? 109 THR A CA  1 
ATOM 770  C C   . THR A 1 109 ? 18.110  -9.890  -30.690 1.00 94.00  ? 109 THR A C   1 
ATOM 771  O O   . THR A 1 109 ? 17.444  -9.622  -31.694 1.00 97.34  ? 109 THR A O   1 
ATOM 772  C CB  . THR A 1 109 ? 19.728  -11.656 -31.429 1.00 95.93  ? 109 THR A CB  1 
ATOM 773  O OG1 . THR A 1 109 ? 20.128  -13.018 -31.232 1.00 98.31  ? 109 THR A OG1 1 
ATOM 774  C CG2 . THR A 1 109 ? 20.927  -10.757 -31.196 1.00 94.04  ? 109 THR A CG2 1 
ATOM 775  N N   . ILE A 1 110 ? 18.431  -8.990  -29.767 1.00 87.47  ? 110 ILE A N   1 
ATOM 776  C CA  . ILE A 1 110 ? 17.945  -7.615  -29.801 1.00 88.36  ? 110 ILE A CA  1 
ATOM 777  C C   . ILE A 1 110 ? 19.013  -6.740  -30.443 1.00 88.81  ? 110 ILE A C   1 
ATOM 778  O O   . ILE A 1 110 ? 20.103  -6.564  -29.884 1.00 91.02  ? 110 ILE A O   1 
ATOM 779  C CB  . ILE A 1 110 ? 17.591  -7.117  -28.391 1.00 85.63  ? 110 ILE A CB  1 
ATOM 780  C CG1 . ILE A 1 110 ? 16.406  -7.911  -27.836 1.00 86.99  ? 110 ILE A CG1 1 
ATOM 781  C CG2 . ILE A 1 110 ? 17.299  -5.627  -28.410 1.00 83.27  ? 110 ILE A CG2 1 
ATOM 782  C CD1 . ILE A 1 110 ? 15.586  -7.166  -26.810 1.00 88.24  ? 110 ILE A CD1 1 
ATOM 783  N N   . GLN A 1 111 ? 18.700  -6.185  -31.615 1.00 81.78  ? 111 GLN A N   1 
ATOM 784  C CA  . GLN A 1 111 ? 19.612  -5.280  -32.302 1.00 81.86  ? 111 GLN A CA  1 
ATOM 785  C C   . GLN A 1 111 ? 19.423  -3.828  -31.893 1.00 85.93  ? 111 GLN A C   1 
ATOM 786  O O   . GLN A 1 111 ? 20.408  -3.092  -31.768 1.00 88.30  ? 111 GLN A O   1 
ATOM 787  C CB  . GLN A 1 111 ? 19.431  -5.383  -33.819 1.00 85.97  ? 111 GLN A CB  1 
ATOM 788  C CG  . GLN A 1 111 ? 20.355  -6.364  -34.511 1.00 88.12  ? 111 GLN A CG  1 
ATOM 789  C CD  . GLN A 1 111 ? 19.914  -7.800  -34.343 1.00 92.31  ? 111 GLN A CD  1 
ATOM 790  O OE1 . GLN A 1 111 ? 20.394  -8.511  -33.460 1.00 92.77  ? 111 GLN A OE1 1 
ATOM 791  N NE2 . GLN A 1 111 ? 18.987  -8.233  -35.185 1.00 91.31  ? 111 GLN A NE2 1 
ATOM 792  N N   . VAL A 1 112 ? 18.179  -3.400  -31.679 1.00 85.66  ? 112 VAL A N   1 
ATOM 793  C CA  . VAL A 1 112 ? 17.856  -2.006  -31.421 1.00 85.60  ? 112 VAL A CA  1 
ATOM 794  C C   . VAL A 1 112 ? 17.187  -1.909  -30.059 1.00 83.88  ? 112 VAL A C   1 
ATOM 795  O O   . VAL A 1 112 ? 16.477  -2.818  -29.622 1.00 84.31  ? 112 VAL A O   1 
ATOM 796  C CB  . VAL A 1 112 ? 16.946  -1.414  -32.519 1.00 84.05  ? 112 VAL A CB  1 
ATOM 797  C CG1 . VAL A 1 112 ? 16.871  0.095   -32.400 1.00 82.23  ? 112 VAL A CG1 1 
ATOM 798  C CG2 . VAL A 1 112 ? 17.439  -1.823  -33.898 1.00 81.02  ? 112 VAL A CG2 1 
ATOM 799  N N   . LYS A 1 113 ? 17.419  -0.782  -29.386 1.00 82.46  ? 113 LYS A N   1 
ATOM 800  C CA  . LYS A 1 113 ? 16.889  -0.564  -28.046 1.00 83.65  ? 113 LYS A CA  1 
ATOM 801  C C   . LYS A 1 113 ? 15.369  -0.608  -27.985 1.00 84.79  ? 113 LYS A C   1 
ATOM 802  O O   . LYS A 1 113 ? 14.823  -0.991  -26.944 1.00 88.17  ? 113 LYS A O   1 
ATOM 803  C CB  . LYS A 1 113 ? 17.381  0.778   -27.499 1.00 84.29  ? 113 LYS A CB  1 
ATOM 804  C CG  . LYS A 1 113 ? 18.827  1.090   -27.834 1.00 85.77  ? 113 LYS A CG  1 
ATOM 805  C CD  . LYS A 1 113 ? 19.744  0.739   -26.675 1.00 87.29  ? 113 LYS A CD  1 
ATOM 806  C CE  . LYS A 1 113 ? 20.989  1.607   -26.675 1.00 86.45  ? 113 LYS A CE  1 
ATOM 807  N NZ  . LYS A 1 113 ? 20.651  3.056   -26.720 1.00 86.71  ? 113 LYS A NZ  1 
ATOM 808  N N   . ASN A 1 114 ? 14.673  -0.235  -29.055 1.00 74.96  ? 114 ASN A N   1 
ATOM 809  C CA  . ASN A 1 114 ? 13.217  -0.243  -29.059 1.00 74.01  ? 114 ASN A CA  1 
ATOM 810  C C   . ASN A 1 114 ? 12.630  -1.632  -29.258 1.00 74.33  ? 114 ASN A C   1 
ATOM 811  O O   . ASN A 1 114 ? 11.414  -1.799  -29.127 1.00 78.54  ? 114 ASN A O   1 
ATOM 812  C CB  . ASN A 1 114 ? 12.680  0.705   -30.137 1.00 75.02  ? 114 ASN A CB  1 
ATOM 813  C CG  . ASN A 1 114 ? 13.020  0.252   -31.542 1.00 76.22  ? 114 ASN A CG  1 
ATOM 814  O OD1 . ASN A 1 114 ? 13.815  -0.666  -31.739 1.00 82.25  ? 114 ASN A OD1 1 
ATOM 815  N ND2 . ASN A 1 114 ? 12.410  0.894   -32.528 1.00 75.38  ? 114 ASN A ND2 1 
ATOM 816  N N   . GLU A 1 115 ? 13.455  -2.626  -29.569 1.00 77.91  ? 115 GLU A N   1 
ATOM 817  C CA  . GLU A 1 115 ? 12.969  -3.988  -29.721 1.00 79.04  ? 115 GLU A CA  1 
ATOM 818  C C   . GLU A 1 115 ? 12.630  -4.567  -28.355 1.00 76.77  ? 115 GLU A C   1 
ATOM 819  O O   . GLU A 1 115 ? 13.455  -4.539  -27.436 1.00 80.19  ? 115 GLU A O   1 
ATOM 820  C CB  . GLU A 1 115 ? 14.012  -4.851  -30.428 1.00 79.55  ? 115 GLU A CB  1 
ATOM 821  C CG  . GLU A 1 115 ? 14.304  -4.411  -31.853 1.00 78.93  ? 115 GLU A CG  1 
ATOM 822  C CD  . GLU A 1 115 ? 15.238  -5.357  -32.578 1.00 88.02  ? 115 GLU A CD  1 
ATOM 823  O OE1 . GLU A 1 115 ? 15.755  -6.294  -31.935 1.00 88.45  ? 115 GLU A OE1 1 
ATOM 824  O OE2 . GLU A 1 115 ? 15.454  -5.165  -33.793 1.00 89.32  ? 115 GLU A OE2 1 
ATOM 825  N N   . ILE A 1 116 ? 11.415  -5.089  -28.221 1.00 66.82  ? 116 ILE A N   1 
ATOM 826  C CA  . ILE A 1 116 ? 10.924  -5.623  -26.960 1.00 71.48  ? 116 ILE A CA  1 
ATOM 827  C C   . ILE A 1 116 ? 10.598  -7.097  -27.147 1.00 69.38  ? 116 ILE A C   1 
ATOM 828  O O   . ILE A 1 116 ? 9.987   -7.499  -28.142 1.00 73.25  ? 116 ILE A O   1 
ATOM 829  C CB  . ILE A 1 116 ? 9.698   -4.838  -26.444 1.00 71.50  ? 116 ILE A CB  1 
ATOM 830  C CG1 . ILE A 1 116 ? 8.581   -4.825  -27.487 1.00 70.77  ? 116 ILE A CG1 1 
ATOM 831  C CG2 . ILE A 1 116 ? 10.090  -3.418  -26.108 1.00 70.08  ? 116 ILE A CG2 1 
ATOM 832  C CD1 . ILE A 1 116 ? 7.282   -4.250  -26.982 1.00 68.89  ? 116 ILE A CD1 1 
ATOM 833  N N   . LEU A 1 117 ? 11.024  -7.907  -26.184 1.00 73.89  ? 117 LEU A N   1 
ATOM 834  C CA  . LEU A 1 117 ? 10.912  -9.356  -26.273 1.00 77.20  ? 117 LEU A CA  1 
ATOM 835  C C   . LEU A 1 117 ? 9.787   -9.848  -25.374 1.00 74.27  ? 117 LEU A C   1 
ATOM 836  O O   . LEU A 1 117 ? 9.731   -9.501  -24.190 1.00 78.32  ? 117 LEU A O   1 
ATOM 837  C CB  . LEU A 1 117 ? 12.233  -10.028 -25.894 1.00 78.02  ? 117 LEU A CB  1 
ATOM 838  C CG  . LEU A 1 117 ? 12.262  -11.548 -26.034 1.00 79.19  ? 117 LEU A CG  1 
ATOM 839  C CD1 . LEU A 1 117 ? 11.997  -11.948 -27.472 1.00 76.31  ? 117 LEU A CD1 1 
ATOM 840  C CD2 . LEU A 1 117 ? 13.598  -12.097 -25.568 1.00 82.05  ? 117 LEU A CD2 1 
ATOM 841  N N   . THR A 1 118 ? 8.896   -10.651 -25.946 1.00 71.71  ? 118 THR A N   1 
ATOM 842  C CA  . THR A 1 118 ? 7.778   -11.220 -25.209 1.00 75.57  ? 118 THR A CA  1 
ATOM 843  C C   . THR A 1 118 ? 8.261   -12.323 -24.275 1.00 76.69  ? 118 THR A C   1 
ATOM 844  O O   . THR A 1 118 ? 9.234   -13.021 -24.567 1.00 83.98  ? 118 THR A O   1 
ATOM 845  C CB  . THR A 1 118 ? 6.739   -11.774 -26.187 1.00 76.46  ? 118 THR A CB  1 
ATOM 846  O OG1 . THR A 1 118 ? 6.375   -10.754 -27.124 1.00 80.49  ? 118 THR A OG1 1 
ATOM 847  C CG2 . THR A 1 118 ? 5.492   -12.245 -25.459 1.00 75.63  ? 118 THR A CG2 1 
ATOM 848  N N   . HIS A 1 119 ? 7.584   -12.466 -23.140 1.00 77.35  ? 119 HIS A N   1 
ATOM 849  C CA  . HIS A 1 119 ? 7.812   -13.568 -22.221 1.00 79.19  ? 119 HIS A CA  1 
ATOM 850  C C   . HIS A 1 119 ? 6.503   -14.312 -21.987 1.00 80.40  ? 119 HIS A C   1 
ATOM 851  O O   . HIS A 1 119 ? 5.417   -13.824 -22.310 1.00 82.03  ? 119 HIS A O   1 
ATOM 852  C CB  . HIS A 1 119 ? 8.408   -13.071 -20.897 1.00 81.70  ? 119 HIS A CB  1 
ATOM 853  C CG  . HIS A 1 119 ? 8.879   -14.172 -19.998 1.00 84.18  ? 119 HIS A CG  1 
ATOM 854  N ND1 . HIS A 1 119 ? 8.175   -14.574 -18.884 1.00 83.94  ? 119 HIS A ND1 1 
ATOM 855  C CD2 . HIS A 1 119 ? 9.964   -14.978 -20.069 1.00 85.90  ? 119 HIS A CD2 1 
ATOM 856  C CE1 . HIS A 1 119 ? 8.819   -15.566 -18.293 1.00 85.15  ? 119 HIS A CE1 1 
ATOM 857  N NE2 . HIS A 1 119 ? 9.908   -15.830 -18.993 1.00 87.38  ? 119 HIS A NE2 1 
ATOM 858  N N   . SER A 1 120 ? 6.618   -15.512 -21.419 1.00 82.30  ? 120 SER A N   1 
ATOM 859  C CA  . SER A 1 120 ? 5.474   -16.388 -21.206 1.00 84.26  ? 120 SER A CA  1 
ATOM 860  C C   . SER A 1 120 ? 4.444   -15.810 -20.245 1.00 83.70  ? 120 SER A C   1 
ATOM 861  O O   . SER A 1 120 ? 3.310   -16.299 -20.213 1.00 83.10  ? 120 SER A O   1 
ATOM 862  C CB  . SER A 1 120 ? 5.945   -17.750 -20.691 1.00 87.08  ? 120 SER A CB  1 
ATOM 863  O OG  . SER A 1 120 ? 7.081   -17.612 -19.857 1.00 89.86  ? 120 SER A OG  1 
ATOM 864  N N   . ASN A 1 121 ? 4.801   -14.787 -19.470 1.00 80.54  ? 121 ASN A N   1 
ATOM 865  C CA  . ASN A 1 121 ? 3.844   -14.140 -18.584 1.00 81.42  ? 121 ASN A CA  1 
ATOM 866  C C   . ASN A 1 121 ? 2.965   -13.129 -19.307 1.00 83.06  ? 121 ASN A C   1 
ATOM 867  O O   . ASN A 1 121 ? 2.093   -12.525 -18.672 1.00 80.35  ? 121 ASN A O   1 
ATOM 868  C CB  . ASN A 1 121 ? 4.574   -13.451 -17.428 1.00 81.77  ? 121 ASN A CB  1 
ATOM 869  C CG  . ASN A 1 121 ? 5.610   -12.453 -17.905 1.00 84.43  ? 121 ASN A CG  1 
ATOM 870  O OD1 . ASN A 1 121 ? 5.852   -12.315 -19.102 1.00 87.67  ? 121 ASN A OD1 1 
ATOM 871  N ND2 . ASN A 1 121 ? 6.228   -11.749 -16.965 1.00 83.31  ? 121 ASN A ND2 1 
ATOM 872  N N   . GLY A 1 122 ? 3.167   -12.936 -20.609 1.00 80.56  ? 122 GLY A N   1 
ATOM 873  C CA  . GLY A 1 122 ? 2.432   -11.953 -21.368 1.00 78.12  ? 122 GLY A CA  1 
ATOM 874  C C   . GLY A 1 122 ? 3.048   -10.573 -21.386 1.00 78.45  ? 122 GLY A C   1 
ATOM 875  O O   . GLY A 1 122 ? 2.468   -9.662  -21.990 1.00 82.77  ? 122 GLY A O   1 
ATOM 876  N N   . ALA A 1 123 ? 4.198   -10.388 -20.747 1.00 72.91  ? 123 ALA A N   1 
ATOM 877  C CA  . ALA A 1 123 ? 4.831   -9.080  -20.678 1.00 72.04  ? 123 ALA A CA  1 
ATOM 878  C C   . ALA A 1 123 ? 5.919   -8.951  -21.733 1.00 71.26  ? 123 ALA A C   1 
ATOM 879  O O   . ALA A 1 123 ? 6.539   -9.941  -22.133 1.00 76.49  ? 123 ALA A O   1 
ATOM 880  C CB  . ALA A 1 123 ? 5.423   -8.849  -19.289 1.00 70.12  ? 123 ALA A CB  1 
ATOM 881  N N   . GLN A 1 124 ? 6.146   -7.721  -22.184 1.00 68.44  ? 124 GLN A N   1 
ATOM 882  C CA  . GLN A 1 124 ? 7.205   -7.415  -23.134 1.00 66.40  ? 124 GLN A CA  1 
ATOM 883  C C   . GLN A 1 124 ? 8.299   -6.652  -22.401 1.00 70.84  ? 124 GLN A C   1 
ATOM 884  O O   . GLN A 1 124 ? 8.016   -5.675  -21.701 1.00 75.32  ? 124 GLN A O   1 
ATOM 885  C CB  . GLN A 1 124 ? 6.677   -6.593  -24.309 1.00 68.04  ? 124 GLN A CB  1 
ATOM 886  C CG  . GLN A 1 124 ? 5.911   -7.398  -25.337 1.00 69.52  ? 124 GLN A CG  1 
ATOM 887  C CD  . GLN A 1 124 ? 4.607   -7.925  -24.789 1.00 72.60  ? 124 GLN A CD  1 
ATOM 888  O OE1 . GLN A 1 124 ? 3.879   -7.207  -24.109 1.00 75.62  ? 124 GLN A OE1 1 
ATOM 889  N NE2 . GLN A 1 124 ? 4.311   -9.183  -25.070 1.00 76.15  ? 124 GLN A NE2 1 
ATOM 890  N N   . TYR A 1 125 ? 9.539   -7.100  -22.558 1.00 72.47  ? 125 TYR A N   1 
ATOM 891  C CA  . TYR A 1 125 ? 10.672  -6.512  -21.864 1.00 72.17  ? 125 TYR A CA  1 
ATOM 892  C C   . TYR A 1 125 ? 11.654  -5.926  -22.867 1.00 73.78  ? 125 TYR A C   1 
ATOM 893  O O   . TYR A 1 125 ? 12.036  -6.589  -23.837 1.00 83.14  ? 125 TYR A O   1 
ATOM 894  C CB  . TYR A 1 125 ? 11.372  -7.553  -20.990 1.00 72.63  ? 125 TYR A CB  1 
ATOM 895  C CG  . TYR A 1 125 ? 10.492  -8.123  -19.903 1.00 73.33  ? 125 TYR A CG  1 
ATOM 896  C CD1 . TYR A 1 125 ? 10.390  -7.501  -18.668 1.00 71.66  ? 125 TYR A CD1 1 
ATOM 897  C CD2 . TYR A 1 125 ? 9.754   -9.278  -20.117 1.00 75.83  ? 125 TYR A CD2 1 
ATOM 898  C CE1 . TYR A 1 125 ? 9.585   -8.017  -17.674 1.00 77.05  ? 125 TYR A CE1 1 
ATOM 899  C CE2 . TYR A 1 125 ? 8.945   -9.801  -19.130 1.00 75.79  ? 125 TYR A CE2 1 
ATOM 900  C CZ  . TYR A 1 125 ? 8.865   -9.167  -17.911 1.00 78.75  ? 125 TYR A CZ  1 
ATOM 901  O OH  . TYR A 1 125 ? 8.060   -9.684  -16.923 1.00 83.04  ? 125 TYR A OH  1 
ATOM 902  N N   . ARG A 1 126 ? 12.053  -4.682  -22.632 1.00 73.41  ? 126 ARG A N   1 
ATOM 903  C CA  . ARG A 1 126 ? 13.078  -4.022  -23.422 1.00 74.34  ? 126 ARG A CA  1 
ATOM 904  C C   . ARG A 1 126 ? 14.398  -4.039  -22.665 1.00 83.67  ? 126 ARG A C   1 
ATOM 905  O O   . ARG A 1 126 ? 14.435  -3.996  -21.432 1.00 88.17  ? 126 ARG A O   1 
ATOM 906  C CB  . ARG A 1 126 ? 12.678  -2.582  -23.759 1.00 76.82  ? 126 ARG A CB  1 
ATOM 907  C CG  . ARG A 1 126 ? 12.585  -1.658  -22.561 1.00 76.71  ? 126 ARG A CG  1 
ATOM 908  C CD  . ARG A 1 126 ? 12.823  -0.217  -22.965 1.00 77.81  ? 126 ARG A CD  1 
ATOM 909  N NE  . ARG A 1 126 ? 12.753  0.688   -21.825 1.00 78.50  ? 126 ARG A NE  1 
ATOM 910  C CZ  . ARG A 1 126 ? 13.758  1.443   -21.406 1.00 81.19  ? 126 ARG A CZ  1 
ATOM 911  N NH1 . ARG A 1 126 ? 14.936  1.418   -22.007 1.00 81.25  ? 126 ARG A NH1 1 
ATOM 912  N NH2 . ARG A 1 126 ? 13.579  2.241   -20.358 1.00 80.02  ? 126 ARG A NH2 1 
ATOM 913  N N   . TRP A 1 127 ? 15.488  -4.108  -23.419 1.00 92.16  ? 127 TRP A N   1 
ATOM 914  C CA  . TRP A 1 127 ? 16.826  -4.176  -22.854 1.00 91.79  ? 127 TRP A CA  1 
ATOM 915  C C   . TRP A 1 127 ? 17.421  -2.778  -22.785 1.00 92.02  ? 127 TRP A C   1 
ATOM 916  O O   . TRP A 1 127 ? 17.471  -2.062  -23.790 1.00 92.77  ? 127 TRP A O   1 
ATOM 917  C CB  . TRP A 1 127 ? 17.723  -5.098  -23.683 1.00 91.58  ? 127 TRP A CB  1 
ATOM 918  C CG  . TRP A 1 127 ? 19.116  -5.201  -23.162 1.00 91.51  ? 127 TRP A CG  1 
ATOM 919  C CD1 . TRP A 1 127 ? 20.239  -4.663  -23.712 1.00 91.23  ? 127 TRP A CD1 1 
ATOM 920  C CD2 . TRP A 1 127 ? 19.535  -5.882  -21.974 1.00 94.32  ? 127 TRP A CD2 1 
ATOM 921  N NE1 . TRP A 1 127 ? 21.335  -4.971  -22.947 1.00 93.60  ? 127 TRP A NE1 1 
ATOM 922  C CE2 . TRP A 1 127 ? 20.929  -5.716  -21.870 1.00 95.79  ? 127 TRP A CE2 1 
ATOM 923  C CE3 . TRP A 1 127 ? 18.868  -6.615  -20.990 1.00 91.77  ? 127 TRP A CE3 1 
ATOM 924  C CZ2 . TRP A 1 127 ? 21.669  -6.258  -20.823 1.00 94.33  ? 127 TRP A CZ2 1 
ATOM 925  C CZ3 . TRP A 1 127 ? 19.604  -7.152  -19.950 1.00 91.53  ? 127 TRP A CZ3 1 
ATOM 926  C CH2 . TRP A 1 127 ? 20.989  -6.970  -19.875 1.00 93.49  ? 127 TRP A CH2 1 
ATOM 927  N N   . ALA A 1 128 ? 17.869  -2.391  -21.592 1.00 94.03  ? 128 ALA A N   1 
ATOM 928  C CA  . ALA A 1 128 ? 18.389  -1.054  -21.349 1.00 97.59  ? 128 ALA A CA  1 
ATOM 929  C C   . ALA A 1 128 ? 19.909  -0.992  -21.337 1.00 99.57  ? 128 ALA A C   1 
ATOM 930  O O   . ALA A 1 128 ? 20.468  0.067   -21.034 1.00 99.38  ? 128 ALA A O   1 
ATOM 931  C CB  . ALA A 1 128 ? 17.842  -0.508  -20.027 1.00 95.31  ? 128 ALA A CB  1 
ATOM 932  N N   . GLY A 1 129 ? 20.558  -2.110  -21.657 1.00 97.47  ? 129 GLY A N   1 
ATOM 933  C CA  . GLY A 1 129 ? 22.026  -2.144  -21.612 1.00 95.86  ? 129 GLY A CA  1 
ATOM 934  C C   . GLY A 1 129 ? 22.636  -1.791  -22.949 1.00 94.69  ? 129 GLY A C   1 
ATOM 935  O O   . GLY A 1 129 ? 23.068  -0.637  -23.124 1.00 96.12  ? 129 GLY A O   1 
ATOM 936  N N   . ALA A 1 130 ? 22.640  -2.753  -23.866 1.00 30.00  ? 130 ALA A N   1 
ATOM 937  C CA  . ALA A 1 130 ? 23.782  -3.092  -24.738 1.00 30.00  ? 130 ALA A CA  1 
ATOM 938  C C   . ALA A 1 130 ? 23.273  -3.313  -26.157 1.00 30.00  ? 130 ALA A C   1 
ATOM 939  O O   . ALA A 1 130 ? 22.411  -4.192  -26.349 1.00 30.00  ? 130 ALA A O   1 
ATOM 940  C CB  . ALA A 1 130 ? 24.466  -4.327  -24.216 1.00 30.00  ? 130 ALA A CB  1 
ATOM 941  N N   . VAL A 1 131 ? 23.807  -2.559  -27.112 1.00 30.00  ? 131 VAL A N   1 
ATOM 942  C CA  . VAL A 1 131 ? 23.340  -2.641  -28.515 1.00 30.00  ? 131 VAL A CA  1 
ATOM 943  C C   . VAL A 1 131 ? 22.861  -4.045  -28.888 1.00 30.00  ? 131 VAL A C   1 
ATOM 944  O O   . VAL A 1 131 ? 21.644  -4.171  -29.131 1.00 30.00  ? 131 VAL A O   1 
ATOM 945  C CB  . VAL A 1 131 ? 24.419  -2.134  -29.455 1.00 30.00  ? 131 VAL A CB  1 
ATOM 946  N N   . PRO A 1 132 ? 23.704  -5.102  -28.957 1.00 97.45  ? 132 PRO A N   1 
ATOM 947  C CA  . PRO A 1 132 ? 23.253  -6.395  -29.442 1.00 94.96  ? 132 PRO A CA  1 
ATOM 948  C C   . PRO A 1 132 ? 22.985  -7.420  -28.360 1.00 96.40  ? 132 PRO A C   1 
ATOM 949  O O   . PRO A 1 132 ? 23.598  -8.499  -28.375 1.00 99.36  ? 132 PRO A O   1 
ATOM 950  C CB  . PRO A 1 132 ? 24.458  -6.757  -30.309 1.00 92.39  ? 132 PRO A CB  1 
ATOM 951  C CG  . PRO A 1 132 ? 25.642  -6.179  -29.558 1.00 94.34  ? 132 PRO A CG  1 
ATOM 952  C CD  . PRO A 1 132 ? 25.099  -5.163  -28.565 1.00 97.37  ? 132 PRO A CD  1 
ATOM 953  N N   . LYS A 1 133 ? 22.067  -7.108  -27.450 1.00 94.37  ? 133 LYS A N   1 
ATOM 954  C CA  . LYS A 1 133 ? 21.698  -8.092  -26.404 1.00 95.38  ? 133 LYS A CA  1 
ATOM 955  C C   . LYS A 1 133 ? 21.296  -9.405  -27.083 1.00 96.07  ? 133 LYS A C   1 
ATOM 956  O O   . LYS A 1 133 ? 20.382  -9.380  -27.922 1.00 99.31  ? 133 LYS A O   1 
ATOM 957  C CB  . LYS A 1 133 ? 20.552  -7.575  -25.531 1.00 92.50  ? 133 LYS A CB  1 
ATOM 958  C CG  . LYS A 1 133 ? 20.011  -8.575  -24.526 1.00 92.66  ? 133 LYS A CG  1 
ATOM 959  C CD  . LYS A 1 133 ? 21.076  -8.999  -23.527 1.00 93.03  ? 133 LYS A CD  1 
ATOM 960  C CE  . LYS A 1 133 ? 20.500  -9.772  -22.392 1.00 93.83  ? 133 LYS A CE  1 
ATOM 961  N NZ  . LYS A 1 133 ? 20.174  -11.146 -22.777 1.00 94.30  ? 133 LYS A NZ  1 
ATOM 962  N N   . VAL A 1 134 ? 21.973  -10.500 -26.742 1.00 92.04  ? 134 VAL A N   1 
ATOM 963  C CA  . VAL A 1 134 ? 21.592  -11.828 -27.303 1.00 93.19  ? 134 VAL A CA  1 
ATOM 964  C C   . VAL A 1 134 ? 20.936  -12.639 -26.182 1.00 94.22  ? 134 VAL A C   1 
ATOM 965  O O   . VAL A 1 134 ? 21.466  -12.632 -25.056 1.00 95.01  ? 134 VAL A O   1 
ATOM 966  C CB  . VAL A 1 134 ? 22.759  -12.604 -27.937 1.00 94.08  ? 134 VAL A CB  1 
ATOM 967  C CG1 . VAL A 1 134 ? 22.283  -13.856 -28.662 1.00 91.87  ? 134 VAL A CG1 1 
ATOM 968  C CG2 . VAL A 1 134 ? 23.587  -11.730 -28.867 1.00 92.44  ? 134 VAL A CG2 1 
ATOM 969  N N   . VAL A 1 135 ? 19.830  -13.299 -26.488 1.00 93.72  ? 135 VAL A N   1 
ATOM 970  C CA  . VAL A 1 135 ? 19.080  -14.078 -25.507 1.00 94.85  ? 135 VAL A CA  1 
ATOM 971  C C   . VAL A 1 135 ? 19.077  -15.532 -25.963 1.00 94.70  ? 135 VAL A C   1 
ATOM 972  O O   . VAL A 1 135 ? 18.548  -15.835 -27.041 1.00 93.80  ? 135 VAL A O   1 
ATOM 973  C CB  . VAL A 1 135 ? 17.646  -13.553 -25.341 1.00 94.49  ? 135 VAL A CB  1 
ATOM 974  C CG1 . VAL A 1 135 ? 16.935  -14.296 -24.222 1.00 91.81  ? 135 VAL A CG1 1 
ATOM 975  C CG2 . VAL A 1 135 ? 17.662  -12.062 -25.077 1.00 92.60  ? 135 VAL A CG2 1 
ATOM 976  N N   . PRO A 1 136 ? 19.651  -16.455 -25.195 1.00 101.17 ? 136 PRO A N   1 
ATOM 977  C CA  . PRO A 1 136 ? 19.607  -17.871 -25.588 1.00 100.29 ? 136 PRO A CA  1 
ATOM 978  C C   . PRO A 1 136 ? 18.213  -18.459 -25.444 1.00 97.94  ? 136 PRO A C   1 
ATOM 979  O O   . PRO A 1 136 ? 17.365  -17.897 -24.744 1.00 99.07  ? 136 PRO A O   1 
ATOM 980  C CB  . PRO A 1 136 ? 20.601  -18.549 -24.635 1.00 100.53 ? 136 PRO A CB  1 
ATOM 981  C CG  . PRO A 1 136 ? 20.931  -17.558 -23.582 1.00 101.14 ? 136 PRO A CG  1 
ATOM 982  C CD  . PRO A 1 136 ? 20.380  -16.220 -23.938 1.00 100.31 ? 136 PRO A CD  1 
ATOM 983  N N   . ALA A 1 137 ? 17.967  -19.585 -26.107 1.00 97.81  ? 137 ALA A N   1 
ATOM 984  C CA  . ALA A 1 137 ? 16.677  -20.260 -26.050 1.00 99.37  ? 137 ALA A CA  1 
ATOM 985  C C   . ALA A 1 137 ? 16.432  -20.763 -24.633 1.00 100.02 ? 137 ALA A C   1 
ATOM 986  O O   . ALA A 1 137 ? 17.367  -21.195 -23.950 1.00 98.10  ? 137 ALA A O   1 
ATOM 987  C CB  . ALA A 1 137 ? 16.629  -21.417 -27.047 1.00 98.53  ? 137 ALA A CB  1 
ATOM 988  N N   . GLY A 1 138 ? 15.180  -20.701 -24.191 1.00 101.37 ? 138 GLY A N   1 
ATOM 989  C CA  . GLY A 1 138 ? 14.812  -21.144 -22.865 1.00 99.02  ? 138 GLY A CA  1 
ATOM 990  C C   . GLY A 1 138 ? 15.127  -20.176 -21.748 1.00 98.21  ? 138 GLY A C   1 
ATOM 991  O O   . GLY A 1 138 ? 15.042  -20.563 -20.578 1.00 98.31  ? 138 GLY A O   1 
ATOM 992  N N   . SER A 1 139 ? 15.487  -18.937 -22.067 1.00 95.19  ? 139 SER A N   1 
ATOM 993  C CA  . SER A 1 139 ? 15.868  -17.972 -21.049 1.00 95.99  ? 139 SER A CA  1 
ATOM 994  C C   . SER A 1 139 ? 14.644  -17.277 -20.468 1.00 96.69  ? 139 SER A C   1 
ATOM 995  O O   . SER A 1 139 ? 13.518  -17.435 -20.949 1.00 97.78  ? 139 SER A O   1 
ATOM 996  C CB  . SER A 1 139 ? 16.824  -16.931 -21.630 1.00 93.89  ? 139 SER A CB  1 
ATOM 997  O OG  . SER A 1 139 ? 18.087  -17.502 -21.917 1.00 97.43  ? 139 SER A OG  1 
ATOM 998  N N   . THR A 1 140 ? 14.878  -16.516 -19.409 1.00 95.21  ? 140 THR A N   1 
ATOM 999  C CA  . THR A 1 140 ? 13.907  -15.650 -18.764 1.00 94.11  ? 140 THR A CA  1 
ATOM 1000 C C   . THR A 1 140 ? 14.535  -14.285 -18.514 1.00 94.25  ? 140 THR A C   1 
ATOM 1001 O O   . THR A 1 140 ? 15.764  -14.155 -18.501 1.00 97.54  ? 140 THR A O   1 
ATOM 1002 C CB  . THR A 1 140 ? 13.426  -16.248 -17.433 1.00 95.88  ? 140 THR A CB  1 
ATOM 1003 O OG1 . THR A 1 140 ? 14.530  -16.360 -16.527 1.00 98.90  ? 140 THR A OG1 1 
ATOM 1004 C CG2 . THR A 1 140 ? 12.802  -17.618 -17.647 1.00 93.84  ? 140 THR A CG2 1 
ATOM 1005 N N   . PRO A 1 141 ? 13.728  -13.235 -18.337 1.00 91.69  ? 141 PRO A N   1 
ATOM 1006 C CA  . PRO A 1 141 ? 14.312  -11.916 -18.041 1.00 92.19  ? 141 PRO A CA  1 
ATOM 1007 C C   . PRO A 1 141 ? 15.208  -11.917 -16.819 1.00 94.94  ? 141 PRO A C   1 
ATOM 1008 O O   . PRO A 1 141 ? 16.228  -11.220 -16.819 1.00 95.73  ? 141 PRO A O   1 
ATOM 1009 C CB  . PRO A 1 141 ? 13.083  -11.020 -17.835 1.00 92.26  ? 141 PRO A CB  1 
ATOM 1010 C CG  . PRO A 1 141 ? 11.983  -11.701 -18.555 1.00 89.75  ? 141 PRO A CG  1 
ATOM 1011 C CD  . PRO A 1 141 ? 12.267  -13.169 -18.511 1.00 90.66  ? 141 PRO A CD  1 
ATOM 1012 N N   . ALA A 1 142 ? 14.863  -12.679 -15.778 1.00 95.38  ? 142 ALA A N   1 
ATOM 1013 C CA  . ALA A 1 142 ? 15.751  -12.804 -14.628 1.00 96.13  ? 142 ALA A CA  1 
ATOM 1014 C C   . ALA A 1 142 ? 17.038  -13.528 -14.997 1.00 96.41  ? 142 ALA A C   1 
ATOM 1015 O O   . ALA A 1 142 ? 18.126  -13.139 -14.556 1.00 93.48  ? 142 ALA A O   1 
ATOM 1016 C CB  . ALA A 1 142 ? 15.034  -13.527 -13.489 1.00 92.29  ? 142 ALA A CB  1 
ATOM 1017 N N   . SER A 1 143 ? 16.937  -14.584 -15.807 1.00 97.35  ? 143 SER A N   1 
ATOM 1018 C CA  . SER A 1 143 ? 18.122  -15.352 -16.175 1.00 96.17  ? 143 SER A CA  1 
ATOM 1019 C C   . SER A 1 143 ? 18.977  -14.611 -17.194 1.00 96.99  ? 143 SER A C   1 
ATOM 1020 O O   . SER A 1 143 ? 20.194  -14.818 -17.260 1.00 99.02  ? 143 SER A O   1 
ATOM 1021 C CB  . SER A 1 143 ? 17.711  -16.720 -16.717 1.00 95.48  ? 143 SER A CB  1 
ATOM 1022 O OG  . SER A 1 143 ? 18.133  -16.881 -18.060 1.00 92.38  ? 143 SER A OG  1 
ATOM 1023 N N   . SER A 1 144 ? 18.363  -13.745 -17.996 1.00 95.13  ? 144 SER A N   1 
ATOM 1024 C CA  . SER A 1 144 ? 19.065  -13.053 -19.069 1.00 93.63  ? 144 SER A CA  1 
ATOM 1025 C C   . SER A 1 144 ? 19.685  -11.735 -18.625 1.00 94.41  ? 144 SER A C   1 
ATOM 1026 O O   . SER A 1 144 ? 20.218  -11.007 -19.469 1.00 97.07  ? 144 SER A O   1 
ATOM 1027 C CB  . SER A 1 144 ? 18.113  -12.805 -20.243 1.00 96.36  ? 144 SER A CB  1 
ATOM 1028 O OG  . SER A 1 144 ? 17.156  -13.844 -20.346 1.00 99.74  ? 144 SER A OG  1 
ATOM 1029 N N   . GLY A 1 145 ? 19.635  -11.409 -17.337 1.00 89.74  ? 145 GLY A N   1 
ATOM 1030 C CA  . GLY A 1 145 ? 20.198  -10.161 -16.865 1.00 93.07  ? 145 GLY A CA  1 
ATOM 1031 C C   . GLY A 1 145 ? 19.396  -9.523  -15.751 1.00 94.49  ? 145 GLY A C   1 
ATOM 1032 O O   . GLY A 1 145 ? 19.821  -8.522  -15.167 1.00 93.43  ? 145 GLY A O   1 
ATOM 1033 N N   . GLY A 1 146 ? 18.233  -10.091 -15.449 1.00 91.99  ? 146 GLY A N   1 
ATOM 1034 C CA  . GLY A 1 146 ? 17.396  -9.564  -14.390 1.00 90.02  ? 146 GLY A CA  1 
ATOM 1035 C C   . GLY A 1 146 ? 16.409  -8.528  -14.882 1.00 91.08  ? 146 GLY A C   1 
ATOM 1036 O O   . GLY A 1 146 ? 16.427  -8.151  -16.056 1.00 95.25  ? 146 GLY A O   1 
ATOM 1037 N N   . ILE A 1 147 ? 15.531  -8.071  -13.992 1.00 87.40  ? 147 ILE A N   1 
ATOM 1038 C CA  . ILE A 1 147 ? 14.573  -7.024  -14.325 1.00 88.39  ? 147 ILE A CA  1 
ATOM 1039 C C   . ILE A 1 147 ? 14.887  -5.790  -13.491 1.00 88.98  ? 147 ILE A C   1 
ATOM 1040 O O   . ILE A 1 147 ? 14.442  -5.674  -12.343 1.00 92.97  ? 147 ILE A O   1 
ATOM 1041 C CB  . ILE A 1 147 ? 13.126  -7.499  -14.101 1.00 86.88  ? 147 ILE A CB  1 
ATOM 1042 C CG1 . ILE A 1 147 ? 12.869  -8.797  -14.865 1.00 83.30  ? 147 ILE A CG1 1 
ATOM 1043 C CG2 . ILE A 1 147 ? 12.139  -6.428  -14.534 1.00 87.38  ? 147 ILE A CG2 1 
ATOM 1044 C CD1 . ILE A 1 147 ? 11.517  -9.411  -14.590 1.00 82.76  ? 147 ILE A CD1 1 
ATOM 1045 N N   . SER A 1 148 ? 15.658  -4.866  -14.056 1.00 89.26  ? 148 SER A N   1 
ATOM 1046 C CA  . SER A 1 148 ? 16.073  -3.657  -13.362 1.00 94.25  ? 148 SER A CA  1 
ATOM 1047 C C   . SER A 1 148 ? 16.200  -2.514  -14.359 1.00 92.42  ? 148 SER A C   1 
ATOM 1048 O O   . SER A 1 148 ? 15.949  -2.673  -15.556 1.00 94.01  ? 148 SER A O   1 
ATOM 1049 C CB  . SER A 1 148 ? 17.399  -3.866  -12.618 1.00 96.18  ? 148 SER A CB  1 
ATOM 1050 O OG  . SER A 1 148 ? 18.502  -3.769  -13.502 1.00 96.95  ? 148 SER A OG  1 
ATOM 1051 N N   . ALA A 1 149 ? 16.597  -1.347  -13.846 1.00 94.87  ? 149 ALA A N   1 
ATOM 1052 C CA  . ALA A 1 149 ? 16.745  -0.166  -14.688 1.00 95.28  ? 149 ALA A CA  1 
ATOM 1053 C C   . ALA A 1 149 ? 17.833  -0.333  -15.741 1.00 97.43  ? 149 ALA A C   1 
ATOM 1054 O O   . ALA A 1 149 ? 17.657  0.130   -16.873 1.00 99.22  ? 149 ALA A O   1 
ATOM 1055 C CB  . ALA A 1 149 ? 17.039  1.062   -13.826 1.00 95.36  ? 149 ALA A CB  1 
ATOM 1056 N N   . SER A 1 150 ? 18.950  -0.971  -15.396 1.00 98.74  ? 150 SER A N   1 
ATOM 1057 C CA  . SER A 1 150 ? 19.999  -1.280  -16.357 1.00 101.12 ? 150 SER A CA  1 
ATOM 1058 C C   . SER A 1 150 ? 19.790  -2.624  -17.040 1.00 101.16 ? 150 SER A C   1 
ATOM 1059 O O   . SER A 1 150 ? 20.641  -3.042  -17.831 1.00 100.95 ? 150 SER A O   1 
ATOM 1060 C CB  . SER A 1 150 ? 21.370  -1.266  -15.669 1.00 102.17 ? 150 SER A CB  1 
ATOM 1061 O OG  . SER A 1 150 ? 21.440  -2.253  -14.654 1.00 101.68 ? 150 SER A OG  1 
ATOM 1062 N N   . ALA A 1 151 ? 18.679  -3.299  -16.752 1.00 95.07  ? 151 ALA A N   1 
ATOM 1063 C CA  . ALA A 1 151 ? 18.377  -4.617  -17.289 1.00 90.86  ? 151 ALA A CA  1 
ATOM 1064 C C   . ALA A 1 151 ? 17.009  -4.591  -17.957 1.00 92.65  ? 151 ALA A C   1 
ATOM 1065 O O   . ALA A 1 151 ? 16.483  -3.512  -18.245 1.00 96.72  ? 151 ALA A O   1 
ATOM 1066 C CB  . ALA A 1 151 ? 18.426  -5.676  -16.187 1.00 91.57  ? 151 ALA A CB  1 
ATOM 1067 N N   . TRP A 1 152 ? 16.453  -5.765  -18.245 1.00 87.19  ? 152 TRP A N   1 
ATOM 1068 C CA  . TRP A 1 152 ? 15.141  -5.879  -18.866 1.00 86.98  ? 152 TRP A CA  1 
ATOM 1069 C C   . TRP A 1 152 ? 14.103  -5.053  -18.119 1.00 86.29  ? 152 TRP A C   1 
ATOM 1070 O O   . TRP A 1 152 ? 14.003  -5.118  -16.891 1.00 88.20  ? 152 TRP A O   1 
ATOM 1071 C CB  . TRP A 1 152 ? 14.695  -7.340  -18.906 1.00 83.83  ? 152 TRP A CB  1 
ATOM 1072 C CG  . TRP A 1 152 ? 15.582  -8.195  -19.730 1.00 86.89  ? 152 TRP A CG  1 
ATOM 1073 C CD1 . TRP A 1 152 ? 16.602  -8.982  -19.290 1.00 87.35  ? 152 TRP A CD1 1 
ATOM 1074 C CD2 . TRP A 1 152 ? 15.546  -8.341  -21.151 1.00 89.00  ? 152 TRP A CD2 1 
ATOM 1075 N NE1 . TRP A 1 152 ? 17.200  -9.617  -20.349 1.00 90.44  ? 152 TRP A NE1 1 
ATOM 1076 C CE2 . TRP A 1 152 ? 16.567  -9.239  -21.504 1.00 89.39  ? 152 TRP A CE2 1 
ATOM 1077 C CE3 . TRP A 1 152 ? 14.743  -7.801  -22.160 1.00 86.56  ? 152 TRP A CE3 1 
ATOM 1078 C CZ2 . TRP A 1 152 ? 16.810  -9.610  -22.821 1.00 89.64  ? 152 TRP A CZ2 1 
ATOM 1079 C CZ3 . TRP A 1 152 ? 14.984  -8.172  -23.466 1.00 87.14  ? 152 TRP A CZ3 1 
ATOM 1080 C CH2 . TRP A 1 152 ? 16.008  -9.067  -23.786 1.00 89.13  ? 152 TRP A CH2 1 
ATOM 1081 N N   . ILE A 1 153 ? 13.336  -4.268  -18.871 1.00 78.40  ? 153 ILE A N   1 
ATOM 1082 C CA  . ILE A 1 153 ? 12.294  -3.413  -18.321 1.00 77.37  ? 153 ILE A CA  1 
ATOM 1083 C C   . ILE A 1 153 ? 10.978  -3.744  -19.006 1.00 81.17  ? 153 ILE A C   1 
ATOM 1084 O O   . ILE A 1 153 ? 10.891  -3.732  -20.238 1.00 88.81  ? 153 ILE A O   1 
ATOM 1085 C CB  . ILE A 1 153 ? 12.627  -1.917  -18.500 1.00 77.55  ? 153 ILE A CB  1 
ATOM 1086 C CG1 . ILE A 1 153 ? 13.977  -1.586  -17.866 1.00 80.11  ? 153 ILE A CG1 1 
ATOM 1087 C CG2 . ILE A 1 153 ? 11.535  -1.058  -17.894 1.00 80.40  ? 153 ILE A CG2 1 
ATOM 1088 C CD1 . ILE A 1 153 ? 14.453  -0.182  -18.150 1.00 77.43  ? 153 ILE A CD1 1 
ATOM 1089 N N   . GLU A 1 154 ? 9.957   -4.037  -18.207 1.00 79.62  ? 154 GLU A N   1 
ATOM 1090 C CA  . GLU A 1 154 ? 8.616   -4.203  -18.748 1.00 79.95  ? 154 GLU A CA  1 
ATOM 1091 C C   . GLU A 1 154 ? 8.117   -2.871  -19.294 1.00 80.01  ? 154 GLU A C   1 
ATOM 1092 O O   . GLU A 1 154 ? 8.281   -1.824  -18.664 1.00 84.10  ? 154 GLU A O   1 
ATOM 1093 C CB  . GLU A 1 154 ? 7.671   -4.729  -17.671 1.00 77.67  ? 154 GLU A CB  1 
ATOM 1094 C CG  . GLU A 1 154 ? 6.557   -5.604  -18.202 1.00 78.76  ? 154 GLU A CG  1 
ATOM 1095 C CD  . GLU A 1 154 ? 5.421   -4.797  -18.790 1.00 83.91  ? 154 GLU A CD  1 
ATOM 1096 O OE1 . GLU A 1 154 ? 5.029   -5.071  -19.944 1.00 86.03  ? 154 GLU A OE1 1 
ATOM 1097 O OE2 . GLU A 1 154 ? 4.917   -3.886  -18.102 1.00 83.56  ? 154 GLU A OE2 1 
ATOM 1098 N N   . VAL A 1 155 ? 7.500   -2.913  -20.476 1.00 75.86  ? 155 VAL A N   1 
ATOM 1099 C CA  . VAL A 1 155 ? 7.237   -1.670  -21.195 1.00 75.76  ? 155 VAL A CA  1 
ATOM 1100 C C   . VAL A 1 155 ? 5.835   -1.133  -20.929 1.00 79.84  ? 155 VAL A C   1 
ATOM 1101 O O   . VAL A 1 155 ? 5.651   0.083   -20.808 1.00 83.13  ? 155 VAL A O   1 
ATOM 1102 C CB  . VAL A 1 155 ? 7.483   -1.868  -22.700 1.00 74.49  ? 155 VAL A CB  1 
ATOM 1103 C CG1 . VAL A 1 155 ? 8.965   -2.015  -22.969 1.00 76.79  ? 155 VAL A CG1 1 
ATOM 1104 C CG2 . VAL A 1 155 ? 6.725   -3.080  -23.213 1.00 77.27  ? 155 VAL A CG2 1 
ATOM 1105 N N   . THR A 1 156 ? 4.826   -2.005  -20.842 1.00 84.13  ? 156 THR A N   1 
ATOM 1106 C CA  . THR A 1 156 ? 3.451   -1.529  -20.730 1.00 84.93  ? 156 THR A CA  1 
ATOM 1107 C C   . THR A 1 156 ? 3.193   -0.803  -19.417 1.00 87.93  ? 156 THR A C   1 
ATOM 1108 O O   . THR A 1 156 ? 2.310   0.057   -19.354 1.00 89.79  ? 156 THR A O   1 
ATOM 1109 C CB  . THR A 1 156 ? 2.470   -2.693  -20.880 1.00 83.35  ? 156 THR A CB  1 
ATOM 1110 O OG1 . THR A 1 156 ? 2.976   -3.840  -20.188 1.00 88.42  ? 156 THR A OG1 1 
ATOM 1111 C CG2 . THR A 1 156 ? 2.277   -3.038  -22.346 1.00 84.22  ? 156 THR A CG2 1 
ATOM 1112 N N   . GLY A 1 157 ? 3.943   -1.128  -18.368 1.00 81.46  ? 157 GLY A N   1 
ATOM 1113 C CA  . GLY A 1 157 ? 3.762   -0.468  -17.092 1.00 80.07  ? 157 GLY A CA  1 
ATOM 1114 C C   . GLY A 1 157 ? 5.017   0.212   -16.589 1.00 82.90  ? 157 GLY A C   1 
ATOM 1115 O O   . GLY A 1 157 ? 5.154   0.448   -15.387 1.00 89.55  ? 157 GLY A O   1 
ATOM 1116 N N   . GLU A 1 158 ? 5.938   0.534   -17.501 1.00 81.66  ? 158 GLU A N   1 
ATOM 1117 C CA  . GLU A 1 158 ? 7.224   1.096   -17.101 1.00 79.51  ? 158 GLU A CA  1 
ATOM 1118 C C   . GLU A 1 158 ? 7.054   2.418   -16.364 1.00 81.08  ? 158 GLU A C   1 
ATOM 1119 O O   . GLU A 1 158 ? 7.584   2.599   -15.261 1.00 88.18  ? 158 GLU A O   1 
ATOM 1120 C CB  . GLU A 1 158 ? 8.115   1.289   -18.328 1.00 81.59  ? 158 GLU A CB  1 
ATOM 1121 C CG  . GLU A 1 158 ? 9.236   2.292   -18.121 1.00 82.39  ? 158 GLU A CG  1 
ATOM 1122 C CD  . GLU A 1 158 ? 10.358  2.130   -19.124 1.00 88.20  ? 158 GLU A CD  1 
ATOM 1123 O OE1 . GLU A 1 158 ? 11.263  2.988   -19.148 1.00 88.67  ? 158 GLU A OE1 1 
ATOM 1124 O OE2 . GLU A 1 158 ? 10.330  1.149   -19.895 1.00 92.15  ? 158 GLU A OE2 1 
ATOM 1125 N N   . GLU A 1 159 ? 6.316   3.356   -16.959 1.00 78.28  ? 159 GLU A N   1 
ATOM 1126 C CA  . GLU A 1 159 ? 6.229   4.691   -16.381 1.00 80.56  ? 159 GLU A CA  1 
ATOM 1127 C C   . GLU A 1 159 ? 5.446   4.694   -15.077 1.00 81.84  ? 159 GLU A C   1 
ATOM 1128 O O   . GLU A 1 159 ? 5.846   5.369   -14.123 1.00 83.07  ? 159 GLU A O   1 
ATOM 1129 C CB  . GLU A 1 159 ? 5.604   5.657   -17.383 1.00 78.92  ? 159 GLU A CB  1 
ATOM 1130 C CG  . GLU A 1 159 ? 6.365   5.722   -18.688 1.00 81.03  ? 159 GLU A CG  1 
ATOM 1131 C CD  . GLU A 1 159 ? 7.748   6.315   -18.522 1.00 85.43  ? 159 GLU A CD  1 
ATOM 1132 O OE1 . GLU A 1 159 ? 7.915   7.214   -17.672 1.00 87.52  ? 159 GLU A OE1 1 
ATOM 1133 O OE2 . GLU A 1 159 ? 8.673   5.873   -19.236 1.00 87.87  ? 159 GLU A OE2 1 
ATOM 1134 N N   . LEU A 1 160 ? 4.342   3.950   -15.009 1.00 77.81  ? 160 LEU A N   1 
ATOM 1135 C CA  . LEU A 1 160 ? 3.596   3.881   -13.760 1.00 72.68  ? 160 LEU A CA  1 
ATOM 1136 C C   . LEU A 1 160 ? 4.378   3.142   -12.682 1.00 71.69  ? 160 LEU A C   1 
ATOM 1137 O O   . LEU A 1 160 ? 4.280   3.493   -11.504 1.00 77.63  ? 160 LEU A O   1 
ATOM 1138 C CB  . LEU A 1 160 ? 2.239   3.221   -13.985 1.00 73.37  ? 160 LEU A CB  1 
ATOM 1139 C CG  . LEU A 1 160 ? 1.298   3.266   -12.782 1.00 70.03  ? 160 LEU A CG  1 
ATOM 1140 C CD1 . LEU A 1 160 ? 1.063   4.697   -12.339 1.00 73.44  ? 160 LEU A CD1 1 
ATOM 1141 C CD2 . LEU A 1 160 ? -0.016  2.590   -13.108 1.00 72.81  ? 160 LEU A CD2 1 
ATOM 1142 N N   . ARG A 1 161 ? 5.152   2.122   -13.059 1.00 76.42  ? 161 ARG A N   1 
ATOM 1143 C CA  . ARG A 1 161 ? 5.999   1.443   -12.084 1.00 75.02  ? 161 ARG A CA  1 
ATOM 1144 C C   . ARG A 1 161 ? 7.065   2.381   -11.532 1.00 77.59  ? 161 ARG A C   1 
ATOM 1145 O O   . ARG A 1 161 ? 7.324   2.394   -10.323 1.00 80.97  ? 161 ARG A O   1 
ATOM 1146 C CB  . ARG A 1 161 ? 6.642   0.210   -12.713 1.00 72.79  ? 161 ARG A CB  1 
ATOM 1147 C CG  . ARG A 1 161 ? 7.735   -0.431  -11.878 1.00 77.31  ? 161 ARG A CG  1 
ATOM 1148 C CD  . ARG A 1 161 ? 8.289   -1.675  -12.552 1.00 77.39  ? 161 ARG A CD  1 
ATOM 1149 N NE  . ARG A 1 161 ? 7.258   -2.407  -13.278 1.00 78.91  ? 161 ARG A NE  1 
ATOM 1150 C CZ  . ARG A 1 161 ? 7.197   -2.511  -14.599 1.00 79.40  ? 161 ARG A CZ  1 
ATOM 1151 N NH1 . ARG A 1 161 ? 8.101   -1.943  -15.379 1.00 77.78  ? 161 ARG A NH1 1 
ATOM 1152 N NH2 . ARG A 1 161 ? 6.200   -3.198  -15.149 1.00 77.40  ? 161 ARG A NH2 1 
ATOM 1153 N N   . ASP A 1 162 ? 7.698   3.170   -12.403 1.00 78.90  ? 162 ASP A N   1 
ATOM 1154 C CA  . ASP A 1 162 ? 8.689   4.132   -11.937 1.00 77.61  ? 162 ASP A CA  1 
ATOM 1155 C C   . ASP A 1 162 ? 8.060   5.215   -11.071 1.00 81.80  ? 162 ASP A C   1 
ATOM 1156 O O   . ASP A 1 162 ? 8.648   5.621   -10.063 1.00 84.77  ? 162 ASP A O   1 
ATOM 1157 C CB  . ASP A 1 162 ? 9.415   4.760   -13.125 1.00 80.40  ? 162 ASP A CB  1 
ATOM 1158 C CG  . ASP A 1 162 ? 10.142  3.735   -13.970 1.00 87.19  ? 162 ASP A CG  1 
ATOM 1159 O OD1 . ASP A 1 162 ? 10.724  4.120   -15.006 1.00 90.67  ? 162 ASP A OD1 1 
ATOM 1160 O OD2 . ASP A 1 162 ? 10.131  2.542   -13.599 1.00 84.23  ? 162 ASP A OD2 1 
ATOM 1161 N N   . GLU A 1 163 ? 6.876   5.696   -11.449 1.00 78.55  ? 163 GLU A N   1 
ATOM 1162 C CA  . GLU A 1 163 ? 6.187   6.721   -10.678 1.00 79.13  ? 163 GLU A CA  1 
ATOM 1163 C C   . GLU A 1 163 ? 5.731   6.205   -9.317  1.00 78.29  ? 163 GLU A C   1 
ATOM 1164 O O   . GLU A 1 163 ? 5.785   6.947   -8.330  1.00 77.04  ? 163 GLU A O   1 
ATOM 1165 C CB  . GLU A 1 163 ? 5.007   7.256   -11.491 1.00 80.32  ? 163 GLU A CB  1 
ATOM 1166 C CG  . GLU A 1 163 ? 3.760   7.572   -10.699 1.00 83.24  ? 163 GLU A CG  1 
ATOM 1167 C CD  . GLU A 1 163 ? 2.568   7.848   -11.591 1.00 85.79  ? 163 GLU A CD  1 
ATOM 1168 O OE1 . GLU A 1 163 ? 2.652   7.561   -12.803 1.00 83.82  ? 163 GLU A OE1 1 
ATOM 1169 O OE2 . GLU A 1 163 ? 1.546   8.353   -11.082 1.00 86.45  ? 163 GLU A OE2 1 
ATOM 1170 N N   . LEU A 1 164 ? 5.290   4.949   -9.242  1.00 71.83  ? 164 LEU A N   1 
ATOM 1171 C CA  . LEU A 1 164 ? 4.938   4.349   -7.961  1.00 66.80  ? 164 LEU A CA  1 
ATOM 1172 C C   . LEU A 1 164 ? 6.159   4.133   -7.081  1.00 70.46  ? 164 LEU A C   1 
ATOM 1173 O O   . LEU A 1 164 ? 6.047   4.172   -5.851  1.00 78.27  ? 164 LEU A O   1 
ATOM 1174 C CB  . LEU A 1 164 ? 4.217   3.018   -8.181  1.00 65.23  ? 164 LEU A CB  1 
ATOM 1175 C CG  . LEU A 1 164 ? 2.768   3.075   -8.667  1.00 70.41  ? 164 LEU A CG  1 
ATOM 1176 C CD1 . LEU A 1 164 ? 2.265   1.679   -8.994  1.00 67.57  ? 164 LEU A CD1 1 
ATOM 1177 C CD2 . LEU A 1 164 ? 1.881   3.735   -7.630  1.00 73.74  ? 164 LEU A CD2 1 
ATOM 1178 N N   . ALA A 1 165 ? 7.326   3.902   -7.683  1.00 74.64  ? 165 ALA A N   1 
ATOM 1179 C CA  . ALA A 1 165 ? 8.551   3.691   -6.927  1.00 74.60  ? 165 ALA A CA  1 
ATOM 1180 C C   . ALA A 1 165 ? 9.112   4.972   -6.331  1.00 78.06  ? 165 ALA A C   1 
ATOM 1181 O O   . ALA A 1 165 ? 10.020  4.901   -5.496  1.00 79.96  ? 165 ALA A O   1 
ATOM 1182 C CB  . ALA A 1 165 ? 9.610   3.033   -7.815  1.00 74.01  ? 165 ALA A CB  1 
ATOM 1183 N N   . THR A 1 166 ? 8.599   6.133   -6.729  1.00 80.24  ? 166 THR A N   1 
ATOM 1184 C CA  . THR A 1 166 ? 9.065   7.398   -6.193  1.00 81.77  ? 166 THR A CA  1 
ATOM 1185 C C   . THR A 1 166 ? 8.463   7.632   -4.808  1.00 81.15  ? 166 THR A C   1 
ATOM 1186 O O   . THR A 1 166 ? 7.723   6.805   -4.272  1.00 78.73  ? 166 THR A O   1 
ATOM 1187 C CB  . THR A 1 166 ? 8.717   8.543   -7.143  1.00 84.48  ? 166 THR A CB  1 
ATOM 1188 O OG1 . THR A 1 166 ? 7.306   8.551   -7.389  1.00 82.69  ? 166 THR A OG1 1 
ATOM 1189 C CG2 . THR A 1 166 ? 9.455   8.381   -8.461  1.00 83.16  ? 166 THR A CG2 1 
ATOM 1190 N N   . THR A 1 167 ? 8.785   8.783   -4.220  1.00 84.78  ? 167 THR A N   1 
ATOM 1191 C CA  . THR A 1 167 ? 8.302   9.112   -2.887  1.00 81.70  ? 167 THR A CA  1 
ATOM 1192 C C   . THR A 1 167 ? 6.806   9.385   -2.847  1.00 83.01  ? 167 THR A C   1 
ATOM 1193 O O   . THR A 1 167 ? 6.218   9.361   -1.760  1.00 89.17  ? 167 THR A O   1 
ATOM 1194 C CB  . THR A 1 167 ? 9.053   10.327  -2.337  1.00 83.96  ? 167 THR A CB  1 
ATOM 1195 O OG1 . THR A 1 167 ? 9.281   11.267  -3.393  1.00 84.90  ? 167 THR A OG1 1 
ATOM 1196 C CG2 . THR A 1 167 ? 10.388  9.903   -1.749  1.00 81.47  ? 167 THR A CG2 1 
ATOM 1197 N N   . GLY A 1 168 ? 6.178   9.639   -3.988  1.00 75.97  ? 168 GLY A N   1 
ATOM 1198 C CA  . GLY A 1 168 ? 4.758   9.900   -4.030  1.00 76.11  ? 168 GLY A CA  1 
ATOM 1199 C C   . GLY A 1 168 ? 3.891   8.715   -4.374  1.00 74.56  ? 168 GLY A C   1 
ATOM 1200 O O   . GLY A 1 168 ? 2.673   8.874   -4.494  1.00 74.64  ? 168 GLY A O   1 
ATOM 1201 N N   . GLY A 1 169 ? 4.479   7.526   -4.527  1.00 73.89  ? 169 GLY A N   1 
ATOM 1202 C CA  . GLY A 1 169 ? 3.708   6.371   -4.956  1.00 74.33  ? 169 GLY A CA  1 
ATOM 1203 C C   . GLY A 1 169 ? 2.610   5.974   -3.991  1.00 77.78  ? 169 GLY A C   1 
ATOM 1204 O O   . GLY A 1 169 ? 1.505   5.625   -4.417  1.00 79.72  ? 169 GLY A O   1 
ATOM 1205 N N   . ALA A 1 170 ? 2.891   6.015   -2.687  1.00 78.67  ? 170 ALA A N   1 
ATOM 1206 C CA  . ALA A 1 170 ? 1.881   5.637   -1.705  1.00 74.52  ? 170 ALA A CA  1 
ATOM 1207 C C   . ALA A 1 170 ? 0.713   6.614   -1.687  1.00 74.85  ? 170 ALA A C   1 
ATOM 1208 O O   . ALA A 1 170 ? -0.402  6.238   -1.312  1.00 76.61  ? 170 ALA A O   1 
ATOM 1209 C CB  . ALA A 1 170 ? 2.510   5.536   -0.316  1.00 73.14  ? 170 ALA A CB  1 
ATOM 1210 N N   . SER A 1 171 ? 0.944   7.864   -2.088  1.00 74.02  ? 171 SER A N   1 
ATOM 1211 C CA  . SER A 1 171 ? -0.104  8.876   -2.079  1.00 75.96  ? 171 SER A CA  1 
ATOM 1212 C C   . SER A 1 171 ? -1.092  8.728   -3.227  1.00 78.47  ? 171 SER A C   1 
ATOM 1213 O O   . SER A 1 171 ? -2.177  9.315   -3.167  1.00 77.48  ? 171 SER A O   1 
ATOM 1214 C CB  . SER A 1 171 ? 0.520   10.271  -2.119  1.00 75.60  ? 171 SER A CB  1 
ATOM 1215 O OG  . SER A 1 171 ? 1.719   10.311  -1.367  1.00 78.62  ? 171 SER A OG  1 
ATOM 1216 N N   . GLN A 1 172 ? -0.749  7.968   -4.269  1.00 80.76  ? 172 GLN A N   1 
ATOM 1217 C CA  . GLN A 1 172 ? -1.651  7.805   -5.402  1.00 79.72  ? 172 GLN A CA  1 
ATOM 1218 C C   . GLN A 1 172 ? -2.576  6.612   -5.234  1.00 78.51  ? 172 GLN A C   1 
ATOM 1219 O O   . GLN A 1 172 ? -3.408  6.352   -6.110  1.00 85.39  ? 172 GLN A O   1 
ATOM 1220 C CB  . GLN A 1 172 ? -0.849  7.654   -6.694  1.00 79.62  ? 172 GLN A CB  1 
ATOM 1221 C CG  . GLN A 1 172 ? 0.530   8.258   -6.615  1.00 83.48  ? 172 GLN A CG  1 
ATOM 1222 C CD  . GLN A 1 172 ? 1.437   7.796   -7.729  1.00 84.69  ? 172 GLN A CD  1 
ATOM 1223 O OE1 . GLN A 1 172 ? 2.487   8.389   -7.979  1.00 85.82  ? 172 GLN A OE1 1 
ATOM 1224 N NE2 . GLN A 1 172 ? 1.030   6.740   -8.419  1.00 78.22  ? 172 GLN A NE2 1 
ATOM 1225 N N   . ILE A 1 173 ? -2.447  5.875   -4.137  1.00 70.48  ? 173 ILE A N   1 
ATOM 1226 C CA  . ILE A 1 173 ? -3.195  4.643   -3.924  1.00 70.28  ? 173 ILE A CA  1 
ATOM 1227 C C   . ILE A 1 173 ? -4.175  4.856   -2.781  1.00 72.83  ? 173 ILE A C   1 
ATOM 1228 O O   . ILE A 1 173 ? -3.766  5.084   -1.638  1.00 80.01  ? 173 ILE A O   1 
ATOM 1229 C CB  . ILE A 1 173 ? -2.247  3.474   -3.626  1.00 67.62  ? 173 ILE A CB  1 
ATOM 1230 C CG1 . ILE A 1 173 ? -1.115  3.464   -4.652  1.00 72.84  ? 173 ILE A CG1 1 
ATOM 1231 C CG2 . ILE A 1 173 ? -3.007  2.163   -3.642  1.00 67.89  ? 173 ILE A CG2 1 
ATOM 1232 C CD1 . ILE A 1 173 ? -0.101  2.394   -4.429  1.00 70.69  ? 173 ILE A CD1 1 
ATOM 1233 N N   . GLY A 1 174 ? -5.468  4.767   -3.088  1.00 75.14  ? 174 GLY A N   1 
ATOM 1234 C CA  . GLY A 1 174 ? -6.501  4.992   -2.095  1.00 76.69  ? 174 GLY A CA  1 
ATOM 1235 C C   . GLY A 1 174 ? -6.886  3.708   -1.390  1.00 79.33  ? 174 GLY A C   1 
ATOM 1236 O O   . GLY A 1 174 ? -6.790  2.620   -1.964  1.00 78.77  ? 174 GLY A O   1 
ATOM 1237 N N   . THR A 1 175 ? -7.314  3.840   -0.138  1.00 85.81  ? 175 THR A N   1 
ATOM 1238 C CA  . THR A 1 175 ? -7.765  2.705   0.647   1.00 81.47  ? 175 THR A CA  1 
ATOM 1239 C C   . THR A 1 175 ? -9.292  2.659   0.668   1.00 83.32  ? 175 THR A C   1 
ATOM 1240 O O   . THR A 1 175 ? -9.975  3.507   0.092   1.00 85.96  ? 175 THR A O   1 
ATOM 1241 C CB  . THR A 1 175 ? -7.195  2.773   2.062   1.00 82.99  ? 175 THR A CB  1 
ATOM 1242 O OG1 . THR A 1 175 ? -7.660  3.964   2.707   1.00 89.54  ? 175 THR A OG1 1 
ATOM 1243 C CG2 . THR A 1 175 ? -5.676  2.791   2.018   1.00 78.95  ? 175 THR A CG2 1 
ATOM 1244 N N   . SER A 1 176 ? -9.837  1.655   1.359   1.00 82.40  ? 176 SER A N   1 
ATOM 1245 C CA  . SER A 1 176 ? -11.276 1.424   1.366   1.00 83.81  ? 176 SER A CA  1 
ATOM 1246 C C   . SER A 1 176 ? -12.067 2.552   2.016   1.00 86.15  ? 176 SER A C   1 
ATOM 1247 O O   . SER A 1 176 ? -13.259 2.691   1.726   1.00 85.64  ? 176 SER A O   1 
ATOM 1248 C CB  . SER A 1 176 ? -11.587 0.107   2.080   1.00 83.32  ? 176 SER A CB  1 
ATOM 1249 O OG  . SER A 1 176 ? -11.677 -0.962  1.156   1.00 86.31  ? 176 SER A OG  1 
ATOM 1250 N N   . ASP A 1 177 ? -11.444 3.356   2.873   1.00 89.02  ? 177 ASP A N   1 
ATOM 1251 C CA  . ASP A 1 177 ? -12.131 4.436   3.566   1.00 87.59  ? 177 ASP A CA  1 
ATOM 1252 C C   . ASP A 1 177 ? -12.001 5.777   2.857   1.00 88.91  ? 177 ASP A C   1 
ATOM 1253 O O   . ASP A 1 177 ? -12.447 6.793   3.399   1.00 91.80  ? 177 ASP A O   1 
ATOM 1254 C CB  . ASP A 1 177 ? -11.608 4.562   4.999   1.00 88.28  ? 177 ASP A CB  1 
ATOM 1255 C CG  . ASP A 1 177 ? -10.113 4.785   5.054   1.00 89.31  ? 177 ASP A CG  1 
ATOM 1256 O OD1 . ASP A 1 177 ? -9.440  4.578   4.023   1.00 91.03  ? 177 ASP A OD1 1 
ATOM 1257 O OD2 . ASP A 1 177 ? -9.608  5.173   6.127   1.00 90.27  ? 177 ASP A OD2 1 
ATOM 1258 N N   . GLY A 1 178 ? -11.407 5.808   1.672   1.00 80.98  ? 178 GLY A N   1 
ATOM 1259 C CA  . GLY A 1 178 ? -11.198 7.046   0.955   1.00 79.58  ? 178 GLY A CA  1 
ATOM 1260 C C   . GLY A 1 178 ? -9.906  7.765   1.263   1.00 80.87  ? 178 GLY A C   1 
ATOM 1261 O O   . GLY A 1 178 ? -9.679  8.849   0.716   1.00 83.83  ? 178 GLY A O   1 
ATOM 1262 N N   . LYS A 1 179 ? -9.058  7.204   2.118   1.00 81.47  ? 179 LYS A N   1 
ATOM 1263 C CA  . LYS A 1 179 ? -7.761  7.775   2.437   1.00 82.39  ? 179 LYS A CA  1 
ATOM 1264 C C   . LYS A 1 179 ? -6.677  7.062   1.641   1.00 83.31  ? 179 LYS A C   1 
ATOM 1265 O O   . LYS A 1 179 ? -6.788  5.871   1.340   1.00 81.87  ? 179 LYS A O   1 
ATOM 1266 C CB  . LYS A 1 179 ? -7.462  7.667   3.935   1.00 82.05  ? 179 LYS A CB  1 
ATOM 1267 C CG  . LYS A 1 179 ? -8.096  8.759   4.778   1.00 82.56  ? 179 LYS A CG  1 
ATOM 1268 C CD  . LYS A 1 179 ? -8.147  8.363   6.244   1.00 82.75  ? 179 LYS A CD  1 
ATOM 1269 C CE  . LYS A 1 179 ? -6.775  8.464   6.890   1.00 83.89  ? 179 LYS A CE  1 
ATOM 1270 N NZ  . LYS A 1 179 ? -6.485  7.296   7.764   1.00 82.45  ? 179 LYS A NZ  1 
ATOM 1271 N N   . THR A 1 180 ? -5.630  7.802   1.292   1.00 78.63  ? 180 THR A N   1 
ATOM 1272 C CA  . THR A 1 180 ? -4.539  7.216   0.535   1.00 75.29  ? 180 THR A CA  1 
ATOM 1273 C C   . THR A 1 180 ? -3.713  6.288   1.419   1.00 71.99  ? 180 THR A C   1 
ATOM 1274 O O   . THR A 1 180 ? -3.768  6.346   2.651   1.00 78.95  ? 180 THR A O   1 
ATOM 1275 C CB  . THR A 1 180 ? -3.642  8.301   -0.061  1.00 78.01  ? 180 THR A CB  1 
ATOM 1276 O OG1 . THR A 1 180 ? -2.943  8.976   0.989   1.00 78.31  ? 180 THR A OG1 1 
ATOM 1277 C CG2 . THR A 1 180 ? -4.475  9.310   -0.831  1.00 77.41  ? 180 THR A CG2 1 
ATOM 1278 N N   . VAL A 1 181 ? -2.943  5.412   0.768   1.00 71.12  ? 181 VAL A N   1 
ATOM 1279 C CA  . VAL A 1 181 ? -2.067  4.503   1.500   1.00 68.93  ? 181 VAL A CA  1 
ATOM 1280 C C   . VAL A 1 181 ? -1.021  5.284   2.282   1.00 75.13  ? 181 VAL A C   1 
ATOM 1281 O O   . VAL A 1 181 ? -0.653  4.898   3.398   1.00 81.37  ? 181 VAL A O   1 
ATOM 1282 C CB  . VAL A 1 181 ? -1.422  3.490   0.533   1.00 71.30  ? 181 VAL A CB  1 
ATOM 1283 C CG1 . VAL A 1 181 ? -0.305  2.722   1.220   1.00 65.57  ? 181 VAL A CG1 1 
ATOM 1284 C CG2 . VAL A 1 181 ? -2.472  2.530   0.007   1.00 74.91  ? 181 VAL A CG2 1 
ATOM 1285 N N   . GLN A 1 182 ? -0.527  6.388   1.720   1.00 77.93  ? 182 GLN A N   1 
ATOM 1286 C CA  . GLN A 1 182 ? 0.426   7.223   2.444   1.00 73.48  ? 182 GLN A CA  1 
ATOM 1287 C C   . GLN A 1 182 ? -0.192  7.798   3.711   1.00 78.98  ? 182 GLN A C   1 
ATOM 1288 O O   . GLN A 1 182 ? 0.454   7.833   4.765   1.00 81.78  ? 182 GLN A O   1 
ATOM 1289 C CB  . GLN A 1 182 ? 0.932   8.346   1.541   1.00 72.93  ? 182 GLN A CB  1 
ATOM 1290 C CG  . GLN A 1 182 ? 1.921   9.272   2.218   1.00 74.62  ? 182 GLN A CG  1 
ATOM 1291 C CD  . GLN A 1 182 ? 3.257   8.606   2.463   1.00 79.96  ? 182 GLN A CD  1 
ATOM 1292 O OE1 . GLN A 1 182 ? 3.867   8.064   1.545   1.00 82.61  ? 182 GLN A OE1 1 
ATOM 1293 N NE2 . GLN A 1 182 ? 3.715   8.638   3.708   1.00 77.96  ? 182 GLN A NE2 1 
ATOM 1294 N N   . GLN A 1 183 ? -1.443  8.259   3.628   1.00 81.17  ? 183 GLN A N   1 
ATOM 1295 C CA  . GLN A 1 183 ? -2.110  8.803   4.805   1.00 79.80  ? 183 GLN A CA  1 
ATOM 1296 C C   . GLN A 1 183 ? -2.280  7.744   5.885   1.00 80.81  ? 183 GLN A C   1 
ATOM 1297 O O   . GLN A 1 183 ? -2.123  8.036   7.074   1.00 86.33  ? 183 GLN A O   1 
ATOM 1298 C CB  . GLN A 1 183 ? -3.464  9.395   4.417   1.00 78.48  ? 183 GLN A CB  1 
ATOM 1299 C CG  . GLN A 1 183 ? -3.371  10.686  3.628   1.00 78.72  ? 183 GLN A CG  1 
ATOM 1300 C CD  . GLN A 1 183 ? -4.714  11.137  3.094   1.00 81.19  ? 183 GLN A CD  1 
ATOM 1301 O OE1 . GLN A 1 183 ? -5.745  10.535  3.391   1.00 82.11  ? 183 GLN A OE1 1 
ATOM 1302 N NE2 . GLN A 1 183 ? -4.710  12.202  2.302   1.00 82.55  ? 183 GLN A NE2 1 
ATOM 1303 N N   . TRP A 1 184 ? -2.606  6.511   5.494   1.00 76.90  ? 184 TRP A N   1 
ATOM 1304 C CA  . TRP A 1 184 ? -2.769  5.450   6.482   1.00 75.73  ? 184 TRP A CA  1 
ATOM 1305 C C   . TRP A 1 184 ? -1.430  5.029   7.072   1.00 73.82  ? 184 TRP A C   1 
ATOM 1306 O O   . TRP A 1 184 ? -1.349  4.666   8.251   1.00 78.35  ? 184 TRP A O   1 
ATOM 1307 C CB  . TRP A 1 184 ? -3.484  4.257   5.854   1.00 75.45  ? 184 TRP A CB  1 
ATOM 1308 C CG  . TRP A 1 184 ? -4.937  4.223   6.183   1.00 77.20  ? 184 TRP A CG  1 
ATOM 1309 C CD1 . TRP A 1 184 ? -5.977  4.282   5.304   1.00 78.34  ? 184 TRP A CD1 1 
ATOM 1310 C CD2 . TRP A 1 184 ? -5.519  4.121   7.487   1.00 81.17  ? 184 TRP A CD2 1 
ATOM 1311 N NE1 . TRP A 1 184 ? -7.170  4.225   5.980   1.00 82.38  ? 184 TRP A NE1 1 
ATOM 1312 C CE2 . TRP A 1 184 ? -6.916  4.126   7.323   1.00 81.93  ? 184 TRP A CE2 1 
ATOM 1313 C CE3 . TRP A 1 184 ? -4.993  4.027   8.779   1.00 80.17  ? 184 TRP A CE3 1 
ATOM 1314 C CZ2 . TRP A 1 184 ? -7.795  4.039   8.399   1.00 80.36  ? 184 TRP A CZ2 1 
ATOM 1315 C CZ3 . TRP A 1 184 ? -5.865  3.942   9.845   1.00 80.86  ? 184 TRP A CZ3 1 
ATOM 1316 C CH2 . TRP A 1 184 ? -7.250  3.948   9.650   1.00 81.78  ? 184 TRP A CH2 1 
ATOM 1317 N N   . ILE A 1 185 ? -0.368  5.060   6.265   1.00 72.13  ? 185 ILE A N   1 
ATOM 1318 C CA  . ILE A 1 185 ? 0.967   4.778   6.783   1.00 76.04  ? 185 ILE A CA  1 
ATOM 1319 C C   . ILE A 1 185 ? 1.365   5.826   7.811   1.00 77.08  ? 185 ILE A C   1 
ATOM 1320 O O   . ILE A 1 185 ? 1.908   5.504   8.875   1.00 77.04  ? 185 ILE A O   1 
ATOM 1321 C CB  . ILE A 1 185 ? 1.981   4.699   5.626   1.00 77.49  ? 185 ILE A CB  1 
ATOM 1322 C CG1 . ILE A 1 185 ? 1.882   3.345   4.922   1.00 73.61  ? 185 ILE A CG1 1 
ATOM 1323 C CG2 . ILE A 1 185 ? 3.393   4.937   6.129   1.00 75.03  ? 185 ILE A CG2 1 
ATOM 1324 C CD1 . ILE A 1 185 ? 1.935   2.164   5.861   1.00 73.58  ? 185 ILE A CD1 1 
ATOM 1325 N N   . ILE A 1 186 ? 1.093   7.099   7.514   1.00 76.30  ? 186 ILE A N   1 
ATOM 1326 C CA  . ILE A 1 186 ? 1.373   8.167   8.469   1.00 74.94  ? 186 ILE A CA  1 
ATOM 1327 C C   . ILE A 1 186 ? 0.477   8.045   9.695   1.00 76.69  ? 186 ILE A C   1 
ATOM 1328 O O   . ILE A 1 186 ? 0.869   8.431   10.802  1.00 79.42  ? 186 ILE A O   1 
ATOM 1329 C CB  . ILE A 1 186 ? 1.224   9.538   7.782   1.00 75.51  ? 186 ILE A CB  1 
ATOM 1330 C CG1 . ILE A 1 186 ? 2.245   9.679   6.653   1.00 75.76  ? 186 ILE A CG1 1 
ATOM 1331 C CG2 . ILE A 1 186 ? 1.395   10.672  8.779   1.00 76.48  ? 186 ILE A CG2 1 
ATOM 1332 C CD1 . ILE A 1 186 ? 3.673   9.467   7.097   1.00 76.17  ? 186 ILE A CD1 1 
ATOM 1333 N N   . ALA A 1 187 ? -0.733  7.512   9.531   1.00 75.16  ? 187 ALA A N   1 
ATOM 1334 C CA  . ALA A 1 187 ? -1.644  7.362   10.657  1.00 71.71  ? 187 ALA A CA  1 
ATOM 1335 C C   . ALA A 1 187 ? -1.244  6.234   11.595  1.00 75.58  ? 187 ALA A C   1 
ATOM 1336 O O   . ALA A 1 187 ? -1.464  6.348   12.806  1.00 81.52  ? 187 ALA A O   1 
ATOM 1337 C CB  . ALA A 1 187 ? -3.069  7.127   10.152  1.00 70.11  ? 187 ALA A CB  1 
ATOM 1338 N N   . ASN A 1 188 ? -0.670  5.153   11.074  1.00 72.89  ? 188 ASN A N   1 
ATOM 1339 C CA  . ASN A 1 188 ? -0.301  4.000   11.882  1.00 69.25  ? 188 ASN A CA  1 
ATOM 1340 C C   . ASN A 1 188 ? 1.173   3.983   12.260  1.00 74.76  ? 188 ASN A C   1 
ATOM 1341 O O   . ASN A 1 188 ? 1.620   3.034   12.910  1.00 78.17  ? 188 ASN A O   1 
ATOM 1342 C CB  . ASN A 1 188 ? -0.659  2.705   11.151  1.00 69.42  ? 188 ASN A CB  1 
ATOM 1343 C CG  . ASN A 1 188 ? -2.135  2.597   10.852  1.00 75.47  ? 188 ASN A CG  1 
ATOM 1344 O OD1 . ASN A 1 188 ? -2.968  3.096   11.604  1.00 75.85  ? 188 ASN A OD1 1 
ATOM 1345 N ND2 . ASN A 1 188 ? -2.469  1.938   9.750   1.00 77.59  ? 188 ASN A ND2 1 
ATOM 1346 N N   . ASP A 1 189 ? 1.939   5.004   11.875  1.00 75.93  ? 189 ASP A N   1 
ATOM 1347 C CA  . ASP A 1 189 ? 3.362   5.020   12.191  1.00 76.30  ? 189 ASP A CA  1 
ATOM 1348 C C   . ASP A 1 189 ? 3.628   5.198   13.678  1.00 77.36  ? 189 ASP A C   1 
ATOM 1349 O O   . ASP A 1 189 ? 4.769   5.006   14.117  1.00 80.88  ? 189 ASP A O   1 
ATOM 1350 C CB  . ASP A 1 189 ? 4.074   6.119   11.394  1.00 73.43  ? 189 ASP A CB  1 
ATOM 1351 C CG  . ASP A 1 189 ? 3.657   7.511   11.810  1.00 77.19  ? 189 ASP A CG  1 
ATOM 1352 O OD1 . ASP A 1 189 ? 2.670   7.648   12.559  1.00 80.94  ? 189 ASP A OD1 1 
ATOM 1353 O OD2 . ASP A 1 189 ? 4.321   8.479   11.383  1.00 76.82  ? 189 ASP A OD2 1 
ATOM 1354 N N   . SER A 1 190 ? 2.606   5.566   14.454  1.00 74.78  ? 190 SER A N   1 
ATOM 1355 C CA  . SER A 1 190 ? 2.759   5.631   15.901  1.00 73.05  ? 190 SER A CA  1 
ATOM 1356 C C   . SER A 1 190 ? 3.163   4.283   16.476  1.00 69.91  ? 190 SER A C   1 
ATOM 1357 O O   . SER A 1 190 ? 3.868   4.236   17.484  1.00 75.28  ? 190 SER A O   1 
ATOM 1358 C CB  . SER A 1 190 ? 1.464   6.120   16.548  1.00 70.40  ? 190 SER A CB  1 
ATOM 1359 O OG  . SER A 1 190 ? 0.352   5.368   16.096  1.00 75.49  ? 190 SER A OG  1 
ATOM 1360 N N   . ALA A 1 191 ? 2.744   3.182   15.848  1.00 61.77  ? 191 ALA A N   1 
ATOM 1361 C CA  . ALA A 1 191 ? 3.188   1.867   16.296  1.00 61.07  ? 191 ALA A CA  1 
ATOM 1362 C C   . ALA A 1 191 ? 4.696   1.710   16.147  1.00 65.73  ? 191 ALA A C   1 
ATOM 1363 O O   . ALA A 1 191 ? 5.371   1.231   17.064  1.00 71.40  ? 191 ALA A O   1 
ATOM 1364 C CB  . ALA A 1 191 ? 2.461   0.772   15.520  1.00 61.05  ? 191 ALA A CB  1 
ATOM 1365 N N   . ASN A 1 192 ? 5.241   2.109   14.996  1.00 66.18  ? 192 ASN A N   1 
ATOM 1366 C CA  . ASN A 1 192 ? 6.683   2.021   14.790  1.00 70.39  ? 192 ASN A CA  1 
ATOM 1367 C C   . ASN A 1 192 ? 7.432   2.951   15.735  1.00 70.63  ? 192 ASN A C   1 
ATOM 1368 O O   . ASN A 1 192 ? 8.470   2.575   16.296  1.00 70.32  ? 192 ASN A O   1 
ATOM 1369 C CB  . ASN A 1 192 ? 7.023   2.342   13.335  1.00 67.86  ? 192 ASN A CB  1 
ATOM 1370 C CG  . ASN A 1 192 ? 8.514   2.369   13.077  1.00 70.79  ? 192 ASN A CG  1 
ATOM 1371 O OD1 . ASN A 1 192 ? 9.233   1.435   13.428  1.00 74.09  ? 192 ASN A OD1 1 
ATOM 1372 N ND2 . ASN A 1 192 ? 8.988   3.445   12.463  1.00 66.33  ? 192 ASN A ND2 1 
ATOM 1373 N N   . TYR A 1 193 ? 6.922   4.172   15.917  1.00 65.24  ? 193 TYR A N   1 
ATOM 1374 C CA  . TYR A 1 193 ? 7.540   5.102   16.855  1.00 64.04  ? 193 TYR A CA  1 
ATOM 1375 C C   . TYR A 1 193 ? 7.546   4.538   18.269  1.00 67.07  ? 193 TYR A C   1 
ATOM 1376 O O   . TYR A 1 193 ? 8.564   4.605   18.965  1.00 67.38  ? 193 TYR A O   1 
ATOM 1377 C CB  . TYR A 1 193 ? 6.810   6.443   16.818  1.00 62.82  ? 193 TYR A CB  1 
ATOM 1378 C CG  . TYR A 1 193 ? 7.200   7.333   15.664  1.00 66.78  ? 193 TYR A CG  1 
ATOM 1379 C CD1 . TYR A 1 193 ? 8.492   7.819   15.546  1.00 64.78  ? 193 TYR A CD1 1 
ATOM 1380 C CD2 . TYR A 1 193 ? 6.278   7.683   14.689  1.00 69.69  ? 193 TYR A CD2 1 
ATOM 1381 C CE1 . TYR A 1 193 ? 8.854   8.633   14.497  1.00 67.94  ? 193 TYR A CE1 1 
ATOM 1382 C CE2 . TYR A 1 193 ? 6.632   8.495   13.631  1.00 68.02  ? 193 TYR A CE2 1 
ATOM 1383 C CZ  . TYR A 1 193 ? 7.921   8.966   13.540  1.00 70.98  ? 193 TYR A CZ  1 
ATOM 1384 O OH  . TYR A 1 193 ? 8.282   9.777   12.490  1.00 69.69  ? 193 TYR A OH  1 
ATOM 1385 N N   . ARG A 1 194 ? 6.419   3.970   18.701  1.00 60.73  ? 194 ARG A N   1 
ATOM 1386 C CA  . ARG A 1 194 ? 6.332   3.374   20.026  1.00 55.22  ? 194 ARG A CA  1 
ATOM 1387 C C   . ARG A 1 194 ? 7.293   2.204   20.172  1.00 60.85  ? 194 ARG A C   1 
ATOM 1388 O O   . ARG A 1 194 ? 7.967   2.075   21.196  1.00 68.87  ? 194 ARG A O   1 
ATOM 1389 C CB  . ARG A 1 194 ? 4.899   2.920   20.295  1.00 58.26  ? 194 ARG A CB  1 
ATOM 1390 C CG  . ARG A 1 194 ? 4.635   2.495   21.721  1.00 59.89  ? 194 ARG A CG  1 
ATOM 1391 C CD  . ARG A 1 194 ? 3.300   1.792   21.833  1.00 53.73  ? 194 ARG A CD  1 
ATOM 1392 N NE  . ARG A 1 194 ? 3.129   1.159   23.133  1.00 62.40  ? 194 ARG A NE  1 
ATOM 1393 C CZ  . ARG A 1 194 ? 2.979   -0.145  23.313  1.00 63.65  ? 194 ARG A CZ  1 
ATOM 1394 N NH1 . ARG A 1 194 ? 2.975   -0.986  22.292  1.00 58.99  ? 194 ARG A NH1 1 
ATOM 1395 N NH2 . ARG A 1 194 ? 2.829   -0.618  24.546  1.00 66.73  ? 194 ARG A NH2 1 
ATOM 1396 N N   . ALA A 1 195 ? 7.369   1.341   19.157  1.00 58.06  ? 195 ALA A N   1 
ATOM 1397 C CA  . ALA A 1 195 ? 8.260   0.190   19.237  1.00 54.81  ? 195 ALA A CA  1 
ATOM 1398 C C   . ALA A 1 195 ? 9.715   0.626   19.346  1.00 60.28  ? 195 ALA A C   1 
ATOM 1399 O O   . ALA A 1 195 ? 10.459  0.122   20.197  1.00 64.93  ? 195 ALA A O   1 
ATOM 1400 C CB  . ALA A 1 195 ? 8.061   -0.714  18.023  1.00 56.43  ? 195 ALA A CB  1 
ATOM 1401 N N   . ARG A 1 196 ? 10.134  1.572   18.504  1.00 62.76  ? 196 ARG A N   1 
ATOM 1402 C CA  . ARG A 1 196 ? 11.516  2.037   18.547  1.00 60.86  ? 196 ARG A CA  1 
ATOM 1403 C C   . ARG A 1 196 ? 11.824  2.738   19.864  1.00 63.70  ? 196 ARG A C   1 
ATOM 1404 O O   . ARG A 1 196 ? 12.886  2.516   20.458  1.00 63.54  ? 196 ARG A O   1 
ATOM 1405 C CB  . ARG A 1 196 ? 11.790  2.961   17.363  1.00 60.85  ? 196 ARG A CB  1 
ATOM 1406 C CG  . ARG A 1 196 ? 12.163  2.224   16.093  1.00 63.64  ? 196 ARG A CG  1 
ATOM 1407 C CD  . ARG A 1 196 ? 12.521  3.190   14.988  1.00 63.21  ? 196 ARG A CD  1 
ATOM 1408 N NE  . ARG A 1 196 ? 11.368  3.976   14.568  1.00 64.85  ? 196 ARG A NE  1 
ATOM 1409 C CZ  . ARG A 1 196 ? 11.439  5.216   14.106  1.00 69.12  ? 196 ARG A CZ  1 
ATOM 1410 N NH1 . ARG A 1 196 ? 12.596  5.845   13.990  1.00 68.09  ? 196 ARG A NH1 1 
ATOM 1411 N NH2 . ARG A 1 196 ? 10.320  5.839   13.750  1.00 64.63  ? 196 ARG A NH2 1 
ATOM 1412 N N   . ASN A 1 197 ? 10.904  3.584   20.337  1.00 62.74  ? 197 ASN A N   1 
ATOM 1413 C CA  . ASN A 1 197 ? 11.114  4.288   21.595  1.00 58.04  ? 197 ASN A CA  1 
ATOM 1414 C C   . ASN A 1 197 ? 11.205  3.316   22.763  1.00 59.16  ? 197 ASN A C   1 
ATOM 1415 O O   . ASN A 1 197 ? 12.066  3.466   23.635  1.00 66.51  ? 197 ASN A O   1 
ATOM 1416 C CB  . ASN A 1 197 ? 9.986   5.294   21.815  1.00 59.62  ? 197 ASN A CB  1 
ATOM 1417 C CG  . ASN A 1 197 ? 10.237  6.205   22.994  1.00 59.41  ? 197 ASN A CG  1 
ATOM 1418 O OD1 . ASN A 1 197 ? 11.366  6.345   23.455  1.00 67.26  ? 197 ASN A OD1 1 
ATOM 1419 N ND2 . ASN A 1 197 ? 9.182   6.838   23.482  1.00 57.27  ? 197 ASN A ND2 1 
ATOM 1420 N N   . ILE A 1 198 ? 10.331  2.310   22.793  1.00 53.06  ? 198 ILE A N   1 
ATOM 1421 C CA  . ILE A 1 198 ? 10.352  1.329   23.870  1.00 54.74  ? 198 ILE A CA  1 
ATOM 1422 C C   . ILE A 1 198 ? 11.640  0.519   23.834  1.00 60.60  ? 198 ILE A C   1 
ATOM 1423 O O   . ILE A 1 198 ? 12.249  0.255   24.877  1.00 68.95  ? 198 ILE A O   1 
ATOM 1424 C CB  . ILE A 1 198 ? 9.107   0.428   23.789  1.00 53.41  ? 198 ILE A CB  1 
ATOM 1425 C CG1 . ILE A 1 198 ? 7.873   1.180   24.285  1.00 58.48  ? 198 ILE A CG1 1 
ATOM 1426 C CG2 . ILE A 1 198 ? 9.311   -0.833  24.591  1.00 53.52  ? 198 ILE A CG2 1 
ATOM 1427 C CD1 . ILE A 1 198 ? 6.581   0.434   24.064  1.00 57.12  ? 198 ILE A CD1 1 
ATOM 1428 N N   . GLN A 1 199 ? 12.077  0.108   22.641  1.00 61.56  ? 199 GLN A N   1 
ATOM 1429 C CA  . GLN A 1 199 ? 13.321  -0.645  22.539  1.00 62.43  ? 199 GLN A CA  1 
ATOM 1430 C C   . GLN A 1 199 ? 14.509  0.184   23.012  1.00 63.11  ? 199 GLN A C   1 
ATOM 1431 O O   . GLN A 1 199 ? 15.374  -0.316  23.744  1.00 61.35  ? 199 GLN A O   1 
ATOM 1432 C CB  . GLN A 1 199 ? 13.533  -1.115  21.101  1.00 65.30  ? 199 GLN A CB  1 
ATOM 1433 C CG  . GLN A 1 199 ? 12.800  -2.398  20.758  1.00 63.98  ? 199 GLN A CG  1 
ATOM 1434 C CD  . GLN A 1 199 ? 13.739  -3.569  20.564  1.00 70.24  ? 199 GLN A CD  1 
ATOM 1435 O OE1 . GLN A 1 199 ? 14.906  -3.514  20.950  1.00 74.74  ? 199 GLN A OE1 1 
ATOM 1436 N NE2 . GLN A 1 199 ? 13.235  -4.638  19.960  1.00 72.36  ? 199 GLN A NE2 1 
ATOM 1437 N N   . LYS A 1 200 ? 14.565  1.456   22.614  1.00 61.46  ? 200 LYS A N   1 
ATOM 1438 C CA  . LYS A 1 200 ? 15.676  2.300   23.037  1.00 60.08  ? 200 LYS A CA  1 
ATOM 1439 C C   . LYS A 1 200 ? 15.636  2.559   24.538  1.00 58.84  ? 200 LYS A C   1 
ATOM 1440 O O   . LYS A 1 200 ? 16.684  2.589   25.193  1.00 67.27  ? 200 LYS A O   1 
ATOM 1441 C CB  . LYS A 1 200 ? 15.673  3.614   22.258  1.00 58.50  ? 200 LYS A CB  1 
ATOM 1442 C CG  . LYS A 1 200 ? 16.993  4.356   22.339  1.00 60.66  ? 200 LYS A CG  1 
ATOM 1443 C CD  . LYS A 1 200 ? 18.158  3.430   22.032  1.00 64.94  ? 200 LYS A CD  1 
ATOM 1444 C CE  . LYS A 1 200 ? 19.428  4.205   21.739  1.00 66.80  ? 200 LYS A CE  1 
ATOM 1445 N NZ  . LYS A 1 200 ? 20.601  3.304   21.574  1.00 66.18  ? 200 LYS A NZ  1 
ATOM 1446 N N   . LEU A 1 201 ? 14.443  2.750   25.104  1.00 55.68  ? 201 LEU A N   1 
ATOM 1447 C CA  . LEU A 1 201 ? 14.336  2.943   26.547  1.00 55.70  ? 201 LEU A CA  1 
ATOM 1448 C C   . LEU A 1 201 ? 14.743  1.688   27.306  1.00 55.49  ? 201 LEU A C   1 
ATOM 1449 O O   . LEU A 1 201 ? 15.369  1.776   28.366  1.00 63.39  ? 201 LEU A O   1 
ATOM 1450 C CB  . LEU A 1 201 ? 12.917  3.364   26.921  1.00 57.59  ? 201 LEU A CB  1 
ATOM 1451 C CG  . LEU A 1 201 ? 12.525  4.800   26.575  1.00 56.32  ? 201 LEU A CG  1 
ATOM 1452 C CD1 . LEU A 1 201 ? 11.041  5.012   26.803  1.00 49.89  ? 201 LEU A CD1 1 
ATOM 1453 C CD2 . LEU A 1 201 ? 13.344  5.782   27.391  1.00 53.14  ? 201 LEU A CD2 1 
ATOM 1454 N N   . ALA A 1 202 ? 14.394  0.509   26.785  1.00 47.78  ? 202 ALA A N   1 
ATOM 1455 C CA  . ALA A 1 202 ? 14.856  -0.733  27.392  1.00 46.26  ? 202 ALA A CA  1 
ATOM 1456 C C   . ALA A 1 202 ? 16.370  -0.839  27.349  1.00 51.82  ? 202 ALA A C   1 
ATOM 1457 O O   . ALA A 1 202 ? 16.999  -1.245  28.337  1.00 62.63  ? 202 ALA A O   1 
ATOM 1458 C CB  . ALA A 1 202 ? 14.231  -1.931  26.683  1.00 49.69  ? 202 ALA A CB  1 
ATOM 1459 N N   . TRP A 1 203 ? 16.973  -0.480  26.215  1.00 59.06  ? 203 TRP A N   1 
ATOM 1460 C CA  . TRP A 1 203 ? 18.427  -0.499  26.119  1.00 59.83  ? 203 TRP A CA  1 
ATOM 1461 C C   . TRP A 1 203 ? 19.051  0.468   27.118  1.00 58.49  ? 203 TRP A C   1 
ATOM 1462 O O   . TRP A 1 203 ? 20.047  0.139   27.770  1.00 56.70  ? 203 TRP A O   1 
ATOM 1463 C CB  . TRP A 1 203 ? 18.861  -0.159  24.695  1.00 56.93  ? 203 TRP A CB  1 
ATOM 1464 C CG  . TRP A 1 203 ? 20.340  -0.159  24.515  1.00 58.84  ? 203 TRP A CG  1 
ATOM 1465 C CD1 . TRP A 1 203 ? 21.134  -1.240  24.276  1.00 58.60  ? 203 TRP A CD1 1 
ATOM 1466 C CD2 . TRP A 1 203 ? 21.214  0.971   24.591  1.00 60.53  ? 203 TRP A CD2 1 
ATOM 1467 N NE1 . TRP A 1 203 ? 22.446  -0.852  24.180  1.00 60.33  ? 203 TRP A NE1 1 
ATOM 1468 C CE2 . TRP A 1 203 ? 22.523  0.502   24.372  1.00 60.60  ? 203 TRP A CE2 1 
ATOM 1469 C CE3 . TRP A 1 203 ? 21.015  2.336   24.816  1.00 53.49  ? 203 TRP A CE3 1 
ATOM 1470 C CZ2 . TRP A 1 203 ? 23.627  1.347   24.372  1.00 60.56  ? 203 TRP A CZ2 1 
ATOM 1471 C CZ3 . TRP A 1 203 ? 22.113  3.171   24.817  1.00 58.40  ? 203 TRP A CZ3 1 
ATOM 1472 C CH2 . TRP A 1 203 ? 23.402  2.676   24.595  1.00 61.19  ? 203 TRP A CH2 1 
ATOM 1473 N N   . VAL A 1 204 ? 18.466  1.659   27.262  1.00 57.01  ? 204 VAL A N   1 
ATOM 1474 C CA  . VAL A 1 204 ? 18.989  2.649   28.199  1.00 58.72  ? 204 VAL A CA  1 
ATOM 1475 C C   . VAL A 1 204 ? 18.865  2.151   29.634  1.00 59.77  ? 204 VAL A C   1 
ATOM 1476 O O   . VAL A 1 204 ? 19.776  2.338   30.451  1.00 66.57  ? 204 VAL A O   1 
ATOM 1477 C CB  . VAL A 1 204 ? 18.271  3.997   28.001  1.00 56.36  ? 204 VAL A CB  1 
ATOM 1478 C CG1 . VAL A 1 204 ? 18.602  4.951   29.135  1.00 57.01  ? 204 VAL A CG1 1 
ATOM 1479 C CG2 . VAL A 1 204 ? 18.659  4.612   26.668  1.00 60.76  ? 204 VAL A CG2 1 
ATOM 1480 N N   . ASP A 1 205 ? 17.740  1.517   29.966  1.00 59.91  ? 205 ASP A N   1 
ATOM 1481 C CA  . ASP A 1 205 ? 17.569  0.958   31.303  1.00 60.42  ? 205 ASP A CA  1 
ATOM 1482 C C   . ASP A 1 205 ? 18.607  -0.119  31.584  1.00 61.94  ? 205 ASP A C   1 
ATOM 1483 O O   . ASP A 1 205 ? 19.185  -0.170  32.679  1.00 68.82  ? 205 ASP A O   1 
ATOM 1484 C CB  . ASP A 1 205 ? 16.157  0.394   31.455  1.00 64.43  ? 205 ASP A CB  1 
ATOM 1485 C CG  . ASP A 1 205 ? 15.846  -0.020  32.876  1.00 72.97  ? 205 ASP A CG  1 
ATOM 1486 O OD1 . ASP A 1 205 ? 15.890  0.848   33.772  1.00 80.40  ? 205 ASP A OD1 1 
ATOM 1487 O OD2 . ASP A 1 205 ? 15.565  -1.215  33.101  1.00 71.46  ? 205 ASP A OD2 1 
ATOM 1488 N N   . LYS A 1 206 ? 18.862  -0.990  30.604  1.00 51.27  ? 206 LYS A N   1 
ATOM 1489 C CA  . LYS A 1 206 ? 19.876  -2.018  30.799  1.00 52.94  ? 206 LYS A CA  1 
ATOM 1490 C C   . LYS A 1 206 ? 21.259  -1.401  30.959  1.00 60.60  ? 206 LYS A C   1 
ATOM 1491 O O   . LYS A 1 206 ? 22.078  -1.893  31.740  1.00 64.93  ? 206 LYS A O   1 
ATOM 1492 C CB  . LYS A 1 206 ? 19.879  -3.010  29.640  1.00 53.36  ? 206 LYS A CB  1 
ATOM 1493 C CG  . LYS A 1 206 ? 20.772  -4.204  29.919  1.00 54.79  ? 206 LYS A CG  1 
ATOM 1494 C CD  . LYS A 1 206 ? 21.545  -4.631  28.699  1.00 56.23  ? 206 LYS A CD  1 
ATOM 1495 C CE  . LYS A 1 206 ? 22.730  -5.496  29.091  1.00 60.84  ? 206 LYS A CE  1 
ATOM 1496 N NZ  . LYS A 1 206 ? 24.024  -4.824  28.801  1.00 61.18  ? 206 LYS A NZ  1 
ATOM 1497 N N   . GLN A 1 207 ? 21.546  -0.334  30.212  1.00 62.03  ? 207 GLN A N   1 
ATOM 1498 C CA  . GLN A 1 207 ? 22.833  0.336   30.359  1.00 53.47  ? 207 GLN A CA  1 
ATOM 1499 C C   . GLN A 1 207 ? 22.972  0.951   31.745  1.00 52.47  ? 207 GLN A C   1 
ATOM 1500 O O   . GLN A 1 207 ? 24.048  0.901   32.352  1.00 58.82  ? 207 GLN A O   1 
ATOM 1501 C CB  . GLN A 1 207 ? 23.003  1.403   29.280  1.00 51.03  ? 207 GLN A CB  1 
ATOM 1502 C CG  . GLN A 1 207 ? 23.023  0.854   27.869  1.00 52.34  ? 207 GLN A CG  1 
ATOM 1503 C CD  . GLN A 1 207 ? 24.156  -0.121  27.636  1.00 65.33  ? 207 GLN A CD  1 
ATOM 1504 O OE1 . GLN A 1 207 ? 25.264  0.068   28.128  1.00 65.35  ? 207 GLN A OE1 1 
ATOM 1505 N NE2 . GLN A 1 207 ? 23.877  -1.178  26.886  1.00 67.37  ? 207 GLN A NE2 1 
ATOM 1506 N N   . VAL A 1 208 ? 21.891  1.542   32.257  1.00 57.16  ? 208 VAL A N   1 
ATOM 1507 C CA  . VAL A 1 208 ? 21.918  2.128   33.594  1.00 55.77  ? 208 VAL A CA  1 
ATOM 1508 C C   . VAL A 1 208 ? 22.168  1.051   34.642  1.00 60.81  ? 208 VAL A C   1 
ATOM 1509 O O   . VAL A 1 208 ? 22.958  1.241   35.573  1.00 67.05  ? 208 VAL A O   1 
ATOM 1510 C CB  . VAL A 1 208 ? 20.611  2.894   33.868  1.00 52.64  ? 208 VAL A CB  1 
ATOM 1511 C CG1 . VAL A 1 208 ? 20.493  3.240   35.343  1.00 52.20  ? 208 VAL A CG1 1 
ATOM 1512 C CG2 . VAL A 1 208 ? 20.551  4.152   33.023  1.00 56.65  ? 208 VAL A CG2 1 
ATOM 1513 N N   . HIS A 1 209 ? 21.509  -0.096  34.502  1.00 57.55  ? 209 HIS A N   1 
ATOM 1514 C CA  . HIS A 1 209 ? 21.627  -1.154  35.497  1.00 54.06  ? 209 HIS A CA  1 
ATOM 1515 C C   . HIS A 1 209 ? 22.750  -2.142  35.206  1.00 58.88  ? 209 HIS A C   1 
ATOM 1516 O O   . HIS A 1 209 ? 22.872  -3.142  35.920  1.00 64.90  ? 209 HIS A O   1 
ATOM 1517 C CB  . HIS A 1 209 ? 20.299  -1.903  35.623  1.00 48.64  ? 209 HIS A CB  1 
ATOM 1518 C CG  . HIS A 1 209 ? 19.217  -1.089  36.258  1.00 53.73  ? 209 HIS A CG  1 
ATOM 1519 N ND1 . HIS A 1 209 ? 18.204  -0.502  35.532  1.00 60.04  ? 209 HIS A ND1 1 
ATOM 1520 C CD2 . HIS A 1 209 ? 18.999  -0.751  37.550  1.00 58.93  ? 209 HIS A CD2 1 
ATOM 1521 C CE1 . HIS A 1 209 ? 17.403  0.157   36.351  1.00 58.72  ? 209 HIS A CE1 1 
ATOM 1522 N NE2 . HIS A 1 209 ? 17.864  0.021   37.581  1.00 66.40  ? 209 HIS A NE2 1 
ATOM 1523 N N   . SER A 1 210 ? 23.567  -1.892  34.187  1.00 51.03  ? 210 SER A N   1 
ATOM 1524 C CA  . SER A 1 210 ? 24.673  -2.770  33.837  1.00 52.85  ? 210 SER A CA  1 
ATOM 1525 C C   . SER A 1 210 ? 26.001  -2.037  33.721  1.00 58.84  ? 210 SER A C   1 
ATOM 1526 O O   . SER A 1 210 ? 26.921  -2.554  33.079  1.00 64.17  ? 210 SER A O   1 
ATOM 1527 C CB  . SER A 1 210 ? 24.370  -3.495  32.523  1.00 54.75  ? 210 SER A CB  1 
ATOM 1528 O OG  . SER A 1 210 ? 24.466  -2.611  31.421  1.00 63.25  ? 210 SER A OG  1 
ATOM 1529 N N   . ARG A 1 211 ? 26.121  -0.849  34.316  1.00 62.00  ? 211 ARG A N   1 
ATOM 1530 C CA  . ARG A 1 211 ? 27.324  -0.025  34.279  1.00 59.51  ? 211 ARG A CA  1 
ATOM 1531 C C   . ARG A 1 211 ? 27.745  0.335   32.862  1.00 62.44  ? 211 ARG A C   1 
ATOM 1532 O O   . ARG A 1 211 ? 28.943  0.446   32.583  1.00 70.08  ? 211 ARG A O   1 
ATOM 1533 C CB  . ARG A 1 211 ? 28.496  -0.702  34.996  1.00 57.47  ? 211 ARG A CB  1 
ATOM 1534 C CG  . ARG A 1 211 ? 28.586  -0.393  36.473  1.00 57.59  ? 211 ARG A CG  1 
ATOM 1535 C CD  . ARG A 1 211 ? 29.538  -1.352  37.161  1.00 64.89  ? 211 ARG A CD  1 
ATOM 1536 N NE  . ARG A 1 211 ? 29.317  -2.734  36.752  1.00 67.64  ? 211 ARG A NE  1 
ATOM 1537 C CZ  . ARG A 1 211 ? 28.287  -3.478  37.134  1.00 64.71  ? 211 ARG A CZ  1 
ATOM 1538 N NH1 . ARG A 1 211 ? 27.360  -3.009  37.951  1.00 63.80  ? 211 ARG A NH1 1 
ATOM 1539 N NH2 . ARG A 1 211 ? 28.188  -4.724  36.684  1.00 65.97  ? 211 ARG A NH2 1 
ATOM 1540 N N   . GLY A 1 212 ? 26.792  0.521   31.953  1.00 48.85  ? 212 GLY A N   1 
ATOM 1541 C CA  . GLY A 1 212 ? 27.091  0.822   30.572  1.00 53.27  ? 212 GLY A CA  1 
ATOM 1542 C C   . GLY A 1 212 ? 27.398  2.290   30.349  1.00 58.23  ? 212 GLY A C   1 
ATOM 1543 O O   . GLY A 1 212 ? 27.980  2.976   31.189  1.00 60.02  ? 212 GLY A O   1 
ATOM 1544 N N   . SER A 1 213 ? 27.008  2.767   29.171  1.00 61.48  ? 213 SER A N   1 
ATOM 1545 C CA  . SER A 1 213 ? 27.167  4.163   28.792  1.00 59.38  ? 213 SER A CA  1 
ATOM 1546 C C   . SER A 1 213 ? 25.947  4.614   28.006  1.00 59.02  ? 213 SER A C   1 
ATOM 1547 O O   . SER A 1 213 ? 25.445  3.885   27.146  1.00 67.47  ? 213 SER A O   1 
ATOM 1548 C CB  . SER A 1 213 ? 28.434  4.373   27.958  1.00 63.45  ? 213 SER A CB  1 
ATOM 1549 O OG  . SER A 1 213 ? 29.595  4.067   28.710  1.00 71.25  ? 213 SER A OG  1 
ATOM 1550 N N   . ILE A 1 214 ? 25.471  5.820   28.305  1.00 52.61  ? 214 ILE A N   1 
ATOM 1551 C CA  . ILE A 1 214 ? 24.335  6.405   27.605  1.00 56.06  ? 214 ILE A CA  1 
ATOM 1552 C C   . ILE A 1 214 ? 24.684  7.833   27.218  1.00 57.58  ? 214 ILE A C   1 
ATOM 1553 O O   . ILE A 1 214 ? 25.322  8.560   27.986  1.00 60.85  ? 214 ILE A O   1 
ATOM 1554 C CB  . ILE A 1 214 ? 23.048  6.374   28.457  1.00 57.02  ? 214 ILE A CB  1 
ATOM 1555 C CG1 . ILE A 1 214 ? 23.301  6.972   29.841  1.00 62.28  ? 214 ILE A CG1 1 
ATOM 1556 C CG2 . ILE A 1 214 ? 22.515  4.958   28.571  1.00 58.06  ? 214 ILE A CG2 1 
ATOM 1557 C CD1 . ILE A 1 214 ? 22.039  7.244   30.621  1.00 57.56  ? 214 ILE A CD1 1 
ATOM 1558 N N   . LYS A 1 215 ? 24.276  8.227   26.018  1.00 64.59  ? 215 LYS A N   1 
ATOM 1559 C CA  . LYS A 1 215 ? 24.365  9.609   25.571  1.00 59.33  ? 215 LYS A CA  1 
ATOM 1560 C C   . LYS A 1 215 ? 22.985  10.233  25.728  1.00 62.19  ? 215 LYS A C   1 
ATOM 1561 O O   . LYS A 1 215 ? 22.006  9.730   25.165  1.00 67.82  ? 215 LYS A O   1 
ATOM 1562 C CB  . LYS A 1 215 ? 24.845  9.690   24.124  1.00 59.22  ? 215 LYS A CB  1 
ATOM 1563 C CG  . LYS A 1 215 ? 26.254  9.168   23.911  1.00 64.07  ? 215 LYS A CG  1 
ATOM 1564 C CD  . LYS A 1 215 ? 26.761  9.505   22.520  1.00 69.94  ? 215 LYS A CD  1 
ATOM 1565 C CE  . LYS A 1 215 ? 26.978  8.250   21.694  1.00 69.49  ? 215 LYS A CE  1 
ATOM 1566 N NZ  . LYS A 1 215 ? 25.775  7.908   20.887  1.00 70.51  ? 215 LYS A NZ  1 
ATOM 1567 N N   . VAL A 1 216 ? 22.906  11.316  26.493  1.00 52.84  ? 216 VAL A N   1 
ATOM 1568 C CA  . VAL A 1 216 ? 21.634  11.895  26.905  1.00 54.96  ? 216 VAL A CA  1 
ATOM 1569 C C   . VAL A 1 216 ? 21.466  13.246  26.227  1.00 57.88  ? 216 VAL A C   1 
ATOM 1570 O O   . VAL A 1 216 ? 22.389  14.068  26.231  1.00 59.34  ? 216 VAL A O   1 
ATOM 1571 C CB  . VAL A 1 216 ? 21.546  12.044  28.434  1.00 58.48  ? 216 VAL A CB  1 
ATOM 1572 C CG1 . VAL A 1 216 ? 20.204  12.628  28.822  1.00 61.94  ? 216 VAL A CG1 1 
ATOM 1573 C CG2 . VAL A 1 216 ? 21.769  10.708  29.112  1.00 55.08  ? 216 VAL A CG2 1 
ATOM 1574 N N   . LEU A 1 217 ? 20.295  13.470  25.642  1.00 57.18  ? 217 LEU A N   1 
ATOM 1575 C CA  . LEU A 1 217 ? 19.933  14.767  25.090  1.00 55.86  ? 217 LEU A CA  1 
ATOM 1576 C C   . LEU A 1 217 ? 19.047  15.494  26.092  1.00 60.27  ? 217 LEU A C   1 
ATOM 1577 O O   . LEU A 1 217 ? 17.974  14.999  26.450  1.00 69.67  ? 217 LEU A O   1 
ATOM 1578 C CB  . LEU A 1 217 ? 19.213  14.620  23.753  1.00 59.18  ? 217 LEU A CB  1 
ATOM 1579 C CG  . LEU A 1 217 ? 18.793  15.963  23.161  1.00 60.36  ? 217 LEU A CG  1 
ATOM 1580 C CD1 . LEU A 1 217 ? 20.020  16.705  22.682  1.00 58.95  ? 217 LEU A CD1 1 
ATOM 1581 C CD2 . LEU A 1 217 ? 17.796  15.784  22.034  1.00 59.84  ? 217 LEU A CD2 1 
ATOM 1582 N N   . PHE A 1 218 ? 19.491  16.662  26.538  1.00 59.63  ? 218 PHE A N   1 
ATOM 1583 C CA  . PHE A 1 218 ? 18.734  17.481  27.475  1.00 54.57  ? 218 PHE A CA  1 
ATOM 1584 C C   . PHE A 1 218 ? 18.065  18.606  26.696  1.00 56.26  ? 218 PHE A C   1 
ATOM 1585 O O   . PHE A 1 218 ? 18.683  19.641  26.430  1.00 65.44  ? 218 PHE A O   1 
ATOM 1586 C CB  . PHE A 1 218 ? 19.642  18.030  28.571  1.00 59.68  ? 218 PHE A CB  1 
ATOM 1587 C CG  . PHE A 1 218 ? 20.252  16.967  29.435  1.00 59.86  ? 218 PHE A CG  1 
ATOM 1588 C CD1 . PHE A 1 218 ? 19.519  16.374  30.447  1.00 59.17  ? 218 PHE A CD1 1 
ATOM 1589 C CD2 . PHE A 1 218 ? 21.561  16.564  29.236  1.00 57.07  ? 218 PHE A CD2 1 
ATOM 1590 C CE1 . PHE A 1 218 ? 20.080  15.399  31.245  1.00 60.16  ? 218 PHE A CE1 1 
ATOM 1591 C CE2 . PHE A 1 218 ? 22.126  15.590  30.031  1.00 59.90  ? 218 PHE A CE2 1 
ATOM 1592 C CZ  . PHE A 1 218 ? 21.386  15.009  31.038  1.00 59.48  ? 218 PHE A CZ  1 
ATOM 1593 N N   . GLN A 1 219 ? 16.805  18.398  26.331  1.00 56.51  ? 219 GLN A N   1 
ATOM 1594 C CA  . GLN A 1 219 ? 16.038  19.351  25.545  1.00 58.74  ? 219 GLN A CA  1 
ATOM 1595 C C   . GLN A 1 219 ? 14.955  19.976  26.411  1.00 65.20  ? 219 GLN A C   1 
ATOM 1596 O O   . GLN A 1 219 ? 14.207  19.266  27.090  1.00 73.29  ? 219 GLN A O   1 
ATOM 1597 C CB  . GLN A 1 219 ? 15.406  18.669  24.332  1.00 58.88  ? 219 GLN A CB  1 
ATOM 1598 C CG  . GLN A 1 219 ? 14.521  19.574  23.502  1.00 63.69  ? 219 GLN A CG  1 
ATOM 1599 C CD  . GLN A 1 219 ? 15.170  19.987  22.202  1.00 67.64  ? 219 GLN A CD  1 
ATOM 1600 O OE1 . GLN A 1 219 ? 16.063  19.307  21.697  1.00 71.31  ? 219 GLN A OE1 1 
ATOM 1601 N NE2 . GLN A 1 219 ? 14.727  21.107  21.649  1.00 71.62  ? 219 GLN A NE2 1 
ATOM 1602 N N   . GLY A 1 220 ? 14.869  21.293  26.390  1.00 59.84  ? 220 GLY A N   1 
ATOM 1603 C CA  . GLY A 1 220 ? 13.849  21.976  27.158  1.00 55.83  ? 220 GLY A CA  1 
ATOM 1604 C C   . GLY A 1 220 ? 14.078  23.472  27.187  1.00 55.30  ? 220 GLY A C   1 
ATOM 1605 O O   . GLY A 1 220 ? 14.871  24.024  26.433  1.00 58.49  ? 220 GLY A O   1 
ATOM 1606 N N   . ASP A 1 221 ? 13.332  24.120  28.079  1.00 67.16  ? 221 ASP A N   1 
ATOM 1607 C CA  . ASP A 1 221 ? 13.371  25.564  28.269  1.00 62.52  ? 221 ASP A CA  1 
ATOM 1608 C C   . ASP A 1 221 ? 14.375  25.957  29.345  1.00 63.32  ? 221 ASP A C   1 
ATOM 1609 O O   . ASP A 1 221 ? 15.267  25.176  29.689  1.00 62.34  ? 221 ASP A O   1 
ATOM 1610 C CB  . ASP A 1 221 ? 11.979  26.099  28.619  1.00 66.49  ? 221 ASP A CB  1 
ATOM 1611 C CG  . ASP A 1 221 ? 11.279  25.268  29.679  1.00 77.98  ? 221 ASP A CG  1 
ATOM 1612 O OD1 . ASP A 1 221 ? 11.952  24.798  30.619  1.00 70.98  ? 221 ASP A OD1 1 
ATOM 1613 O OD2 . ASP A 1 221 ? 10.048  25.088  29.572  1.00 81.11  ? 221 ASP A OD2 1 
ATOM 1614 N N   . SER A 1 222 ? 14.248  27.190  29.844  1.00 61.53  ? 222 SER A N   1 
ATOM 1615 C CA  . SER A 1 222 ? 15.122  27.718  30.887  1.00 58.85  ? 222 SER A CA  1 
ATOM 1616 C C   . SER A 1 222 ? 15.323  26.759  32.053  1.00 59.26  ? 222 SER A C   1 
ATOM 1617 O O   . SER A 1 222 ? 16.411  26.739  32.637  1.00 62.60  ? 222 SER A O   1 
ATOM 1618 C CB  . SER A 1 222 ? 14.550  29.035  31.410  1.00 60.95  ? 222 SER A CB  1 
ATOM 1619 O OG  . SER A 1 222 ? 13.202  28.879  31.808  1.00 63.27  ? 222 SER A OG  1 
ATOM 1620 N N   . MET A 1 223 ? 14.307  25.977  32.415  1.00 59.41  ? 223 MET A N   1 
ATOM 1621 C CA  . MET A 1 223 ? 14.460  25.036  33.517  1.00 52.80  ? 223 MET A CA  1 
ATOM 1622 C C   . MET A 1 223 ? 15.436  23.920  33.181  1.00 59.53  ? 223 MET A C   1 
ATOM 1623 O O   . MET A 1 223 ? 16.196  23.486  34.053  1.00 73.68  ? 223 MET A O   1 
ATOM 1624 C CB  . MET A 1 223 ? 13.103  24.452  33.903  1.00 59.26  ? 223 MET A CB  1 
ATOM 1625 C CG  . MET A 1 223 ? 12.128  25.487  34.417  1.00 61.84  ? 223 MET A CG  1 
ATOM 1626 S SD  . MET A 1 223 ? 12.774  26.428  35.808  1.00 77.52  ? 223 MET A SD  1 
ATOM 1627 C CE  . MET A 1 223 ? 12.868  25.165  37.066  1.00 54.73  ? 223 MET A CE  1 
ATOM 1628 N N   . THR A 1 224 ? 15.427  23.440  31.937  1.00 59.62  ? 224 THR A N   1 
ATOM 1629 C CA  . THR A 1 224 ? 16.417  22.457  31.516  1.00 55.94  ? 224 THR A CA  1 
ATOM 1630 C C   . THR A 1 224 ? 17.803  23.070  31.392  1.00 58.04  ? 224 THR A C   1 
ATOM 1631 O O   . THR A 1 224 ? 18.793  22.441  31.779  1.00 63.71  ? 224 THR A O   1 
ATOM 1632 C CB  . THR A 1 224 ? 16.001  21.822  30.190  1.00 60.43  ? 224 THR A CB  1 
ATOM 1633 O OG1 . THR A 1 224 ? 14.710  21.219  30.333  1.00 74.79  ? 224 THR A OG1 1 
ATOM 1634 C CG2 . THR A 1 224 ? 17.003  20.761  29.764  1.00 44.22  ? 224 THR A CG2 1 
ATOM 1635 N N   . ALA A 1 225 ? 17.896  24.291  30.875  1.00 58.77  ? 225 ALA A N   1 
ATOM 1636 C CA  . ALA A 1 225 ? 19.178  24.968  30.738  1.00 52.49  ? 225 ALA A CA  1 
ATOM 1637 C C   . ALA A 1 225 ? 19.800  25.333  32.076  1.00 53.27  ? 225 ALA A C   1 
ATOM 1638 O O   . ALA A 1 225 ? 21.012  25.565  32.134  1.00 56.81  ? 225 ALA A O   1 
ATOM 1639 C CB  . ALA A 1 225 ? 19.016  26.228  29.885  1.00 50.20  ? 225 ALA A CB  1 
ATOM 1640 N N   . GLY A 1 226 ? 19.014  25.380  33.146  1.00 59.39  ? 226 GLY A N   1 
ATOM 1641 C CA  . GLY A 1 226 ? 19.512  25.819  34.430  1.00 54.49  ? 226 GLY A CA  1 
ATOM 1642 C C   . GLY A 1 226 ? 19.493  27.313  34.633  1.00 55.95  ? 226 GLY A C   1 
ATOM 1643 O O   . GLY A 1 226 ? 20.455  27.860  35.179  1.00 59.96  ? 226 GLY A O   1 
ATOM 1644 N N   . TYR A 1 227 ? 18.428  27.988  34.209  1.00 49.49  ? 227 TYR A N   1 
ATOM 1645 C CA  . TYR A 1 227 ? 18.354  29.442  34.268  1.00 51.56  ? 227 TYR A CA  1 
ATOM 1646 C C   . TYR A 1 227 ? 18.491  29.914  35.710  1.00 54.44  ? 227 TYR A C   1 
ATOM 1647 O O   . TYR A 1 227 ? 17.854  29.369  36.616  1.00 59.38  ? 227 TYR A O   1 
ATOM 1648 C CB  . TYR A 1 227 ? 17.032  29.908  33.663  1.00 49.73  ? 227 TYR A CB  1 
ATOM 1649 C CG  . TYR A 1 227 ? 16.700  31.385  33.792  1.00 54.02  ? 227 TYR A CG  1 
ATOM 1650 C CD1 . TYR A 1 227 ? 16.766  32.222  32.689  1.00 55.46  ? 227 TYR A CD1 1 
ATOM 1651 C CD2 . TYR A 1 227 ? 16.277  31.931  34.997  1.00 56.01  ? 227 TYR A CD2 1 
ATOM 1652 C CE1 . TYR A 1 227 ? 16.453  33.561  32.787  1.00 57.92  ? 227 TYR A CE1 1 
ATOM 1653 C CE2 . TYR A 1 227 ? 15.964  33.268  35.105  1.00 55.77  ? 227 TYR A CE2 1 
ATOM 1654 C CZ  . TYR A 1 227 ? 16.050  34.078  33.997  1.00 59.64  ? 227 TYR A CZ  1 
ATOM 1655 O OH  . TYR A 1 227 ? 15.736  35.412  34.102  1.00 58.34  ? 227 TYR A OH  1 
ATOM 1656 N N   . ASP A 1 228 ? 19.326  30.927  35.918  1.00 61.16  ? 228 ASP A N   1 
ATOM 1657 C CA  . ASP A 1 228 ? 19.479  31.584  37.213  1.00 60.82  ? 228 ASP A CA  1 
ATOM 1658 C C   . ASP A 1 228 ? 20.031  32.978  36.937  1.00 66.28  ? 228 ASP A C   1 
ATOM 1659 O O   . ASP A 1 228 ? 21.196  33.127  36.560  1.00 69.88  ? 228 ASP A O   1 
ATOM 1660 C CB  . ASP A 1 228 ? 20.391  30.789  38.140  1.00 60.95  ? 228 ASP A CB  1 
ATOM 1661 C CG  . ASP A 1 228 ? 20.463  31.375  39.539  1.00 69.06  ? 228 ASP A CG  1 
ATOM 1662 O OD1 . ASP A 1 228 ? 19.826  32.417  39.792  1.00 72.97  ? 228 ASP A OD1 1 
ATOM 1663 O OD2 . ASP A 1 228 ? 21.155  30.785  40.394  1.00 76.69  ? 228 ASP A OD2 1 
ATOM 1664 N N   . THR A 1 229 ? 19.188  33.992  37.106  1.00 62.97  ? 229 THR A N   1 
ATOM 1665 C CA  . THR A 1 229 ? 19.594  35.383  36.967  1.00 60.64  ? 229 THR A CA  1 
ATOM 1666 C C   . THR A 1 229 ? 19.304  36.190  38.223  1.00 62.81  ? 229 THR A C   1 
ATOM 1667 O O   . THR A 1 229 ? 19.325  37.423  38.178  1.00 70.11  ? 229 THR A O   1 
ATOM 1668 C CB  . THR A 1 229 ? 18.900  36.025  35.763  1.00 66.74  ? 229 THR A CB  1 
ATOM 1669 O OG1 . THR A 1 229 ? 17.481  35.967  35.942  1.00 68.59  ? 229 THR A OG1 1 
ATOM 1670 C CG2 . THR A 1 229 ? 19.272  35.296  34.482  1.00 59.82  ? 229 THR A CG2 1 
ATOM 1671 N N   . THR A 1 230 ? 19.037  35.521  39.342  1.00 59.81  ? 230 THR A N   1 
ATOM 1672 C CA  . THR A 1 230 ? 18.666  36.183  40.584  1.00 63.67  ? 230 THR A CA  1 
ATOM 1673 C C   . THR A 1 230 ? 19.717  36.071  41.674  1.00 67.20  ? 230 THR A C   1 
ATOM 1674 O O   . THR A 1 230 ? 20.022  37.074  42.323  1.00 69.42  ? 230 THR A O   1 
ATOM 1675 C CB  . THR A 1 230 ? 17.348  35.611  41.115  1.00 61.81  ? 230 THR A CB  1 
ATOM 1676 O OG1 . THR A 1 230 ? 16.488  35.290  40.013  1.00 63.29  ? 230 THR A OG1 1 
ATOM 1677 C CG2 . THR A 1 230 ? 16.657  36.615  42.009  1.00 62.93  ? 230 THR A CG2 1 
ATOM 1678 N N   . SER A 1 231 ? 20.274  34.887  41.890  1.00 69.66  ? 231 SER A N   1 
ATOM 1679 C CA  . SER A 1 231 ? 21.280  34.669  42.915  1.00 70.44  ? 231 SER A CA  1 
ATOM 1680 C C   . SER A 1 231 ? 22.665  35.009  42.382  1.00 67.42  ? 231 SER A C   1 
ATOM 1681 O O   . SER A 1 231 ? 22.859  35.232  41.187  1.00 70.72  ? 231 SER A O   1 
ATOM 1682 C CB  . SER A 1 231 ? 21.248  33.219  43.404  1.00 68.45  ? 231 SER A CB  1 
ATOM 1683 O OG  . SER A 1 231 ? 21.695  32.332  42.396  1.00 67.21  ? 231 SER A OG  1 
ATOM 1684 N N   . THR A 1 232 ? 23.634  35.060  43.294  1.00 61.37  ? 232 THR A N   1 
ATOM 1685 C CA  . THR A 1 232 ? 25.024  35.210  42.891  1.00 68.53  ? 232 THR A CA  1 
ATOM 1686 C C   . THR A 1 232 ? 25.697  33.872  42.626  1.00 71.41  ? 232 THR A C   1 
ATOM 1687 O O   . THR A 1 232 ? 26.851  33.852  42.185  1.00 75.35  ? 232 THR A O   1 
ATOM 1688 C CB  . THR A 1 232 ? 25.811  35.980  43.953  1.00 73.70  ? 232 THR A CB  1 
ATOM 1689 O OG1 . THR A 1 232 ? 25.901  35.196  45.148  1.00 72.59  ? 232 THR A OG1 1 
ATOM 1690 C CG2 . THR A 1 232 ? 25.136  37.306  44.259  1.00 73.06  ? 232 THR A CG2 1 
ATOM 1691 N N   . ASP A 1 233 ? 25.003  32.768  42.877  1.00 63.66  ? 233 ASP A N   1 
ATOM 1692 C CA  . ASP A 1 233 ? 25.502  31.429  42.575  1.00 61.67  ? 233 ASP A CA  1 
ATOM 1693 C C   . ASP A 1 233 ? 25.302  31.091  41.103  1.00 63.40  ? 233 ASP A C   1 
ATOM 1694 O O   . ASP A 1 233 ? 24.648  30.112  40.747  1.00 65.53  ? 233 ASP A O   1 
ATOM 1695 C CB  . ASP A 1 233 ? 24.810  30.410  43.471  1.00 63.78  ? 233 ASP A CB  1 
ATOM 1696 C CG  . ASP A 1 233 ? 25.526  29.080  43.500  1.00 66.78  ? 233 ASP A CG  1 
ATOM 1697 O OD1 . ASP A 1 233 ? 26.685  29.020  43.044  1.00 73.21  ? 233 ASP A OD1 1 
ATOM 1698 O OD2 . ASP A 1 233 ? 24.932  28.097  43.982  1.00 72.92  ? 233 ASP A OD2 1 
ATOM 1699 N N   . ARG A 1 234 ? 25.870  31.916  40.229  1.00 67.33  ? 234 ARG A N   1 
ATOM 1700 C CA  . ARG A 1 234 ? 25.668  31.791  38.795  1.00 62.04  ? 234 ARG A CA  1 
ATOM 1701 C C   . ARG A 1 234 ? 26.974  31.501  38.071  1.00 62.67  ? 234 ARG A C   1 
ATOM 1702 O O   . ARG A 1 234 ? 28.067  31.737  38.590  1.00 72.27  ? 234 ARG A O   1 
ATOM 1703 C CB  . ARG A 1 234 ? 25.052  33.062  38.210  1.00 64.31  ? 234 ARG A CB  1 
ATOM 1704 C CG  . ARG A 1 234 ? 23.647  33.361  38.667  1.00 68.23  ? 234 ARG A CG  1 
ATOM 1705 C CD  . ARG A 1 234 ? 23.233  34.751  38.223  1.00 69.81  ? 234 ARG A CD  1 
ATOM 1706 N NE  . ARG A 1 234 ? 24.310  35.719  38.383  1.00 71.34  ? 234 ARG A NE  1 
ATOM 1707 C CZ  . ARG A 1 234 ? 24.149  37.032  38.307  1.00 72.30  ? 234 ARG A CZ  1 
ATOM 1708 N NH1 . ARG A 1 234 ? 22.963  37.571  38.079  1.00 68.95  ? 234 ARG A NH1 1 
ATOM 1709 N NH2 . ARG A 1 234 ? 25.205  37.825  38.466  1.00 70.49  ? 234 ARG A NH2 1 
ATOM 1710 N N   . VAL A 1 235 ? 26.837  30.985  36.855  1.00 57.13  ? 235 VAL A N   1 
ATOM 1711 C CA  . VAL A 1 235 ? 27.948  30.847  35.919  1.00 62.03  ? 235 VAL A CA  1 
ATOM 1712 C C   . VAL A 1 235 ? 27.517  31.517  34.621  1.00 63.59  ? 235 VAL A C   1 
ATOM 1713 O O   . VAL A 1 235 ? 26.316  31.546  34.317  1.00 66.86  ? 235 VAL A O   1 
ATOM 1714 C CB  . VAL A 1 235 ? 28.325  29.373  35.705  1.00 60.81  ? 235 VAL A CB  1 
ATOM 1715 C CG1 . VAL A 1 235 ? 28.879  28.780  36.987  1.00 61.89  ? 235 VAL A CG1 1 
ATOM 1716 C CG2 . VAL A 1 235 ? 27.123  28.580  35.220  1.00 58.53  ? 235 VAL A CG2 1 
ATOM 1717 N N   . PRO A 1 236 ? 28.438  32.067  33.832  1.00 67.82  ? 236 PRO A N   1 
ATOM 1718 C CA  . PRO A 1 236 ? 28.041  32.752  32.597  1.00 62.98  ? 236 PRO A CA  1 
ATOM 1719 C C   . PRO A 1 236 ? 27.336  31.804  31.638  1.00 64.89  ? 236 PRO A C   1 
ATOM 1720 O O   . PRO A 1 236 ? 27.511  30.585  31.673  1.00 73.03  ? 236 PRO A O   1 
ATOM 1721 C CB  . PRO A 1 236 ? 29.356  33.263  32.000  1.00 65.80  ? 236 PRO A CB  1 
ATOM 1722 C CG  . PRO A 1 236 ? 30.421  32.958  32.980  1.00 65.96  ? 236 PRO A CG  1 
ATOM 1723 C CD  . PRO A 1 236 ? 29.870  32.207  34.141  1.00 66.24  ? 236 PRO A CD  1 
ATOM 1724 N N   . ALA A 1 237 ? 26.506  32.398  30.780  1.00 63.23  ? 237 ALA A N   1 
ATOM 1725 C CA  . ALA A 1 237 ? 25.702  31.657  29.815  1.00 65.03  ? 237 ALA A CA  1 
ATOM 1726 C C   . ALA A 1 237 ? 26.552  30.710  28.980  1.00 71.33  ? 237 ALA A C   1 
ATOM 1727 O O   . ALA A 1 237 ? 27.507  31.136  28.323  1.00 72.58  ? 237 ALA A O   1 
ATOM 1728 C CB  . ALA A 1 237 ? 24.948  32.627  28.905  1.00 68.77  ? 237 ALA A CB  1 
ATOM 1729 N N   . ASN A 1 238 ? 26.218  29.429  29.007  1.00 69.94  ? 238 ASN A N   1 
ATOM 1730 C CA  . ASN A 1 238 ? 26.958  28.396  28.289  1.00 65.20  ? 238 ASN A CA  1 
ATOM 1731 C C   . ASN A 1 238 ? 25.954  27.410  27.684  1.00 64.75  ? 238 ASN A C   1 
ATOM 1732 O O   . ASN A 1 238 ? 24.749  27.644  27.820  1.00 65.89  ? 238 ASN A O   1 
ATOM 1733 C CB  . ASN A 1 238 ? 27.989  27.774  29.222  1.00 64.16  ? 238 ASN A CB  1 
ATOM 1734 C CG  . ASN A 1 238 ? 27.377  27.263  30.516  1.00 70.15  ? 238 ASN A CG  1 
ATOM 1735 O OD1 . ASN A 1 238 ? 26.191  26.944  30.577  1.00 70.09  ? 238 ASN A OD1 1 
ATOM 1736 N ND2 . ASN A 1 238 ? 28.193  27.184  31.560  1.00 71.16  ? 238 ASN A ND2 1 
ATOM 1737 N N   . ASN A 1 239 ? 26.394  26.338  27.024  1.00 66.44  ? 239 ASN A N   1 
ATOM 1738 C CA  . ASN A 1 239 ? 25.517  25.288  26.518  1.00 67.31  ? 239 ASN A CA  1 
ATOM 1739 C C   . ASN A 1 239 ? 24.470  25.822  25.549  1.00 70.21  ? 239 ASN A C   1 
ATOM 1740 O O   . ASN A 1 239 ? 23.346  25.313  25.499  1.00 71.97  ? 239 ASN A O   1 
ATOM 1741 C CB  . ASN A 1 239 ? 24.838  24.560  27.680  1.00 66.45  ? 239 ASN A CB  1 
ATOM 1742 C CG  . ASN A 1 239 ? 25.832  24.001  28.677  1.00 68.58  ? 239 ASN A CG  1 
ATOM 1743 O OD1 . ASN A 1 239 ? 26.887  23.494  28.299  1.00 70.40  ? 239 ASN A OD1 1 
ATOM 1744 N ND2 . ASN A 1 239 ? 25.501  24.095  29.957  1.00 70.75  ? 239 ASN A ND2 1 
ATOM 1745 N N   . GLY A 1 240 ? 24.827  26.842  24.773  1.00 65.41  ? 240 GLY A N   1 
ATOM 1746 C CA  . GLY A 1 240 ? 23.957  27.364  23.743  1.00 62.50  ? 240 GLY A CA  1 
ATOM 1747 C C   . GLY A 1 240 ? 22.836  28.257  24.223  1.00 68.39  ? 240 GLY A C   1 
ATOM 1748 O O   . GLY A 1 240 ? 21.971  28.618  23.418  1.00 74.52  ? 240 GLY A O   1 
ATOM 1749 N N   . ASP A 1 241 ? 22.816  28.622  25.500  1.00 62.82  ? 241 ASP A N   1 
ATOM 1750 C CA  . ASP A 1 241 ? 21.781  29.482  26.048  1.00 62.74  ? 241 ASP A CA  1 
ATOM 1751 C C   . ASP A 1 241 ? 22.326  30.888  26.261  1.00 65.22  ? 241 ASP A C   1 
ATOM 1752 O O   . ASP A 1 241 ? 23.527  31.094  26.449  1.00 66.70  ? 241 ASP A O   1 
ATOM 1753 C CB  . ASP A 1 241 ? 21.240  28.922  27.367  1.00 62.39  ? 241 ASP A CB  1 
ATOM 1754 C CG  . ASP A 1 241 ? 19.968  29.616  27.817  1.00 68.13  ? 241 ASP A CG  1 
ATOM 1755 O OD1 . ASP A 1 241 ? 19.424  30.425  27.039  1.00 76.17  ? 241 ASP A OD1 1 
ATOM 1756 O OD2 . ASP A 1 241 ? 19.514  29.357  28.950  1.00 69.58  ? 241 ASP A OD2 1 
ATOM 1757 N N   . TRP A 1 242 ? 21.417  31.860  26.220  1.00 64.13  ? 242 TRP A N   1 
ATOM 1758 C CA  . TRP A 1 242 ? 21.757  33.264  26.391  1.00 59.03  ? 242 TRP A CA  1 
ATOM 1759 C C   . TRP A 1 242 ? 21.740  33.713  27.844  1.00 61.17  ? 242 TRP A C   1 
ATOM 1760 O O   . TRP A 1 242 ? 22.381  34.716  28.173  1.00 65.67  ? 242 TRP A O   1 
ATOM 1761 C CB  . TRP A 1 242 ? 20.783  34.139  25.596  1.00 61.24  ? 242 TRP A CB  1 
ATOM 1762 C CG  . TRP A 1 242 ? 19.355  33.870  25.943  1.00 63.76  ? 242 TRP A CG  1 
ATOM 1763 C CD1 . TRP A 1 242 ? 18.520  32.976  25.343  1.00 66.17  ? 242 TRP A CD1 1 
ATOM 1764 C CD2 . TRP A 1 242 ? 18.592  34.497  26.980  1.00 65.92  ? 242 TRP A CD2 1 
ATOM 1765 N NE1 . TRP A 1 242 ? 17.285  33.008  25.941  1.00 65.59  ? 242 TRP A NE1 1 
ATOM 1766 C CE2 . TRP A 1 242 ? 17.302  33.934  26.949  1.00 63.17  ? 242 TRP A CE2 1 
ATOM 1767 C CE3 . TRP A 1 242 ? 18.873  35.483  27.931  1.00 64.04  ? 242 TRP A CE3 1 
ATOM 1768 C CZ2 . TRP A 1 242 ? 16.297  34.322  27.830  1.00 65.80  ? 242 TRP A CZ2 1 
ATOM 1769 C CZ3 . TRP A 1 242 ? 17.875  35.864  28.806  1.00 64.04  ? 242 TRP A CZ3 1 
ATOM 1770 C CH2 . TRP A 1 242 ? 16.604  35.286  28.749  1.00 67.02  ? 242 TRP A CH2 1 
ATOM 1771 N N   . ALA A 1 243 ? 21.029  33.004  28.712  1.00 65.49  ? 243 ALA A N   1 
ATOM 1772 C CA  . ALA A 1 243 ? 20.805  33.436  30.081  1.00 64.16  ? 243 ALA A CA  1 
ATOM 1773 C C   . ALA A 1 243 ? 21.873  32.882  31.013  1.00 63.48  ? 243 ALA A C   1 
ATOM 1774 O O   . ALA A 1 243 ? 22.449  31.820  30.771  1.00 70.96  ? 243 ALA A O   1 
ATOM 1775 C CB  . ALA A 1 243 ? 19.422  33.002  30.567  1.00 63.02  ? 243 ALA A CB  1 
ATOM 1776 N N   . THR A 1 244 ? 22.127  33.623  32.087  1.00 62.69  ? 244 THR A N   1 
ATOM 1777 C CA  . THR A 1 244 ? 23.060  33.174  33.110  1.00 56.92  ? 244 THR A CA  1 
ATOM 1778 C C   . THR A 1 244 ? 22.513  31.923  33.787  1.00 60.41  ? 244 THR A C   1 
ATOM 1779 O O   . THR A 1 244 ? 21.319  31.836  34.081  1.00 68.38  ? 244 THR A O   1 
ATOM 1780 C CB  . THR A 1 244 ? 23.284  34.283  34.136  1.00 62.50  ? 244 THR A CB  1 
ATOM 1781 O OG1 . THR A 1 244 ? 23.267  35.552  33.473  1.00 74.63  ? 244 THR A OG1 1 
ATOM 1782 C CG2 . THR A 1 244 ? 24.623  34.115  34.814  1.00 61.77  ? 244 THR A CG2 1 
ATOM 1783 N N   . HIS A 1 245 ? 23.384  30.950  34.024  1.00 62.53  ? 245 HIS A N   1 
ATOM 1784 C CA  . HIS A 1 245 ? 22.983  29.681  34.609  1.00 58.65  ? 245 HIS A CA  1 
ATOM 1785 C C   . HIS A 1 245 ? 23.465  29.569  36.048  1.00 64.77  ? 245 HIS A C   1 
ATOM 1786 O O   . HIS A 1 245 ? 24.448  30.192  36.451  1.00 69.25  ? 245 HIS A O   1 
ATOM 1787 C CB  . HIS A 1 245 ? 23.529  28.504  33.800  1.00 59.00  ? 245 HIS A CB  1 
ATOM 1788 C CG  . HIS A 1 245 ? 23.077  28.487  32.376  1.00 58.82  ? 245 HIS A CG  1 
ATOM 1789 N ND1 . HIS A 1 245 ? 21.791  28.152  32.010  1.00 58.14  ? 245 HIS A ND1 1 
ATOM 1790 C CD2 . HIS A 1 245 ? 23.738  28.754  31.227  1.00 64.73  ? 245 HIS A CD2 1 
ATOM 1791 C CE1 . HIS A 1 245 ? 21.681  28.220  30.696  1.00 60.63  ? 245 HIS A CE1 1 
ATOM 1792 N NE2 . HIS A 1 245 ? 22.848  28.581  30.197  1.00 67.70  ? 245 HIS A NE2 1 
ATOM 1793 N N   . ALA A 1 246 ? 22.758  28.750  36.819  1.00 58.97  ? 246 ALA A N   1 
ATOM 1794 C CA  . ALA A 1 246 ? 23.209  28.414  38.158  1.00 56.37  ? 246 ALA A CA  1 
ATOM 1795 C C   . ALA A 1 246 ? 24.487  27.583  38.088  1.00 62.08  ? 246 ALA A C   1 
ATOM 1796 O O   . ALA A 1 246 ? 24.790  26.949  37.073  1.00 65.40  ? 246 ALA A O   1 
ATOM 1797 C CB  . ALA A 1 246 ? 22.123  27.651  38.916  1.00 49.93  ? 246 ALA A CB  1 
ATOM 1798 N N   . SER A 1 247 ? 25.244  27.598  39.182  1.00 56.36  ? 247 SER A N   1 
ATOM 1799 C CA  . SER A 1 247 ? 26.508  26.874  39.238  1.00 49.15  ? 247 SER A CA  1 
ATOM 1800 C C   . SER A 1 247 ? 26.343  25.376  39.018  1.00 60.41  ? 247 SER A C   1 
ATOM 1801 O O   . SER A 1 247 ? 27.312  24.713  38.634  1.00 65.53  ? 247 SER A O   1 
ATOM 1802 C CB  . SER A 1 247 ? 27.205  27.127  40.574  1.00 52.26  ? 247 SER A CB  1 
ATOM 1803 O OG  . SER A 1 247 ? 26.458  26.597  41.654  1.00 67.36  ? 247 SER A OG  1 
ATOM 1804 N N   . MET A 1 248 ? 25.152  24.831  39.251  1.00 52.53  ? 248 MET A N   1 
ATOM 1805 C CA  . MET A 1 248 ? 24.837  23.459  38.875  1.00 57.24  ? 248 MET A CA  1 
ATOM 1806 C C   . MET A 1 248 ? 23.430  23.411  38.311  1.00 58.59  ? 248 MET A C   1 
ATOM 1807 O O   . MET A 1 248 ? 22.467  23.756  39.002  1.00 62.08  ? 248 MET A O   1 
ATOM 1808 C CB  . MET A 1 248 ? 24.981  22.500  40.059  1.00 56.10  ? 248 MET A CB  1 
ATOM 1809 C CG  . MET A 1 248 ? 24.638  21.058  39.721  1.00 48.04  ? 248 MET A CG  1 
ATOM 1810 S SD  . MET A 1 248 ? 26.057  20.071  39.219  1.00 64.80  ? 248 MET A SD  1 
ATOM 1811 C CE  . MET A 1 248 ? 27.359  20.808  40.190  1.00 58.22  ? 248 MET A CE  1 
ATOM 1812 N N   . THR A 1 249 ? 23.317  22.990  37.059  1.00 54.79  ? 249 THR A N   1 
ATOM 1813 C CA  . THR A 1 249 ? 22.038  22.780  36.404  1.00 52.61  ? 249 THR A CA  1 
ATOM 1814 C C   . THR A 1 249 ? 21.612  21.327  36.572  1.00 54.44  ? 249 THR A C   1 
ATOM 1815 O O   . THR A 1 249 ? 22.391  20.470  36.991  1.00 65.49  ? 249 THR A O   1 
ATOM 1816 C CB  . THR A 1 249 ? 22.127  23.149  34.922  1.00 54.75  ? 249 THR A CB  1 
ATOM 1817 O OG1 . THR A 1 249 ? 22.896  22.161  34.229  1.00 58.76  ? 249 THR A OG1 1 
ATOM 1818 C CG2 . THR A 1 249 ? 22.803  24.498  34.761  1.00 57.26  ? 249 THR A CG2 1 
ATOM 1819 N N   . TYR A 1 250 ? 20.349  21.058  36.256  1.00 48.08  ? 250 TYR A N   1 
ATOM 1820 C CA  . TYR A 1 250 ? 19.848  19.696  36.401  1.00 37.82  ? 250 TYR A CA  1 
ATOM 1821 C C   . TYR A 1 250 ? 20.565  18.727  35.463  1.00 49.36  ? 250 TYR A C   1 
ATOM 1822 O O   . TYR A 1 250 ? 20.895  17.619  35.896  1.00 59.33  ? 250 TYR A O   1 
ATOM 1823 C CB  . TYR A 1 250 ? 18.319  19.656  36.232  1.00 54.07  ? 250 TYR A CB  1 
ATOM 1824 C CG  . TYR A 1 250 ? 17.747  19.057  34.957  1.00 51.52  ? 250 TYR A CG  1 
ATOM 1825 C CD1 . TYR A 1 250 ? 17.047  19.846  34.058  1.00 51.11  ? 250 TYR A CD1 1 
ATOM 1826 C CD2 . TYR A 1 250 ? 17.845  17.696  34.684  1.00 50.99  ? 250 TYR A CD2 1 
ATOM 1827 C CE1 . TYR A 1 250 ? 16.505  19.313  32.912  1.00 49.35  ? 250 TYR A CE1 1 
ATOM 1828 C CE2 . TYR A 1 250 ? 17.316  17.161  33.533  1.00 50.20  ? 250 TYR A CE2 1 
ATOM 1829 C CZ  . TYR A 1 250 ? 16.644  17.972  32.653  1.00 52.67  ? 250 TYR A CZ  1 
ATOM 1830 O OH  . TYR A 1 250 ? 16.104  17.438  31.507  1.00 68.06  ? 250 TYR A OH  1 
ATOM 1831 N N   . PRO A 1 251 ? 20.802  19.055  34.183  1.00 58.08  ? 251 PRO A N   1 
ATOM 1832 C CA  . PRO A 1 251 ? 21.562  18.109  33.349  1.00 50.07  ? 251 PRO A CA  1 
ATOM 1833 C C   . PRO A 1 251 ? 22.983  17.892  33.830  1.00 49.13  ? 251 PRO A C   1 
ATOM 1834 O O   . PRO A 1 251 ? 23.496  16.769  33.757  1.00 58.34  ? 251 PRO A O   1 
ATOM 1835 C CB  . PRO A 1 251 ? 21.529  18.759  31.960  1.00 50.90  ? 251 PRO A CB  1 
ATOM 1836 C CG  . PRO A 1 251 ? 20.405  19.708  32.001  1.00 52.15  ? 251 PRO A CG  1 
ATOM 1837 C CD  . PRO A 1 251 ? 20.374  20.222  33.393  1.00 56.36  ? 251 PRO A CD  1 
ATOM 1838 N N   . GLN A 1 252 ? 23.640  18.944  34.320  1.00 44.79  ? 252 GLN A N   1 
ATOM 1839 C CA  . GLN A 1 252 ? 24.997  18.796  34.833  1.00 49.37  ? 252 GLN A CA  1 
ATOM 1840 C C   . GLN A 1 252 ? 25.026  17.878  36.048  1.00 53.26  ? 252 GLN A C   1 
ATOM 1841 O O   . GLN A 1 252 ? 25.878  16.983  36.143  1.00 62.75  ? 252 GLN A O   1 
ATOM 1842 C CB  . GLN A 1 252 ? 25.565  20.173  35.174  1.00 46.63  ? 252 GLN A CB  1 
ATOM 1843 C CG  . GLN A 1 252 ? 26.933  20.155  35.814  1.00 54.39  ? 252 GLN A CG  1 
ATOM 1844 C CD  . GLN A 1 252 ? 27.384  21.538  36.231  1.00 59.68  ? 252 GLN A CD  1 
ATOM 1845 O OE1 . GLN A 1 252 ? 26.677  22.523  36.019  1.00 57.62  ? 252 GLN A OE1 1 
ATOM 1846 N NE2 . GLN A 1 252 ? 28.566  21.621  36.827  1.00 55.66  ? 252 GLN A NE2 1 
ATOM 1847 N N   . ARG A 1 253 ? 24.089  18.072  36.978  1.00 53.01  ? 253 ARG A N   1 
ATOM 1848 C CA  . ARG A 1 253 ? 24.007  17.187  38.132  1.00 48.89  ? 253 ARG A CA  1 
ATOM 1849 C C   . ARG A 1 253 ? 23.636  15.772  37.724  1.00 52.71  ? 253 ARG A C   1 
ATOM 1850 O O   . ARG A 1 253 ? 24.135  14.813  38.314  1.00 66.75  ? 253 ARG A O   1 
ATOM 1851 C CB  . ARG A 1 253 ? 23.002  17.726  39.147  1.00 50.45  ? 253 ARG A CB  1 
ATOM 1852 C CG  . ARG A 1 253 ? 22.881  16.865  40.388  1.00 51.09  ? 253 ARG A CG  1 
ATOM 1853 C CD  . ARG A 1 253 ? 23.886  17.275  41.450  1.00 50.59  ? 253 ARG A CD  1 
ATOM 1854 N NE  . ARG A 1 253 ? 25.231  16.792  41.161  1.00 54.04  ? 253 ARG A NE  1 
ATOM 1855 C CZ  . ARG A 1 253 ? 25.806  15.767  41.775  1.00 59.45  ? 253 ARG A CZ  1 
ATOM 1856 N NH1 . ARG A 1 253 ? 25.174  15.081  42.712  1.00 59.99  ? 253 ARG A NH1 1 
ATOM 1857 N NH2 . ARG A 1 253 ? 27.044  15.423  41.442  1.00 58.22  ? 253 ARG A NH2 1 
ATOM 1858 N N   . PHE A 1 254 ? 22.765  15.617  36.725  1.00 52.54  ? 254 PHE A N   1 
ATOM 1859 C CA  . PHE A 1 254 ? 22.437  14.288  36.223  1.00 47.27  ? 254 PHE A CA  1 
ATOM 1860 C C   . PHE A 1 254 ? 23.675  13.586  35.686  1.00 50.49  ? 254 PHE A C   1 
ATOM 1861 O O   . PHE A 1 254 ? 23.919  12.414  35.994  1.00 61.90  ? 254 PHE A O   1 
ATOM 1862 C CB  . PHE A 1 254 ? 21.367  14.405  35.138  1.00 49.04  ? 254 PHE A CB  1 
ATOM 1863 C CG  . PHE A 1 254 ? 20.872  13.087  34.620  1.00 47.04  ? 254 PHE A CG  1 
ATOM 1864 C CD1 . PHE A 1 254 ? 19.853  12.413  35.265  1.00 49.14  ? 254 PHE A CD1 1 
ATOM 1865 C CD2 . PHE A 1 254 ? 21.419  12.527  33.479  1.00 51.21  ? 254 PHE A CD2 1 
ATOM 1866 C CE1 . PHE A 1 254 ? 19.393  11.205  34.785  1.00 54.51  ? 254 PHE A CE1 1 
ATOM 1867 C CE2 . PHE A 1 254 ? 20.963  11.319  32.997  1.00 55.70  ? 254 PHE A CE2 1 
ATOM 1868 C CZ  . PHE A 1 254 ? 19.948  10.658  33.651  1.00 58.16  ? 254 PHE A CZ  1 
ATOM 1869 N N   . MET A 1 255 ? 24.482  14.299  34.899  1.00 57.65  ? 255 MET A N   1 
ATOM 1870 C CA  . MET A 1 255 ? 25.673  13.703  34.306  1.00 54.01  ? 255 MET A CA  1 
ATOM 1871 C C   . MET A 1 255 ? 26.748  13.427  35.347  1.00 57.17  ? 255 MET A C   1 
ATOM 1872 O O   . MET A 1 255 ? 27.590  12.546  35.143  1.00 65.49  ? 255 MET A O   1 
ATOM 1873 C CB  . MET A 1 255 ? 26.224  14.615  33.213  1.00 58.11  ? 255 MET A CB  1 
ATOM 1874 C CG  . MET A 1 255 ? 25.355  14.694  31.974  1.00 56.06  ? 255 MET A CG  1 
ATOM 1875 S SD  . MET A 1 255 ? 26.114  15.709  30.698  1.00 72.37  ? 255 MET A SD  1 
ATOM 1876 C CE  . MET A 1 255 ? 26.075  17.317  31.476  1.00 60.51  ? 255 MET A CE  1 
ATOM 1877 N N   . ALA A 1 256 ? 26.760  14.177  36.447  1.00 52.57  ? 256 ALA A N   1 
ATOM 1878 C CA  . ALA A 1 256 ? 27.721  13.901  37.509  1.00 49.20  ? 256 ALA A CA  1 
ATOM 1879 C C   . ALA A 1 256 ? 27.202  12.879  38.515  1.00 57.57  ? 256 ALA A C   1 
ATOM 1880 O O   . ALA A 1 256 ? 27.984  12.321  39.291  1.00 66.24  ? 256 ALA A O   1 
ATOM 1881 C CB  . ALA A 1 256 ? 28.093  15.196  38.232  1.00 57.37  ? 256 ALA A CB  1 
ATOM 1882 N N   . TYR A 1 257 ? 25.895  12.620  38.509  1.00 54.70  ? 257 TYR A N   1 
ATOM 1883 C CA  . TYR A 1 257 ? 25.272  11.815  39.551  1.00 48.06  ? 257 TYR A CA  1 
ATOM 1884 C C   . TYR A 1 257 ? 24.976  10.398  39.079  1.00 47.90  ? 257 TYR A C   1 
ATOM 1885 O O   . TYR A 1 257 ? 25.266  9.435   39.795  1.00 63.51  ? 257 TYR A O   1 
ATOM 1886 C CB  . TYR A 1 257 ? 23.992  12.507  40.019  1.00 50.45  ? 257 TYR A CB  1 
ATOM 1887 C CG  . TYR A 1 257 ? 23.299  11.870  41.199  1.00 46.48  ? 257 TYR A CG  1 
ATOM 1888 C CD1 . TYR A 1 257 ? 23.816  11.977  42.481  1.00 51.81  ? 257 TYR A CD1 1 
ATOM 1889 C CD2 . TYR A 1 257 ? 22.112  11.177  41.029  1.00 48.37  ? 257 TYR A CD2 1 
ATOM 1890 C CE1 . TYR A 1 257 ? 23.172  11.401  43.556  1.00 49.61  ? 257 TYR A CE1 1 
ATOM 1891 C CE2 . TYR A 1 257 ? 21.465  10.599  42.093  1.00 46.65  ? 257 TYR A CE2 1 
ATOM 1892 C CZ  . TYR A 1 257 ? 21.995  10.713  43.353  1.00 48.48  ? 257 TYR A CZ  1 
ATOM 1893 O OH  . TYR A 1 257 ? 21.341  10.131  44.410  1.00 58.37  ? 257 TYR A OH  1 
ATOM 1894 N N   . LEU A 1 258 ? 24.395  10.247  37.888  1.00 45.89  ? 258 LEU A N   1 
ATOM 1895 C CA  . LEU A 1 258 ? 24.075  8.908   37.399  1.00 53.67  ? 258 LEU A CA  1 
ATOM 1896 C C   . LEU A 1 258 ? 25.299  8.005   37.281  1.00 52.88  ? 258 LEU A C   1 
ATOM 1897 O O   . LEU A 1 258 ? 25.211  6.846   37.722  1.00 55.73  ? 258 LEU A O   1 
ATOM 1898 C CB  . LEU A 1 258 ? 23.325  9.003   36.065  1.00 49.19  ? 258 LEU A CB  1 
ATOM 1899 C CG  . LEU A 1 258 ? 22.662  7.702   35.609  1.00 47.23  ? 258 LEU A CG  1 
ATOM 1900 C CD1 . LEU A 1 258 ? 21.669  7.237   36.646  1.00 46.10  ? 258 LEU A CD1 1 
ATOM 1901 C CD2 . LEU A 1 258 ? 21.978  7.872   34.268  1.00 54.04  ? 258 LEU A CD2 1 
ATOM 1902 N N   . PRO A 1 259 ? 26.434  8.429   36.709  1.00 55.16  ? 259 PRO A N   1 
ATOM 1903 C CA  . PRO A 1 259 ? 27.629  7.571   36.766  1.00 57.23  ? 259 PRO A CA  1 
ATOM 1904 C C   . PRO A 1 259 ? 28.109  7.289   38.176  1.00 55.67  ? 259 PRO A C   1 
ATOM 1905 O O   . PRO A 1 259 ? 28.642  6.202   38.422  1.00 68.61  ? 259 PRO A O   1 
ATOM 1906 C CB  . PRO A 1 259 ? 28.681  8.358   35.971  1.00 58.14  ? 259 PRO A CB  1 
ATOM 1907 C CG  . PRO A 1 259 ? 27.945  9.367   35.206  1.00 54.44  ? 259 PRO A CG  1 
ATOM 1908 C CD  . PRO A 1 259 ? 26.659  9.639   35.900  1.00 55.73  ? 259 PRO A CD  1 
ATOM 1909 N N   . GLU A 1 260 ? 27.947  8.230   39.106  1.00 54.20  ? 260 GLU A N   1 
ATOM 1910 C CA  . GLU A 1 260 ? 28.422  8.023   40.468  1.00 54.63  ? 260 GLU A CA  1 
ATOM 1911 C C   . GLU A 1 260 ? 27.591  6.973   41.196  1.00 54.69  ? 260 GLU A C   1 
ATOM 1912 O O   . GLU A 1 260 ? 28.130  6.162   41.956  1.00 63.93  ? 260 GLU A O   1 
ATOM 1913 C CB  . GLU A 1 260 ? 28.404  9.345   41.234  1.00 56.67  ? 260 GLU A CB  1 
ATOM 1914 C CG  . GLU A 1 260 ? 28.765  9.217   42.702  1.00 61.63  ? 260 GLU A CG  1 
ATOM 1915 C CD  . GLU A 1 260 ? 28.693  10.539  43.436  1.00 70.79  ? 260 GLU A CD  1 
ATOM 1916 O OE1 . GLU A 1 260 ? 27.607  11.156  43.447  1.00 67.40  ? 260 GLU A OE1 1 
ATOM 1917 O OE2 . GLU A 1 260 ? 29.722  10.963  44.002  1.00 72.60  ? 260 GLU A OE2 1 
ATOM 1918 N N   . GLN A 1 261 ? 26.280  6.970   40.971  1.00 51.23  ? 261 GLN A N   1 
ATOM 1919 C CA  . GLN A 1 261 ? 25.378  6.114   41.727  1.00 45.51  ? 261 GLN A CA  1 
ATOM 1920 C C   . GLN A 1 261 ? 25.020  4.822   41.008  1.00 45.77  ? 261 GLN A C   1 
ATOM 1921 O O   . GLN A 1 261 ? 24.530  3.889   41.653  1.00 56.29  ? 261 GLN A O   1 
ATOM 1922 C CB  . GLN A 1 261 ? 24.095  6.877   42.062  1.00 46.99  ? 261 GLN A CB  1 
ATOM 1923 C CG  . GLN A 1 261 ? 24.341  8.279   42.571  1.00 45.95  ? 261 GLN A CG  1 
ATOM 1924 C CD  . GLN A 1 261 ? 24.785  8.300   44.013  1.00 51.80  ? 261 GLN A CD  1 
ATOM 1925 O OE1 . GLN A 1 261 ? 24.380  7.457   44.806  1.00 53.86  ? 261 GLN A OE1 1 
ATOM 1926 N NE2 . GLN A 1 261 ? 25.629  9.261   44.361  1.00 58.88  ? 261 GLN A NE2 1 
ATOM 1927 N N   . SER A 1 262 ? 25.245  4.738   39.698  1.00 52.36  ? 262 SER A N   1 
ATOM 1928 C CA  . SER A 1 262 ? 24.924  3.539   38.942  1.00 57.44  ? 262 SER A CA  1 
ATOM 1929 C C   . SER A 1 262 ? 26.099  2.953   38.180  1.00 58.54  ? 262 SER A C   1 
ATOM 1930 O O   . SER A 1 262 ? 26.014  1.799   37.749  1.00 58.52  ? 262 SER A O   1 
ATOM 1931 C CB  . SER A 1 262 ? 23.790  3.823   37.943  1.00 52.56  ? 262 SER A CB  1 
ATOM 1932 O OG  . SER A 1 262 ? 24.195  4.774   36.976  1.00 64.03  ? 262 SER A OG  1 
ATOM 1933 N N   . GLY A 1 263 ? 27.184  3.700   38.004  1.00 54.51  ? 263 GLY A N   1 
ATOM 1934 C CA  . GLY A 1 263 ? 28.299  3.240   37.208  1.00 54.94  ? 263 GLY A CA  1 
ATOM 1935 C C   . GLY A 1 263 ? 28.118  3.401   35.718  1.00 60.88  ? 263 GLY A C   1 
ATOM 1936 O O   . GLY A 1 263 ? 29.034  3.061   34.960  1.00 63.56  ? 263 GLY A O   1 
ATOM 1937 N N   . CYS A 1 264 ? 26.974  3.913   35.276  1.00 59.80  ? 264 CYS A N   1 
ATOM 1938 C CA  . CYS A 1 264 ? 26.716  4.116   33.858  1.00 59.96  ? 264 CYS A CA  1 
ATOM 1939 C C   . CYS A 1 264 ? 27.236  5.485   33.442  1.00 66.27  ? 264 CYS A C   1 
ATOM 1940 O O   . CYS A 1 264 ? 26.719  6.513   33.891  1.00 74.28  ? 264 CYS A O   1 
ATOM 1941 C CB  . CYS A 1 264 ? 25.221  3.991   33.572  1.00 55.32  ? 264 CYS A CB  1 
ATOM 1942 S SG  . CYS A 1 264 ? 24.771  4.128   31.830  1.00 73.30  ? 264 CYS A SG  1 
ATOM 1943 N N   . SER A 1 265 ? 28.259  5.497   32.590  1.00 62.58  ? 265 SER A N   1 
ATOM 1944 C CA  . SER A 1 265 ? 28.840  6.744   32.107  1.00 57.36  ? 265 SER A CA  1 
ATOM 1945 C C   . SER A 1 265 ? 27.790  7.521   31.326  1.00 60.06  ? 265 SER A C   1 
ATOM 1946 O O   . SER A 1 265 ? 27.061  6.945   30.513  1.00 59.94  ? 265 SER A O   1 
ATOM 1947 C CB  . SER A 1 265 ? 30.062  6.462   31.238  1.00 58.01  ? 265 SER A CB  1 
ATOM 1948 O OG  . SER A 1 265 ? 30.882  5.466   31.822  1.00 70.14  ? 265 SER A OG  1 
ATOM 1949 N N   . VAL A 1 266 ? 27.705  8.824   31.577  1.00 60.07  ? 266 VAL A N   1 
ATOM 1950 C CA  . VAL A 1 266 ? 26.706  9.686   30.959  1.00 61.10  ? 266 VAL A CA  1 
ATOM 1951 C C   . VAL A 1 266 ? 27.411  10.844  30.272  1.00 59.75  ? 266 VAL A C   1 
ATOM 1952 O O   . VAL A 1 266 ? 28.183  11.574  30.904  1.00 63.54  ? 266 VAL A O   1 
ATOM 1953 C CB  . VAL A 1 266 ? 25.689  10.202  31.993  1.00 60.53  ? 266 VAL A CB  1 
ATOM 1954 C CG1 . VAL A 1 266 ? 24.663  11.095  31.322  1.00 56.73  ? 266 VAL A CG1 1 
ATOM 1955 C CG2 . VAL A 1 266 ? 25.010  9.041   32.688  1.00 58.09  ? 266 VAL A CG2 1 
ATOM 1956 N N   . THR A 1 267 ? 27.145  11.009  28.981  1.00 61.64  ? 267 THR A N   1 
ATOM 1957 C CA  . THR A 1 267 ? 27.572  12.174  28.222  1.00 58.71  ? 267 THR A CA  1 
ATOM 1958 C C   . THR A 1 267 ? 26.335  12.874  27.686  1.00 63.43  ? 267 THR A C   1 
ATOM 1959 O O   . THR A 1 267 ? 25.428  12.228  27.153  1.00 70.49  ? 267 THR A O   1 
ATOM 1960 C CB  . THR A 1 267 ? 28.504  11.791  27.069  1.00 60.67  ? 267 THR A CB  1 
ATOM 1961 O OG1 . THR A 1 267 ? 27.886  10.778  26.268  1.00 67.60  ? 267 THR A OG1 1 
ATOM 1962 C CG2 . THR A 1 267 ? 29.827  11.273  27.605  1.00 60.35  ? 267 THR A CG2 1 
ATOM 1963 N N   . GLY A 1 268 ? 26.294  14.193  27.831  1.00 64.25  ? 268 GLY A N   1 
ATOM 1964 C CA  . GLY A 1 268 ? 25.092  14.921  27.483  1.00 61.52  ? 268 GLY A CA  1 
ATOM 1965 C C   . GLY A 1 268 ? 25.255  15.966  26.403  1.00 61.22  ? 268 GLY A C   1 
ATOM 1966 O O   . GLY A 1 268 ? 26.326  16.559  26.248  1.00 64.33  ? 268 GLY A O   1 
ATOM 1967 N N   . VAL A 1 269 ? 24.184  16.196  25.651  1.00 62.73  ? 269 VAL A N   1 
ATOM 1968 C CA  . VAL A 1 269 ? 24.120  17.257  24.656  1.00 66.28  ? 269 VAL A CA  1 
ATOM 1969 C C   . VAL A 1 269 ? 23.046  18.239  25.094  1.00 67.72  ? 269 VAL A C   1 
ATOM 1970 O O   . VAL A 1 269 ? 21.901  17.843  25.339  1.00 70.11  ? 269 VAL A O   1 
ATOM 1971 C CB  . VAL A 1 269 ? 23.818  16.712  23.248  1.00 64.84  ? 269 VAL A CB  1 
ATOM 1972 C CG1 . VAL A 1 269 ? 23.565  17.856  22.283  1.00 63.73  ? 269 VAL A CG1 1 
ATOM 1973 C CG2 . VAL A 1 269 ? 24.968  15.850  22.760  1.00 64.33  ? 269 VAL A CG2 1 
ATOM 1974 N N   . TYR A 1 270 ? 23.413  19.511  25.192  1.00 66.50  ? 270 TYR A N   1 
ATOM 1975 C CA  . TYR A 1 270 ? 22.504  20.547  25.657  1.00 55.67  ? 270 TYR A CA  1 
ATOM 1976 C C   . TYR A 1 270 ? 21.742  21.149  24.485  1.00 65.82  ? 270 TYR A C   1 
ATOM 1977 O O   . TYR A 1 270 ? 22.342  21.723  23.572  1.00 73.38  ? 270 TYR A O   1 
ATOM 1978 C CB  . TYR A 1 270 ? 23.273  21.642  26.394  1.00 64.21  ? 270 TYR A CB  1 
ATOM 1979 C CG  . TYR A 1 270 ? 23.670  21.282  27.803  1.00 65.48  ? 270 TYR A CG  1 
ATOM 1980 C CD1 . TYR A 1 270 ? 22.793  21.478  28.860  1.00 62.71  ? 270 TYR A CD1 1 
ATOM 1981 C CD2 . TYR A 1 270 ? 24.918  20.744  28.078  1.00 66.48  ? 270 TYR A CD2 1 
ATOM 1982 C CE1 . TYR A 1 270 ? 23.153  21.158  30.149  1.00 60.58  ? 270 TYR A CE1 1 
ATOM 1983 C CE2 . TYR A 1 270 ? 25.284  20.416  29.365  1.00 64.68  ? 270 TYR A CE2 1 
ATOM 1984 C CZ  . TYR A 1 270 ? 24.398  20.625  30.397  1.00 64.90  ? 270 TYR A CZ  1 
ATOM 1985 O OH  . TYR A 1 270 ? 24.757  20.301  31.683  1.00 69.24  ? 270 TYR A OH  1 
ATOM 1986 N N   . ARG A 1 271 ? 20.423  21.015  24.520  1.00 61.09  ? 271 ARG A N   1 
ATOM 1987 C CA  . ARG A 1 271 ? 19.521  21.677  23.588  1.00 62.02  ? 271 ARG A CA  1 
ATOM 1988 C C   . ARG A 1 271 ? 18.456  22.450  24.351  1.00 61.22  ? 271 ARG A C   1 
ATOM 1989 O O   . ARG A 1 271 ? 17.260  22.326  24.087  1.00 69.66  ? 271 ARG A O   1 
ATOM 1990 C CB  . ARG A 1 271 ? 18.886  20.678  22.627  1.00 58.06  ? 271 ARG A CB  1 
ATOM 1991 C CG  . ARG A 1 271 ? 19.864  20.048  21.659  1.00 60.21  ? 271 ARG A CG  1 
ATOM 1992 C CD  . ARG A 1 271 ? 19.222  19.822  20.306  1.00 62.61  ? 271 ARG A CD  1 
ATOM 1993 N NE  . ARG A 1 271 ? 20.216  19.742  19.243  1.00 66.46  ? 271 ARG A NE  1 
ATOM 1994 C CZ  . ARG A 1 271 ? 20.122  18.942  18.191  1.00 63.43  ? 271 ARG A CZ  1 
ATOM 1995 N NH1 . ARG A 1 271 ? 19.079  18.149  18.017  1.00 65.59  ? 271 ARG A NH1 1 
ATOM 1996 N NH2 . ARG A 1 271 ? 21.098  18.941  17.288  1.00 66.34  ? 271 ARG A NH2 1 
ATOM 1997 N N   . ALA A 1 272 ? 18.887  23.239  25.328  1.00 56.51  ? 272 ALA A N   1 
ATOM 1998 C CA  . ALA A 1 272 ? 17.990  24.007  26.176  1.00 56.64  ? 272 ALA A CA  1 
ATOM 1999 C C   . ALA A 1 272 ? 18.360  25.480  26.121  1.00 60.18  ? 272 ALA A C   1 
ATOM 2000 O O   . ALA A 1 272 ? 19.503  25.851  26.406  1.00 68.11  ? 272 ALA A O   1 
ATOM 2001 C CB  . ALA A 1 272 ? 18.043  23.501  27.617  1.00 62.28  ? 272 ALA A CB  1 
ATOM 2002 N N   . ILE A 1 273 ? 17.392  26.315  25.755  1.00 58.36  ? 273 ILE A N   1 
ATOM 2003 C CA  . ILE A 1 273 ? 17.559  27.762  25.707  1.00 55.49  ? 273 ILE A CA  1 
ATOM 2004 C C   . ILE A 1 273 ? 16.454  28.397  26.535  1.00 55.46  ? 273 ILE A C   1 
ATOM 2005 O O   . ILE A 1 273 ? 15.287  28.006  26.434  1.00 69.42  ? 273 ILE A O   1 
ATOM 2006 C CB  . ILE A 1 273 ? 17.536  28.297  24.260  1.00 57.34  ? 273 ILE A CB  1 
ATOM 2007 C CG1 . ILE A 1 273 ? 18.629  27.629  23.428  1.00 57.20  ? 273 ILE A CG1 1 
ATOM 2008 C CG2 . ILE A 1 273 ? 17.714  29.803  24.245  1.00 58.49  ? 273 ILE A CG2 1 
ATOM 2009 C CD1 . ILE A 1 273 ? 18.722  28.151  22.016  1.00 58.09  ? 273 ILE A CD1 1 
ATOM 2010 N N   . SER A 1 274 ? 16.827  29.371  27.360  1.00 52.21  ? 274 SER A N   1 
ATOM 2011 C CA  . SER A 1 274 ? 15.861  30.038  28.220  1.00 50.72  ? 274 SER A CA  1 
ATOM 2012 C C   . SER A 1 274 ? 14.809  30.757  27.386  1.00 59.01  ? 274 SER A C   1 
ATOM 2013 O O   . SER A 1 274 ? 15.130  31.413  26.391  1.00 69.84  ? 274 SER A O   1 
ATOM 2014 C CB  . SER A 1 274 ? 16.572  31.025  29.142  1.00 60.04  ? 274 SER A CB  1 
ATOM 2015 O OG  . SER A 1 274 ? 17.386  30.345  30.080  1.00 65.40  ? 274 SER A OG  1 
ATOM 2016 N N   . GLY A 1 275 ? 13.553  30.629  27.793  1.00 65.37  ? 275 GLY A N   1 
ATOM 2017 C CA  . GLY A 1 275 ? 12.450  31.254  27.097  1.00 66.84  ? 275 GLY A CA  1 
ATOM 2018 C C   . GLY A 1 275 ? 11.951  30.519  25.876  1.00 65.47  ? 275 GLY A C   1 
ATOM 2019 O O   . GLY A 1 275 ? 11.069  31.038  25.183  1.00 72.77  ? 275 GLY A O   1 
ATOM 2020 N N   . HIS A 1 276 ? 12.474  29.330  25.592  1.00 67.19  ? 276 HIS A N   1 
ATOM 2021 C CA  . HIS A 1 276 ? 12.115  28.617  24.375  1.00 69.98  ? 276 HIS A CA  1 
ATOM 2022 C C   . HIS A 1 276 ? 10.861  27.779  24.577  1.00 71.25  ? 276 HIS A C   1 
ATOM 2023 O O   . HIS A 1 276 ? 10.616  27.254  25.667  1.00 76.59  ? 276 HIS A O   1 
ATOM 2024 C CB  . HIS A 1 276 ? 13.268  27.730  23.913  1.00 64.77  ? 276 HIS A CB  1 
ATOM 2025 C CG  . HIS A 1 276 ? 14.123  28.360  22.861  1.00 66.61  ? 276 HIS A CG  1 
ATOM 2026 N ND1 . HIS A 1 276 ? 14.515  29.680  22.915  1.00 69.91  ? 276 HIS A ND1 1 
ATOM 2027 C CD2 . HIS A 1 276 ? 14.674  27.848  21.737  1.00 64.71  ? 276 HIS A CD2 1 
ATOM 2028 C CE1 . HIS A 1 276 ? 15.264  29.956  21.862  1.00 74.53  ? 276 HIS A CE1 1 
ATOM 2029 N NE2 . HIS A 1 276 ? 15.376  28.862  21.131  1.00 75.26  ? 276 HIS A NE2 1 
ATOM 2030 N N   . THR A 1 277 ? 10.072  27.661  23.518  1.00 66.81  ? 277 THR A N   1 
ATOM 2031 C CA  . THR A 1 277 ? 8.854   26.869  23.516  1.00 66.61  ? 277 THR A CA  1 
ATOM 2032 C C   . THR A 1 277 ? 9.025   25.641  22.626  1.00 65.65  ? 277 THR A C   1 
ATOM 2033 O O   . THR A 1 277 ? 10.072  25.423  22.015  1.00 68.87  ? 277 THR A O   1 
ATOM 2034 C CB  . THR A 1 277 ? 7.678   27.717  23.039  1.00 65.65  ? 277 THR A CB  1 
ATOM 2035 O OG1 . THR A 1 277 ? 8.020   28.339  21.797  1.00 71.87  ? 277 THR A OG1 1 
ATOM 2036 C CG2 . THR A 1 277 ? 7.366   28.796  24.054  1.00 63.57  ? 277 THR A CG2 1 
ATOM 2037 N N   . ALA A 1 278 ? 7.970   24.826  22.561  1.00 72.04  ? 278 ALA A N   1 
ATOM 2038 C CA  . ALA A 1 278 ? 8.002   23.652  21.695  1.00 68.52  ? 278 ALA A CA  1 
ATOM 2039 C C   . ALA A 1 278 ? 8.113   24.043  20.228  1.00 72.78  ? 278 ALA A C   1 
ATOM 2040 O O   . ALA A 1 278 ? 8.865   23.416  19.474  1.00 76.88  ? 278 ALA A O   1 
ATOM 2041 C CB  . ALA A 1 278 ? 6.760   22.792  21.923  1.00 63.18  ? 278 ALA A CB  1 
ATOM 2042 N N   . ILE A 1 279 ? 7.374   25.071  19.807  1.00 73.79  ? 279 ILE A N   1 
ATOM 2043 C CA  . ILE A 1 279 ? 7.462   25.545  18.430  1.00 68.49  ? 279 ILE A CA  1 
ATOM 2044 C C   . ILE A 1 279 ? 8.859   26.073  18.129  1.00 70.68  ? 279 ILE A C   1 
ATOM 2045 O O   . ILE A 1 279 ? 9.427   25.782  17.071  1.00 75.97  ? 279 ILE A O   1 
ATOM 2046 C CB  . ILE A 1 279 ? 6.373   26.607  18.173  1.00 72.24  ? 279 ILE A CB  1 
ATOM 2047 C CG1 . ILE A 1 279 ? 6.593   27.314  16.836  1.00 72.56  ? 279 ILE A CG1 1 
ATOM 2048 C CG2 . ILE A 1 279 ? 6.316   27.614  19.300  1.00 75.41  ? 279 ILE A CG2 1 
ATOM 2049 C CD1 . ILE A 1 279 ? 6.494   26.411  15.648  1.00 74.24  ? 279 ILE A CD1 1 
ATOM 2050 N N   . GLN A 1 280 ? 9.440   26.845  19.050  1.00 66.84  ? 280 GLN A N   1 
ATOM 2051 C CA  . GLN A 1 280 ? 10.794  27.347  18.847  1.00 64.69  ? 280 GLN A CA  1 
ATOM 2052 C C   . GLN A 1 280 ? 11.813  26.215  18.869  1.00 69.56  ? 280 GLN A C   1 
ATOM 2053 O O   . GLN A 1 280 ? 12.771  26.220  18.086  1.00 80.87  ? 280 GLN A O   1 
ATOM 2054 C CB  . GLN A 1 280 ? 11.131  28.392  19.908  1.00 67.31  ? 280 GLN A CB  1 
ATOM 2055 C CG  . GLN A 1 280 ? 10.340  29.680  19.787  1.00 67.45  ? 280 GLN A CG  1 
ATOM 2056 C CD  . GLN A 1 280 ? 10.695  30.678  20.868  1.00 72.72  ? 280 GLN A CD  1 
ATOM 2057 O OE1 . GLN A 1 280 ? 11.567  30.427  21.697  1.00 75.69  ? 280 GLN A OE1 1 
ATOM 2058 N NE2 . GLN A 1 280 ? 10.021  31.821  20.864  1.00 75.95  ? 280 GLN A NE2 1 
ATOM 2059 N N   . SER A 1 281 ? 11.631  25.242  19.764  1.00 66.55  ? 281 SER A N   1 
ATOM 2060 C CA  . SER A 1 281 ? 12.581  24.139  19.863  1.00 63.06  ? 281 SER A CA  1 
ATOM 2061 C C   . SER A 1 281 ? 12.558  23.271  18.612  1.00 63.85  ? 281 SER A C   1 
ATOM 2062 O O   . SER A 1 281 ? 13.606  22.803  18.154  1.00 61.95  ? 281 SER A O   1 
ATOM 2063 C CB  . SER A 1 281 ? 12.278  23.299  21.103  1.00 65.78  ? 281 SER A CB  1 
ATOM 2064 O OG  . SER A 1 281 ? 12.383  24.078  22.280  1.00 72.46  ? 281 SER A OG  1 
ATOM 2065 N N   . TYR A 1 282 ? 11.371  23.036  18.053  1.00 69.97  ? 282 TYR A N   1 
ATOM 2066 C CA  . TYR A 1 282 ? 11.266  22.203  16.861  1.00 65.63  ? 282 TYR A CA  1 
ATOM 2067 C C   . TYR A 1 282 ? 11.888  22.877  15.644  1.00 70.03  ? 282 TYR A C   1 
ATOM 2068 O O   . TYR A 1 282 ? 12.505  22.207  14.810  1.00 75.15  ? 282 TYR A O   1 
ATOM 2069 C CB  . TYR A 1 282 ? 9.803   21.859  16.586  1.00 65.98  ? 282 TYR A CB  1 
ATOM 2070 C CG  . TYR A 1 282 ? 9.615   20.852  15.478  1.00 71.33  ? 282 TYR A CG  1 
ATOM 2071 C CD1 . TYR A 1 282 ? 9.883   19.507  15.686  1.00 70.09  ? 282 TYR A CD1 1 
ATOM 2072 C CD2 . TYR A 1 282 ? 9.172   21.245  14.223  1.00 72.12  ? 282 TYR A CD2 1 
ATOM 2073 C CE1 . TYR A 1 282 ? 9.716   18.582  14.678  1.00 69.74  ? 282 TYR A CE1 1 
ATOM 2074 C CE2 . TYR A 1 282 ? 9.001   20.326  13.208  1.00 71.06  ? 282 TYR A CE2 1 
ATOM 2075 C CZ  . TYR A 1 282 ? 9.274   18.996  13.441  1.00 72.00  ? 282 TYR A CZ  1 
ATOM 2076 O OH  . TYR A 1 282 ? 9.105   18.075  12.434  1.00 77.01  ? 282 TYR A OH  1 
ATOM 2077 N N   . ASN A 1 283 ? 11.739  24.195  15.528  1.00 70.62  ? 283 ASN A N   1 
ATOM 2078 C CA  . ASN A 1 283 ? 12.241  24.937  14.380  1.00 66.82  ? 283 ASN A CA  1 
ATOM 2079 C C   . ASN A 1 283 ? 13.527  25.693  14.678  1.00 68.29  ? 283 ASN A C   1 
ATOM 2080 O O   . ASN A 1 283 ? 13.847  26.650  13.967  1.00 77.38  ? 283 ASN A O   1 
ATOM 2081 C CB  . ASN A 1 283 ? 11.175  25.905  13.868  1.00 66.49  ? 283 ASN A CB  1 
ATOM 2082 C CG  . ASN A 1 283 ? 9.998   25.192  13.244  1.00 71.53  ? 283 ASN A CG  1 
ATOM 2083 O OD1 . ASN A 1 283 ? 10.168  24.246  12.476  1.00 77.42  ? 283 ASN A OD1 1 
ATOM 2084 N ND2 . ASN A 1 283 ? 8.796   25.647  13.561  1.00 68.96  ? 283 ASN A ND2 1 
ATOM 2085 N N   . GLU A 1 284 ? 14.266  25.297  15.703  1.00 69.08  ? 284 GLU A N   1 
ATOM 2086 C CA  . GLU A 1 284 ? 15.551  25.927  15.971  1.00 72.73  ? 284 GLU A CA  1 
ATOM 2087 C C   . GLU A 1 284 ? 16.545  25.556  14.877  1.00 78.91  ? 284 GLU A C   1 
ATOM 2088 O O   . GLU A 1 284 ? 16.719  24.369  14.584  1.00 77.87  ? 284 GLU A O   1 
ATOM 2089 C CB  . GLU A 1 284 ? 16.084  25.507  17.336  1.00 70.01  ? 284 GLU A CB  1 
ATOM 2090 C CG  . GLU A 1 284 ? 17.460  26.060  17.664  1.00 72.71  ? 284 GLU A CG  1 
ATOM 2091 C CD  . GLU A 1 284 ? 17.415  27.505  18.110  1.00 78.34  ? 284 GLU A CD  1 
ATOM 2092 O OE1 . GLU A 1 284 ? 16.304  28.038  18.296  1.00 75.93  ? 284 GLU A OE1 1 
ATOM 2093 O OE2 . GLU A 1 284 ? 18.495  28.112  18.273  1.00 81.32  ? 284 GLU A OE2 1 
ATOM 2094 N N   . PRO A 1 285 ? 17.199  26.535  14.246  1.00 81.72  ? 285 PRO A N   1 
ATOM 2095 C CA  . PRO A 1 285 ? 18.088  26.212  13.115  1.00 80.97  ? 285 PRO A CA  1 
ATOM 2096 C C   . PRO A 1 285 ? 19.235  25.287  13.480  1.00 81.06  ? 285 PRO A C   1 
ATOM 2097 O O   . PRO A 1 285 ? 19.625  24.449  12.658  1.00 80.32  ? 285 PRO A O   1 
ATOM 2098 C CB  . PRO A 1 285 ? 18.605  27.583  12.651  1.00 80.21  ? 285 PRO A CB  1 
ATOM 2099 C CG  . PRO A 1 285 ? 17.934  28.610  13.479  1.00 78.75  ? 285 PRO A CG  1 
ATOM 2100 C CD  . PRO A 1 285 ? 17.156  27.970  14.571  1.00 77.66  ? 285 PRO A CD  1 
ATOM 2101 N N   . SER A 1 286 ? 19.785  25.407  14.685  1.00 72.85  ? 286 SER A N   1 
ATOM 2102 C CA  . SER A 1 286 ? 20.917  24.586  15.091  1.00 76.59  ? 286 SER A CA  1 
ATOM 2103 C C   . SER A 1 286 ? 20.506  23.246  15.684  1.00 81.46  ? 286 SER A C   1 
ATOM 2104 O O   . SER A 1 286 ? 21.378  22.417  15.960  1.00 77.68  ? 286 SER A O   1 
ATOM 2105 C CB  . SER A 1 286 ? 21.783  25.347  16.101  1.00 74.50  ? 286 SER A CB  1 
ATOM 2106 O OG  . SER A 1 286 ? 21.101  25.518  17.331  1.00 78.24  ? 286 SER A OG  1 
ATOM 2107 N N   . TRP A 1 287 ? 19.211  23.013  15.884  1.00 70.46  ? 287 TRP A N   1 
ATOM 2108 C CA  . TRP A 1 287 ? 18.723  21.778  16.479  1.00 67.14  ? 287 TRP A CA  1 
ATOM 2109 C C   . TRP A 1 287 ? 18.091  20.842  15.459  1.00 70.77  ? 287 TRP A C   1 
ATOM 2110 O O   . TRP A 1 287 ? 17.479  19.844  15.847  1.00 77.61  ? 287 TRP A O   1 
ATOM 2111 C CB  . TRP A 1 287 ? 17.718  22.089  17.588  1.00 66.18  ? 287 TRP A CB  1 
ATOM 2112 C CG  . TRP A 1 287 ? 18.324  22.798  18.751  1.00 65.45  ? 287 TRP A CG  1 
ATOM 2113 C CD1 . TRP A 1 287 ? 19.650  23.013  18.979  1.00 59.77  ? 287 TRP A CD1 1 
ATOM 2114 C CD2 . TRP A 1 287 ? 17.626  23.393  19.848  1.00 66.55  ? 287 TRP A CD2 1 
ATOM 2115 N NE1 . TRP A 1 287 ? 19.822  23.705  20.151  1.00 58.39  ? 287 TRP A NE1 1 
ATOM 2116 C CE2 . TRP A 1 287 ? 18.593  23.950  20.704  1.00 62.49  ? 287 TRP A CE2 1 
ATOM 2117 C CE3 . TRP A 1 287 ? 16.276  23.508  20.190  1.00 65.56  ? 287 TRP A CE3 1 
ATOM 2118 C CZ2 . TRP A 1 287 ? 18.254  24.611  21.877  1.00 62.03  ? 287 TRP A CZ2 1 
ATOM 2119 C CZ3 . TRP A 1 287 ? 15.942  24.166  21.355  1.00 65.29  ? 287 TRP A CZ3 1 
ATOM 2120 C CH2 . TRP A 1 287 ? 16.926  24.709  22.184  1.00 64.90  ? 287 TRP A CH2 1 
ATOM 2121 N N   . GLN A 1 288 ? 18.218  21.141  14.170  1.00 74.78  ? 288 GLN A N   1 
ATOM 2122 C CA  . GLN A 1 288 ? 17.663  20.283  13.134  1.00 73.63  ? 288 GLN A CA  1 
ATOM 2123 C C   . GLN A 1 288 ? 18.526  19.063  12.850  1.00 71.28  ? 288 GLN A C   1 
ATOM 2124 O O   . GLN A 1 288 ? 18.071  18.151  12.154  1.00 71.22  ? 288 GLN A O   1 
ATOM 2125 C CB  . GLN A 1 288 ? 17.456  21.083  11.847  1.00 71.32  ? 288 GLN A CB  1 
ATOM 2126 C CG  . GLN A 1 288 ? 16.642  22.343  12.046  1.00 72.02  ? 288 GLN A CG  1 
ATOM 2127 C CD  . GLN A 1 288 ? 15.187  22.048  12.335  1.00 75.14  ? 288 GLN A CD  1 
ATOM 2128 O OE1 . GLN A 1 288 ? 14.638  21.052  11.867  1.00 77.50  ? 288 GLN A OE1 1 
ATOM 2129 N NE2 . GLN A 1 288 ? 14.556  22.910  13.120  1.00 74.77  ? 288 GLN A NE2 1 
ATOM 2130 N N   . SER A 1 289 ? 19.749  19.026  13.366  1.00 69.24  ? 289 SER A N   1 
ATOM 2131 C CA  . SER A 1 289 ? 20.637  17.895  13.165  1.00 71.77  ? 289 SER A CA  1 
ATOM 2132 C C   . SER A 1 289 ? 20.480  16.882  14.297  1.00 75.61  ? 289 SER A C   1 
ATOM 2133 O O   . SER A 1 289 ? 20.077  17.212  15.415  1.00 78.50  ? 289 SER A O   1 
ATOM 2134 C CB  . SER A 1 289 ? 22.087  18.366  13.067  1.00 74.27  ? 289 SER A CB  1 
ATOM 2135 O OG  . SER A 1 289 ? 22.472  19.073  14.233  1.00 74.90  ? 289 SER A OG  1 
ATOM 2136 N N   . ASN A 1 290 ? 20.804  15.637  13.992  1.00 74.99  ? 290 ASN A N   1 
ATOM 2137 C CA  . ASN A 1 290 ? 20.753  14.562  14.975  1.00 71.39  ? 290 ASN A CA  1 
ATOM 2138 C C   . ASN A 1 290 ? 21.917  14.703  15.948  1.00 77.04  ? 290 ASN A C   1 
ATOM 2139 O O   . ASN A 1 290 ? 23.076  14.680  15.520  1.00 77.60  ? 290 ASN A O   1 
ATOM 2140 C CB  . ASN A 1 290 ? 20.813  13.207  14.280  1.00 72.43  ? 290 ASN A CB  1 
ATOM 2141 C CG  . ASN A 1 290 ? 20.557  12.044  15.222  1.00 74.75  ? 290 ASN A CG  1 
ATOM 2142 O OD1 . ASN A 1 290 ? 20.397  12.221  16.427  1.00 78.56  ? 290 ASN A OD1 1 
ATOM 2143 N ND2 . ASN A 1 290 ? 20.516  10.840  14.667  1.00 74.38  ? 290 ASN A ND2 1 
ATOM 2144 N N   . PRO A 1 291 ? 21.658  14.850  17.246  1.00 75.37  ? 291 PRO A N   1 
ATOM 2145 C CA  . PRO A 1 291 ? 22.750  14.937  18.227  1.00 70.02  ? 291 PRO A CA  1 
ATOM 2146 C C   . PRO A 1 291 ? 23.415  13.609  18.560  1.00 71.69  ? 291 PRO A C   1 
ATOM 2147 O O   . PRO A 1 291 ? 24.361  13.605  19.354  1.00 73.90  ? 291 PRO A O   1 
ATOM 2148 C CB  . PRO A 1 291 ? 22.045  15.505  19.469  1.00 69.93  ? 291 PRO A CB  1 
ATOM 2149 C CG  . PRO A 1 291 ? 20.619  15.158  19.315  1.00 68.63  ? 291 PRO A CG  1 
ATOM 2150 C CD  . PRO A 1 291 ? 20.328  14.979  17.861  1.00 70.25  ? 291 PRO A CD  1 
ATOM 2151 N N   . ASN A 1 292 ? 22.946  12.503  17.980  1.00 77.29  ? 292 ASN A N   1 
ATOM 2152 C CA  . ASN A 1 292 ? 23.562  11.188  18.149  1.00 78.03  ? 292 ASN A CA  1 
ATOM 2153 C C   . ASN A 1 292 ? 23.608  10.782  19.621  1.00 77.85  ? 292 ASN A C   1 
ATOM 2154 O O   . ASN A 1 292 ? 24.650  10.396  20.155  1.00 79.39  ? 292 ASN A O   1 
ATOM 2155 C CB  . ASN A 1 292 ? 24.957  11.155  17.521  1.00 75.30  ? 292 ASN A CB  1 
ATOM 2156 C CG  . ASN A 1 292 ? 24.933  11.479  16.041  1.00 77.84  ? 292 ASN A CG  1 
ATOM 2157 O OD1 . ASN A 1 292 ? 24.000  11.110  15.330  1.00 75.35  ? 292 ASN A OD1 1 
ATOM 2158 N ND2 . ASN A 1 292 ? 25.959  12.177  15.572  1.00 81.40  ? 292 ASN A ND2 1 
ATOM 2159 N N   . CYS A 1 293 ? 22.457  10.873  20.278  1.00 70.21  ? 293 CYS A N   1 
ATOM 2160 C CA  . CYS A 1 293 ? 22.312  10.482  21.670  1.00 68.87  ? 293 CYS A CA  1 
ATOM 2161 C C   . CYS A 1 293 ? 21.501  9.199   21.759  1.00 73.22  ? 293 CYS A C   1 
ATOM 2162 O O   . CYS A 1 293 ? 21.079  8.632   20.749  1.00 78.12  ? 293 CYS A O   1 
ATOM 2163 C CB  . CYS A 1 293 ? 21.643  11.589  22.494  1.00 67.31  ? 293 CYS A CB  1 
ATOM 2164 S SG  . CYS A 1 293 ? 22.605  13.110  22.613  1.00 72.71  ? 293 CYS A SG  1 
ATOM 2165 N N   . ASP A 1 294 ? 21.290  8.739   22.991  1.00 65.30  ? 294 ASP A N   1 
ATOM 2166 C CA  . ASP A 1 294 ? 20.505  7.537   23.238  1.00 58.22  ? 294 ASP A CA  1 
ATOM 2167 C C   . ASP A 1 294 ? 19.154  7.824   23.869  1.00 61.21  ? 294 ASP A C   1 
ATOM 2168 O O   . ASP A 1 294 ? 18.178  7.139   23.554  1.00 63.17  ? 294 ASP A O   1 
ATOM 2169 C CB  . ASP A 1 294 ? 21.280  6.570   24.138  1.00 60.45  ? 294 ASP A CB  1 
ATOM 2170 C CG  . ASP A 1 294 ? 22.658  6.252   23.602  1.00 67.27  ? 294 ASP A CG  1 
ATOM 2171 O OD1 . ASP A 1 294 ? 22.766  5.908   22.408  1.00 68.80  ? 294 ASP A OD1 1 
ATOM 2172 O OD2 . ASP A 1 294 ? 23.635  6.347   24.373  1.00 69.03  ? 294 ASP A OD2 1 
ATOM 2173 N N   . VAL A 1 295 ? 19.076  8.810   24.755  1.00 61.48  ? 295 VAL A N   1 
ATOM 2174 C CA  . VAL A 1 295 ? 17.831  9.172   25.419  1.00 53.66  ? 295 VAL A CA  1 
ATOM 2175 C C   . VAL A 1 295 ? 17.716  10.690  25.449  1.00 55.85  ? 295 VAL A C   1 
ATOM 2176 O O   . VAL A 1 295 ? 18.698  11.394  25.702  1.00 59.86  ? 295 VAL A O   1 
ATOM 2177 C CB  . VAL A 1 295 ? 17.749  8.568   26.838  1.00 52.56  ? 295 VAL A CB  1 
ATOM 2178 C CG1 . VAL A 1 295 ? 18.921  9.018   27.684  1.00 51.98  ? 295 VAL A CG1 1 
ATOM 2179 C CG2 . VAL A 1 295 ? 16.439  8.941   27.503  1.00 50.99  ? 295 VAL A CG2 1 
ATOM 2180 N N   . VAL A 1 296 ? 16.520  11.194  25.162  1.00 53.20  ? 296 VAL A N   1 
ATOM 2181 C CA  . VAL A 1 296 ? 16.214  12.615  25.260  1.00 51.47  ? 296 VAL A CA  1 
ATOM 2182 C C   . VAL A 1 296 ? 15.305  12.824  26.462  1.00 56.66  ? 296 VAL A C   1 
ATOM 2183 O O   . VAL A 1 296 ? 14.320  12.097  26.641  1.00 65.32  ? 296 VAL A O   1 
ATOM 2184 C CB  . VAL A 1 296 ? 15.560  13.153  23.975  1.00 57.01  ? 296 VAL A CB  1 
ATOM 2185 C CG1 . VAL A 1 296 ? 14.439  12.242  23.525  1.00 56.77  ? 296 VAL A CG1 1 
ATOM 2186 C CG2 . VAL A 1 296 ? 15.050  14.568  24.193  1.00 54.28  ? 296 VAL A CG2 1 
ATOM 2187 N N   . ILE A 1 297 ? 15.646  13.798  27.292  1.00 56.55  ? 297 ILE A N   1 
ATOM 2188 C CA  . ILE A 1 297 ? 14.852  14.152  28.460  1.00 55.79  ? 297 ILE A CA  1 
ATOM 2189 C C   . ILE A 1 297 ? 14.228  15.509  28.163  1.00 57.38  ? 297 ILE A C   1 
ATOM 2190 O O   . ILE A 1 297 ? 14.890  16.549  28.251  1.00 61.43  ? 297 ILE A O   1 
ATOM 2191 C CB  . ILE A 1 297 ? 15.698  14.170  29.734  1.00 58.18  ? 297 ILE A CB  1 
ATOM 2192 C CG1 . ILE A 1 297 ? 16.364  12.807  29.922  1.00 55.59  ? 297 ILE A CG1 1 
ATOM 2193 C CG2 . ILE A 1 297 ? 14.830  14.474  30.924  1.00 53.71  ? 297 ILE A CG2 1 
ATOM 2194 C CD1 . ILE A 1 297 ? 17.371  12.760  31.034  1.00 57.14  ? 297 ILE A CD1 1 
ATOM 2195 N N   . LEU A 1 298 ? 12.946  15.499  27.813  1.00 57.53  ? 298 LEU A N   1 
ATOM 2196 C CA  . LEU A 1 298 ? 12.280  16.663  27.244  1.00 57.23  ? 298 LEU A CA  1 
ATOM 2197 C C   . LEU A 1 298 ? 11.355  17.298  28.275  1.00 63.00  ? 298 LEU A C   1 
ATOM 2198 O O   . LEU A 1 298 ? 10.463  16.631  28.811  1.00 74.89  ? 298 LEU A O   1 
ATOM 2199 C CB  . LEU A 1 298 ? 11.505  16.248  25.994  1.00 53.69  ? 298 LEU A CB  1 
ATOM 2200 C CG  . LEU A 1 298 ? 10.540  17.229  25.334  1.00 62.59  ? 298 LEU A CG  1 
ATOM 2201 C CD1 . LEU A 1 298 ? 11.289  18.413  24.759  1.00 62.24  ? 298 LEU A CD1 1 
ATOM 2202 C CD2 . LEU A 1 298 ? 9.768   16.506  24.248  1.00 61.13  ? 298 LEU A CD2 1 
ATOM 2203 N N   . MET A 1 299 ? 11.564  18.586  28.546  1.00 57.58  ? 299 MET A N   1 
ATOM 2204 C CA  . MET A 1 299 ? 10.741  19.348  29.486  1.00 56.82  ? 299 MET A CA  1 
ATOM 2205 C C   . MET A 1 299 ? 10.459  20.719  28.880  1.00 62.05  ? 299 MET A C   1 
ATOM 2206 O O   . MET A 1 299 ? 11.286  21.630  28.986  1.00 62.08  ? 299 MET A O   1 
ATOM 2207 C CB  . MET A 1 299 ? 11.425  19.489  30.841  1.00 62.97  ? 299 MET A CB  1 
ATOM 2208 C CG  . MET A 1 299 ? 10.490  19.960  31.943  1.00 59.32  ? 299 MET A CG  1 
ATOM 2209 S SD  . MET A 1 299 ? 11.318  20.835  33.283  1.00 78.07  ? 299 MET A SD  1 
ATOM 2210 C CE  . MET A 1 299 ? 12.947  20.101  33.237  1.00 61.96  ? 299 MET A CE  1 
ATOM 2211 N N   . LEU A 1 300 ? 9.295   20.871  28.257  1.00 56.08  ? 300 LEU A N   1 
ATOM 2212 C CA  . LEU A 1 300 ? 8.871   22.146  27.702  1.00 57.92  ? 300 LEU A CA  1 
ATOM 2213 C C   . LEU A 1 300 ? 7.421   22.405  28.076  1.00 59.81  ? 300 LEU A C   1 
ATOM 2214 O O   . LEU A 1 300 ? 6.645   21.466  28.271  1.00 63.52  ? 300 LEU A O   1 
ATOM 2215 C CB  . LEU A 1 300 ? 9.028   22.171  26.178  1.00 60.59  ? 300 LEU A CB  1 
ATOM 2216 C CG  . LEU A 1 300 ? 10.434  22.428  25.637  1.00 59.17  ? 300 LEU A CG  1 
ATOM 2217 C CD1 . LEU A 1 300 ? 10.529  21.982  24.191  1.00 62.61  ? 300 LEU A CD1 1 
ATOM 2218 C CD2 . LEU A 1 300 ? 10.803  23.892  25.776  1.00 59.42  ? 300 LEU A CD2 1 
ATOM 2219 N N   . GLY A 1 301 ? 7.059   23.681  28.173  1.00 63.66  ? 301 GLY A N   1 
ATOM 2220 C CA  . GLY A 1 301 ? 5.680   24.041  28.432  1.00 58.60  ? 301 GLY A CA  1 
ATOM 2221 C C   . GLY A 1 301 ? 5.482   25.244  29.327  1.00 60.02  ? 301 GLY A C   1 
ATOM 2222 O O   . GLY A 1 301 ? 4.417   25.866  29.299  1.00 67.87  ? 301 GLY A O   1 
ATOM 2223 N N   . LEU A 1 302 ? 6.491   25.588  30.130  1.00 63.51  ? 302 LEU A N   1 
ATOM 2224 C CA  . LEU A 1 302 ? 6.373   26.764  30.986  1.00 64.69  ? 302 LEU A CA  1 
ATOM 2225 C C   . LEU A 1 302 ? 6.285   28.037  30.156  1.00 68.76  ? 302 LEU A C   1 
ATOM 2226 O O   . LEU A 1 302 ? 5.458   28.914  30.429  1.00 71.37  ? 302 LEU A O   1 
ATOM 2227 C CB  . LEU A 1 302 ? 7.549   26.832  31.957  1.00 61.21  ? 302 LEU A CB  1 
ATOM 2228 C CG  . LEU A 1 302 ? 7.332   26.085  33.271  1.00 69.57  ? 302 LEU A CG  1 
ATOM 2229 C CD1 . LEU A 1 302 ? 8.638   25.924  34.016  1.00 68.53  ? 302 LEU A CD1 1 
ATOM 2230 C CD2 . LEU A 1 302 ? 6.311   26.809  34.130  1.00 67.40  ? 302 LEU A CD2 1 
ATOM 2231 N N   . ASN A 1 303 ? 7.133   28.155  29.135  1.00 74.15  ? 303 ASN A N   1 
ATOM 2232 C CA  . ASN A 1 303 ? 7.077   29.317  28.258  1.00 69.67  ? 303 ASN A CA  1 
ATOM 2233 C C   . ASN A 1 303 ? 5.922   29.216  27.273  1.00 69.24  ? 303 ASN A C   1 
ATOM 2234 O O   . ASN A 1 303 ? 5.365   30.241  26.867  1.00 74.95  ? 303 ASN A O   1 
ATOM 2235 C CB  . ASN A 1 303 ? 8.404   29.467  27.521  1.00 67.91  ? 303 ASN A CB  1 
ATOM 2236 C CG  . ASN A 1 303 ? 9.547   29.783  28.456  1.00 74.01  ? 303 ASN A CG  1 
ATOM 2237 O OD1 . ASN A 1 303 ? 10.580  29.115  28.439  1.00 81.00  ? 303 ASN A OD1 1 
ATOM 2238 N ND2 . ASN A 1 303 ? 9.370   30.808  29.279  1.00 70.39  ? 303 ASN A ND2 1 
ATOM 2239 N N   . ASP A 1 304 ? 5.553   27.996  26.880  1.00 68.59  ? 304 ASP A N   1 
ATOM 2240 C CA  . ASP A 1 304 ? 4.435   27.816  25.963  1.00 68.78  ? 304 ASP A CA  1 
ATOM 2241 C C   . ASP A 1 304 ? 3.119   28.267  26.582  1.00 71.71  ? 304 ASP A C   1 
ATOM 2242 O O   . ASP A 1 304 ? 2.286   28.866  25.893  1.00 76.72  ? 304 ASP A O   1 
ATOM 2243 C CB  . ASP A 1 304 ? 4.350   26.355  25.530  1.00 66.49  ? 304 ASP A CB  1 
ATOM 2244 C CG  . ASP A 1 304 ? 5.703   25.778  25.175  1.00 71.30  ? 304 ASP A CG  1 
ATOM 2245 O OD1 . ASP A 1 304 ? 5.811   25.111  24.127  1.00 74.95  ? 304 ASP A OD1 1 
ATOM 2246 O OD2 . ASP A 1 304 ? 6.662   25.997  25.943  1.00 74.19  ? 304 ASP A OD2 1 
ATOM 2247 N N   . ALA A 1 305 ? 2.913   27.991  27.870  1.00 62.78  ? 305 ALA A N   1 
ATOM 2248 C CA  . ALA A 1 305 ? 1.709   28.445  28.553  1.00 60.20  ? 305 ALA A CA  1 
ATOM 2249 C C   . ALA A 1 305 ? 1.626   29.960  28.652  1.00 63.09  ? 305 ALA A C   1 
ATOM 2250 O O   . ALA A 1 305 ? 0.523   30.498  28.794  1.00 67.67  ? 305 ALA A O   1 
ATOM 2251 C CB  . ALA A 1 305 ? 1.633   27.839  29.953  1.00 62.64  ? 305 ALA A CB  1 
ATOM 2252 N N   . GLY A 1 306 ? 2.757   30.654  28.584  1.00 67.81  ? 306 GLY A N   1 
ATOM 2253 C CA  . GLY A 1 306 ? 2.773   32.099  28.604  1.00 68.84  ? 306 GLY A CA  1 
ATOM 2254 C C   . GLY A 1 306 ? 2.492   32.764  27.279  1.00 76.27  ? 306 GLY A C   1 
ATOM 2255 O O   . GLY A 1 306 ? 2.499   33.995  27.201  1.00 79.38  ? 306 GLY A O   1 
ATOM 2256 N N   . GLY A 1 307 ? 2.242   31.986  26.230  1.00 74.83  ? 307 GLY A N   1 
ATOM 2257 C CA  . GLY A 1 307 ? 1.973   32.548  24.925  1.00 76.75  ? 307 GLY A CA  1 
ATOM 2258 C C   . GLY A 1 307 ? 3.196   32.963  24.144  1.00 78.90  ? 307 GLY A C   1 
ATOM 2259 O O   . GLY A 1 307 ? 3.067   33.698  23.158  1.00 80.23  ? 307 GLY A O   1 
ATOM 2260 N N   . VAL A 1 308 ? 4.380   32.524  24.553  1.00 75.14  ? 308 VAL A N   1 
ATOM 2261 C CA  . VAL A 1 308 ? 5.624   32.855  23.869  1.00 73.44  ? 308 VAL A CA  1 
ATOM 2262 C C   . VAL A 1 308 ? 5.592   32.254  22.472  1.00 76.06  ? 308 VAL A C   1 
ATOM 2263 O O   . VAL A 1 308 ? 5.212   31.094  22.280  1.00 77.36  ? 308 VAL A O   1 
ATOM 2264 C CB  . VAL A 1 308 ? 6.843   32.362  24.674  1.00 71.83  ? 308 VAL A CB  1 
ATOM 2265 C CG1 . VAL A 1 308 ? 8.130   32.600  23.902  1.00 72.37  ? 308 VAL A CG1 1 
ATOM 2266 C CG2 . VAL A 1 308 ? 6.895   33.051  26.026  1.00 70.97  ? 308 VAL A CG2 1 
ATOM 2267 N N   . ALA A 1 309 ? 5.984   33.059  21.484  1.00 82.06  ? 309 ALA A N   1 
ATOM 2268 C CA  . ALA A 1 309 ? 5.963   32.708  20.067  1.00 82.66  ? 309 ALA A CA  1 
ATOM 2269 C C   . ALA A 1 309 ? 4.567   32.364  19.568  1.00 83.44  ? 309 ALA A C   1 
ATOM 2270 O O   . ALA A 1 309 ? 4.425   31.531  18.665  1.00 82.55  ? 309 ALA A O   1 
ATOM 2271 C CB  . ALA A 1 309 ? 6.926   31.554  19.754  1.00 77.27  ? 309 ALA A CB  1 
ATOM 2272 N N   . GLY A 1 310 ? 3.531   32.983  20.131  1.00 82.18  ? 310 GLY A N   1 
ATOM 2273 C CA  . GLY A 1 310 ? 2.173   32.680  19.733  1.00 80.74  ? 310 GLY A CA  1 
ATOM 2274 C C   . GLY A 1 310 ? 1.740   31.262  20.007  1.00 82.78  ? 310 GLY A C   1 
ATOM 2275 O O   . GLY A 1 310 ? 0.890   30.735  19.282  1.00 84.16  ? 310 GLY A O   1 
ATOM 2276 N N   . THR A 1 311 ? 2.299   30.624  21.031  1.00 78.41  ? 311 THR A N   1 
ATOM 2277 C CA  . THR A 1 311 ? 2.009   29.224  21.310  1.00 78.51  ? 311 THR A CA  1 
ATOM 2278 C C   . THR A 1 311 ? 0.664   29.104  22.011  1.00 78.67  ? 311 THR A C   1 
ATOM 2279 O O   . THR A 1 311 ? 0.421   29.769  23.025  1.00 77.44  ? 311 THR A O   1 
ATOM 2280 C CB  . THR A 1 311 ? 3.110   28.610  22.169  1.00 76.91  ? 311 THR A CB  1 
ATOM 2281 O OG1 . THR A 1 311 ? 4.382   28.838  21.554  1.00 78.04  ? 311 THR A OG1 1 
ATOM 2282 C CG2 . THR A 1 311 ? 2.892   27.115  22.313  1.00 75.47  ? 311 THR A CG2 1 
ATOM 2283 N N   . THR A 1 312 ? -0.205  28.261  21.475  1.00 73.35  ? 312 THR A N   1 
ATOM 2284 C CA  . THR A 1 312 ? -1.454  27.906  22.119  1.00 73.21  ? 312 THR A CA  1 
ATOM 2285 C C   . THR A 1 312 ? -1.345  26.477  22.643  1.00 72.86  ? 312 THR A C   1 
ATOM 2286 O O   . THR A 1 312 ? -0.324  25.806  22.471  1.00 77.13  ? 312 THR A O   1 
ATOM 2287 C CB  . THR A 1 312 ? -2.622  28.072  21.145  1.00 75.43  ? 312 THR A CB  1 
ATOM 2288 O OG1 . THR A 1 312 ? -2.450  27.185  20.033  1.00 75.59  ? 312 THR A OG1 1 
ATOM 2289 C CG2 . THR A 1 312 ? -2.691  29.503  20.639  1.00 71.88  ? 312 THR A CG2 1 
ATOM 2290 N N   . GLU A 1 313 ? -2.403  26.004  23.302  1.00 70.71  ? 313 GLU A N   1 
ATOM 2291 C CA  . GLU A 1 313 ? -2.396  24.632  23.795  1.00 70.01  ? 313 GLU A CA  1 
ATOM 2292 C C   . GLU A 1 313 ? -2.313  23.634  22.647  1.00 71.53  ? 313 GLU A C   1 
ATOM 2293 O O   . GLU A 1 313 ? -1.571  22.649  22.727  1.00 73.42  ? 313 GLU A O   1 
ATOM 2294 C CB  . GLU A 1 313 ? -3.638  24.373  24.646  1.00 71.06  ? 313 GLU A CB  1 
ATOM 2295 C CG  . GLU A 1 313 ? -3.737  22.955  25.164  1.00 71.28  ? 313 GLU A CG  1 
ATOM 2296 C CD  . GLU A 1 313 ? -5.143  22.591  25.580  1.00 78.92  ? 313 GLU A CD  1 
ATOM 2297 O OE1 . GLU A 1 313 ? -5.923  23.507  25.914  1.00 81.84  ? 313 GLU A OE1 1 
ATOM 2298 O OE2 . GLU A 1 313 ? -5.474  21.387  25.559  1.00 79.61  ? 313 GLU A OE2 1 
ATOM 2299 N N   . ASP A 1 314 ? -3.068  23.871  21.572  1.00 73.60  ? 314 ASP A N   1 
ATOM 2300 C CA  . ASP A 1 314 ? -2.995  22.992  20.410  1.00 73.80  ? 314 ASP A CA  1 
ATOM 2301 C C   . ASP A 1 314 ? -1.626  23.046  19.747  1.00 72.59  ? 314 ASP A C   1 
ATOM 2302 O O   . ASP A 1 314 ? -1.092  22.003  19.350  1.00 70.86  ? 314 ASP A O   1 
ATOM 2303 C CB  . ASP A 1 314 ? -4.085  23.359  19.404  1.00 72.56  ? 314 ASP A CB  1 
ATOM 2304 C CG  . ASP A 1 314 ? -5.479  23.177  19.966  1.00 79.40  ? 314 ASP A CG  1 
ATOM 2305 O OD1 . ASP A 1 314 ? -5.648  22.340  20.876  1.00 80.20  ? 314 ASP A OD1 1 
ATOM 2306 O OD2 . ASP A 1 314 ? -6.404  23.871  19.497  1.00 81.35  ? 314 ASP A OD2 1 
ATOM 2307 N N   . ILE A 1 315 ? -1.047  24.240  19.615  1.00 71.70  ? 315 ILE A N   1 
ATOM 2308 C CA  . ILE A 1 315 ? 0.285   24.362  19.032  1.00 71.60  ? 315 ILE A CA  1 
ATOM 2309 C C   . ILE A 1 315 ? 1.312   23.649  19.901  1.00 71.62  ? 315 ILE A C   1 
ATOM 2310 O O   . ILE A 1 315 ? 2.180   22.927  19.394  1.00 73.02  ? 315 ILE A O   1 
ATOM 2311 C CB  . ILE A 1 315 ? 0.643   25.846  18.830  1.00 70.87  ? 315 ILE A CB  1 
ATOM 2312 C CG1 . ILE A 1 315 ? -0.217  26.455  17.723  1.00 70.16  ? 315 ILE A CG1 1 
ATOM 2313 C CG2 . ILE A 1 315 ? 2.119   26.004  18.507  1.00 70.14  ? 315 ILE A CG2 1 
ATOM 2314 C CD1 . ILE A 1 315 ? -0.011  27.940  17.541  1.00 72.70  ? 315 ILE A CD1 1 
ATOM 2315 N N   . TYR A 1 316 ? 1.227   23.838  21.220  1.00 67.93  ? 316 TYR A N   1 
ATOM 2316 C CA  . TYR A 1 316 ? 2.129   23.144  22.130  1.00 64.27  ? 316 TYR A CA  1 
ATOM 2317 C C   . TYR A 1 316 ? 2.003   21.636  21.982  1.00 68.13  ? 316 TYR A C   1 
ATOM 2318 O O   . TYR A 1 316 ? 3.009   20.930  21.878  1.00 69.32  ? 316 TYR A O   1 
ATOM 2319 C CB  . TYR A 1 316 ? 1.841   23.560  23.572  1.00 66.30  ? 316 TYR A CB  1 
ATOM 2320 C CG  . TYR A 1 316 ? 2.511   22.691  24.612  1.00 66.46  ? 316 TYR A CG  1 
ATOM 2321 C CD1 . TYR A 1 316 ? 3.844   22.876  24.945  1.00 65.60  ? 316 TYR A CD1 1 
ATOM 2322 C CD2 . TYR A 1 316 ? 1.812   21.679  25.257  1.00 66.14  ? 316 TYR A CD2 1 
ATOM 2323 C CE1 . TYR A 1 316 ? 4.459   22.088  25.892  1.00 62.78  ? 316 TYR A CE1 1 
ATOM 2324 C CE2 . TYR A 1 316 ? 2.422   20.881  26.202  1.00 66.89  ? 316 TYR A CE2 1 
ATOM 2325 C CZ  . TYR A 1 316 ? 3.745   21.091  26.517  1.00 65.45  ? 316 TYR A CZ  1 
ATOM 2326 O OH  . TYR A 1 316 ? 4.360   20.302  27.460  1.00 69.84  ? 316 TYR A OH  1 
ATOM 2327 N N   . MET A 1 317 ? 0.771   21.126  21.965  1.00 69.24  ? 317 MET A N   1 
ATOM 2328 C CA  . MET A 1 317 ? 0.558   19.689  21.848  1.00 68.29  ? 317 MET A CA  1 
ATOM 2329 C C   . MET A 1 317 ? 1.132   19.155  20.542  1.00 72.78  ? 317 MET A C   1 
ATOM 2330 O O   . MET A 1 317 ? 1.880   18.167  20.538  1.00 74.66  ? 317 MET A O   1 
ATOM 2331 C CB  . MET A 1 317 ? -0.939  19.393  21.940  1.00 68.48  ? 317 MET A CB  1 
ATOM 2332 C CG  . MET A 1 317 ? -1.467  19.275  23.360  1.00 69.40  ? 317 MET A CG  1 
ATOM 2333 S SD  . MET A 1 317 ? -0.527  18.152  24.398  1.00 80.10  ? 317 MET A SD  1 
ATOM 2334 C CE  . MET A 1 317 ? -0.818  16.620  23.527  1.00 70.78  ? 317 MET A CE  1 
ATOM 2335 N N   . GLU A 1 318 ? 0.821   19.828  19.432  1.00 79.82  ? 318 GLU A N   1 
ATOM 2336 C CA  . GLU A 1 318 ? 1.284   19.389  18.121  1.00 78.05  ? 318 GLU A CA  1 
ATOM 2337 C C   . GLU A 1 318 ? 2.803   19.377  18.048  1.00 78.39  ? 318 GLU A C   1 
ATOM 2338 O O   . GLU A 1 318 ? 3.406   18.415  17.559  1.00 79.73  ? 318 GLU A O   1 
ATOM 2339 C CB  . GLU A 1 318 ? 0.705   20.303  17.043  1.00 78.88  ? 318 GLU A CB  1 
ATOM 2340 C CG  . GLU A 1 318 ? 1.312   20.114  15.665  1.00 82.88  ? 318 GLU A CG  1 
ATOM 2341 C CD  . GLU A 1 318 ? 1.002   21.270  14.739  1.00 87.12  ? 318 GLU A CD  1 
ATOM 2342 O OE1 . GLU A 1 318 ? 0.269   22.189  15.162  1.00 88.24  ? 318 GLU A OE1 1 
ATOM 2343 O OE2 . GLU A 1 318 ? 1.488   21.264  13.589  1.00 86.66  ? 318 GLU A OE2 1 
ATOM 2344 N N   . TYR A 1 319 ? 3.448   20.433  18.545  1.00 72.77  ? 319 TYR A N   1 
ATOM 2345 C CA  . TYR A 1 319 ? 4.887   20.530  18.354  1.00 73.14  ? 319 TYR A CA  1 
ATOM 2346 C C   . TYR A 1 319 ? 5.657   19.695  19.368  1.00 73.03  ? 319 TYR A C   1 
ATOM 2347 O O   . TYR A 1 319 ? 6.757   19.228  19.061  1.00 73.06  ? 319 TYR A O   1 
ATOM 2348 C CB  . TYR A 1 319 ? 5.315   21.994  18.378  1.00 72.75  ? 319 TYR A CB  1 
ATOM 2349 C CG  . TYR A 1 319 ? 5.147   22.626  17.018  1.00 76.89  ? 319 TYR A CG  1 
ATOM 2350 C CD1 . TYR A 1 319 ? 6.021   22.327  15.983  1.00 77.07  ? 319 TYR A CD1 1 
ATOM 2351 C CD2 . TYR A 1 319 ? 4.086   23.480  16.754  1.00 77.53  ? 319 TYR A CD2 1 
ATOM 2352 C CE1 . TYR A 1 319 ? 5.862   22.884  14.732  1.00 75.37  ? 319 TYR A CE1 1 
ATOM 2353 C CE2 . TYR A 1 319 ? 3.918   24.040  15.505  1.00 76.90  ? 319 TYR A CE2 1 
ATOM 2354 C CZ  . TYR A 1 319 ? 4.808   23.738  14.497  1.00 78.20  ? 319 TYR A CZ  1 
ATOM 2355 O OH  . TYR A 1 319 ? 4.647   24.298  13.251  1.00 80.54  ? 319 TYR A OH  1 
ATOM 2356 N N   . MET A 1 320 ? 5.095   19.450  20.553  1.00 69.98  ? 320 MET A N   1 
ATOM 2357 C CA  . MET A 1 320 ? 5.711   18.473  21.444  1.00 67.06  ? 320 MET A CA  1 
ATOM 2358 C C   . MET A 1 320 ? 5.604   17.070  20.866  1.00 68.90  ? 320 MET A C   1 
ATOM 2359 O O   . MET A 1 320 ? 6.552   16.280  20.958  1.00 72.55  ? 320 MET A O   1 
ATOM 2360 C CB  . MET A 1 320 ? 5.078   18.538  22.832  1.00 62.64  ? 320 MET A CB  1 
ATOM 2361 C CG  . MET A 1 320 ? 5.333   19.845  23.544  1.00 67.35  ? 320 MET A CG  1 
ATOM 2362 S SD  . MET A 1 320 ? 6.954   19.970  24.316  1.00 82.68  ? 320 MET A SD  1 
ATOM 2363 C CE  . MET A 1 320 ? 6.996   18.467  25.277  1.00 63.71  ? 320 MET A CE  1 
ATOM 2364 N N   . GLU A 1 321 ? 4.464   16.742  20.250  1.00 70.82  ? 321 GLU A N   1 
ATOM 2365 C CA  . GLU A 1 321 ? 4.358   15.456  19.571  1.00 71.27  ? 321 GLU A CA  1 
ATOM 2366 C C   . GLU A 1 321 ? 5.362   15.355  18.429  1.00 74.28  ? 321 GLU A C   1 
ATOM 2367 O O   . GLU A 1 321 ? 6.010   14.318  18.256  1.00 74.07  ? 321 GLU A O   1 
ATOM 2368 C CB  . GLU A 1 321 ? 2.935   15.247  19.059  1.00 69.40  ? 321 GLU A CB  1 
ATOM 2369 C CG  . GLU A 1 321 ? 2.707   13.893  18.418  1.00 69.52  ? 321 GLU A CG  1 
ATOM 2370 C CD  . GLU A 1 321 ? 1.267   13.681  18.008  1.00 76.53  ? 321 GLU A CD  1 
ATOM 2371 O OE1 . GLU A 1 321 ? 0.444   14.589  18.237  1.00 78.62  ? 321 GLU A OE1 1 
ATOM 2372 O OE2 . GLU A 1 321 ? 0.958   12.603  17.458  1.00 78.73  ? 321 GLU A OE2 1 
ATOM 2373 N N   . LYS A 1 322 ? 5.511   16.428  17.648  1.00 73.11  ? 322 LYS A N   1 
ATOM 2374 C CA  . LYS A 1 322 ? 6.486   16.432  16.561  1.00 68.70  ? 322 LYS A CA  1 
ATOM 2375 C C   . LYS A 1 322 ? 7.905   16.270  17.087  1.00 71.78  ? 322 LYS A C   1 
ATOM 2376 O O   . LYS A 1 322 ? 8.715   15.554  16.490  1.00 74.20  ? 322 LYS A O   1 
ATOM 2377 C CB  . LYS A 1 322 ? 6.362   17.718  15.747  1.00 72.03  ? 322 LYS A CB  1 
ATOM 2378 C CG  . LYS A 1 322 ? 5.184   17.739  14.793  1.00 75.22  ? 322 LYS A CG  1 
ATOM 2379 C CD  . LYS A 1 322 ? 5.234   18.962  13.896  1.00 74.02  ? 322 LYS A CD  1 
ATOM 2380 C CE  . LYS A 1 322 ? 3.920   19.160  13.165  1.00 74.31  ? 322 LYS A CE  1 
ATOM 2381 N NZ  . LYS A 1 322 ? 3.871   20.473  12.466  1.00 81.21  ? 322 LYS A NZ  1 
ATOM 2382 N N   . LEU A 1 323 ? 8.226   16.936  18.199  1.00 67.85  ? 323 LEU A N   1 
ATOM 2383 C CA  . LEU A 1 323 ? 9.544   16.781  18.805  1.00 64.58  ? 323 LEU A CA  1 
ATOM 2384 C C   . LEU A 1 323 ? 9.775   15.348  19.258  1.00 65.04  ? 323 LEU A C   1 
ATOM 2385 O O   . LEU A 1 323 ? 10.868  14.805  19.079  1.00 70.45  ? 323 LEU A O   1 
ATOM 2386 C CB  . LEU A 1 323 ? 9.698   17.743  19.981  1.00 62.83  ? 323 LEU A CB  1 
ATOM 2387 C CG  . LEU A 1 323 ? 10.134  19.170  19.651  1.00 65.93  ? 323 LEU A CG  1 
ATOM 2388 C CD1 . LEU A 1 323 ? 9.951   20.070  20.859  1.00 65.33  ? 323 LEU A CD1 1 
ATOM 2389 C CD2 . LEU A 1 323 ? 11.578  19.186  19.182  1.00 67.58  ? 323 LEU A CD2 1 
ATOM 2390 N N   . ILE A 1 324 ? 8.757   14.721  19.851  1.00 61.25  ? 324 ILE A N   1 
ATOM 2391 C CA  . ILE A 1 324 ? 8.894   13.333  20.292  1.00 62.94  ? 324 ILE A CA  1 
ATOM 2392 C C   . ILE A 1 324 ? 9.141   12.418  19.098  1.00 68.70  ? 324 ILE A C   1 
ATOM 2393 O O   . ILE A 1 324 ? 10.006  11.534  19.136  1.00 66.54  ? 324 ILE A O   1 
ATOM 2394 C CB  . ILE A 1 324 ? 7.653   12.902  21.092  1.00 60.31  ? 324 ILE A CB  1 
ATOM 2395 C CG1 . ILE A 1 324 ? 7.618   13.617  22.443  1.00 59.05  ? 324 ILE A CG1 1 
ATOM 2396 C CG2 . ILE A 1 324 ? 7.635   11.396  21.285  1.00 55.90  ? 324 ILE A CG2 1 
ATOM 2397 C CD1 . ILE A 1 324 ? 6.295   13.503  23.157  1.00 62.25  ? 324 ILE A CD1 1 
ATOM 2398 N N   . ARG A 1 325 ? 8.382   12.618  18.017  1.00 69.79  ? 325 ARG A N   1 
ATOM 2399 C CA  . ARG A 1 325 ? 8.570   11.799  16.823  1.00 66.30  ? 325 ARG A CA  1 
ATOM 2400 C C   . ARG A 1 325 ? 9.957   12.004  16.228  1.00 66.80  ? 325 ARG A C   1 
ATOM 2401 O O   . ARG A 1 325 ? 10.602  11.045  15.792  1.00 70.54  ? 325 ARG A O   1 
ATOM 2402 C CB  . ARG A 1 325 ? 7.495   12.117  15.786  1.00 63.65  ? 325 ARG A CB  1 
ATOM 2403 C CG  . ARG A 1 325 ? 6.083   12.045  16.320  1.00 63.05  ? 325 ARG A CG  1 
ATOM 2404 C CD  . ARG A 1 325 ? 5.060   12.223  15.221  1.00 64.83  ? 325 ARG A CD  1 
ATOM 2405 N NE  . ARG A 1 325 ? 4.175   11.073  15.113  1.00 68.18  ? 325 ARG A NE  1 
ATOM 2406 C CZ  . ARG A 1 325 ? 3.870   10.466  13.976  1.00 70.12  ? 325 ARG A CZ  1 
ATOM 2407 N NH1 . ARG A 1 325 ? 4.395   10.851  12.824  1.00 67.60  ? 325 ARG A NH1 1 
ATOM 2408 N NH2 . ARG A 1 325 ? 3.014   9.450   13.995  1.00 71.99  ? 325 ARG A NH2 1 
ATOM 2409 N N   . ARG A 1 326 ? 10.426  13.252  16.194  1.00 61.87  ? 326 ARG A N   1 
ATOM 2410 C CA  . ARG A 1 326 ? 11.757  13.537  15.671  1.00 64.47  ? 326 ARG A CA  1 
ATOM 2411 C C   . ARG A 1 326 ? 12.837  12.891  16.529  1.00 69.36  ? 326 ARG A C   1 
ATOM 2412 O O   . ARG A 1 326 ? 13.811  12.339  16.005  1.00 75.46  ? 326 ARG A O   1 
ATOM 2413 C CB  . ARG A 1 326 ? 11.961  15.049  15.583  1.00 64.10  ? 326 ARG A CB  1 
ATOM 2414 C CG  . ARG A 1 326 ? 13.402  15.504  15.680  1.00 63.75  ? 326 ARG A CG  1 
ATOM 2415 C CD  . ARG A 1 326 ? 13.479  17.014  15.790  1.00 68.84  ? 326 ARG A CD  1 
ATOM 2416 N NE  . ARG A 1 326 ? 13.160  17.667  14.526  1.00 73.70  ? 326 ARG A NE  1 
ATOM 2417 C CZ  . ARG A 1 326 ? 13.181  18.978  14.336  1.00 69.12  ? 326 ARG A CZ  1 
ATOM 2418 N NH1 . ARG A 1 326 ? 13.512  19.813  15.305  1.00 66.95  ? 326 ARG A NH1 1 
ATOM 2419 N NH2 . ARG A 1 326 ? 12.861  19.463  13.140  1.00 68.61  ? 326 ARG A NH2 1 
ATOM 2420 N N   . PHE A 1 327 ? 12.679  12.951  17.852  1.00 68.05  ? 327 PHE A N   1 
ATOM 2421 C CA  . PHE A 1 327 ? 13.636  12.323  18.754  1.00 60.75  ? 327 PHE A CA  1 
ATOM 2422 C C   . PHE A 1 327 ? 13.665  10.812  18.574  1.00 66.18  ? 327 PHE A C   1 
ATOM 2423 O O   . PHE A 1 327 ? 14.743  10.208  18.589  1.00 69.76  ? 327 PHE A O   1 
ATOM 2424 C CB  . PHE A 1 327 ? 13.297  12.675  20.201  1.00 60.22  ? 327 PHE A CB  1 
ATOM 2425 C CG  . PHE A 1 327 ? 13.469  14.130  20.530  1.00 63.11  ? 327 PHE A CG  1 
ATOM 2426 C CD1 . PHE A 1 327 ? 14.403  14.899  19.862  1.00 67.06  ? 327 PHE A CD1 1 
ATOM 2427 C CD2 . PHE A 1 327 ? 12.693  14.727  21.508  1.00 66.01  ? 327 PHE A CD2 1 
ATOM 2428 C CE1 . PHE A 1 327 ? 14.562  16.236  20.163  1.00 68.73  ? 327 PHE A CE1 1 
ATOM 2429 C CE2 . PHE A 1 327 ? 12.846  16.064  21.811  1.00 67.63  ? 327 PHE A CE2 1 
ATOM 2430 C CZ  . PHE A 1 327 ? 13.782  16.819  21.139  1.00 66.93  ? 327 PHE A CZ  1 
ATOM 2431 N N   . ILE A 1 328 ? 12.497  10.186  18.414  1.00 62.40  ? 328 ILE A N   1 
ATOM 2432 C CA  . ILE A 1 328 ? 12.461  8.748   18.169  1.00 64.97  ? 328 ILE A CA  1 
ATOM 2433 C C   . ILE A 1 328 ? 13.111  8.418   16.832  1.00 68.28  ? 328 ILE A C   1 
ATOM 2434 O O   . ILE A 1 328 ? 13.867  7.445   16.724  1.00 63.97  ? 328 ILE A O   1 
ATOM 2435 C CB  . ILE A 1 328 ? 11.015  8.226   18.240  1.00 63.26  ? 328 ILE A CB  1 
ATOM 2436 C CG1 . ILE A 1 328 ? 10.461  8.395   19.654  1.00 59.03  ? 328 ILE A CG1 1 
ATOM 2437 C CG2 . ILE A 1 328 ? 10.958  6.764   17.835  1.00 61.23  ? 328 ILE A CG2 1 
ATOM 2438 C CD1 . ILE A 1 328 ? 8.971   8.183   19.752  1.00 63.70  ? 328 ILE A CD1 1 
ATOM 2439 N N   . ASP A 1 329 ? 12.838  9.217   15.799  1.00 74.46  ? 329 ASP A N   1 
ATOM 2440 C CA  . ASP A 1 329 ? 13.455  9.019   14.494  1.00 68.18  ? 329 ASP A CA  1 
ATOM 2441 C C   . ASP A 1 329 ? 14.967  9.176   14.531  1.00 67.74  ? 329 ASP A C   1 
ATOM 2442 O O   . ASP A 1 329 ? 15.655  8.629   13.664  1.00 75.18  ? 329 ASP A O   1 
ATOM 2443 C CB  . ASP A 1 329 ? 12.864  9.997   13.480  1.00 66.12  ? 329 ASP A CB  1 
ATOM 2444 C CG  . ASP A 1 329 ? 11.619  9.459   12.812  1.00 74.10  ? 329 ASP A CG  1 
ATOM 2445 O OD1 . ASP A 1 329 ? 11.442  8.223   12.797  1.00 73.35  ? 329 ASP A OD1 1 
ATOM 2446 O OD2 . ASP A 1 329 ? 10.815  10.269  12.308  1.00 78.81  ? 329 ASP A OD2 1 
ATOM 2447 N N   . TRP A 1 330 ? 15.495  9.902   15.510  1.00 63.21  ? 330 TRP A N   1 
ATOM 2448 C CA  . TRP A 1 330 ? 16.931  10.036  15.694  1.00 63.74  ? 330 TRP A CA  1 
ATOM 2449 C C   . TRP A 1 330 ? 17.528  8.889   16.498  1.00 70.63  ? 330 TRP A C   1 
ATOM 2450 O O   . TRP A 1 330 ? 18.706  8.956   16.864  1.00 73.07  ? 330 TRP A O   1 
ATOM 2451 C CB  . TRP A 1 330 ? 17.252  11.369  16.374  1.00 68.54  ? 330 TRP A CB  1 
ATOM 2452 C CG  . TRP A 1 330 ? 17.219  12.535  15.439  1.00 70.45  ? 330 TRP A CG  1 
ATOM 2453 C CD1 . TRP A 1 330 ? 17.299  12.495  14.079  1.00 68.51  ? 330 TRP A CD1 1 
ATOM 2454 C CD2 . TRP A 1 330 ? 17.101  13.916  15.795  1.00 72.36  ? 330 TRP A CD2 1 
ATOM 2455 N NE1 . TRP A 1 330 ? 17.237  13.765  13.565  1.00 69.47  ? 330 TRP A NE1 1 
ATOM 2456 C CE2 . TRP A 1 330 ? 17.116  14.657  14.598  1.00 70.29  ? 330 TRP A CE2 1 
ATOM 2457 C CE3 . TRP A 1 330 ? 16.982  14.599  17.008  1.00 70.01  ? 330 TRP A CE3 1 
ATOM 2458 C CZ2 . TRP A 1 330 ? 17.019  16.045  14.578  1.00 69.61  ? 330 TRP A CZ2 1 
ATOM 2459 C CZ3 . TRP A 1 330 ? 16.887  15.976  16.986  1.00 70.34  ? 330 TRP A CZ3 1 
ATOM 2460 C CH2 . TRP A 1 330 ? 16.906  16.684  15.780  1.00 71.36  ? 330 TRP A CH2 1 
ATOM 2461 N N   . GLY A 1 331 ? 16.748  7.850   16.785  1.00 70.47  ? 331 GLY A N   1 
ATOM 2462 C CA  . GLY A 1 331 ? 17.250  6.728   17.550  1.00 72.72  ? 331 GLY A CA  1 
ATOM 2463 C C   . GLY A 1 331 ? 17.328  6.963   19.037  1.00 72.46  ? 331 GLY A C   1 
ATOM 2464 O O   . GLY A 1 331 ? 18.062  6.251   19.728  1.00 73.18  ? 331 GLY A O   1 
ATOM 2465 N N   . MET A 1 332 ? 16.601  7.947   19.554  1.00 69.58  ? 332 MET A N   1 
ATOM 2466 C CA  . MET A 1 332 ? 16.676  8.308   20.960  1.00 69.44  ? 332 MET A CA  1 
ATOM 2467 C C   . MET A 1 332 ? 15.400  7.923   21.693  1.00 70.68  ? 332 MET A C   1 
ATOM 2468 O O   . MET A 1 332 ? 14.292  8.166   21.208  1.00 77.37  ? 332 MET A O   1 
ATOM 2469 C CB  . MET A 1 332 ? 16.930  9.808   21.106  1.00 65.29  ? 332 MET A CB  1 
ATOM 2470 C CG  . MET A 1 332 ? 18.335  10.228  20.720  1.00 77.21  ? 332 MET A CG  1 
ATOM 2471 S SD  . MET A 1 332 ? 18.578  12.011  20.672  1.00 93.52  ? 332 MET A SD  1 
ATOM 2472 C CE  . MET A 1 332 ? 16.886  12.575  20.667  1.00 70.54  ? 332 MET A CE  1 
ATOM 2473 N N   . GLY A 1 333 ? 15.566  7.310   22.864  1.00 61.25  ? 333 GLY A N   1 
ATOM 2474 C CA  . GLY A 1 333 ? 14.436  7.087   23.746  1.00 55.44  ? 333 GLY A CA  1 
ATOM 2475 C C   . GLY A 1 333 ? 13.984  8.401   24.363  1.00 60.56  ? 333 GLY A C   1 
ATOM 2476 O O   . GLY A 1 333 ? 14.791  9.259   24.714  1.00 64.46  ? 333 GLY A O   1 
ATOM 2477 N N   . VAL A 1 334 ? 12.671  8.558   24.487  1.00 56.37  ? 334 VAL A N   1 
ATOM 2478 C CA  . VAL A 1 334 ? 12.075  9.820   24.907  1.00 56.80  ? 334 VAL A CA  1 
ATOM 2479 C C   . VAL A 1 334 ? 11.611  9.687   26.350  1.00 62.57  ? 334 VAL A C   1 
ATOM 2480 O O   . VAL A 1 334 ? 10.803  8.809   26.675  1.00 63.08  ? 334 VAL A O   1 
ATOM 2481 C CB  . VAL A 1 334 ? 10.915  10.231  23.990  1.00 59.68  ? 334 VAL A CB  1 
ATOM 2482 C CG1 . VAL A 1 334 ? 10.321  11.550  24.453  1.00 59.07  ? 334 VAL A CG1 1 
ATOM 2483 C CG2 . VAL A 1 334 ? 11.395  10.337  22.557  1.00 62.73  ? 334 VAL A CG2 1 
ATOM 2484 N N   . VAL A 1 335 ? 12.125  10.560  27.209  1.00 59.53  ? 335 VAL A N   1 
ATOM 2485 C CA  . VAL A 1 335 ? 11.647  10.702  28.579  1.00 54.66  ? 335 VAL A CA  1 
ATOM 2486 C C   . VAL A 1 335 ? 11.048  12.092  28.712  1.00 56.21  ? 335 VAL A C   1 
ATOM 2487 O O   . VAL A 1 335 ? 11.773  13.093  28.718  1.00 62.67  ? 335 VAL A O   1 
ATOM 2488 C CB  . VAL A 1 335 ? 12.776  10.483  29.597  1.00 56.65  ? 335 VAL A CB  1 
ATOM 2489 C CG1 . VAL A 1 335 ? 12.251  10.669  31.010  1.00 52.39  ? 335 VAL A CG1 1 
ATOM 2490 C CG2 . VAL A 1 335 ? 13.373  9.103   29.430  1.00 58.29  ? 335 VAL A CG2 1 
ATOM 2491 N N   . VAL A 1 336 ? 9.727   12.160  28.817  1.00 50.99  ? 336 VAL A N   1 
ATOM 2492 C CA  . VAL A 1 336 ? 9.020   13.432  28.887  1.00 48.23  ? 336 VAL A CA  1 
ATOM 2493 C C   . VAL A 1 336 ? 8.889   13.841  30.348  1.00 46.76  ? 336 VAL A C   1 
ATOM 2494 O O   . VAL A 1 336 ? 8.590   13.012  31.213  1.00 57.94  ? 336 VAL A O   1 
ATOM 2495 C CB  . VAL A 1 336 ? 7.647   13.346  28.203  1.00 51.41  ? 336 VAL A CB  1 
ATOM 2496 C CG1 . VAL A 1 336 ? 7.818   13.119  26.713  1.00 55.10  ? 336 VAL A CG1 1 
ATOM 2497 C CG2 . VAL A 1 336 ? 6.808   12.234  28.810  1.00 50.00  ? 336 VAL A CG2 1 
ATOM 2498 N N   . GLN A 1 337 ? 9.142   15.114  30.627  1.00 45.98  ? 337 GLN A N   1 
ATOM 2499 C CA  . GLN A 1 337 ? 8.986   15.650  31.969  1.00 45.27  ? 337 GLN A CA  1 
ATOM 2500 C C   . GLN A 1 337 ? 7.808   16.608  32.020  1.00 50.46  ? 337 GLN A C   1 
ATOM 2501 O O   . GLN A 1 337 ? 7.530   17.322  31.054  1.00 66.32  ? 337 GLN A O   1 
ATOM 2502 C CB  . GLN A 1 337 ? 10.248  16.385  32.419  1.00 43.04  ? 337 GLN A CB  1 
ATOM 2503 C CG  . GLN A 1 337 ? 11.544  15.646  32.204  1.00 47.18  ? 337 GLN A CG  1 
ATOM 2504 C CD  . GLN A 1 337 ? 12.669  16.239  33.022  1.00 53.95  ? 337 GLN A CD  1 
ATOM 2505 O OE1 . GLN A 1 337 ? 12.758  16.019  34.227  1.00 59.38  ? 337 GLN A OE1 1 
ATOM 2506 N NE2 . GLN A 1 337 ? 13.527  17.013  32.372  1.00 58.40  ? 337 GLN A NE2 1 
ATOM 2507 N N   . THR A 1 338 ? 7.118   16.617  33.153  1.00 53.90  ? 338 THR A N   1 
ATOM 2508 C CA  . THR A 1 338 ? 6.173   17.684  33.431  1.00 56.25  ? 338 THR A CA  1 
ATOM 2509 C C   . THR A 1 338 ? 6.937   18.973  33.700  1.00 52.43  ? 338 THR A C   1 
ATOM 2510 O O   . THR A 1 338 ? 8.142   18.960  33.961  1.00 60.22  ? 338 THR A O   1 
ATOM 2511 C CB  . THR A 1 338 ? 5.288   17.328  34.625  1.00 58.22  ? 338 THR A CB  1 
ATOM 2512 O OG1 . THR A 1 338 ? 6.073   17.338  35.823  1.00 60.58  ? 338 THR A OG1 1 
ATOM 2513 C CG2 . THR A 1 338 ? 4.678   15.951  34.437  1.00 56.74  ? 338 THR A CG2 1 
ATOM 2514 N N   . CYS A 1 339 ? 6.235   20.096  33.614  1.00 63.74  ? 339 CYS A N   1 
ATOM 2515 C CA  . CYS A 1 339 ? 6.890   21.386  33.771  1.00 63.49  ? 339 CYS A CA  1 
ATOM 2516 C C   . CYS A 1 339 ? 7.354   21.566  35.211  1.00 66.38  ? 339 CYS A C   1 
ATOM 2517 O O   . CYS A 1 339 ? 6.540   21.798  36.109  1.00 71.03  ? 339 CYS A O   1 
ATOM 2518 C CB  . CYS A 1 339 ? 5.948   22.513  33.361  1.00 66.15  ? 339 CYS A CB  1 
ATOM 2519 S SG  . CYS A 1 339 ? 5.449   22.448  31.630  1.00 86.89  ? 339 CYS A SG  1 
ATOM 2520 N N   . SER A 1 340 ? 8.661   21.454  35.430  1.00 53.30  ? 340 SER A N   1 
ATOM 2521 C CA  . SER A 1 340 ? 9.241   21.680  36.748  1.00 45.98  ? 340 SER A CA  1 
ATOM 2522 C C   . SER A 1 340 ? 9.321   23.180  36.984  1.00 52.58  ? 340 SER A C   1 
ATOM 2523 O O   . SER A 1 340 ? 10.059  23.886  36.292  1.00 64.47  ? 340 SER A O   1 
ATOM 2524 C CB  . SER A 1 340 ? 10.618  21.033  36.850  1.00 48.44  ? 340 SER A CB  1 
ATOM 2525 O OG  . SER A 1 340 ? 11.636  21.940  36.474  1.00 55.96  ? 340 SER A OG  1 
ATOM 2526 N N   . THR A 1 341 ? 8.556   23.671  37.947  1.00 56.82  ? 341 THR A N   1 
ATOM 2527 C CA  . THR A 1 341 ? 8.506   25.087  38.270  1.00 56.71  ? 341 THR A CA  1 
ATOM 2528 C C   . THR A 1 341 ? 8.564   25.267  39.783  1.00 56.21  ? 341 THR A C   1 
ATOM 2529 O O   . THR A 1 341 ? 8.570   24.302  40.549  1.00 56.37  ? 341 THR A O   1 
ATOM 2530 C CB  . THR A 1 341 ? 7.246   25.733  37.686  1.00 64.99  ? 341 THR A CB  1 
ATOM 2531 O OG1 . THR A 1 341 ? 7.233   27.133  37.995  1.00 68.73  ? 341 THR A OG1 1 
ATOM 2532 C CG2 . THR A 1 341 ? 6.002   25.078  38.259  1.00 55.30  ? 341 THR A CG2 1 
ATOM 2533 N N   . GLY A 1 342 ? 8.606   26.525  40.209  1.00 58.17  ? 342 GLY A N   1 
ATOM 2534 C CA  . GLY A 1 342 ? 8.663   26.832  41.621  1.00 50.31  ? 342 GLY A CA  1 
ATOM 2535 C C   . GLY A 1 342 ? 7.298   27.018  42.245  1.00 52.05  ? 342 GLY A C   1 
ATOM 2536 O O   . GLY A 1 342 ? 6.283   27.033  41.544  1.00 60.00  ? 342 GLY A O   1 
ATOM 2537 N N   . GLY A 1 343 ? 7.263   27.157  43.566  1.00 51.10  ? 343 GLY A N   1 
ATOM 2538 C CA  . GLY A 1 343 ? 6.022   27.400  44.267  1.00 50.40  ? 343 GLY A CA  1 
ATOM 2539 C C   . GLY A 1 343 ? 5.247   26.170  44.674  1.00 53.58  ? 343 GLY A C   1 
ATOM 2540 O O   . GLY A 1 343 ? 4.203   26.308  45.323  1.00 64.59  ? 343 GLY A O   1 
ATOM 2541 N N   . GLN A 1 344 ? 5.719   24.975  44.317  1.00 49.14  ? 344 GLN A N   1 
ATOM 2542 C CA  . GLN A 1 344 ? 5.091   23.721  44.722  1.00 49.33  ? 344 GLN A CA  1 
ATOM 2543 C C   . GLN A 1 344 ? 3.620   23.666  44.330  1.00 49.73  ? 344 GLN A C   1 
ATOM 2544 O O   . GLN A 1 344 ? 2.755   23.417  45.175  1.00 49.71  ? 344 GLN A O   1 
ATOM 2545 C CB  . GLN A 1 344 ? 5.242   23.514  46.230  1.00 42.34  ? 344 GLN A CB  1 
ATOM 2546 C CG  . GLN A 1 344 ? 6.618   23.042  46.645  1.00 46.84  ? 344 GLN A CG  1 
ATOM 2547 C CD  . GLN A 1 344 ? 7.222   23.889  47.740  1.00 53.91  ? 344 GLN A CD  1 
ATOM 2548 O OE1 . GLN A 1 344 ? 6.634   24.878  48.172  1.00 62.52  ? 344 GLN A OE1 1 
ATOM 2549 N NE2 . GLN A 1 344 ? 8.403   23.503  48.202  1.00 56.06  ? 344 GLN A NE2 1 
ATOM 2550 N N   . GLY A 1 345 ? 3.328   23.896  43.055  1.00 58.79  ? 345 GLY A N   1 
ATOM 2551 C CA  . GLY A 1 345 ? 1.973   23.858  42.545  1.00 54.65  ? 345 GLY A CA  1 
ATOM 2552 C C   . GLY A 1 345 ? 1.289   25.203  42.472  1.00 57.15  ? 345 GLY A C   1 
ATOM 2553 O O   . GLY A 1 345 ? 0.216   25.297  41.864  1.00 63.13  ? 345 GLY A O   1 
ATOM 2554 N N   . SER A 1 346 ? 1.865   26.244  43.069  1.00 49.74  ? 346 SER A N   1 
ATOM 2555 C CA  . SER A 1 346 ? 1.288   27.578  43.006  1.00 50.99  ? 346 SER A CA  1 
ATOM 2556 C C   . SER A 1 346 ? 1.510   28.258  41.664  1.00 61.05  ? 346 SER A C   1 
ATOM 2557 O O   . SER A 1 346 ? 0.762   29.179  41.322  1.00 63.16  ? 346 SER A O   1 
ATOM 2558 C CB  . SER A 1 346 ? 1.867   28.457  44.116  1.00 54.64  ? 346 SER A CB  1 
ATOM 2559 O OG  . SER A 1 346 ? 3.227   28.752  43.868  1.00 64.36  ? 346 SER A OG  1 
ATOM 2560 N N   . GLY A 1 347 ? 2.512   27.830  40.901  1.00 57.44  ? 347 GLY A N   1 
ATOM 2561 C CA  . GLY A 1 347 ? 2.791   28.426  39.612  1.00 53.50  ? 347 GLY A CA  1 
ATOM 2562 C C   . GLY A 1 347 ? 2.865   27.404  38.499  1.00 61.07  ? 347 GLY A C   1 
ATOM 2563 O O   . GLY A 1 347 ? 3.005   26.205  38.757  1.00 62.48  ? 347 GLY A O   1 
ATOM 2564 N N   . GLY A 1 348 ? 2.768   27.868  37.256  1.00 67.19  ? 348 GLY A N   1 
ATOM 2565 C CA  . GLY A 1 348 ? 2.796   26.982  36.110  1.00 61.59  ? 348 GLY A CA  1 
ATOM 2566 C C   . GLY A 1 348 ? 1.630   26.017  36.082  1.00 61.10  ? 348 GLY A C   1 
ATOM 2567 O O   . GLY A 1 348 ? 1.789   24.855  35.699  1.00 63.78  ? 348 GLY A O   1 
ATOM 2568 N N   . VAL A 1 349 ? 0.450   26.488  36.490  1.00 58.52  ? 349 VAL A N   1 
ATOM 2569 C CA  . VAL A 1 349 ? -0.729  25.628  36.494  1.00 57.53  ? 349 VAL A CA  1 
ATOM 2570 C C   . VAL A 1 349 ? -1.133  25.265  35.071  1.00 60.47  ? 349 VAL A C   1 
ATOM 2571 O O   . VAL A 1 349 ? -1.357  24.090  34.757  1.00 67.37  ? 349 VAL A O   1 
ATOM 2572 C CB  . VAL A 1 349 ? -1.880  26.310  37.254  1.00 54.78  ? 349 VAL A CB  1 
ATOM 2573 C CG1 . VAL A 1 349 ? -3.148  25.483  37.150  1.00 57.47  ? 349 VAL A CG1 1 
ATOM 2574 C CG2 . VAL A 1 349 ? -1.497  26.528  38.707  1.00 57.45  ? 349 VAL A CG2 1 
ATOM 2575 N N   . VAL A 1 350 ? -1.223  26.261  34.189  1.00 61.26  ? 350 VAL A N   1 
ATOM 2576 C CA  . VAL A 1 350 ? -1.544  25.992  32.791  1.00 59.37  ? 350 VAL A CA  1 
ATOM 2577 C C   . VAL A 1 350 ? -0.419  25.209  32.129  1.00 59.93  ? 350 VAL A C   1 
ATOM 2578 O O   . VAL A 1 350 ? -0.660  24.281  31.345  1.00 64.70  ? 350 VAL A O   1 
ATOM 2579 C CB  . VAL A 1 350 ? -1.835  27.309  32.051  1.00 57.49  ? 350 VAL A CB  1 
ATOM 2580 C CG1 . VAL A 1 350 ? -2.184  27.039  30.600  1.00 60.70  ? 350 VAL A CG1 1 
ATOM 2581 C CG2 . VAL A 1 350 ? -2.953  28.066  32.744  1.00 58.19  ? 350 VAL A CG2 1 
ATOM 2582 N N   . ALA A 1 351 ? 0.829   25.574  32.433  1.00 57.47  ? 351 ALA A N   1 
ATOM 2583 C CA  . ALA A 1 351 ? 1.970   24.847  31.893  1.00 56.94  ? 351 ALA A CA  1 
ATOM 2584 C C   . ALA A 1 351 ? 1.942   23.385  32.297  1.00 57.10  ? 351 ALA A C   1 
ATOM 2585 O O   . ALA A 1 351 ? 2.193   22.508  31.467  1.00 61.37  ? 351 ALA A O   1 
ATOM 2586 C CB  . ALA A 1 351 ? 3.272   25.497  32.355  1.00 50.45  ? 351 ALA A CB  1 
ATOM 2587 N N   . ASN A 1 352 ? 1.616   23.098  33.556  1.00 59.15  ? 352 ASN A N   1 
ATOM 2588 C CA  . ASN A 1 352 ? 1.580   21.714  34.003  1.00 51.33  ? 352 ASN A CA  1 
ATOM 2589 C C   . ASN A 1 352 ? 0.349   20.971  33.500  1.00 53.89  ? 352 ASN A C   1 
ATOM 2590 O O   . ASN A 1 352 ? 0.413   19.756  33.305  1.00 62.55  ? 352 ASN A O   1 
ATOM 2591 C CB  . ASN A 1 352 ? 1.656   21.659  35.523  1.00 58.88  ? 352 ASN A CB  1 
ATOM 2592 C CG  . ASN A 1 352 ? 3.082   21.657  36.030  1.00 60.47  ? 352 ASN A CG  1 
ATOM 2593 O OD1 . ASN A 1 352 ? 3.918   20.891  35.552  1.00 52.60  ? 352 ASN A OD1 1 
ATOM 2594 N ND2 . ASN A 1 352 ? 3.369   22.513  37.001  1.00 64.85  ? 352 ASN A ND2 1 
ATOM 2595 N N   . LEU A 1 353 ? -0.771  21.663  33.280  1.00 52.92  ? 353 LEU A N   1 
ATOM 2596 C CA  . LEU A 1 353 ? -1.900  21.024  32.610  1.00 51.89  ? 353 LEU A CA  1 
ATOM 2597 C C   . LEU A 1 353 ? -1.516  20.587  31.204  1.00 56.97  ? 353 LEU A C   1 
ATOM 2598 O O   . LEU A 1 353 ? -1.790  19.448  30.792  1.00 65.86  ? 353 LEU A O   1 
ATOM 2599 C CB  . LEU A 1 353 ? -3.091  21.979  32.564  1.00 48.10  ? 353 LEU A CB  1 
ATOM 2600 C CG  . LEU A 1 353 ? -3.880  22.183  33.856  1.00 55.94  ? 353 LEU A CG  1 
ATOM 2601 C CD1 . LEU A 1 353 ? -4.794  23.386  33.727  1.00 54.31  ? 353 LEU A CD1 1 
ATOM 2602 C CD2 . LEU A 1 353 ? -4.682  20.939  34.187  1.00 57.13  ? 353 LEU A CD2 1 
ATOM 2603 N N   . TRP A 1 354 ? -0.861  21.479  30.457  1.00 55.73  ? 354 TRP A N   1 
ATOM 2604 C CA  . TRP A 1 354 ? -0.388  21.120  29.126  1.00 52.91  ? 354 TRP A CA  1 
ATOM 2605 C C   . TRP A 1 354 ? 0.647   20.006  29.199  1.00 57.19  ? 354 TRP A C   1 
ATOM 2606 O O   . TRP A 1 354 ? 0.684   19.131  28.330  1.00 60.41  ? 354 TRP A O   1 
ATOM 2607 C CB  . TRP A 1 354 ? 0.195   22.344  28.420  1.00 59.97  ? 354 TRP A CB  1 
ATOM 2608 C CG  . TRP A 1 354 ? -0.780  23.460  28.193  1.00 59.73  ? 354 TRP A CG  1 
ATOM 2609 C CD1 . TRP A 1 354 ? -2.052  23.555  28.674  1.00 59.20  ? 354 TRP A CD1 1 
ATOM 2610 C CD2 . TRP A 1 354 ? -0.560  24.638  27.411  1.00 63.46  ? 354 TRP A CD2 1 
ATOM 2611 N NE1 . TRP A 1 354 ? -2.634  24.722  28.248  1.00 60.51  ? 354 TRP A NE1 1 
ATOM 2612 C CE2 . TRP A 1 354 ? -1.738  25.405  27.469  1.00 66.58  ? 354 TRP A CE2 1 
ATOM 2613 C CE3 . TRP A 1 354 ? 0.522   25.118  26.667  1.00 60.59  ? 354 TRP A CE3 1 
ATOM 2614 C CZ2 . TRP A 1 354 ? -1.865  26.626  26.815  1.00 64.53  ? 354 TRP A CZ2 1 
ATOM 2615 C CZ3 . TRP A 1 354 ? 0.393   26.329  26.018  1.00 58.31  ? 354 TRP A CZ3 1 
ATOM 2616 C CH2 . TRP A 1 354 ? -0.791  27.070  26.097  1.00 59.14  ? 354 TRP A CH2 1 
ATOM 2617 N N   . ALA A 1 355 ? 1.495   20.024  30.228  1.00 58.66  ? 355 ALA A N   1 
ATOM 2618 C CA  . ALA A 1 355 ? 2.503   18.981  30.385  1.00 55.28  ? 355 ALA A CA  1 
ATOM 2619 C C   . ALA A 1 355 ? 1.866   17.627  30.674  1.00 65.10  ? 355 ALA A C   1 
ATOM 2620 O O   . ALA A 1 355 ? 2.341   16.599  30.188  1.00 70.24  ? 355 ALA A O   1 
ATOM 2621 C CB  . ALA A 1 355 ? 3.483   19.361  31.494  1.00 54.01  ? 355 ALA A CB  1 
ATOM 2622 N N   . LYS A 1 356 ? 0.804   17.603  31.480  1.00 57.26  ? 356 LYS A N   1 
ATOM 2623 C CA  . LYS A 1 356 ? 0.095   16.352  31.731  1.00 54.26  ? 356 LYS A CA  1 
ATOM 2624 C C   . LYS A 1 356 ? -0.562  15.830  30.460  1.00 59.60  ? 356 LYS A C   1 
ATOM 2625 O O   . LYS A 1 356 ? -0.511  14.624  30.173  1.00 71.77  ? 356 LYS A O   1 
ATOM 2626 C CB  . LYS A 1 356 ? -0.949  16.547  32.829  1.00 60.71  ? 356 LYS A CB  1 
ATOM 2627 C CG  . LYS A 1 356 ? -0.414  16.357  34.236  1.00 58.64  ? 356 LYS A CG  1 
ATOM 2628 C CD  . LYS A 1 356 ? -1.461  15.724  35.136  1.00 61.90  ? 356 LYS A CD  1 
ATOM 2629 C CE  . LYS A 1 356 ? -1.403  16.300  36.540  1.00 68.16  ? 356 LYS A CE  1 
ATOM 2630 N NZ  . LYS A 1 356 ? -1.531  15.243  37.581  1.00 66.52  ? 356 LYS A NZ  1 
ATOM 2631 N N   . ARG A 1 357 ? -1.183  16.724  29.684  1.00 55.92  ? 357 ARG A N   1 
ATOM 2632 C CA  . ARG A 1 357 ? -1.744  16.304  28.403  1.00 59.32  ? 357 ARG A CA  1 
ATOM 2633 C C   . ARG A 1 357 ? -0.656  15.757  27.486  1.00 60.95  ? 357 ARG A C   1 
ATOM 2634 O O   . ARG A 1 357 ? -0.851  14.735  26.816  1.00 62.09  ? 357 ARG A O   1 
ATOM 2635 C CB  . ARG A 1 357 ? -2.473  17.470  27.738  1.00 57.95  ? 357 ARG A CB  1 
ATOM 2636 C CG  . ARG A 1 357 ? -3.391  17.044  26.610  1.00 57.55  ? 357 ARG A CG  1 
ATOM 2637 C CD  . ARG A 1 357 ? -4.242  18.186  26.094  1.00 58.58  ? 357 ARG A CD  1 
ATOM 2638 N NE  . ARG A 1 357 ? -4.833  17.858  24.802  1.00 65.00  ? 357 ARG A NE  1 
ATOM 2639 C CZ  . ARG A 1 357 ? -4.996  18.721  23.808  1.00 62.47  ? 357 ARG A CZ  1 
ATOM 2640 N NH1 . ARG A 1 357 ? -4.635  19.986  23.926  1.00 67.00  ? 357 ARG A NH1 1 
ATOM 2641 N NH2 . ARG A 1 357 ? -5.535  18.302  22.668  1.00 66.49  ? 357 ARG A NH2 1 
ATOM 2642 N N   . MET A 1 358 ? 0.501   16.418  27.462  1.00 60.61  ? 358 MET A N   1 
ATOM 2643 C CA  . MET A 1 358 ? 1.614   15.972  26.632  1.00 53.35  ? 358 MET A CA  1 
ATOM 2644 C C   . MET A 1 358 ? 2.139   14.622  27.101  1.00 60.60  ? 358 MET A C   1 
ATOM 2645 O O   . MET A 1 358 ? 2.524   13.781  26.285  1.00 66.01  ? 358 MET A O   1 
ATOM 2646 C CB  . MET A 1 358 ? 2.711   17.042  26.640  1.00 58.13  ? 358 MET A CB  1 
ATOM 2647 C CG  . MET A 1 358 ? 4.052   16.664  26.015  1.00 67.83  ? 358 MET A CG  1 
ATOM 2648 S SD  . MET A 1 358 ? 5.125   15.568  26.966  1.00 78.77  ? 358 MET A SD  1 
ATOM 2649 C CE  . MET A 1 358 ? 5.234   16.463  28.512  1.00 59.10  ? 358 MET A CE  1 
ATOM 2650 N N   . ARG A 1 359 ? 2.187   14.406  28.416  1.00 59.10  ? 359 ARG A N   1 
ATOM 2651 C CA  . ARG A 1 359 ? 2.630   13.122  28.948  1.00 57.92  ? 359 ARG A CA  1 
ATOM 2652 C C   . ARG A 1 359 ? 1.689   12.002  28.533  1.00 58.62  ? 359 ARG A C   1 
ATOM 2653 O O   . ARG A 1 359 ? 2.134   10.923  28.114  1.00 68.11  ? 359 ARG A O   1 
ATOM 2654 C CB  . ARG A 1 359 ? 2.729   13.193  30.471  1.00 60.63  ? 359 ARG A CB  1 
ATOM 2655 C CG  . ARG A 1 359 ? 3.400   11.988  31.101  1.00 63.86  ? 359 ARG A CG  1 
ATOM 2656 C CD  . ARG A 1 359 ? 3.291   12.010  32.615  1.00 61.94  ? 359 ARG A CD  1 
ATOM 2657 N NE  . ARG A 1 359 ? 1.920   12.206  33.066  1.00 66.06  ? 359 ARG A NE  1 
ATOM 2658 C CZ  . ARG A 1 359 ? 1.585   12.723  34.239  1.00 64.60  ? 359 ARG A CZ  1 
ATOM 2659 N NH1 . ARG A 1 359 ? 2.501   13.100  35.114  1.00 61.93  ? 359 ARG A NH1 1 
ATOM 2660 N NH2 . ARG A 1 359 ? 0.298   12.861  34.544  1.00 67.60  ? 359 ARG A NH2 1 
ATOM 2661 N N   . MET A 1 360 ? 0.380   12.238  28.633  1.00 57.39  ? 360 MET A N   1 
ATOM 2662 C CA  . MET A 1 360 ? -0.553  11.206  28.203  1.00 61.97  ? 360 MET A CA  1 
ATOM 2663 C C   . MET A 1 360 ? -0.428  10.956  26.704  1.00 68.22  ? 360 MET A C   1 
ATOM 2664 O O   . MET A 1 360 ? -0.490  9.806   26.256  1.00 71.90  ? 360 MET A O   1 
ATOM 2665 C CB  . MET A 1 360 ? -1.988  11.570  28.574  1.00 62.13  ? 360 MET A CB  1 
ATOM 2666 C CG  . MET A 1 360 ? -3.007  10.678  27.884  1.00 66.06  ? 360 MET A CG  1 
ATOM 2667 S SD  . MET A 1 360 ? -4.414  10.225  28.908  1.00 81.28  ? 360 MET A SD  1 
ATOM 2668 C CE  . MET A 1 360 ? -5.041  8.819   27.996  1.00 65.44  ? 360 MET A CE  1 
ATOM 2669 N N   . MET A 1 361 ? -0.229  12.016  25.913  1.00 60.99  ? 361 MET A N   1 
ATOM 2670 C CA  . MET A 1 361 ? -0.009  11.821  24.482  1.00 56.02  ? 361 MET A CA  1 
ATOM 2671 C C   . MET A 1 361 ? 1.244   10.990  24.233  1.00 65.18  ? 361 MET A C   1 
ATOM 2672 O O   . MET A 1 361 ? 1.236   10.075  23.404  1.00 68.76  ? 361 MET A O   1 
ATOM 2673 C CB  . MET A 1 361 ? 0.114   13.164  23.764  1.00 64.21  ? 361 MET A CB  1 
ATOM 2674 C CG  . MET A 1 361 ? 0.905   13.076  22.456  1.00 64.73  ? 361 MET A CG  1 
ATOM 2675 S SD  . MET A 1 361 ? 2.617   13.646  22.514  1.00 71.90  ? 361 MET A SD  1 
ATOM 2676 C CE  . MET A 1 361 ? 2.426   15.317  23.111  1.00 64.80  ? 361 MET A CE  1 
ATOM 2677 N N   . ALA A 1 362 ? 2.329   11.298  24.945  1.00 60.93  ? 362 ALA A N   1 
ATOM 2678 C CA  . ALA A 1 362 ? 3.579   10.568  24.790  1.00 61.07  ? 362 ALA A CA  1 
ATOM 2679 C C   . ALA A 1 362 ? 3.446   9.117   25.214  1.00 64.63  ? 362 ALA A C   1 
ATOM 2680 O O   . ALA A 1 362 ? 4.253   8.283   24.788  1.00 67.39  ? 362 ALA A O   1 
ATOM 2681 C CB  . ALA A 1 362 ? 4.684   11.250  25.595  1.00 57.37  ? 362 ALA A CB  1 
ATOM 2682 N N   . ASP A 1 363 ? 2.459   8.802   26.055  1.00 68.04  ? 363 ASP A N   1 
ATOM 2683 C CA  . ASP A 1 363 ? 2.171   7.397   26.331  1.00 66.01  ? 363 ASP A CA  1 
ATOM 2684 C C   . ASP A 1 363 ? 1.870   6.624   25.052  1.00 70.56  ? 363 ASP A C   1 
ATOM 2685 O O   . ASP A 1 363 ? 2.133   5.418   24.983  1.00 75.27  ? 363 ASP A O   1 
ATOM 2686 C CB  . ASP A 1 363 ? 0.997   7.259   27.297  1.00 68.39  ? 363 ASP A CB  1 
ATOM 2687 C CG  . ASP A 1 363 ? 0.739   5.816   27.683  1.00 74.97  ? 363 ASP A CG  1 
ATOM 2688 O OD1 . ASP A 1 363 ? 1.710   5.109   28.020  1.00 74.16  ? 363 ASP A OD1 1 
ATOM 2689 O OD2 . ASP A 1 363 ? -0.426  5.377   27.608  1.00 77.39  ? 363 ASP A OD2 1 
ATOM 2690 N N   . THR A 1 364 ? 1.311   7.291   24.038  1.00 68.30  ? 364 THR A N   1 
ATOM 2691 C CA  . THR A 1 364 ? 1.090   6.635   22.752  1.00 71.09  ? 364 THR A CA  1 
ATOM 2692 C C   . THR A 1 364 ? 2.395   6.125   22.160  1.00 69.22  ? 364 THR A C   1 
ATOM 2693 O O   . THR A 1 364 ? 2.434   5.030   21.588  1.00 73.96  ? 364 THR A O   1 
ATOM 2694 C CB  . THR A 1 364 ? 0.412   7.597   21.772  1.00 70.47  ? 364 THR A CB  1 
ATOM 2695 O OG1 . THR A 1 364 ? -0.902  7.916   22.241  1.00 80.78  ? 364 THR A OG1 1 
ATOM 2696 C CG2 . THR A 1 364 ? 0.312   6.980   20.388  1.00 69.93  ? 364 THR A CG2 1 
ATOM 2697 N N   . TYR A 1 365 ? 3.472   6.891   22.303  1.00 65.26  ? 365 TYR A N   1 
ATOM 2698 C CA  . TYR A 1 365 ? 4.772   6.510   21.783  1.00 63.87  ? 365 TYR A CA  1 
ATOM 2699 C C   . TYR A 1 365 ? 5.597   5.703   22.772  1.00 63.71  ? 365 TYR A C   1 
ATOM 2700 O O   . TYR A 1 365 ? 6.793   5.501   22.534  1.00 70.40  ? 365 TYR A O   1 
ATOM 2701 C CB  . TYR A 1 365 ? 5.554   7.762   21.362  1.00 63.17  ? 365 TYR A CB  1 
ATOM 2702 C CG  . TYR A 1 365 ? 4.829   8.577   20.319  1.00 64.43  ? 365 TYR A CG  1 
ATOM 2703 C CD1 . TYR A 1 365 ? 4.763   8.151   19.002  1.00 62.78  ? 365 TYR A CD1 1 
ATOM 2704 C CD2 . TYR A 1 365 ? 4.195   9.763   20.656  1.00 70.12  ? 365 TYR A CD2 1 
ATOM 2705 C CE1 . TYR A 1 365 ? 4.096   8.887   18.047  1.00 69.74  ? 365 TYR A CE1 1 
ATOM 2706 C CE2 . TYR A 1 365 ? 3.525   10.508  19.706  1.00 68.40  ? 365 TYR A CE2 1 
ATOM 2707 C CZ  . TYR A 1 365 ? 3.479   10.064  18.403  1.00 70.04  ? 365 TYR A CZ  1 
ATOM 2708 O OH  . TYR A 1 365 ? 2.813   10.798  17.449  1.00 75.05  ? 365 TYR A OH  1 
ATOM 2709 N N   . GLY A 1 366 ? 4.999   5.243   23.867  1.00 63.43  ? 366 GLY A N   1 
ATOM 2710 C CA  . GLY A 1 366 ? 5.722   4.462   24.848  1.00 66.16  ? 366 GLY A CA  1 
ATOM 2711 C C   . GLY A 1 366 ? 6.770   5.234   25.608  1.00 66.57  ? 366 GLY A C   1 
ATOM 2712 O O   . GLY A 1 366 ? 7.710   4.629   26.137  1.00 69.39  ? 366 GLY A O   1 
ATOM 2713 N N   . CYS A 1 367 ? 6.641   6.553   25.684  1.00 66.31  ? 367 CYS A N   1 
ATOM 2714 C CA  . CYS A 1 367 ? 7.652   7.394   26.304  1.00 68.01  ? 367 CYS A CA  1 
ATOM 2715 C C   . CYS A 1 367 ? 7.633   7.232   27.816  1.00 68.49  ? 367 CYS A C   1 
ATOM 2716 O O   . CYS A 1 367 ? 6.572   7.263   28.444  1.00 70.27  ? 367 CYS A O   1 
ATOM 2717 C CB  . CYS A 1 367 ? 7.429   8.861   25.938  1.00 65.04  ? 367 CYS A CB  1 
ATOM 2718 S SG  . CYS A 1 367 ? 7.491   9.205   24.169  1.00 83.47  ? 367 CYS A SG  1 
ATOM 2719 N N   . ALA A 1 368 ? 8.817   7.054   28.392  1.00 59.86  ? 368 ALA A N   1 
ATOM 2720 C CA  . ALA A 1 368 ? 8.952   7.129   29.837  1.00 58.68  ? 368 ALA A CA  1 
ATOM 2721 C C   . ALA A 1 368 ? 8.688   8.556   30.294  1.00 62.62  ? 368 ALA A C   1 
ATOM 2722 O O   . ALA A 1 368 ? 8.879   9.511   29.537  1.00 70.69  ? 368 ALA A O   1 
ATOM 2723 C CB  . ALA A 1 368 ? 10.345  6.679   30.270  1.00 56.66  ? 368 ALA A CB  1 
ATOM 2724 N N   . HIS A 1 369 ? 8.231   8.704   31.529  1.00 54.19  ? 369 HIS A N   1 
ATOM 2725 C CA  . HIS A 1 369 ? 7.870   10.011  32.046  1.00 50.26  ? 369 HIS A CA  1 
ATOM 2726 C C   . HIS A 1 369 ? 8.517   10.238  33.403  1.00 54.26  ? 369 HIS A C   1 
ATOM 2727 O O   . HIS A 1 369 ? 8.773   9.302   34.164  1.00 59.57  ? 369 HIS A O   1 
ATOM 2728 C CB  . HIS A 1 369 ? 6.351   10.164  32.166  1.00 50.34  ? 369 HIS A CB  1 
ATOM 2729 C CG  . HIS A 1 369 ? 5.737   9.280   33.203  1.00 54.11  ? 369 HIS A CG  1 
ATOM 2730 N ND1 . HIS A 1 369 ? 5.534   9.690   34.503  1.00 54.53  ? 369 HIS A ND1 1 
ATOM 2731 C CD2 . HIS A 1 369 ? 5.289   8.005   33.137  1.00 54.05  ? 369 HIS A CD2 1 
ATOM 2732 C CE1 . HIS A 1 369 ? 4.982   8.707   35.191  1.00 60.98  ? 369 HIS A CE1 1 
ATOM 2733 N NE2 . HIS A 1 369 ? 4.824   7.673   34.385  1.00 60.31  ? 369 HIS A NE2 1 
ATOM 2734 N N   . PHE A 1 370 ? 8.788   11.508  33.690  1.00 48.11  ? 370 PHE A N   1 
ATOM 2735 C CA  . PHE A 1 370 ? 9.298   11.933  34.984  1.00 45.43  ? 370 PHE A CA  1 
ATOM 2736 C C   . PHE A 1 370 ? 8.450   13.098  35.462  1.00 47.20  ? 370 PHE A C   1 
ATOM 2737 O O   . PHE A 1 370 ? 8.401   14.142  34.805  1.00 52.79  ? 370 PHE A O   1 
ATOM 2738 C CB  . PHE A 1 370 ? 10.770  12.340  34.895  1.00 42.73  ? 370 PHE A CB  1 
ATOM 2739 C CG  . PHE A 1 370 ? 11.357  12.768  36.206  1.00 46.08  ? 370 PHE A CG  1 
ATOM 2740 C CD1 . PHE A 1 370 ? 11.645  11.838  37.187  1.00 42.59  ? 370 PHE A CD1 1 
ATOM 2741 C CD2 . PHE A 1 370 ? 11.617  14.102  36.459  1.00 45.56  ? 370 PHE A CD2 1 
ATOM 2742 C CE1 . PHE A 1 370 ? 12.184  12.231  38.391  1.00 41.37  ? 370 PHE A CE1 1 
ATOM 2743 C CE2 . PHE A 1 370 ? 12.153  14.499  37.662  1.00 45.93  ? 370 PHE A CE2 1 
ATOM 2744 C CZ  . PHE A 1 370 ? 12.437  13.562  38.629  1.00 47.25  ? 370 PHE A CZ  1 
ATOM 2745 N N   . ASN A 1 371 ? 7.782   12.922  36.597  1.00 58.59  ? 371 ASN A N   1 
ATOM 2746 C CA  . ASN A 1 371 ? 6.961   13.985  37.166  1.00 54.23  ? 371 ASN A CA  1 
ATOM 2747 C C   . ASN A 1 371 ? 7.908   15.019  37.756  1.00 54.72  ? 371 ASN A C   1 
ATOM 2748 O O   . ASN A 1 371 ? 8.259   14.980  38.935  1.00 59.92  ? 371 ASN A O   1 
ATOM 2749 C CB  . ASN A 1 371 ? 5.995   13.430  38.202  1.00 55.00  ? 371 ASN A CB  1 
ATOM 2750 C CG  . ASN A 1 371 ? 4.869   12.638  37.578  1.00 61.47  ? 371 ASN A CG  1 
ATOM 2751 O OD1 . ASN A 1 371 ? 4.459   12.906  36.450  1.00 68.77  ? 371 ASN A OD1 1 
ATOM 2752 N ND2 . ASN A 1 371 ? 4.361   11.655  38.309  1.00 68.11  ? 371 ASN A ND2 1 
ATOM 2753 N N   . ALA A 1 372 ? 8.339   15.950  36.907  1.00 48.54  ? 372 ALA A N   1 
ATOM 2754 C CA  . ALA A 1 372 ? 9.328   16.939  37.306  1.00 43.63  ? 372 ALA A CA  1 
ATOM 2755 C C   . ALA A 1 372 ? 8.750   18.012  38.215  1.00 53.09  ? 372 ALA A C   1 
ATOM 2756 O O   . ALA A 1 372 ? 9.510   18.701  38.901  1.00 60.85  ? 372 ALA A O   1 
ATOM 2757 C CB  . ALA A 1 372 ? 9.934   17.582  36.064  1.00 47.19  ? 372 ALA A CB  1 
ATOM 2758 N N   . ASP A 1 373 ? 7.427   18.172  38.234  1.00 51.62  ? 373 ASP A N   1 
ATOM 2759 C CA  . ASP A 1 373 ? 6.816   19.220  39.038  1.00 53.19  ? 373 ASP A CA  1 
ATOM 2760 C C   . ASP A 1 373 ? 6.880   18.927  40.531  1.00 58.46  ? 373 ASP A C   1 
ATOM 2761 O O   . ASP A 1 373 ? 6.793   19.860  41.335  1.00 67.45  ? 373 ASP A O   1 
ATOM 2762 C CB  . ASP A 1 373 ? 5.363   19.420  38.611  1.00 61.85  ? 373 ASP A CB  1 
ATOM 2763 C CG  . ASP A 1 373 ? 4.616   18.112  38.469  1.00 67.44  ? 373 ASP A CG  1 
ATOM 2764 O OD1 . ASP A 1 373 ? 5.223   17.127  38.003  1.00 73.89  ? 373 ASP A OD1 1 
ATOM 2765 O OD2 . ASP A 1 373 ? 3.422   18.066  38.823  1.00 72.07  ? 373 ASP A OD2 1 
ATOM 2766 N N   . GLU A 1 374 ? 7.036   17.663  40.923  1.00 51.13  ? 374 GLU A N   1 
ATOM 2767 C CA  . GLU A 1 374 ? 6.967   17.272  42.324  1.00 55.17  ? 374 GLU A CA  1 
ATOM 2768 C C   . GLU A 1 374 ? 8.340   17.065  42.953  1.00 59.16  ? 374 GLU A C   1 
ATOM 2769 O O   . GLU A 1 374 ? 8.430   16.519  44.057  1.00 66.40  ? 374 GLU A O   1 
ATOM 2770 C CB  . GLU A 1 374 ? 6.130   16.003  42.480  1.00 57.67  ? 374 GLU A CB  1 
ATOM 2771 C CG  . GLU A 1 374 ? 6.370   14.952  41.427  1.00 62.61  ? 374 GLU A CG  1 
ATOM 2772 C CD  . GLU A 1 374 ? 5.369   13.819  41.499  1.00 71.06  ? 374 GLU A CD  1 
ATOM 2773 O OE1 . GLU A 1 374 ? 5.795   12.653  41.621  1.00 69.05  ? 374 GLU A OE1 1 
ATOM 2774 O OE2 . GLU A 1 374 ? 4.153   14.095  41.429  1.00 74.27  ? 374 GLU A OE2 1 
ATOM 2775 N N   . VAL A 1 375 ? 9.411   17.487  42.280  1.00 53.96  ? 375 VAL A N   1 
ATOM 2776 C CA  . VAL A 1 375 ? 10.746  17.273  42.830  1.00 46.77  ? 375 VAL A CA  1 
ATOM 2777 C C   . VAL A 1 375 ? 11.061  18.219  43.982  1.00 46.27  ? 375 VAL A C   1 
ATOM 2778 O O   . VAL A 1 375 ? 11.995  17.954  44.748  1.00 56.55  ? 375 VAL A O   1 
ATOM 2779 C CB  . VAL A 1 375 ? 11.815  17.397  41.732  1.00 42.71  ? 375 VAL A CB  1 
ATOM 2780 C CG1 . VAL A 1 375 ? 11.500  16.453  40.589  1.00 51.32  ? 375 VAL A CG1 1 
ATOM 2781 C CG2 . VAL A 1 375 ? 11.898  18.824  41.228  1.00 52.44  ? 375 VAL A CG2 1 
ATOM 2782 N N   . GLN A 1 376 ? 10.316  19.311  44.136  1.00 49.31  ? 376 GLN A N   1 
ATOM 2783 C CA  . GLN A 1 376 ? 10.529  20.247  45.233  1.00 44.61  ? 376 GLN A CA  1 
ATOM 2784 C C   . GLN A 1 376 ? 9.308   20.333  46.141  1.00 49.01  ? 376 GLN A C   1 
ATOM 2785 O O   . GLN A 1 376 ? 9.202   21.246  46.961  1.00 56.51  ? 376 GLN A O   1 
ATOM 2786 C CB  . GLN A 1 376 ? 10.895  21.635  44.708  1.00 49.32  ? 376 GLN A CB  1 
ATOM 2787 C CG  . GLN A 1 376 ? 11.813  21.635  43.503  1.00 43.31  ? 376 GLN A CG  1 
ATOM 2788 C CD  . GLN A 1 376 ? 13.231  21.238  43.850  1.00 52.76  ? 376 GLN A CD  1 
ATOM 2789 O OE1 . GLN A 1 376 ? 13.637  21.293  45.008  1.00 64.92  ? 376 GLN A OE1 1 
ATOM 2790 N NE2 . GLN A 1 376 ? 13.997  20.842  42.842  1.00 53.38  ? 376 GLN A NE2 1 
ATOM 2791 N N   . TYR A 1 377 ? 8.383   19.385  46.012  1.00 49.57  ? 377 TYR A N   1 
ATOM 2792 C CA  . TYR A 1 377 ? 7.133   19.425  46.757  1.00 47.80  ? 377 TYR A CA  1 
ATOM 2793 C C   . TYR A 1 377 ? 7.326   19.316  48.261  1.00 51.92  ? 377 TYR A C   1 
ATOM 2794 O O   . TYR A 1 377 ? 6.604   19.978  49.014  1.00 64.33  ? 377 TYR A O   1 
ATOM 2795 C CB  . TYR A 1 377 ? 6.200   18.308  46.288  1.00 44.07  ? 377 TYR A CB  1 
ATOM 2796 C CG  . TYR A 1 377 ? 5.310   18.710  45.139  1.00 42.11  ? 377 TYR A CG  1 
ATOM 2797 C CD1 . TYR A 1 377 ? 5.432   19.958  44.549  1.00 43.75  ? 377 TYR A CD1 1 
ATOM 2798 C CD2 . TYR A 1 377 ? 4.345   17.846  44.649  1.00 42.84  ? 377 TYR A CD2 1 
ATOM 2799 C CE1 . TYR A 1 377 ? 4.623   20.331  43.499  1.00 49.80  ? 377 TYR A CE1 1 
ATOM 2800 C CE2 . TYR A 1 377 ? 3.536   18.208  43.594  1.00 49.19  ? 377 TYR A CE2 1 
ATOM 2801 C CZ  . TYR A 1 377 ? 3.676   19.453  43.026  1.00 55.33  ? 377 TYR A CZ  1 
ATOM 2802 O OH  . TYR A 1 377 ? 2.866   19.819  41.979  1.00 59.76  ? 377 TYR A OH  1 
ATOM 2803 N N   . TYR A 1 378 ? 8.275   18.503  48.715  1.00 40.55  ? 378 TYR A N   1 
ATOM 2804 C CA  . TYR A 1 378 ? 8.514   18.289  50.133  1.00 41.21  ? 378 TYR A CA  1 
ATOM 2805 C C   . TYR A 1 378 ? 9.711   19.078  50.639  1.00 42.10  ? 378 TYR A C   1 
ATOM 2806 O O   . TYR A 1 378 ? 10.248  18.766  51.706  1.00 50.74  ? 378 TYR A O   1 
ATOM 2807 C CB  . TYR A 1 378 ? 8.691   16.796  50.406  1.00 45.15  ? 378 TYR A CB  1 
ATOM 2808 C CG  . TYR A 1 378 ? 7.433   16.005  50.151  1.00 41.44  ? 378 TYR A CG  1 
ATOM 2809 C CD1 . TYR A 1 378 ? 6.567   15.690  51.184  1.00 41.71  ? 378 TYR A CD1 1 
ATOM 2810 C CD2 . TYR A 1 378 ? 7.094   15.598  48.868  1.00 42.48  ? 378 TYR A CD2 1 
ATOM 2811 C CE1 . TYR A 1 378 ? 5.413   14.978  50.952  1.00 39.06  ? 378 TYR A CE1 1 
ATOM 2812 C CE2 . TYR A 1 378 ? 5.939   14.891  48.627  1.00 38.89  ? 378 TYR A CE2 1 
ATOM 2813 C CZ  . TYR A 1 378 ? 5.102   14.582  49.674  1.00 43.28  ? 378 TYR A CZ  1 
ATOM 2814 O OH  . TYR A 1 378 ? 3.949   13.872  49.443  1.00 60.17  ? 378 TYR A OH  1 
ATOM 2815 N N   . ARG A 1 379 ? 10.138  20.092  49.897  1.00 42.07  ? 379 ARG A N   1 
ATOM 2816 C CA  . ARG A 1 379 ? 11.284  20.917  50.238  1.00 40.85  ? 379 ARG A CA  1 
ATOM 2817 C C   . ARG A 1 379 ? 10.840  22.343  50.542  1.00 47.63  ? 379 ARG A C   1 
ATOM 2818 O O   . ARG A 1 379 ? 9.708   22.743  50.265  1.00 54.65  ? 379 ARG A O   1 
ATOM 2819 C CB  . ARG A 1 379 ? 12.295  20.914  49.092  1.00 35.54  ? 379 ARG A CB  1 
ATOM 2820 C CG  . ARG A 1 379 ? 12.375  19.595  48.355  1.00 43.09  ? 379 ARG A CG  1 
ATOM 2821 C CD  . ARG A 1 379 ? 13.795  19.289  47.963  1.00 38.22  ? 379 ARG A CD  1 
ATOM 2822 N NE  . ARG A 1 379 ? 13.959  17.931  47.464  1.00 38.65  ? 379 ARG A NE  1 
ATOM 2823 C CZ  . ARG A 1 379 ? 14.827  17.060  47.961  1.00 48.12  ? 379 ARG A CZ  1 
ATOM 2824 N NH1 . ARG A 1 379 ? 15.619  17.376  48.969  1.00 53.09  ? 379 ARG A NH1 1 
ATOM 2825 N NH2 . ARG A 1 379 ? 14.905  15.846  47.429  1.00 47.21  ? 379 ARG A NH2 1 
ATOM 2826 N N   . HIS A 1 380 ? 11.754  23.112  51.122  1.00 55.55  ? 380 HIS A N   1 
ATOM 2827 C CA  . HIS A 1 380 ? 11.520  24.537  51.303  1.00 45.35  ? 380 HIS A CA  1 
ATOM 2828 C C   . HIS A 1 380 ? 11.717  25.258  49.979  1.00 48.75  ? 380 HIS A C   1 
ATOM 2829 O O   . HIS A 1 380 ? 12.735  25.072  49.305  1.00 60.35  ? 380 HIS A O   1 
ATOM 2830 C CB  . HIS A 1 380 ? 12.464  25.107  52.358  1.00 47.05  ? 380 HIS A CB  1 
ATOM 2831 C CG  . HIS A 1 380 ? 12.171  24.641  53.749  1.00 44.82  ? 380 HIS A CG  1 
ATOM 2832 N ND1 . HIS A 1 380 ? 11.160  25.179  54.516  1.00 50.40  ? 380 HIS A ND1 1 
ATOM 2833 C CD2 . HIS A 1 380 ? 12.761  23.694  54.515  1.00 44.63  ? 380 HIS A CD2 1 
ATOM 2834 C CE1 . HIS A 1 380 ? 11.138  24.580  55.693  1.00 52.47  ? 380 HIS A CE1 1 
ATOM 2835 N NE2 . HIS A 1 380 ? 12.098  23.675  55.717  1.00 52.12  ? 380 HIS A NE2 1 
ATOM 2836 N N   . ASN A 1 381 ? 10.739  26.082  49.600  1.00 51.37  ? 381 ASN A N   1 
ATOM 2837 C CA  . ASN A 1 381 ? 10.850  26.827  48.351  1.00 45.99  ? 381 ASN A CA  1 
ATOM 2838 C C   . ASN A 1 381 ? 12.028  27.789  48.378  1.00 47.99  ? 381 ASN A C   1 
ATOM 2839 O O   . ASN A 1 381 ? 12.768  27.888  47.395  1.00 55.30  ? 381 ASN A O   1 
ATOM 2840 C CB  . ASN A 1 381 ? 9.555   27.584  48.075  1.00 57.37  ? 381 ASN A CB  1 
ATOM 2841 C CG  . ASN A 1 381 ? 9.289   27.764  46.597  1.00 57.27  ? 381 ASN A CG  1 
ATOM 2842 O OD1 . ASN A 1 381 ? 9.151   26.792  45.857  1.00 58.13  ? 381 ASN A OD1 1 
ATOM 2843 N ND2 . ASN A 1 381 ? 9.216   29.014  46.158  1.00 55.60  ? 381 ASN A ND2 1 
ATOM 2844 N N   . GLY A 1 382 ? 12.229  28.494  49.492  1.00 47.71  ? 382 GLY A N   1 
ATOM 2845 C CA  . GLY A 1 382 ? 13.341  29.421  49.575  1.00 45.32  ? 382 GLY A CA  1 
ATOM 2846 C C   . GLY A 1 382 ? 14.689  28.750  49.418  1.00 49.54  ? 382 GLY A C   1 
ATOM 2847 O O   . GLY A 1 382 ? 15.631  29.358  48.901  1.00 58.16  ? 382 GLY A O   1 
ATOM 2848 N N   . ALA A 1 383 ? 14.800  27.492  49.842  1.00 46.10  ? 383 ALA A N   1 
ATOM 2849 C CA  . ALA A 1 383 ? 16.064  26.776  49.755  1.00 46.27  ? 383 ALA A CA  1 
ATOM 2850 C C   . ALA A 1 383 ? 16.383  26.290  48.349  1.00 47.24  ? 383 ALA A C   1 
ATOM 2851 O O   . ALA A 1 383 ? 17.548  25.994  48.064  1.00 50.55  ? 383 ALA A O   1 
ATOM 2852 C CB  . ALA A 1 383 ? 16.059  25.585  50.714  1.00 41.16  ? 383 ALA A CB  1 
ATOM 2853 N N   . VAL A 1 384 ? 15.393  26.200  47.465  1.00 42.99  ? 384 VAL A N   1 
ATOM 2854 C CA  . VAL A 1 384 ? 15.580  25.568  46.164  1.00 41.78  ? 384 VAL A CA  1 
ATOM 2855 C C   . VAL A 1 384 ? 15.280  26.487  44.992  1.00 48.71  ? 384 VAL A C   1 
ATOM 2856 O O   . VAL A 1 384 ? 15.492  26.077  43.842  1.00 53.14  ? 384 VAL A O   1 
ATOM 2857 C CB  . VAL A 1 384 ? 14.742  24.277  46.040  1.00 46.14  ? 384 VAL A CB  1 
ATOM 2858 C CG1 . VAL A 1 384 ? 15.152  23.280  47.101  1.00 45.49  ? 384 VAL A CG1 1 
ATOM 2859 C CG2 . VAL A 1 384 ? 13.261  24.594  46.132  1.00 46.51  ? 384 VAL A CG2 1 
ATOM 2860 N N   . GLN A 1 385 ? 14.794  27.702  45.221  1.00 49.86  ? 385 GLN A N   1 
ATOM 2861 C CA  . GLN A 1 385 ? 14.417  28.602  44.139  1.00 47.53  ? 385 GLN A CA  1 
ATOM 2862 C C   . GLN A 1 385 ? 15.370  29.784  44.079  1.00 51.38  ? 385 GLN A C   1 
ATOM 2863 O O   . GLN A 1 385 ? 15.768  30.320  45.117  1.00 56.12  ? 385 GLN A O   1 
ATOM 2864 C CB  . GLN A 1 385 ? 12.983  29.105  44.308  1.00 46.89  ? 385 GLN A CB  1 
ATOM 2865 C CG  . GLN A 1 385 ? 11.951  28.014  44.472  1.00 48.64  ? 385 GLN A CG  1 
ATOM 2866 C CD  . GLN A 1 385 ? 11.717  27.233  43.206  1.00 52.80  ? 385 GLN A CD  1 
ATOM 2867 O OE1 . GLN A 1 385 ? 11.948  27.725  42.104  1.00 58.58  ? 385 GLN A OE1 1 
ATOM 2868 N NE2 . GLN A 1 385 ? 11.254  25.999  43.357  1.00 63.40  ? 385 GLN A NE2 1 
ATOM 2869 N N   . SER A 1 386 ? 15.729  30.185  42.861  1.00 53.52  ? 386 SER A N   1 
ATOM 2870 C CA  . SER A 1 386 ? 16.419  31.448  42.640  1.00 52.83  ? 386 SER A CA  1 
ATOM 2871 C C   . SER A 1 386 ? 15.431  32.588  42.439  1.00 53.41  ? 386 SER A C   1 
ATOM 2872 O O   . SER A 1 386 ? 15.571  33.648  43.057  1.00 58.50  ? 386 SER A O   1 
ATOM 2873 C CB  . SER A 1 386 ? 17.349  31.340  41.432  1.00 56.55  ? 386 SER A CB  1 
ATOM 2874 O OG  . SER A 1 386 ? 16.693  30.727  40.337  1.00 59.99  ? 386 SER A OG  1 
ATOM 2875 N N   . ASP A 1 387 ? 14.431  32.383  41.588  1.00 54.41  ? 387 ASP A N   1 
ATOM 2876 C CA  . ASP A 1 387 ? 13.297  33.281  41.460  1.00 52.58  ? 387 ASP A CA  1 
ATOM 2877 C C   . ASP A 1 387 ? 12.012  32.484  41.627  1.00 61.19  ? 387 ASP A C   1 
ATOM 2878 O O   . ASP A 1 387 ? 12.029  31.326  42.052  1.00 65.18  ? 387 ASP A O   1 
ATOM 2879 C CB  . ASP A 1 387 ? 13.314  34.042  40.119  1.00 57.63  ? 387 ASP A CB  1 
ATOM 2880 C CG  . ASP A 1 387 ? 13.230  33.128  38.901  1.00 63.85  ? 387 ASP A CG  1 
ATOM 2881 O OD1 . ASP A 1 387 ? 12.593  32.059  38.962  1.00 66.87  ? 387 ASP A OD1 1 
ATOM 2882 O OD2 . ASP A 1 387 ? 13.813  33.493  37.860  1.00 66.98  ? 387 ASP A OD2 1 
ATOM 2883 N N   . GLY A 1 388 ? 10.894  33.114  41.285  1.00 59.80  ? 388 GLY A N   1 
ATOM 2884 C CA  . GLY A 1 388 ? 9.594   32.505  41.483  1.00 53.39  ? 388 GLY A CA  1 
ATOM 2885 C C   . GLY A 1 388 ? 9.395   31.187  40.764  1.00 58.32  ? 388 GLY A C   1 
ATOM 2886 O O   . GLY A 1 388 ? 8.718   30.294  41.281  1.00 62.98  ? 388 GLY A O   1 
ATOM 2887 N N   . GLY A 1 389 ? 9.979   31.043  39.578  1.00 57.09  ? 389 GLY A N   1 
ATOM 2888 C CA  . GLY A 1 389 ? 9.750   29.853  38.784  1.00 56.98  ? 389 GLY A CA  1 
ATOM 2889 C C   . GLY A 1 389 ? 10.989  29.061  38.421  1.00 53.44  ? 389 GLY A C   1 
ATOM 2890 O O   . GLY A 1 389 ? 10.882  27.966  37.864  1.00 57.43  ? 389 GLY A O   1 
ATOM 2891 N N   . HIS A 1 390 ? 12.169  29.592  38.729  1.00 56.92  ? 390 HIS A N   1 
ATOM 2892 C CA  . HIS A 1 390 ? 13.425  28.935  38.404  1.00 50.97  ? 390 HIS A CA  1 
ATOM 2893 C C   . HIS A 1 390 ? 14.137  28.517  39.682  1.00 56.67  ? 390 HIS A C   1 
ATOM 2894 O O   . HIS A 1 390 ? 14.082  29.213  40.699  1.00 59.06  ? 390 HIS A O   1 
ATOM 2895 C CB  . HIS A 1 390 ? 14.337  29.850  37.581  1.00 47.73  ? 390 HIS A CB  1 
ATOM 2896 C CG  . HIS A 1 390 ? 13.742  30.284  36.279  1.00 50.98  ? 390 HIS A CG  1 
ATOM 2897 N ND1 . HIS A 1 390 ? 13.264  31.560  36.068  1.00 59.17  ? 390 HIS A ND1 1 
ATOM 2898 C CD2 . HIS A 1 390 ? 13.559  29.618  35.115  1.00 52.04  ? 390 HIS A CD2 1 
ATOM 2899 C CE1 . HIS A 1 390 ? 12.805  31.657  34.835  1.00 60.20  ? 390 HIS A CE1 1 
ATOM 2900 N NE2 . HIS A 1 390 ? 12.971  30.492  34.235  1.00 60.20  ? 390 HIS A NE2 1 
ATOM 2901 N N   . PHE A 1 391 ? 14.804  27.370  39.619  1.00 50.27  ? 391 PHE A N   1 
ATOM 2902 C CA  . PHE A 1 391 ? 15.550  26.847  40.751  1.00 45.69  ? 391 PHE A CA  1 
ATOM 2903 C C   . PHE A 1 391 ? 16.896  27.549  40.870  1.00 44.34  ? 391 PHE A C   1 
ATOM 2904 O O   . PHE A 1 391 ? 17.353  28.221  39.943  1.00 55.21  ? 391 PHE A O   1 
ATOM 2905 C CB  . PHE A 1 391 ? 15.782  25.339  40.623  1.00 42.28  ? 391 PHE A CB  1 
ATOM 2906 C CG  . PHE A 1 391 ? 14.524  24.536  40.478  1.00 46.46  ? 391 PHE A CG  1 
ATOM 2907 C CD1 . PHE A 1 391 ? 13.389  24.861  41.196  1.00 40.92  ? 391 PHE A CD1 1 
ATOM 2908 C CD2 . PHE A 1 391 ? 14.494  23.427  39.653  1.00 50.77  ? 391 PHE A CD2 1 
ATOM 2909 C CE1 . PHE A 1 391 ? 12.238  24.115  41.065  1.00 41.94  ? 391 PHE A CE1 1 
ATOM 2910 C CE2 . PHE A 1 391 ? 13.346  22.674  39.525  1.00 49.12  ? 391 PHE A CE2 1 
ATOM 2911 C CZ  . PHE A 1 391 ? 12.218  23.020  40.231  1.00 51.00  ? 391 PHE A CZ  1 
ATOM 2912 N N   . ASN A 1 392 ? 17.520  27.396  42.034  1.00 41.41  ? 392 ASN A N   1 
ATOM 2913 C CA  . ASN A 1 392 ? 18.915  27.775  42.200  1.00 42.51  ? 392 ASN A CA  1 
ATOM 2914 C C   . ASN A 1 392 ? 19.784  26.571  41.863  1.00 50.11  ? 392 ASN A C   1 
ATOM 2915 O O   . ASN A 1 392 ? 19.289  25.591  41.300  1.00 53.06  ? 392 ASN A O   1 
ATOM 2916 C CB  . ASN A 1 392 ? 19.187  28.277  43.619  1.00 45.28  ? 392 ASN A CB  1 
ATOM 2917 C CG  . ASN A 1 392 ? 18.579  27.386  44.681  1.00 48.19  ? 392 ASN A CG  1 
ATOM 2918 O OD1 . ASN A 1 392 ? 18.323  26.208  44.447  1.00 61.99  ? 392 ASN A OD1 1 
ATOM 2919 N ND2 . ASN A 1 392 ? 18.341  27.950  45.857  1.00 52.46  ? 392 ASN A ND2 1 
ATOM 2920 N N   . SER A 1 393 ? 21.073  26.628  42.198  1.00 56.14  ? 393 SER A N   1 
ATOM 2921 C CA  . SER A 1 393 ? 21.940  25.485  41.941  1.00 51.59  ? 393 SER A CA  1 
ATOM 2922 C C   . SER A 1 393 ? 21.456  24.243  42.675  1.00 60.48  ? 393 SER A C   1 
ATOM 2923 O O   . SER A 1 393 ? 21.457  23.146  42.104  1.00 59.71  ? 393 SER A O   1 
ATOM 2924 C CB  . SER A 1 393 ? 23.376  25.808  42.349  1.00 45.69  ? 393 SER A CB  1 
ATOM 2925 O OG  . SER A 1 393 ? 23.860  26.943  41.657  1.00 62.74  ? 393 SER A OG  1 
ATOM 2926 N N   . MET A 1 394 ? 21.026  24.397  43.928  1.00 56.48  ? 394 MET A N   1 
ATOM 2927 C CA  . MET A 1 394 ? 20.587  23.245  44.703  1.00 45.03  ? 394 MET A CA  1 
ATOM 2928 C C   . MET A 1 394 ? 19.284  22.669  44.160  1.00 47.76  ? 394 MET A C   1 
ATOM 2929 O O   . MET A 1 394 ? 19.108  21.449  44.137  1.00 56.66  ? 394 MET A O   1 
ATOM 2930 C CB  . MET A 1 394 ? 20.434  23.628  46.172  1.00 48.57  ? 394 MET A CB  1 
ATOM 2931 C CG  . MET A 1 394 ? 19.911  22.509  47.042  1.00 56.66  ? 394 MET A CG  1 
ATOM 2932 S SD  . MET A 1 394 ? 20.837  20.975  46.855  1.00 72.54  ? 394 MET A SD  1 
ATOM 2933 C CE  . MET A 1 394 ? 22.450  21.488  47.431  1.00 50.25  ? 394 MET A CE  1 
ATOM 2934 N N   . GLY A 1 395 ? 18.357  23.523  43.726  1.00 54.20  ? 395 GLY A N   1 
ATOM 2935 C CA  . GLY A 1 395 ? 17.111  23.018  43.169  1.00 46.12  ? 395 GLY A CA  1 
ATOM 2936 C C   . GLY A 1 395 ? 17.320  22.225  41.894  1.00 52.20  ? 395 GLY A C   1 
ATOM 2937 O O   . GLY A 1 395 ? 16.739  21.150  41.712  1.00 58.72  ? 395 GLY A O   1 
ATOM 2938 N N   . TYR A 1 396 ? 18.157  22.740  40.993  1.00 52.02  ? 396 TYR A N   1 
ATOM 2939 C CA  . TYR A 1 396 ? 18.494  21.997  39.785  1.00 48.44  ? 396 TYR A CA  1 
ATOM 2940 C C   . TYR A 1 396 ? 19.242  20.714  40.113  1.00 48.98  ? 396 TYR A C   1 
ATOM 2941 O O   . TYR A 1 396 ? 19.027  19.686  39.460  1.00 55.52  ? 396 TYR A O   1 
ATOM 2942 C CB  . TYR A 1 396 ? 19.322  22.874  38.848  1.00 47.85  ? 396 TYR A CB  1 
ATOM 2943 C CG  . TYR A 1 396 ? 18.537  23.998  38.218  1.00 44.31  ? 396 TYR A CG  1 
ATOM 2944 C CD1 . TYR A 1 396 ? 17.314  23.760  37.611  1.00 48.54  ? 396 TYR A CD1 1 
ATOM 2945 C CD2 . TYR A 1 396 ? 19.015  25.298  38.238  1.00 39.77  ? 396 TYR A CD2 1 
ATOM 2946 C CE1 . TYR A 1 396 ? 16.592  24.785  37.037  1.00 51.21  ? 396 TYR A CE1 1 
ATOM 2947 C CE2 . TYR A 1 396 ? 18.300  26.329  37.670  1.00 42.54  ? 396 TYR A CE2 1 
ATOM 2948 C CZ  . TYR A 1 396 ? 17.090  26.067  37.069  1.00 50.33  ? 396 TYR A CZ  1 
ATOM 2949 O OH  . TYR A 1 396 ? 16.375  27.092  36.501  1.00 53.54  ? 396 TYR A OH  1 
ATOM 2950 N N   . ALA A 1 397 ? 20.121  20.755  41.117  1.00 52.82  ? 397 ALA A N   1 
ATOM 2951 C CA  . ALA A 1 397 ? 20.790  19.539  41.561  1.00 53.77  ? 397 ALA A CA  1 
ATOM 2952 C C   . ALA A 1 397 ? 19.791  18.503  42.054  1.00 52.70  ? 397 ALA A C   1 
ATOM 2953 O O   . ALA A 1 397 ? 19.916  17.319  41.729  1.00 61.90  ? 397 ALA A O   1 
ATOM 2954 C CB  . ALA A 1 397 ? 21.793  19.870  42.663  1.00 46.72  ? 397 ALA A CB  1 
ATOM 2955 N N   . ILE A 1 398 ? 18.794  18.934  42.826  1.00 47.01  ? 398 ILE A N   1 
ATOM 2956 C CA  . ILE A 1 398 ? 17.752  18.031  43.300  1.00 45.16  ? 398 ILE A CA  1 
ATOM 2957 C C   . ILE A 1 398 ? 16.993  17.435  42.127  1.00 45.38  ? 398 ILE A C   1 
ATOM 2958 O O   . ILE A 1 398 ? 16.702  16.234  42.104  1.00 56.72  ? 398 ILE A O   1 
ATOM 2959 C CB  . ILE A 1 398 ? 16.805  18.775  44.256  1.00 45.44  ? 398 ILE A CB  1 
ATOM 2960 C CG1 . ILE A 1 398 ? 17.549  19.192  45.519  1.00 46.93  ? 398 ILE A CG1 1 
ATOM 2961 C CG2 . ILE A 1 398 ? 15.603  17.912  44.592  1.00 43.71  ? 398 ILE A CG2 1 
ATOM 2962 C CD1 . ILE A 1 398 ? 16.824  20.201  46.354  1.00 45.25  ? 398 ILE A CD1 1 
ATOM 2963 N N   . HIS A 1 399 ? 16.643  18.266  41.146  1.00 47.75  ? 399 HIS A N   1 
ATOM 2964 C CA  . HIS A 1 399 ? 15.908  17.770  39.988  1.00 50.49  ? 399 HIS A CA  1 
ATOM 2965 C C   . HIS A 1 399 ? 16.711  16.720  39.230  1.00 58.13  ? 399 HIS A C   1 
ATOM 2966 O O   . HIS A 1 399 ? 16.185  15.655  38.879  1.00 71.79  ? 399 HIS A O   1 
ATOM 2967 C CB  . HIS A 1 399 ? 15.542  18.934  39.072  1.00 52.95  ? 399 HIS A CB  1 
ATOM 2968 C CG  . HIS A 1 399 ? 14.799  18.518  37.845  1.00 53.59  ? 399 HIS A CG  1 
ATOM 2969 N ND1 . HIS A 1 399 ? 13.446  18.268  37.843  1.00 64.51  ? 399 HIS A ND1 1 
ATOM 2970 C CD2 . HIS A 1 399 ? 15.224  18.296  36.581  1.00 57.49  ? 399 HIS A CD2 1 
ATOM 2971 C CE1 . HIS A 1 399 ? 13.069  17.917  36.628  1.00 64.95  ? 399 HIS A CE1 1 
ATOM 2972 N NE2 . HIS A 1 399 ? 14.129  17.926  35.842  1.00 57.69  ? 399 HIS A NE2 1 
ATOM 2973 N N   . GLY A 1 400 ? 17.993  16.995  38.983  1.00 48.31  ? 400 GLY A N   1 
ATOM 2974 C CA  . GLY A 1 400 ? 18.825  16.024  38.289  1.00 44.27  ? 400 GLY A CA  1 
ATOM 2975 C C   . GLY A 1 400 ? 19.013  14.744  39.079  1.00 58.04  ? 400 GLY A C   1 
ATOM 2976 O O   . GLY A 1 400 ? 19.017  13.646  38.513  1.00 67.26  ? 400 GLY A O   1 
ATOM 2977 N N   . GLN A 1 401 ? 19.168  14.865  40.399  1.00 55.00  ? 401 GLN A N   1 
ATOM 2978 C CA  . GLN A 1 401 ? 19.340  13.684  41.235  1.00 40.44  ? 401 GLN A CA  1 
ATOM 2979 C C   . GLN A 1 401 ? 18.078  12.830  41.257  1.00 44.42  ? 401 GLN A C   1 
ATOM 2980 O O   . GLN A 1 401 ? 18.162  11.600  41.206  1.00 55.88  ? 401 GLN A O   1 
ATOM 2981 C CB  . GLN A 1 401 ? 19.746  14.101  42.645  1.00 41.86  ? 401 GLN A CB  1 
ATOM 2982 C CG  . GLN A 1 401 ? 21.186  14.567  42.739  1.00 39.67  ? 401 GLN A CG  1 
ATOM 2983 C CD  . GLN A 1 401 ? 21.467  15.347  44.002  1.00 53.48  ? 401 GLN A CD  1 
ATOM 2984 O OE1 . GLN A 1 401 ? 22.601  15.751  44.255  1.00 57.56  ? 401 GLN A OE1 1 
ATOM 2985 N NE2 . GLN A 1 401 ? 20.435  15.564  44.804  1.00 56.44  ? 401 GLN A NE2 1 
ATOM 2986 N N   . MET A 1 402 ? 16.900  13.455  41.330  1.00 48.47  ? 402 MET A N   1 
ATOM 2987 C CA  . MET A 1 402 ? 15.664  12.681  41.246  1.00 38.98  ? 402 MET A CA  1 
ATOM 2988 C C   . MET A 1 402 ? 15.483  12.044  39.878  1.00 46.57  ? 402 MET A C   1 
ATOM 2989 O O   . MET A 1 402 ? 14.952  10.933  39.781  1.00 69.08  ? 402 MET A O   1 
ATOM 2990 C CB  . MET A 1 402 ? 14.449  13.546  41.572  1.00 51.07  ? 402 MET A CB  1 
ATOM 2991 C CG  . MET A 1 402 ? 14.450  14.179  42.941  1.00 47.12  ? 402 MET A CG  1 
ATOM 2992 S SD  . MET A 1 402 ? 12.867  13.843  43.728  1.00 76.51  ? 402 MET A SD  1 
ATOM 2993 C CE  . MET A 1 402 ? 12.934  14.944  45.127  1.00 59.69  ? 402 MET A CE  1 
ATOM 2994 N N   . LEU A 1 403 ? 15.896  12.727  38.812  1.00 46.32  ? 403 LEU A N   1 
ATOM 2995 C CA  . LEU A 1 403 ? 15.818  12.119  37.489  1.00 46.88  ? 403 LEU A CA  1 
ATOM 2996 C C   . LEU A 1 403 ? 16.712  10.886  37.398  1.00 51.74  ? 403 LEU A C   1 
ATOM 2997 O O   . LEU A 1 403 ? 16.299  9.842   36.872  1.00 55.26  ? 403 LEU A O   1 
ATOM 2998 C CB  . LEU A 1 403 ? 16.196  13.150  36.433  1.00 46.04  ? 403 LEU A CB  1 
ATOM 2999 C CG  . LEU A 1 403 ? 15.952  12.783  34.977  1.00 51.49  ? 403 LEU A CG  1 
ATOM 3000 C CD1 . LEU A 1 403 ? 14.513  12.368  34.766  1.00 47.42  ? 403 LEU A CD1 1 
ATOM 3001 C CD2 . LEU A 1 403 ? 16.280  13.983  34.141  1.00 53.72  ? 403 LEU A CD2 1 
ATOM 3002 N N   . ALA A 1 404 ? 17.934  10.982  37.922  1.00 47.97  ? 404 ALA A N   1 
ATOM 3003 C CA  . ALA A 1 404 ? 18.813  9.816   37.946  1.00 45.05  ? 404 ALA A CA  1 
ATOM 3004 C C   . ALA A 1 404 ? 18.257  8.726   38.852  1.00 53.90  ? 404 ALA A C   1 
ATOM 3005 O O   . ALA A 1 404 ? 18.434  7.534   38.579  1.00 64.09  ? 404 ALA A O   1 
ATOM 3006 C CB  . ALA A 1 404 ? 20.215  10.225  38.386  1.00 46.31  ? 404 ALA A CB  1 
ATOM 3007 N N   . SER A 1 405 ? 17.586  9.113   39.938  1.00 52.57  ? 405 SER A N   1 
ATOM 3008 C CA  . SER A 1 405 ? 16.932  8.136   40.799  1.00 38.89  ? 405 SER A CA  1 
ATOM 3009 C C   . SER A 1 405 ? 15.839  7.389   40.056  1.00 46.25  ? 405 SER A C   1 
ATOM 3010 O O   . SER A 1 405 ? 15.690  6.175   40.226  1.00 55.86  ? 405 SER A O   1 
ATOM 3011 C CB  . SER A 1 405 ? 16.351  8.826   42.032  1.00 49.18  ? 405 SER A CB  1 
ATOM 3012 O OG  . SER A 1 405 ? 17.377  9.331   42.865  1.00 53.01  ? 405 SER A OG  1 
ATOM 3013 N N   . MET A 1 406 ? 15.057  8.098   39.241  1.00 49.87  ? 406 MET A N   1 
ATOM 3014 C CA  . MET A 1 406 ? 14.054  7.432   38.418  1.00 40.95  ? 406 MET A CA  1 
ATOM 3015 C C   . MET A 1 406 ? 14.715  6.494   37.420  1.00 49.03  ? 406 MET A C   1 
ATOM 3016 O O   . MET A 1 406 ? 14.210  5.396   37.157  1.00 63.55  ? 406 MET A O   1 
ATOM 3017 C CB  . MET A 1 406 ? 13.186  8.465   37.695  1.00 50.29  ? 406 MET A CB  1 
ATOM 3018 C CG  . MET A 1 406 ? 12.154  7.867   36.737  1.00 50.07  ? 406 MET A CG  1 
ATOM 3019 S SD  . MET A 1 406 ? 12.729  7.542   35.059  1.00 67.23  ? 406 MET A SD  1 
ATOM 3020 C CE  . MET A 1 406 ? 12.764  9.197   34.386  1.00 50.48  ? 406 MET A CE  1 
ATOM 3021 N N   . PHE A 1 407 ? 15.846  6.914   36.847  1.00 52.08  ? 407 PHE A N   1 
ATOM 3022 C CA  . PHE A 1 407 ? 16.556  6.047   35.908  1.00 50.90  ? 407 PHE A CA  1 
ATOM 3023 C C   . PHE A 1 407 ? 17.021  4.759   36.579  1.00 49.85  ? 407 PHE A C   1 
ATOM 3024 O O   . PHE A 1 407 ? 16.832  3.665   36.035  1.00 56.98  ? 407 PHE A O   1 
ATOM 3025 C CB  . PHE A 1 407 ? 17.747  6.786   35.301  1.00 48.71  ? 407 PHE A CB  1 
ATOM 3026 C CG  . PHE A 1 407 ? 17.421  7.539   34.045  1.00 49.21  ? 407 PHE A CG  1 
ATOM 3027 C CD1 . PHE A 1 407 ? 16.286  8.325   33.965  1.00 56.48  ? 407 PHE A CD1 1 
ATOM 3028 C CD2 . PHE A 1 407 ? 18.245  7.449   32.938  1.00 56.61  ? 407 PHE A CD2 1 
ATOM 3029 C CE1 . PHE A 1 407 ? 15.987  9.016   32.808  1.00 55.36  ? 407 PHE A CE1 1 
ATOM 3030 C CE2 . PHE A 1 407 ? 17.949  8.134   31.779  1.00 48.24  ? 407 PHE A CE2 1 
ATOM 3031 C CZ  . PHE A 1 407 ? 16.818  8.919   31.714  1.00 49.20  ? 407 PHE A CZ  1 
ATOM 3032 N N   . MET A 1 408 ? 17.628  4.866   37.764  1.00 43.16  ? 408 MET A N   1 
ATOM 3033 C CA  . MET A 1 408 ? 18.167  3.681   38.427  1.00 46.41  ? 408 MET A CA  1 
ATOM 3034 C C   . MET A 1 408 ? 17.078  2.825   39.061  1.00 50.21  ? 408 MET A C   1 
ATOM 3035 O O   . MET A 1 408 ? 17.264  1.614   39.220  1.00 52.86  ? 408 MET A O   1 
ATOM 3036 C CB  . MET A 1 408 ? 19.197  4.075   39.484  1.00 45.94  ? 408 MET A CB  1 
ATOM 3037 C CG  . MET A 1 408 ? 20.217  5.077   39.013  1.00 46.82  ? 408 MET A CG  1 
ATOM 3038 S SD  . MET A 1 408 ? 21.418  5.504   40.280  1.00 58.99  ? 408 MET A SD  1 
ATOM 3039 C CE  . MET A 1 408 ? 20.500  6.724   41.213  1.00 48.68  ? 408 MET A CE  1 
ATOM 3040 N N   . ALA A 1 409 ? 15.953  3.423   39.436  1.00 51.52  ? 409 ALA A N   1 
ATOM 3041 C CA  . ALA A 1 409 ? 14.872  2.677   40.062  1.00 41.90  ? 409 ALA A CA  1 
ATOM 3042 C C   . ALA A 1 409 ? 14.148  1.756   39.095  1.00 52.51  ? 409 ALA A C   1 
ATOM 3043 O O   . ALA A 1 409 ? 13.372  0.904   39.540  1.00 65.96  ? 409 ALA A O   1 
ATOM 3044 C CB  . ALA A 1 409 ? 13.864  3.641   40.689  1.00 46.67  ? 409 ALA A CB  1 
ATOM 3045 N N   . GLY A 1 410 ? 14.390  1.891   37.797  1.00 53.59  ? 410 GLY A N   1 
ATOM 3046 C CA  . GLY A 1 410 ? 13.586  1.205   36.812  1.00 52.02  ? 410 GLY A CA  1 
ATOM 3047 C C   . GLY A 1 410 ? 12.341  1.950   36.404  1.00 60.16  ? 410 GLY A C   1 
ATOM 3048 O O   . GLY A 1 410 ? 11.438  1.342   35.819  1.00 59.41  ? 410 GLY A O   1 
ATOM 3049 N N   . GLY A 1 411 ? 12.259  3.247   36.698  1.00 54.09  ? 411 GLY A N   1 
ATOM 3050 C CA  . GLY A 1 411 ? 11.113  4.045   36.306  1.00 45.49  ? 411 GLY A CA  1 
ATOM 3051 C C   . GLY A 1 411 ? 10.952  4.217   34.812  1.00 54.46  ? 411 GLY A C   1 
ATOM 3052 O O   . GLY A 1 411 ? 9.854   4.559   34.363  1.00 59.49  ? 411 GLY A O   1 
ATOM 3053 N N   . LEU A 1 412 ? 12.017  3.996   34.039  1.00 61.34  ? 412 LEU A N   1 
ATOM 3054 C CA  . LEU A 1 412 ? 11.892  3.981   32.589  1.00 57.62  ? 412 LEU A CA  1 
ATOM 3055 C C   . LEU A 1 412 ? 11.004  2.844   32.111  1.00 56.08  ? 412 LEU A C   1 
ATOM 3056 O O   . LEU A 1 412 ? 10.256  3.018   31.144  1.00 60.41  ? 412 LEU A O   1 
ATOM 3057 C CB  . LEU A 1 412 ? 13.272  3.868   31.940  1.00 54.68  ? 412 LEU A CB  1 
ATOM 3058 C CG  . LEU A 1 412 ? 14.255  5.008   32.208  1.00 55.99  ? 412 LEU A CG  1 
ATOM 3059 C CD1 . LEU A 1 412 ? 15.587  4.732   31.535  1.00 58.51  ? 412 LEU A CD1 1 
ATOM 3060 C CD2 . LEU A 1 412 ? 13.682  6.329   31.742  1.00 45.39  ? 412 LEU A CD2 1 
ATOM 3061 N N   . LEU A 1 413 ? 11.068  1.690   32.768  1.00 54.82  ? 413 LEU A N   1 
ATOM 3062 C CA  . LEU A 1 413 ? 10.288  0.491   32.503  1.00 55.69  ? 413 LEU A CA  1 
ATOM 3063 C C   . LEU A 1 413 ? 8.811   0.752   32.781  1.00 54.89  ? 413 LEU A C   1 
ATOM 3064 O O   . LEU A 1 413 ? 8.472   1.409   33.768  1.00 57.35  ? 413 LEU A O   1 
ATOM 3065 C CB  . LEU A 1 413 ? 10.768  -0.667  33.372  1.00 57.97  ? 413 LEU A CB  1 
ATOM 3066 C CG  . LEU A 1 413 ? 12.242  -1.060  33.258  1.00 57.41  ? 413 LEU A CG  1 
ATOM 3067 C CD1 . LEU A 1 413 ? 12.609  -2.062  34.339  1.00 58.07  ? 413 LEU A CD1 1 
ATOM 3068 C CD2 . LEU A 1 413 ? 12.547  -1.623  31.886  1.00 53.50  ? 413 LEU A CD2 1 
ATOM 3069 N N   . PRO A 1 414 ? 7.918   0.250   31.925  1.00 61.07  ? 414 PRO A N   1 
ATOM 3070 C CA  . PRO A 1 414 ? 6.481   0.443   32.165  1.00 58.88  ? 414 PRO A CA  1 
ATOM 3071 C C   . PRO A 1 414 ? 5.932   -0.438  33.269  1.00 58.97  ? 414 PRO A C   1 
ATOM 3072 O O   . PRO A 1 414 ? 4.809   -0.197  33.730  1.00 64.51  ? 414 PRO A O   1 
ATOM 3073 C CB  . PRO A 1 414 ? 5.841   0.096   30.814  1.00 56.07  ? 414 PRO A CB  1 
ATOM 3074 C CG  . PRO A 1 414 ? 6.926   -0.519  29.979  1.00 57.89  ? 414 PRO A CG  1 
ATOM 3075 C CD  . PRO A 1 414 ? 8.183   -0.611  30.765  1.00 58.73  ? 414 PRO A CD  1 
ATOM 3076 N N   . THR A 1 415 ? 6.684   -1.448  33.707  1.00 58.44  ? 415 THR A N   1 
ATOM 3077 C CA  . THR A 1 415 ? 6.263   -2.348  34.769  1.00 58.84  ? 415 THR A CA  1 
ATOM 3078 C C   . THR A 1 415 ? 6.667   -1.844  36.147  1.00 58.47  ? 415 THR A C   1 
ATOM 3079 O O   . THR A 1 415 ? 6.450   -2.542  37.143  1.00 61.32  ? 415 THR A O   1 
ATOM 3080 C CB  . THR A 1 415 ? 6.833   -3.747  34.535  1.00 59.27  ? 415 THR A CB  1 
ATOM 3081 O OG1 . THR A 1 415 ? 8.263   -3.696  34.597  1.00 59.15  ? 415 THR A OG1 1 
ATOM 3082 C CG2 . THR A 1 415 ? 6.409   -4.274  33.178  1.00 58.41  ? 415 THR A CG2 1 
ATOM 3083 N N   . TYR A 1 416 ? 7.260   -0.655  36.226  1.00 52.44  ? 416 TYR A N   1 
ATOM 3084 C CA  . TYR A 1 416 ? 7.695   -0.128  37.510  1.00 51.03  ? 416 TYR A CA  1 
ATOM 3085 C C   . TYR A 1 416 ? 6.495   0.173   38.398  1.00 53.86  ? 416 TYR A C   1 
ATOM 3086 O O   . TYR A 1 416 ? 5.452   0.632   37.922  1.00 59.02  ? 416 TYR A O   1 
ATOM 3087 C CB  . TYR A 1 416 ? 8.532   1.135   37.331  1.00 45.78  ? 416 TYR A CB  1 
ATOM 3088 C CG  . TYR A 1 416 ? 9.000   1.688   38.655  1.00 52.97  ? 416 TYR A CG  1 
ATOM 3089 C CD1 . TYR A 1 416 ? 10.117  1.167   39.287  1.00 51.06  ? 416 TYR A CD1 1 
ATOM 3090 C CD2 . TYR A 1 416 ? 8.299   2.701   39.295  1.00 54.91  ? 416 TYR A CD2 1 
ATOM 3091 C CE1 . TYR A 1 416 ? 10.536  1.650   40.502  1.00 49.07  ? 416 TYR A CE1 1 
ATOM 3092 C CE2 . TYR A 1 416 ? 8.710   3.188   40.514  1.00 51.41  ? 416 TYR A CE2 1 
ATOM 3093 C CZ  . TYR A 1 416 ? 9.831   2.660   41.113  1.00 50.58  ? 416 TYR A CZ  1 
ATOM 3094 O OH  . TYR A 1 416 ? 10.250  3.142   42.328  1.00 57.40  ? 416 TYR A OH  1 
ATOM 3095 N N   . ARG A 1 417 ? 6.651   -0.082  39.688  1.00 52.64  ? 417 ARG A N   1 
ATOM 3096 C CA  . ARG A 1 417 ? 5.672   0.224   40.709  1.00 52.94  ? 417 ARG A CA  1 
ATOM 3097 C C   . ARG A 1 417 ? 6.347   0.922   41.880  1.00 59.88  ? 417 ARG A C   1 
ATOM 3098 O O   . ARG A 1 417 ? 7.393   0.463   42.347  1.00 62.63  ? 417 ARG A O   1 
ATOM 3099 C CB  . ARG A 1 417 ? 4.988   -1.050  41.209  1.00 58.01  ? 417 ARG A CB  1 
ATOM 3100 C CG  . ARG A 1 417 ? 4.294   -1.834  40.120  1.00 63.80  ? 417 ARG A CG  1 
ATOM 3101 C CD  . ARG A 1 417 ? 3.784   -3.155  40.644  1.00 62.19  ? 417 ARG A CD  1 
ATOM 3102 N NE  . ARG A 1 417 ? 4.516   -3.594  41.825  1.00 59.85  ? 417 ARG A NE  1 
ATOM 3103 C CZ  . ARG A 1 417 ? 5.135   -4.763  41.932  1.00 63.82  ? 417 ARG A CZ  1 
ATOM 3104 N NH1 . ARG A 1 417 ? 5.128   -5.641  40.943  1.00 61.07  ? 417 ARG A NH1 1 
ATOM 3105 N NH2 . ARG A 1 417 ? 5.776   -5.057  43.058  1.00 62.41  ? 417 ARG A NH2 1 
ATOM 3106 N N   . PRO A 1 418 ? 5.794   2.025   42.371  1.00 49.01  ? 418 PRO A N   1 
ATOM 3107 C CA  . PRO A 1 418 ? 6.396   2.689   43.531  1.00 44.94  ? 418 PRO A CA  1 
ATOM 3108 C C   . PRO A 1 418 ? 6.312   1.815   44.769  1.00 44.89  ? 418 PRO A C   1 
ATOM 3109 O O   . PRO A 1 418 ? 5.435   0.961   44.911  1.00 49.84  ? 418 PRO A O   1 
ATOM 3110 C CB  . PRO A 1 418 ? 5.574   3.969   43.706  1.00 43.48  ? 418 PRO A CB  1 
ATOM 3111 C CG  . PRO A 1 418 ? 4.630   4.025   42.594  1.00 48.37  ? 418 PRO A CG  1 
ATOM 3112 C CD  . PRO A 1 418 ? 4.642   2.755   41.824  1.00 47.77  ? 418 PRO A CD  1 
ATOM 3113 N N   . LEU A 1 419 ? 7.259   2.038   45.674  1.00 47.39  ? 419 LEU A N   1 
ATOM 3114 C CA  . LEU A 1 419 ? 7.325   1.273   46.909  1.00 46.02  ? 419 LEU A CA  1 
ATOM 3115 C C   . LEU A 1 419 ? 6.226   1.739   47.854  1.00 45.38  ? 419 LEU A C   1 
ATOM 3116 O O   . LEU A 1 419 ? 6.185   2.912   48.241  1.00 51.23  ? 419 LEU A O   1 
ATOM 3117 C CB  . LEU A 1 419 ? 8.699   1.427   47.549  1.00 40.94  ? 419 LEU A CB  1 
ATOM 3118 C CG  . LEU A 1 419 ? 8.967   0.497   48.725  1.00 45.92  ? 419 LEU A CG  1 
ATOM 3119 C CD1 . LEU A 1 419 ? 8.784   -0.942  48.290  1.00 57.24  ? 419 LEU A CD1 1 
ATOM 3120 C CD2 . LEU A 1 419 ? 10.370  0.726   49.231  1.00 44.60  ? 419 LEU A CD2 1 
ATOM 3121 N N   . THR A 1 420 ? 5.336   0.821   48.225  1.00 47.12  ? 420 THR A N   1 
ATOM 3122 C CA  . THR A 1 420 ? 4.178   1.145   49.044  1.00 49.75  ? 420 THR A CA  1 
ATOM 3123 C C   . THR A 1 420 ? 4.211   0.525   50.430  1.00 46.48  ? 420 THR A C   1 
ATOM 3124 O O   . THR A 1 420 ? 3.670   1.115   51.366  1.00 56.93  ? 420 THR A O   1 
ATOM 3125 C CB  . THR A 1 420 ? 2.890   0.700   48.341  1.00 54.43  ? 420 THR A CB  1 
ATOM 3126 O OG1 . THR A 1 420 ? 2.962   -0.702  48.061  1.00 61.53  ? 420 THR A OG1 1 
ATOM 3127 C CG2 . THR A 1 420 ? 2.708   1.458   47.041  1.00 53.03  ? 420 THR A CG2 1 
ATOM 3128 N N   . ASN A 1 421 ? 4.827   -0.642  50.586  1.00 53.23  ? 421 ASN A N   1 
ATOM 3129 C CA  . ASN A 1 421 ? 4.881   -1.342  51.859  1.00 53.28  ? 421 ASN A CA  1 
ATOM 3130 C C   . ASN A 1 421 ? 6.335   -1.624  52.212  1.00 54.94  ? 421 ASN A C   1 
ATOM 3131 O O   . ASN A 1 421 ? 7.253   -1.319  51.446  1.00 65.45  ? 421 ASN A O   1 
ATOM 3132 C CB  . ASN A 1 421 ? 4.075   -2.645  51.812  1.00 44.11  ? 421 ASN A CB  1 
ATOM 3133 C CG  . ASN A 1 421 ? 2.585   -2.406  51.845  1.00 53.71  ? 421 ASN A CG  1 
ATOM 3134 O OD1 . ASN A 1 421 ? 2.089   -1.613  52.644  1.00 67.73  ? 421 ASN A OD1 1 
ATOM 3135 N ND2 . ASN A 1 421 ? 1.858   -3.089  50.974  1.00 52.80  ? 421 ASN A ND2 1 
ATOM 3136 N N   . GLU A 1 422 ? 6.539   -2.205  53.391  1.00 52.56  ? 422 GLU A N   1 
ATOM 3137 C CA  . GLU A 1 422 ? 7.880   -2.587  53.806  1.00 50.57  ? 422 GLU A CA  1 
ATOM 3138 C C   . GLU A 1 422 ? 8.435   -3.650  52.871  1.00 57.27  ? 422 GLU A C   1 
ATOM 3139 O O   . GLU A 1 422 ? 7.730   -4.586  52.488  1.00 60.65  ? 422 GLU A O   1 
ATOM 3140 C CB  . GLU A 1 422 ? 7.866   -3.108  55.241  1.00 52.94  ? 422 GLU A CB  1 
ATOM 3141 C CG  . GLU A 1 422 ? 9.153   -3.803  55.646  1.00 56.96  ? 422 GLU A CG  1 
ATOM 3142 C CD  . GLU A 1 422 ? 9.002   -4.628  56.901  1.00 63.72  ? 422 GLU A CD  1 
ATOM 3143 O OE1 . GLU A 1 422 ? 7.934   -4.546  57.535  1.00 68.78  ? 422 GLU A OE1 1 
ATOM 3144 O OE2 . GLU A 1 422 ? 9.950   -5.358  57.255  1.00 68.86  ? 422 GLU A OE2 1 
ATOM 3145 N N   . ILE A 1 423 ? 9.700   -3.498  52.497  1.00 54.58  ? 423 ILE A N   1 
ATOM 3146 C CA  . ILE A 1 423 ? 10.383  -4.453  51.638  1.00 48.68  ? 423 ILE A CA  1 
ATOM 3147 C C   . ILE A 1 423 ? 11.748  -4.753  52.238  1.00 48.89  ? 423 ILE A C   1 
ATOM 3148 O O   . ILE A 1 423 ? 12.417  -3.851  52.753  1.00 54.25  ? 423 ILE A O   1 
ATOM 3149 C CB  . ILE A 1 423 ? 10.520  -3.932  50.195  1.00 55.79  ? 423 ILE A CB  1 
ATOM 3150 C CG1 . ILE A 1 423 ? 11.146  -5.001  49.303  1.00 46.60  ? 423 ILE A CG1 1 
ATOM 3151 C CG2 . ILE A 1 423 ? 11.336  -2.654  50.154  1.00 50.70  ? 423 ILE A CG2 1 
ATOM 3152 C CD1 . ILE A 1 423 ? 10.849  -4.822  47.850  1.00 44.46  ? 423 ILE A CD1 1 
ATOM 3153 N N   . ASN A 1 424 ? 12.140  -6.019  52.201  1.00 57.42  ? 424 ASN A N   1 
ATOM 3154 C CA  . ASN A 1 424 ? 13.482  -6.441  52.573  1.00 50.97  ? 424 ASN A CA  1 
ATOM 3155 C C   . ASN A 1 424 ? 14.226  -6.807  51.297  1.00 53.70  ? 424 ASN A C   1 
ATOM 3156 O O   . ASN A 1 424 ? 14.025  -7.895  50.749  1.00 70.16  ? 424 ASN A O   1 
ATOM 3157 C CB  . ASN A 1 424 ? 13.444  -7.628  53.534  1.00 53.39  ? 424 ASN A CB  1 
ATOM 3158 C CG  . ASN A 1 424 ? 12.898  -7.257  54.893  1.00 59.05  ? 424 ASN A CG  1 
ATOM 3159 O OD1 . ASN A 1 424 ? 13.289  -6.249  55.477  1.00 66.54  ? 424 ASN A OD1 1 
ATOM 3160 N ND2 . ASN A 1 424 ? 11.983  -8.069  55.404  1.00 64.23  ? 424 ASN A ND2 1 
ATOM 3161 N N   . THR A 1 425 ? 15.069  -5.899  50.824  1.00 49.28  ? 425 THR A N   1 
ATOM 3162 C CA  . THR A 1 425 ? 15.823  -6.106  49.601  1.00 48.22  ? 425 THR A CA  1 
ATOM 3163 C C   . THR A 1 425 ? 17.297  -6.269  49.936  1.00 52.59  ? 425 THR A C   1 
ATOM 3164 O O   . THR A 1 425 ? 17.779  -5.776  50.960  1.00 59.14  ? 425 THR A O   1 
ATOM 3165 C CB  . THR A 1 425 ? 15.629  -4.946  48.614  1.00 50.21  ? 425 THR A CB  1 
ATOM 3166 O OG1 . THR A 1 425 ? 16.264  -5.264  47.371  1.00 59.10  ? 425 THR A OG1 1 
ATOM 3167 C CG2 . THR A 1 425 ? 16.225  -3.662  49.166  1.00 47.99  ? 425 THR A CG2 1 
ATOM 3168 N N   . TRP A 1 426 ? 18.004  -6.984  49.076  1.00 45.04  ? 426 TRP A N   1 
ATOM 3169 C CA  . TRP A 1 426 ? 19.429  -7.218  49.230  1.00 47.18  ? 426 TRP A CA  1 
ATOM 3170 C C   . TRP A 1 426 ? 20.141  -6.787  47.953  1.00 44.73  ? 426 TRP A C   1 
ATOM 3171 O O   . TRP A 1 426 ? 19.513  -6.390  46.968  1.00 50.41  ? 426 TRP A O   1 
ATOM 3172 C CB  . TRP A 1 426 ? 19.697  -8.685  49.569  1.00 49.55  ? 426 TRP A CB  1 
ATOM 3173 C CG  . TRP A 1 426 ? 19.106  -9.643  48.589  1.00 49.12  ? 426 TRP A CG  1 
ATOM 3174 C CD1 . TRP A 1 426 ? 19.734  -10.224 47.531  1.00 47.15  ? 426 TRP A CD1 1 
ATOM 3175 C CD2 . TRP A 1 426 ? 17.761  -10.130 48.574  1.00 50.31  ? 426 TRP A CD2 1 
ATOM 3176 N NE1 . TRP A 1 426 ? 18.866  -11.045 46.857  1.00 51.94  ? 426 TRP A NE1 1 
ATOM 3177 C CE2 . TRP A 1 426 ? 17.647  -11.004 47.478  1.00 50.25  ? 426 TRP A CE2 1 
ATOM 3178 C CE3 . TRP A 1 426 ? 16.643  -9.912  49.381  1.00 40.20  ? 426 TRP A CE3 1 
ATOM 3179 C CZ2 . TRP A 1 426 ? 16.459  -11.659 47.168  1.00 47.63  ? 426 TRP A CZ2 1 
ATOM 3180 C CZ3 . TRP A 1 426 ? 15.467  -10.560 49.072  1.00 42.32  ? 426 TRP A CZ3 1 
ATOM 3181 C CH2 . TRP A 1 426 ? 15.384  -11.425 47.976  1.00 46.99  ? 426 TRP A CH2 1 
ATOM 3182 N N   . CYS A 1 427 ? 21.466  -6.863  47.977  1.00 60.50  ? 427 CYS A N   1 
ATOM 3183 C CA  . CYS A 1 427 ? 22.283  -6.536  46.816  1.00 52.54  ? 427 CYS A CA  1 
ATOM 3184 C C   . CYS A 1 427 ? 22.001  -7.567  45.732  1.00 54.99  ? 427 CYS A C   1 
ATOM 3185 O O   . CYS A 1 427 ? 22.030  -8.774  45.990  1.00 62.72  ? 427 CYS A O   1 
ATOM 3186 C CB  . CYS A 1 427 ? 23.762  -6.511  47.190  1.00 60.98  ? 427 CYS A CB  1 
ATOM 3187 S SG  . CYS A 1 427 ? 24.327  -4.952  47.892  1.00 78.66  ? 427 CYS A SG  1 
ATOM 3188 N N   . GLY A 1 428 ? 21.721  -7.094  44.521  1.00 52.86  ? 428 GLY A N   1 
ATOM 3189 C CA  . GLY A 1 428 ? 21.434  -7.966  43.401  1.00 53.89  ? 428 GLY A CA  1 
ATOM 3190 C C   . GLY A 1 428 ? 19.988  -8.387  43.277  1.00 54.91  ? 428 GLY A C   1 
ATOM 3191 O O   . GLY A 1 428 ? 19.644  -9.061  42.299  1.00 60.55  ? 428 GLY A O   1 
ATOM 3192 N N   . ARG A 1 429 ? 19.131  -8.025  44.227  1.00 52.42  ? 429 ARG A N   1 
ATOM 3193 C CA  . ARG A 1 429 ? 17.716  -8.351  44.129  1.00 48.99  ? 429 ARG A CA  1 
ATOM 3194 C C   . ARG A 1 429 ? 17.069  -7.545  43.012  1.00 52.46  ? 429 ARG A C   1 
ATOM 3195 O O   . ARG A 1 429 ? 17.343  -6.352  42.854  1.00 63.36  ? 429 ARG A O   1 
ATOM 3196 C CB  . ARG A 1 429 ? 16.997  -8.077  45.446  1.00 44.65  ? 429 ARG A CB  1 
ATOM 3197 C CG  . ARG A 1 429 ? 15.565  -8.569  45.427  1.00 49.41  ? 429 ARG A CG  1 
ATOM 3198 C CD  . ARG A 1 429 ? 14.795  -8.194  46.667  1.00 59.37  ? 429 ARG A CD  1 
ATOM 3199 N NE  . ARG A 1 429 ? 13.379  -8.499  46.512  1.00 54.49  ? 429 ARG A NE  1 
ATOM 3200 C CZ  . ARG A 1 429 ? 12.460  -8.266  47.437  1.00 52.92  ? 429 ARG A CZ  1 
ATOM 3201 N NH1 . ARG A 1 429 ? 12.775  -7.737  48.607  1.00 58.12  ? 429 ARG A NH1 1 
ATOM 3202 N NH2 . ARG A 1 429 ? 11.193  -8.583  47.186  1.00 59.73  ? 429 ARG A NH2 1 
ATOM 3203 N N   . LEU A 1 430 ? 16.204  -8.198  42.245  1.00 50.62  ? 430 LEU A N   1 
ATOM 3204 C CA  . LEU A 1 430 ? 15.495  -7.553  41.149  1.00 52.72  ? 430 LEU A CA  1 
ATOM 3205 C C   . LEU A 1 430 ? 14.026  -7.424  41.521  1.00 51.07  ? 430 LEU A C   1 
ATOM 3206 O O   . LEU A 1 430 ? 13.321  -8.428  41.661  1.00 61.48  ? 430 LEU A O   1 
ATOM 3207 C CB  . LEU A 1 430 ? 15.669  -8.348  39.862  1.00 50.41  ? 430 LEU A CB  1 
ATOM 3208 C CG  . LEU A 1 430 ? 17.128  -8.571  39.481  1.00 51.75  ? 430 LEU A CG  1 
ATOM 3209 C CD1 . LEU A 1 430 ? 17.204  -9.595  38.388  1.00 51.90  ? 430 LEU A CD1 1 
ATOM 3210 C CD2 . LEU A 1 430 ? 17.774  -7.268  39.048  1.00 54.71  ? 430 LEU A CD2 1 
ATOM 3211 N N   . ASP A 1 431 ? 13.567  -6.190  41.686  1.00 63.12  ? 431 ASP A N   1 
ATOM 3212 C CA  . ASP A 1 431 ? 12.173  -5.905  41.971  1.00 65.75  ? 431 ASP A CA  1 
ATOM 3213 C C   . ASP A 1 431 ? 11.670  -4.820  41.033  1.00 64.41  ? 431 ASP A C   1 
ATOM 3214 O O   . ASP A 1 431 ? 12.444  -4.023  40.495  1.00 65.11  ? 431 ASP A O   1 
ATOM 3215 C CB  . ASP A 1 431 ? 11.973  -5.463  43.425  1.00 65.32  ? 431 ASP A CB  1 
ATOM 3216 C CG  . ASP A 1 431 ? 10.520  -5.507  43.847  1.00 76.68  ? 431 ASP A CG  1 
ATOM 3217 O OD1 . ASP A 1 431 ? 9.730   -6.215  43.189  1.00 75.78  ? 431 ASP A OD1 1 
ATOM 3218 O OD2 . ASP A 1 431 ? 10.161  -4.815  44.818  1.00 81.94  ? 431 ASP A OD2 1 
ATOM 3219 N N   . ASP A 1 432 ? 10.356  -4.797  40.842  1.00 62.18  ? 432 ASP A N   1 
ATOM 3220 C CA  . ASP A 1 432 ? 9.717   -3.746  40.067  1.00 66.65  ? 432 ASP A CA  1 
ATOM 3221 C C   . ASP A 1 432 ? 9.538   -2.460  40.860  1.00 66.95  ? 432 ASP A C   1 
ATOM 3222 O O   . ASP A 1 432 ? 8.982   -1.496  40.328  1.00 72.60  ? 432 ASP A O   1 
ATOM 3223 C CB  . ASP A 1 432 ? 8.358   -4.225  39.549  1.00 70.40  ? 432 ASP A CB  1 
ATOM 3224 C CG  . ASP A 1 432 ? 8.488   -5.234  38.428  1.00 76.07  ? 432 ASP A CG  1 
ATOM 3225 O OD1 . ASP A 1 432 ? 9.469   -5.147  37.660  1.00 69.15  ? 432 ASP A OD1 1 
ATOM 3226 O OD2 . ASP A 1 432 ? 7.610   -6.114  38.311  1.00 77.12  ? 432 ASP A OD2 1 
ATOM 3227 N N   . SER A 1 433 ? 9.987   -2.427  42.114  1.00 56.76  ? 433 SER A N   1 
ATOM 3228 C CA  . SER A 1 433 ? 9.877   -1.237  42.944  1.00 51.44  ? 433 SER A CA  1 
ATOM 3229 C C   . SER A 1 433 ? 11.219  -0.619  43.301  1.00 58.15  ? 433 SER A C   1 
ATOM 3230 O O   . SER A 1 433 ? 11.346  0.608   43.268  1.00 67.83  ? 433 SER A O   1 
ATOM 3231 C CB  . SER A 1 433 ? 9.120   -1.555  44.237  1.00 54.72  ? 433 SER A CB  1 
ATOM 3232 O OG  . SER A 1 433 ? 7.927   -2.267  43.964  1.00 64.09  ? 433 SER A OG  1 
ATOM 3233 N N   . ILE A 1 434 ? 12.218  -1.427  43.637  1.00 53.54  ? 434 ILE A N   1 
ATOM 3234 C CA  . ILE A 1 434 ? 13.526  -0.934  44.049  1.00 49.45  ? 434 ILE A CA  1 
ATOM 3235 C C   . ILE A 1 434 ? 14.540  -1.354  43.000  1.00 54.62  ? 434 ILE A C   1 
ATOM 3236 O O   . ILE A 1 434 ? 14.663  -2.545  42.687  1.00 61.02  ? 434 ILE A O   1 
ATOM 3237 C CB  . ILE A 1 434 ? 13.926  -1.457  45.437  1.00 52.18  ? 434 ILE A CB  1 
ATOM 3238 C CG1 . ILE A 1 434 ? 13.101  -0.769  46.523  1.00 55.93  ? 434 ILE A CG1 1 
ATOM 3239 C CG2 . ILE A 1 434 ? 15.411  -1.238  45.677  1.00 51.41  ? 434 ILE A CG2 1 
ATOM 3240 C CD1 . ILE A 1 434 ? 13.655  -0.950  47.916  1.00 57.26  ? 434 ILE A CD1 1 
ATOM 3241 N N   . GLY A 1 435 ? 15.268  -0.379  42.456  1.00 54.63  ? 435 GLY A N   1 
ATOM 3242 C CA  . GLY A 1 435 ? 16.307  -0.637  41.492  1.00 52.54  ? 435 GLY A CA  1 
ATOM 3243 C C   . GLY A 1 435 ? 17.667  -0.637  42.155  1.00 55.99  ? 435 GLY A C   1 
ATOM 3244 O O   . GLY A 1 435 ? 18.091  0.368   42.727  1.00 60.76  ? 435 GLY A O   1 
ATOM 3245 N N   . TYR A 1 436 ? 18.348  -1.776  42.079  1.00 52.89  ? 436 TYR A N   1 
ATOM 3246 C CA  . TYR A 1 436 ? 19.679  -1.921  42.646  1.00 46.97  ? 436 TYR A CA  1 
ATOM 3247 C C   . TYR A 1 436 ? 20.724  -1.615  41.584  1.00 52.71  ? 436 TYR A C   1 
ATOM 3248 O O   . TYR A 1 436 ? 20.649  -2.131  40.465  1.00 64.73  ? 436 TYR A O   1 
ATOM 3249 C CB  . TYR A 1 436 ? 19.883  -3.334  43.190  1.00 51.94  ? 436 TYR A CB  1 
ATOM 3250 C CG  . TYR A 1 436 ? 21.330  -3.689  43.439  1.00 53.59  ? 436 TYR A CG  1 
ATOM 3251 C CD1 . TYR A 1 436 ? 22.018  -3.161  44.521  1.00 53.59  ? 436 TYR A CD1 1 
ATOM 3252 C CD2 . TYR A 1 436 ? 22.010  -4.543  42.583  1.00 45.27  ? 436 TYR A CD2 1 
ATOM 3253 C CE1 . TYR A 1 436 ? 23.340  -3.483  44.749  1.00 49.39  ? 436 TYR A CE1 1 
ATOM 3254 C CE2 . TYR A 1 436 ? 23.331  -4.869  42.802  1.00 47.84  ? 436 TYR A CE2 1 
ATOM 3255 C CZ  . TYR A 1 436 ? 23.991  -4.336  43.885  1.00 51.43  ? 436 TYR A CZ  1 
ATOM 3256 O OH  . TYR A 1 436 ? 25.308  -4.660  44.106  1.00 59.99  ? 436 TYR A OH  1 
ATOM 3257 N N   . CYS A 1 437 ? 21.692  -0.773  41.933  1.00 42.94  ? 437 CYS A N   1 
ATOM 3258 C CA  . CYS A 1 437 ? 22.786  -0.431  41.033  1.00 45.12  ? 437 CYS A CA  1 
ATOM 3259 C C   . CYS A 1 437 ? 24.106  -0.675  41.743  1.00 49.61  ? 437 CYS A C   1 
ATOM 3260 O O   . CYS A 1 437 ? 24.346  -0.127  42.823  1.00 53.22  ? 437 CYS A O   1 
ATOM 3261 C CB  . CYS A 1 437 ? 22.688  1.023   40.564  1.00 44.32  ? 437 CYS A CB  1 
ATOM 3262 S SG  . CYS A 1 437 ? 21.410  1.318   39.329  1.00 68.32  ? 437 CYS A SG  1 
ATOM 3263 N N   . ASP A 1 438 ? 24.953  -1.501  41.138  1.00 64.44  ? 438 ASP A N   1 
ATOM 3264 C CA  . ASP A 1 438 ? 26.331  -1.684  41.583  1.00 63.05  ? 438 ASP A CA  1 
ATOM 3265 C C   . ASP A 1 438 ? 27.179  -0.680  40.812  1.00 64.56  ? 438 ASP A C   1 
ATOM 3266 O O   . ASP A 1 438 ? 27.661  -0.968  39.716  1.00 68.50  ? 438 ASP A O   1 
ATOM 3267 C CB  . ASP A 1 438 ? 26.785  -3.120  41.347  1.00 64.06  ? 438 ASP A CB  1 
ATOM 3268 C CG  . ASP A 1 438 ? 28.172  -3.396  41.895  1.00 72.78  ? 438 ASP A CG  1 
ATOM 3269 O OD1 . ASP A 1 438 ? 28.820  -2.460  42.404  1.00 77.42  ? 438 ASP A OD1 1 
ATOM 3270 O OD2 . ASP A 1 438 ? 28.615  -4.561  41.817  1.00 72.29  ? 438 ASP A OD2 1 
ATOM 3271 N N   . ALA A 1 439 ? 27.351  0.513   41.387  1.00 61.34  ? 439 ALA A N   1 
ATOM 3272 C CA  . ALA A 1 439 ? 28.033  1.589   40.677  1.00 62.21  ? 439 ALA A CA  1 
ATOM 3273 C C   . ALA A 1 439 ? 29.485  1.250   40.381  1.00 67.65  ? 439 ALA A C   1 
ATOM 3274 O O   . ALA A 1 439 ? 29.968  1.510   39.273  1.00 73.00  ? 439 ALA A O   1 
ATOM 3275 C CB  . ALA A 1 439 ? 27.946  2.885   41.480  1.00 59.52  ? 439 ALA A CB  1 
ATOM 3276 N N   . THR A 1 440 ? 30.198  0.674   41.344  1.00 57.02  ? 440 THR A N   1 
ATOM 3277 C CA  . THR A 1 440 ? 31.609  0.370   41.176  1.00 59.47  ? 440 THR A CA  1 
ATOM 3278 C C   . THR A 1 440 ? 31.865  -1.017  40.606  1.00 61.14  ? 440 THR A C   1 
ATOM 3279 O O   . THR A 1 440 ? 33.014  -1.331  40.281  1.00 60.18  ? 440 THR A O   1 
ATOM 3280 C CB  . THR A 1 440 ? 32.336  0.511   42.514  1.00 60.71  ? 440 THR A CB  1 
ATOM 3281 O OG1 . THR A 1 440 ? 31.680  -0.303  43.492  1.00 66.75  ? 440 THR A OG1 1 
ATOM 3282 C CG2 . THR A 1 440 ? 32.316  1.957   42.974  1.00 57.27  ? 440 THR A CG2 1 
ATOM 3283 N N   . GLY A 1 441 ? 30.835  -1.850  40.482  1.00 57.71  ? 441 GLY A N   1 
ATOM 3284 C CA  . GLY A 1 441 ? 30.990  -3.160  39.889  1.00 55.34  ? 441 GLY A CA  1 
ATOM 3285 C C   . GLY A 1 441 ? 31.761  -4.163  40.713  1.00 56.51  ? 441 GLY A C   1 
ATOM 3286 O O   . GLY A 1 441 ? 32.168  -5.198  40.176  1.00 64.62  ? 441 GLY A O   1 
ATOM 3287 N N   . ASN A 1 442 ? 31.982  -3.895  41.999  1.00 55.10  ? 442 ASN A N   1 
ATOM 3288 C CA  . ASN A 1 442 ? 32.760  -4.781  42.852  1.00 53.00  ? 442 ASN A CA  1 
ATOM 3289 C C   . ASN A 1 442 ? 31.982  -5.263  44.069  1.00 58.33  ? 442 ASN A C   1 
ATOM 3290 O O   . ASN A 1 442 ? 32.590  -5.776  45.015  1.00 65.61  ? 442 ASN A O   1 
ATOM 3291 C CB  . ASN A 1 442 ? 34.051  -4.089  43.294  1.00 56.73  ? 442 ASN A CB  1 
ATOM 3292 C CG  . ASN A 1 442 ? 33.802  -2.712  43.866  1.00 61.55  ? 442 ASN A CG  1 
ATOM 3293 O OD1 . ASN A 1 442 ? 32.659  -2.276  43.986  1.00 66.90  ? 442 ASN A OD1 1 
ATOM 3294 N ND2 . ASN A 1 442 ? 34.875  -2.016  44.221  1.00 62.23  ? 442 ASN A ND2 1 
ATOM 3295 N N   . ILE A 1 443 ? 30.662  -5.110  44.078  1.00 56.82  ? 443 ILE A N   1 
ATOM 3296 C CA  . ILE A 1 443 ? 29.854  -5.627  45.175  1.00 62.22  ? 443 ILE A CA  1 
ATOM 3297 C C   . ILE A 1 443 ? 29.741  -7.136  45.026  1.00 60.49  ? 443 ILE A C   1 
ATOM 3298 O O   . ILE A 1 443 ? 29.233  -7.639  44.017  1.00 60.26  ? 443 ILE A O   1 
ATOM 3299 C CB  . ILE A 1 443 ? 28.469  -4.963  45.201  1.00 61.57  ? 443 ILE A CB  1 
ATOM 3300 C CG1 . ILE A 1 443 ? 28.608  -3.448  45.357  1.00 55.80  ? 443 ILE A CG1 1 
ATOM 3301 C CG2 . ILE A 1 443 ? 27.621  -5.550  46.317  1.00 50.69  ? 443 ILE A CG2 1 
ATOM 3302 C CD1 . ILE A 1 443 ? 28.824  -2.994  46.776  1.00 59.32  ? 443 ILE A CD1 1 
ATOM 3303 N N   . ASN A 1 444 ? 30.213  -7.862  46.035  1.00 60.74  ? 444 ASN A N   1 
ATOM 3304 C CA  . ASN A 1 444 ? 30.305  -9.315  45.966  1.00 57.95  ? 444 ASN A CA  1 
ATOM 3305 C C   . ASN A 1 444 ? 28.930  -9.921  46.214  1.00 59.85  ? 444 ASN A C   1 
ATOM 3306 O O   . ASN A 1 444 ? 28.502  -10.053 47.363  1.00 64.37  ? 444 ASN A O   1 
ATOM 3307 C CB  . ASN A 1 444 ? 31.318  -9.828  46.983  1.00 57.29  ? 444 ASN A CB  1 
ATOM 3308 C CG  . ASN A 1 444 ? 31.429  -11.337 46.985  1.00 65.25  ? 444 ASN A CG  1 
ATOM 3309 O OD1 . ASN A 1 444 ? 31.089  -11.998 46.006  1.00 66.31  ? 444 ASN A OD1 1 
ATOM 3310 N ND2 . ASN A 1 444 ? 31.901  -11.891 48.094  1.00 68.18  ? 444 ASN A ND2 1 
ATOM 3311 N N   . LEU A 1 445 ? 28.246  -10.310 45.141  1.00 61.00  ? 445 LEU A N   1 
ATOM 3312 C CA  . LEU A 1 445 ? 27.001  -11.066 45.264  1.00 55.69  ? 445 LEU A CA  1 
ATOM 3313 C C   . LEU A 1 445 ? 27.263  -12.543 45.496  1.00 60.05  ? 445 LEU A C   1 
ATOM 3314 O O   . LEU A 1 445 ? 26.744  -13.396 44.774  1.00 68.52  ? 445 LEU A O   1 
ATOM 3315 C CB  . LEU A 1 445 ? 26.138  -10.861 44.024  1.00 54.63  ? 445 LEU A CB  1 
ATOM 3316 C CG  . LEU A 1 445 ? 25.853  -9.421  43.604  1.00 56.09  ? 445 LEU A CG  1 
ATOM 3317 C CD1 . LEU A 1 445 ? 24.955  -9.394  42.380  1.00 53.10  ? 445 LEU A CD1 1 
ATOM 3318 C CD2 . LEU A 1 445 ? 25.224  -8.657  44.749  1.00 58.23  ? 445 LEU A CD2 1 
ATOM 3319 N N   . GLY A 1 446 ? 28.077  -12.875 46.492  1.00 55.37  ? 446 GLY A N   1 
ATOM 3320 C CA  . GLY A 1 446 ? 28.380  -14.258 46.795  1.00 53.00  ? 446 GLY A CA  1 
ATOM 3321 C C   . GLY A 1 446 ? 27.452  -14.787 47.875  1.00 57.39  ? 446 GLY A C   1 
ATOM 3322 O O   . GLY A 1 446 ? 26.933  -14.031 48.693  1.00 69.26  ? 446 GLY A O   1 
ATOM 3323 N N   . ARG A 1 447 ? 27.242  -16.097 47.857  1.00 56.85  ? 447 ARG A N   1 
ATOM 3324 C CA  . ARG A 1 447 ? 26.395  -16.722 48.861  1.00 48.20  ? 447 ARG A CA  1 
ATOM 3325 C C   . ARG A 1 447 ? 27.249  -17.315 49.971  1.00 58.11  ? 447 ARG A C   1 
ATOM 3326 O O   . ARG A 1 447 ? 28.180  -18.084 49.711  1.00 70.34  ? 447 ARG A O   1 
ATOM 3327 C CB  . ARG A 1 447 ? 25.527  -17.800 48.221  1.00 55.30  ? 447 ARG A CB  1 
ATOM 3328 C CG  . ARG A 1 447 ? 24.565  -17.273 47.177  1.00 53.28  ? 447 ARG A CG  1 
ATOM 3329 C CD  . ARG A 1 447 ? 23.690  -18.395 46.656  1.00 60.07  ? 447 ARG A CD  1 
ATOM 3330 N NE  . ARG A 1 447 ? 22.729  -18.829 47.662  1.00 60.24  ? 447 ARG A NE  1 
ATOM 3331 C CZ  . ARG A 1 447 ? 21.757  -18.072 48.154  1.00 59.33  ? 447 ARG A CZ  1 
ATOM 3332 N NH1 . ARG A 1 447 ? 21.516  -16.859 47.686  1.00 56.39  ? 447 ARG A NH1 1 
ATOM 3333 N NH2 . ARG A 1 447 ? 21.006  -18.545 49.143  1.00 62.05  ? 447 ARG A NH2 1 
ATOM 3334 N N   . SER A 1 448 ? 26.937  -16.953 51.211  1.00 54.43  ? 448 SER A N   1 
ATOM 3335 C CA  . SER A 1 448 ? 27.672  -17.444 52.364  1.00 60.78  ? 448 SER A CA  1 
ATOM 3336 C C   . SER A 1 448 ? 26.719  -17.623 53.534  1.00 57.91  ? 448 SER A C   1 
ATOM 3337 O O   . SER A 1 448 ? 25.782  -16.843 53.717  1.00 60.98  ? 448 SER A O   1 
ATOM 3338 C CB  . SER A 1 448 ? 28.811  -16.492 52.754  1.00 61.29  ? 448 SER A CB  1 
ATOM 3339 O OG  . SER A 1 448 ? 29.305  -16.790 54.047  1.00 66.69  ? 448 SER A OG  1 
ATOM 3340 N N   . ASP A 1 449 ? 26.970  -18.664 54.328  1.00 66.82  ? 449 ASP A N   1 
ATOM 3341 C CA  . ASP A 1 449 ? 26.213  -18.880 55.554  1.00 66.59  ? 449 ASP A CA  1 
ATOM 3342 C C   . ASP A 1 449 ? 26.508  -17.832 56.615  1.00 68.45  ? 449 ASP A C   1 
ATOM 3343 O O   . ASP A 1 449 ? 25.780  -17.762 57.611  1.00 68.77  ? 449 ASP A O   1 
ATOM 3344 C CB  . ASP A 1 449 ? 26.498  -20.274 56.116  1.00 72.06  ? 449 ASP A CB  1 
ATOM 3345 C CG  . ASP A 1 449 ? 25.930  -21.379 55.251  1.00 78.97  ? 449 ASP A CG  1 
ATOM 3346 O OD1 . ASP A 1 449 ? 24.951  -21.119 54.523  1.00 77.57  ? 449 ASP A OD1 1 
ATOM 3347 O OD2 . ASP A 1 449 ? 26.462  -22.507 55.300  1.00 79.64  ? 449 ASP A OD2 1 
ATOM 3348 N N   . GLY A 1 450 ? 27.549  -17.025 56.431  1.00 61.94  ? 450 GLY A N   1 
ATOM 3349 C CA  . GLY A 1 450 ? 27.845  -15.936 57.334  1.00 60.10  ? 450 GLY A CA  1 
ATOM 3350 C C   . GLY A 1 450 ? 26.930  -14.746 57.208  1.00 65.52  ? 450 GLY A C   1 
ATOM 3351 O O   . GLY A 1 450 ? 26.982  -13.839 58.042  1.00 67.11  ? 450 GLY A O   1 
ATOM 3352 N N   . ALA A 1 451 ? 26.091  -14.721 56.177  1.00 60.84  ? 451 ALA A N   1 
ATOM 3353 C CA  . ALA A 1 451 ? 25.087  -13.680 56.042  1.00 53.82  ? 451 ALA A CA  1 
ATOM 3354 C C   . ALA A 1 451 ? 24.031  -13.820 57.129  1.00 53.62  ? 451 ALA A C   1 
ATOM 3355 O O   . ALA A 1 451 ? 23.754  -14.917 57.622  1.00 61.98  ? 451 ALA A O   1 
ATOM 3356 C CB  . ALA A 1 451 ? 24.421  -13.741 54.669  1.00 52.33  ? 451 ALA A CB  1 
ATOM 3357 N N   . TYR A 1 452 ? 23.441  -12.692 57.498  1.00 43.78  ? 452 TYR A N   1 
ATOM 3358 C CA  . TYR A 1 452 ? 22.390  -12.664 58.503  1.00 48.04  ? 452 TYR A CA  1 
ATOM 3359 C C   . TYR A 1 452 ? 21.003  -12.773 57.892  1.00 54.52  ? 452 TYR A C   1 
ATOM 3360 O O   . TYR A 1 452 ? 20.009  -12.616 58.606  1.00 62.38  ? 452 TYR A O   1 
ATOM 3361 C CB  . TYR A 1 452 ? 22.507  -11.390 59.338  1.00 49.28  ? 452 TYR A CB  1 
ATOM 3362 C CG  . TYR A 1 452 ? 23.934  -11.079 59.719  1.00 56.66  ? 452 TYR A CG  1 
ATOM 3363 C CD1 . TYR A 1 452 ? 24.698  -12.002 60.415  1.00 54.68  ? 452 TYR A CD1 1 
ATOM 3364 C CD2 . TYR A 1 452 ? 24.519  -9.870  59.375  1.00 53.65  ? 452 TYR A CD2 1 
ATOM 3365 C CE1 . TYR A 1 452 ? 26.004  -11.732 60.759  1.00 50.27  ? 452 TYR A CE1 1 
ATOM 3366 C CE2 . TYR A 1 452 ? 25.824  -9.591  59.717  1.00 54.54  ? 452 TYR A CE2 1 
ATOM 3367 C CZ  . TYR A 1 452 ? 26.561  -10.524 60.411  1.00 56.28  ? 452 TYR A CZ  1 
ATOM 3368 O OH  . TYR A 1 452 ? 27.863  -10.254 60.757  1.00 62.71  ? 452 TYR A OH  1 
ATOM 3369 N N   . THR A 1 453 ? 20.918  -13.035 56.593  1.00 45.17  ? 453 THR A N   1 
ATOM 3370 C CA  . THR A 1 453 ? 19.656  -13.164 55.889  1.00 45.65  ? 453 THR A CA  1 
ATOM 3371 C C   . THR A 1 453 ? 19.497  -14.584 55.366  1.00 52.86  ? 453 THR A C   1 
ATOM 3372 O O   . THR A 1 453 ? 20.466  -15.337 55.242  1.00 50.60  ? 453 THR A O   1 
ATOM 3373 C CB  . THR A 1 453 ? 19.567  -12.172 54.725  1.00 46.23  ? 453 THR A CB  1 
ATOM 3374 O OG1 . THR A 1 453 ? 20.497  -12.550 53.703  1.00 52.17  ? 453 THR A OG1 1 
ATOM 3375 C CG2 . THR A 1 453 ? 19.908  -10.782 55.206  1.00 46.33  ? 453 THR A CG2 1 
ATOM 3376 N N   . ARG A 1 454 ? 18.250  -14.945 55.064  1.00 50.12  ? 454 ARG A N   1 
ATOM 3377 C CA  . ARG A 1 454 ? 17.966  -16.254 54.495  1.00 39.79  ? 454 ARG A CA  1 
ATOM 3378 C C   . ARG A 1 454 ? 18.320  -16.342 53.019  1.00 49.82  ? 454 ARG A C   1 
ATOM 3379 O O   . ARG A 1 454 ? 18.473  -17.454 52.502  1.00 55.79  ? 454 ARG A O   1 
ATOM 3380 C CB  . ARG A 1 454 ? 16.495  -16.602 54.702  1.00 38.12  ? 454 ARG A CB  1 
ATOM 3381 C CG  . ARG A 1 454 ? 16.233  -17.309 56.009  1.00 41.89  ? 454 ARG A CG  1 
ATOM 3382 C CD  . ARG A 1 454 ? 14.841  -17.889 56.066  1.00 44.58  ? 454 ARG A CD  1 
ATOM 3383 N NE  . ARG A 1 454 ? 14.460  -18.232 57.429  1.00 43.42  ? 454 ARG A NE  1 
ATOM 3384 C CZ  . ARG A 1 454 ? 14.113  -17.350 58.356  1.00 43.01  ? 454 ARG A CZ  1 
ATOM 3385 N NH1 . ARG A 1 454 ? 14.065  -16.054 58.095  1.00 48.64  ? 454 ARG A NH1 1 
ATOM 3386 N NH2 . ARG A 1 454 ? 13.802  -17.779 59.575  1.00 47.69  ? 454 ARG A NH2 1 
ATOM 3387 N N   . THR A 1 455 ? 18.452  -15.209 52.333  1.00 47.85  ? 455 THR A N   1 
ATOM 3388 C CA  . THR A 1 455 ? 18.889  -15.196 50.946  1.00 48.05  ? 455 THR A CA  1 
ATOM 3389 C C   . THR A 1 455 ? 20.377  -15.468 50.795  1.00 46.88  ? 455 THR A C   1 
ATOM 3390 O O   . THR A 1 455 ? 20.830  -15.738 49.679  1.00 58.95  ? 455 THR A O   1 
ATOM 3391 C CB  . THR A 1 455 ? 18.560  -13.849 50.296  1.00 53.46  ? 455 THR A CB  1 
ATOM 3392 O OG1 . THR A 1 455 ? 19.064  -12.788 51.114  1.00 62.66  ? 455 THR A OG1 1 
ATOM 3393 C CG2 . THR A 1 455 ? 17.063  -13.690 50.148  1.00 50.13  ? 455 THR A CG2 1 
ATOM 3394 N N   . LYS A 1 456 ? 21.144  -15.363 51.882  1.00 48.48  ? 456 LYS A N   1 
ATOM 3395 C CA  . LYS A 1 456 ? 22.569  -15.678 51.914  1.00 45.40  ? 456 LYS A CA  1 
ATOM 3396 C C   . LYS A 1 456 ? 23.396  -14.788 50.996  1.00 48.95  ? 456 LYS A C   1 
ATOM 3397 O O   . LYS A 1 456 ? 24.611  -14.973 50.889  1.00 55.63  ? 456 LYS A O   1 
ATOM 3398 C CB  . LYS A 1 456 ? 22.807  -17.147 51.562  1.00 44.82  ? 456 LYS A CB  1 
ATOM 3399 C CG  . LYS A 1 456 ? 22.455  -18.110 52.673  1.00 45.94  ? 456 LYS A CG  1 
ATOM 3400 C CD  . LYS A 1 456 ? 22.906  -19.514 52.334  1.00 52.89  ? 456 LYS A CD  1 
ATOM 3401 C CE  . LYS A 1 456 ? 22.094  -20.543 53.086  1.00 57.37  ? 456 LYS A CE  1 
ATOM 3402 N NZ  . LYS A 1 456 ? 22.299  -21.908 52.539  1.00 56.01  ? 456 LYS A NZ  1 
ATOM 3403 N N   . VAL A 1 457 ? 22.766  -13.821 50.334  1.00 57.52  ? 457 VAL A N   1 
ATOM 3404 C CA  . VAL A 1 457 ? 23.524  -12.859 49.547  1.00 48.75  ? 457 VAL A CA  1 
ATOM 3405 C C   . VAL A 1 457 ? 24.227  -11.915 50.509  1.00 54.45  ? 457 VAL A C   1 
ATOM 3406 O O   . VAL A 1 457 ? 23.586  -11.239 51.322  1.00 64.29  ? 457 VAL A O   1 
ATOM 3407 C CB  . VAL A 1 457 ? 22.618  -12.100 48.571  1.00 54.54  ? 457 VAL A CB  1 
ATOM 3408 C CG1 . VAL A 1 457 ? 23.430  -11.092 47.780  1.00 50.77  ? 457 VAL A CG1 1 
ATOM 3409 C CG2 . VAL A 1 457 ? 21.920  -13.072 47.638  1.00 48.54  ? 457 VAL A CG2 1 
ATOM 3410 N N   . VAL A 1 458 ? 25.551  -11.858 50.416  1.00 52.80  ? 458 VAL A N   1 
ATOM 3411 C CA  . VAL A 1 458 ? 26.367  -11.188 51.420  1.00 53.43  ? 458 VAL A CA  1 
ATOM 3412 C C   . VAL A 1 458 ? 26.874  -9.868  50.869  1.00 57.68  ? 458 VAL A C   1 
ATOM 3413 O O   . VAL A 1 458 ? 27.932  -9.387  51.291  1.00 72.71  ? 458 VAL A O   1 
ATOM 3414 C CB  . VAL A 1 458 ? 27.541  -12.079 51.870  1.00 60.25  ? 458 VAL A CB  1 
ATOM 3415 C CG1 . VAL A 1 458 ? 27.036  -13.423 52.327  1.00 62.72  ? 458 VAL A CG1 1 
ATOM 3416 C CG2 . VAL A 1 458 ? 28.547  -12.265 50.742  1.00 54.77  ? 458 VAL A CG2 1 
ATOM 3417 N N   . GLY A 1 459 ? 26.093  -9.248  49.977  1.00 58.11  ? 459 GLY A N   1 
ATOM 3418 C CA  . GLY A 1 459 ? 26.613  -8.267  49.041  1.00 55.13  ? 459 GLY A CA  1 
ATOM 3419 C C   . GLY A 1 459 ? 27.613  -7.335  49.680  1.00 56.58  ? 459 GLY A C   1 
ATOM 3420 O O   . GLY A 1 459 ? 27.272  -6.486  50.507  1.00 60.17  ? 459 GLY A O   1 
ATOM 3421 N N   . GLY A 1 460 ? 28.868  -7.499  49.280  1.00 60.41  ? 460 GLY A N   1 
ATOM 3422 C CA  . GLY A 1 460 ? 29.970  -7.026  50.083  1.00 49.37  ? 460 GLY A CA  1 
ATOM 3423 C C   . GLY A 1 460 ? 30.848  -6.000  49.415  1.00 65.34  ? 460 GLY A C   1 
ATOM 3424 O O   . GLY A 1 460 ? 31.151  -6.089  48.221  1.00 75.42  ? 460 GLY A O   1 
ATOM 3425 N N   . MET A 1 461 ? 31.259  -5.013  50.194  1.00 59.88  ? 461 MET A N   1 
ATOM 3426 C CA  . MET A 1 461 ? 32.197  -3.993  49.757  1.00 61.63  ? 461 MET A CA  1 
ATOM 3427 C C   . MET A 1 461 ? 33.561  -4.371  50.315  1.00 60.25  ? 461 MET A C   1 
ATOM 3428 O O   . MET A 1 461 ? 33.791  -4.270  51.521  1.00 68.93  ? 461 MET A O   1 
ATOM 3429 C CB  . MET A 1 461 ? 31.744  -2.621  50.244  1.00 67.51  ? 461 MET A CB  1 
ATOM 3430 C CG  . MET A 1 461 ? 30.255  -2.407  50.061  1.00 59.16  ? 461 MET A CG  1 
ATOM 3431 S SD  . MET A 1 461 ? 29.743  -0.685  50.062  1.00 83.15  ? 461 MET A SD  1 
ATOM 3432 C CE  . MET A 1 461 ? 27.967  -0.892  50.062  1.00 63.40  ? 461 MET A CE  1 
ATOM 3433 N N   . LEU A 1 462 ? 34.455  -4.825  49.442  1.00 61.57  ? 462 LEU A N   1 
ATOM 3434 C CA  . LEU A 1 462 ? 35.746  -5.318  49.893  1.00 62.78  ? 462 LEU A CA  1 
ATOM 3435 C C   . LEU A 1 462 ? 36.561  -4.197  50.528  1.00 63.87  ? 462 LEU A C   1 
ATOM 3436 O O   . LEU A 1 462 ? 36.419  -3.017  50.200  1.00 68.53  ? 462 LEU A O   1 
ATOM 3437 C CB  . LEU A 1 462 ? 36.523  -5.934  48.731  1.00 68.10  ? 462 LEU A CB  1 
ATOM 3438 C CG  . LEU A 1 462 ? 35.897  -7.159  48.066  1.00 69.70  ? 462 LEU A CG  1 
ATOM 3439 C CD1 . LEU A 1 462 ? 36.671  -7.534  46.816  1.00 67.18  ? 462 LEU A CD1 1 
ATOM 3440 C CD2 . LEU A 1 462 ? 35.842  -8.324  49.039  1.00 66.39  ? 462 LEU A CD2 1 
ATOM 3441 N N   . ALA A 1 463 ? 37.418  -4.586  51.467  1.00 65.02  ? 463 ALA A N   1 
ATOM 3442 C CA  . ALA A 1 463 ? 38.294  -3.627  52.118  1.00 61.86  ? 463 ALA A CA  1 
ATOM 3443 C C   . ALA A 1 463 ? 39.306  -3.071  51.124  1.00 63.47  ? 463 ALA A C   1 
ATOM 3444 O O   . ALA A 1 463 ? 39.703  -3.740  50.167  1.00 70.88  ? 463 ALA A O   1 
ATOM 3445 C CB  . ALA A 1 463 ? 39.020  -4.276  53.294  1.00 60.42  ? 463 ALA A CB  1 
ATOM 3446 N N   . ASN A 1 464 ? 39.704  -1.822  51.352  1.00 65.78  ? 464 ASN A N   1 
ATOM 3447 C CA  . ASN A 1 464 ? 40.718  -1.097  50.594  1.00 67.21  ? 464 ASN A CA  1 
ATOM 3448 C C   . ASN A 1 464 ? 40.299  -0.809  49.159  1.00 69.07  ? 464 ASN A C   1 
ATOM 3449 O O   . ASN A 1 464 ? 41.151  -0.432  48.347  1.00 71.27  ? 464 ASN A O   1 
ATOM 3450 C CB  . ASN A 1 464 ? 42.066  -1.829  50.578  1.00 68.57  ? 464 ASN A CB  1 
ATOM 3451 C CG  . ASN A 1 464 ? 42.626  -2.040  51.967  1.00 71.26  ? 464 ASN A CG  1 
ATOM 3452 O OD1 . ASN A 1 464 ? 42.515  -1.171  52.831  1.00 70.79  ? 464 ASN A OD1 1 
ATOM 3453 N ND2 . ASN A 1 464 ? 43.224  -3.202  52.194  1.00 73.80  ? 464 ASN A ND2 1 
ATOM 3454 N N   . VAL A 1 465 ? 39.027  -0.975  48.815  1.00 61.40  ? 465 VAL A N   1 
ATOM 3455 C CA  . VAL A 1 465 ? 38.522  -0.617  47.496  1.00 62.84  ? 465 VAL A CA  1 
ATOM 3456 C C   . VAL A 1 465 ? 37.239  0.184   47.674  1.00 64.16  ? 465 VAL A C   1 
ATOM 3457 O O   . VAL A 1 465 ? 36.457  -0.050  48.604  1.00 69.09  ? 465 VAL A O   1 
ATOM 3458 C CB  . VAL A 1 465 ? 38.295  -1.857  46.602  1.00 57.96  ? 465 VAL A CB  1 
ATOM 3459 C CG1 . VAL A 1 465 ? 37.089  -2.655  47.064  1.00 59.91  ? 465 VAL A CG1 1 
ATOM 3460 C CG2 . VAL A 1 465 ? 38.141  -1.446  45.147  1.00 60.20  ? 465 VAL A CG2 1 
ATOM 3461 N N   . ALA A 1 466 ? 37.040  1.156   46.792  1.00 59.53  ? 466 ALA A N   1 
ATOM 3462 C CA  . ALA A 1 466 ? 35.861  2.009   46.832  1.00 59.87  ? 466 ALA A CA  1 
ATOM 3463 C C   . ALA A 1 466 ? 34.699  1.284   46.170  1.00 61.91  ? 466 ALA A C   1 
ATOM 3464 O O   . ALA A 1 466 ? 34.726  1.031   44.960  1.00 64.55  ? 466 ALA A O   1 
ATOM 3465 C CB  . ALA A 1 466 ? 36.132  3.342   46.138  1.00 61.46  ? 466 ALA A CB  1 
ATOM 3466 N N   . SER A 1 467 ? 33.685  0.944   46.960  1.00 57.83  ? 467 SER A N   1 
ATOM 3467 C CA  . SER A 1 467 ? 32.501  0.251   46.474  1.00 54.90  ? 467 SER A CA  1 
ATOM 3468 C C   . SER A 1 467 ? 31.277  1.105   46.752  1.00 51.82  ? 467 SER A C   1 
ATOM 3469 O O   . SER A 1 467 ? 31.132  1.645   47.852  1.00 63.26  ? 467 SER A O   1 
ATOM 3470 C CB  . SER A 1 467 ? 32.351  -1.119  47.135  1.00 56.07  ? 467 SER A CB  1 
ATOM 3471 O OG  . SER A 1 467 ? 33.544  -1.876  47.029  1.00 63.02  ? 467 SER A OG  1 
ATOM 3472 N N   . ILE A 1 468 ? 30.403  1.228   45.758  1.00 45.25  ? 468 ILE A N   1 
ATOM 3473 C CA  . ILE A 1 468 ? 29.184  2.021   45.870  1.00 49.38  ? 468 ILE A CA  1 
ATOM 3474 C C   . ILE A 1 468 ? 28.006  1.137   45.491  1.00 55.26  ? 468 ILE A C   1 
ATOM 3475 O O   . ILE A 1 468 ? 27.937  0.635   44.363  1.00 63.10  ? 468 ILE A O   1 
ATOM 3476 C CB  . ILE A 1 468 ? 29.231  3.274   44.982  1.00 50.77  ? 468 ILE A CB  1 
ATOM 3477 C CG1 . ILE A 1 468 ? 30.399  4.173   45.386  1.00 50.79  ? 468 ILE A CG1 1 
ATOM 3478 C CG2 . ILE A 1 468 ? 27.917  4.030   45.062  1.00 51.81  ? 468 ILE A CG2 1 
ATOM 3479 C CD1 . ILE A 1 468 ? 30.553  5.395   44.517  1.00 54.32  ? 468 ILE A CD1 1 
ATOM 3480 N N   . ALA A 1 469 ? 27.086  0.947   46.430  1.00 48.64  ? 469 ALA A N   1 
ATOM 3481 C CA  . ALA A 1 469 ? 25.840  0.232   46.187  1.00 52.82  ? 469 ALA A CA  1 
ATOM 3482 C C   . ALA A 1 469 ? 24.686  1.193   46.431  1.00 51.94  ? 469 ALA A C   1 
ATOM 3483 O O   . ALA A 1 469 ? 24.571  1.765   47.519  1.00 62.11  ? 469 ALA A O   1 
ATOM 3484 C CB  . ALA A 1 469 ? 25.722  -0.997  47.087  1.00 52.54  ? 469 ALA A CB  1 
ATOM 3485 N N   . THR A 1 470 ? 23.838  1.370   45.425  1.00 40.67  ? 470 THR A N   1 
ATOM 3486 C CA  . THR A 1 470 ? 22.724  2.300   45.508  1.00 43.40  ? 470 THR A CA  1 
ATOM 3487 C C   . THR A 1 470 ? 21.413  1.577   45.240  1.00 44.79  ? 470 THR A C   1 
ATOM 3488 O O   . THR A 1 470 ? 21.330  0.726   44.350  1.00 52.39  ? 470 THR A O   1 
ATOM 3489 C CB  . THR A 1 470 ? 22.888  3.456   44.518  1.00 44.05  ? 470 THR A CB  1 
ATOM 3490 O OG1 . THR A 1 470 ? 22.940  2.943   43.183  1.00 61.37  ? 470 THR A OG1 1 
ATOM 3491 C CG2 . THR A 1 470 ? 24.164  4.223   44.810  1.00 47.19  ? 470 THR A CG2 1 
ATOM 3492 N N   . PHE A 1 471 ? 20.397  1.917   46.023  1.00 50.90  ? 471 PHE A N   1 
ATOM 3493 C CA  . PHE A 1 471 ? 19.046  1.408   45.842  1.00 56.49  ? 471 PHE A CA  1 
ATOM 3494 C C   . PHE A 1 471 ? 18.136  2.585   45.530  1.00 50.52  ? 471 PHE A C   1 
ATOM 3495 O O   . PHE A 1 471 ? 18.058  3.537   46.313  1.00 59.26  ? 471 PHE A O   1 
ATOM 3496 C CB  . PHE A 1 471 ? 18.570  0.665   47.089  1.00 52.79  ? 471 PHE A CB  1 
ATOM 3497 C CG  . PHE A 1 471 ? 19.313  -0.609  47.349  1.00 48.16  ? 471 PHE A CG  1 
ATOM 3498 C CD1 . PHE A 1 471 ? 18.835  -1.813  46.869  1.00 46.88  ? 471 PHE A CD1 1 
ATOM 3499 C CD2 . PHE A 1 471 ? 20.498  -0.600  48.058  1.00 48.70  ? 471 PHE A CD2 1 
ATOM 3500 C CE1 . PHE A 1 471 ? 19.518  -2.986  47.103  1.00 54.29  ? 471 PHE A CE1 1 
ATOM 3501 C CE2 . PHE A 1 471 ? 21.184  -1.768  48.294  1.00 52.09  ? 471 PHE A CE2 1 
ATOM 3502 C CZ  . PHE A 1 471 ? 20.696  -2.962  47.817  1.00 56.64  ? 471 PHE A CZ  1 
ATOM 3503 N N   . SER A 1 472 ? 17.455  2.521   44.392  1.00 39.31  ? 472 SER A N   1 
ATOM 3504 C CA  . SER A 1 472 ? 16.610  3.608   43.922  1.00 35.46  ? 472 SER A CA  1 
ATOM 3505 C C   . SER A 1 472 ? 15.175  3.118   43.810  1.00 43.50  ? 472 SER A C   1 
ATOM 3506 O O   . SER A 1 472 ? 14.931  1.999   43.351  1.00 49.16  ? 472 SER A O   1 
ATOM 3507 C CB  . SER A 1 472 ? 17.099  4.146   42.578  1.00 53.36  ? 472 SER A CB  1 
ATOM 3508 O OG  . SER A 1 472 ? 18.392  4.709   42.702  1.00 55.04  ? 472 SER A OG  1 
ATOM 3509 N N   . PHE A 1 473 ? 14.235  3.959   44.231  1.00 45.77  ? 473 PHE A N   1 
ATOM 3510 C CA  . PHE A 1 473 ? 12.824  3.612   44.232  1.00 38.37  ? 473 PHE A CA  1 
ATOM 3511 C C   . PHE A 1 473 ? 11.996  4.883   44.340  1.00 44.80  ? 473 PHE A C   1 
ATOM 3512 O O   . PHE A 1 473 ? 12.485  5.936   44.753  1.00 53.94  ? 473 PHE A O   1 
ATOM 3513 C CB  . PHE A 1 473 ? 12.483  2.659   45.383  1.00 40.94  ? 473 PHE A CB  1 
ATOM 3514 C CG  . PHE A 1 473 ? 12.895  3.169   46.733  1.00 47.86  ? 473 PHE A CG  1 
ATOM 3515 C CD1 . PHE A 1 473 ? 14.181  2.968   47.199  1.00 43.92  ? 473 PHE A CD1 1 
ATOM 3516 C CD2 . PHE A 1 473 ? 11.998  3.855   47.532  1.00 43.90  ? 473 PHE A CD2 1 
ATOM 3517 C CE1 . PHE A 1 473 ? 14.564  3.436   48.433  1.00 33.62  ? 473 PHE A CE1 1 
ATOM 3518 C CE2 . PHE A 1 473 ? 12.378  4.326   48.769  1.00 41.60  ? 473 PHE A CE2 1 
ATOM 3519 C CZ  . PHE A 1 473 ? 13.662  4.116   49.219  1.00 39.68  ? 473 PHE A CZ  1 
ATOM 3520 N N   . TYR A 1 474 ? 10.728  4.772   43.964  1.00 51.04  ? 474 TYR A N   1 
ATOM 3521 C CA  . TYR A 1 474 ? 9.744   5.814   44.216  1.00 38.67  ? 474 TYR A CA  1 
ATOM 3522 C C   . TYR A 1 474 ? 9.025   5.479   45.514  1.00 43.05  ? 474 TYR A C   1 
ATOM 3523 O O   . TYR A 1 474 ? 8.337   4.456   45.598  1.00 59.43  ? 474 TYR A O   1 
ATOM 3524 C CB  . TYR A 1 474 ? 8.742   5.931   43.068  1.00 42.12  ? 474 TYR A CB  1 
ATOM 3525 C CG  . TYR A 1 474 ? 7.901   7.187   43.124  1.00 47.73  ? 474 TYR A CG  1 
ATOM 3526 C CD1 . TYR A 1 474 ? 8.289   8.337   42.457  1.00 49.91  ? 474 TYR A CD1 1 
ATOM 3527 C CD2 . TYR A 1 474 ? 6.728   7.228   43.866  1.00 53.29  ? 474 TYR A CD2 1 
ATOM 3528 C CE1 . TYR A 1 474 ? 7.525   9.484   42.507  1.00 48.57  ? 474 TYR A CE1 1 
ATOM 3529 C CE2 . TYR A 1 474 ? 5.961   8.370   43.927  1.00 49.42  ? 474 TYR A CE2 1 
ATOM 3530 C CZ  . TYR A 1 474 ? 6.364   9.496   43.248  1.00 54.26  ? 474 TYR A CZ  1 
ATOM 3531 O OH  . TYR A 1 474 ? 5.600   10.638  43.307  1.00 55.40  ? 474 TYR A OH  1 
ATOM 3532 N N   . LEU A 1 475 ? 9.190   6.326   46.522  1.00 39.83  ? 475 LEU A N   1 
ATOM 3533 C CA  . LEU A 1 475 ? 8.512   6.144   47.801  1.00 51.10  ? 475 LEU A CA  1 
ATOM 3534 C C   . LEU A 1 475 ? 7.101   6.702   47.678  1.00 52.22  ? 475 LEU A C   1 
ATOM 3535 O O   . LEU A 1 475 ? 6.915   7.915   47.547  1.00 56.23  ? 475 LEU A O   1 
ATOM 3536 C CB  . LEU A 1 475 ? 9.280   6.826   48.927  1.00 42.70  ? 475 LEU A CB  1 
ATOM 3537 C CG  . LEU A 1 475 ? 8.602   6.751   50.294  1.00 38.87  ? 475 LEU A CG  1 
ATOM 3538 C CD1 . LEU A 1 475 ? 8.520   5.313   50.769  1.00 38.50  ? 475 LEU A CD1 1 
ATOM 3539 C CD2 . LEU A 1 475 ? 9.337   7.613   51.301  1.00 48.87  ? 475 LEU A CD2 1 
ATOM 3540 N N   . ASP A 1 476 ? 6.105   5.816   47.723  1.00 48.21  ? 476 ASP A N   1 
ATOM 3541 C CA  . ASP A 1 476 ? 4.706   6.203   47.602  1.00 48.52  ? 476 ASP A CA  1 
ATOM 3542 C C   . ASP A 1 476 ? 4.104   6.648   48.928  1.00 58.76  ? 476 ASP A C   1 
ATOM 3543 O O   . ASP A 1 476 ? 2.875   6.666   49.074  1.00 68.41  ? 476 ASP A O   1 
ATOM 3544 C CB  . ASP A 1 476 ? 3.893   5.054   47.006  1.00 54.48  ? 476 ASP A CB  1 
ATOM 3545 C CG  . ASP A 1 476 ? 2.933   5.519   45.933  1.00 66.06  ? 476 ASP A CG  1 
ATOM 3546 O OD1 . ASP A 1 476 ? 3.110   6.645   45.426  1.00 64.59  ? 476 ASP A OD1 1 
ATOM 3547 O OD2 . ASP A 1 476 ? 2.001   4.759   45.596  1.00 68.05  ? 476 ASP A OD2 1 
ATOM 3548 N N   . ALA A 1 477 ? 4.937   7.002   49.901  1.00 47.28  ? 477 ALA A N   1 
ATOM 3549 C CA  . ALA A 1 477 ? 4.488   7.465   51.203  1.00 41.28  ? 477 ALA A CA  1 
ATOM 3550 C C   . ALA A 1 477 ? 5.203   8.766   51.542  1.00 46.56  ? 477 ALA A C   1 
ATOM 3551 O O   . ALA A 1 477 ? 6.137   9.187   50.855  1.00 53.44  ? 477 ALA A O   1 
ATOM 3552 C CB  . ALA A 1 477 ? 4.735   6.408   52.285  1.00 40.58  ? 477 ALA A CB  1 
ATOM 3553 N N   . GLU A 1 478 ? 4.752   9.407   52.618  1.00 55.84  ? 478 GLU A N   1 
ATOM 3554 C CA  . GLU A 1 478 ? 5.363   10.649  53.067  1.00 54.90  ? 478 GLU A CA  1 
ATOM 3555 C C   . GLU A 1 478 ? 6.692   10.431  53.771  1.00 50.62  ? 478 GLU A C   1 
ATOM 3556 O O   . GLU A 1 478 ? 7.497   11.365  53.854  1.00 53.12  ? 478 GLU A O   1 
ATOM 3557 C CB  . GLU A 1 478 ? 4.405   11.393  53.996  1.00 53.93  ? 478 GLU A CB  1 
ATOM 3558 C CG  . GLU A 1 478 ? 3.092   11.728  53.337  1.00 53.11  ? 478 GLU A CG  1 
ATOM 3559 C CD  . GLU A 1 478 ? 3.086   13.122  52.767  1.00 64.57  ? 478 GLU A CD  1 
ATOM 3560 O OE1 . GLU A 1 478 ? 3.768   13.998  53.339  1.00 69.58  ? 478 GLU A OE1 1 
ATOM 3561 O OE2 . GLU A 1 478 ? 2.421   13.339  51.735  1.00 69.65  ? 478 GLU A OE2 1 
ATOM 3562 N N   . ALA A 1 479 ? 6.939   9.226   54.271  1.00 48.62  ? 479 ALA A N   1 
ATOM 3563 C CA  . ALA A 1 479 ? 8.165   8.934   54.993  1.00 39.08  ? 479 ALA A CA  1 
ATOM 3564 C C   . ALA A 1 479 ? 8.430   7.441   54.915  1.00 42.53  ? 479 ALA A C   1 
ATOM 3565 O O   . ALA A 1 479 ? 7.539   6.660   54.572  1.00 54.39  ? 479 ALA A O   1 
ATOM 3566 C CB  . ALA A 1 479 ? 8.081   9.385   56.454  1.00 32.39  ? 479 ALA A CB  1 
ATOM 3567 N N   . ALA A 1 480 ? 9.663   7.058   55.224  1.00 37.34  ? 480 ALA A N   1 
ATOM 3568 C CA  . ALA A 1 480 ? 10.037  5.657   55.281  1.00 41.77  ? 480 ALA A CA  1 
ATOM 3569 C C   . ALA A 1 480 ? 11.236  5.489   56.197  1.00 45.03  ? 480 ALA A C   1 
ATOM 3570 O O   . ALA A 1 480 ? 12.174  6.290   56.174  1.00 54.87  ? 480 ALA A O   1 
ATOM 3571 C CB  . ALA A 1 480 ? 10.357  5.092   53.893  1.00 37.87  ? 480 ALA A CB  1 
ATOM 3572 N N   . HIS A 1 481 ? 11.193  4.440   57.007  1.00 40.31  ? 481 HIS A N   1 
ATOM 3573 C CA  . HIS A 1 481 ? 12.307  4.058   57.861  1.00 36.06  ? 481 HIS A CA  1 
ATOM 3574 C C   . HIS A 1 481 ? 13.251  3.152   57.085  1.00 44.27  ? 481 HIS A C   1 
ATOM 3575 O O   . HIS A 1 481 ? 12.816  2.222   56.401  1.00 47.16  ? 481 HIS A O   1 
ATOM 3576 C CB  . HIS A 1 481 ? 11.808  3.351   59.118  1.00 31.80  ? 481 HIS A CB  1 
ATOM 3577 C CG  . HIS A 1 481 ? 11.309  4.282   60.176  1.00 38.47  ? 481 HIS A CG  1 
ATOM 3578 N ND1 . HIS A 1 481 ? 11.692  4.186   61.496  1.00 62.08  ? 481 HIS A ND1 1 
ATOM 3579 C CD2 . HIS A 1 481 ? 10.485  5.351   60.103  1.00 44.53  ? 481 HIS A CD2 1 
ATOM 3580 C CE1 . HIS A 1 481 ? 11.104  5.141   62.193  1.00 51.91  ? 481 HIS A CE1 1 
ATOM 3581 N NE2 . HIS A 1 481 ? 10.366  5.861   61.371  1.00 46.93  ? 481 HIS A NE2 1 
ATOM 3582 N N   . ILE A 1 482 ? 14.545  3.434   57.191  1.00 46.70  ? 482 ILE A N   1 
ATOM 3583 C CA  . ILE A 1 482 ? 15.572  2.687   56.478  1.00 37.50  ? 482 ILE A CA  1 
ATOM 3584 C C   . ILE A 1 482 ? 16.296  1.810   57.486  1.00 40.65  ? 482 ILE A C   1 
ATOM 3585 O O   . ILE A 1 482 ? 16.869  2.314   58.459  1.00 51.41  ? 482 ILE A O   1 
ATOM 3586 C CB  . ILE A 1 482 ? 16.554  3.617   55.749  1.00 38.52  ? 482 ILE A CB  1 
ATOM 3587 C CG1 . ILE A 1 482 ? 15.787  4.688   54.973  1.00 43.79  ? 482 ILE A CG1 1 
ATOM 3588 C CG2 . ILE A 1 482 ? 17.452  2.820   54.823  1.00 37.48  ? 482 ILE A CG2 1 
ATOM 3589 C CD1 . ILE A 1 482 ? 15.108  4.169   53.729  1.00 38.31  ? 482 ILE A CD1 1 
ATOM 3590 N N   . PHE A 1 483 ? 16.259  0.503   57.259  1.00 44.74  ? 483 PHE A N   1 
ATOM 3591 C CA  . PHE A 1 483 ? 16.932  -0.468  58.105  1.00 34.07  ? 483 PHE A CA  1 
ATOM 3592 C C   . PHE A 1 483 ? 17.927  -1.254  57.267  1.00 32.70  ? 483 PHE A C   1 
ATOM 3593 O O   . PHE A 1 483 ? 17.703  -1.486  56.076  1.00 45.40  ? 483 PHE A O   1 
ATOM 3594 C CB  . PHE A 1 483 ? 15.936  -1.429  58.752  1.00 33.09  ? 483 PHE A CB  1 
ATOM 3595 C CG  . PHE A 1 483 ? 14.870  -0.751  59.553  1.00 34.75  ? 483 PHE A CG  1 
ATOM 3596 C CD1 . PHE A 1 483 ? 15.113  -0.350  60.853  1.00 39.26  ? 483 PHE A CD1 1 
ATOM 3597 C CD2 . PHE A 1 483 ? 13.621  -0.522  59.010  1.00 33.59  ? 483 PHE A CD2 1 
ATOM 3598 C CE1 . PHE A 1 483 ? 14.131  0.267   61.594  1.00 41.66  ? 483 PHE A CE1 1 
ATOM 3599 C CE2 . PHE A 1 483 ? 12.636  0.093   59.746  1.00 42.63  ? 483 PHE A CE2 1 
ATOM 3600 C CZ  . PHE A 1 483 ? 12.890  0.490   61.039  1.00 44.04  ? 483 PHE A CZ  1 
ATOM 3601 N N   . VAL A 1 484 ? 19.025  -1.660  57.892  1.00 39.26  ? 484 VAL A N   1 
ATOM 3602 C CA  . VAL A 1 484 ? 20.075  -2.402  57.211  1.00 35.05  ? 484 VAL A CA  1 
ATOM 3603 C C   . VAL A 1 484 ? 20.509  -3.569  58.086  1.00 40.44  ? 484 VAL A C   1 
ATOM 3604 O O   . VAL A 1 484 ? 20.600  -3.444  59.312  1.00 51.88  ? 484 VAL A O   1 
ATOM 3605 C CB  . VAL A 1 484 ? 21.274  -1.496  56.859  1.00 40.62  ? 484 VAL A CB  1 
ATOM 3606 C CG1 . VAL A 1 484 ? 21.983  -1.025  58.110  1.00 47.03  ? 484 VAL A CG1 1 
ATOM 3607 C CG2 . VAL A 1 484 ? 22.239  -2.229  55.971  1.00 47.66  ? 484 VAL A CG2 1 
ATOM 3608 N N   . HIS A 1 485 ? 20.733  -4.716  57.455  1.00 37.35  ? 485 HIS A N   1 
ATOM 3609 C CA  . HIS A 1 485 ? 21.430  -5.830  58.088  1.00 39.72  ? 485 HIS A CA  1 
ATOM 3610 C C   . HIS A 1 485 ? 22.838  -5.840  57.513  1.00 48.96  ? 485 HIS A C   1 
ATOM 3611 O O   . HIS A 1 485 ? 23.105  -6.495  56.505  1.00 65.34  ? 485 HIS A O   1 
ATOM 3612 C CB  . HIS A 1 485 ? 20.704  -7.146  57.840  1.00 47.95  ? 485 HIS A CB  1 
ATOM 3613 C CG  . HIS A 1 485 ? 19.872  -7.602  58.996  1.00 48.26  ? 485 HIS A CG  1 
ATOM 3614 N ND1 . HIS A 1 485 ? 20.394  -8.309  60.056  1.00 47.88  ? 485 HIS A ND1 1 
ATOM 3615 C CD2 . HIS A 1 485 ? 18.552  -7.451  59.257  1.00 47.43  ? 485 HIS A CD2 1 
ATOM 3616 C CE1 . HIS A 1 485 ? 19.433  -8.573  60.922  1.00 53.80  ? 485 HIS A CE1 1 
ATOM 3617 N NE2 . HIS A 1 485 ? 18.305  -8.065  60.462  1.00 55.52  ? 485 HIS A NE2 1 
ATOM 3618 N N   . GLY A 1 486 ? 23.735  -5.098  58.139  1.00 53.39  ? 486 GLY A N   1 
ATOM 3619 C CA  . GLY A 1 486 ? 25.080  -4.907  57.620  1.00 51.20  ? 486 GLY A CA  1 
ATOM 3620 C C   . GLY A 1 486 ? 26.129  -5.108  58.693  1.00 51.13  ? 486 GLY A C   1 
ATOM 3621 O O   . GLY A 1 486 ? 25.899  -4.804  59.862  1.00 67.05  ? 486 GLY A O   1 
ATOM 3622 N N   . SER A 1 487 ? 27.282  -5.623  58.282  1.00 49.53  ? 487 SER A N   1 
ATOM 3623 C CA  . SER A 1 487 ? 28.424  -5.798  59.162  1.00 52.06  ? 487 SER A CA  1 
ATOM 3624 C C   . SER A 1 487 ? 29.693  -5.474  58.389  1.00 55.01  ? 487 SER A C   1 
ATOM 3625 O O   . SER A 1 487 ? 29.729  -5.518  57.157  1.00 62.19  ? 487 SER A O   1 
ATOM 3626 C CB  . SER A 1 487 ? 28.487  -7.222  59.728  1.00 57.48  ? 487 SER A CB  1 
ATOM 3627 O OG  . SER A 1 487 ? 28.841  -8.156  58.726  1.00 64.63  ? 487 SER A OG  1 
ATOM 3628 N N   . GLY A 1 488 ? 30.737  -5.143  59.125  1.00 56.38  ? 488 GLY A N   1 
ATOM 3629 C CA  . GLY A 1 488 ? 32.014  -4.825  58.529  1.00 54.15  ? 488 GLY A CA  1 
ATOM 3630 C C   . GLY A 1 488 ? 32.847  -4.001  59.487  1.00 59.83  ? 488 GLY A C   1 
ATOM 3631 O O   . GLY A 1 488 ? 32.392  -3.605  60.555  1.00 68.10  ? 488 GLY A O   1 
ATOM 3632 N N   . ALA A 1 489 ? 34.085  -3.744  59.071  1.00 66.78  ? 489 ALA A N   1 
ATOM 3633 C CA  . ALA A 1 489 ? 35.034  -3.010  59.894  1.00 70.08  ? 489 ALA A CA  1 
ATOM 3634 C C   . ALA A 1 489 ? 35.223  -1.568  59.452  1.00 74.90  ? 489 ALA A C   1 
ATOM 3635 O O   . ALA A 1 489 ? 35.300  -0.682  60.308  1.00 79.99  ? 489 ALA A O   1 
ATOM 3636 C CB  . ALA A 1 489 ? 36.392  -3.720  59.893  1.00 69.36  ? 489 ALA A CB  1 
ATOM 3637 N N   . GLY A 1 490 ? 35.287  -1.309  58.150  1.00 78.45  ? 490 GLY A N   1 
ATOM 3638 C CA  . GLY A 1 490 ? 35.559  0.017   57.654  1.00 75.07  ? 490 GLY A CA  1 
ATOM 3639 C C   . GLY A 1 490 ? 34.304  0.843   57.515  1.00 73.85  ? 490 GLY A C   1 
ATOM 3640 O O   . GLY A 1 490 ? 33.192  0.316   57.437  1.00 70.99  ? 490 GLY A O   1 
ATOM 3641 N N   . PRO A 1 491 ? 34.466  2.165   57.460  1.00 68.98  ? 491 PRO A N   1 
ATOM 3642 C CA  . PRO A 1 491 ? 33.298  3.056   57.510  1.00 62.43  ? 491 PRO A CA  1 
ATOM 3643 C C   . PRO A 1 491 ? 32.386  2.851   56.310  1.00 64.33  ? 491 PRO A C   1 
ATOM 3644 O O   . PRO A 1 491 ? 32.833  2.867   55.161  1.00 68.98  ? 491 PRO A O   1 
ATOM 3645 C CB  . PRO A 1 491 ? 33.909  4.464   57.514  1.00 65.54  ? 491 PRO A CB  1 
ATOM 3646 C CG  . PRO A 1 491 ? 35.352  4.311   57.239  1.00 65.45  ? 491 PRO A CG  1 
ATOM 3647 C CD  . PRO A 1 491 ? 35.741  2.877   57.273  1.00 63.46  ? 491 PRO A CD  1 
ATOM 3648 N N   . ILE A 1 492 ? 31.105  2.649   56.589  1.00 56.67  ? 492 ILE A N   1 
ATOM 3649 C CA  . ILE A 1 492 ? 30.070  2.604   55.564  1.00 55.55  ? 492 ILE A CA  1 
ATOM 3650 C C   . ILE A 1 492 ? 29.300  3.914   55.638  1.00 56.55  ? 492 ILE A C   1 
ATOM 3651 O O   . ILE A 1 492 ? 28.892  4.350   56.721  1.00 63.24  ? 492 ILE A O   1 
ATOM 3652 C CB  . ILE A 1 492 ? 29.149  1.384   55.739  1.00 55.39  ? 492 ILE A CB  1 
ATOM 3653 C CG1 . ILE A 1 492 ? 28.138  1.299   54.592  1.00 50.49  ? 492 ILE A CG1 1 
ATOM 3654 C CG2 . ILE A 1 492 ? 28.448  1.397   57.088  1.00 50.79  ? 492 ILE A CG2 1 
ATOM 3655 C CD1 . ILE A 1 492 ? 28.760  1.382   53.223  1.00 48.33  ? 492 ILE A CD1 1 
ATOM 3656 N N   . ASN A 1 493 ? 29.135  4.567   54.495  1.00 48.67  ? 493 ASN A N   1 
ATOM 3657 C CA  . ASN A 1 493 ? 28.492  5.870   54.430  1.00 51.15  ? 493 ASN A CA  1 
ATOM 3658 C C   . ASN A 1 493 ? 27.192  5.752   53.651  1.00 54.71  ? 493 ASN A C   1 
ATOM 3659 O O   . ASN A 1 493 ? 27.154  5.127   52.586  1.00 59.91  ? 493 ASN A O   1 
ATOM 3660 C CB  . ASN A 1 493 ? 29.417  6.894   53.779  1.00 46.11  ? 493 ASN A CB  1 
ATOM 3661 C CG  . ASN A 1 493 ? 30.712  7.071   54.538  1.00 56.41  ? 493 ASN A CG  1 
ATOM 3662 O OD1 . ASN A 1 493 ? 30.711  7.405   55.722  1.00 63.70  ? 493 ASN A OD1 1 
ATOM 3663 N ND2 . ASN A 1 493 ? 31.829  6.834   53.861  1.00 52.04  ? 493 ASN A ND2 1 
ATOM 3664 N N   . VAL A 1 494 ? 26.129  6.345   54.186  1.00 51.36  ? 494 VAL A N   1 
ATOM 3665 C CA  . VAL A 1 494 ? 24.807  6.290   53.580  1.00 44.04  ? 494 VAL A CA  1 
ATOM 3666 C C   . VAL A 1 494 ? 24.348  7.711   53.293  1.00 46.17  ? 494 VAL A C   1 
ATOM 3667 O O   . VAL A 1 494 ? 24.330  8.557   54.194  1.00 53.64  ? 494 VAL A O   1 
ATOM 3668 C CB  . VAL A 1 494 ? 23.795  5.563   54.483  1.00 45.56  ? 494 VAL A CB  1 
ATOM 3669 C CG1 . VAL A 1 494 ? 22.516  5.270   53.715  1.00 41.93  ? 494 VAL A CG1 1 
ATOM 3670 C CG2 . VAL A 1 494 ? 24.399  4.290   55.038  1.00 44.61  ? 494 VAL A CG2 1 
ATOM 3671 N N   . LEU A 1 495 ? 23.987  7.971   52.040  1.00 41.05  ? 495 LEU A N   1 
ATOM 3672 C CA  . LEU A 1 495 ? 23.408  9.244   51.630  1.00 48.31  ? 495 LEU A CA  1 
ATOM 3673 C C   . LEU A 1 495 ? 22.001  8.972   51.125  1.00 49.05  ? 495 LEU A C   1 
ATOM 3674 O O   . LEU A 1 495 ? 21.806  8.122   50.250  1.00 49.76  ? 495 LEU A O   1 
ATOM 3675 C CB  . LEU A 1 495 ? 24.258  9.918   50.553  1.00 43.10  ? 495 LEU A CB  1 
ATOM 3676 C CG  . LEU A 1 495 ? 25.733  10.123  50.904  1.00 40.52  ? 495 LEU A CG  1 
ATOM 3677 C CD1 . LEU A 1 495 ? 26.478  10.761  49.746  1.00 47.80  ? 495 LEU A CD1 1 
ATOM 3678 C CD2 . LEU A 1 495 ? 25.891  10.948  52.169  1.00 45.97  ? 495 LEU A CD2 1 
ATOM 3679 N N   . VAL A 1 496 ? 21.025  9.685   51.677  1.00 56.12  ? 496 VAL A N   1 
ATOM 3680 C CA  . VAL A 1 496 ? 19.615  9.396   51.457  1.00 49.43  ? 496 VAL A CA  1 
ATOM 3681 C C   . VAL A 1 496 ? 18.921  10.520  50.696  1.00 48.79  ? 496 VAL A C   1 
ATOM 3682 O O   . VAL A 1 496 ? 18.043  10.269  49.871  1.00 56.42  ? 496 VAL A O   1 
ATOM 3683 C CB  . VAL A 1 496 ? 18.896  9.106   52.794  1.00 55.46  ? 496 VAL A CB  1 
ATOM 3684 C CG1 . VAL A 1 496 ? 19.259  7.721   53.293  1.00 50.10  ? 496 VAL A CG1 1 
ATOM 3685 C CG2 . VAL A 1 496 ? 19.248  10.159  53.830  1.00 55.68  ? 496 VAL A CG2 1 
ATOM 3686 N N   . ASP A 1 497 ? 19.294  11.766  50.964  1.00 52.04  ? 497 ASP A N   1 
ATOM 3687 C CA  . ASP A 1 497 ? 18.593  12.905  50.388  1.00 48.41  ? 497 ASP A CA  1 
ATOM 3688 C C   . ASP A 1 497 ? 19.582  13.857  49.716  1.00 49.25  ? 497 ASP A C   1 
ATOM 3689 O O   . ASP A 1 497 ? 20.796  13.638  49.717  1.00 60.05  ? 497 ASP A O   1 
ATOM 3690 C CB  . ASP A 1 497 ? 17.759  13.611  51.457  1.00 58.59  ? 497 ASP A CB  1 
ATOM 3691 C CG  . ASP A 1 497 ? 16.556  14.325  50.880  1.00 64.28  ? 497 ASP A CG  1 
ATOM 3692 O OD1 . ASP A 1 497 ? 16.370  14.278  49.647  1.00 63.71  ? 497 ASP A OD1 1 
ATOM 3693 O OD2 . ASP A 1 497 ? 15.792  14.932  51.657  1.00 68.64  ? 497 ASP A OD2 1 
ATOM 3694 N N   . ALA A 1 498 ? 19.039  14.933  49.152  1.00 55.54  ? 498 ALA A N   1 
ATOM 3695 C CA  . ALA A 1 498 ? 19.686  15.784  48.161  1.00 62.68  ? 498 ALA A CA  1 
ATOM 3696 C C   . ALA A 1 498 ? 20.974  16.476  48.607  1.00 74.27  ? 498 ALA A C   1 
ATOM 3697 O O   . ALA A 1 498 ? 21.989  16.360  47.909  1.00 76.75  ? 498 ALA A O   1 
ATOM 3698 C CB  . ALA A 1 498 ? 18.689  16.836  47.678  1.00 53.81  ? 498 ALA A CB  1 
ATOM 3699 N N   . PRO A 1 499 ? 21.000  17.211  49.738  1.00 63.63  ? 499 PRO A N   1 
ATOM 3700 C CA  . PRO A 1 499 ? 22.218  17.972  50.056  1.00 53.57  ? 499 PRO A CA  1 
ATOM 3701 C C   . PRO A 1 499 ? 23.376  17.072  50.451  1.00 55.00  ? 499 PRO A C   1 
ATOM 3702 O O   . PRO A 1 499 ? 24.520  17.525  50.557  1.00 62.50  ? 499 PRO A O   1 
ATOM 3703 C CB  . PRO A 1 499 ? 21.786  18.884  51.210  1.00 49.07  ? 499 PRO A CB  1 
ATOM 3704 C CG  . PRO A 1 499 ? 20.591  18.260  51.795  1.00 55.74  ? 499 PRO A CG  1 
ATOM 3705 C CD  . PRO A 1 499 ? 19.999  17.293  50.818  1.00 54.82  ? 499 PRO A CD  1 
ATOM 3706 N N   . SER A 1 500 ? 23.087  15.788  50.663  1.00 50.13  ? 500 SER A N   1 
ATOM 3707 C CA  . SER A 1 500 ? 24.131  14.833  51.014  1.00 52.84  ? 500 SER A CA  1 
ATOM 3708 C C   . SER A 1 500 ? 25.011  14.471  49.825  1.00 58.10  ? 500 SER A C   1 
ATOM 3709 O O   . SER A 1 500 ? 26.196  14.184  50.016  1.00 60.84  ? 500 SER A O   1 
ATOM 3710 C CB  . SER A 1 500 ? 23.505  13.570  51.600  1.00 56.79  ? 500 SER A CB  1 
ATOM 3711 O OG  . SER A 1 500 ? 22.882  13.841  52.842  1.00 72.00  ? 500 SER A OG  1 
ATOM 3712 N N   . TRP A 1 501 ? 24.464  14.477  48.610  1.00 54.86  ? 501 TRP A N   1 
ATOM 3713 C CA  . TRP A 1 501 ? 25.242  14.077  47.443  1.00 49.02  ? 501 TRP A CA  1 
ATOM 3714 C C   . TRP A 1 501 ? 26.065  15.236  46.898  1.00 55.17  ? 501 TRP A C   1 
ATOM 3715 O O   . TRP A 1 501 ? 27.281  15.113  46.719  1.00 65.24  ? 501 TRP A O   1 
ATOM 3716 C CB  . TRP A 1 501 ? 24.319  13.521  46.362  1.00 49.76  ? 501 TRP A CB  1 
ATOM 3717 C CG  . TRP A 1 501 ? 23.652  12.249  46.759  1.00 52.56  ? 501 TRP A CG  1 
ATOM 3718 C CD1 . TRP A 1 501 ? 24.261  11.078  47.094  1.00 48.15  ? 501 TRP A CD1 1 
ATOM 3719 C CD2 . TRP A 1 501 ? 22.245  12.015  46.865  1.00 55.77  ? 501 TRP A CD2 1 
ATOM 3720 N NE1 . TRP A 1 501 ? 23.321  10.128  47.403  1.00 50.57  ? 501 TRP A NE1 1 
ATOM 3721 C CE2 . TRP A 1 501 ? 22.074  10.679  47.271  1.00 51.02  ? 501 TRP A CE2 1 
ATOM 3722 C CE3 . TRP A 1 501 ? 21.112  12.806  46.655  1.00 47.37  ? 501 TRP A CE3 1 
ATOM 3723 C CZ2 . TRP A 1 501 ? 20.819  10.116  47.470  1.00 48.77  ? 501 TRP A CZ2 1 
ATOM 3724 C CZ3 . TRP A 1 501 ? 19.867  12.244  46.852  1.00 51.93  ? 501 TRP A CZ3 1 
ATOM 3725 C CH2 . TRP A 1 501 ? 19.730  10.913  47.256  1.00 52.60  ? 501 TRP A CH2 1 
ATOM 3726 N N   . TRP A 1 502 ? 25.422  16.366  46.623  1.00 51.47  ? 502 TRP A N   1 
ATOM 3727 C CA  . TRP A 1 502 ? 26.106  17.548  46.122  1.00 49.17  ? 502 TRP A CA  1 
ATOM 3728 C C   . TRP A 1 502 ? 25.665  18.771  46.905  1.00 54.40  ? 502 TRP A C   1 
ATOM 3729 O O   . TRP A 1 502 ? 24.470  18.960  47.151  1.00 62.90  ? 502 TRP A O   1 
ATOM 3730 C CB  . TRP A 1 502 ? 25.837  17.767  44.631  1.00 56.04  ? 502 TRP A CB  1 
ATOM 3731 C CG  . TRP A 1 502 ? 26.460  19.024  44.120  1.00 56.04  ? 502 TRP A CG  1 
ATOM 3732 C CD1 . TRP A 1 502 ? 27.712  19.167  43.606  1.00 58.20  ? 502 TRP A CD1 1 
ATOM 3733 C CD2 . TRP A 1 502 ? 25.861  20.324  44.088  1.00 55.66  ? 502 TRP A CD2 1 
ATOM 3734 N NE1 . TRP A 1 502 ? 27.932  20.476  43.256  1.00 59.81  ? 502 TRP A NE1 1 
ATOM 3735 C CE2 . TRP A 1 502 ? 26.809  21.206  43.540  1.00 57.76  ? 502 TRP A CE2 1 
ATOM 3736 C CE3 . TRP A 1 502 ? 24.616  20.829  44.473  1.00 54.45  ? 502 TRP A CE3 1 
ATOM 3737 C CZ2 . TRP A 1 502 ? 26.550  22.561  43.360  1.00 58.58  ? 502 TRP A CZ2 1 
ATOM 3738 C CZ3 . TRP A 1 502 ? 24.361  22.172  44.296  1.00 56.43  ? 502 TRP A CZ3 1 
ATOM 3739 C CH2 . TRP A 1 502 ? 25.323  23.023  43.745  1.00 57.85  ? 502 TRP A CH2 1 
ATOM 3740 N N   . ASN A 1 503 ? 26.633  19.596  47.294  1.00 53.18  ? 503 ASN A N   1 
ATOM 3741 C CA  . ASN A 1 503 ? 26.375  20.902  47.882  1.00 50.12  ? 503 ASN A CA  1 
ATOM 3742 C C   . ASN A 1 503 ? 27.647  21.726  47.781  1.00 59.82  ? 503 ASN A C   1 
ATOM 3743 O O   . ASN A 1 503 ? 28.656  21.387  48.404  1.00 67.54  ? 503 ASN A O   1 
ATOM 3744 C CB  . ASN A 1 503 ? 25.930  20.783  49.343  1.00 54.40  ? 503 ASN A CB  1 
ATOM 3745 C CG  . ASN A 1 503 ? 25.376  22.082  49.890  1.00 55.68  ? 503 ASN A CG  1 
ATOM 3746 O OD1 . ASN A 1 503 ? 25.226  23.060  49.161  1.00 67.01  ? 503 ASN A OD1 1 
ATOM 3747 N ND2 . ASN A 1 503 ? 25.069  22.097  51.180  1.00 52.75  ? 503 ASN A ND2 1 
ATOM 3748 N N   . ASN A 1 504 ? 27.601  22.802  46.999  1.00 55.17  ? 504 ASN A N   1 
ATOM 3749 C CA  . ASN A 1 504 ? 28.764  23.667  46.846  1.00 51.19  ? 504 ASN A CA  1 
ATOM 3750 C C   . ASN A 1 504 ? 28.918  24.662  47.986  1.00 58.57  ? 504 ASN A C   1 
ATOM 3751 O O   . ASN A 1 504 ? 29.934  25.362  48.041  1.00 63.29  ? 504 ASN A O   1 
ATOM 3752 C CB  . ASN A 1 504 ? 28.698  24.420  45.512  1.00 52.84  ? 504 ASN A CB  1 
ATOM 3753 C CG  . ASN A 1 504 ? 27.402  25.181  45.327  1.00 61.89  ? 504 ASN A CG  1 
ATOM 3754 O OD1 . ASN A 1 504 ? 26.582  25.269  46.240  1.00 75.51  ? 504 ASN A OD1 1 
ATOM 3755 N ND2 . ASN A 1 504 ? 27.207  25.733  44.137  1.00 57.60  ? 504 ASN A ND2 1 
ATOM 3756 N N   . GLY A 1 505 ? 27.900  24.734  48.845  1.00 59.22  ? 505 GLY A N   1 
ATOM 3757 C CA  . GLY A 1 505 ? 27.939  25.635  50.007  1.00 58.43  ? 505 GLY A CA  1 
ATOM 3758 C C   . GLY A 1 505 ? 27.786  27.071  49.584  1.00 63.61  ? 505 GLY A C   1 
ATOM 3759 O O   . GLY A 1 505 ? 28.114  27.959  50.387  1.00 67.51  ? 505 GLY A O   1 
ATOM 3760 N N   . ALA A 1 506 ? 27.281  27.302  48.377  1.00 60.08  ? 506 ALA A N   1 
ATOM 3761 C CA  . ALA A 1 506 ? 27.204  28.684  47.865  1.00 57.82  ? 506 ALA A CA  1 
ATOM 3762 C C   . ALA A 1 506 ? 26.179  29.467  48.670  1.00 61.60  ? 506 ALA A C   1 
ATOM 3763 O O   . ALA A 1 506 ? 26.393  30.655  48.964  1.00 63.81  ? 506 ALA A O   1 
ATOM 3764 C CB  . ALA A 1 506 ? 26.838  28.650  46.423  1.00 52.43  ? 506 ALA A CB  1 
ATOM 3765 N N   . GLN A 1 507 ? 25.091  28.795  49.022  1.00 56.45  ? 507 GLN A N   1 
ATOM 3766 C CA  . GLN A 1 507 ? 24.135  29.379  49.983  1.00 63.72  ? 507 GLN A CA  1 
ATOM 3767 C C   . GLN A 1 507 ? 24.085  28.504  51.231  1.00 66.16  ? 507 GLN A C   1 
ATOM 3768 O O   . GLN A 1 507 ? 24.240  27.282  51.102  1.00 63.33  ? 507 GLN A O   1 
ATOM 3769 C CB  . GLN A 1 507 ? 22.780  29.507  49.297  1.00 66.48  ? 507 GLN A CB  1 
ATOM 3770 C CG  . GLN A 1 507 ? 22.815  30.249  47.967  1.00 66.25  ? 507 GLN A CG  1 
ATOM 3771 C CD  . GLN A 1 507 ? 23.167  31.714  48.101  1.00 66.32  ? 507 GLN A CD  1 
ATOM 3772 O OE1 . GLN A 1 507 ? 23.189  32.283  49.197  1.00 66.04  ? 507 GLN A OE1 1 
ATOM 3773 N NE2 . GLN A 1 507 ? 23.449  32.345  46.972  1.00 67.87  ? 507 GLN A NE2 1 
ATOM 3774 N N   . ASP A 1 508 ? 23.899  29.118  52.393  1.00 30.00  ? 508 ASP A N   1 
ATOM 3775 C CA  . ASP A 1 508 ? 23.751  28.362  53.652  1.00 30.00  ? 508 ASP A CA  1 
ATOM 3776 C C   . ASP A 1 508 ? 22.491  27.510  53.561  1.00 30.00  ? 508 ASP A C   1 
ATOM 3777 O O   . ASP A 1 508 ? 22.422  26.448  54.194  1.00 30.00  ? 508 ASP A O   1 
ATOM 3778 C CB  . ASP A 1 508 ? 23.651  29.347  54.779  1.00 30.00  ? 508 ASP A CB  1 
ATOM 3779 N N   . TYR A 1 509 ? 21.516  27.991  52.791  1.00 67.27  ? 509 TYR A N   1 
ATOM 3780 C CA  . TYR A 1 509 ? 20.122  27.492  52.848  1.00 54.97  ? 509 TYR A CA  1 
ATOM 3781 C C   . TYR A 1 509 ? 20.025  26.295  51.933  1.00 55.73  ? 509 TYR A C   1 
ATOM 3782 O O   . TYR A 1 509 ? 18.990  25.626  51.920  1.00 61.23  ? 509 TYR A O   1 
ATOM 3783 C CB  . TYR A 1 509 ? 19.166  28.645  52.537  1.00 48.17  ? 509 TYR A CB  1 
ATOM 3784 C CG  . TYR A 1 509 ? 19.325  29.394  51.224  1.00 55.40  ? 509 TYR A CG  1 
ATOM 3785 C CD1 . TYR A 1 509 ? 19.806  30.696  51.200  1.00 52.84  ? 509 TYR A CD1 1 
ATOM 3786 C CD2 . TYR A 1 509 ? 18.942  28.820  50.021  1.00 48.29  ? 509 TYR A CD2 1 
ATOM 3787 C CE1 . TYR A 1 509 ? 19.924  31.397  50.013  1.00 50.96  ? 509 TYR A CE1 1 
ATOM 3788 C CE2 . TYR A 1 509 ? 19.059  29.509  48.828  1.00 52.74  ? 509 TYR A CE2 1 
ATOM 3789 C CZ  . TYR A 1 509 ? 19.550  30.799  48.824  1.00 55.86  ? 509 TYR A CZ  1 
ATOM 3790 O OH  . TYR A 1 509 ? 19.666  31.474  47.646  1.00 61.21  ? 509 TYR A OH  1 
ATOM 3791 N N   . TYR A 1 510 ? 21.096  26.012  51.204  1.00 49.01  ? 510 TYR A N   1 
ATOM 3792 C CA  . TYR A 1 510 ? 21.134  24.810  50.342  1.00 45.84  ? 510 TYR A CA  1 
ATOM 3793 C C   . TYR A 1 510 ? 21.091  23.592  51.237  1.00 55.08  ? 510 TYR A C   1 
ATOM 3794 O O   . TYR A 1 510 ? 20.705  22.512  50.778  1.00 62.07  ? 510 TYR A O   1 
ATOM 3795 C CB  . TYR A 1 510 ? 22.445  24.908  49.572  1.00 56.87  ? 510 TYR A CB  1 
ATOM 3796 C CG  . TYR A 1 510 ? 22.443  25.741  48.302  1.00 55.41  ? 510 TYR A CG  1 
ATOM 3797 C CD1 . TYR A 1 510 ? 21.370  26.556  47.976  1.00 56.47  ? 510 TYR A CD1 1 
ATOM 3798 C CD2 . TYR A 1 510 ? 23.525  25.706  47.436  1.00 53.33  ? 510 TYR A CD2 1 
ATOM 3799 C CE1 . TYR A 1 510 ? 21.376  27.314  46.819  1.00 55.22  ? 510 TYR A CE1 1 
ATOM 3800 C CE2 . TYR A 1 510 ? 23.538  26.456  46.275  1.00 56.22  ? 510 TYR A CE2 1 
ATOM 3801 C CZ  . TYR A 1 510 ? 22.461  27.261  45.966  1.00 57.37  ? 510 TYR A CZ  1 
ATOM 3802 O OH  . TYR A 1 510 ? 22.468  28.007  44.826  1.00 61.88  ? 510 TYR A OH  1 
ATOM 3803 N N   . ASP A 1 511 ? 21.478  23.757  52.500  1.00 55.37  ? 511 ASP A N   1 
ATOM 3804 C CA  . ASP A 1 511 ? 21.478  22.648  53.484  1.00 52.01  ? 511 ASP A CA  1 
ATOM 3805 C C   . ASP A 1 511 ? 20.053  22.359  53.940  1.00 56.49  ? 511 ASP A C   1 
ATOM 3806 O O   . ASP A 1 511 ? 19.790  21.219  54.344  1.00 63.59  ? 511 ASP A O   1 
ATOM 3807 C CB  . ASP A 1 511 ? 22.360  23.007  54.662  1.00 56.25  ? 511 ASP A CB  1 
ATOM 3808 C CG  . ASP A 1 511 ? 23.757  23.490  54.309  1.00 69.00  ? 511 ASP A CG  1 
ATOM 3809 O OD1 . ASP A 1 511 ? 23.999  23.771  53.118  1.00 72.96  ? 511 ASP A OD1 1 
ATOM 3810 O OD2 . ASP A 1 511 ? 24.590  23.585  55.229  1.00 69.29  ? 511 ASP A OD2 1 
ATOM 3811 N N   . PHE A 1 512 ? 19.182  23.357  53.906  1.00 49.17  ? 512 PHE A N   1 
ATOM 3812 C CA  . PHE A 1 512 ? 17.786  23.178  54.276  1.00 53.57  ? 512 PHE A CA  1 
ATOM 3813 C C   . PHE A 1 512 ? 16.950  22.591  53.149  1.00 55.70  ? 512 PHE A C   1 
ATOM 3814 O O   . PHE A 1 512 ? 15.726  22.504  53.287  1.00 56.18  ? 512 PHE A O   1 
ATOM 3815 C CB  . PHE A 1 512 ? 17.175  24.511  54.714  1.00 48.41  ? 512 PHE A CB  1 
ATOM 3816 C CG  . PHE A 1 512 ? 17.960  25.219  55.775  1.00 52.69  ? 512 PHE A CG  1 
ATOM 3817 C CD1 . PHE A 1 512 ? 18.322  24.566  56.939  1.00 54.26  ? 512 PHE A CD1 1 
ATOM 3818 C CD2 . PHE A 1 512 ? 18.323  26.544  55.615  1.00 52.93  ? 512 PHE A CD2 1 
ATOM 3819 C CE1 . PHE A 1 512 ? 19.041  25.218  57.919  1.00 54.56  ? 512 PHE A CE1 1 
ATOM 3820 C CE2 . PHE A 1 512 ? 19.041  27.201  56.591  1.00 56.25  ? 512 PHE A CE2 1 
ATOM 3821 C CZ  . PHE A 1 512 ? 19.400  26.538  57.744  1.00 55.44  ? 512 PHE A CZ  1 
ATOM 3822 N N   . ALA A 1 513 ? 17.576  22.192  52.042  1.00 47.45  ? 513 ALA A N   1 
ATOM 3823 C CA  . ALA A 1 513 ? 16.859  21.730  50.862  1.00 50.43  ? 513 ALA A CA  1 
ATOM 3824 C C   . ALA A 1 513 ? 16.633  20.226  50.852  1.00 51.86  ? 513 ALA A C   1 
ATOM 3825 O O   . ALA A 1 513 ? 16.345  19.657  49.792  1.00 57.51  ? 513 ALA A O   1 
ATOM 3826 C CB  . ALA A 1 513 ? 17.598  22.164  49.599  1.00 47.70  ? 513 ALA A CB  1 
ATOM 3827 N N   . ASN A 1 514 ? 16.767  19.561  51.992  1.00 54.29  ? 514 ASN A N   1 
ATOM 3828 C CA  . ASN A 1 514 ? 16.387  18.163  52.079  1.00 48.76  ? 514 ASN A CA  1 
ATOM 3829 C C   . ASN A 1 514 ? 14.870  18.048  52.198  1.00 49.83  ? 514 ASN A C   1 
ATOM 3830 O O   . ASN A 1 514 ? 14.172  19.001  52.546  1.00 64.72  ? 514 ASN A O   1 
ATOM 3831 C CB  . ASN A 1 514 ? 17.075  17.484  53.262  1.00 50.82  ? 514 ASN A CB  1 
ATOM 3832 C CG  . ASN A 1 514 ? 17.023  18.316  54.519  1.00 54.62  ? 514 ASN A CG  1 
ATOM 3833 O OD1 . ASN A 1 514 ? 16.359  19.348  54.566  1.00 59.86  ? 514 ASN A OD1 1 
ATOM 3834 N ND2 . ASN A 1 514 ? 17.719  17.866  55.553  1.00 62.95  ? 514 ASN A ND2 1 
ATOM 3835 N N   . ASN A 1 515 ? 14.358  16.860  51.889  1.00 49.79  ? 515 ASN A N   1 
ATOM 3836 C CA  . ASN A 1 515 ? 12.923  16.622  51.958  1.00 44.20  ? 515 ASN A CA  1 
ATOM 3837 C C   . ASN A 1 515 ? 12.442  16.760  53.397  1.00 46.72  ? 515 ASN A C   1 
ATOM 3838 O O   . ASN A 1 515 ? 13.066  16.232  54.322  1.00 54.28  ? 515 ASN A O   1 
ATOM 3839 C CB  . ASN A 1 515 ? 12.587  15.239  51.413  1.00 36.90  ? 515 ASN A CB  1 
ATOM 3840 C CG  . ASN A 1 515 ? 12.432  15.230  49.911  1.00 45.41  ? 515 ASN A CG  1 
ATOM 3841 O OD1 . ASN A 1 515 ? 12.840  14.285  49.239  1.00 56.25  ? 515 ASN A OD1 1 
ATOM 3842 N ND2 . ASN A 1 515 ? 11.838  16.285  49.373  1.00 55.31  ? 515 ASN A ND2 1 
ATOM 3843 N N   . GLN A 1 516 ? 11.338  17.472  53.581  1.00 46.08  ? 516 GLN A N   1 
ATOM 3844 C CA  . GLN A 1 516 ? 10.774  17.717  54.896  1.00 38.72  ? 516 GLN A CA  1 
ATOM 3845 C C   . GLN A 1 516 ? 9.338   17.212  54.960  1.00 47.15  ? 516 GLN A C   1 
ATOM 3846 O O   . GLN A 1 516 ? 8.747   16.805  53.958  1.00 52.11  ? 516 GLN A O   1 
ATOM 3847 C CB  . GLN A 1 516 ? 10.818  19.210  55.229  1.00 35.56  ? 516 GLN A CB  1 
ATOM 3848 C CG  . GLN A 1 516 ? 12.158  19.867  54.983  1.00 41.50  ? 516 GLN A CG  1 
ATOM 3849 C CD  . GLN A 1 516 ? 13.116  19.669  56.133  1.00 50.65  ? 516 GLN A CD  1 
ATOM 3850 O OE1 . GLN A 1 516 ? 12.721  19.705  57.297  1.00 59.79  ? 516 GLN A OE1 1 
ATOM 3851 N NE2 . GLN A 1 516 ? 14.383  19.449  55.814  1.00 59.07  ? 516 GLN A NE2 1 
ATOM 3852 N N   . SER A 1 517 ? 8.782   17.235  56.165  1.00 55.10  ? 517 SER A N   1 
ATOM 3853 C CA  . SER A 1 517 ? 7.356   17.008  56.317  1.00 49.83  ? 517 SER A CA  1 
ATOM 3854 C C   . SER A 1 517 ? 6.587   18.217  55.798  1.00 50.02  ? 517 SER A C   1 
ATOM 3855 O O   . SER A 1 517 ? 7.014   19.364  55.952  1.00 55.32  ? 517 SER A O   1 
ATOM 3856 C CB  . SER A 1 517 ? 7.000   16.752  57.778  1.00 45.03  ? 517 SER A CB  1 
ATOM 3857 O OG  . SER A 1 517 ? 6.667   17.961  58.432  1.00 53.96  ? 517 SER A OG  1 
ATOM 3858 N N   . ILE A 1 518 ? 5.446   17.950  55.166  1.00 43.56  ? 518 ILE A N   1 
ATOM 3859 C CA  . ILE A 1 518 ? 4.650   19.044  54.623  1.00 40.76  ? 518 ILE A CA  1 
ATOM 3860 C C   . ILE A 1 518 ? 4.140   19.954  55.730  1.00 44.43  ? 518 ILE A C   1 
ATOM 3861 O O   . ILE A 1 518 ? 4.208   21.181  55.608  1.00 56.43  ? 518 ILE A O   1 
ATOM 3862 C CB  . ILE A 1 518 ? 3.493   18.495  53.773  1.00 39.87  ? 518 ILE A CB  1 
ATOM 3863 C CG1 . ILE A 1 518 ? 4.052   17.760  52.559  1.00 42.41  ? 518 ILE A CG1 1 
ATOM 3864 C CG2 . ILE A 1 518 ? 2.563   19.616  53.346  1.00 37.47  ? 518 ILE A CG2 1 
ATOM 3865 C CD1 . ILE A 1 518 ? 4.811   18.657  51.616  1.00 40.48  ? 518 ILE A CD1 1 
ATOM 3866 N N   . ASN A 1 519 ? 3.650   19.385  56.823  1.00 52.98  ? 519 ASN A N   1 
ATOM 3867 C CA  . ASN A 1 519 ? 3.066   20.155  57.908  1.00 43.29  ? 519 ASN A CA  1 
ATOM 3868 C C   . ASN A 1 519 ? 4.125   20.517  58.940  1.00 45.98  ? 519 ASN A C   1 
ATOM 3869 O O   . ASN A 1 519 ? 5.004   19.715  59.265  1.00 51.44  ? 519 ASN A O   1 
ATOM 3870 C CB  . ASN A 1 519 ? 1.936   19.372  58.573  1.00 45.68  ? 519 ASN A CB  1 
ATOM 3871 C CG  . ASN A 1 519 ? 0.834   19.012  57.602  1.00 50.44  ? 519 ASN A CG  1 
ATOM 3872 O OD1 . ASN A 1 519 ? 0.388   19.845  56.816  1.00 52.90  ? 519 ASN A OD1 1 
ATOM 3873 N ND2 . ASN A 1 519 ? 0.389   17.763  57.650  1.00 53.23  ? 519 ASN A ND2 1 
ATOM 3874 N N   . PHE A 1 520 ? 4.031   21.741  59.450  1.00 51.43  ? 520 PHE A N   1 
ATOM 3875 C CA  . PHE A 1 520 ? 4.945   22.237  60.468  1.00 44.53  ? 520 PHE A CA  1 
ATOM 3876 C C   . PHE A 1 520 ? 4.682   21.654  61.849  1.00 47.56  ? 520 PHE A C   1 
ATOM 3877 O O   . PHE A 1 520 ? 5.585   21.674  62.690  1.00 57.08  ? 520 PHE A O   1 
ATOM 3878 C CB  . PHE A 1 520 ? 4.858   23.763  60.556  1.00 45.36  ? 520 PHE A CB  1 
ATOM 3879 C CG  . PHE A 1 520 ? 5.818   24.482  59.659  1.00 40.68  ? 520 PHE A CG  1 
ATOM 3880 C CD1 . PHE A 1 520 ? 7.182   24.316  59.805  1.00 41.97  ? 520 PHE A CD1 1 
ATOM 3881 C CD2 . PHE A 1 520 ? 5.354   25.340  58.678  1.00 44.42  ? 520 PHE A CD2 1 
ATOM 3882 C CE1 . PHE A 1 520 ? 8.065   24.984  58.984  1.00 45.40  ? 520 PHE A CE1 1 
ATOM 3883 C CE2 . PHE A 1 520 ? 6.233   26.010  57.855  1.00 48.83  ? 520 PHE A CE2 1 
ATOM 3884 C CZ  . PHE A 1 520 ? 7.590   25.832  58.008  1.00 49.45  ? 520 PHE A CZ  1 
ATOM 3885 N N   . SER A 1 521 ? 3.483   21.134  62.098  1.00 54.40  ? 521 SER A N   1 
ATOM 3886 C CA  . SER A 1 521 ? 3.073   20.773  63.450  1.00 52.66  ? 521 SER A CA  1 
ATOM 3887 C C   . SER A 1 521 ? 3.987   19.708  64.038  1.00 57.30  ? 521 SER A C   1 
ATOM 3888 O O   . SER A 1 521 ? 3.990   18.559  63.585  1.00 64.83  ? 521 SER A O   1 
ATOM 3889 C CB  . SER A 1 521 ? 1.628   20.282  63.438  1.00 55.49  ? 521 SER A CB  1 
ATOM 3890 O OG  . SER A 1 521 ? 1.165   20.031  64.754  1.00 67.00  ? 521 SER A OG  1 
ATOM 3891 N N   . ASN A 1 522 ? 4.765   20.103  65.049  1.00 50.49  ? 522 ASN A N   1 
ATOM 3892 C CA  . ASN A 1 522 ? 5.641   19.204  65.794  1.00 49.03  ? 522 ASN A CA  1 
ATOM 3893 C C   . ASN A 1 522 ? 6.626   18.492  64.877  1.00 55.44  ? 522 ASN A C   1 
ATOM 3894 O O   . ASN A 1 522 ? 7.075   17.382  65.179  1.00 59.62  ? 522 ASN A O   1 
ATOM 3895 C CB  . ASN A 1 522 ? 4.815   18.189  66.586  1.00 54.57  ? 522 ASN A CB  1 
ATOM 3896 C CG  . ASN A 1 522 ? 4.043   18.828  67.720  1.00 54.92  ? 522 ASN A CG  1 
ATOM 3897 O OD1 . ASN A 1 522 ? 4.534   19.740  68.383  1.00 54.65  ? 522 ASN A OD1 1 
ATOM 3898 N ND2 . ASN A 1 522 ? 2.824   18.356  67.946  1.00 65.03  ? 522 ASN A ND2 1 
ATOM 3899 N N   . SER A 1 523 ? 6.967   19.124  63.756  1.00 62.29  ? 523 SER A N   1 
ATOM 3900 C CA  . SER A 1 523 ? 7.929   18.563  62.822  1.00 51.93  ? 523 SER A CA  1 
ATOM 3901 C C   . SER A 1 523 ? 9.012   19.596  62.557  1.00 54.23  ? 523 SER A C   1 
ATOM 3902 O O   . SER A 1 523 ? 8.885   20.378  61.602  1.00 59.16  ? 523 SER A O   1 
ATOM 3903 C CB  . SER A 1 523 ? 7.249   18.162  61.523  1.00 48.74  ? 523 SER A CB  1 
ATOM 3904 O OG  . SER A 1 523 ? 6.223   17.215  61.756  1.00 64.68  ? 523 SER A OG  1 
ATOM 3905 N N   . PRO A 1 524 ? 10.076  19.648  63.355  1.00 54.40  ? 524 PRO A N   1 
ATOM 3906 C CA  . PRO A 1 524 ? 11.128  20.642  63.115  1.00 52.66  ? 524 PRO A CA  1 
ATOM 3907 C C   . PRO A 1 524 ? 11.899  20.355  61.837  1.00 60.07  ? 524 PRO A C   1 
ATOM 3908 O O   . PRO A 1 524 ? 11.640  19.353  61.165  1.00 66.75  ? 524 PRO A O   1 
ATOM 3909 C CB  . PRO A 1 524 ? 12.021  20.521  64.354  1.00 51.07  ? 524 PRO A CB  1 
ATOM 3910 C CG  . PRO A 1 524 ? 11.768  19.160  64.878  1.00 56.27  ? 524 PRO A CG  1 
ATOM 3911 C CD  . PRO A 1 524 ? 10.370  18.782  64.508  1.00 49.97  ? 524 PRO A CD  1 
ATOM 3912 N N   . GLN A 1 525 ? 12.838  21.233  61.491  1.00 59.71  ? 525 GLN A N   1 
ATOM 3913 C CA  . GLN A 1 525 ? 13.606  21.061  60.267  1.00 47.23  ? 525 GLN A CA  1 
ATOM 3914 C C   . GLN A 1 525 ? 14.328  19.722  60.282  1.00 53.43  ? 525 GLN A C   1 
ATOM 3915 O O   . GLN A 1 525 ? 15.022  19.386  61.246  1.00 63.22  ? 525 GLN A O   1 
ATOM 3916 C CB  . GLN A 1 525 ? 14.608  22.201  60.102  1.00 49.52  ? 525 GLN A CB  1 
ATOM 3917 C CG  . GLN A 1 525 ? 15.611  21.985  58.988  1.00 47.68  ? 525 GLN A CG  1 
ATOM 3918 C CD  . GLN A 1 525 ? 15.067  22.378  57.633  1.00 56.44  ? 525 GLN A CD  1 
ATOM 3919 O OE1 . GLN A 1 525 ? 14.044  23.054  57.533  1.00 63.06  ? 525 GLN A OE1 1 
ATOM 3920 N NE2 . GLN A 1 525 ? 15.749  21.955  56.579  1.00 56.79  ? 525 GLN A NE2 1 
ATOM 3921 N N   . ALA A 1 526 ? 14.155  18.956  59.211  1.00 50.37  ? 526 ALA A N   1 
ATOM 3922 C CA  . ALA A 1 526 ? 14.743  17.629  59.130  1.00 50.62  ? 526 ALA A CA  1 
ATOM 3923 C C   . ALA A 1 526 ? 16.145  17.715  58.545  1.00 51.72  ? 526 ALA A C   1 
ATOM 3924 O O   . ALA A 1 526 ? 16.357  18.336  57.500  1.00 60.64  ? 526 ALA A O   1 
ATOM 3925 C CB  . ALA A 1 526 ? 13.871  16.710  58.279  1.00 46.79  ? 526 ALA A CB  1 
ATOM 3926 N N   . ALA A 1 527 ? 17.100  17.096  59.226  1.00 50.18  ? 527 ALA A N   1 
ATOM 3927 C CA  . ALA A 1 527 ? 18.457  16.958  58.728  1.00 43.74  ? 527 ALA A CA  1 
ATOM 3928 C C   . ALA A 1 527 ? 18.687  15.516  58.304  1.00 44.02  ? 527 ALA A C   1 
ATOM 3929 O O   . ALA A 1 527 ? 18.163  14.582  58.917  1.00 51.59  ? 527 ALA A O   1 
ATOM 3930 C CB  . ALA A 1 527 ? 19.484  17.370  59.785  1.00 49.96  ? 527 ALA A CB  1 
ATOM 3931 N N   . ASN A 1 528 ? 19.461  15.342  57.240  1.00 52.08  ? 528 ASN A N   1 
ATOM 3932 C CA  . ASN A 1 528 ? 19.742  14.006  56.735  1.00 48.36  ? 528 ASN A CA  1 
ATOM 3933 C C   . ASN A 1 528 ? 20.617  13.254  57.725  1.00 54.98  ? 528 ASN A C   1 
ATOM 3934 O O   . ASN A 1 528 ? 21.754  13.656  57.993  1.00 61.47  ? 528 ASN A O   1 
ATOM 3935 C CB  . ASN A 1 528 ? 20.417  14.086  55.372  1.00 50.43  ? 528 ASN A CB  1 
ATOM 3936 C CG  . ASN A 1 528 ? 19.499  14.625  54.309  1.00 56.35  ? 528 ASN A CG  1 
ATOM 3937 O OD1 . ASN A 1 528 ? 18.283  14.466  54.389  1.00 63.40  ? 528 ASN A OD1 1 
ATOM 3938 N ND2 . ASN A 1 528 ? 20.072  15.268  53.303  1.00 59.54  ? 528 ASN A ND2 1 
ATOM 3939 N N   . ASN A 1 529 ? 20.086  12.165  58.271  1.00 51.37  ? 529 ASN A N   1 
ATOM 3940 C CA  . ASN A 1 529 ? 20.805  11.324  59.223  1.00 50.29  ? 529 ASN A CA  1 
ATOM 3941 C C   . ASN A 1 529 ? 20.670  9.881   58.753  1.00 52.90  ? 529 ASN A C   1 
ATOM 3942 O O   . ASN A 1 529 ? 19.641  9.240   58.981  1.00 64.27  ? 529 ASN A O   1 
ATOM 3943 C CB  . ASN A 1 529 ? 20.269  11.506  60.637  1.00 53.03  ? 529 ASN A CB  1 
ATOM 3944 C CG  . ASN A 1 529 ? 21.249  11.045  61.691  1.00 60.46  ? 529 ASN A CG  1 
ATOM 3945 O OD1 . ASN A 1 529 ? 21.138  9.939   62.216  1.00 60.75  ? 529 ASN A OD1 1 
ATOM 3946 N ND2 . ASN A 1 529 ? 22.223  11.889  61.999  1.00 61.26  ? 529 ASN A ND2 1 
ATOM 3947 N N   . ALA A 1 530 ? 21.706  9.380   58.089  1.00 45.09  ? 530 ALA A N   1 
ATOM 3948 C CA  . ALA A 1 530 ? 21.744  8.017   57.570  1.00 46.95  ? 530 ALA A CA  1 
ATOM 3949 C C   . ALA A 1 530 ? 23.050  7.391   58.048  1.00 54.05  ? 530 ALA A C   1 
ATOM 3950 O O   . ALA A 1 530 ? 24.093  7.534   57.405  1.00 62.98  ? 530 ALA A O   1 
ATOM 3951 C CB  . ALA A 1 530 ? 21.629  8.004   56.055  1.00 45.76  ? 530 ALA A CB  1 
ATOM 3952 N N   . ILE A 1 531 ? 22.989  6.698   59.181  1.00 50.54  ? 531 ILE A N   1 
ATOM 3953 C CA  . ILE A 1 531 ? 24.163  6.118   59.817  1.00 55.09  ? 531 ILE A CA  1 
ATOM 3954 C C   . ILE A 1 531 ? 23.936  4.628   60.020  1.00 54.26  ? 531 ILE A C   1 
ATOM 3955 O O   . ILE A 1 531 ? 22.845  4.200   60.413  1.00 66.01  ? 531 ILE A O   1 
ATOM 3956 C CB  . ILE A 1 531 ? 24.488  6.817   61.155  1.00 54.86  ? 531 ILE A CB  1 
ATOM 3957 C CG1 . ILE A 1 531 ? 23.299  6.740   62.118  1.00 51.54  ? 531 ILE A CG1 1 
ATOM 3958 C CG2 . ILE A 1 531 ? 24.894  8.261   60.918  1.00 55.99  ? 531 ILE A CG2 1 
ATOM 3959 C CD1 . ILE A 1 531 ? 23.477  5.745   63.242  1.00 52.19  ? 531 ILE A CD1 1 
ATOM 3960 N N   . VAL A 1 532 ? 24.962  3.838   59.728  1.00 53.95  ? 532 VAL A N   1 
ATOM 3961 C CA  . VAL A 1 532 ? 24.969  2.407   59.998  1.00 54.46  ? 532 VAL A CA  1 
ATOM 3962 C C   . VAL A 1 532 ? 26.039  2.160   61.050  1.00 57.90  ? 532 VAL A C   1 
ATOM 3963 O O   . VAL A 1 532 ? 27.230  2.381   60.800  1.00 65.72  ? 532 VAL A O   1 
ATOM 3964 C CB  . VAL A 1 532 ? 25.234  1.584   58.731  1.00 51.29  ? 532 VAL A CB  1 
ATOM 3965 C CG1 . VAL A 1 532 ? 25.324  0.106   59.070  1.00 53.05  ? 532 VAL A CG1 1 
ATOM 3966 C CG2 . VAL A 1 532 ? 24.153  1.837   57.700  1.00 48.39  ? 532 VAL A CG2 1 
ATOM 3967 N N   . ASP A 1 533 ? 25.623  1.705   62.226  1.00 54.22  ? 533 ASP A N   1 
ATOM 3968 C CA  . ASP A 1 533 ? 26.546  1.464   63.326  1.00 54.32  ? 533 ASP A CA  1 
ATOM 3969 C C   . ASP A 1 533 ? 27.182  0.091   63.156  1.00 63.99  ? 533 ASP A C   1 
ATOM 3970 O O   . ASP A 1 533 ? 26.500  -0.933  63.259  1.00 70.03  ? 533 ASP A O   1 
ATOM 3971 C CB  . ASP A 1 533 ? 25.830  1.566   64.670  1.00 56.32  ? 533 ASP A CB  1 
ATOM 3972 C CG  . ASP A 1 533 ? 26.794  1.640   65.830  1.00 65.98  ? 533 ASP A CG  1 
ATOM 3973 O OD1 . ASP A 1 533 ? 27.066  2.760   66.306  1.00 71.03  ? 533 ASP A OD1 1 
ATOM 3974 O OD2 . ASP A 1 533 ? 27.282  0.579   66.267  1.00 69.25  ? 533 ASP A OD2 1 
ATOM 3975 N N   . LEU A 1 534 ? 28.484  0.074   62.897  1.00 60.99  ? 534 LEU A N   1 
ATOM 3976 C CA  . LEU A 1 534 ? 29.212  -1.169  62.652  1.00 57.75  ? 534 LEU A CA  1 
ATOM 3977 C C   . LEU A 1 534 ? 29.871  -1.676  63.931  1.00 61.83  ? 534 LEU A C   1 
ATOM 3978 O O   . LEU A 1 534 ? 31.080  -1.885  64.005  1.00 72.01  ? 534 LEU A O   1 
ATOM 3979 C CB  . LEU A 1 534 ? 30.240  -0.966  61.548  1.00 59.09  ? 534 LEU A CB  1 
ATOM 3980 C CG  . LEU A 1 534 ? 29.664  -0.442  60.239  1.00 58.25  ? 534 LEU A CG  1 
ATOM 3981 C CD1 . LEU A 1 534 ? 30.785  -0.184  59.271  1.00 62.77  ? 534 LEU A CD1 1 
ATOM 3982 C CD2 . LEU A 1 534 ? 28.675  -1.438  59.669  1.00 61.38  ? 534 LEU A CD2 1 
ATOM 3983 N N   . SER A 1 535 ? 29.047  -1.879  64.953  1.00 60.73  ? 535 SER A N   1 
ATOM 3984 C CA  . SER A 1 535 ? 29.519  -2.492  66.182  1.00 58.75  ? 535 SER A CA  1 
ATOM 3985 C C   . SER A 1 535 ? 29.545  -4.004  66.011  1.00 63.98  ? 535 SER A C   1 
ATOM 3986 O O   . SER A 1 535 ? 28.520  -4.616  65.699  1.00 75.70  ? 535 SER A O   1 
ATOM 3987 C CB  . SER A 1 535 ? 28.623  -2.102  67.357  1.00 62.32  ? 535 SER A CB  1 
ATOM 3988 O OG  . SER A 1 535 ? 29.017  -2.767  68.543  1.00 69.00  ? 535 SER A OG  1 
ATOM 3989 N N   . THR A 1 536 ? 30.721  -4.604  66.208  1.00 61.44  ? 536 THR A N   1 
ATOM 3990 C CA  . THR A 1 536 ? 30.840  -6.052  66.104  1.00 62.57  ? 536 THR A CA  1 
ATOM 3991 C C   . THR A 1 536 ? 29.966  -6.780  67.114  1.00 63.75  ? 536 THR A C   1 
ATOM 3992 O O   . THR A 1 536 ? 29.648  -7.954  66.901  1.00 69.86  ? 536 THR A O   1 
ATOM 3993 C CB  . THR A 1 536 ? 32.298  -6.478  66.284  1.00 66.55  ? 536 THR A CB  1 
ATOM 3994 O OG1 . THR A 1 536 ? 32.778  -6.021  67.554  1.00 71.29  ? 536 THR A OG1 1 
ATOM 3995 C CG2 . THR A 1 536 ? 33.160  -5.888  65.182  1.00 63.51  ? 536 THR A CG2 1 
ATOM 3996 N N   . THR A 1 537 ? 29.580  -6.114  68.201  1.00 57.34  ? 537 THR A N   1 
ATOM 3997 C CA  . THR A 1 537 ? 28.621  -6.680  69.137  1.00 57.54  ? 537 THR A CA  1 
ATOM 3998 C C   . THR A 1 537 ? 27.265  -6.919  68.489  1.00 59.47  ? 537 THR A C   1 
ATOM 3999 O O   . THR A 1 537 ? 26.656  -7.974  68.703  1.00 67.82  ? 537 THR A O   1 
ATOM 4000 C CB  . THR A 1 537 ? 28.470  -5.752  70.344  1.00 57.61  ? 537 THR A CB  1 
ATOM 4001 O OG1 . THR A 1 537 ? 29.689  -5.738  71.095  1.00 67.89  ? 537 THR A OG1 1 
ATOM 4002 C CG2 . THR A 1 537 ? 27.334  -6.205  71.232  1.00 54.68  ? 537 THR A CG2 1 
ATOM 4003 N N   . TYR A 1 538 ? 26.785  -5.969  67.688  1.00 57.69  ? 538 TYR A N   1 
ATOM 4004 C CA  . TYR A 1 538 ? 25.479  -6.055  67.051  1.00 55.75  ? 538 TYR A CA  1 
ATOM 4005 C C   . TYR A 1 538 ? 25.593  -6.207  65.539  1.00 55.75  ? 538 TYR A C   1 
ATOM 4006 O O   . TYR A 1 538 ? 24.689  -5.810  64.802  1.00 64.10  ? 538 TYR A O   1 
ATOM 4007 C CB  . TYR A 1 538 ? 24.638  -4.830  67.398  1.00 56.51  ? 538 TYR A CB  1 
ATOM 4008 C CG  . TYR A 1 538 ? 24.550  -4.571  68.880  1.00 59.49  ? 538 TYR A CG  1 
ATOM 4009 C CD1 . TYR A 1 538 ? 23.727  -5.339  69.689  1.00 57.31  ? 538 TYR A CD1 1 
ATOM 4010 C CD2 . TYR A 1 538 ? 25.306  -3.573  69.474  1.00 55.72  ? 538 TYR A CD2 1 
ATOM 4011 C CE1 . TYR A 1 538 ? 23.648  -5.111  71.045  1.00 59.86  ? 538 TYR A CE1 1 
ATOM 4012 C CE2 . TYR A 1 538 ? 25.237  -3.339  70.827  1.00 57.86  ? 538 TYR A CE2 1 
ATOM 4013 C CZ  . TYR A 1 538 ? 24.406  -4.111  71.609  1.00 62.88  ? 538 TYR A CZ  1 
ATOM 4014 O OH  . TYR A 1 538 ? 24.331  -3.882  72.962  1.00 70.01  ? 538 TYR A OH  1 
ATOM 4015 N N   . SER A 1 539 ? 26.697  -6.788  65.064  1.00 57.00  ? 539 SER A N   1 
ATOM 4016 C CA  . SER A 1 539 ? 26.908  -6.919  63.627  1.00 56.87  ? 539 SER A CA  1 
ATOM 4017 C C   . SER A 1 539 ? 25.816  -7.752  62.970  1.00 59.71  ? 539 SER A C   1 
ATOM 4018 O O   . SER A 1 539 ? 25.349  -7.410  61.879  1.00 64.66  ? 539 SER A O   1 
ATOM 4019 C CB  . SER A 1 539 ? 28.280  -7.530  63.352  1.00 51.97  ? 539 SER A CB  1 
ATOM 4020 O OG  . SER A 1 539 ? 28.393  -8.810  63.944  1.00 66.14  ? 539 SER A OG  1 
ATOM 4021 N N   . ALA A 1 540 ? 25.390  -8.833  63.618  1.00 56.87  ? 540 ALA A N   1 
ATOM 4022 C CA  . ALA A 1 540 ? 24.317  -9.675  63.114  1.00 48.57  ? 540 ALA A CA  1 
ATOM 4023 C C   . ALA A 1 540 ? 22.946  -9.039  63.263  1.00 48.62  ? 540 ALA A C   1 
ATOM 4024 O O   . ALA A 1 540 ? 21.974  -9.550  62.698  1.00 54.51  ? 540 ALA A O   1 
ATOM 4025 C CB  . ALA A 1 540 ? 24.331  -11.026 63.829  1.00 47.66  ? 540 ALA A CB  1 
ATOM 4026 N N   . ASP A 1 541 ? 22.842  -7.943  64.001  1.00 56.93  ? 541 ASP A N   1 
ATOM 4027 C CA  . ASP A 1 541 ? 21.572  -7.300  64.285  1.00 52.11  ? 541 ASP A CA  1 
ATOM 4028 C C   . ASP A 1 541 ? 21.280  -6.213  63.258  1.00 60.74  ? 541 ASP A C   1 
ATOM 4029 O O   . ASP A 1 541 ? 22.178  -5.654  62.628  1.00 66.28  ? 541 ASP A O   1 
ATOM 4030 C CB  . ASP A 1 541 ? 21.586  -6.719  65.699  1.00 50.53  ? 541 ASP A CB  1 
ATOM 4031 C CG  . ASP A 1 541 ? 21.799  -7.780  66.755  1.00 65.70  ? 541 ASP A CG  1 
ATOM 4032 O OD1 . ASP A 1 541 ? 21.245  -8.888  66.604  1.00 65.55  ? 541 ASP A OD1 1 
ATOM 4033 O OD2 . ASP A 1 541 ? 22.541  -7.516  67.722  1.00 73.06  ? 541 ASP A OD2 1 
ATOM 4034 N N   . ARG A 1 542 ? 19.995  -5.925  63.093  1.00 47.42  ? 542 ARG A N   1 
ATOM 4035 C CA  . ARG A 1 542 ? 19.544  -4.887  62.180  1.00 42.94  ? 542 ARG A CA  1 
ATOM 4036 C C   . ARG A 1 542 ? 19.940  -3.520  62.717  1.00 44.14  ? 542 ARG A C   1 
ATOM 4037 O O   . ARG A 1 542 ? 19.918  -3.285  63.928  1.00 53.44  ? 542 ARG A O   1 
ATOM 4038 C CB  . ARG A 1 542 ? 18.030  -4.963  61.997  1.00 41.00  ? 542 ARG A CB  1 
ATOM 4039 C CG  . ARG A 1 542 ? 17.478  -4.132  60.857  1.00 37.35  ? 542 ARG A CG  1 
ATOM 4040 C CD  . ARG A 1 542 ? 16.175  -4.729  60.367  1.00 45.86  ? 542 ARG A CD  1 
ATOM 4041 N NE  . ARG A 1 542 ? 15.023  -3.981  60.851  1.00 47.47  ? 542 ARG A NE  1 
ATOM 4042 C CZ  . ARG A 1 542 ? 13.848  -3.935  60.240  1.00 40.71  ? 542 ARG A CZ  1 
ATOM 4043 N NH1 . ARG A 1 542 ? 13.631  -4.594  59.115  1.00 47.37  ? 542 ARG A NH1 1 
ATOM 4044 N NH2 . ARG A 1 542 ? 12.867  -3.216  60.774  1.00 40.49  ? 542 ARG A NH2 1 
ATOM 4045 N N   . LYS A 1 543 ? 20.314  -2.623  61.812  1.00 42.44  ? 543 LYS A N   1 
ATOM 4046 C CA  . LYS A 1 543 ? 20.659  -1.254  62.163  1.00 41.20  ? 543 LYS A CA  1 
ATOM 4047 C C   . LYS A 1 543 ? 19.632  -0.309  61.564  1.00 41.56  ? 543 LYS A C   1 
ATOM 4048 O O   . LYS A 1 543 ? 19.295  -0.421  60.381  1.00 49.25  ? 543 LYS A O   1 
ATOM 4049 C CB  . LYS A 1 543 ? 22.060  -0.883  61.671  1.00 45.14  ? 543 LYS A CB  1 
ATOM 4050 C CG  . LYS A 1 543 ? 23.185  -1.580  62.402  1.00 40.66  ? 543 LYS A CG  1 
ATOM 4051 C CD  . LYS A 1 543 ? 23.564  -2.874  61.716  1.00 45.60  ? 543 LYS A CD  1 
ATOM 4052 C CE  . LYS A 1 543 ? 24.679  -3.562  62.463  1.00 40.36  ? 543 LYS A CE  1 
ATOM 4053 N NZ  . LYS A 1 543 ? 24.240  -3.887  63.840  1.00 59.34  ? 543 LYS A NZ  1 
ATOM 4054 N N   . PHE A 1 544 ? 19.135  0.612   62.381  1.00 38.43  ? 544 PHE A N   1 
ATOM 4055 C CA  . PHE A 1 544 ? 18.240  1.647   61.888  1.00 35.84  ? 544 PHE A CA  1 
ATOM 4056 C C   . PHE A 1 544 ? 19.057  2.752   61.232  1.00 44.40  ? 544 PHE A C   1 
ATOM 4057 O O   . PHE A 1 544 ? 19.668  3.573   61.923  1.00 54.80  ? 544 PHE A O   1 
ATOM 4058 C CB  . PHE A 1 544 ? 17.400  2.202   63.033  1.00 33.83  ? 544 PHE A CB  1 
ATOM 4059 C CG  . PHE A 1 544 ? 16.608  3.418   62.665  1.00 43.74  ? 544 PHE A CG  1 
ATOM 4060 C CD1 . PHE A 1 544 ? 15.577  3.337   61.748  1.00 43.54  ? 544 PHE A CD1 1 
ATOM 4061 C CD2 . PHE A 1 544 ? 16.894  4.644   63.236  1.00 47.73  ? 544 PHE A CD2 1 
ATOM 4062 C CE1 . PHE A 1 544 ? 14.847  4.451   61.411  1.00 41.40  ? 544 PHE A CE1 1 
ATOM 4063 C CE2 . PHE A 1 544 ? 16.166  5.763   62.900  1.00 48.30  ? 544 PHE A CE2 1 
ATOM 4064 C CZ  . PHE A 1 544 ? 15.141  5.665   61.988  1.00 42.37  ? 544 PHE A CZ  1 
ATOM 4065 N N   . VAL A 1 545 ? 19.084  2.761   59.900  1.00 37.16  ? 545 VAL A N   1 
ATOM 4066 C CA  . VAL A 1 545 ? 19.837  3.774   59.172  1.00 43.89  ? 545 VAL A CA  1 
ATOM 4067 C C   . VAL A 1 545 ? 19.308  5.182   59.413  1.00 48.79  ? 545 VAL A C   1 
ATOM 4068 O O   . VAL A 1 545 ? 20.102  6.098   59.668  1.00 55.11  ? 545 VAL A O   1 
ATOM 4069 C CB  . VAL A 1 545 ? 19.832  3.481   57.661  1.00 39.85  ? 545 VAL A CB  1 
ATOM 4070 C CG1 . VAL A 1 545 ? 20.623  4.533   56.910  1.00 42.25  ? 545 VAL A CG1 1 
ATOM 4071 C CG2 . VAL A 1 545 ? 20.393  2.102   57.391  1.00 42.34  ? 545 VAL A CG2 1 
ATOM 4072 N N   . GLY A 1 546 ? 18.000  5.375   59.362  1.00 46.34  ? 546 GLY A N   1 
ATOM 4073 C CA  . GLY A 1 546 ? 17.375  6.667   59.492  1.00 46.39  ? 546 GLY A CA  1 
ATOM 4074 C C   . GLY A 1 546 ? 16.063  6.692   58.755  1.00 51.33  ? 546 GLY A C   1 
ATOM 4075 O O   . GLY A 1 546 ? 15.440  5.655   58.502  1.00 49.81  ? 546 GLY A O   1 
ATOM 4076 N N   . ARG A 1 547 ? 15.628  7.893   58.397  1.00 50.95  ? 547 ARG A N   1 
ATOM 4077 C CA  . ARG A 1 547 ? 14.372  8.089   57.696  1.00 36.36  ? 547 ARG A CA  1 
ATOM 4078 C C   . ARG A 1 547 ? 14.606  8.850   56.400  1.00 43.39  ? 547 ARG A C   1 
ATOM 4079 O O   . ARG A 1 547 ? 15.555  9.628   56.278  1.00 54.43  ? 547 ARG A O   1 
ATOM 4080 C CB  . ARG A 1 547 ? 13.366  8.849   58.564  1.00 37.21  ? 547 ARG A CB  1 
ATOM 4081 C CG  . ARG A 1 547 ? 13.744  10.297  58.809  1.00 33.63  ? 547 ARG A CG  1 
ATOM 4082 C CD  . ARG A 1 547 ? 12.563  11.104  59.290  1.00 38.29  ? 547 ARG A CD  1 
ATOM 4083 N NE  . ARG A 1 547 ? 12.951  12.449  59.692  1.00 41.56  ? 547 ARG A NE  1 
ATOM 4084 C CZ  . ARG A 1 547 ? 12.165  13.287  60.353  1.00 44.35  ? 547 ARG A CZ  1 
ATOM 4085 N NH1 . ARG A 1 547 ? 10.937  12.949  60.704  1.00 42.83  ? 547 ARG A NH1 1 
ATOM 4086 N NH2 . ARG A 1 547 ? 12.624  14.494  60.666  1.00 46.61  ? 547 ARG A NH2 1 
ATOM 4087 N N   . ILE A 1 548 ? 13.736  8.602   55.429  1.00 40.57  ? 548 ILE A N   1 
ATOM 4088 C CA  . ILE A 1 548 ? 13.654  9.400   54.213  1.00 37.35  ? 548 ILE A CA  1 
ATOM 4089 C C   . ILE A 1 548 ? 12.275  10.040  54.194  1.00 40.42  ? 548 ILE A C   1 
ATOM 4090 O O   . ILE A 1 548 ? 11.265  9.360   54.413  1.00 56.45  ? 548 ILE A O   1 
ATOM 4091 C CB  . ILE A 1 548 ? 13.895  8.561   52.950  1.00 39.57  ? 548 ILE A CB  1 
ATOM 4092 C CG1 . ILE A 1 548 ? 13.084  7.269   52.995  1.00 46.01  ? 548 ILE A CG1 1 
ATOM 4093 C CG2 . ILE A 1 548 ? 15.370  8.251   52.794  1.00 41.64  ? 548 ILE A CG2 1 
ATOM 4094 C CD1 . ILE A 1 548 ? 13.021  6.550   51.676  1.00 44.05  ? 548 ILE A CD1 1 
ATOM 4095 N N   . LEU A 1 549 ? 12.230  11.344  53.958  1.00 40.55  ? 549 LEU A N   1 
ATOM 4096 C CA  . LEU A 1 549 ? 10.971  12.067  53.967  1.00 37.42  ? 549 LEU A CA  1 
ATOM 4097 C C   . LEU A 1 549 ? 10.508  12.353  52.547  1.00 47.74  ? 549 LEU A C   1 
ATOM 4098 O O   . LEU A 1 549 ? 11.306  12.423  51.612  1.00 50.19  ? 549 LEU A O   1 
ATOM 4099 C CB  . LEU A 1 549 ? 11.105  13.377  54.744  1.00 29.06  ? 549 LEU A CB  1 
ATOM 4100 C CG  . LEU A 1 549 ? 11.230  13.244  56.262  1.00 36.65  ? 549 LEU A CG  1 
ATOM 4101 C CD1 . LEU A 1 549 ? 11.238  14.610  56.916  1.00 44.60  ? 549 LEU A CD1 1 
ATOM 4102 C CD2 . LEU A 1 549 ? 10.108  12.392  56.817  1.00 43.30  ? 549 LEU A CD2 1 
ATOM 4103 N N   . GLY A 1 550 ? 9.196   12.493  52.392  1.00 53.49  ? 550 GLY A N   1 
ATOM 4104 C CA  . GLY A 1 550 ? 8.634   12.935  51.134  1.00 40.02  ? 550 GLY A CA  1 
ATOM 4105 C C   . GLY A 1 550 ? 8.248   11.835  50.173  1.00 43.96  ? 550 GLY A C   1 
ATOM 4106 O O   . GLY A 1 550 ? 8.813   10.739  50.200  1.00 59.91  ? 550 GLY A O   1 
ATOM 4107 N N   . ARG A 1 551 ? 7.276   12.125  49.317  1.00 52.25  ? 551 ARG A N   1 
ATOM 4108 C CA  . ARG A 1 551 ? 6.879   11.237  48.238  1.00 42.82  ? 551 ARG A CA  1 
ATOM 4109 C C   . ARG A 1 551 ? 7.640   11.615  46.975  1.00 52.86  ? 551 ARG A C   1 
ATOM 4110 O O   . ARG A 1 551 ? 7.580   12.761  46.522  1.00 65.25  ? 551 ARG A O   1 
ATOM 4111 C CB  . ARG A 1 551 ? 5.373   11.327  47.984  1.00 44.80  ? 551 ARG A CB  1 
ATOM 4112 C CG  . ARG A 1 551 ? 4.841   10.253  47.063  1.00 55.85  ? 551 ARG A CG  1 
ATOM 4113 C CD  . ARG A 1 551 ? 3.367   10.441  46.769  1.00 51.85  ? 551 ARG A CD  1 
ATOM 4114 N NE  . ARG A 1 551 ? 2.587   9.276   47.170  1.00 61.30  ? 551 ARG A NE  1 
ATOM 4115 C CZ  . ARG A 1 551 ? 1.395   8.966   46.680  1.00 64.24  ? 551 ARG A CZ  1 
ATOM 4116 N NH1 . ARG A 1 551 ? 0.829   9.693   45.732  1.00 63.71  ? 551 ARG A NH1 1 
ATOM 4117 N NH2 . ARG A 1 551 ? 0.762   7.895   47.145  1.00 60.29  ? 551 ARG A NH2 1 
ATOM 4118 N N   . GLY A 1 552 ? 8.352   10.657  46.415  1.00 39.86  ? 552 GLY A N   1 
ATOM 4119 C CA  . GLY A 1 552 ? 9.125   10.909  45.216  1.00 49.34  ? 552 GLY A CA  1 
ATOM 4120 C C   . GLY A 1 552 ? 10.167  9.829   45.012  1.00 49.24  ? 552 GLY A C   1 
ATOM 4121 O O   . GLY A 1 552 ? 10.170  8.798   45.677  1.00 58.78  ? 552 GLY A O   1 
ATOM 4122 N N   . TRP A 1 553 ? 11.058  10.096  44.064  1.00 42.23  ? 553 TRP A N   1 
ATOM 4123 C CA  . TRP A 1 553 ? 12.135  9.180   43.716  1.00 38.54  ? 553 TRP A CA  1 
ATOM 4124 C C   . TRP A 1 553 ? 13.246  9.309   44.747  1.00 48.58  ? 553 TRP A C   1 
ATOM 4125 O O   . TRP A 1 553 ? 13.719  10.416  45.023  1.00 49.61  ? 553 TRP A O   1 
ATOM 4126 C CB  . TRP A 1 553 ? 12.661  9.463   42.311  1.00 42.69  ? 553 TRP A CB  1 
ATOM 4127 C CG  . TRP A 1 553 ? 11.631  9.252   41.257  1.00 43.69  ? 553 TRP A CG  1 
ATOM 4128 C CD1 . TRP A 1 553 ? 10.857  10.202  40.668  1.00 43.35  ? 553 TRP A CD1 1 
ATOM 4129 C CD2 . TRP A 1 553 ? 11.240  8.002   40.685  1.00 43.58  ? 553 TRP A CD2 1 
ATOM 4130 N NE1 . TRP A 1 553 ? 10.015  9.625   39.751  1.00 45.14  ? 553 TRP A NE1 1 
ATOM 4131 C CE2 . TRP A 1 553 ? 10.231  8.273   39.743  1.00 47.60  ? 553 TRP A CE2 1 
ATOM 4132 C CE3 . TRP A 1 553 ? 11.650  6.680   40.872  1.00 39.68  ? 553 TRP A CE3 1 
ATOM 4133 C CZ2 . TRP A 1 553 ? 9.624   7.272   38.993  1.00 52.57  ? 553 TRP A CZ2 1 
ATOM 4134 C CZ3 . TRP A 1 553 ? 11.049  5.690   40.125  1.00 40.53  ? 553 TRP A CZ3 1 
ATOM 4135 C CH2 . TRP A 1 553 ? 10.049  5.991   39.197  1.00 43.14  ? 553 TRP A CH2 1 
ATOM 4136 N N   . LYS A 1 554 ? 13.659  8.179   45.310  1.00 53.28  ? 554 LYS A N   1 
ATOM 4137 C CA  . LYS A 1 554 ? 14.657  8.137   46.365  1.00 41.69  ? 554 LYS A CA  1 
ATOM 4138 C C   . LYS A 1 554 ? 15.827  7.275   45.920  1.00 45.15  ? 554 LYS A C   1 
ATOM 4139 O O   . LYS A 1 554 ? 15.636  6.285   45.209  1.00 49.16  ? 554 LYS A O   1 
ATOM 4140 C CB  . LYS A 1 554 ? 14.061  7.580   47.658  1.00 41.69  ? 554 LYS A CB  1 
ATOM 4141 C CG  . LYS A 1 554 ? 12.782  8.261   48.087  1.00 45.55  ? 554 LYS A CG  1 
ATOM 4142 C CD  . LYS A 1 554 ? 13.067  9.613   48.701  1.00 49.08  ? 554 LYS A CD  1 
ATOM 4143 C CE  . LYS A 1 554 ? 11.825  10.185  49.344  1.00 45.95  ? 554 LYS A CE  1 
ATOM 4144 N NZ  . LYS A 1 554 ? 11.860  11.669  49.372  1.00 62.75  ? 554 LYS A NZ  1 
ATOM 4145 N N   . THR A 1 555 ? 17.030  7.661   46.327  1.00 49.53  ? 555 THR A N   1 
ATOM 4146 C CA  . THR A 1 555 ? 18.225  6.848   46.150  1.00 48.78  ? 555 THR A CA  1 
ATOM 4147 C C   . THR A 1 555 ? 18.899  6.672   47.500  1.00 47.52  ? 555 THR A C   1 
ATOM 4148 O O   . THR A 1 555 ? 19.137  7.652   48.212  1.00 53.04  ? 555 THR A O   1 
ATOM 4149 C CB  . THR A 1 555 ? 19.196  7.487   45.155  1.00 48.47  ? 555 THR A CB  1 
ATOM 4150 O OG1 . THR A 1 555 ? 18.563  7.606   43.877  1.00 62.17  ? 555 THR A OG1 1 
ATOM 4151 C CG2 . THR A 1 555 ? 20.448  6.639   45.013  1.00 43.13  ? 555 THR A CG2 1 
ATOM 4152 N N   . LEU A 1 556 ? 19.193  5.427   47.855  1.00 53.79  ? 556 LEU A N   1 
ATOM 4153 C CA  . LEU A 1 556 ? 19.929  5.116   49.073  1.00 56.76  ? 556 LEU A CA  1 
ATOM 4154 C C   . LEU A 1 556 ? 21.328  4.674   48.664  1.00 56.61  ? 556 LEU A C   1 
ATOM 4155 O O   . LEU A 1 556 ? 21.518  3.548   48.198  1.00 62.43  ? 556 LEU A O   1 
ATOM 4156 C CB  . LEU A 1 556 ? 19.220  4.036   49.885  1.00 54.85  ? 556 LEU A CB  1 
ATOM 4157 C CG  . LEU A 1 556 ? 17.733  4.272   50.142  1.00 53.35  ? 556 LEU A CG  1 
ATOM 4158 C CD1 . LEU A 1 556 ? 17.120  3.069   50.829  1.00 52.93  ? 556 LEU A CD1 1 
ATOM 4159 C CD2 . LEU A 1 556 ? 17.510  5.533   50.955  1.00 50.70  ? 556 LEU A CD2 1 
ATOM 4160 N N   . THR A 1 557 ? 22.300  5.560   48.839  1.00 43.45  ? 557 THR A N   1 
ATOM 4161 C CA  . THR A 1 557 ? 23.673  5.307   48.424  1.00 38.04  ? 557 THR A CA  1 
ATOM 4162 C C   . THR A 1 557 ? 24.445  4.702   49.588  1.00 41.57  ? 557 THR A C   1 
ATOM 4163 O O   . THR A 1 557 ? 24.653  5.363   50.609  1.00 46.95  ? 557 THR A O   1 
ATOM 4164 C CB  . THR A 1 557 ? 24.347  6.594   47.951  1.00 49.70  ? 557 THR A CB  1 
ATOM 4165 O OG1 . THR A 1 557 ? 23.589  7.162   46.876  1.00 56.15  ? 557 THR A OG1 1 
ATOM 4166 C CG2 . THR A 1 557 ? 25.759  6.306   47.472  1.00 41.28  ? 557 THR A CG2 1 
ATOM 4167 N N   . PHE A 1 558 ? 24.866  3.454   49.430  1.00 51.38  ? 558 PHE A N   1 
ATOM 4168 C CA  . PHE A 1 558 ? 25.725  2.772   50.390  1.00 48.50  ? 558 PHE A CA  1 
ATOM 4169 C C   . PHE A 1 558 ? 27.112  2.686   49.770  1.00 52.26  ? 558 PHE A C   1 
ATOM 4170 O O   . PHE A 1 558 ? 27.307  1.980   48.777  1.00 64.61  ? 558 PHE A O   1 
ATOM 4171 C CB  . PHE A 1 558 ? 25.187  1.382   50.720  1.00 47.78  ? 558 PHE A CB  1 
ATOM 4172 C CG  . PHE A 1 558 ? 23.962  1.392   51.582  1.00 52.14  ? 558 PHE A CG  1 
ATOM 4173 C CD1 . PHE A 1 558 ? 24.069  1.342   52.960  1.00 45.06  ? 558 PHE A CD1 1 
ATOM 4174 C CD2 . PHE A 1 558 ? 22.702  1.456   51.014  1.00 50.29  ? 558 PHE A CD2 1 
ATOM 4175 C CE1 . PHE A 1 558 ? 22.943  1.350   53.754  1.00 48.41  ? 558 PHE A CE1 1 
ATOM 4176 C CE2 . PHE A 1 558 ? 21.573  1.466   51.804  1.00 49.41  ? 558 PHE A CE2 1 
ATOM 4177 C CZ  . PHE A 1 558 ? 21.694  1.414   53.176  1.00 52.49  ? 558 PHE A CZ  1 
ATOM 4178 N N   . PHE A 1 559 ? 28.067  3.413   50.337  1.00 45.85  ? 559 PHE A N   1 
ATOM 4179 C CA  . PHE A 1 559 ? 29.424  3.418   49.818  1.00 44.50  ? 559 PHE A CA  1 
ATOM 4180 C C   . PHE A 1 559 ? 30.438  3.429   50.951  1.00 46.67  ? 559 PHE A C   1 
ATOM 4181 O O   . PHE A 1 559 ? 30.247  4.092   51.976  1.00 60.30  ? 559 PHE A O   1 
ATOM 4182 C CB  . PHE A 1 559 ? 29.662  4.614   48.884  1.00 51.26  ? 559 PHE A CB  1 
ATOM 4183 C CG  . PHE A 1 559 ? 29.611  5.951   49.567  1.00 51.74  ? 559 PHE A CG  1 
ATOM 4184 C CD1 . PHE A 1 559 ? 28.401  6.573   49.812  1.00 51.16  ? 559 PHE A CD1 1 
ATOM 4185 C CD2 . PHE A 1 559 ? 30.776  6.598   49.939  1.00 51.71  ? 559 PHE A CD2 1 
ATOM 4186 C CE1 . PHE A 1 559 ? 28.353  7.804   50.430  1.00 52.64  ? 559 PHE A CE1 1 
ATOM 4187 C CE2 . PHE A 1 559 ? 30.734  7.831   50.557  1.00 53.01  ? 559 PHE A CE2 1 
ATOM 4188 C CZ  . PHE A 1 559 ? 29.520  8.436   50.797  1.00 53.13  ? 559 PHE A CZ  1 
ATOM 4189 N N   . THR A 1 560 ? 31.514  2.676   50.756  1.00 54.87  ? 560 THR A N   1 
ATOM 4190 C CA  . THR A 1 560 ? 32.635  2.664   51.678  1.00 60.54  ? 560 THR A CA  1 
ATOM 4191 C C   . THR A 1 560 ? 33.562  3.837   51.371  1.00 59.69  ? 560 THR A C   1 
ATOM 4192 O O   . THR A 1 560 ? 33.212  4.761   50.633  1.00 69.74  ? 560 THR A O   1 
ATOM 4193 C CB  . THR A 1 560 ? 33.378  1.333   51.601  1.00 58.53  ? 560 THR A CB  1 
ATOM 4194 O OG1 . THR A 1 560 ? 33.587  0.980   50.229  1.00 62.76  ? 560 THR A OG1 1 
ATOM 4195 C CG2 . THR A 1 560 ? 32.579  0.239   52.285  1.00 56.14  ? 560 THR A CG2 1 
ATOM 4196 N N   . ASN A 1 561 ? 34.756  3.806   51.956  1.00 67.18  ? 561 ASN A N   1 
ATOM 4197 C CA  . ASN A 1 561 ? 35.724  4.873   51.741  1.00 66.85  ? 561 ASN A CA  1 
ATOM 4198 C C   . ASN A 1 561 ? 36.035  5.020   50.257  1.00 72.30  ? 561 ASN A C   1 
ATOM 4199 O O   . ASN A 1 561 ? 36.577  4.108   49.629  1.00 78.72  ? 561 ASN A O   1 
ATOM 4200 C CB  . ASN A 1 561 ? 37.002  4.588   52.529  1.00 70.51  ? 561 ASN A CB  1 
ATOM 4201 C CG  . ASN A 1 561 ? 37.848  5.825   52.733  1.00 75.59  ? 561 ASN A CG  1 
ATOM 4202 O OD1 . ASN A 1 561 ? 37.666  6.834   52.055  1.00 79.71  ? 561 ASN A OD1 1 
ATOM 4203 N ND2 . ASN A 1 561 ? 38.781  5.754   53.673  1.00 76.97  ? 561 ASN A ND2 1 
ATOM 4204 N N   . LEU A 1 562 ? 35.682  6.179   49.698  1.00 66.71  ? 562 LEU A N   1 
ATOM 4205 C CA  . LEU A 1 562 ? 35.869  6.431   48.275  1.00 68.26  ? 562 LEU A CA  1 
ATOM 4206 C C   . LEU A 1 562 ? 37.332  6.554   47.879  1.00 71.36  ? 562 LEU A C   1 
ATOM 4207 O O   . LEU A 1 562 ? 37.645  6.421   46.692  1.00 72.51  ? 562 LEU A O   1 
ATOM 4208 C CB  . LEU A 1 562 ? 35.116  7.696   47.868  1.00 69.53  ? 562 LEU A CB  1 
ATOM 4209 C CG  . LEU A 1 562 ? 33.594  7.610   47.964  1.00 69.24  ? 562 LEU A CG  1 
ATOM 4210 C CD1 . LEU A 1 562 ? 32.947  8.858   47.394  1.00 70.75  ? 562 LEU A CD1 1 
ATOM 4211 C CD2 . LEU A 1 562 ? 33.093  6.369   47.246  1.00 66.41  ? 562 LEU A CD2 1 
ATOM 4212 N N   . GLN A 1 563 ? 38.228  6.800   48.829  1.00 80.72  ? 563 GLN A N   1 
ATOM 4213 C CA  . GLN A 1 563 ? 39.652  6.906   48.549  1.00 83.02  ? 563 GLN A CA  1 
ATOM 4214 C C   . GLN A 1 563 ? 40.354  5.556   48.562  1.00 83.35  ? 563 GLN A C   1 
ATOM 4215 O O   . GLN A 1 563 ? 41.565  5.502   48.332  1.00 83.10  ? 563 GLN A O   1 
ATOM 4216 C CB  . GLN A 1 563 ? 40.327  7.850   49.553  1.00 82.54  ? 563 GLN A CB  1 
ATOM 4217 C CG  . GLN A 1 563 ? 39.958  9.321   49.392  1.00 81.57  ? 563 GLN A CG  1 
ATOM 4218 C CD  . GLN A 1 563 ? 38.522  9.626   49.773  1.00 86.53  ? 563 GLN A CD  1 
ATOM 4219 O OE1 . GLN A 1 563 ? 38.093  9.352   50.893  1.00 84.43  ? 563 GLN A OE1 1 
ATOM 4220 N NE2 . GLN A 1 563 ? 37.770  10.192  48.837  1.00 85.99  ? 563 GLN A NE2 1 
ATOM 4221 N N   . GLY A 1 564 ? 39.628  4.471   48.825  1.00 81.36  ? 564 GLY A N   1 
ATOM 4222 C CA  . GLY A 1 564 ? 40.205  3.147   48.845  1.00 77.35  ? 564 GLY A CA  1 
ATOM 4223 C C   . GLY A 1 564 ? 41.013  2.820   50.080  1.00 81.06  ? 564 GLY A C   1 
ATOM 4224 O O   . GLY A 1 564 ? 41.799  1.865   50.050  1.00 87.39  ? 564 GLY A O   1 
ATOM 4225 N N   . THR A 1 565 ? 40.861  3.585   51.161  1.00 78.59  ? 565 THR A N   1 
ATOM 4226 C CA  . THR A 1 565 ? 41.602  3.362   52.395  1.00 82.04  ? 565 THR A CA  1 
ATOM 4227 C C   . THR A 1 565 ? 40.697  2.924   53.541  1.00 80.64  ? 565 THR A C   1 
ATOM 4228 O O   . THR A 1 565 ? 41.017  3.161   54.710  1.00 81.89  ? 565 THR A O   1 
ATOM 4229 C CB  . THR A 1 565 ? 42.377  4.620   52.785  1.00 85.52  ? 565 THR A CB  1 
ATOM 4230 O OG1 . THR A 1 565 ? 41.456  5.681   53.069  1.00 86.92  ? 565 THR A OG1 1 
ATOM 4231 C CG2 . THR A 1 565 ? 43.299  5.046   51.654  1.00 81.23  ? 565 THR A CG2 1 
ATOM 4232 N N   . GLY A 1 566 ? 39.573  2.288   53.228  1.00 71.00  ? 566 GLY A N   1 
ATOM 4233 C CA  . GLY A 1 566 ? 38.658  1.833   54.252  1.00 69.25  ? 566 GLY A CA  1 
ATOM 4234 C C   . GLY A 1 566 ? 38.530  0.326   54.289  1.00 68.82  ? 566 GLY A C   1 
ATOM 4235 O O   . GLY A 1 566 ? 39.063  -0.370  53.421  1.00 75.52  ? 566 GLY A O   1 
ATOM 4236 N N   . GLY A 1 567 ? 37.825  -0.190  55.288  1.00 62.56  ? 567 GLY A N   1 
ATOM 4237 C CA  . GLY A 1 567 ? 37.625  -1.609  55.451  1.00 62.18  ? 567 GLY A CA  1 
ATOM 4238 C C   . GLY A 1 567 ? 36.413  -2.112  54.697  1.00 62.32  ? 567 GLY A C   1 
ATOM 4239 O O   . GLY A 1 567 ? 35.912  -1.471  53.766  1.00 63.23  ? 567 GLY A O   1 
ATOM 4240 N N   . ASP A 1 568 ? 35.930  -3.276  55.112  1.00 62.16  ? 568 ASP A N   1 
ATOM 4241 C CA  . ASP A 1 568 ? 34.875  -3.984  54.405  1.00 62.07  ? 568 ASP A CA  1 
ATOM 4242 C C   . ASP A 1 568 ? 33.510  -3.660  54.997  1.00 65.85  ? 568 ASP A C   1 
ATOM 4243 O O   . ASP A 1 568 ? 33.405  -3.222  56.145  1.00 72.62  ? 568 ASP A O   1 
ATOM 4244 C CB  . ASP A 1 568 ? 35.113  -5.496  54.443  1.00 63.96  ? 568 ASP A CB  1 
ATOM 4245 C CG  . ASP A 1 568 ? 35.136  -6.048  55.854  1.00 72.75  ? 568 ASP A CG  1 
ATOM 4246 O OD1 . ASP A 1 568 ? 35.322  -5.260  56.803  1.00 78.64  ? 568 ASP A OD1 1 
ATOM 4247 O OD2 . ASP A 1 568 ? 34.975  -7.274  56.014  1.00 73.51  ? 568 ASP A OD2 1 
ATOM 4248 N N   . PHE A 1 569 ? 32.473  -3.864  54.191  1.00 50.37  ? 569 PHE A N   1 
ATOM 4249 C CA  . PHE A 1 569 ? 31.088  -3.791  54.631  1.00 52.10  ? 569 PHE A CA  1 
ATOM 4250 C C   . PHE A 1 569 ? 30.271  -4.799  53.841  1.00 52.27  ? 569 PHE A C   1 
ATOM 4251 O O   . PHE A 1 569 ? 30.440  -4.932  52.627  1.00 61.75  ? 569 PHE A O   1 
ATOM 4252 C CB  . PHE A 1 569 ? 30.502  -2.388  54.449  1.00 50.95  ? 569 PHE A CB  1 
ATOM 4253 C CG  . PHE A 1 569 ? 29.054  -2.291  54.828  1.00 49.97  ? 569 PHE A CG  1 
ATOM 4254 C CD1 . PHE A 1 569 ? 28.670  -2.291  56.157  1.00 51.54  ? 569 PHE A CD1 1 
ATOM 4255 C CD2 . PHE A 1 569 ? 28.075  -2.212  53.854  1.00 50.76  ? 569 PHE A CD2 1 
ATOM 4256 C CE1 . PHE A 1 569 ? 27.338  -2.208  56.505  1.00 51.83  ? 569 PHE A CE1 1 
ATOM 4257 C CE2 . PHE A 1 569 ? 26.743  -2.128  54.199  1.00 52.29  ? 569 PHE A CE2 1 
ATOM 4258 C CZ  . PHE A 1 569 ? 26.374  -2.126  55.527  1.00 51.11  ? 569 PHE A CZ  1 
ATOM 4259 N N   . TYR A 1 570 ? 29.386  -5.506  54.533  1.00 52.82  ? 570 TYR A N   1 
ATOM 4260 C CA  . TYR A 1 570 ? 28.541  -6.527  53.921  1.00 52.35  ? 570 TYR A CA  1 
ATOM 4261 C C   . TYR A 1 570 ? 27.093  -6.064  54.022  1.00 51.65  ? 570 TYR A C   1 
ATOM 4262 O O   . TYR A 1 570 ? 26.512  -6.044  55.109  1.00 61.68  ? 570 TYR A O   1 
ATOM 4263 C CB  . TYR A 1 570 ? 28.754  -7.878  54.593  1.00 50.94  ? 570 TYR A CB  1 
ATOM 4264 C CG  . TYR A 1 570 ? 30.158  -8.397  54.429  1.00 51.21  ? 570 TYR A CG  1 
ATOM 4265 C CD1 . TYR A 1 570 ? 30.578  -8.950  53.228  1.00 53.91  ? 570 TYR A CD1 1 
ATOM 4266 C CD2 . TYR A 1 570 ? 31.073  -8.317  55.467  1.00 52.53  ? 570 TYR A CD2 1 
ATOM 4267 C CE1 . TYR A 1 570 ? 31.864  -9.418  53.071  1.00 58.55  ? 570 TYR A CE1 1 
ATOM 4268 C CE2 . TYR A 1 570 ? 32.360  -8.781  55.321  1.00 59.71  ? 570 TYR A CE2 1 
ATOM 4269 C CZ  . TYR A 1 570 ? 32.752  -9.331  54.121  1.00 63.36  ? 570 TYR A CZ  1 
ATOM 4270 O OH  . TYR A 1 570 ? 34.037  -9.797  53.971  1.00 67.70  ? 570 TYR A OH  1 
ATOM 4271 N N   . LEU A 1 571 ? 26.518  -5.696  52.883  1.00 47.23  ? 571 LEU A N   1 
ATOM 4272 C CA  . LEU A 1 571 ? 25.146  -5.199  52.820  1.00 43.77  ? 571 LEU A CA  1 
ATOM 4273 C C   . LEU A 1 571 ? 24.221  -6.390  52.605  1.00 51.85  ? 571 LEU A C   1 
ATOM 4274 O O   . LEU A 1 571 ? 23.757  -6.640  51.490  1.00 63.91  ? 571 LEU A O   1 
ATOM 4275 C CB  . LEU A 1 571 ? 25.020  -4.166  51.707  1.00 54.07  ? 571 LEU A CB  1 
ATOM 4276 C CG  . LEU A 1 571 ? 23.721  -3.383  51.529  1.00 58.63  ? 571 LEU A CG  1 
ATOM 4277 C CD1 . LEU A 1 571 ? 23.441  -2.570  52.756  1.00 51.00  ? 571 LEU A CD1 1 
ATOM 4278 C CD2 . LEU A 1 571 ? 23.852  -2.465  50.336  1.00 55.48  ? 571 LEU A CD2 1 
ATOM 4279 N N   . ASN A 1 572 ? 23.955  -7.136  53.678  1.00 43.65  ? 572 ASN A N   1 
ATOM 4280 C CA  . ASN A 1 572 ? 23.185  -8.371  53.586  1.00 43.70  ? 572 ASN A CA  1 
ATOM 4281 C C   . ASN A 1 572 ? 21.731  -8.134  53.205  1.00 46.98  ? 572 ASN A C   1 
ATOM 4282 O O   . ASN A 1 572 ? 21.176  -8.888  52.399  1.00 60.06  ? 572 ASN A O   1 
ATOM 4283 C CB  . ASN A 1 572 ? 23.255  -9.137  54.909  1.00 38.07  ? 572 ASN A CB  1 
ATOM 4284 C CG  . ASN A 1 572 ? 24.630  -9.703  55.178  1.00 54.28  ? 572 ASN A CG  1 
ATOM 4285 O OD1 . ASN A 1 572 ? 25.171  -10.457 54.374  1.00 62.82  ? 572 ASN A OD1 1 
ATOM 4286 N ND2 . ASN A 1 572 ? 25.209  -9.336  56.312  1.00 61.21  ? 572 ASN A ND2 1 
ATOM 4287 N N   . SER A 1 573 ? 21.095  -7.110  53.767  1.00 39.78  ? 573 SER A N   1 
ATOM 4288 C CA  . SER A 1 573 ? 19.727  -6.785  53.394  1.00 41.74  ? 573 SER A CA  1 
ATOM 4289 C C   . SER A 1 573 ? 19.454  -5.324  53.705  1.00 46.01  ? 573 SER A C   1 
ATOM 4290 O O   . SER A 1 573 ? 20.051  -4.755  54.621  1.00 55.39  ? 573 SER A O   1 
ATOM 4291 C CB  . SER A 1 573 ? 18.710  -7.671  54.121  1.00 44.19  ? 573 SER A CB  1 
ATOM 4292 O OG  . SER A 1 573 ? 18.485  -7.215  55.442  1.00 54.21  ? 573 SER A OG  1 
ATOM 4293 N N   . LEU A 1 574 ? 18.551  -4.732  52.935  1.00 45.61  ? 574 LEU A N   1 
ATOM 4294 C CA  . LEU A 1 574 ? 18.093  -3.365  53.140  1.00 40.52  ? 574 LEU A CA  1 
ATOM 4295 C C   . LEU A 1 574 ? 16.583  -3.388  53.318  1.00 37.96  ? 574 LEU A C   1 
ATOM 4296 O O   . LEU A 1 574 ? 15.869  -3.984  52.505  1.00 42.92  ? 574 LEU A O   1 
ATOM 4297 C CB  . LEU A 1 574 ? 18.483  -2.476  51.962  1.00 50.07  ? 574 LEU A CB  1 
ATOM 4298 C CG  . LEU A 1 574 ? 17.880  -1.073  51.964  1.00 41.33  ? 574 LEU A CG  1 
ATOM 4299 C CD1 . LEU A 1 574 ? 18.497  -0.225  53.058  1.00 43.55  ? 574 LEU A CD1 1 
ATOM 4300 C CD2 . LEU A 1 574 ? 18.061  -0.425  50.610  1.00 50.11  ? 574 LEU A CD2 1 
ATOM 4301 N N   . THR A 1 575 ? 16.101  -2.746  54.374  1.00 41.15  ? 575 THR A N   1 
ATOM 4302 C CA  . THR A 1 575 ? 14.673  -2.647  54.637  1.00 39.50  ? 575 THR A CA  1 
ATOM 4303 C C   . THR A 1 575 ? 14.235  -1.198  54.482  1.00 42.30  ? 575 THR A C   1 
ATOM 4304 O O   . THR A 1 575 ? 14.758  -0.310  55.162  1.00 50.11  ? 575 THR A O   1 
ATOM 4305 C CB  . THR A 1 575 ? 14.327  -3.157  56.035  1.00 51.22  ? 575 THR A CB  1 
ATOM 4306 O OG1 . THR A 1 575 ? 14.793  -4.503  56.186  1.00 63.28  ? 575 THR A OG1 1 
ATOM 4307 C CG2 . THR A 1 575 ? 12.823  -3.114  56.256  1.00 42.54  ? 575 THR A CG2 1 
ATOM 4308 N N   . VAL A 1 576 ? 13.282  -0.965  53.586  1.00 40.54  ? 576 VAL A N   1 
ATOM 4309 C CA  . VAL A 1 576 ? 12.648  0.337   53.428  1.00 48.33  ? 576 VAL A CA  1 
ATOM 4310 C C   . VAL A 1 576 ? 11.191  0.178   53.827  1.00 49.11  ? 576 VAL A C   1 
ATOM 4311 O O   . VAL A 1 576 ? 10.411  -0.466  53.117  1.00 46.73  ? 576 VAL A O   1 
ATOM 4312 C CB  . VAL A 1 576 ? 12.775  0.867   51.993  1.00 47.83  ? 576 VAL A CB  1 
ATOM 4313 C CG1 . VAL A 1 576 ? 12.197  2.268   51.902  1.00 42.76  ? 576 VAL A CG1 1 
ATOM 4314 C CG2 . VAL A 1 576 ? 14.225  0.848   51.549  1.00 49.16  ? 576 VAL A CG2 1 
ATOM 4315 N N   . GLN A 1 577 ? 10.825  0.762   54.961  1.00 51.00  ? 577 GLN A N   1 
ATOM 4316 C CA  . GLN A 1 577 ? 9.475   0.621   55.488  1.00 45.17  ? 577 GLN A CA  1 
ATOM 4317 C C   . GLN A 1 577 ? 8.768   1.965   55.465  1.00 48.16  ? 577 GLN A C   1 
ATOM 4318 O O   . GLN A 1 577 ? 9.070   2.829   56.302  1.00 51.73  ? 577 GLN A O   1 
ATOM 4319 C CB  . GLN A 1 577 ? 9.507   0.064   56.909  1.00 44.83  ? 577 GLN A CB  1 
ATOM 4320 C CG  . GLN A 1 577 ? 8.134   -0.250  57.457  1.00 43.51  ? 577 GLN A CG  1 
ATOM 4321 C CD  . GLN A 1 577 ? 8.192   -1.022  58.750  1.00 50.91  ? 577 GLN A CD  1 
ATOM 4322 O OE1 . GLN A 1 577 ? 9.170   -0.940  59.492  1.00 60.13  ? 577 GLN A OE1 1 
ATOM 4323 N NE2 . GLN A 1 577 ? 7.147   -1.788  59.025  1.00 51.07  ? 577 GLN A NE2 1 
ATOM 4324 N N   . PRO A 1 578 ? 7.841   2.194   54.535  1.00 49.70  ? 578 PRO A N   1 
ATOM 4325 C CA  . PRO A 1 578 ? 7.056   3.436   54.567  1.00 46.02  ? 578 PRO A CA  1 
ATOM 4326 C C   . PRO A 1 578 ? 6.307   3.565   55.884  1.00 41.39  ? 578 PRO A C   1 
ATOM 4327 O O   . PRO A 1 578 ? 5.717   2.602   56.378  1.00 55.61  ? 578 PRO A O   1 
ATOM 4328 C CB  . PRO A 1 578 ? 6.094   3.296   53.381  1.00 40.50  ? 578 PRO A CB  1 
ATOM 4329 C CG  . PRO A 1 578 ? 6.467   2.068   52.662  1.00 42.78  ? 578 PRO A CG  1 
ATOM 4330 C CD  . PRO A 1 578 ? 7.557   1.351   53.366  1.00 45.64  ? 578 PRO A CD  1 
ATOM 4331 N N   . VAL A 1 579 ? 6.338   4.765   56.450  1.00 34.69  ? 579 VAL A N   1 
ATOM 4332 C CA  . VAL A 1 579 ? 5.733   5.033   57.752  1.00 43.88  ? 579 VAL A CA  1 
ATOM 4333 C C   . VAL A 1 579 ? 4.959   6.341   57.671  1.00 41.84  ? 579 VAL A C   1 
ATOM 4334 O O   . VAL A 1 579 ? 5.192   7.140   56.754  1.00 46.29  ? 579 VAL A O   1 
ATOM 4335 C CB  . VAL A 1 579 ? 6.792   5.109   58.861  1.00 45.46  ? 579 VAL A CB  1 
ATOM 4336 C CG1 . VAL A 1 579 ? 7.515   3.782   59.019  1.00 39.90  ? 579 VAL A CG1 1 
ATOM 4337 C CG2 . VAL A 1 579 ? 7.762   6.235   58.567  1.00 37.47  ? 579 VAL A CG2 1 
ATOM 4338 N N   . PRO A 1 580 ? 4.028   6.594   58.584  1.00 44.86  ? 580 PRO A N   1 
ATOM 4339 C CA  . PRO A 1 580 ? 3.490   7.948   58.724  1.00 42.36  ? 580 PRO A CA  1 
ATOM 4340 C C   . PRO A 1 580 ? 4.601   8.935   59.040  1.00 43.80  ? 580 PRO A C   1 
ATOM 4341 O O   . PRO A 1 580 ? 5.535   8.647   59.790  1.00 54.63  ? 580 PRO A O   1 
ATOM 4342 C CB  . PRO A 1 580 ? 2.502   7.833   59.889  1.00 38.65  ? 580 PRO A CB  1 
ATOM 4343 C CG  . PRO A 1 580 ? 2.212   6.390   60.029  1.00 39.92  ? 580 PRO A CG  1 
ATOM 4344 C CD  . PRO A 1 580 ? 3.319   5.608   59.415  1.00 30.42  ? 580 PRO A CD  1 
ATOM 4345 N N   . VAL A 1 581 ? 4.489   10.122  58.442  1.00 41.26  ? 581 VAL A N   1 
ATOM 4346 C CA  . VAL A 1 581 ? 5.542   11.122  58.580  1.00 41.17  ? 581 VAL A CA  1 
ATOM 4347 C C   . VAL A 1 581 ? 5.706   11.596  60.020  1.00 49.80  ? 581 VAL A C   1 
ATOM 4348 O O   . VAL A 1 581 ? 6.817   11.969  60.417  1.00 54.51  ? 581 VAL A O   1 
ATOM 4349 C CB  . VAL A 1 581 ? 5.279   12.305  57.631  1.00 44.92  ? 581 VAL A CB  1 
ATOM 4350 C CG1 . VAL A 1 581 ? 4.107   13.146  58.113  1.00 50.06  ? 581 VAL A CG1 1 
ATOM 4351 C CG2 . VAL A 1 581 ? 6.529   13.154  57.480  1.00 47.16  ? 581 VAL A CG2 1 
ATOM 4352 N N   . GLY A 1 582 ? 4.643   11.577  60.818  1.00 47.84  ? 582 GLY A N   1 
ATOM 4353 C CA  . GLY A 1 582 ? 4.749   11.935  62.218  1.00 42.09  ? 582 GLY A CA  1 
ATOM 4354 C C   . GLY A 1 582 ? 5.379   10.829  63.035  1.00 50.52  ? 582 GLY A C   1 
ATOM 4355 O O   . GLY A 1 582 ? 5.892   11.066  64.133  1.00 58.06  ? 582 GLY A O   1 
ATOM 4356 N N   . MET A 1 583 ? 5.343   9.611   62.504  1.00 48.51  ? 583 MET A N   1 
ATOM 4357 C CA  . MET A 1 583 ? 5.976   8.462   63.132  1.00 45.19  ? 583 MET A CA  1 
ATOM 4358 C C   . MET A 1 583 ? 7.395   8.231   62.636  1.00 46.01  ? 583 MET A C   1 
ATOM 4359 O O   . MET A 1 583 ? 8.065   7.315   63.121  1.00 49.59  ? 583 MET A O   1 
ATOM 4360 C CB  . MET A 1 583 ? 5.140   7.204   62.888  1.00 45.26  ? 583 MET A CB  1 
ATOM 4361 C CG  . MET A 1 583 ? 3.720   7.314   63.392  1.00 44.91  ? 583 MET A CG  1 
ATOM 4362 S SD  . MET A 1 583 ? 3.528   6.692   65.066  1.00 63.07  ? 583 MET A SD  1 
ATOM 4363 C CE  . MET A 1 583 ? 1.747   6.652   65.171  1.00 56.09  ? 583 MET A CE  1 
ATOM 4364 N N   . SER A 1 584 ? 7.862   9.032   61.684  1.00 41.47  ? 584 SER A N   1 
ATOM 4365 C CA  . SER A 1 584 ? 9.209   8.882   61.161  1.00 42.22  ? 584 SER A CA  1 
ATOM 4366 C C   . SER A 1 584 ? 10.229  9.367   62.181  1.00 46.62  ? 584 SER A C   1 
ATOM 4367 O O   . SER A 1 584 ? 10.088  10.446  62.761  1.00 52.83  ? 584 SER A O   1 
ATOM 4368 C CB  . SER A 1 584 ? 9.362   9.657   59.854  1.00 42.48  ? 584 SER A CB  1 
ATOM 4369 O OG  . SER A 1 584 ? 8.838   10.967  59.976  1.00 55.16  ? 584 SER A OG  1 
ATOM 4370 N N   . VAL A 1 585 ? 11.262  8.559   62.395  1.00 49.93  ? 585 VAL A N   1 
ATOM 4371 C CA  . VAL A 1 585 ? 12.326  8.869   63.339  1.00 41.87  ? 585 VAL A CA  1 
ATOM 4372 C C   . VAL A 1 585 ? 13.560  9.280   62.555  1.00 39.24  ? 585 VAL A C   1 
ATOM 4373 O O   . VAL A 1 585 ? 14.063  8.513   61.725  1.00 59.03  ? 585 VAL A O   1 
ATOM 4374 C CB  . VAL A 1 585 ? 12.628  7.668   64.252  1.00 42.87  ? 585 VAL A CB  1 
ATOM 4375 C CG1 . VAL A 1 585 ? 13.832  7.957   65.127  1.00 37.74  ? 585 VAL A CG1 1 
ATOM 4376 C CG2 . VAL A 1 585 ? 11.415  7.333   65.102  1.00 41.45  ? 585 VAL A CG2 1 
ATOM 4377 N N   . GLN A 1 586 ? 14.046  10.493  62.806  1.00 46.47  ? 586 GLN A N   1 
ATOM 4378 C CA  . GLN A 1 586 ? 15.266  10.949  62.151  1.00 50.28  ? 586 GLN A CA  1 
ATOM 4379 C C   . GLN A 1 586 ? 16.493  10.282  62.757  1.00 52.90  ? 586 GLN A C   1 
ATOM 4380 O O   . GLN A 1 586 ? 17.245  9.593   62.059  1.00 58.29  ? 586 GLN A O   1 
ATOM 4381 C CB  . GLN A 1 586 ? 15.374  12.470  62.250  1.00 43.74  ? 586 GLN A CB  1 
ATOM 4382 C CG  . GLN A 1 586 ? 16.650  13.036  61.671  1.00 51.97  ? 586 GLN A CG  1 
ATOM 4383 C CD  . GLN A 1 586 ? 16.697  14.543  61.748  1.00 53.86  ? 586 GLN A CD  1 
ATOM 4384 O OE1 . GLN A 1 586 ? 15.693  15.192  62.029  1.00 62.51  ? 586 GLN A OE1 1 
ATOM 4385 N NE2 . GLN A 1 586 ? 17.872  15.108  61.517  1.00 57.52  ? 586 GLN A NE2 1 
ATOM 4386 N N   . ALA A 1 587 ? 16.707  10.475  64.052  1.00 58.99  ? 587 ALA A N   1 
ATOM 4387 C CA  . ALA A 1 587 ? 17.771  9.812   64.785  1.00 51.71  ? 587 ALA A CA  1 
ATOM 4388 C C   . ALA A 1 587 ? 17.201  9.247   66.075  1.00 52.42  ? 587 ALA A C   1 
ATOM 4389 O O   . ALA A 1 587 ? 16.426  9.909   66.773  1.00 64.97  ? 587 ALA A O   1 
ATOM 4390 C CB  . ALA A 1 587 ? 18.930  10.767  65.094  1.00 53.71  ? 587 ALA A CB  1 
ATOM 4391 N N   . ARG A 1 588 ? 17.580  8.012   66.382  1.00 58.33  ? 588 ARG A N   1 
ATOM 4392 C CA  . ARG A 1 588 ? 17.087  7.358   67.584  1.00 60.19  ? 588 ARG A CA  1 
ATOM 4393 C C   . ARG A 1 588 ? 17.650  8.037   68.824  1.00 65.04  ? 588 ARG A C   1 
ATOM 4394 O O   . ARG A 1 588 ? 18.822  8.423   68.852  1.00 73.15  ? 588 ARG A O   1 
ATOM 4395 C CB  . ARG A 1 588 ? 17.464  5.881   67.575  1.00 56.75  ? 588 ARG A CB  1 
ATOM 4396 C CG  . ARG A 1 588 ? 16.507  5.019   66.790  1.00 66.28  ? 588 ARG A CG  1 
ATOM 4397 C CD  . ARG A 1 588 ? 16.581  3.579   67.233  1.00 65.49  ? 588 ARG A CD  1 
ATOM 4398 N NE  . ARG A 1 588 ? 17.934  3.176   67.594  1.00 65.21  ? 588 ARG A NE  1 
ATOM 4399 C CZ  . ARG A 1 588 ? 18.251  2.542   68.715  1.00 66.72  ? 588 ARG A CZ  1 
ATOM 4400 N NH1 . ARG A 1 588 ? 17.337  2.242   69.622  1.00 62.80  ? 588 ARG A NH1 1 
ATOM 4401 N NH2 . ARG A 1 588 ? 19.517  2.201   68.930  1.00 64.92  ? 588 ARG A NH2 1 
ATOM 4402 N N   . ASN A 1 589 ? 16.802  8.199   69.841  1.00 60.52  ? 589 ASN A N   1 
ATOM 4403 C CA  . ASN A 1 589 ? 17.214  8.731   71.142  1.00 50.65  ? 589 ASN A CA  1 
ATOM 4404 C C   . ASN A 1 589 ? 17.965  10.049  70.991  1.00 56.05  ? 589 ASN A C   1 
ATOM 4405 O O   . ASN A 1 589 ? 18.952  10.310  71.682  1.00 68.96  ? 589 ASN A O   1 
ATOM 4406 C CB  . ASN A 1 589 ? 18.051  7.707   71.909  1.00 47.32  ? 589 ASN A CB  1 
ATOM 4407 C CG  . ASN A 1 589 ? 17.235  6.519   72.362  1.00 55.80  ? 589 ASN A CG  1 
ATOM 4408 O OD1 . ASN A 1 589 ? 16.075  6.658   72.744  1.00 60.43  ? 589 ASN A OD1 1 
ATOM 4409 N ND2 . ASN A 1 589 ? 17.834  5.337   72.312  1.00 68.30  ? 589 ASN A ND2 1 
ATOM 4410 N N   . TRP A 1 590 ? 17.495  10.883  70.074  1.00 60.78  ? 590 TRP A N   1 
ATOM 4411 C CA  . TRP A 1 590 ? 18.105  12.164  69.765  1.00 51.62  ? 590 TRP A CA  1 
ATOM 4412 C C   . TRP A 1 590 ? 17.476  13.247  70.635  1.00 59.86  ? 590 TRP A C   1 
ATOM 4413 O O   . TRP A 1 590 ? 16.758  12.966  71.598  1.00 62.75  ? 590 TRP A O   1 
ATOM 4414 C CB  . TRP A 1 590 ? 17.940  12.487  68.274  1.00 57.26  ? 590 TRP A CB  1 
ATOM 4415 C CG  . TRP A 1 590 ? 18.886  13.521  67.763  1.00 58.65  ? 590 TRP A CG  1 
ATOM 4416 C CD1 . TRP A 1 590 ? 20.182  13.701  68.136  1.00 57.86  ? 590 TRP A CD1 1 
ATOM 4417 C CD2 . TRP A 1 590 ? 18.603  14.533  66.793  1.00 61.73  ? 590 TRP A CD2 1 
ATOM 4418 N NE1 . TRP A 1 590 ? 20.731  14.758  67.453  1.00 60.42  ? 590 TRP A NE1 1 
ATOM 4419 C CE2 . TRP A 1 590 ? 19.779  15.287  66.622  1.00 62.02  ? 590 TRP A CE2 1 
ATOM 4420 C CE3 . TRP A 1 590 ? 17.470  14.874  66.049  1.00 57.41  ? 590 TRP A CE3 1 
ATOM 4421 C CZ2 . TRP A 1 590 ? 19.855  16.359  65.740  1.00 60.37  ? 590 TRP A CZ2 1 
ATOM 4422 C CZ3 . TRP A 1 590 ? 17.548  15.938  65.174  1.00 64.94  ? 590 TRP A CZ3 1 
ATOM 4423 C CH2 . TRP A 1 590 ? 18.732  16.668  65.026  1.00 62.53  ? 590 TRP A CH2 1 
ATOM 4424 N N   . ALA A 1 591 ? 17.763  14.494  70.293  1.00 58.58  ? 591 ALA A N   1 
ATOM 4425 C CA  . ALA A 1 591 ? 17.259  15.654  71.025  1.00 60.42  ? 591 ALA A CA  1 
ATOM 4426 C C   . ALA A 1 591 ? 15.768  15.891  70.832  1.00 59.62  ? 591 ALA A C   1 
ATOM 4427 O O   . ALA A 1 591 ? 15.282  16.927  71.300  1.00 65.27  ? 591 ALA A O   1 
ATOM 4428 C CB  . ALA A 1 591 ? 18.039  16.901  70.610  1.00 60.16  ? 591 ALA A CB  1 
ATOM 4429 N N   . ARG A 1 592 ? 15.023  15.008  70.183  1.00 62.48  ? 592 ARG A N   1 
ATOM 4430 C CA  . ARG A 1 592 ? 13.606  15.205  69.914  1.00 60.30  ? 592 ARG A CA  1 
ATOM 4431 C C   . ARG A 1 592 ? 12.793  14.067  70.521  1.00 63.72  ? 592 ARG A C   1 
ATOM 4432 O O   . ARG A 1 592 ? 13.324  13.022  70.903  1.00 64.74  ? 592 ARG A O   1 
ATOM 4433 C CB  . ARG A 1 592 ? 13.346  15.300  68.409  1.00 60.77  ? 592 ARG A CB  1 
ATOM 4434 C CG  . ARG A 1 592 ? 13.100  16.705  67.902  1.00 65.64  ? 592 ARG A CG  1 
ATOM 4435 C CD  . ARG A 1 592 ? 13.970  17.001  66.697  1.00 69.11  ? 592 ARG A CD  1 
ATOM 4436 N NE  . ARG A 1 592 ? 13.496  16.291  65.515  1.00 71.09  ? 592 ARG A NE  1 
ATOM 4437 C CZ  . ARG A 1 592 ? 13.939  16.504  64.284  1.00 68.50  ? 592 ARG A CZ  1 
ATOM 4438 N NH1 . ARG A 1 592 ? 14.859  17.419  64.030  1.00 64.89  ? 592 ARG A NH1 1 
ATOM 4439 N NH2 . ARG A 1 592 ? 13.441  15.786  63.283  1.00 69.47  ? 592 ARG A NH2 1 
ATOM 4440 N N   . PHE A 1 593 ? 11.483  14.284  70.604  1.00 57.45  ? 593 PHE A N   1 
ATOM 4441 C CA  . PHE A 1 593 ? 10.543  13.249  71.012  1.00 52.15  ? 593 PHE A CA  1 
ATOM 4442 C C   . PHE A 1 593 ? 10.152  12.431  69.789  1.00 53.91  ? 593 PHE A C   1 
ATOM 4443 O O   . PHE A 1 593 ? 9.508   12.949  68.871  1.00 62.31  ? 593 PHE A O   1 
ATOM 4444 C CB  . PHE A 1 593 ? 9.307   13.861  71.668  1.00 48.37  ? 593 PHE A CB  1 
ATOM 4445 C CG  . PHE A 1 593 ? 9.318   13.790  73.164  1.00 50.48  ? 593 PHE A CG  1 
ATOM 4446 C CD1 . PHE A 1 593 ? 8.944   12.629  73.816  1.00 52.47  ? 593 PHE A CD1 1 
ATOM 4447 C CD2 . PHE A 1 593 ? 9.706   14.880  73.920  1.00 55.48  ? 593 PHE A CD2 1 
ATOM 4448 C CE1 . PHE A 1 593 ? 8.955   12.556  75.192  1.00 49.38  ? 593 PHE A CE1 1 
ATOM 4449 C CE2 . PHE A 1 593 ? 9.721   14.813  75.298  1.00 54.77  ? 593 PHE A CE2 1 
ATOM 4450 C CZ  . PHE A 1 593 ? 9.346   13.649  75.934  1.00 51.55  ? 593 PHE A CZ  1 
ATOM 4451 N N   . ASP A 1 594 ? 10.542  11.162  69.777  1.00 57.72  ? 594 ASP A N   1 
ATOM 4452 C CA  . ASP A 1 594 ? 10.232  10.266  68.673  1.00 53.34  ? 594 ASP A CA  1 
ATOM 4453 C C   . ASP A 1 594 ? 8.872   9.629   68.918  1.00 46.69  ? 594 ASP A C   1 
ATOM 4454 O O   . ASP A 1 594 ? 8.689   8.906   69.902  1.00 56.12  ? 594 ASP A O   1 
ATOM 4455 C CB  . ASP A 1 594 ? 11.311  9.196   68.528  1.00 53.64  ? 594 ASP A CB  1 
ATOM 4456 C CG  . ASP A 1 594 ? 12.589  9.738   67.927  1.00 69.86  ? 594 ASP A CG  1 
ATOM 4457 O OD1 . ASP A 1 594 ? 12.517  10.711  67.149  1.00 70.47  ? 594 ASP A OD1 1 
ATOM 4458 O OD2 . ASP A 1 594 ? 13.669  9.192   68.237  1.00 74.03  ? 594 ASP A OD2 1 
ATOM 4459 N N   . LYS A 1 595 ? 7.921   9.898   68.029  1.00 45.12  ? 595 LYS A N   1 
ATOM 4460 C CA  . LYS A 1 595 ? 6.593   9.317   68.154  1.00 38.45  ? 595 LYS A CA  1 
ATOM 4461 C C   . LYS A 1 595 ? 6.610   7.896   67.608  1.00 49.54  ? 595 LYS A C   1 
ATOM 4462 O O   . LYS A 1 595 ? 6.909   7.677   66.430  1.00 58.37  ? 595 LYS A O   1 
ATOM 4463 C CB  . LYS A 1 595 ? 5.555   10.156  67.416  1.00 42.34  ? 595 LYS A CB  1 
ATOM 4464 C CG  . LYS A 1 595 ? 4.142   9.621   67.567  1.00 37.44  ? 595 LYS A CG  1 
ATOM 4465 C CD  . LYS A 1 595 ? 3.134   10.469  66.820  1.00 50.02  ? 595 LYS A CD  1 
ATOM 4466 C CE  . LYS A 1 595 ? 1.724   9.951   67.033  1.00 44.57  ? 595 LYS A CE  1 
ATOM 4467 N NZ  . LYS A 1 595 ? 0.695   10.944  66.626  1.00 48.52  ? 595 LYS A NZ  1 
ATOM 4468 N N   . GLY A 1 596 ? 6.292   6.937   68.466  1.00 47.06  ? 596 GLY A N   1 
ATOM 4469 C CA  . GLY A 1 596 ? 6.165   5.559   68.050  1.00 31.67  ? 596 GLY A CA  1 
ATOM 4470 C C   . GLY A 1 596 ? 4.944   4.932   68.680  1.00 40.59  ? 596 GLY A C   1 
ATOM 4471 O O   . GLY A 1 596 ? 4.148   5.623   69.319  1.00 61.19  ? 596 GLY A O   1 
ATOM 4472 N N   . HIS A 1 597 ? 4.779   3.633   68.504  1.00 46.96  ? 597 HIS A N   1 
ATOM 4473 C CA  . HIS A 1 597 ? 3.673   2.904   69.098  1.00 40.92  ? 597 HIS A CA  1 
ATOM 4474 C C   . HIS A 1 597 ? 4.216   1.988   70.188  1.00 43.98  ? 597 HIS A C   1 
ATOM 4475 O O   . HIS A 1 597 ? 5.419   1.942   70.450  1.00 50.19  ? 597 HIS A O   1 
ATOM 4476 C CB  . HIS A 1 597 ? 2.909   2.115   68.032  1.00 37.84  ? 597 HIS A CB  1 
ATOM 4477 C CG  . HIS A 1 597 ? 3.609   0.874   67.584  1.00 43.89  ? 597 HIS A CG  1 
ATOM 4478 N ND1 . HIS A 1 597 ? 3.214   -0.385  67.979  1.00 62.00  ? 597 HIS A ND1 1 
ATOM 4479 C CD2 . HIS A 1 597 ? 4.696   0.698   66.799  1.00 41.61  ? 597 HIS A CD2 1 
ATOM 4480 C CE1 . HIS A 1 597 ? 4.015   -1.284  67.441  1.00 50.63  ? 597 HIS A CE1 1 
ATOM 4481 N NE2 . HIS A 1 597 ? 4.924   -0.653  66.720  1.00 44.09  ? 597 HIS A NE2 1 
ATOM 4482 N N   . ARG A 1 598 ? 3.315   1.258   70.830  1.00 45.07  ? 598 ARG A N   1 
ATOM 4483 C CA  . ARG A 1 598 ? 3.675   0.341   71.905  1.00 41.00  ? 598 ARG A CA  1 
ATOM 4484 C C   . ARG A 1 598 ? 3.685   -1.073  71.337  1.00 42.34  ? 598 ARG A C   1 
ATOM 4485 O O   . ARG A 1 598 ? 2.644   -1.729  71.255  1.00 58.93  ? 598 ARG A O   1 
ATOM 4486 C CB  . ARG A 1 598 ? 2.707   0.473   73.074  1.00 44.62  ? 598 ARG A CB  1 
ATOM 4487 C CG  . ARG A 1 598 ? 3.039   -0.424  74.244  1.00 47.26  ? 598 ARG A CG  1 
ATOM 4488 C CD  . ARG A 1 598 ? 4.308   0.024   74.947  1.00 50.89  ? 598 ARG A CD  1 
ATOM 4489 N NE  . ARG A 1 598 ? 4.087   1.190   75.793  1.00 50.73  ? 598 ARG A NE  1 
ATOM 4490 C CZ  . ARG A 1 598 ? 4.978   2.151   75.991  1.00 52.02  ? 598 ARG A CZ  1 
ATOM 4491 N NH1 . ARG A 1 598 ? 6.169   2.118   75.418  1.00 46.35  ? 598 ARG A NH1 1 
ATOM 4492 N NH2 . ARG A 1 598 ? 4.667   3.170   76.787  1.00 53.28  ? 598 ARG A NH2 1 
ATOM 4493 N N   . ALA A 1 599 ? 4.864   -1.541  70.936  1.00 44.55  ? 599 ALA A N   1 
ATOM 4494 C CA  . ALA A 1 599 ? 5.015   -2.904  70.447  1.00 40.90  ? 599 ALA A CA  1 
ATOM 4495 C C   . ALA A 1 599 ? 4.965   -3.865  71.626  1.00 48.83  ? 599 ALA A C   1 
ATOM 4496 O O   . ALA A 1 599 ? 5.694   -3.687  72.609  1.00 63.39  ? 599 ALA A O   1 
ATOM 4497 C CB  . ALA A 1 599 ? 6.325   -3.059  69.679  1.00 44.34  ? 599 ALA A CB  1 
ATOM 4498 N N   . VAL A 1 600 ? 4.111   -4.877  71.533  1.00 44.23  ? 600 VAL A N   1 
ATOM 4499 C CA  . VAL A 1 600 ? 3.895   -5.831  72.613  1.00 40.95  ? 600 VAL A CA  1 
ATOM 4500 C C   . VAL A 1 600 ? 4.230   -7.225  72.105  1.00 47.59  ? 600 VAL A C   1 
ATOM 4501 O O   . VAL A 1 600 ? 3.704   -7.663  71.075  1.00 61.16  ? 600 VAL A O   1 
ATOM 4502 C CB  . VAL A 1 600 ? 2.451   -5.769  73.137  1.00 34.07  ? 600 VAL A CB  1 
ATOM 4503 C CG1 . VAL A 1 600 ? 2.310   -6.607  74.393  1.00 42.20  ? 600 VAL A CG1 1 
ATOM 4504 C CG2 . VAL A 1 600 ? 2.044   -4.331  73.399  1.00 37.72  ? 600 VAL A CG2 1 
ATOM 4505 N N   . TYR A 1 601 ? 5.105   -7.918  72.828  1.00 51.02  ? 601 TYR A N   1 
ATOM 4506 C CA  . TYR A 1 601 ? 5.477   -9.294  72.521  1.00 49.14  ? 601 TYR A CA  1 
ATOM 4507 C C   . TYR A 1 601 ? 4.649   -10.209 73.413  1.00 49.46  ? 601 TYR A C   1 
ATOM 4508 O O   . TYR A 1 601 ? 4.867   -10.263 74.627  1.00 61.71  ? 601 TYR A O   1 
ATOM 4509 C CB  . TYR A 1 601 ? 6.970   -9.514  72.745  1.00 46.82  ? 601 TYR A CB  1 
ATOM 4510 C CG  . TYR A 1 601 ? 7.858   -8.821  71.740  1.00 48.09  ? 601 TYR A CG  1 
ATOM 4511 C CD1 . TYR A 1 601 ? 8.232   -9.449  70.561  1.00 47.20  ? 601 TYR A CD1 1 
ATOM 4512 C CD2 . TYR A 1 601 ? 8.323   -7.534  71.971  1.00 49.15  ? 601 TYR A CD2 1 
ATOM 4513 C CE1 . TYR A 1 601 ? 9.045   -8.817  69.644  1.00 52.04  ? 601 TYR A CE1 1 
ATOM 4514 C CE2 . TYR A 1 601 ? 9.135   -6.893  71.059  1.00 50.96  ? 601 TYR A CE2 1 
ATOM 4515 C CZ  . TYR A 1 601 ? 9.492   -7.539  69.898  1.00 55.40  ? 601 TYR A CZ  1 
ATOM 4516 O OH  . TYR A 1 601 ? 10.302  -6.902  68.988  1.00 58.28  ? 601 TYR A OH  1 
ATOM 4517 N N   . SER A 1 602 ? 3.705   -10.927 72.816  1.00 57.55  ? 602 SER A N   1 
ATOM 4518 C CA  . SER A 1 602 ? 2.758   -11.745 73.559  1.00 50.01  ? 602 SER A CA  1 
ATOM 4519 C C   . SER A 1 602 ? 3.070   -13.224 73.381  1.00 51.34  ? 602 SER A C   1 
ATOM 4520 O O   . SER A 1 602 ? 3.297   -13.692 72.262  1.00 65.71  ? 602 SER A O   1 
ATOM 4521 C CB  . SER A 1 602 ? 1.324   -11.462 73.109  1.00 57.67  ? 602 SER A CB  1 
ATOM 4522 O OG  . SER A 1 602 ? 0.436   -12.460 73.579  1.00 60.99  ? 602 SER A OG  1 
ATOM 4523 N N   . LYS A 1 603 ? 3.084   -13.953 74.494  1.00 45.81  ? 603 LYS A N   1 
ATOM 4524 C CA  . LYS A 1 603 ? 3.225   -15.400 74.469  1.00 49.62  ? 603 LYS A CA  1 
ATOM 4525 C C   . LYS A 1 603 ? 2.427   -15.983 75.624  1.00 57.65  ? 603 LYS A C   1 
ATOM 4526 O O   . LYS A 1 603 ? 2.269   -15.340 76.664  1.00 67.32  ? 603 LYS A O   1 
ATOM 4527 C CB  . LYS A 1 603 ? 4.691   -15.834 74.568  1.00 54.64  ? 603 LYS A CB  1 
ATOM 4528 C CG  . LYS A 1 603 ? 4.912   -17.318 74.338  1.00 51.02  ? 603 LYS A CG  1 
ATOM 4529 C CD  . LYS A 1 603 ? 6.376   -17.687 74.443  1.00 56.53  ? 603 LYS A CD  1 
ATOM 4530 C CE  . LYS A 1 603 ? 6.591   -19.155 74.130  1.00 57.90  ? 603 LYS A CE  1 
ATOM 4531 N NZ  . LYS A 1 603 ? 8.036   -19.488 74.022  1.00 64.67  ? 603 LYS A NZ  1 
ATOM 4532 N N   . LYS A 1 604 ? 1.925   -17.199 75.433  1.00 59.67  ? 604 LYS A N   1 
ATOM 4533 C CA  . LYS A 1 604 ? 1.185   -17.922 76.460  1.00 50.32  ? 604 LYS A CA  1 
ATOM 4534 C C   . LYS A 1 604 ? 2.012   -19.128 76.883  1.00 53.99  ? 604 LYS A C   1 
ATOM 4535 O O   . LYS A 1 604 ? 2.419   -19.935 76.042  1.00 64.79  ? 604 LYS A O   1 
ATOM 4536 C CB  . LYS A 1 604 ? -0.188  -18.349 75.945  1.00 52.45  ? 604 LYS A CB  1 
ATOM 4537 C CG  . LYS A 1 604 ? -1.246  -17.270 76.045  1.00 59.51  ? 604 LYS A CG  1 
ATOM 4538 C CD  . LYS A 1 604 ? -2.625  -17.831 75.760  1.00 58.27  ? 604 LYS A CD  1 
ATOM 4539 C CE  . LYS A 1 604 ? -3.112  -18.688 76.909  1.00 55.38  ? 604 LYS A CE  1 
ATOM 4540 N NZ  . LYS A 1 604 ? -3.506  -17.868 78.085  1.00 61.86  ? 604 LYS A NZ  1 
ATOM 4541 N N   . ILE A 1 605 ? 2.267   -19.241 78.182  1.00 61.67  ? 605 ILE A N   1 
ATOM 4542 C CA  . ILE A 1 605 ? 2.982   -20.386 78.740  1.00 59.09  ? 605 ILE A CA  1 
ATOM 4543 C C   . ILE A 1 605 ? 2.057   -21.102 79.716  1.00 59.35  ? 605 ILE A C   1 
ATOM 4544 O O   . ILE A 1 605 ? 1.778   -20.573 80.802  1.00 70.82  ? 605 ILE A O   1 
ATOM 4545 C CB  . ILE A 1 605 ? 4.288   -19.956 79.423  1.00 63.44  ? 605 ILE A CB  1 
ATOM 4546 C CG1 . ILE A 1 605 ? 5.220   -19.283 78.415  1.00 65.47  ? 605 ILE A CG1 1 
ATOM 4547 C CG2 . ILE A 1 605 ? 4.965   -21.152 80.071  1.00 60.59  ? 605 ILE A CG2 1 
ATOM 4548 C CD1 . ILE A 1 605 ? 6.014   -20.253 77.575  1.00 68.85  ? 605 ILE A CD1 1 
ATOM 4549 N N   . PRO A 1 606 ? 1.552   -22.294 79.382  1.00 54.56  ? 606 PRO A N   1 
ATOM 4550 C CA  . PRO A 1 606 ? 1.797   -23.057 78.155  1.00 55.02  ? 606 PRO A CA  1 
ATOM 4551 C C   . PRO A 1 606 ? 0.988   -22.526 76.979  1.00 59.46  ? 606 PRO A C   1 
ATOM 4552 O O   . PRO A 1 606 ? 0.056   -21.749 77.159  1.00 63.10  ? 606 PRO A O   1 
ATOM 4553 C CB  . PRO A 1 606 ? 1.382   -24.482 78.544  1.00 59.34  ? 606 PRO A CB  1 
ATOM 4554 C CG  . PRO A 1 606 ? 0.427   -24.338 79.705  1.00 54.05  ? 606 PRO A CG  1 
ATOM 4555 C CD  . PRO A 1 606 ? 0.524   -22.925 80.227  1.00 55.71  ? 606 PRO A CD  1 
ATOM 4556 N N   . GLN A 1 607 ? 1.339   -22.928 75.761  1.00 60.96  ? 607 GLN A N   1 
ATOM 4557 C CA  . GLN A 1 607 ? 0.653   -22.433 74.577  1.00 53.98  ? 607 GLN A CA  1 
ATOM 4558 C C   . GLN A 1 607 ? -0.795  -22.902 74.560  1.00 60.28  ? 607 GLN A C   1 
ATOM 4559 O O   . GLN A 1 607 ? -1.126  -23.967 75.087  1.00 66.61  ? 607 GLN A O   1 
ATOM 4560 C CB  . GLN A 1 607 ? 1.386   -22.901 73.317  1.00 57.53  ? 607 GLN A CB  1 
ATOM 4561 C CG  . GLN A 1 607 ? 0.862   -24.194 72.719  1.00 59.11  ? 607 GLN A CG  1 
ATOM 4562 C CD  . GLN A 1 607 ? 1.774   -24.750 71.650  1.00 60.06  ? 607 GLN A CD  1 
ATOM 4563 O OE1 . GLN A 1 607 ? 2.819   -24.178 71.351  1.00 69.09  ? 607 GLN A OE1 1 
ATOM 4564 N NE2 . GLN A 1 607 ? 1.379   -25.872 71.062  1.00 62.32  ? 607 GLN A NE2 1 
ATOM 4565 N N   . ALA A 1 608 ? -1.662  -22.081 73.975  1.00 59.70  ? 608 ALA A N   1 
ATOM 4566 C CA  . ALA A 1 608 ? -3.078  -22.391 73.858  1.00 55.06  ? 608 ALA A CA  1 
ATOM 4567 C C   . ALA A 1 608 ? -3.463  -22.889 72.474  1.00 54.22  ? 608 ALA A C   1 
ATOM 4568 O O   . ALA A 1 608 ? -4.652  -23.088 72.212  1.00 63.50  ? 608 ALA A O   1 
ATOM 4569 C CB  . ALA A 1 608 ? -3.916  -21.159 74.214  1.00 57.09  ? 608 ALA A CB  1 
ATOM 4570 N N   . TYR A 1 609 ? -2.494  -23.096 71.589  1.00 57.61  ? 609 TYR A N   1 
ATOM 4571 C CA  . TYR A 1 609 ? -2.775  -23.479 70.214  1.00 57.50  ? 609 TYR A CA  1 
ATOM 4572 C C   . TYR A 1 609 ? -2.797  -24.994 70.065  1.00 61.30  ? 609 TYR A C   1 
ATOM 4573 O O   . TYR A 1 609 ? -1.848  -25.682 70.451  1.00 63.96  ? 609 TYR A O   1 
ATOM 4574 C CB  . TYR A 1 609 ? -1.734  -22.883 69.267  1.00 56.13  ? 609 TYR A CB  1 
ATOM 4575 C CG  . TYR A 1 609 ? -2.050  -23.111 67.809  1.00 56.04  ? 609 TYR A CG  1 
ATOM 4576 C CD1 . TYR A 1 609 ? -3.012  -22.351 67.160  1.00 56.28  ? 609 TYR A CD1 1 
ATOM 4577 C CD2 . TYR A 1 609 ? -1.395  -24.096 67.083  1.00 56.68  ? 609 TYR A CD2 1 
ATOM 4578 C CE1 . TYR A 1 609 ? -3.306  -22.559 65.831  1.00 56.75  ? 609 TYR A CE1 1 
ATOM 4579 C CE2 . TYR A 1 609 ? -1.684  -24.312 65.754  1.00 52.12  ? 609 TYR A CE2 1 
ATOM 4580 C CZ  . TYR A 1 609 ? -2.641  -23.541 65.134  1.00 58.26  ? 609 TYR A CZ  1 
ATOM 4581 O OH  . TYR A 1 609 ? -2.932  -23.753 63.808  1.00 65.24  ? 609 TYR A OH  1 
ATOM 4582 N N   . ASN A 1 610 ? -3.891  -25.501 69.492  1.00 64.05  ? 610 ASN A N   1 
ATOM 4583 C CA  . ASN A 1 610 ? -4.032  -26.918 69.148  1.00 62.17  ? 610 ASN A CA  1 
ATOM 4584 C C   . ASN A 1 610 ? -3.793  -27.825 70.350  1.00 67.26  ? 610 ASN A C   1 
ATOM 4585 O O   . ASN A 1 610 ? -3.139  -28.865 70.243  1.00 73.43  ? 610 ASN A O   1 
ATOM 4586 C CB  . ASN A 1 610 ? -3.099  -27.300 67.998  1.00 63.92  ? 610 ASN A CB  1 
ATOM 4587 C CG  . ASN A 1 610 ? -3.766  -27.176 66.646  1.00 70.41  ? 610 ASN A CG  1 
ATOM 4588 O OD1 . ASN A 1 610 ? -4.847  -26.601 66.526  1.00 73.96  ? 610 ASN A OD1 1 
ATOM 4589 N ND2 . ASN A 1 610 ? -3.125  -27.719 65.620  1.00 74.11  ? 610 ASN A ND2 1 
ATOM 4590 N N   . GLN A 1 611 ? -4.317  -27.437 71.507  1.00 68.23  ? 611 GLN A N   1 
ATOM 4591 C CA  . GLN A 1 611 ? -4.184  -28.245 72.715  1.00 65.74  ? 611 GLN A CA  1 
ATOM 4592 C C   . GLN A 1 611 ? -5.393  -29.162 72.829  1.00 74.17  ? 611 GLN A C   1 
ATOM 4593 O O   . GLN A 1 611 ? -6.378  -28.831 73.492  1.00 76.88  ? 611 GLN A O   1 
ATOM 4594 C CB  . GLN A 1 611 ? -4.050  -27.350 73.940  1.00 63.43  ? 611 GLN A CB  1 
ATOM 4595 C CG  . GLN A 1 611 ? -2.780  -26.523 73.959  1.00 67.44  ? 611 GLN A CG  1 
ATOM 4596 C CD  . GLN A 1 611 ? -1.563  -27.332 74.351  1.00 71.70  ? 611 GLN A CD  1 
ATOM 4597 O OE1 . GLN A 1 611 ? -0.436  -26.990 73.998  1.00 73.38  ? 611 GLN A OE1 1 
ATOM 4598 N NE2 . GLN A 1 611 ? -1.784  -28.415 75.085  1.00 76.63  ? 611 GLN A NE2 1 
ATOM 4599 N N   . ALA A 1 612 ? -5.322  -30.328 72.179  1.00 79.18  ? 612 ALA A N   1 
ATOM 4600 C CA  . ALA A 1 612 ? -6.418  -31.286 72.217  1.00 76.41  ? 612 ALA A CA  1 
ATOM 4601 C C   . ALA A 1 612 ? -6.761  -31.725 73.632  1.00 77.45  ? 612 ALA A C   1 
ATOM 4602 O O   . ALA A 1 612 ? -7.921  -32.050 73.905  1.00 77.81  ? 612 ALA A O   1 
ATOM 4603 C CB  . ALA A 1 612 ? -6.079  -32.510 71.366  1.00 74.93  ? 612 ALA A CB  1 
ATOM 4604 N N   . THR A 1 613 ? -5.782  -31.739 74.530  1.00 77.58  ? 613 THR A N   1 
ATOM 4605 C CA  . THR A 1 613 ? -6.002  -31.978 75.945  1.00 79.36  ? 613 THR A CA  1 
ATOM 4606 C C   . THR A 1 613 ? -5.518  -30.766 76.729  1.00 78.66  ? 613 THR A C   1 
ATOM 4607 O O   . THR A 1 613 ? -4.651  -30.016 76.273  1.00 83.20  ? 613 THR A O   1 
ATOM 4608 C CB  . THR A 1 613 ? -5.274  -33.240 76.424  1.00 79.92  ? 613 THR A CB  1 
ATOM 4609 O OG1 . THR A 1 613 ? -5.227  -33.252 77.855  1.00 81.20  ? 613 THR A OG1 1 
ATOM 4610 C CG2 . THR A 1 613 ? -3.858  -33.278 75.874  1.00 76.76  ? 613 THR A CG2 1 
ATOM 4611 N N   . LEU A 1 614 ? -6.094  -30.576 77.908  1.00 71.00  ? 614 LEU A N   1 
ATOM 4612 C CA  . LEU A 1 614 ? -5.729  -29.437 78.739  1.00 70.52  ? 614 LEU A CA  1 
ATOM 4613 C C   . LEU A 1 614 ? -4.265  -29.546 79.142  1.00 73.62  ? 614 LEU A C   1 
ATOM 4614 O O   . LEU A 1 614 ? -3.874  -30.548 79.752  1.00 76.43  ? 614 LEU A O   1 
ATOM 4615 C CB  . LEU A 1 614 ? -6.610  -29.372 79.977  1.00 71.96  ? 614 LEU A CB  1 
ATOM 4616 C CG  . LEU A 1 614 ? -6.432  -28.134 80.856  1.00 72.45  ? 614 LEU A CG  1 
ATOM 4617 C CD1 . LEU A 1 614 ? -7.054  -26.917 80.199  1.00 71.31  ? 614 LEU A CD1 1 
ATOM 4618 C CD2 . LEU A 1 614 ? -7.026  -28.364 82.236  1.00 73.39  ? 614 LEU A CD2 1 
ATOM 4619 N N   . PRO A 1 615 ? -3.428  -28.562 78.820  1.00 72.07  ? 615 PRO A N   1 
ATOM 4620 C CA  . PRO A 1 615 ? -2.017  -28.640 79.209  1.00 65.57  ? 615 PRO A CA  1 
ATOM 4621 C C   . PRO A 1 615 ? -1.856  -28.513 80.715  1.00 66.99  ? 615 PRO A C   1 
ATOM 4622 O O   . PRO A 1 615 ? -2.680  -27.919 81.412  1.00 69.97  ? 615 PRO A O   1 
ATOM 4623 C CB  . PRO A 1 615 ? -1.371  -27.458 78.477  1.00 66.83  ? 615 PRO A CB  1 
ATOM 4624 C CG  . PRO A 1 615 ? -2.482  -26.540 78.135  1.00 68.82  ? 615 PRO A CG  1 
ATOM 4625 C CD  . PRO A 1 615 ? -3.756  -27.321 78.098  1.00 69.89  ? 615 PRO A CD  1 
ATOM 4626 N N   . THR A 1 616 ? -0.777  -29.100 81.218  1.00 74.86  ? 616 THR A N   1 
ATOM 4627 C CA  . THR A 1 616 ? -0.462  -28.998 82.632  1.00 75.18  ? 616 THR A CA  1 
ATOM 4628 C C   . THR A 1 616 ? 0.030   -27.596 82.964  1.00 74.78  ? 616 THR A C   1 
ATOM 4629 O O   . THR A 1 616 ? 0.737   -26.960 82.177  1.00 74.39  ? 616 THR A O   1 
ATOM 4630 C CB  . THR A 1 616 ? 0.598   -30.026 83.026  1.00 74.20  ? 616 THR A CB  1 
ATOM 4631 O OG1 . THR A 1 616 ? 1.792   -29.795 82.270  1.00 75.64  ? 616 THR A OG1 1 
ATOM 4632 C CG2 . THR A 1 616 ? 0.099   -31.434 82.751  1.00 75.34  ? 616 THR A CG2 1 
ATOM 4633 N N   . ALA A 1 617 ? -0.366  -27.111 84.137  1.00 73.07  ? 617 ALA A N   1 
ATOM 4634 C CA  . ALA A 1 617 ? 0.110   -25.818 84.604  1.00 68.40  ? 617 ALA A CA  1 
ATOM 4635 C C   . ALA A 1 617 ? 1.618   -25.855 84.805  1.00 70.30  ? 617 ALA A C   1 
ATOM 4636 O O   . ALA A 1 617 ? 2.160   -26.796 85.393  1.00 75.03  ? 617 ALA A O   1 
ATOM 4637 C CB  . ALA A 1 617 ? -0.589  -25.430 85.905  1.00 69.52  ? 617 ALA A CB  1 
ATOM 4638 N N   . THR A 1 618 ? 2.297   -24.829 84.310  1.00 70.72  ? 618 THR A N   1 
ATOM 4639 C CA  . THR A 1 618 ? 3.749   -24.761 84.341  1.00 72.52  ? 618 THR A CA  1 
ATOM 4640 C C   . THR A 1 618 ? 4.202   -23.584 85.193  1.00 69.72  ? 618 THR A C   1 
ATOM 4641 O O   . THR A 1 618 ? 3.474   -22.610 85.396  1.00 73.26  ? 618 THR A O   1 
ATOM 4642 C CB  . THR A 1 618 ? 4.331   -24.639 82.927  1.00 71.22  ? 618 THR A CB  1 
ATOM 4643 O OG1 . THR A 1 618 ? 3.955   -23.379 82.359  1.00 65.82  ? 618 THR A OG1 1 
ATOM 4644 C CG2 . THR A 1 618 ? 3.819   -25.761 82.040  1.00 72.14  ? 618 THR A CG2 1 
ATOM 4645 N N   . ALA A 1 619 ? 5.426   -23.692 85.696  1.00 67.38  ? 619 ALA A N   1 
ATOM 4646 C CA  . ALA A 1 619 ? 6.054   -22.617 86.444  1.00 65.34  ? 619 ALA A CA  1 
ATOM 4647 C C   . ALA A 1 619 ? 6.796   -21.692 85.490  1.00 69.32  ? 619 ALA A C   1 
ATOM 4648 O O   . ALA A 1 619 ? 7.462   -22.149 84.557  1.00 75.46  ? 619 ALA A O   1 
ATOM 4649 C CB  . ALA A 1 619 ? 7.018   -23.178 87.489  1.00 65.70  ? 619 ALA A CB  1 
ATOM 4650 N N   . LEU A 1 620 ? 6.674   -20.391 85.726  1.00 65.35  ? 620 LEU A N   1 
ATOM 4651 C CA  . LEU A 1 620 ? 7.307   -19.379 84.886  1.00 63.92  ? 620 LEU A CA  1 
ATOM 4652 C C   . LEU A 1 620 ? 8.559   -18.882 85.598  1.00 68.69  ? 620 LEU A C   1 
ATOM 4653 O O   . LEU A 1 620 ? 8.497   -17.966 86.421  1.00 71.67  ? 620 LEU A O   1 
ATOM 4654 C CB  . LEU A 1 620 ? 6.340   -18.239 84.591  1.00 59.83  ? 620 LEU A CB  1 
ATOM 4655 C CG  . LEU A 1 620 ? 6.767   -17.354 83.425  1.00 58.88  ? 620 LEU A CG  1 
ATOM 4656 C CD1 . LEU A 1 620 ? 6.711   -18.153 82.138  1.00 64.79  ? 620 LEU A CD1 1 
ATOM 4657 C CD2 . LEU A 1 620 ? 5.885   -16.127 83.337  1.00 62.50  ? 620 LEU A CD2 1 
ATOM 4658 N N   . VAL A 1 621 ? 9.699   -19.488 85.275  1.00 67.84  ? 621 VAL A N   1 
ATOM 4659 C CA  . VAL A 1 621 ? 10.962  -19.125 85.906  1.00 67.36  ? 621 VAL A CA  1 
ATOM 4660 C C   . VAL A 1 621 ? 11.947  -18.640 84.851  1.00 70.08  ? 621 VAL A C   1 
ATOM 4661 O O   . VAL A 1 621 ? 12.887  -17.900 85.160  1.00 70.27  ? 621 VAL A O   1 
ATOM 4662 C CB  . VAL A 1 621 ? 11.548  -20.307 86.699  1.00 65.19  ? 621 VAL A CB  1 
ATOM 4663 C CG1 . VAL A 1 621 ? 10.619  -20.690 87.836  1.00 66.68  ? 621 VAL A CG1 1 
ATOM 4664 C CG2 . VAL A 1 621 ? 11.790  -21.495 85.785  1.00 60.13  ? 621 VAL A CG2 1 
ATOM 4665 N N   . ASN A 1 622 ? 11.741  -19.049 83.602  1.00 72.05  ? 622 ASN A N   1 
ATOM 4666 C CA  . ASN A 1 622 ? 12.660  -18.725 82.520  1.00 63.45  ? 622 ASN A CA  1 
ATOM 4667 C C   . ASN A 1 622 ? 11.917  -18.721 81.194  1.00 65.94  ? 622 ASN A C   1 
ATOM 4668 O O   . ASN A 1 622 ? 11.228  -19.689 80.860  1.00 69.59  ? 622 ASN A O   1 
ATOM 4669 C CB  . ASN A 1 622 ? 13.819  -19.724 82.465  1.00 63.80  ? 622 ASN A CB  1 
ATOM 4670 C CG  . ASN A 1 622 ? 14.954  -19.248 81.585  1.00 68.55  ? 622 ASN A CG  1 
ATOM 4671 O OD1 . ASN A 1 622 ? 14.999  -18.087 81.183  1.00 69.49  ? 622 ASN A OD1 1 
ATOM 4672 N ND2 . ASN A 1 622 ? 15.880  -20.148 81.275  1.00 69.26  ? 622 ASN A ND2 1 
ATOM 4673 N N   . PHE A 1 623 ? 12.062  -17.631 80.446  1.00 58.76  ? 623 PHE A N   1 
ATOM 4674 C CA  . PHE A 1 623 ? 11.573  -17.565 79.079  1.00 52.97  ? 623 PHE A CA  1 
ATOM 4675 C C   . PHE A 1 623 ? 12.406  -16.539 78.328  1.00 58.91  ? 623 PHE A C   1 
ATOM 4676 O O   . PHE A 1 623 ? 13.028  -15.659 78.928  1.00 60.24  ? 623 PHE A O   1 
ATOM 4677 C CB  . PHE A 1 623 ? 10.081  -17.213 79.014  1.00 57.18  ? 623 PHE A CB  1 
ATOM 4678 C CG  . PHE A 1 623 ? 9.725   -15.926 79.700  1.00 53.09  ? 623 PHE A CG  1 
ATOM 4679 C CD1 . PHE A 1 623 ? 9.432   -15.903 81.053  1.00 52.68  ? 623 PHE A CD1 1 
ATOM 4680 C CD2 . PHE A 1 623 ? 9.666   -14.741 78.989  1.00 54.79  ? 623 PHE A CD2 1 
ATOM 4681 C CE1 . PHE A 1 623 ? 9.098   -14.723 81.681  1.00 53.33  ? 623 PHE A CE1 1 
ATOM 4682 C CE2 . PHE A 1 623 ? 9.333   -13.559 79.614  1.00 54.95  ? 623 PHE A CE2 1 
ATOM 4683 C CZ  . PHE A 1 623 ? 9.047   -13.551 80.961  1.00 51.79  ? 623 PHE A CZ  1 
ATOM 4684 N N   . GLN A 1 624 ? 12.413  -16.667 77.006  1.00 61.27  ? 624 GLN A N   1 
ATOM 4685 C CA  . GLN A 1 624 ? 13.203  -15.805 76.138  1.00 51.96  ? 624 GLN A CA  1 
ATOM 4686 C C   . GLN A 1 624 ? 12.265  -15.018 75.238  1.00 56.80  ? 624 GLN A C   1 
ATOM 4687 O O   . GLN A 1 624 ? 11.541  -15.601 74.426  1.00 69.40  ? 624 GLN A O   1 
ATOM 4688 C CB  . GLN A 1 624 ? 14.191  -16.629 75.314  1.00 57.55  ? 624 GLN A CB  1 
ATOM 4689 C CG  . GLN A 1 624 ? 15.177  -17.397 76.167  1.00 55.85  ? 624 GLN A CG  1 
ATOM 4690 C CD  . GLN A 1 624 ? 14.716  -18.810 76.444  1.00 62.53  ? 624 GLN A CD  1 
ATOM 4691 O OE1 . GLN A 1 624 ? 13.919  -19.372 75.696  1.00 67.09  ? 624 GLN A OE1 1 
ATOM 4692 N NE2 . GLN A 1 624 ? 15.202  -19.385 77.537  1.00 64.13  ? 624 GLN A NE2 1 
ATOM 4693 N N   . VAL A 1 625 ? 12.282  -13.699 75.387  1.00 56.11  ? 625 VAL A N   1 
ATOM 4694 C CA  . VAL A 1 625 ? 11.453  -12.809 74.582  1.00 54.17  ? 625 VAL A CA  1 
ATOM 4695 C C   . VAL A 1 625 ? 12.392  -11.987 73.707  1.00 53.21  ? 625 VAL A C   1 
ATOM 4696 O O   . VAL A 1 625 ? 13.494  -11.638 74.152  1.00 58.89  ? 625 VAL A O   1 
ATOM 4697 C CB  . VAL A 1 625 ? 10.562  -11.928 75.474  1.00 54.08  ? 625 VAL A CB  1 
ATOM 4698 C CG1 . VAL A 1 625 ? 11.404  -11.138 76.464  1.00 50.72  ? 625 VAL A CG1 1 
ATOM 4699 C CG2 . VAL A 1 625 ? 9.691   -11.006 74.644  1.00 53.85  ? 625 VAL A CG2 1 
ATOM 4700 N N   . PRO A 1 626 ? 12.030  -11.691 72.459  1.00 59.40  ? 626 PRO A N   1 
ATOM 4701 C CA  . PRO A 1 626 ? 12.893  -10.842 71.633  1.00 57.83  ? 626 PRO A CA  1 
ATOM 4702 C C   . PRO A 1 626 ? 13.143  -9.497  72.293  1.00 60.17  ? 626 PRO A C   1 
ATOM 4703 O O   . PRO A 1 626 ? 12.252  -8.900  72.901  1.00 64.07  ? 626 PRO A O   1 
ATOM 4704 C CB  . PRO A 1 626 ? 12.105  -10.677 70.329  1.00 48.62  ? 626 PRO A CB  1 
ATOM 4705 C CG  . PRO A 1 626 ? 11.105  -11.764 70.314  1.00 54.34  ? 626 PRO A CG  1 
ATOM 4706 C CD  . PRO A 1 626 ? 10.950  -12.329 71.688  1.00 53.11  ? 626 PRO A CD  1 
ATOM 4707 N N   . MET A 1 627 ? 14.376  -9.031  72.175  1.00 58.79  ? 627 MET A N   1 
ATOM 4708 C CA  . MET A 1 627 ? 14.751  -7.752  72.759  1.00 55.89  ? 627 MET A CA  1 
ATOM 4709 C C   . MET A 1 627 ? 13.986  -6.639  72.058  1.00 63.22  ? 627 MET A C   1 
ATOM 4710 O O   . MET A 1 627 ? 14.021  -6.559  70.825  1.00 62.83  ? 627 MET A O   1 
ATOM 4711 C CB  . MET A 1 627 ? 16.253  -7.528  72.635  1.00 57.01  ? 627 MET A CB  1 
ATOM 4712 C CG  . MET A 1 627 ? 16.785  -6.406  73.505  1.00 55.01  ? 627 MET A CG  1 
ATOM 4713 S SD  . MET A 1 627 ? 18.500  -6.667  73.989  1.00 84.55  ? 627 MET A SD  1 
ATOM 4714 C CE  . MET A 1 627 ? 18.863  -5.112  74.795  1.00 63.28  ? 627 MET A CE  1 
ATOM 4715 N N   . PRO A 1 628 ? 13.280  -5.779  72.784  1.00 52.51  ? 628 PRO A N   1 
ATOM 4716 C CA  . PRO A 1 628 ? 12.506  -4.722  72.130  1.00 45.07  ? 628 PRO A CA  1 
ATOM 4717 C C   . PRO A 1 628 ? 13.401  -3.575  71.687  1.00 50.79  ? 628 PRO A C   1 
ATOM 4718 O O   . PRO A 1 628 ? 14.565  -3.461  72.072  1.00 63.55  ? 628 PRO A O   1 
ATOM 4719 C CB  . PRO A 1 628 ? 11.516  -4.275  73.205  1.00 46.70  ? 628 PRO A CB  1 
ATOM 4720 C CG  . PRO A 1 628 ? 12.067  -4.757  74.497  1.00 54.75  ? 628 PRO A CG  1 
ATOM 4721 C CD  . PRO A 1 628 ? 13.155  -5.752  74.250  1.00 51.29  ? 628 PRO A CD  1 
ATOM 4722 N N   . GLN A 1 629 ? 12.824  -2.711  70.850  1.00 47.82  ? 629 GLN A N   1 
ATOM 4723 C CA  . GLN A 1 629 ? 13.592  -1.617  70.267  1.00 52.93  ? 629 GLN A CA  1 
ATOM 4724 C C   . GLN A 1 629 ? 14.074  -0.628  71.319  1.00 55.49  ? 629 GLN A C   1 
ATOM 4725 O O   . GLN A 1 629 ? 15.224  -0.180  71.261  1.00 58.73  ? 629 GLN A O   1 
ATOM 4726 C CB  . GLN A 1 629 ? 12.760  -0.889  69.217  1.00 48.78  ? 629 GLN A CB  1 
ATOM 4727 C CG  . GLN A 1 629 ? 13.478  0.299   68.625  1.00 45.24  ? 629 GLN A CG  1 
ATOM 4728 C CD  . GLN A 1 629 ? 14.462  -0.116  67.559  1.00 53.39  ? 629 GLN A CD  1 
ATOM 4729 O OE1 . GLN A 1 629 ? 14.244  -1.093  66.848  1.00 59.29  ? 629 GLN A OE1 1 
ATOM 4730 N NE2 . GLN A 1 629 ? 15.571  0.599   67.469  1.00 55.55  ? 629 GLN A NE2 1 
ATOM 4731 N N   . SER A 1 630 ? 13.218  -0.275  72.279  1.00 55.32  ? 630 SER A N   1 
ATOM 4732 C CA  . SER A 1 630 ? 13.575  0.736   73.266  1.00 54.75  ? 630 SER A CA  1 
ATOM 4733 C C   . SER A 1 630 ? 14.787  0.340   74.096  1.00 57.08  ? 630 SER A C   1 
ATOM 4734 O O   . SER A 1 630 ? 15.478  1.220   74.618  1.00 66.75  ? 630 SER A O   1 
ATOM 4735 C CB  . SER A 1 630 ? 12.386  1.010   74.187  1.00 55.19  ? 630 SER A CB  1 
ATOM 4736 O OG  . SER A 1 630 ? 12.069  -0.134  74.957  1.00 61.63  ? 630 SER A OG  1 
ATOM 4737 N N   . MET A 1 631 ? 15.066  -0.953  74.216  1.00 59.81  ? 631 MET A N   1 
ATOM 4738 C CA  . MET A 1 631 ? 16.178  -1.438  75.018  1.00 53.76  ? 631 MET A CA  1 
ATOM 4739 C C   . MET A 1 631 ? 17.500  -1.458  74.266  1.00 56.68  ? 631 MET A C   1 
ATOM 4740 O O   . MET A 1 631 ? 18.526  -1.796  74.863  1.00 62.97  ? 631 MET A O   1 
ATOM 4741 C CB  . MET A 1 631 ? 15.869  -2.846  75.529  1.00 54.87  ? 631 MET A CB  1 
ATOM 4742 C CG  . MET A 1 631 ? 14.708  -2.900  76.493  1.00 57.26  ? 631 MET A CG  1 
ATOM 4743 S SD  . MET A 1 631 ? 14.607  -4.490  77.315  1.00 68.34  ? 631 MET A SD  1 
ATOM 4744 C CE  . MET A 1 631 ? 14.845  -3.991  79.009  1.00 62.70  ? 631 MET A CE  1 
ATOM 4745 N N   . LEU A 1 632 ? 17.505  -1.108  72.984  1.00 57.44  ? 632 LEU A N   1 
ATOM 4746 C CA  . LEU A 1 632 ? 18.777  -1.242  72.289  1.00 55.13  ? 632 LEU A CA  1 
ATOM 4747 C C   . LEU A 1 632 ? 19.630  0.010   72.476  1.00 59.65  ? 632 LEU A C   1 
ATOM 4748 O O   . LEU A 1 632 ? 19.093  1.103   72.671  1.00 65.43  ? 632 LEU A O   1 
ATOM 4749 C CB  . LEU A 1 632 ? 18.557  -1.484  70.801  1.00 54.74  ? 632 LEU A CB  1 
ATOM 4750 C CG  . LEU A 1 632 ? 17.778  -2.746  70.439  1.00 61.07  ? 632 LEU A CG  1 
ATOM 4751 C CD1 . LEU A 1 632 ? 17.929  -3.034  68.962  1.00 56.92  ? 632 LEU A CD1 1 
ATOM 4752 C CD2 . LEU A 1 632 ? 18.234  -3.922  71.278  1.00 57.28  ? 632 LEU A CD2 1 
ATOM 4753 N N   . PRO A 1 633 ? 20.953  -0.132  72.424  1.00 57.96  ? 633 PRO A N   1 
ATOM 4754 C CA  . PRO A 1 633 ? 21.818  1.050   72.483  1.00 58.50  ? 633 PRO A CA  1 
ATOM 4755 C C   . PRO A 1 633 ? 21.670  1.911   71.243  1.00 54.04  ? 633 PRO A C   1 
ATOM 4756 O O   . PRO A 1 633 ? 21.376  1.425   70.148  1.00 59.27  ? 633 PRO A O   1 
ATOM 4757 C CB  . PRO A 1 633 ? 23.231  0.463   72.577  1.00 61.43  ? 633 PRO A CB  1 
ATOM 4758 C CG  . PRO A 1 633 ? 23.117  -0.934  72.126  1.00 58.98  ? 633 PRO A CG  1 
ATOM 4759 C CD  . PRO A 1 633 ? 21.712  -1.388  72.321  1.00 54.41  ? 633 PRO A CD  1 
ATOM 4760 N N   . THR A 1 634 ? 21.881  3.207   71.427  1.00 59.39  ? 634 THR A N   1 
ATOM 4761 C CA  . THR A 1 634 ? 21.914  4.142   70.316  1.00 60.83  ? 634 THR A CA  1 
ATOM 4762 C C   . THR A 1 634 ? 23.355  4.475   69.966  1.00 59.01  ? 634 THR A C   1 
ATOM 4763 O O   . THR A 1 634 ? 24.109  4.970   70.808  1.00 71.27  ? 634 THR A O   1 
ATOM 4764 C CB  . THR A 1 634 ? 21.155  5.422   70.654  1.00 63.00  ? 634 THR A CB  1 
ATOM 4765 O OG1 . THR A 1 634 ? 19.941  5.093   71.340  1.00 68.60  ? 634 THR A OG1 1 
ATOM 4766 C CG2 . THR A 1 634 ? 20.830  6.176   69.390  1.00 58.94  ? 634 THR A CG2 1 
ATOM 4767 N N   . THR A 1 635 ? 23.722  4.219   68.711  1.00 59.20  ? 635 THR A N   1 
ATOM 4768 C CA  . THR A 1 635 ? 25.082  4.369   68.204  1.00 62.98  ? 635 THR A CA  1 
ATOM 4769 C C   . THR A 1 635 ? 26.096  3.771   69.174  1.00 64.95  ? 635 THR A C   1 
ATOM 4770 O O   . THR A 1 635 ? 26.885  4.512   69.775  1.00 67.39  ? 635 THR A O   1 
ATOM 4771 C CB  . THR A 1 635 ? 25.410  5.842   67.941  1.00 62.41  ? 635 THR A CB  1 
ATOM 4772 O OG1 . THR A 1 635 ? 25.164  6.616   69.121  1.00 66.04  ? 635 THR A OG1 1 
ATOM 4773 C CG2 . THR A 1 635 ? 24.558  6.381   66.807  1.00 56.95  ? 635 THR A CG2 1 
ATOM 4774 N N   . PRO A 1 636 ? 26.103  2.447   69.364  1.00 61.95  ? 636 PRO A N   1 
ATOM 4775 C CA  . PRO A 1 636 ? 27.041  1.851   70.332  1.00 59.76  ? 636 PRO A CA  1 
ATOM 4776 C C   . PRO A 1 636 ? 28.499  2.129   70.020  1.00 60.97  ? 636 PRO A C   1 
ATOM 4777 O O   . PRO A 1 636 ? 29.306  2.221   70.952  1.00 64.78  ? 636 PRO A O   1 
ATOM 4778 C CB  . PRO A 1 636 ? 26.740  0.348   70.254  1.00 59.01  ? 636 PRO A CB  1 
ATOM 4779 C CG  . PRO A 1 636 ? 25.472  0.206   69.524  1.00 57.14  ? 636 PRO A CG  1 
ATOM 4780 C CD  . PRO A 1 636 ? 25.158  1.467   68.801  1.00 57.73  ? 636 PRO A CD  1 
ATOM 4781 N N   . SER A 1 637 ? 28.868  2.256   68.746  1.00 63.37  ? 637 SER A N   1 
ATOM 4782 C CA  . SER A 1 637 ? 30.258  2.525   68.400  1.00 64.19  ? 637 SER A CA  1 
ATOM 4783 C C   . SER A 1 637 ? 30.708  3.905   68.861  1.00 67.33  ? 637 SER A C   1 
ATOM 4784 O O   . SER A 1 637 ? 31.901  4.110   69.109  1.00 69.60  ? 637 SER A O   1 
ATOM 4785 C CB  . SER A 1 637 ? 30.464  2.383   66.893  1.00 63.38  ? 637 SER A CB  1 
ATOM 4786 O OG  . SER A 1 637 ? 29.831  1.215   66.402  1.00 69.12  ? 637 SER A OG  1 
ATOM 4787 N N   . ILE A 1 638 ? 29.784  4.852   68.983  1.00 64.85  ? 638 ILE A N   1 
ATOM 4788 C CA  . ILE A 1 638 ? 30.113  6.207   69.399  1.00 64.61  ? 638 ILE A CA  1 
ATOM 4789 C C   . ILE A 1 638 ? 29.716  6.467   70.846  1.00 62.32  ? 638 ILE A C   1 
ATOM 4790 O O   . ILE A 1 638 ? 30.535  6.924   71.642  1.00 69.00  ? 638 ILE A O   1 
ATOM 4791 C CB  . ILE A 1 638 ? 29.452  7.231   68.451  1.00 63.09  ? 638 ILE A CB  1 
ATOM 4792 C CG1 . ILE A 1 638 ? 29.963  7.041   67.024  1.00 63.22  ? 638 ILE A CG1 1 
ATOM 4793 C CG2 . ILE A 1 638 ? 29.719  8.645   68.932  1.00 60.85  ? 638 ILE A CG2 1 
ATOM 4794 C CD1 . ILE A 1 638 ? 29.252  7.897   66.004  1.00 65.91  ? 638 ILE A CD1 1 
ATOM 4795 N N   . SER A 1 639 ? 28.468  6.176   71.205  1.00 62.20  ? 639 SER A N   1 
ATOM 4796 C CA  . SER A 1 639 ? 27.967  6.466   72.541  1.00 62.54  ? 639 SER A CA  1 
ATOM 4797 C C   . SER A 1 639 ? 28.212  5.340   73.534  1.00 67.31  ? 639 SER A C   1 
ATOM 4798 O O   . SER A 1 639 ? 27.852  5.484   74.707  1.00 70.23  ? 639 SER A O   1 
ATOM 4799 C CB  . SER A 1 639 ? 26.469  6.780   72.490  1.00 61.53  ? 639 SER A CB  1 
ATOM 4800 O OG  . SER A 1 639 ? 25.739  5.675   71.993  1.00 72.23  ? 639 SER A OG  1 
ATOM 4801 N N   . GLY A 1 640 ? 28.809  4.234   73.104  1.00 61.61  ? 640 GLY A N   1 
ATOM 4802 C CA  . GLY A 1 640 ? 29.084  3.137   74.007  1.00 60.54  ? 640 GLY A CA  1 
ATOM 4803 C C   . GLY A 1 640 ? 27.964  2.119   74.064  1.00 66.39  ? 640 GLY A C   1 
ATOM 4804 O O   . GLY A 1 640 ? 26.811  2.435   73.761  1.00 73.43  ? 640 GLY A O   1 
ATOM 4805 N N   . ASP A 1 641 ? 28.294  0.896   74.455  1.00 73.34  ? 641 ASP A N   1 
ATOM 4806 C CA  . ASP A 1 641 ? 27.324  -0.182  74.544  1.00 71.86  ? 641 ASP A CA  1 
ATOM 4807 C C   . ASP A 1 641 ? 26.687  -0.211  75.932  1.00 70.77  ? 641 ASP A C   1 
ATOM 4808 O O   . ASP A 1 641 ? 27.125  0.473   76.859  1.00 76.13  ? 641 ASP A O   1 
ATOM 4809 C CB  . ASP A 1 641 ? 27.991  -1.521  74.230  1.00 68.04  ? 641 ASP A CB  1 
ATOM 4810 C CG  . ASP A 1 641 ? 26.997  -2.596  73.859  1.00 71.61  ? 641 ASP A CG  1 
ATOM 4811 O OD1 . ASP A 1 641 ? 25.796  -2.281  73.741  1.00 77.30  ? 641 ASP A OD1 1 
ATOM 4812 O OD2 . ASP A 1 641 ? 27.417  -3.757  73.679  1.00 74.65  ? 641 ASP A OD2 1 
ATOM 4813 N N   . LEU A 1 642 ? 25.632  -1.020  76.062  1.00 70.73  ? 642 LEU A N   1 
ATOM 4814 C CA  . LEU A 1 642 ? 24.954  -1.167  77.345  1.00 71.33  ? 642 LEU A CA  1 
ATOM 4815 C C   . LEU A 1 642 ? 25.841  -1.797  78.408  1.00 75.22  ? 642 LEU A C   1 
ATOM 4816 O O   . LEU A 1 642 ? 25.535  -1.676  79.599  1.00 77.73  ? 642 LEU A O   1 
ATOM 4817 C CB  . LEU A 1 642 ? 23.688  -2.007  77.187  1.00 71.83  ? 642 LEU A CB  1 
ATOM 4818 C CG  . LEU A 1 642 ? 22.963  -1.928  75.852  1.00 71.71  ? 642 LEU A CG  1 
ATOM 4819 C CD1 . LEU A 1 642 ? 21.919  -3.021  75.752  1.00 72.75  ? 642 LEU A CD1 1 
ATOM 4820 C CD2 . LEU A 1 642 ? 22.320  -0.571  75.753  1.00 75.79  ? 642 LEU A CD2 1 
ATOM 4821 N N   . GLY A 1 643 ? 26.918  -2.476  78.009  1.00 78.44  ? 643 GLY A N   1 
ATOM 4822 C CA  . GLY A 1 643 ? 27.769  -3.129  78.988  1.00 78.24  ? 643 GLY A CA  1 
ATOM 4823 C C   . GLY A 1 643 ? 28.344  -2.162  80.004  1.00 81.55  ? 643 GLY A C   1 
ATOM 4824 O O   . GLY A 1 643 ? 28.340  -2.433  81.207  1.00 84.00  ? 643 GLY A O   1 
ATOM 4825 N N   . THR A 1 644 ? 28.728  -0.978  79.532  1.00 79.36  ? 644 THR A N   1 
ATOM 4826 C CA  . THR A 1 644 ? 29.251  0.045   80.449  1.00 79.56  ? 644 THR A CA  1 
ATOM 4827 C C   . THR A 1 644 ? 28.276  1.191   80.509  1.00 79.63  ? 644 THR A C   1 
ATOM 4828 O O   . THR A 1 644 ? 27.735  1.440   81.597  1.00 81.02  ? 644 THR A O   1 
ATOM 4829 C CB  . THR A 1 644 ? 30.623  0.494   79.963  1.00 80.65  ? 644 THR A CB  1 
ATOM 4830 O OG1 . THR A 1 644 ? 30.434  0.803   78.586  1.00 83.48  ? 644 THR A OG1 1 
ATOM 4831 C CG2 . THR A 1 644 ? 31.669  -0.596  80.107  1.00 77.19  ? 644 THR A CG2 1 
ATOM 4832 N N   . ASN A 1 645 ? 28.060  1.870   79.383  1.00 76.85  ? 645 ASN A N   1 
ATOM 4833 C CA  . ASN A 1 645 ? 27.113  3.011   79.334  1.00 74.08  ? 645 ASN A CA  1 
ATOM 4834 C C   . ASN A 1 645 ? 25.705  2.433   79.443  1.00 76.42  ? 645 ASN A C   1 
ATOM 4835 O O   . ASN A 1 645 ? 25.052  2.290   78.400  1.00 84.88  ? 645 ASN A O   1 
ATOM 4836 C CB  . ASN A 1 645 ? 27.351  3.854   78.091  1.00 73.93  ? 645 ASN A CB  1 
ATOM 4837 C CG  . ASN A 1 645 ? 28.763  4.380   78.018  1.00 76.13  ? 645 ASN A CG  1 
ATOM 4838 O OD1 . ASN A 1 645 ? 29.628  3.947   78.785  1.00 80.35  ? 645 ASN A OD1 1 
ATOM 4839 N ND2 . ASN A 1 645 ? 29.016  5.310   77.112  1.00 75.75  ? 645 ASN A ND2 1 
ATOM 4840 N N   . PHE A 1 646 ? 25.253  2.131   80.659  1.00 30.00  ? 646 PHE A N   1 
ATOM 4841 C CA  . PHE A 1 646 ? 23.937  1.466   80.856  1.00 30.00  ? 646 PHE A CA  1 
ATOM 4842 C C   . PHE A 1 646 ? 22.816  2.482   80.694  1.00 30.00  ? 646 PHE A C   1 
ATOM 4843 O O   . PHE A 1 646 ? 21.656  2.154   80.997  1.00 30.00  ? 646 PHE A O   1 
ATOM 4844 C CB  . PHE A 1 646 ? 23.939  0.758   82.213  1.00 30.00  ? 646 PHE A CB  1 
ATOM 4845 C CG  . PHE A 1 646 ? 24.098  1.646   83.436  1.00 30.00  ? 646 PHE A CG  1 
ATOM 4846 C CD1 . PHE A 1 646 ? 22.991  2.204   84.060  1.00 30.00  ? 646 PHE A CD1 1 
ATOM 4847 C CD2 . PHE A 1 646 ? 25.354  1.904   83.967  1.00 30.00  ? 646 PHE A CD2 1 
ATOM 4848 C CE1 . PHE A 1 646 ? 23.140  3.011   85.172  1.00 30.00  ? 646 PHE A CE1 1 
ATOM 4849 C CE2 . PHE A 1 646 ? 25.496  2.707   85.083  1.00 30.00  ? 646 PHE A CE2 1 
ATOM 4850 C CZ  . PHE A 1 646 ? 24.391  3.259   85.682  1.00 30.00  ? 646 PHE A CZ  1 
ATOM 4851 N N   . TYR A 1 647 ? 23.143  3.687   80.241  1.00 74.85  ? 647 TYR A N   1 
ATOM 4852 C CA  . TYR A 1 647 ? 22.099  4.692   79.947  1.00 73.13  ? 647 TYR A CA  1 
ATOM 4853 C C   . TYR A 1 647 ? 21.747  4.578   78.479  1.00 72.04  ? 647 TYR A C   1 
ATOM 4854 O O   . TYR A 1 647 ? 20.657  5.001   78.108  1.00 75.34  ? 647 TYR A O   1 
ATOM 4855 C CB  . TYR A 1 647 ? 22.689  6.068   80.250  1.00 76.08  ? 647 TYR A CB  1 
ATOM 4856 C CG  . TYR A 1 647 ? 23.390  6.718   79.068  1.00 77.87  ? 647 TYR A CG  1 
ATOM 4857 C CD1 . TYR A 1 647 ? 24.642  6.285   78.655  1.00 75.16  ? 647 TYR A CD1 1 
ATOM 4858 C CD2 . TYR A 1 647 ? 22.788  7.745   78.353  1.00 74.07  ? 647 TYR A CD2 1 
ATOM 4859 C CE1 . TYR A 1 647 ? 25.275  6.850   77.564  1.00 77.33  ? 647 TYR A CE1 1 
ATOM 4860 C CE2 . TYR A 1 647 ? 23.415  8.325   77.265  1.00 76.45  ? 647 TYR A CE2 1 
ATOM 4861 C CZ  . TYR A 1 647 ? 24.661  7.873   76.870  1.00 81.12  ? 647 TYR A CZ  1 
ATOM 4862 O OH  . TYR A 1 647 ? 25.297  8.430   75.804  1.00 84.37  ? 647 TYR A OH  1 
ATOM 4863 N N   . ASN A 1 648 ? 22.634  4.007   77.664  1.00 58.54  ? 648 ASN A N   1 
ATOM 4864 C CA  . ASN A 1 648 ? 22.419  3.980   76.192  1.00 65.72  ? 648 ASN A CA  1 
ATOM 4865 C C   . ASN A 1 648 ? 21.217  3.099   75.846  1.00 73.34  ? 648 ASN A C   1 
ATOM 4866 O O   . ASN A 1 648 ? 20.878  3.020   74.658  1.00 78.39  ? 648 ASN A O   1 
ATOM 4867 C CB  . ASN A 1 648 ? 23.690  3.582   75.451  1.00 66.00  ? 648 ASN A CB  1 
ATOM 4868 C CG  . ASN A 1 648 ? 23.742  4.119   74.045  1.00 65.70  ? 648 ASN A CG  1 
ATOM 4869 O OD1 . ASN A 1 648 ? 22.974  5.018   73.700  1.00 68.96  ? 648 ASN A OD1 1 
ATOM 4870 N ND2 . ASN A 1 648 ? 24.629  3.585   73.222  1.00 67.55  ? 648 ASN A ND2 1 
ATOM 4871 N N   . CYS A 1 649 ? 20.560  2.509   76.836  1.00 66.25  ? 649 CYS A N   1 
ATOM 4872 C CA  . CYS A 1 649 ? 19.337  1.714   76.582  1.00 64.06  ? 649 CYS A CA  1 
ATOM 4873 C C   . CYS A 1 649 ? 18.104  2.417   77.143  1.00 69.75  ? 649 CYS A C   1 
ATOM 4874 O O   . CYS A 1 649 ? 18.267  3.395   77.887  1.00 72.32  ? 649 CYS A O   1 
ATOM 4875 C CB  . CYS A 1 649 ? 19.399  0.390   77.322  1.00 64.97  ? 649 CYS A CB  1 
ATOM 4876 S SG  . CYS A 1 649 ? 20.063  0.541   78.996  1.00 75.27  ? 649 CYS A SG  1 
ATOM 4877 N N   . GLY A 1 650 ? 16.914  1.932   76.804  1.00 63.08  ? 650 GLY A N   1 
ATOM 4878 C CA  . GLY A 1 650 ? 15.681  2.467   77.403  1.00 59.30  ? 650 GLY A CA  1 
ATOM 4879 C C   . GLY A 1 650 ? 15.035  1.383   78.228  1.00 65.10  ? 650 GLY A C   1 
ATOM 4880 O O   . GLY A 1 650 ? 15.741  0.432   78.599  1.00 65.81  ? 650 GLY A O   1 
ATOM 4881 N N   . HIS A 1 651 ? 13.738  1.487   78.489  1.00 59.90  ? 651 HIS A N   1 
ATOM 4882 C CA  . HIS A 1 651 ? 13.144  0.502   79.373  1.00 50.02  ? 651 HIS A CA  1 
ATOM 4883 C C   . HIS A 1 651 ? 12.014  -0.210  78.648  1.00 59.50  ? 651 HIS A C   1 
ATOM 4884 O O   . HIS A 1 651 ? 11.439  0.305   77.687  1.00 64.16  ? 651 HIS A O   1 
ATOM 4885 C CB  . HIS A 1 651 ? 12.617  1.137   80.665  1.00 56.77  ? 651 HIS A CB  1 
ATOM 4886 C CG  . HIS A 1 651 ? 11.497  2.105   80.449  1.00 58.51  ? 651 HIS A CG  1 
ATOM 4887 N ND1 . HIS A 1 651 ? 11.696  3.465   80.355  1.00 65.87  ? 651 HIS A ND1 1 
ATOM 4888 C CD2 . HIS A 1 651 ? 10.165  1.910   80.309  1.00 50.05  ? 651 HIS A CD2 1 
ATOM 4889 C CE1 . HIS A 1 651 ? 10.536  4.067   80.167  1.00 59.98  ? 651 HIS A CE1 1 
ATOM 4890 N NE2 . HIS A 1 651 ? 9.590   3.145   80.135  1.00 59.02  ? 651 HIS A NE2 1 
ATOM 4891 N N   . SER A 1 652 ? 11.711  -1.412  79.123  1.00 61.99  ? 652 SER A N   1 
ATOM 4892 C CA  . SER A 1 652 ? 10.570  -2.173  78.648  1.00 51.31  ? 652 SER A CA  1 
ATOM 4893 C C   . SER A 1 652 ? 9.807   -2.692  79.855  1.00 54.13  ? 652 SER A C   1 
ATOM 4894 O O   . SER A 1 652 ? 10.395  -2.997  80.895  1.00 57.74  ? 652 SER A O   1 
ATOM 4895 C CB  . SER A 1 652 ? 10.998  -3.332  77.742  1.00 50.40  ? 652 SER A CB  1 
ATOM 4896 O OG  . SER A 1 652 ? 11.202  -4.516  78.490  1.00 68.51  ? 652 SER A OG  1 
ATOM 4897 N N   . VAL A 1 653 ? 8.490   -2.782  79.715  1.00 54.68  ? 653 VAL A N   1 
ATOM 4898 C CA  . VAL A 1 653 ? 7.616   -3.234  80.788  1.00 50.75  ? 653 VAL A CA  1 
ATOM 4899 C C   . VAL A 1 653 ? 7.173   -4.656  80.484  1.00 51.54  ? 653 VAL A C   1 
ATOM 4900 O O   . VAL A 1 653 ? 6.589   -4.927  79.429  1.00 62.12  ? 653 VAL A O   1 
ATOM 4901 C CB  . VAL A 1 653 ? 6.403   -2.305  80.968  1.00 52.76  ? 653 VAL A CB  1 
ATOM 4902 C CG1 . VAL A 1 653 ? 5.477   -2.852  82.038  1.00 54.67  ? 653 VAL A CG1 1 
ATOM 4903 C CG2 . VAL A 1 653 ? 6.863   -0.904  81.326  1.00 53.57  ? 653 VAL A CG2 1 
ATOM 4904 N N   . LEU A 1 654 ? 7.457   -5.562  81.412  1.00 55.96  ? 654 LEU A N   1 
ATOM 4905 C CA  . LEU A 1 654 ? 7.085   -6.963  81.290  1.00 55.93  ? 654 LEU A CA  1 
ATOM 4906 C C   . LEU A 1 654 ? 5.810   -7.199  82.087  1.00 55.16  ? 654 LEU A C   1 
ATOM 4907 O O   . LEU A 1 654 ? 5.834   -7.186  83.322  1.00 64.65  ? 654 LEU A O   1 
ATOM 4908 C CB  . LEU A 1 654 ? 8.215   -7.864  81.788  1.00 57.75  ? 654 LEU A CB  1 
ATOM 4909 C CG  . LEU A 1 654 ? 8.037   -9.374  81.650  1.00 57.13  ? 654 LEU A CG  1 
ATOM 4910 C CD1 . LEU A 1 654 ? 7.981   -9.777  80.190  1.00 61.19  ? 654 LEU A CD1 1 
ATOM 4911 C CD2 . LEU A 1 654 ? 9.172   -10.086 82.358  1.00 55.93  ? 654 LEU A CD2 1 
ATOM 4912 N N   . LYS A 1 655 ? 4.703   -7.407  81.383  1.00 56.51  ? 655 LYS A N   1 
ATOM 4913 C CA  . LYS A 1 655 ? 3.397   -7.609  82.001  1.00 57.10  ? 655 LYS A CA  1 
ATOM 4914 C C   . LYS A 1 655 ? 3.077   -9.096  81.957  1.00 58.43  ? 655 LYS A C   1 
ATOM 4915 O O   . LYS A 1 655 ? 2.879   -9.663  80.877  1.00 64.23  ? 655 LYS A O   1 
ATOM 4916 C CB  . LYS A 1 655 ? 2.326   -6.786  81.290  1.00 57.39  ? 655 LYS A CB  1 
ATOM 4917 C CG  . LYS A 1 655 ? 2.545   -5.288  81.394  1.00 63.48  ? 655 LYS A CG  1 
ATOM 4918 C CD  . LYS A 1 655 ? 1.405   -4.509  80.769  1.00 62.38  ? 655 LYS A CD  1 
ATOM 4919 C CE  . LYS A 1 655 ? 1.516   -3.030  81.090  1.00 62.65  ? 655 LYS A CE  1 
ATOM 4920 N NZ  . LYS A 1 655 ? 0.550   -2.217  80.303  1.00 69.06  ? 655 LYS A NZ  1 
ATOM 4921 N N   . ILE A 1 656 ? 3.029   -9.724  83.127  1.00 64.47  ? 656 ILE A N   1 
ATOM 4922 C CA  . ILE A 1 656 ? 2.796   -11.157 83.253  1.00 64.41  ? 656 ILE A CA  1 
ATOM 4923 C C   . ILE A 1 656 ? 1.503   -11.376 84.022  1.00 61.89  ? 656 ILE A C   1 
ATOM 4924 O O   . ILE A 1 656 ? 1.319   -10.825 85.113  1.00 68.41  ? 656 ILE A O   1 
ATOM 4925 C CB  . ILE A 1 656 ? 3.972   -11.861 83.948  1.00 60.95  ? 656 ILE A CB  1 
ATOM 4926 C CG1 . ILE A 1 656 ? 5.266   -11.639 83.165  1.00 60.47  ? 656 ILE A CG1 1 
ATOM 4927 C CG2 . ILE A 1 656 ? 3.685   -13.340 84.104  1.00 58.05  ? 656 ILE A CG2 1 
ATOM 4928 C CD1 . ILE A 1 656 ? 6.506   -12.020 83.930  1.00 62.38  ? 656 ILE A CD1 1 
ATOM 4929 N N   . SER A 1 657 ? 0.611   -12.177 83.450  1.00 59.74  ? 657 SER A N   1 
ATOM 4930 C CA  . SER A 1 657 ? -0.639  -12.556 84.087  1.00 60.41  ? 657 SER A CA  1 
ATOM 4931 C C   . SER A 1 657 ? -0.862  -14.046 83.879  1.00 61.05  ? 657 SER A C   1 
ATOM 4932 O O   . SER A 1 657 ? -0.428  -14.608 82.871  1.00 68.15  ? 657 SER A O   1 
ATOM 4933 C CB  . SER A 1 657 ? -1.811  -11.753 83.521  1.00 62.11  ? 657 SER A CB  1 
ATOM 4934 O OG  . SER A 1 657 ? -2.360  -12.386 82.380  1.00 67.75  ? 657 SER A OG  1 
ATOM 4935 N N   . ASN A 1 658 ? -1.525  -14.686 84.834  1.00 58.78  ? 658 ASN A N   1 
ATOM 4936 C CA  . ASN A 1 658 ? -1.771  -16.119 84.774  1.00 59.99  ? 658 ASN A CA  1 
ATOM 4937 C C   . ASN A 1 658 ? -3.258  -16.410 84.957  1.00 61.06  ? 658 ASN A C   1 
ATOM 4938 O O   . ASN A 1 658 ? -4.044  -15.546 85.350  1.00 64.05  ? 658 ASN A O   1 
ATOM 4939 C CB  . ASN A 1 658 ? -0.920  -16.854 85.814  1.00 61.21  ? 658 ASN A CB  1 
ATOM 4940 C CG  . ASN A 1 658 ? -1.224  -16.430 87.236  1.00 66.76  ? 658 ASN A CG  1 
ATOM 4941 O OD1 . ASN A 1 658 ? -2.173  -15.691 87.492  1.00 73.90  ? 658 ASN A OD1 1 
ATOM 4942 N ND2 . ASN A 1 658 ? -0.413  -16.900 88.173  1.00 66.94  ? 658 ASN A ND2 1 
ATOM 4943 N N   . SER A 1 659 ? -3.637  -17.659 84.681  1.00 64.09  ? 659 SER A N   1 
ATOM 4944 C CA  . SER A 1 659 ? -5.033  -18.067 84.779  1.00 62.04  ? 659 SER A CA  1 
ATOM 4945 C C   . SER A 1 659 ? -5.565  -18.016 86.204  1.00 66.20  ? 659 SER A C   1 
ATOM 4946 O O   . SER A 1 659 ? -6.784  -18.087 86.393  1.00 75.15  ? 659 SER A O   1 
ATOM 4947 C CB  . SER A 1 659 ? -5.209  -19.478 84.219  1.00 64.14  ? 659 SER A CB  1 
ATOM 4948 O OG  . SER A 1 659 ? -4.573  -20.432 85.049  1.00 68.70  ? 659 SER A OG  1 
ATOM 4949 N N   . SER A 1 660 ? -4.695  -17.894 87.202  1.00 63.24  ? 660 SER A N   1 
ATOM 4950 C CA  . SER A 1 660 ? -5.104  -17.770 88.592  1.00 66.10  ? 660 SER A CA  1 
ATOM 4951 C C   . SER A 1 660 ? -5.449  -16.337 88.973  1.00 70.70  ? 660 SER A C   1 
ATOM 4952 O O   . SER A 1 660 ? -5.768  -16.076 90.136  1.00 71.33  ? 660 SER A O   1 
ATOM 4953 C CB  . SER A 1 660 ? -4.004  -18.300 89.515  1.00 65.60  ? 660 SER A CB  1 
ATOM 4954 O OG  . SER A 1 660 ? -3.516  -19.549 89.059  1.00 70.42  ? 660 SER A OG  1 
ATOM 4955 N N   . GLY A 1 661 ? -5.391  -15.409 88.022  1.00 70.91  ? 661 GLY A N   1 
ATOM 4956 C CA  . GLY A 1 661 ? -5.660  -14.015 88.292  1.00 65.29  ? 661 GLY A CA  1 
ATOM 4957 C C   . GLY A 1 661 ? -4.484  -13.226 88.814  1.00 69.86  ? 661 GLY A C   1 
ATOM 4958 O O   . GLY A 1 661 ? -4.623  -12.019 89.041  1.00 76.54  ? 661 GLY A O   1 
ATOM 4959 N N   . ASP A 1 662 ? -3.335  -13.862 89.010  1.00 69.07  ? 662 ASP A N   1 
ATOM 4960 C CA  . ASP A 1 662 ? -2.150  -13.179 89.504  1.00 68.68  ? 662 ASP A CA  1 
ATOM 4961 C C   . ASP A 1 662 ? -1.537  -12.349 88.385  1.00 73.10  ? 662 ASP A C   1 
ATOM 4962 O O   . ASP A 1 662 ? -1.327  -12.849 87.276  1.00 78.32  ? 662 ASP A O   1 
ATOM 4963 C CB  . ASP A 1 662 ? -1.138  -14.188 90.046  1.00 70.19  ? 662 ASP A CB  1 
ATOM 4964 C CG  . ASP A 1 662 ? -1.681  -14.981 91.216  1.00 80.56  ? 662 ASP A CG  1 
ATOM 4965 O OD1 . ASP A 1 662 ? -2.553  -14.453 91.939  1.00 81.95  ? 662 ASP A OD1 1 
ATOM 4966 O OD2 . ASP A 1 662 ? -1.249  -16.136 91.406  1.00 80.65  ? 662 ASP A OD2 1 
ATOM 4967 N N   . TYR A 1 663 ? -1.258  -11.084 88.679  1.00 70.32  ? 663 TYR A N   1 
ATOM 4968 C CA  . TYR A 1 663 ? -0.707  -10.148 87.710  1.00 62.24  ? 663 TYR A CA  1 
ATOM 4969 C C   . TYR A 1 663 ? 0.684   -9.732  88.165  1.00 67.39  ? 663 TYR A C   1 
ATOM 4970 O O   . TYR A 1 663 ? 0.955   -9.675  89.367  1.00 75.04  ? 663 TYR A O   1 
ATOM 4971 C CB  . TYR A 1 663 ? -1.609  -8.923  87.558  1.00 61.99  ? 663 TYR A CB  1 
ATOM 4972 C CG  . TYR A 1 663 ? -1.112  -7.905  86.559  1.00 65.93  ? 663 TYR A CG  1 
ATOM 4973 C CD1 . TYR A 1 663 ? -1.275  -8.107  85.196  1.00 63.95  ? 663 TYR A CD1 1 
ATOM 4974 C CD2 . TYR A 1 663 ? -0.487  -6.742  86.979  1.00 69.08  ? 663 TYR A CD2 1 
ATOM 4975 C CE1 . TYR A 1 663 ? -0.826  -7.179  84.280  1.00 65.50  ? 663 TYR A CE1 1 
ATOM 4976 C CE2 . TYR A 1 663 ? -0.036  -5.808  86.071  1.00 66.48  ? 663 TYR A CE2 1 
ATOM 4977 C CZ  . TYR A 1 663 ? -0.207  -6.032  84.723  1.00 68.58  ? 663 TYR A CZ  1 
ATOM 4978 O OH  . TYR A 1 663 ? 0.243   -5.103  83.816  1.00 72.50  ? 663 TYR A OH  1 
ATOM 4979 N N   . LEU A 1 664 ? 1.561   -9.454  87.205  1.00 67.52  ? 664 LEU A N   1 
ATOM 4980 C CA  . LEU A 1 664 ? 2.939   -9.075  87.492  1.00 64.42  ? 664 LEU A CA  1 
ATOM 4981 C C   . LEU A 1 664 ? 3.403   -8.073  86.447  1.00 64.65  ? 664 LEU A C   1 
ATOM 4982 O O   . LEU A 1 664 ? 3.621   -8.440  85.287  1.00 72.57  ? 664 LEU A O   1 
ATOM 4983 C CB  . LEU A 1 664 ? 3.850   -10.304 87.507  1.00 63.21  ? 664 LEU A CB  1 
ATOM 4984 C CG  . LEU A 1 664 ? 5.250   -10.132 88.094  1.00 67.21  ? 664 LEU A CG  1 
ATOM 4985 C CD1 . LEU A 1 664 ? 5.181   -9.955  89.597  1.00 67.28  ? 664 LEU A CD1 1 
ATOM 4986 C CD2 . LEU A 1 664 ? 6.118   -11.323 87.735  1.00 68.28  ? 664 LEU A CD2 1 
ATOM 4987 N N   . GLU A 1 665 ? 3.549   -6.816  86.853  1.00 66.98  ? 665 GLU A N   1 
ATOM 4988 C CA  . GLU A 1 665 ? 4.061   -5.754  85.992  1.00 67.57  ? 665 GLU A CA  1 
ATOM 4989 C C   . GLU A 1 665 ? 5.499   -5.472  86.408  1.00 72.77  ? 665 GLU A C   1 
ATOM 4990 O O   . GLU A 1 665 ? 5.748   -5.009  87.526  1.00 76.91  ? 665 GLU A O   1 
ATOM 4991 C CB  . GLU A 1 665 ? 3.201   -4.498  86.095  1.00 67.65  ? 665 GLU A CB  1 
ATOM 4992 C CG  . GLU A 1 665 ? 3.099   -3.712  84.802  1.00 72.14  ? 665 GLU A CG  1 
ATOM 4993 C CD  . GLU A 1 665 ? 2.410   -2.376  84.986  1.00 80.46  ? 665 GLU A CD  1 
ATOM 4994 O OE1 . GLU A 1 665 ? 3.112   -1.345  85.028  1.00 79.35  ? 665 GLU A OE1 1 
ATOM 4995 O OE2 . GLU A 1 665 ? 1.166   -2.356  85.090  1.00 81.81  ? 665 GLU A OE2 1 
ATOM 4996 N N   . VAL A 1 666 ? 6.439   -5.744  85.508  1.00 61.07  ? 666 VAL A N   1 
ATOM 4997 C CA  . VAL A 1 666 ? 7.863   -5.652  85.799  1.00 55.83  ? 666 VAL A CA  1 
ATOM 4998 C C   . VAL A 1 666 ? 8.482   -4.615  84.877  1.00 61.05  ? 666 VAL A C   1 
ATOM 4999 O O   . VAL A 1 666 ? 8.325   -4.690  83.653  1.00 69.32  ? 666 VAL A O   1 
ATOM 5000 C CB  . VAL A 1 666 ? 8.559   -7.013  85.630  1.00 54.88  ? 666 VAL A CB  1 
ATOM 5001 C CG1 . VAL A 1 666 ? 9.962   -6.967  86.206  1.00 58.30  ? 666 VAL A CG1 1 
ATOM 5002 C CG2 . VAL A 1 666 ? 7.734   -8.107  86.277  1.00 57.98  ? 666 VAL A CG2 1 
ATOM 5003 N N   . LEU A 1 667 ? 9.190   -3.653  85.462  1.00 64.23  ? 667 LEU A N   1 
ATOM 5004 C CA  . LEU A 1 667 ? 9.943   -2.668  84.695  1.00 56.60  ? 667 LEU A CA  1 
ATOM 5005 C C   . LEU A 1 667 ? 11.336  -3.225  84.441  1.00 59.44  ? 667 LEU A C   1 
ATOM 5006 O O   . LEU A 1 667 ? 12.159  -3.301  85.357  1.00 70.47  ? 667 LEU A O   1 
ATOM 5007 C CB  . LEU A 1 667 ? 10.020  -1.337  85.435  1.00 58.70  ? 667 LEU A CB  1 
ATOM 5008 C CG  . LEU A 1 667 ? 10.959  -0.315  84.793  1.00 55.82  ? 667 LEU A CG  1 
ATOM 5009 C CD1 . LEU A 1 667 ? 10.319  0.309   83.565  1.00 60.89  ? 667 LEU A CD1 1 
ATOM 5010 C CD2 . LEU A 1 667 ? 11.371  0.748   85.792  1.00 60.58  ? 667 LEU A CD2 1 
ATOM 5011 N N   . LEU A 1 668 ? 11.599  -3.620  83.201  1.00 57.35  ? 668 LEU A N   1 
ATOM 5012 C CA  . LEU A 1 668 ? 12.916  -4.106  82.807  1.00 56.00  ? 668 LEU A CA  1 
ATOM 5013 C C   . LEU A 1 668 ? 13.768  -2.902  82.429  1.00 60.06  ? 668 LEU A C   1 
ATOM 5014 O O   . LEU A 1 668 ? 13.564  -2.292  81.375  1.00 62.88  ? 668 LEU A O   1 
ATOM 5015 C CB  . LEU A 1 668 ? 12.805  -5.097  81.654  1.00 51.07  ? 668 LEU A CB  1 
ATOM 5016 C CG  . LEU A 1 668 ? 12.026  -6.377  81.947  1.00 57.62  ? 668 LEU A CG  1 
ATOM 5017 C CD1 . LEU A 1 668 ? 11.949  -7.237  80.702  1.00 60.89  ? 668 LEU A CD1 1 
ATOM 5018 C CD2 . LEU A 1 668 ? 12.662  -7.139  83.096  1.00 60.16  ? 668 LEU A CD2 1 
ATOM 5019 N N   . ILE A 1 669 ? 14.712  -2.552  83.294  1.00 61.82  ? 669 ILE A N   1 
ATOM 5020 C CA  . ILE A 1 669 ? 15.567  -1.390  83.104  1.00 61.65  ? 669 ILE A CA  1 
ATOM 5021 C C   . ILE A 1 669 ? 16.968  -1.735  83.585  1.00 61.44  ? 669 ILE A C   1 
ATOM 5022 O O   . ILE A 1 669 ? 17.137  -2.541  84.505  1.00 66.21  ? 669 ILE A O   1 
ATOM 5023 C CB  . ILE A 1 669 ? 15.012  -0.154  83.844  1.00 59.64  ? 669 ILE A CB  1 
ATOM 5024 C CG1 . ILE A 1 669 ? 15.750  1.109   83.409  1.00 57.68  ? 669 ILE A CG1 1 
ATOM 5025 C CG2 . ILE A 1 669 ? 15.082  -0.343  85.352  1.00 56.06  ? 669 ILE A CG2 1 
ATOM 5026 C CD1 . ILE A 1 669 ? 15.016  2.367   83.744  1.00 64.54  ? 669 ILE A CD1 1 
ATOM 5027 N N   . LYS A 1 670 ? 17.973  -1.144  82.948  1.00 61.01  ? 670 LYS A N   1 
ATOM 5028 C CA  . LYS A 1 670 ? 19.360  -1.398  83.305  1.00 62.92  ? 670 LYS A CA  1 
ATOM 5029 C C   . LYS A 1 670 ? 19.826  -0.366  84.322  1.00 64.32  ? 670 LYS A C   1 
ATOM 5030 O O   . LYS A 1 670 ? 19.896  0.830   84.018  1.00 69.43  ? 670 LYS A O   1 
ATOM 5031 C CB  . LYS A 1 670 ? 20.256  -1.376  82.070  1.00 58.90  ? 670 LYS A CB  1 
ATOM 5032 C CG  . LYS A 1 670 ? 21.491  -2.226  82.240  1.00 60.67  ? 670 LYS A CG  1 
ATOM 5033 C CD  . LYS A 1 670 ? 22.239  -2.402  80.945  1.00 61.73  ? 670 LYS A CD  1 
ATOM 5034 C CE  . LYS A 1 670 ? 23.294  -3.471  81.107  1.00 63.04  ? 670 LYS A CE  1 
ATOM 5035 N NZ  . LYS A 1 670 ? 23.927  -3.828  79.817  1.00 70.75  ? 670 LYS A NZ  1 
ATOM 5036 N N   . THR A 1 671 ? 20.144  -0.834  85.529  1.00 66.72  ? 671 THR A N   1 
ATOM 5037 C CA  . THR A 1 671 ? 20.639  0.023   86.593  1.00 67.93  ? 671 THR A CA  1 
ATOM 5038 C C   . THR A 1 671 ? 22.127  -0.133  86.853  1.00 70.70  ? 671 THR A C   1 
ATOM 5039 O O   . THR A 1 671 ? 22.718  0.735   87.499  1.00 71.39  ? 671 THR A O   1 
ATOM 5040 C CB  . THR A 1 671 ? 19.882  -0.260  87.898  1.00 67.16  ? 671 THR A CB  1 
ATOM 5041 O OG1 . THR A 1 671 ? 20.194  -1.582  88.354  1.00 74.51  ? 671 THR A OG1 1 
ATOM 5042 C CG2 . THR A 1 671 ? 18.390  -0.163  87.668  1.00 68.44  ? 671 THR A CG2 1 
ATOM 5043 N N   . THR A 1 672 ? 22.739  -1.209  86.372  1.00 79.13  ? 672 THR A N   1 
ATOM 5044 C CA  . THR A 1 672 ? 24.143  -1.499  86.615  1.00 76.74  ? 672 THR A CA  1 
ATOM 5045 C C   . THR A 1 672 ? 24.889  -1.681  85.298  1.00 77.38  ? 672 THR A C   1 
ATOM 5046 O O   . THR A 1 672 ? 24.314  -2.059  84.275  1.00 81.00  ? 672 THR A O   1 
ATOM 5047 C CB  . THR A 1 672 ? 24.300  -2.758  87.472  1.00 78.84  ? 672 THR A CB  1 
ATOM 5048 O OG1 . THR A 1 672 ? 23.919  -3.908  86.707  1.00 76.37  ? 672 THR A OG1 1 
ATOM 5049 C CG2 . THR A 1 672 ? 23.429  -2.677  88.716  1.00 75.61  ? 672 THR A CG2 1 
ATOM 5050 N N   . GLY A 1 673 ? 26.191  -1.402  85.341  1.00 77.27  ? 673 GLY A N   1 
ATOM 5051 C CA  . GLY A 1 673 ? 27.069  -1.639  84.219  1.00 75.48  ? 673 GLY A CA  1 
ATOM 5052 C C   . GLY A 1 673 ? 27.936  -2.873  84.426  1.00 76.76  ? 673 GLY A C   1 
ATOM 5053 O O   . GLY A 1 673 ? 27.824  -3.600  85.410  1.00 77.93  ? 673 GLY A O   1 
ATOM 5054 N N   . GLY A 1 674 ? 28.812  -3.106  83.454  1.00 80.19  ? 674 GLY A N   1 
ATOM 5055 C CA  . GLY A 1 674 ? 29.746  -4.211  83.537  1.00 81.26  ? 674 GLY A CA  1 
ATOM 5056 C C   . GLY A 1 674 ? 29.211  -5.490  82.930  1.00 82.07  ? 674 GLY A C   1 
ATOM 5057 O O   . GLY A 1 674 ? 29.946  -6.471  82.781  1.00 85.18  ? 674 GLY A O   1 
ATOM 5058 N N   . GLY A 1 675 ? 27.937  -5.491  82.582  1.00 76.14  ? 675 GLY A N   1 
ATOM 5059 C CA  . GLY A 1 675 ? 27.322  -6.649  81.981  1.00 71.74  ? 675 GLY A CA  1 
ATOM 5060 C C   . GLY A 1 675 ? 26.171  -6.252  81.092  1.00 71.60  ? 675 GLY A C   1 
ATOM 5061 O O   . GLY A 1 675 ? 25.978  -5.076  80.783  1.00 78.79  ? 675 GLY A O   1 
ATOM 5062 N N   . TYR A 1 676 ? 25.400  -7.252  80.680  1.00 67.46  ? 676 TYR A N   1 
ATOM 5063 C CA  . TYR A 1 676 ? 24.226  -7.055  79.837  1.00 69.94  ? 676 TYR A CA  1 
ATOM 5064 C C   . TYR A 1 676 ? 22.968  -7.568  80.528  1.00 71.11  ? 676 TYR A C   1 
ATOM 5065 O O   . TYR A 1 676 ? 22.144  -8.263  79.932  1.00 75.39  ? 676 TYR A O   1 
ATOM 5066 C CB  . TYR A 1 676 ? 24.425  -7.715  78.478  1.00 63.96  ? 676 TYR A CB  1 
ATOM 5067 C CG  . TYR A 1 676 ? 25.458  -7.002  77.641  1.00 67.41  ? 676 TYR A CG  1 
ATOM 5068 C CD1 . TYR A 1 676 ? 25.101  -5.944  76.817  1.00 68.63  ? 676 TYR A CD1 1 
ATOM 5069 C CD2 . TYR A 1 676 ? 26.796  -7.362  77.701  1.00 67.05  ? 676 TYR A CD2 1 
ATOM 5070 C CE1 . TYR A 1 676 ? 26.045  -5.281  76.060  1.00 71.85  ? 676 TYR A CE1 1 
ATOM 5071 C CE2 . TYR A 1 676 ? 27.747  -6.704  76.950  1.00 67.67  ? 676 TYR A CE2 1 
ATOM 5072 C CZ  . TYR A 1 676 ? 27.366  -5.665  76.131  1.00 73.47  ? 676 TYR A CZ  1 
ATOM 5073 O OH  . TYR A 1 676 ? 28.311  -5.008  75.379  1.00 75.57  ? 676 TYR A OH  1 
ATOM 5074 N N   . VAL A 1 677 ? 22.818  -7.218  81.801  1.00 63.15  ? 677 VAL A N   1 
ATOM 5075 C CA  . VAL A 1 677 ? 21.706  -7.657  82.634  1.00 61.61  ? 677 VAL A CA  1 
ATOM 5076 C C   . VAL A 1 677 ? 20.810  -6.458  82.899  1.00 66.15  ? 677 VAL A C   1 
ATOM 5077 O O   . VAL A 1 677 ? 21.285  -5.398  83.325  1.00 68.35  ? 677 VAL A O   1 
ATOM 5078 C CB  . VAL A 1 677 ? 22.203  -8.276  83.948  1.00 62.19  ? 677 VAL A CB  1 
ATOM 5079 C CG1 . VAL A 1 677 ? 21.091  -8.306  84.975  1.00 64.44  ? 677 VAL A CG1 1 
ATOM 5080 C CG2 . VAL A 1 677 ? 22.742  -9.674  83.701  1.00 61.67  ? 677 VAL A CG2 1 
ATOM 5081 N N   . PHE A 1 678 ? 19.516  -6.621  82.645  1.00 63.62  ? 678 PHE A N   1 
ATOM 5082 C CA  . PHE A 1 678 ? 18.533  -5.586  82.926  1.00 58.00  ? 678 PHE A CA  1 
ATOM 5083 C C   . PHE A 1 678 ? 17.827  -5.904  84.236  1.00 62.85  ? 678 PHE A C   1 
ATOM 5084 O O   . PHE A 1 678 ? 17.297  -7.004  84.412  1.00 70.54  ? 678 PHE A O   1 
ATOM 5085 C CB  . PHE A 1 678 ? 17.518  -5.482  81.789  1.00 57.50  ? 678 PHE A CB  1 
ATOM 5086 C CG  . PHE A 1 678 ? 18.059  -4.833  80.551  1.00 59.91  ? 678 PHE A CG  1 
ATOM 5087 C CD1 . PHE A 1 678 ? 17.982  -3.464  80.381  1.00 59.24  ? 678 PHE A CD1 1 
ATOM 5088 C CD2 . PHE A 1 678 ? 18.652  -5.595  79.559  1.00 58.39  ? 678 PHE A CD2 1 
ATOM 5089 C CE1 . PHE A 1 678 ? 18.478  -2.865  79.243  1.00 60.66  ? 678 PHE A CE1 1 
ATOM 5090 C CE2 . PHE A 1 678 ? 19.152  -5.001  78.419  1.00 60.08  ? 678 PHE A CE2 1 
ATOM 5091 C CZ  . PHE A 1 678 ? 19.065  -3.635  78.263  1.00 64.95  ? 678 PHE A CZ  1 
ATOM 5092 N N   . THR A 1 679 ? 17.824  -4.940  85.152  1.00 67.02  ? 679 THR A N   1 
ATOM 5093 C CA  . THR A 1 679 ? 17.205  -5.132  86.455  1.00 66.41  ? 679 THR A CA  1 
ATOM 5094 C C   . THR A 1 679 ? 15.691  -5.045  86.315  1.00 65.88  ? 679 THR A C   1 
ATOM 5095 O O   . THR A 1 679 ? 15.158  -4.012  85.896  1.00 70.69  ? 679 THR A O   1 
ATOM 5096 C CB  . THR A 1 679 ? 17.712  -4.091  87.449  1.00 70.90  ? 679 THR A CB  1 
ATOM 5097 O OG1 . THR A 1 679 ? 19.143  -4.128  87.492  1.00 74.59  ? 679 THR A OG1 1 
ATOM 5098 C CG2 . THR A 1 679 ? 17.160  -4.371  88.837  1.00 67.05  ? 679 THR A CG2 1 
ATOM 5099 N N   . GLY A 1 680 ? 15.000  -6.125  86.662  1.00 61.70  ? 680 GLY A N   1 
ATOM 5100 C CA  . GLY A 1 680 ? 13.555  -6.142  86.589  1.00 61.60  ? 680 GLY A CA  1 
ATOM 5101 C C   . GLY A 1 680 ? 12.899  -5.692  87.876  1.00 65.33  ? 680 GLY A C   1 
ATOM 5102 O O   . GLY A 1 680 ? 12.839  -6.449  88.848  1.00 71.92  ? 680 GLY A O   1 
ATOM 5103 N N   . LYS A 1 681 ? 12.408  -4.458  87.895  1.00 68.09  ? 681 LYS A N   1 
ATOM 5104 C CA  . LYS A 1 681 ? 11.725  -3.916  89.059  1.00 63.31  ? 681 LYS A CA  1 
ATOM 5105 C C   . LYS A 1 681 ? 10.228  -4.153  88.931  1.00 68.53  ? 681 LYS A C   1 
ATOM 5106 O O   . LYS A 1 681 ? 9.615   -3.764  87.932  1.00 76.12  ? 681 LYS A O   1 
ATOM 5107 C CB  . LYS A 1 681 ? 12.011  -2.422  89.209  1.00 65.08  ? 681 LYS A CB  1 
ATOM 5108 C CG  . LYS A 1 681 ? 13.420  -2.102  89.664  1.00 69.79  ? 681 LYS A CG  1 
ATOM 5109 C CD  . LYS A 1 681 ? 13.523  -0.663  90.130  1.00 70.00  ? 681 LYS A CD  1 
ATOM 5110 C CE  . LYS A 1 681 ? 14.802  -0.422  90.908  1.00 70.72  ? 681 LYS A CE  1 
ATOM 5111 N NZ  . LYS A 1 681 ? 14.606  0.589   91.982  1.00 74.63  ? 681 LYS A NZ  1 
ATOM 5112 N N   . ILE A 1 682 ? 9.644   -4.790  89.940  1.00 64.96  ? 682 ILE A N   1 
ATOM 5113 C CA  . ILE A 1 682 ? 8.216   -5.079  89.933  1.00 64.96  ? 682 ILE A CA  1 
ATOM 5114 C C   . ILE A 1 682 ? 7.457   -3.793  90.226  1.00 68.72  ? 682 ILE A C   1 
ATOM 5115 O O   . ILE A 1 682 ? 7.631   -3.185  91.286  1.00 70.64  ? 682 ILE A O   1 
ATOM 5116 C CB  . ILE A 1 682 ? 7.866   -6.172  90.952  1.00 60.84  ? 682 ILE A CB  1 
ATOM 5117 C CG1 . ILE A 1 682 ? 8.583   -7.476  90.603  1.00 60.59  ? 682 ILE A CG1 1 
ATOM 5118 C CG2 . ILE A 1 682 ? 6.369   -6.388  90.996  1.00 64.52  ? 682 ILE A CG2 1 
ATOM 5119 C CD1 . ILE A 1 682 ? 8.483   -8.528  91.680  1.00 62.49  ? 682 ILE A CD1 1 
ATOM 5120 N N   . LEU A 1 683 ? 6.612   -3.375  89.285  1.00 69.68  ? 683 LEU A N   1 
ATOM 5121 C CA  . LEU A 1 683 ? 5.822   -2.165  89.467  1.00 67.71  ? 683 LEU A CA  1 
ATOM 5122 C C   . LEU A 1 683 ? 4.491   -2.461  90.149  1.00 68.12  ? 683 LEU A C   1 
ATOM 5123 O O   . LEU A 1 683 ? 4.228   -1.965  91.247  1.00 76.07  ? 683 LEU A O   1 
ATOM 5124 C CB  . LEU A 1 683 ? 5.587   -1.485  88.115  1.00 68.02  ? 683 LEU A CB  1 
ATOM 5125 C CG  . LEU A 1 683 ? 6.847   -1.090  87.345  1.00 65.62  ? 683 LEU A CG  1 
ATOM 5126 C CD1 . LEU A 1 683 ? 6.485   -0.465  86.008  1.00 64.98  ? 683 LEU A CD1 1 
ATOM 5127 C CD2 . LEU A 1 683 ? 7.705   -0.147  88.169  1.00 62.89  ? 683 LEU A CD2 1 
ATOM 5128 N N   . LYS A 1 684 ? 3.652   -3.280  89.524  1.00 66.58  ? 684 LYS A N   1 
ATOM 5129 C CA  . LYS A 1 684 ? 2.404   -3.704  90.138  1.00 69.73  ? 684 LYS A CA  1 
ATOM 5130 C C   . LYS A 1 684 ? 2.316   -5.218  90.100  1.00 69.76  ? 684 LYS A C   1 
ATOM 5131 O O   . LYS A 1 684 ? 2.584   -5.833  89.065  1.00 76.83  ? 684 LYS A O   1 
ATOM 5132 C CB  . LYS A 1 684 ? 1.185   -3.091  89.442  1.00 70.14  ? 684 LYS A CB  1 
ATOM 5133 C CG  . LYS A 1 684 ? -0.120  -3.721  89.892  1.00 74.27  ? 684 LYS A CG  1 
ATOM 5134 C CD  . LYS A 1 684 ? -0.448  -3.339  91.324  1.00 70.51  ? 684 LYS A CD  1 
ATOM 5135 C CE  . LYS A 1 684 ? -1.646  -4.118  91.841  1.00 75.79  ? 684 LYS A CE  1 
ATOM 5136 N NZ  . LYS A 1 684 ? -1.421  -4.626  93.222  1.00 77.41  ? 684 LYS A NZ  1 
ATOM 5137 N N   . THR A 1 685 ? 1.947   -5.811  91.230  1.00 72.71  ? 685 THR A N   1 
ATOM 5138 C CA  . THR A 1 685 ? 1.738   -7.246  91.317  1.00 73.40  ? 685 THR A CA  1 
ATOM 5139 C C   . THR A 1 685 ? 0.586   -7.525  92.268  1.00 73.32  ? 685 THR A C   1 
ATOM 5140 O O   . THR A 1 685 ? 0.432   -6.845  93.286  1.00 81.36  ? 685 THR A O   1 
ATOM 5141 C CB  . THR A 1 685 ? 3.000   -7.971  91.796  1.00 75.30  ? 685 THR A CB  1 
ATOM 5142 O OG1 . THR A 1 685 ? 2.682   -9.334  92.094  1.00 80.80  ? 685 THR A OG1 1 
ATOM 5143 C CG2 . THR A 1 685 ? 3.551   -7.304  93.042  1.00 74.99  ? 685 THR A CG2 1 
ATOM 5144 N N   . THR A 1 686 ? -0.228  -8.515  91.921  1.00 73.00  ? 686 THR A N   1 
ATOM 5145 C CA  . THR A 1 686 ? -1.268  -8.995  92.817  1.00 77.69  ? 686 THR A CA  1 
ATOM 5146 C C   . THR A 1 686 ? -0.742  -10.000 93.831  1.00 76.94  ? 686 THR A C   1 
ATOM 5147 O O   . THR A 1 686 ? -1.482  -10.389 94.740  1.00 80.97  ? 686 THR A O   1 
ATOM 5148 C CB  . THR A 1 686 ? -2.411  -9.624  92.017  1.00 78.32  ? 686 THR A CB  1 
ATOM 5149 O OG1 . THR A 1 686 ? -1.866  -10.440 90.978  1.00 79.18  ? 686 THR A OG1 1 
ATOM 5150 C CG2 . THR A 1 686 ? -3.281  -8.545  91.396  1.00 72.31  ? 686 THR A CG2 1 
ATOM 5151 N N   . TYR A 1 687 ? 0.510   -10.426 93.691  1.00 72.83  ? 687 TYR A N   1 
ATOM 5152 C CA  . TYR A 1 687 ? 1.135   -11.320 94.649  1.00 73.73  ? 687 TYR A CA  1 
ATOM 5153 C C   . TYR A 1 687 ? 1.364   -10.612 95.977  1.00 80.20  ? 687 TYR A C   1 
ATOM 5154 O O   . TYR A 1 687 ? 1.578   -9.398  96.032  1.00 81.41  ? 687 TYR A O   1 
ATOM 5155 C CB  . TYR A 1 687 ? 2.470   -11.831 94.110  1.00 73.25  ? 687 TYR A CB  1 
ATOM 5156 C CG  . TYR A 1 687 ? 2.348   -12.919 93.072  1.00 75.56  ? 687 TYR A CG  1 
ATOM 5157 C CD1 . TYR A 1 687 ? 1.581   -14.048 93.311  1.00 75.98  ? 687 TYR A CD1 1 
ATOM 5158 C CD2 . TYR A 1 687 ? 2.994   -12.812 91.848  1.00 77.28  ? 687 TYR A CD2 1 
ATOM 5159 C CE1 . TYR A 1 687 ? 1.469   -15.044 92.367  1.00 77.94  ? 687 TYR A CE1 1 
ATOM 5160 C CE2 . TYR A 1 687 ? 2.885   -13.802 90.896  1.00 74.48  ? 687 TYR A CE2 1 
ATOM 5161 C CZ  . TYR A 1 687 ? 2.121   -14.916 91.161  1.00 73.48  ? 687 TYR A CZ  1 
ATOM 5162 O OH  . TYR A 1 687 ? 2.006   -15.907 90.217  1.00 75.06  ? 687 TYR A OH  1 
ATOM 5163 N N   . ALA A 1 688 ? 1.319   -11.388 97.055  1.00 86.25  ? 688 ALA A N   1 
ATOM 5164 C CA  . ALA A 1 688 ? 1.707   -10.876 98.356  1.00 82.31  ? 688 ALA A CA  1 
ATOM 5165 C C   . ALA A 1 688 ? 3.218   -10.670 98.400  1.00 83.90  ? 688 ALA A C   1 
ATOM 5166 O O   . ALA A 1 688 ? 3.969   -11.185 97.567  1.00 87.30  ? 688 ALA A O   1 
ATOM 5167 C CB  . ALA A 1 688 ? 1.259   -11.827 99.464  1.00 81.56  ? 688 ALA A CB  1 
ATOM 5168 N N   . THR A 1 689 ? 3.667   -9.893  99.389  1.00 89.57  ? 689 THR A N   1 
ATOM 5169 C CA  . THR A 1 689 ? 5.090   -9.604  99.516  1.00 91.19  ? 689 THR A CA  1 
ATOM 5170 C C   . THR A 1 689 ? 5.923   -10.868 99.687  1.00 91.25  ? 689 THR A C   1 
ATOM 5171 O O   . THR A 1 689 ? 7.055   -10.923 99.196  1.00 89.08  ? 689 THR A O   1 
ATOM 5172 C CB  . THR A 1 689 ? 5.334   -8.657  100.692 1.00 92.98  ? 689 THR A CB  1 
ATOM 5173 O OG1 . THR A 1 689 ? 4.363   -7.604  100.665 1.00 93.63  ? 689 THR A OG1 1 
ATOM 5174 C CG2 . THR A 1 689 ? 6.726   -8.050  100.607 1.00 90.60  ? 689 THR A CG2 1 
ATOM 5175 N N   . GLY A 1 690 ? 5.388   -11.883 100.358 1.00 91.70  ? 690 GLY A N   1 
ATOM 5176 C CA  . GLY A 1 690 ? 6.093   -13.139 100.507 1.00 90.28  ? 690 GLY A CA  1 
ATOM 5177 C C   . GLY A 1 690 ? 5.948   -14.036 99.296  1.00 90.55  ? 690 GLY A C   1 
ATOM 5178 O O   . GLY A 1 690 ? 6.615   -15.069 99.196  1.00 91.65  ? 690 GLY A O   1 
ATOM 5179 N N   . ASN A 1 691 ? 5.073   -13.650 98.367  1.00 90.96  ? 691 ASN A N   1 
ATOM 5180 C CA  . ASN A 1 691 ? 4.861   -14.396 97.138  1.00 89.21  ? 691 ASN A CA  1 
ATOM 5181 C C   . ASN A 1 691 ? 5.408   -13.692 95.904  1.00 87.67  ? 691 ASN A C   1 
ATOM 5182 O O   . ASN A 1 691 ? 5.466   -14.310 94.836  1.00 86.65  ? 691 ASN A O   1 
ATOM 5183 C CB  . ASN A 1 691 ? 3.366   -14.678 96.936  1.00 88.57  ? 691 ASN A CB  1 
ATOM 5184 C CG  . ASN A 1 691 ? 2.812   -15.635 97.969  1.00 90.14  ? 691 ASN A CG  1 
ATOM 5185 O OD1 . ASN A 1 691 ? 3.485   -16.579 98.380  1.00 89.24  ? 691 ASN A OD1 1 
ATOM 5186 N ND2 . ASN A 1 691 ? 1.580   -15.394 98.397  1.00 90.65  ? 691 ASN A ND2 1 
ATOM 5187 N N   . GLN A 1 692 ? 5.803   -12.426 96.020  1.00 87.54  ? 692 GLN A N   1 
ATOM 5188 C CA  . GLN A 1 692 ? 6.408   -11.686 94.922  1.00 80.28  ? 692 GLN A CA  1 
ATOM 5189 C C   . GLN A 1 692 ? 7.718   -12.348 94.526  1.00 85.61  ? 692 GLN A C   1 
ATOM 5190 O O   . GLN A 1 692 ? 8.453   -12.827 95.399  1.00 90.38  ? 692 GLN A O   1 
ATOM 5191 C CB  . GLN A 1 692 ? 6.663   -10.233 95.321  1.00 81.50  ? 692 GLN A CB  1 
ATOM 5192 C CG  . GLN A 1 692 ? 5.440   -9.348  95.308  1.00 88.32  ? 692 GLN A CG  1 
ATOM 5193 C CD  . GLN A 1 692 ? 5.771   -7.910  95.650  1.00 90.99  ? 692 GLN A CD  1 
ATOM 5194 O OE1 . GLN A 1 692 ? 6.873   -7.434  95.377  1.00 87.70  ? 692 GLN A OE1 1 
ATOM 5195 N NE2 . GLN A 1 692 ? 4.818   -7.208  96.251  1.00 87.75  ? 692 GLN A NE2 1 
ATOM 5196 N N   . PRO A 1 693 ? 8.043   -12.411 93.238  1.00 78.90  ? 693 PRO A N   1 
ATOM 5197 C CA  . PRO A 1 693 ? 9.361   -12.918 92.845  1.00 77.91  ? 693 PRO A CA  1 
ATOM 5198 C C   . PRO A 1 693 ? 10.469  -12.077 93.457  1.00 78.55  ? 693 PRO A C   1 
ATOM 5199 O O   . PRO A 1 693 ? 10.413  -10.845 93.474  1.00 82.76  ? 693 PRO A O   1 
ATOM 5200 C CB  . PRO A 1 693 ? 9.364   -12.810 91.315  1.00 71.32  ? 693 PRO A CB  1 
ATOM 5201 C CG  . PRO A 1 693 ? 8.016   -12.369 90.906  1.00 73.80  ? 693 PRO A CG  1 
ATOM 5202 C CD  . PRO A 1 693 ? 7.184   -12.056 92.097  1.00 76.61  ? 693 PRO A CD  1 
ATOM 5203 N N   . THR A 1 694 ? 11.487  -12.765 93.973  1.00 76.58  ? 694 THR A N   1 
ATOM 5204 C CA  . THR A 1 694 ? 12.587  -12.088 94.647  1.00 76.64  ? 694 THR A CA  1 
ATOM 5205 C C   . THR A 1 694 ? 13.448  -11.273 93.697  1.00 77.43  ? 694 THR A C   1 
ATOM 5206 O O   . THR A 1 694 ? 13.816  -10.139 94.025  1.00 81.62  ? 694 THR A O   1 
ATOM 5207 C CB  . THR A 1 694 ? 13.468  -13.105 95.377  1.00 78.83  ? 694 THR A CB  1 
ATOM 5208 O OG1 . THR A 1 694 ? 13.844  -14.151 94.473  1.00 80.14  ? 694 THR A OG1 1 
ATOM 5209 C CG2 . THR A 1 694 ? 12.721  -13.703 96.552  1.00 78.84  ? 694 THR A CG2 1 
ATOM 5210 N N   . ALA A 1 695 ? 13.777  -11.819 92.529  1.00 76.22  ? 695 ALA A N   1 
ATOM 5211 C CA  . ALA A 1 695 ? 14.613  -11.130 91.557  1.00 75.11  ? 695 ALA A CA  1 
ATOM 5212 C C   . ALA A 1 695 ? 14.173  -11.538 90.162  1.00 80.19  ? 695 ALA A C   1 
ATOM 5213 O O   . ALA A 1 695 ? 14.068  -12.733 89.868  1.00 81.00  ? 695 ALA A O   1 
ATOM 5214 C CB  . ALA A 1 695 ? 16.094  -11.453 91.769  1.00 72.53  ? 695 ALA A CB  1 
ATOM 5215 N N   . ILE A 1 696 ? 13.913  -10.551 89.312  1.00 71.97  ? 696 ILE A N   1 
ATOM 5216 C CA  . ILE A 1 696 ? 13.566  -10.779 87.915  1.00 68.43  ? 696 ILE A CA  1 
ATOM 5217 C C   . ILE A 1 696 ? 14.678  -10.184 87.067  1.00 68.24  ? 696 ILE A C   1 
ATOM 5218 O O   . ILE A 1 696 ? 14.955  -8.981  87.146  1.00 68.51  ? 696 ILE A O   1 
ATOM 5219 C CB  . ILE A 1 696 ? 12.200  -10.174 87.565  1.00 68.09  ? 696 ILE A CB  1 
ATOM 5220 C CG1 . ILE A 1 696 ? 11.108  -10.869 88.378  1.00 69.74  ? 696 ILE A CG1 1 
ATOM 5221 C CG2 . ILE A 1 696 ? 11.929  -10.296 86.076  1.00 63.99  ? 696 ILE A CG2 1 
ATOM 5222 C CD1 . ILE A 1 696 ? 9.745   -10.265 88.221  1.00 66.29  ? 696 ILE A CD1 1 
ATOM 5223 N N   . THR A 1 697 ? 15.315  -11.026 86.262  1.00 69.72  ? 697 THR A N   1 
ATOM 5224 C CA  . THR A 1 697 ? 16.511  -10.661 85.516  1.00 67.17  ? 697 THR A CA  1 
ATOM 5225 C C   . THR A 1 697 ? 16.249  -10.791 84.025  1.00 65.29  ? 697 THR A C   1 
ATOM 5226 O O   . THR A 1 697 ? 15.832  -11.854 83.555  1.00 69.41  ? 697 THR A O   1 
ATOM 5227 C CB  . THR A 1 697 ? 17.691  -11.548 85.922  1.00 73.00  ? 697 THR A CB  1 
ATOM 5228 O OG1 . THR A 1 697 ? 17.852  -11.514 87.345  1.00 71.19  ? 697 THR A OG1 1 
ATOM 5229 C CG2 . THR A 1 697 ? 18.965  -11.084 85.254  1.00 68.25  ? 697 THR A CG2 1 
ATOM 5230 N N   . ALA A 1 698 ? 16.500  -9.714  83.286  1.00 57.17  ? 698 ALA A N   1 
ATOM 5231 C CA  . ALA A 1 698 ? 16.417  -9.709  81.830  1.00 59.63  ? 698 ALA A CA  1 
ATOM 5232 C C   . ALA A 1 698 ? 17.832  -9.585  81.284  1.00 62.33  ? 698 ALA A C   1 
ATOM 5233 O O   . ALA A 1 698 ? 18.472  -8.541  81.435  1.00 64.30  ? 698 ALA A O   1 
ATOM 5234 C CB  . ALA A 1 698 ? 15.530  -8.571  81.332  1.00 59.03  ? 698 ALA A CB  1 
ATOM 5235 N N   . THR A 1 699 ? 18.319  -10.647 80.653  1.00 61.40  ? 699 THR A N   1 
ATOM 5236 C CA  . THR A 1 699 ? 19.678  -10.678 80.136  1.00 59.43  ? 699 THR A CA  1 
ATOM 5237 C C   . THR A 1 699 ? 19.658  -10.585 78.617  1.00 60.68  ? 699 THR A C   1 
ATOM 5238 O O   . THR A 1 699 ? 19.046  -11.420 77.945  1.00 63.28  ? 699 THR A O   1 
ATOM 5239 C CB  . THR A 1 699 ? 20.394  -11.954 80.578  1.00 59.14  ? 699 THR A CB  1 
ATOM 5240 O OG1 . THR A 1 699 ? 20.301  -12.084 82.001  1.00 68.40  ? 699 THR A OG1 1 
ATOM 5241 C CG2 . THR A 1 699 ? 21.853  -11.904 80.181  1.00 62.02  ? 699 THR A CG2 1 
ATOM 5242 N N   . ALA A 1 700 ? 20.329  -9.568  78.082  1.00 56.73  ? 700 ALA A N   1 
ATOM 5243 C CA  . ALA A 1 700 ? 20.419  -9.392  76.641  1.00 53.49  ? 700 ALA A CA  1 
ATOM 5244 C C   . ALA A 1 700 ? 21.283  -10.493 76.040  1.00 60.84  ? 700 ALA A C   1 
ATOM 5245 O O   . ALA A 1 700 ? 22.365  -10.793 76.553  1.00 68.61  ? 700 ALA A O   1 
ATOM 5246 C CB  . ALA A 1 700 ? 20.994  -8.018  76.306  1.00 52.57  ? 700 ALA A CB  1 
ATOM 5247 N N   . ALA A 1 701 ? 20.806  -11.093 74.953  1.00 56.36  ? 701 ALA A N   1 
ATOM 5248 C CA  . ALA A 1 701 ? 21.491  -12.226 74.353  1.00 50.71  ? 701 ALA A CA  1 
ATOM 5249 C C   . ALA A 1 701 ? 21.127  -12.316 72.879  1.00 57.52  ? 701 ALA A C   1 
ATOM 5250 O O   . ALA A 1 701 ? 20.168  -11.698 72.412  1.00 65.38  ? 701 ALA A O   1 
ATOM 5251 C CB  . ALA A 1 701 ? 21.144  -13.531 75.075  1.00 50.40  ? 701 ALA A CB  1 
ATOM 5252 N N   . HIS A 1 702 ? 21.918  -13.094 72.147  1.00 56.55  ? 702 HIS A N   1 
ATOM 5253 C CA  . HIS A 1 702 ? 21.654  -13.409 70.752  1.00 54.20  ? 702 HIS A CA  1 
ATOM 5254 C C   . HIS A 1 702 ? 21.341  -14.891 70.615  1.00 56.12  ? 702 HIS A C   1 
ATOM 5255 O O   . HIS A 1 702 ? 22.004  -15.730 71.230  1.00 59.42  ? 702 HIS A O   1 
ATOM 5256 C CB  . HIS A 1 702 ? 22.851  -13.066 69.858  1.00 53.12  ? 702 HIS A CB  1 
ATOM 5257 C CG  . HIS A 1 702 ? 23.213  -11.615 69.848  1.00 52.55  ? 702 HIS A CG  1 
ATOM 5258 N ND1 . HIS A 1 702 ? 24.240  -11.100 70.609  1.00 63.53  ? 702 HIS A ND1 1 
ATOM 5259 C CD2 . HIS A 1 702 ? 22.695  -10.571 69.161  1.00 52.26  ? 702 HIS A CD2 1 
ATOM 5260 C CE1 . HIS A 1 702 ? 24.335  -9.800  70.394  1.00 60.31  ? 702 HIS A CE1 1 
ATOM 5261 N NE2 . HIS A 1 702 ? 23.408  -9.455  69.519  1.00 61.17  ? 702 HIS A NE2 1 
ATOM 5262 N N   . TYR A 1 703 ? 20.330  -15.209 69.812  1.00 56.74  ? 703 TYR A N   1 
ATOM 5263 C CA  . TYR A 1 703 ? 20.081  -16.601 69.470  1.00 55.35  ? 703 TYR A CA  1 
ATOM 5264 C C   . TYR A 1 703 ? 21.228  -17.145 68.630  1.00 58.44  ? 703 TYR A C   1 
ATOM 5265 O O   . TYR A 1 703 ? 21.803  -16.436 67.801  1.00 64.22  ? 703 TYR A O   1 
ATOM 5266 C CB  . TYR A 1 703 ? 18.771  -16.757 68.700  1.00 56.80  ? 703 TYR A CB  1 
ATOM 5267 C CG  . TYR A 1 703 ? 17.537  -16.864 69.561  1.00 59.21  ? 703 TYR A CG  1 
ATOM 5268 C CD1 . TYR A 1 703 ? 17.528  -17.658 70.697  1.00 60.37  ? 703 TYR A CD1 1 
ATOM 5269 C CD2 . TYR A 1 703 ? 16.365  -16.215 69.208  1.00 55.38  ? 703 TYR A CD2 1 
ATOM 5270 C CE1 . TYR A 1 703 ? 16.400  -17.769 71.480  1.00 65.23  ? 703 TYR A CE1 1 
ATOM 5271 C CE2 . TYR A 1 703 ? 15.230  -16.323 69.983  1.00 58.00  ? 703 TYR A CE2 1 
ATOM 5272 C CZ  . TYR A 1 703 ? 15.253  -17.100 71.118  1.00 65.25  ? 703 TYR A CZ  1 
ATOM 5273 O OH  . TYR A 1 703 ? 14.122  -17.211 71.893  1.00 68.03  ? 703 TYR A OH  1 
ATOM 5274 N N   . SER A 1 704 ? 21.563  -18.409 68.851  1.00 57.60  ? 704 SER A N   1 
ATOM 5275 C CA  . SER A 1 704 ? 22.509  -19.088 67.985  1.00 52.65  ? 704 SER A CA  1 
ATOM 5276 C C   . SER A 1 704 ? 21.804  -19.564 66.722  1.00 59.49  ? 704 SER A C   1 
ATOM 5277 O O   . SER A 1 704 ? 20.577  -19.674 66.673  1.00 70.25  ? 704 SER A O   1 
ATOM 5278 C CB  . SER A 1 704 ? 23.152  -20.271 68.705  1.00 58.64  ? 704 SER A CB  1 
ATOM 5279 O OG  . SER A 1 704 ? 23.496  -19.931 70.035  1.00 70.71  ? 704 SER A OG  1 
ATOM 5280 N N   . MET A 1 705 ? 22.594  -19.834 65.690  1.00 61.19  ? 705 MET A N   1 
ATOM 5281 C CA  . MET A 1 705 ? 22.064  -20.359 64.443  1.00 59.17  ? 705 MET A CA  1 
ATOM 5282 C C   . MET A 1 705 ? 22.325  -21.856 64.360  1.00 66.09  ? 705 MET A C   1 
ATOM 5283 O O   . MET A 1 705 ? 23.398  -22.334 64.737  1.00 71.26  ? 705 MET A O   1 
ATOM 5284 C CB  . MET A 1 705 ? 22.688  -19.645 63.245  1.00 56.50  ? 705 MET A CB  1 
ATOM 5285 C CG  . MET A 1 705 ? 22.423  -18.151 63.212  1.00 60.23  ? 705 MET A CG  1 
ATOM 5286 S SD  . MET A 1 705 ? 20.832  -17.730 62.478  1.00 71.15  ? 705 MET A SD  1 
ATOM 5287 C CE  . MET A 1 705 ? 20.797  -18.845 61.080  1.00 68.33  ? 705 MET A CE  1 
ATOM 5288 N N   . LYS A 1 706 ? 21.332  -22.590 63.871  1.00 68.57  ? 706 LYS A N   1 
ATOM 5289 C CA  . LYS A 1 706 ? 21.409  -24.036 63.748  1.00 66.08  ? 706 LYS A CA  1 
ATOM 5290 C C   . LYS A 1 706 ? 21.091  -24.435 62.315  1.00 66.82  ? 706 LYS A C   1 
ATOM 5291 O O   . LYS A 1 706 ? 20.441  -23.700 61.569  1.00 74.32  ? 706 LYS A O   1 
ATOM 5292 C CB  . LYS A 1 706 ? 20.452  -24.732 64.725  1.00 62.75  ? 706 LYS A CB  1 
ATOM 5293 C CG  . LYS A 1 706 ? 18.995  -24.668 64.313  1.00 62.49  ? 706 LYS A CG  1 
ATOM 5294 C CD  . LYS A 1 706 ? 18.094  -25.224 65.398  1.00 67.93  ? 706 LYS A CD  1 
ATOM 5295 C CE  . LYS A 1 706 ? 16.664  -25.357 64.913  1.00 66.80  ? 706 LYS A CE  1 
ATOM 5296 N NZ  . LYS A 1 706 ? 15.937  -26.438 65.629  1.00 70.78  ? 706 LYS A NZ  1 
ATOM 5297 N N   . ASP A 1 707 ? 21.569  -25.613 61.930  1.00 66.28  ? 707 ASP A N   1 
ATOM 5298 C CA  . ASP A 1 707 ? 21.357  -26.133 60.587  1.00 67.41  ? 707 ASP A CA  1 
ATOM 5299 C C   . ASP A 1 707 ? 20.114  -27.014 60.571  1.00 71.56  ? 707 ASP A C   1 
ATOM 5300 O O   . ASP A 1 707 ? 20.093  -28.077 61.200  1.00 72.03  ? 707 ASP A O   1 
ATOM 5301 C CB  . ASP A 1 707 ? 22.576  -26.927 60.116  1.00 66.51  ? 707 ASP A CB  1 
ATOM 5302 C CG  . ASP A 1 707 ? 23.836  -26.090 60.075  1.00 76.80  ? 707 ASP A CG  1 
ATOM 5303 O OD1 . ASP A 1 707 ? 23.727  -24.854 59.944  1.00 81.62  ? 707 ASP A OD1 1 
ATOM 5304 O OD2 . ASP A 1 707 ? 24.939  -26.668 60.175  1.00 75.60  ? 707 ASP A OD2 1 
ATOM 5305 N N   . LEU A 1 708 ? 19.078  -26.566 59.860  1.00 61.62  ? 708 LEU A N   1 
ATOM 5306 C CA  . LEU A 1 708 ? 17.930  -27.431 59.615  1.00 57.89  ? 708 LEU A CA  1 
ATOM 5307 C C   . LEU A 1 708 ? 18.313  -28.611 58.735  1.00 58.66  ? 708 LEU A C   1 
ATOM 5308 O O   . LEU A 1 708 ? 17.856  -29.736 58.959  1.00 66.30  ? 708 LEU A O   1 
ATOM 5309 C CB  . LEU A 1 708 ? 16.796  -26.640 58.965  1.00 50.56  ? 708 LEU A CB  1 
ATOM 5310 C CG  . LEU A 1 708 ? 16.084  -25.609 59.834  1.00 56.60  ? 708 LEU A CG  1 
ATOM 5311 C CD1 . LEU A 1 708 ? 15.002  -24.914 59.033  1.00 59.80  ? 708 LEU A CD1 1 
ATOM 5312 C CD2 . LEU A 1 708 ? 15.503  -26.264 61.074  1.00 61.12  ? 708 LEU A CD2 1 
ATOM 5313 N N   . LYS A 1 709 ? 19.150  -28.366 57.731  1.00 54.66  ? 709 LYS A N   1 
ATOM 5314 C CA  . LYS A 1 709 ? 19.599  -29.414 56.821  1.00 57.51  ? 709 LYS A CA  1 
ATOM 5315 C C   . LYS A 1 709 ? 20.967  -29.009 56.296  1.00 56.51  ? 709 LYS A C   1 
ATOM 5316 O O   . LYS A 1 709 ? 21.068  -28.096 55.472  1.00 64.55  ? 709 LYS A O   1 
ATOM 5317 C CB  . LYS A 1 709 ? 18.606  -29.616 55.681  1.00 55.76  ? 709 LYS A CB  1 
ATOM 5318 C CG  . LYS A 1 709 ? 18.594  -31.020 55.109  1.00 58.40  ? 709 LYS A CG  1 
ATOM 5319 C CD  . LYS A 1 709 ? 18.486  -32.067 56.198  1.00 59.05  ? 709 LYS A CD  1 
ATOM 5320 C CE  . LYS A 1 709 ? 18.179  -33.428 55.609  1.00 56.79  ? 709 LYS A CE  1 
ATOM 5321 N NZ  . LYS A 1 709 ? 18.300  -34.509 56.621  1.00 64.22  ? 709 LYS A NZ  1 
ATOM 5322 N N   . VAL A 1 710 ? 22.016  -29.676 56.783  1.00 60.39  ? 710 VAL A N   1 
ATOM 5323 C CA  . VAL A 1 710 ? 23.358  -29.409 56.284  1.00 56.28  ? 710 VAL A CA  1 
ATOM 5324 C C   . VAL A 1 710 ? 23.451  -29.808 54.815  1.00 53.35  ? 710 VAL A C   1 
ATOM 5325 O O   . VAL A 1 710 ? 22.830  -30.773 54.359  1.00 62.16  ? 710 VAL A O   1 
ATOM 5326 C CB  . VAL A 1 710 ? 24.409  -30.146 57.129  1.00 56.54  ? 710 VAL A CB  1 
ATOM 5327 C CG1 . VAL A 1 710 ? 25.805  -29.647 56.806  1.00 59.44  ? 710 VAL A CG1 1 
ATOM 5328 C CG2 . VAL A 1 710 ? 24.112  -29.974 58.608  1.00 56.22  ? 710 VAL A CG2 1 
ATOM 5329 N N   . ALA A 1 711 ? 24.231  -29.037 54.061  1.00 54.80  ? 711 ALA A N   1 
ATOM 5330 C CA  . ALA A 1 711 ? 24.413  -29.315 52.642  1.00 57.45  ? 711 ALA A CA  1 
ATOM 5331 C C   . ALA A 1 711 ? 24.995  -30.707 52.449  1.00 63.44  ? 711 ALA A C   1 
ATOM 5332 O O   . ALA A 1 711 ? 26.033  -31.042 53.028  1.00 68.04  ? 711 ALA A O   1 
ATOM 5333 C CB  . ALA A 1 711 ? 25.322  -28.261 52.013  1.00 56.29  ? 711 ALA A CB  1 
ATOM 5334 N N   . GLY A 1 712 ? 24.323  -31.517 51.635  1.00 58.04  ? 712 GLY A N   1 
ATOM 5335 C CA  . GLY A 1 712 ? 24.739  -32.880 51.393  1.00 53.40  ? 712 GLY A CA  1 
ATOM 5336 C C   . GLY A 1 712 ? 24.287  -33.887 52.427  1.00 62.01  ? 712 GLY A C   1 
ATOM 5337 O O   . GLY A 1 712 ? 24.775  -35.023 52.410  1.00 70.99  ? 712 GLY A O   1 
ATOM 5338 N N   . ALA A 1 713 ? 23.378  -33.509 53.332  1.00 60.55  ? 713 ALA A N   1 
ATOM 5339 C CA  . ALA A 1 713 ? 22.931  -34.435 54.366  1.00 58.90  ? 713 ALA A CA  1 
ATOM 5340 C C   . ALA A 1 713 ? 22.186  -35.628 53.781  1.00 64.32  ? 713 ALA A C   1 
ATOM 5341 O O   . ALA A 1 713 ? 22.405  -36.765 54.214  1.00 66.19  ? 713 ALA A O   1 
ATOM 5342 C CB  . ALA A 1 713 ? 22.048  -33.709 55.379  1.00 58.65  ? 713 ALA A CB  1 
ATOM 5343 N N   . ASN A 1 714 ? 21.308  -35.397 52.807  1.00 66.86  ? 714 ASN A N   1 
ATOM 5344 C CA  . ASN A 1 714 ? 20.533  -36.469 52.202  1.00 64.72  ? 714 ASN A CA  1 
ATOM 5345 C C   . ASN A 1 714 ? 21.295  -37.220 51.121  1.00 68.31  ? 714 ASN A C   1 
ATOM 5346 O O   . ASN A 1 714 ? 20.788  -38.225 50.612  1.00 74.12  ? 714 ASN A O   1 
ATOM 5347 C CB  . ASN A 1 714 ? 19.234  -35.915 51.609  1.00 63.37  ? 714 ASN A CB  1 
ATOM 5348 C CG  . ASN A 1 714 ? 18.226  -35.534 52.672  1.00 68.47  ? 714 ASN A CG  1 
ATOM 5349 O OD1 . ASN A 1 714 ? 18.152  -36.162 53.726  1.00 75.19  ? 714 ASN A OD1 1 
ATOM 5350 N ND2 . ASN A 1 714 ? 17.437  -34.506 52.396  1.00 71.04  ? 714 ASN A ND2 1 
ATOM 5351 N N   . GLY A 1 715 ? 22.489  -36.763 50.763  1.00 67.51  ? 715 GLY A N   1 
ATOM 5352 C CA  . GLY A 1 715 ? 23.272  -37.386 49.726  1.00 64.16  ? 715 GLY A CA  1 
ATOM 5353 C C   . GLY A 1 715 ? 24.099  -36.357 48.988  1.00 68.41  ? 715 GLY A C   1 
ATOM 5354 O O   . GLY A 1 715 ? 24.181  -35.195 49.394  1.00 74.66  ? 715 GLY A O   1 
ATOM 5355 N N   . PRO A 1 716 ? 24.737  -36.766 47.890  1.00 72.58  ? 716 PRO A N   1 
ATOM 5356 C CA  . PRO A 1 716 ? 25.558  -35.822 47.116  1.00 65.66  ? 716 PRO A CA  1 
ATOM 5357 C C   . PRO A 1 716 ? 24.737  -34.623 46.657  1.00 63.79  ? 716 PRO A C   1 
ATOM 5358 O O   . PRO A 1 716 ? 23.790  -34.764 45.880  1.00 68.26  ? 716 PRO A O   1 
ATOM 5359 C CB  . PRO A 1 716 ? 26.041  -36.656 45.923  1.00 65.57  ? 716 PRO A CB  1 
ATOM 5360 C CG  . PRO A 1 716 ? 25.889  -38.072 46.333  1.00 68.69  ? 716 PRO A CG  1 
ATOM 5361 C CD  . PRO A 1 716 ? 24.854  -38.153 47.412  1.00 70.54  ? 716 PRO A CD  1 
ATOM 5362 N N   . ASN A 1 717 ? 25.100  -33.446 47.168  1.00 65.94  ? 717 ASN A N   1 
ATOM 5363 C CA  . ASN A 1 717 ? 24.508  -32.170 46.772  1.00 67.93  ? 717 ASN A CA  1 
ATOM 5364 C C   . ASN A 1 717 ? 23.029  -32.073 47.125  1.00 66.38  ? 717 ASN A C   1 
ATOM 5365 O O   . ASN A 1 717 ? 22.310  -31.241 46.562  1.00 65.21  ? 717 ASN A O   1 
ATOM 5366 C CB  . ASN A 1 717 ? 24.705  -31.932 45.273  1.00 63.62  ? 717 ASN A CB  1 
ATOM 5367 C CG  . ASN A 1 717 ? 26.144  -31.634 44.915  1.00 68.72  ? 717 ASN A CG  1 
ATOM 5368 O OD1 . ASN A 1 717 ? 26.906  -31.123 45.732  1.00 75.89  ? 717 ASN A OD1 1 
ATOM 5369 N ND2 . ASN A 1 717 ? 26.525  -31.959 43.685  1.00 72.07  ? 717 ASN A ND2 1 
ATOM 5370 N N   . MET A 1 718 ? 22.559  -32.915 48.041  1.00 63.86  ? 718 MET A N   1 
ATOM 5371 C CA  . MET A 1 718 ? 21.184  -32.817 48.513  1.00 59.87  ? 718 MET A CA  1 
ATOM 5372 C C   . MET A 1 718 ? 21.161  -32.565 50.015  1.00 63.80  ? 718 MET A C   1 
ATOM 5373 O O   . MET A 1 718 ? 21.408  -33.489 50.800  1.00 69.35  ? 718 MET A O   1 
ATOM 5374 C CB  . MET A 1 718 ? 20.392  -34.081 48.173  1.00 65.50  ? 718 MET A CB  1 
ATOM 5375 C CG  . MET A 1 718 ? 19.996  -34.192 46.710  1.00 64.36  ? 718 MET A CG  1 
ATOM 5376 S SD  . MET A 1 718 ? 19.678  -35.884 46.176  1.00 79.29  ? 718 MET A SD  1 
ATOM 5377 C CE  . MET A 1 718 ? 20.784  -36.800 47.238  1.00 65.69  ? 718 MET A CE  1 
ATOM 5378 N N   . PRO A 1 719 ? 20.871  -31.336 50.459  1.00 58.30  ? 719 PRO A N   1 
ATOM 5379 C CA  . PRO A 1 719 ? 20.564  -30.137 49.666  1.00 50.46  ? 719 PRO A CA  1 
ATOM 5380 C C   . PRO A 1 719 ? 21.807  -29.499 49.065  1.00 57.81  ? 719 PRO A C   1 
ATOM 5381 O O   . PRO A 1 719 ? 22.928  -29.803 49.461  1.00 66.90  ? 719 PRO A O   1 
ATOM 5382 C CB  . PRO A 1 719 ? 19.897  -29.195 50.683  1.00 50.36  ? 719 PRO A CB  1 
ATOM 5383 C CG  . PRO A 1 719 ? 19.879  -29.907 52.009  1.00 50.43  ? 719 PRO A CG  1 
ATOM 5384 C CD  . PRO A 1 719 ? 20.817  -31.066 51.902  1.00 55.14  ? 719 PRO A CD  1 
ATOM 5385 N N   . LEU A 1 720 ? 21.621  -28.606 48.091  1.00 56.67  ? 720 LEU A N   1 
ATOM 5386 C CA  . LEU A 1 720 ? 22.752  -27.900 47.499  1.00 56.31  ? 720 LEU A CA  1 
ATOM 5387 C C   . LEU A 1 720 ? 23.476  -27.056 48.540  1.00 59.67  ? 720 LEU A C   1 
ATOM 5388 O O   . LEU A 1 720 ? 24.711  -27.050 48.606  1.00 60.86  ? 720 LEU A O   1 
ATOM 5389 C CB  . LEU A 1 720 ? 22.271  -27.020 46.349  1.00 51.48  ? 720 LEU A CB  1 
ATOM 5390 C CG  . LEU A 1 720 ? 23.355  -26.167 45.692  1.00 56.60  ? 720 LEU A CG  1 
ATOM 5391 C CD1 . LEU A 1 720 ? 24.257  -27.020 44.814  1.00 57.97  ? 720 LEU A CD1 1 
ATOM 5392 C CD2 . LEU A 1 720 ? 22.742  -25.019 44.916  1.00 60.18  ? 720 LEU A CD2 1 
ATOM 5393 N N   . GLU A 1 721 ? 22.721  -26.339 49.363  1.00 66.74  ? 721 GLU A N   1 
ATOM 5394 C CA  . GLU A 1 721 ? 23.265  -25.451 50.376  1.00 56.73  ? 721 GLU A CA  1 
ATOM 5395 C C   . GLU A 1 721 ? 22.688  -25.810 51.736  1.00 57.87  ? 721 GLU A C   1 
ATOM 5396 O O   . GLU A 1 721 ? 21.643  -26.458 51.846  1.00 65.54  ? 721 GLU A O   1 
ATOM 5397 C CB  . GLU A 1 721 ? 22.963  -23.985 50.044  1.00 54.77  ? 721 GLU A CB  1 
ATOM 5398 C CG  . GLU A 1 721 ? 23.600  -23.493 48.763  1.00 64.48  ? 721 GLU A CG  1 
ATOM 5399 C CD  . GLU A 1 721 ? 23.353  -22.019 48.523  1.00 73.25  ? 721 GLU A CD  1 
ATOM 5400 O OE1 . GLU A 1 721 ? 22.598  -21.407 49.308  1.00 67.81  ? 721 GLU A OE1 1 
ATOM 5401 O OE2 . GLU A 1 721 ? 23.917  -21.472 47.553  1.00 73.25  ? 721 GLU A OE2 1 
ATOM 5402 N N   . THR A 1 722 ? 23.385  -25.380 52.782  1.00 58.08  ? 722 THR A N   1 
ATOM 5403 C CA  . THR A 1 722 ? 22.915  -25.593 54.141  1.00 55.13  ? 722 THR A CA  1 
ATOM 5404 C C   . THR A 1 722 ? 21.679  -24.743 54.399  1.00 59.38  ? 722 THR A C   1 
ATOM 5405 O O   . THR A 1 722 ? 21.690  -23.531 54.169  1.00 68.66  ? 722 THR A O   1 
ATOM 5406 C CB  . THR A 1 722 ? 24.010  -25.248 55.149  1.00 59.03  ? 722 THR A CB  1 
ATOM 5407 O OG1 . THR A 1 722 ? 25.189  -26.007 54.855  1.00 70.20  ? 722 THR A OG1 1 
ATOM 5408 C CG2 . THR A 1 722 ? 23.550  -25.563 56.559  1.00 60.73  ? 722 THR A CG2 1 
ATOM 5409 N N   . ILE A 1 723 ? 20.615  -25.381 54.872  1.00 54.23  ? 723 ILE A N   1 
ATOM 5410 C CA  . ILE A 1 723 ? 19.399  -24.678 55.262  1.00 52.05  ? 723 ILE A CA  1 
ATOM 5411 C C   . ILE A 1 723 ? 19.504  -24.397 56.754  1.00 53.53  ? 723 ILE A C   1 
ATOM 5412 O O   . ILE A 1 723 ? 19.461  -25.317 57.574  1.00 64.06  ? 723 ILE A O   1 
ATOM 5413 C CB  . ILE A 1 723 ? 18.145  -25.491 54.930  1.00 56.01  ? 723 ILE A CB  1 
ATOM 5414 C CG1 . ILE A 1 723 ? 18.095  -25.790 53.434  1.00 52.42  ? 723 ILE A CG1 1 
ATOM 5415 C CG2 . ILE A 1 723 ? 16.898  -24.744 55.369  1.00 49.12  ? 723 ILE A CG2 1 
ATOM 5416 C CD1 . ILE A 1 723 ? 16.968  -26.696 53.040  1.00 54.99  ? 723 ILE A CD1 1 
ATOM 5417 N N   . ARG A 1 724 ? 19.647  -23.126 57.108  1.00 58.21  ? 724 ARG A N   1 
ATOM 5418 C CA  . ARG A 1 724 ? 19.929  -22.728 58.477  1.00 61.40  ? 724 ARG A CA  1 
ATOM 5419 C C   . ARG A 1 724 ? 18.708  -22.073 59.104  1.00 60.38  ? 724 ARG A C   1 
ATOM 5420 O O   . ARG A 1 724 ? 17.824  -21.574 58.403  1.00 62.76  ? 724 ARG A O   1 
ATOM 5421 C CB  . ARG A 1 724 ? 21.122  -21.773 58.529  1.00 60.95  ? 724 ARG A CB  1 
ATOM 5422 C CG  . ARG A 1 724 ? 22.405  -22.389 58.017  1.00 59.30  ? 724 ARG A CG  1 
ATOM 5423 C CD  . ARG A 1 724 ? 23.619  -21.627 58.498  1.00 62.37  ? 724 ARG A CD  1 
ATOM 5424 N NE  . ARG A 1 724 ? 24.204  -22.241 59.683  1.00 66.40  ? 724 ARG A NE  1 
ATOM 5425 C CZ  . ARG A 1 724 ? 24.666  -21.563 60.723  1.00 68.41  ? 724 ARG A CZ  1 
ATOM 5426 N NH1 . ARG A 1 724 ? 24.656  -20.241 60.744  1.00 66.54  ? 724 ARG A NH1 1 
ATOM 5427 N NH2 . ARG A 1 724 ? 25.157  -22.228 61.765  1.00 68.25  ? 724 ARG A NH2 1 
ATOM 5428 N N   . ASP A 1 725 ? 18.668  -22.095 60.432  1.00 63.71  ? 725 ASP A N   1 
ATOM 5429 C CA  . ASP A 1 725 ? 17.605  -21.480 61.207  1.00 59.64  ? 725 ASP A CA  1 
ATOM 5430 C C   . ASP A 1 725 ? 18.203  -20.977 62.511  1.00 56.86  ? 725 ASP A C   1 
ATOM 5431 O O   . ASP A 1 725 ? 19.303  -21.374 62.907  1.00 62.91  ? 725 ASP A O   1 
ATOM 5432 C CB  . ASP A 1 725 ? 16.465  -22.468 61.470  1.00 65.44  ? 725 ASP A CB  1 
ATOM 5433 C CG  . ASP A 1 725 ? 15.230  -21.797 62.021  1.00 70.40  ? 725 ASP A CG  1 
ATOM 5434 O OD1 . ASP A 1 725 ? 15.188  -20.550 62.018  1.00 70.16  ? 725 ASP A OD1 1 
ATOM 5435 O OD2 . ASP A 1 725 ? 14.311  -22.511 62.472  1.00 75.02  ? 725 ASP A OD2 1 
ATOM 5436 N N   . ILE A 1 726 ? 17.481  -20.101 63.180  1.00 52.83  ? 726 ILE A N   1 
ATOM 5437 C CA  . ILE A 1 726 ? 17.881  -19.644 64.503  1.00 54.80  ? 726 ILE A CA  1 
ATOM 5438 C C   . ILE A 1 726 ? 17.562  -20.745 65.501  1.00 59.06  ? 726 ILE A C   1 
ATOM 5439 O O   . ILE A 1 726 ? 16.528  -21.417 65.405  1.00 65.59  ? 726 ILE A O   1 
ATOM 5440 C CB  . ILE A 1 726 ? 17.187  -18.320 64.867  1.00 59.58  ? 726 ILE A CB  1 
ATOM 5441 C CG1 . ILE A 1 726 ? 15.691  -18.521 65.104  1.00 56.85  ? 726 ILE A CG1 1 
ATOM 5442 C CG2 . ILE A 1 726 ? 17.383  -17.319 63.757  1.00 54.77  ? 726 ILE A CG2 1 
ATOM 5443 C CD1 . ILE A 1 726 ? 15.012  -17.327 65.729  1.00 53.33  ? 726 ILE A CD1 1 
ATOM 5444 N N   . ASP A 1 727 ? 18.474  -20.965 66.440  1.00 66.34  ? 727 ASP A N   1 
ATOM 5445 C CA  . ASP A 1 727 ? 18.296  -21.987 67.462  1.00 62.62  ? 727 ASP A CA  1 
ATOM 5446 C C   . ASP A 1 727 ? 17.633  -21.338 68.671  1.00 68.45  ? 727 ASP A C   1 
ATOM 5447 O O   . ASP A 1 727 ? 18.299  -20.678 69.474  1.00 70.09  ? 727 ASP A O   1 
ATOM 5448 C CB  . ASP A 1 727 ? 19.633  -22.622 67.831  1.00 63.24  ? 727 ASP A CB  1 
ATOM 5449 C CG  . ASP A 1 727 ? 19.471  -23.934 68.567  1.00 72.97  ? 727 ASP A CG  1 
ATOM 5450 O OD1 . ASP A 1 727 ? 18.317  -24.351 68.794  1.00 75.43  ? 727 ASP A OD1 1 
ATOM 5451 O OD2 . ASP A 1 727 ? 20.498  -24.554 68.912  1.00 75.75  ? 727 ASP A OD2 1 
ATOM 5452 N N   . MET A 1 728 ? 16.321  -21.520 68.794  1.00 72.18  ? 728 MET A N   1 
ATOM 5453 C CA  . MET A 1 728 ? 15.566  -20.941 69.896  1.00 70.21  ? 728 MET A CA  1 
ATOM 5454 C C   . MET A 1 728 ? 15.970  -21.506 71.249  1.00 75.15  ? 728 MET A C   1 
ATOM 5455 O O   . MET A 1 728 ? 15.682  -20.881 72.275  1.00 73.23  ? 728 MET A O   1 
ATOM 5456 C CB  . MET A 1 728 ? 14.068  -21.157 69.674  1.00 71.39  ? 728 MET A CB  1 
ATOM 5457 C CG  . MET A 1 728 ? 13.517  -20.464 68.441  1.00 72.16  ? 728 MET A CG  1 
ATOM 5458 S SD  . MET A 1 728 ? 13.186  -18.716 68.704  1.00 85.39  ? 728 MET A SD  1 
ATOM 5459 C CE  . MET A 1 728 ? 11.398  -18.705 68.723  1.00 73.97  ? 728 MET A CE  1 
ATOM 5460 N N   . ALA A 1 729 ? 16.627  -22.665 71.277  1.00 73.63  ? 729 ALA A N   1 
ATOM 5461 C CA  . ALA A 1 729 ? 17.101  -23.259 72.518  1.00 74.21  ? 729 ALA A CA  1 
ATOM 5462 C C   . ALA A 1 729 ? 18.513  -22.835 72.887  1.00 76.75  ? 729 ALA A C   1 
ATOM 5463 O O   . ALA A 1 729 ? 18.906  -22.994 74.048  1.00 79.10  ? 729 ALA A O   1 
ATOM 5464 C CB  . ALA A 1 729 ? 17.046  -24.789 72.428  1.00 72.42  ? 729 ALA A CB  1 
ATOM 5465 N N   . SER A 1 730 ? 19.280  -22.303 71.940  1.00 65.63  ? 730 SER A N   1 
ATOM 5466 C CA  . SER A 1 730 ? 20.656  -21.889 72.179  1.00 65.83  ? 730 SER A CA  1 
ATOM 5467 C C   . SER A 1 730 ? 20.758  -20.381 72.010  1.00 68.61  ? 730 SER A C   1 
ATOM 5468 O O   . SER A 1 730 ? 20.622  -19.865 70.896  1.00 72.94  ? 730 SER A O   1 
ATOM 5469 C CB  . SER A 1 730 ? 21.616  -22.602 71.227  1.00 66.44  ? 730 SER A CB  1 
ATOM 5470 O OG  . SER A 1 730 ? 22.958  -22.235 71.490  1.00 70.02  ? 730 SER A OG  1 
ATOM 5471 N N   . TYR A 1 731 ? 21.001  -19.682 73.114  1.00 66.83  ? 731 TYR A N   1 
ATOM 5472 C CA  . TYR A 1 731 ? 21.194  -18.242 73.109  1.00 62.55  ? 731 TYR A CA  1 
ATOM 5473 C C   . TYR A 1 731 ? 22.397  -17.913 73.977  1.00 66.28  ? 731 TYR A C   1 
ATOM 5474 O O   . TYR A 1 731 ? 22.596  -18.508 75.039  1.00 63.43  ? 731 TYR A O   1 
ATOM 5475 C CB  . TYR A 1 731 ? 19.948  -17.502 73.611  1.00 61.08  ? 731 TYR A CB  1 
ATOM 5476 C CG  . TYR A 1 731 ? 19.404  -18.053 74.905  1.00 64.07  ? 731 TYR A CG  1 
ATOM 5477 C CD1 . TYR A 1 731 ? 18.508  -19.112 74.907  1.00 62.59  ? 731 TYR A CD1 1 
ATOM 5478 C CD2 . TYR A 1 731 ? 19.796  -17.526 76.125  1.00 64.14  ? 731 TYR A CD2 1 
ATOM 5479 C CE1 . TYR A 1 731 ? 18.016  -19.627 76.084  1.00 63.40  ? 731 TYR A CE1 1 
ATOM 5480 C CE2 . TYR A 1 731 ? 19.307  -18.035 77.308  1.00 66.74  ? 731 TYR A CE2 1 
ATOM 5481 C CZ  . TYR A 1 731 ? 18.417  -19.083 77.283  1.00 68.82  ? 731 TYR A CZ  1 
ATOM 5482 O OH  . TYR A 1 731 ? 17.926  -19.593 78.461  1.00 75.00  ? 731 TYR A OH  1 
ATOM 5483 N N   . VAL A 1 732 ? 23.200  -16.961 73.516  1.00 70.40  ? 732 VAL A N   1 
ATOM 5484 C CA  . VAL A 1 732 ? 24.451  -16.603 74.169  1.00 64.29  ? 732 VAL A CA  1 
ATOM 5485 C C   . VAL A 1 732 ? 24.370  -15.157 74.634  1.00 66.23  ? 732 VAL A C   1 
ATOM 5486 O O   . VAL A 1 732 ? 24.020  -14.264 73.855  1.00 70.18  ? 732 VAL A O   1 
ATOM 5487 C CB  . VAL A 1 732 ? 25.661  -16.807 73.236  1.00 65.34  ? 732 VAL A CB  1 
ATOM 5488 C CG1 . VAL A 1 732 ? 26.951  -16.568 73.992  1.00 64.49  ? 732 VAL A CG1 1 
ATOM 5489 C CG2 . VAL A 1 732 ? 25.637  -18.202 72.637  1.00 67.07  ? 732 VAL A CG2 1 
ATOM 5490 N N   . THR A 1 733 ? 24.697  -14.936 75.903  1.00 60.59  ? 733 THR A N   1 
ATOM 5491 C CA  . THR A 1 733 ? 24.726  -13.592 76.459  1.00 56.77  ? 733 THR A CA  1 
ATOM 5492 C C   . THR A 1 733 ? 25.715  -12.717 75.697  1.00 61.03  ? 733 THR A C   1 
ATOM 5493 O O   . THR A 1 733 ? 26.787  -13.166 75.284  1.00 71.71  ? 733 THR A O   1 
ATOM 5494 C CB  . THR A 1 733 ? 25.107  -13.640 77.940  1.00 61.76  ? 733 THR A CB  1 
ATOM 5495 O OG1 . THR A 1 733 ? 24.218  -14.523 78.636  1.00 68.86  ? 733 THR A OG1 1 
ATOM 5496 C CG2 . THR A 1 733 ? 25.036  -12.257 78.565  1.00 64.39  ? 733 THR A CG2 1 
ATOM 5497 N N   . ILE A 1 734 ? 25.331  -11.455 75.496  1.00 58.03  ? 734 ILE A N   1 
ATOM 5498 C CA  . ILE A 1 734 ? 26.205  -10.510 74.815  1.00 62.04  ? 734 ILE A CA  1 
ATOM 5499 C C   . ILE A 1 734 ? 27.511  -10.371 75.584  1.00 66.16  ? 734 ILE A C   1 
ATOM 5500 O O   . ILE A 1 734 ? 27.525  -10.253 76.816  1.00 70.00  ? 734 ILE A O   1 
ATOM 5501 C CB  . ILE A 1 734 ? 25.505  -9.152  74.655  1.00 64.58  ? 734 ILE A CB  1 
ATOM 5502 C CG1 . ILE A 1 734 ? 24.215  -9.305  73.853  1.00 62.49  ? 734 ILE A CG1 1 
ATOM 5503 C CG2 . ILE A 1 734 ? 26.421  -8.166  73.977  1.00 58.89  ? 734 ILE A CG2 1 
ATOM 5504 C CD1 . ILE A 1 734 ? 23.480  -8.007  73.649  1.00 60.45  ? 734 ILE A CD1 1 
ATOM 5505 N N   . GLY A 1 735 ? 28.622  -10.390 74.851  1.00 64.57  ? 735 GLY A N   1 
ATOM 5506 C CA  . GLY A 1 735 ? 29.942  -10.390 75.431  1.00 67.05  ? 735 GLY A CA  1 
ATOM 5507 C C   . GLY A 1 735 ? 30.508  -11.774 75.671  1.00 69.21  ? 735 GLY A C   1 
ATOM 5508 O O   . GLY A 1 735 ? 31.719  -11.973 75.534  1.00 71.09  ? 735 GLY A O   1 
ATOM 5509 N N   . VAL A 1 736 ? 29.659  -12.735 76.025  1.00 66.27  ? 736 VAL A N   1 
ATOM 5510 C CA  . VAL A 1 736 ? 30.096  -14.119 76.134  1.00 63.76  ? 736 VAL A CA  1 
ATOM 5511 C C   . VAL A 1 736 ? 30.380  -14.725 74.763  1.00 68.84  ? 736 VAL A C   1 
ATOM 5512 O O   . VAL A 1 736 ? 31.355  -15.465 74.605  1.00 75.24  ? 736 VAL A O   1 
ATOM 5513 C CB  . VAL A 1 736 ? 29.051  -14.948 76.899  1.00 62.29  ? 736 VAL A CB  1 
ATOM 5514 C CG1 . VAL A 1 736 ? 29.542  -16.373 77.096  1.00 66.00  ? 736 VAL A CG1 1 
ATOM 5515 C CG2 . VAL A 1 736 ? 28.737  -14.298 78.233  1.00 63.60  ? 736 VAL A CG2 1 
ATOM 5516 N N   . GLY A 1 737 ? 29.556  -14.418 73.769  1.00 68.72  ? 737 GLY A N   1 
ATOM 5517 C CA  . GLY A 1 737 ? 29.752  -14.951 72.437  1.00 70.50  ? 737 GLY A CA  1 
ATOM 5518 C C   . GLY A 1 737 ? 28.870  -14.234 71.444  1.00 70.97  ? 737 GLY A C   1 
ATOM 5519 O O   . GLY A 1 737 ? 28.043  -13.393 71.809  1.00 71.13  ? 737 GLY A O   1 
ATOM 5520 N N   . ALA A 1 738 ? 29.060  -14.581 70.175  1.00 76.92  ? 738 ALA A N   1 
ATOM 5521 C CA  . ALA A 1 738 ? 28.343  -13.957 69.073  1.00 75.78  ? 738 ALA A CA  1 
ATOM 5522 C C   . ALA A 1 738 ? 27.289  -14.919 68.542  1.00 79.79  ? 738 ALA A C   1 
ATOM 5523 O O   . ALA A 1 738 ? 27.583  -16.092 68.292  1.00 82.92  ? 738 ALA A O   1 
ATOM 5524 C CB  . ALA A 1 738 ? 29.306  -13.550 67.959  1.00 75.72  ? 738 ALA A CB  1 
ATOM 5525 N N   . GLY A 1 739 ? 26.067  -14.423 68.380  1.00 72.70  ? 739 GLY A N   1 
ATOM 5526 C CA  . GLY A 1 739 ? 24.999  -15.197 67.782  1.00 62.47  ? 739 GLY A CA  1 
ATOM 5527 C C   . GLY A 1 739 ? 24.284  -14.416 66.701  1.00 58.88  ? 739 GLY A C   1 
ATOM 5528 O O   . GLY A 1 739 ? 24.020  -13.223 66.868  1.00 66.63  ? 739 GLY A O   1 
ATOM 5529 N N   . ASN A 1 740 ? 23.968  -15.069 65.586  1.00 56.01  ? 740 ASN A N   1 
ATOM 5530 C CA  . ASN A 1 740 ? 23.324  -14.398 64.465  1.00 58.68  ? 740 ASN A CA  1 
ATOM 5531 C C   . ASN A 1 740 ? 21.822  -14.635 64.415  1.00 60.94  ? 740 ASN A C   1 
ATOM 5532 O O   . ASN A 1 740 ? 21.214  -14.439 63.356  1.00 61.76  ? 740 ASN A O   1 
ATOM 5533 C CB  . ASN A 1 740 ? 23.962  -14.841 63.147  1.00 62.88  ? 740 ASN A CB  1 
ATOM 5534 C CG  . ASN A 1 740 ? 25.463  -14.634 63.124  1.00 66.52  ? 740 ASN A CG  1 
ATOM 5535 O OD1 . ASN A 1 740 ? 25.987  -13.731 63.773  1.00 68.99  ? 740 ASN A OD1 1 
ATOM 5536 N ND2 . ASN A 1 740 ? 26.162  -15.469 62.368  1.00 68.49  ? 740 ASN A ND2 1 
ATOM 5537 N N   . GLY A 1 741 ? 21.209  -15.041 65.523  1.00 56.21  ? 741 GLY A N   1 
ATOM 5538 C CA  . GLY A 1 741 ? 19.803  -15.388 65.518  1.00 49.92  ? 741 GLY A CA  1 
ATOM 5539 C C   . GLY A 1 741 ? 18.873  -14.288 65.982  1.00 56.96  ? 741 GLY A C   1 
ATOM 5540 O O   . GLY A 1 741 ? 17.652  -14.469 65.990  1.00 65.67  ? 741 GLY A O   1 
ATOM 5541 N N   . GLY A 1 742 ? 19.426  -13.145 66.370  1.00 45.74  ? 742 GLY A N   1 
ATOM 5542 C CA  . GLY A 1 742 ? 18.604  -12.027 66.784  1.00 49.44  ? 742 GLY A CA  1 
ATOM 5543 C C   . GLY A 1 742 ? 18.736  -11.674 68.250  1.00 53.93  ? 742 GLY A C   1 
ATOM 5544 O O   . GLY A 1 742 ? 19.031  -12.536 69.081  1.00 54.95  ? 742 GLY A O   1 
ATOM 5545 N N   . LEU A 1 743 ? 18.512  -10.404 68.576  1.00 55.91  ? 743 LEU A N   1 
ATOM 5546 C CA  . LEU A 1 743 ? 18.641  -9.921  69.944  1.00 47.07  ? 743 LEU A CA  1 
ATOM 5547 C C   . LEU A 1 743 ? 17.453  -10.392 70.771  1.00 52.89  ? 743 LEU A C   1 
ATOM 5548 O O   . LEU A 1 743 ? 16.299  -10.184 70.384  1.00 64.43  ? 743 LEU A O   1 
ATOM 5549 C CB  . LEU A 1 743 ? 18.734  -8.399  69.958  1.00 51.83  ? 743 LEU A CB  1 
ATOM 5550 C CG  . LEU A 1 743 ? 20.145  -7.828  69.861  1.00 52.37  ? 743 LEU A CG  1 
ATOM 5551 C CD1 . LEU A 1 743 ? 20.099  -6.360  69.492  1.00 49.38  ? 743 LEU A CD1 1 
ATOM 5552 C CD2 . LEU A 1 743 ? 20.877  -8.030  71.169  1.00 53.40  ? 743 LEU A CD2 1 
ATOM 5553 N N   . VAL A 1 744 ? 17.734  -11.030 71.908  1.00 53.66  ? 744 VAL A N   1 
ATOM 5554 C CA  . VAL A 1 744 ? 16.702  -11.572 72.778  1.00 52.82  ? 744 VAL A CA  1 
ATOM 5555 C C   . VAL A 1 744 ? 16.997  -11.182 74.217  1.00 51.61  ? 744 VAL A C   1 
ATOM 5556 O O   . VAL A 1 744 ? 18.108  -10.776 74.565  1.00 57.43  ? 744 VAL A O   1 
ATOM 5557 C CB  . VAL A 1 744 ? 16.582  -13.106 72.665  1.00 50.06  ? 744 VAL A CB  1 
ATOM 5558 C CG1 . VAL A 1 744 ? 16.623  -13.523 71.226  1.00 63.33  ? 744 VAL A CG1 1 
ATOM 5559 C CG2 . VAL A 1 744 ? 17.696  -13.785 73.439  1.00 50.55  ? 744 VAL A CG2 1 
ATOM 5560 N N   . LEU A 1 745 ? 15.974  -11.308 75.053  1.00 50.45  ? 745 LEU A N   1 
ATOM 5561 C CA  . LEU A 1 745 ? 16.116  -11.135 76.491  1.00 48.73  ? 745 LEU A CA  1 
ATOM 5562 C C   . LEU A 1 745 ? 15.928  -12.486 77.167  1.00 52.91  ? 745 LEU A C   1 
ATOM 5563 O O   . LEU A 1 745 ? 14.891  -13.133 76.991  1.00 62.64  ? 745 LEU A O   1 
ATOM 5564 C CB  . LEU A 1 745 ? 15.098  -10.133 77.026  1.00 51.63  ? 745 LEU A CB  1 
ATOM 5565 C CG  . LEU A 1 745 ? 15.230  -8.676  76.600  1.00 52.46  ? 745 LEU A CG  1 
ATOM 5566 C CD1 . LEU A 1 745 ? 14.008  -7.917  77.066  1.00 55.80  ? 745 LEU A CD1 1 
ATOM 5567 C CD2 . LEU A 1 745 ? 16.498  -8.066  77.164  1.00 51.30  ? 745 LEU A CD2 1 
ATOM 5568 N N   . ASP A 1 746 ? 16.925  -12.910 77.935  1.00 65.12  ? 746 ASP A N   1 
ATOM 5569 C CA  . ASP A 1 746 ? 16.809  -14.108 78.757  1.00 58.12  ? 746 ASP A CA  1 
ATOM 5570 C C   . ASP A 1 746 ? 16.198  -13.699 80.089  1.00 58.15  ? 746 ASP A C   1 
ATOM 5571 O O   . ASP A 1 746 ? 16.908  -13.257 80.998  1.00 63.93  ? 746 ASP A O   1 
ATOM 5572 C CB  . ASP A 1 746 ? 18.168  -14.772 78.952  1.00 61.06  ? 746 ASP A CB  1 
ATOM 5573 C CG  . ASP A 1 746 ? 18.064  -16.104 79.662  1.00 68.17  ? 746 ASP A CG  1 
ATOM 5574 O OD1 . ASP A 1 746 ? 16.949  -16.663 79.715  1.00 64.40  ? 746 ASP A OD1 1 
ATOM 5575 O OD2 . ASP A 1 746 ? 19.094  -16.592 80.171  1.00 73.18  ? 746 ASP A OD2 1 
ATOM 5576 N N   . ILE A 1 747 ? 14.883  -13.838 80.205  1.00 55.21  ? 747 ILE A N   1 
ATOM 5577 C CA  . ILE A 1 747 ? 14.152  -13.425 81.396  1.00 58.73  ? 747 ILE A CA  1 
ATOM 5578 C C   . ILE A 1 747 ? 14.207  -14.559 82.407  1.00 59.24  ? 747 ILE A C   1 
ATOM 5579 O O   . ILE A 1 747 ? 13.755  -15.675 82.128  1.00 58.14  ? 747 ILE A O   1 
ATOM 5580 C CB  . ILE A 1 747 ? 12.701  -13.048 81.068  1.00 57.64  ? 747 ILE A CB  1 
ATOM 5581 C CG1 . ILE A 1 747 ? 12.646  -12.207 79.793  1.00 57.50  ? 747 ILE A CG1 1 
ATOM 5582 C CG2 . ILE A 1 747 ? 12.072  -12.316 82.242  1.00 59.41  ? 747 ILE A CG2 1 
ATOM 5583 C CD1 . ILE A 1 747 ? 12.853  -10.732 80.022  1.00 54.95  ? 747 ILE A CD1 1 
ATOM 5584 N N   . ASN A 1 748 ? 14.761  -14.272 83.579  1.00 65.03  ? 748 ASN A N   1 
ATOM 5585 C CA  . ASN A 1 748 ? 14.868  -15.236 84.665  1.00 63.19  ? 748 ASN A CA  1 
ATOM 5586 C C   . ASN A 1 748 ? 14.098  -14.701 85.863  1.00 66.81  ? 748 ASN A C   1 
ATOM 5587 O O   . ASN A 1 748 ? 14.451  -13.653 86.414  1.00 69.24  ? 748 ASN A O   1 
ATOM 5588 C CB  . ASN A 1 748 ? 16.330  -15.490 85.029  1.00 66.84  ? 748 ASN A CB  1 
ATOM 5589 C CG  . ASN A 1 748 ? 17.027  -16.390 84.032  1.00 72.50  ? 748 ASN A CG  1 
ATOM 5590 O OD1 . ASN A 1 748 ? 16.493  -17.423 83.633  1.00 74.36  ? 748 ASN A OD1 1 
ATOM 5591 N ND2 . ASN A 1 748 ? 18.224  -15.998 83.618  1.00 70.72  ? 748 ASN A ND2 1 
ATOM 5592 N N   . ILE A 1 749 ? 13.052  -15.416 86.259  1.00 71.11  ? 749 ILE A N   1 
ATOM 5593 C CA  . ILE A 1 749 ? 12.216  -15.032 87.388  1.00 66.62  ? 749 ILE A CA  1 
ATOM 5594 C C   . ILE A 1 749 ? 12.566  -15.951 88.549  1.00 70.40  ? 749 ILE A C   1 
ATOM 5595 O O   . ILE A 1 749 ? 12.452  -17.176 88.440  1.00 74.39  ? 749 ILE A O   1 
ATOM 5596 C CB  . ILE A 1 749 ? 10.725  -15.110 87.042  1.00 62.69  ? 749 ILE A CB  1 
ATOM 5597 C CG1 . ILE A 1 749 ? 10.417  -14.258 85.811  1.00 66.67  ? 749 ILE A CG1 1 
ATOM 5598 C CG2 . ILE A 1 749 ? 9.884   -14.657 88.219  1.00 63.35  ? 749 ILE A CG2 1 
ATOM 5599 C CD1 . ILE A 1 749 ? 9.005   -14.416 85.306  1.00 68.27  ? 749 ILE A CD1 1 
ATOM 5600 N N   . THR A 1 750 ? 12.998  -15.364 89.660  1.00 71.82  ? 750 THR A N   1 
ATOM 5601 C CA  . THR A 1 750 ? 13.359  -16.114 90.855  1.00 71.52  ? 750 THR A CA  1 
ATOM 5602 C C   . THR A 1 750 ? 12.242  -15.973 91.878  1.00 70.84  ? 750 THR A C   1 
ATOM 5603 O O   . THR A 1 750 ? 11.879  -14.855 92.258  1.00 73.31  ? 750 THR A O   1 
ATOM 5604 C CB  . THR A 1 750 ? 14.685  -15.621 91.432  1.00 71.17  ? 750 THR A CB  1 
ATOM 5605 O OG1 . THR A 1 750 ? 15.694  -15.664 90.417  1.00 72.95  ? 750 THR A OG1 1 
ATOM 5606 C CG2 . THR A 1 750 ? 15.113  -16.497 92.595  1.00 70.09  ? 750 THR A CG2 1 
ATOM 5607 N N   . TRP A 1 751 ? 11.708  -17.091 92.320  1.00 67.40  ? 751 TRP A N   1 
ATOM 5608 C CA  . TRP A 1 751 ? 10.603  -17.069 93.262  1.00 70.55  ? 751 TRP A CA  1 
ATOM 5609 C C   . TRP A 1 751 ? 11.093  -17.374 94.675  1.00 75.82  ? 751 TRP A C   1 
ATOM 5610 O O   . TRP A 1 751 ? 11.997  -18.194 94.863  1.00 78.41  ? 751 TRP A O   1 
ATOM 5611 C CB  . TRP A 1 751 ? 9.543   -18.087 92.851  1.00 72.76  ? 751 TRP A CB  1 
ATOM 5612 C CG  . TRP A 1 751 ? 8.977   -17.831 91.486  1.00 72.86  ? 751 TRP A CG  1 
ATOM 5613 C CD1 . TRP A 1 751 ? 9.413   -18.359 90.306  1.00 70.23  ? 751 TRP A CD1 1 
ATOM 5614 C CD2 . TRP A 1 751 ? 7.868   -16.984 91.159  1.00 74.68  ? 751 TRP A CD2 1 
ATOM 5615 N NE1 . TRP A 1 751 ? 8.647   -17.893 89.267  1.00 66.37  ? 751 TRP A NE1 1 
ATOM 5616 C CE2 . TRP A 1 751 ? 7.691   -17.048 89.764  1.00 72.23  ? 751 TRP A CE2 1 
ATOM 5617 C CE3 . TRP A 1 751 ? 7.009   -16.180 91.912  1.00 69.91  ? 751 TRP A CE3 1 
ATOM 5618 C CZ2 . TRP A 1 751 ? 6.690   -16.339 89.106  1.00 70.25  ? 751 TRP A CZ2 1 
ATOM 5619 C CZ3 . TRP A 1 751 ? 6.016   -15.477 91.257  1.00 68.84  ? 751 TRP A CZ3 1 
ATOM 5620 C CH2 . TRP A 1 751 ? 5.865   -15.560 89.868  1.00 70.23  ? 751 TRP A CH2 1 
ATOM 5621 N N   . PRO A 1 752 ? 10.516  -16.715 95.685  1.00 81.76  ? 752 PRO A N   1 
ATOM 5622 C CA  . PRO A 1 752 ? 10.982  -16.953 97.063  1.00 80.89  ? 752 PRO A CA  1 
ATOM 5623 C C   . PRO A 1 752 ? 10.732  -18.370 97.541  1.00 80.48  ? 752 PRO A C   1 
ATOM 5624 O O   . PRO A 1 752 ? 11.503  -18.893 98.354  1.00 80.93  ? 752 PRO A O   1 
ATOM 5625 C CB  . PRO A 1 752 ? 10.195  -15.926 97.887  1.00 79.89  ? 752 PRO A CB  1 
ATOM 5626 C CG  . PRO A 1 752 ? 9.011   -15.575 97.066  1.00 78.53  ? 752 PRO A CG  1 
ATOM 5627 C CD  . PRO A 1 752 ? 9.302   -15.883 95.630  1.00 77.83  ? 752 PRO A CD  1 
ATOM 5628 N N   . SER A 1 753 ? 9.671   -19.008 97.046  1.00 86.78  ? 753 SER A N   1 
ATOM 5629 C CA  . SER A 1 753 ? 9.297   -20.354 97.466  1.00 87.02  ? 753 SER A CA  1 
ATOM 5630 C C   . SER A 1 753 ? 9.216   -21.186 96.197  1.00 87.27  ? 753 SER A C   1 
ATOM 5631 O O   . SER A 1 753 ? 9.726   -20.756 95.166  1.00 88.89  ? 753 SER A O   1 
ATOM 5632 C CB  . SER A 1 753 ? 8.031   -20.336 98.303  1.00 87.07  ? 753 SER A CB  1 
ATOM 5633 O OG  . SER A 1 753 ? 7.274   -21.518 98.104  1.00 89.21  ? 753 SER A OG  1 
ATOM 5634 N N   . THR A 1 754 ? 8.629   -22.382 96.251  1.00 87.01  ? 754 THR A N   1 
ATOM 5635 C CA  . THR A 1 754 ? 8.456   -23.130 95.014  1.00 87.72  ? 754 THR A CA  1 
ATOM 5636 C C   . THR A 1 754 ? 7.667   -22.291 94.006  1.00 86.90  ? 754 THR A C   1 
ATOM 5637 O O   . THR A 1 754 ? 6.732   -21.580 94.382  1.00 83.30  ? 754 THR A O   1 
ATOM 5638 C CB  . THR A 1 754 ? 7.754   -24.470 95.280  1.00 84.38  ? 754 THR A CB  1 
ATOM 5639 O OG1 . THR A 1 754 ? 8.011   -25.373 94.195  1.00 84.82  ? 754 THR A OG1 1 
ATOM 5640 C CG2 . THR A 1 754 ? 6.250   -24.308 95.464  1.00 82.28  ? 754 THR A CG2 1 
ATOM 5641 N N   . PRO A 1 755 ? 8.077   -22.293 92.742  1.00 77.71  ? 755 PRO A N   1 
ATOM 5642 C CA  . PRO A 1 755 ? 7.447   -21.408 91.755  1.00 71.57  ? 755 PRO A CA  1 
ATOM 5643 C C   . PRO A 1 755 ? 5.992   -21.783 91.538  1.00 73.98  ? 755 PRO A C   1 
ATOM 5644 O O   . PRO A 1 755 ? 5.662   -22.968 91.388  1.00 73.61  ? 755 PRO A O   1 
ATOM 5645 C CB  . PRO A 1 755 ? 8.273   -21.626 90.479  1.00 75.09  ? 755 PRO A CB  1 
ATOM 5646 C CG  . PRO A 1 755 ? 9.360   -22.563 90.814  1.00 73.39  ? 755 PRO A CG  1 
ATOM 5647 C CD  . PRO A 1 755 ? 9.215   -23.056 92.205  1.00 75.03  ? 755 PRO A CD  1 
ATOM 5648 N N   . PRO A 1 756 ? 5.094   -20.800 91.526  1.00 67.45  ? 756 PRO A N   1 
ATOM 5649 C CA  . PRO A 1 756 ? 3.682   -21.102 91.259  1.00 67.39  ? 756 PRO A CA  1 
ATOM 5650 C C   . PRO A 1 756 ? 3.498   -21.656 89.857  1.00 71.13  ? 756 PRO A C   1 
ATOM 5651 O O   . PRO A 1 756 ? 4.177   -21.252 88.912  1.00 76.20  ? 756 PRO A O   1 
ATOM 5652 C CB  . PRO A 1 756 ? 2.975   -19.750 91.422  1.00 66.77  ? 756 PRO A CB  1 
ATOM 5653 C CG  . PRO A 1 756 ? 4.027   -18.727 91.590  1.00 67.85  ? 756 PRO A CG  1 
ATOM 5654 C CD  . PRO A 1 756 ? 5.358   -19.368 91.740  1.00 65.62  ? 756 PRO A CD  1 
ATOM 5655 N N   . THR A 1 757 ? 2.565   -22.593 89.730  1.00 74.37  ? 757 THR A N   1 
ATOM 5656 C CA  . THR A 1 757 ? 2.242   -23.204 88.451  1.00 74.04  ? 757 THR A CA  1 
ATOM 5657 C C   . THR A 1 757 ? 0.853   -22.766 88.012  1.00 72.89  ? 757 THR A C   1 
ATOM 5658 O O   . THR A 1 757 ? -0.122  -22.924 88.752  1.00 80.49  ? 757 THR A O   1 
ATOM 5659 C CB  . THR A 1 757 ? 2.303   -24.730 88.537  1.00 73.83  ? 757 THR A CB  1 
ATOM 5660 O OG1 . THR A 1 757 ? 1.554   -25.177 89.674  1.00 76.63  ? 757 THR A OG1 1 
ATOM 5661 C CG2 . THR A 1 757 ? 3.742   -25.197 88.670  1.00 70.67  ? 757 THR A CG2 1 
ATOM 5662 N N   . SER A 1 758 ? 0.769   -22.215 86.808  1.00 62.75  ? 758 SER A N   1 
ATOM 5663 C CA  . SER A 1 758 ? -0.497  -21.740 86.267  1.00 68.21  ? 758 SER A CA  1 
ATOM 5664 C C   . SER A 1 758 ? -0.355  -21.621 84.754  1.00 64.79  ? 758 SER A C   1 
ATOM 5665 O O   . SER A 1 758 ? 0.624   -22.089 84.166  1.00 67.42  ? 758 SER A O   1 
ATOM 5666 C CB  . SER A 1 758 ? -0.902  -20.412 86.913  1.00 67.21  ? 758 SER A CB  1 
ATOM 5667 O OG  . SER A 1 758 ? -1.985  -19.823 86.219  1.00 74.47  ? 758 SER A OG  1 
ATOM 5668 N N   . TYR A 1 759 ? -1.345  -20.997 84.125  1.00 62.65  ? 759 TYR A N   1 
ATOM 5669 C CA  . TYR A 1 759 ? -1.348  -20.758 82.688  1.00 58.82  ? 759 TYR A CA  1 
ATOM 5670 C C   . TYR A 1 759 ? -1.045  -19.282 82.464  1.00 62.55  ? 759 TYR A C   1 
ATOM 5671 O O   . TYR A 1 759 ? -1.912  -18.427 82.664  1.00 68.26  ? 759 TYR A O   1 
ATOM 5672 C CB  . TYR A 1 759 ? -2.690  -21.157 82.082  1.00 63.07  ? 759 TYR A CB  1 
ATOM 5673 C CG  . TYR A 1 759 ? -3.049  -22.601 82.338  1.00 62.77  ? 759 TYR A CG  1 
ATOM 5674 C CD1 . TYR A 1 759 ? -2.646  -23.599 81.465  1.00 67.51  ? 759 TYR A CD1 1 
ATOM 5675 C CD2 . TYR A 1 759 ? -3.769  -22.969 83.464  1.00 58.74  ? 759 TYR A CD2 1 
ATOM 5676 C CE1 . TYR A 1 759 ? -2.964  -24.916 81.696  1.00 65.34  ? 759 TYR A CE1 1 
ATOM 5677 C CE2 . TYR A 1 759 ? -4.090  -24.288 83.705  1.00 63.68  ? 759 TYR A CE2 1 
ATOM 5678 C CZ  . TYR A 1 759 ? -3.685  -25.257 82.818  1.00 67.12  ? 759 TYR A CZ  1 
ATOM 5679 O OH  . TYR A 1 759 ? -4.001  -26.575 83.051  1.00 69.94  ? 759 TYR A OH  1 
ATOM 5680 N N   . TRP A 1 760 ? 0.177   -18.990 82.034  1.00 59.24  ? 760 TRP A N   1 
ATOM 5681 C CA  . TRP A 1 760 ? 0.717   -17.640 82.067  1.00 57.02  ? 760 TRP A CA  1 
ATOM 5682 C C   . TRP A 1 760 ? 0.462   -16.906 80.758  1.00 53.59  ? 760 TRP A C   1 
ATOM 5683 O O   . TRP A 1 760 ? 0.513   -17.497 79.677  1.00 56.70  ? 760 TRP A O   1 
ATOM 5684 C CB  . TRP A 1 760 ? 2.219   -17.677 82.349  1.00 58.00  ? 760 TRP A CB  1 
ATOM 5685 C CG  . TRP A 1 760 ? 2.561   -18.367 83.628  1.00 57.10  ? 760 TRP A CG  1 
ATOM 5686 C CD1 . TRP A 1 760 ? 2.813   -19.695 83.799  1.00 57.31  ? 760 TRP A CD1 1 
ATOM 5687 C CD2 . TRP A 1 760 ? 2.691   -17.765 84.920  1.00 60.24  ? 760 TRP A CD2 1 
ATOM 5688 N NE1 . TRP A 1 760 ? 3.090   -19.959 85.116  1.00 59.84  ? 760 TRP A NE1 1 
ATOM 5689 C CE2 . TRP A 1 760 ? 3.023   -18.789 85.826  1.00 62.98  ? 760 TRP A CE2 1 
ATOM 5690 C CE3 . TRP A 1 760 ? 2.560   -16.459 85.398  1.00 57.08  ? 760 TRP A CE3 1 
ATOM 5691 C CZ2 . TRP A 1 760 ? 3.225   -18.549 87.181  1.00 61.44  ? 760 TRP A CZ2 1 
ATOM 5692 C CZ3 . TRP A 1 760 ? 2.760   -16.223 86.743  1.00 56.28  ? 760 TRP A CZ3 1 
ATOM 5693 C CH2 . TRP A 1 760 ? 3.088   -17.262 87.619  1.00 59.48  ? 760 TRP A CH2 1 
ATOM 5694 N N   . ASN A 1 761 ? 0.180   -15.611 80.872  1.00 58.77  ? 761 ASN A N   1 
ATOM 5695 C CA  . ASN A 1 761 ? 0.124   -14.699 79.735  1.00 53.70  ? 761 ASN A CA  1 
ATOM 5696 C C   . ASN A 1 761 ? 1.276   -13.715 79.891  1.00 54.64  ? 761 ASN A C   1 
ATOM 5697 O O   . ASN A 1 761 ? 1.315   -12.948 80.858  1.00 65.23  ? 761 ASN A O   1 
ATOM 5698 C CB  . ASN A 1 761 ? -1.214  -13.968 79.680  1.00 52.94  ? 761 ASN A CB  1 
ATOM 5699 C CG  . ASN A 1 761 ? -2.385  -14.906 79.508  1.00 59.09  ? 761 ASN A CG  1 
ATOM 5700 O OD1 . ASN A 1 761 ? -2.339  -15.834 78.704  1.00 68.07  ? 761 ASN A OD1 1 
ATOM 5701 N ND2 . ASN A 1 761 ? -3.446  -14.672 80.269  1.00 58.84  ? 761 ASN A ND2 1 
ATOM 5702 N N   . ILE A 1 762 ? 2.209   -13.733 78.947  1.00 54.48  ? 762 ILE A N   1 
ATOM 5703 C CA  . ILE A 1 762 ? 3.402   -12.898 79.006  1.00 56.57  ? 762 ILE A CA  1 
ATOM 5704 C C   . ILE A 1 762 ? 3.295   -11.837 77.923  1.00 51.96  ? 762 ILE A C   1 
ATOM 5705 O O   . ILE A 1 762 ? 3.112   -12.158 76.744  1.00 60.42  ? 762 ILE A O   1 
ATOM 5706 C CB  . ILE A 1 762 ? 4.684   -13.722 78.836  1.00 58.48  ? 762 ILE A CB  1 
ATOM 5707 C CG1 . ILE A 1 762 ? 4.720   -14.867 79.843  1.00 55.06  ? 762 ILE A CG1 1 
ATOM 5708 C CG2 . ILE A 1 762 ? 5.904   -12.838 79.011  1.00 53.00  ? 762 ILE A CG2 1 
ATOM 5709 C CD1 . ILE A 1 762 ? 5.781   -15.886 79.540  1.00 57.64  ? 762 ILE A CD1 1 
ATOM 5710 N N   . GLU A 1 763 ? 3.408   -10.575 78.323  1.00 56.31  ? 763 GLU A N   1 
ATOM 5711 C CA  . GLU A 1 763 ? 3.437   -9.452  77.398  1.00 58.26  ? 763 GLU A CA  1 
ATOM 5712 C C   . GLU A 1 763 ? 4.633   -8.572  77.729  1.00 55.93  ? 763 GLU A C   1 
ATOM 5713 O O   . GLU A 1 763 ? 4.828   -8.196  78.889  1.00 64.20  ? 763 GLU A O   1 
ATOM 5714 C CB  . GLU A 1 763 ? 2.143   -8.638  77.468  1.00 58.09  ? 763 GLU A CB  1 
ATOM 5715 C CG  . GLU A 1 763 ? 0.922   -9.370  76.936  1.00 61.66  ? 763 GLU A CG  1 
ATOM 5716 C CD  . GLU A 1 763 ? -0.327  -8.513  76.963  1.00 72.38  ? 763 GLU A CD  1 
ATOM 5717 O OE1 . GLU A 1 763 ? -0.264  -7.381  77.486  1.00 73.31  ? 763 GLU A OE1 1 
ATOM 5718 O OE2 . GLU A 1 763 ? -1.376  -8.973  76.462  1.00 70.29  ? 763 GLU A OE2 1 
ATOM 5719 N N   . LEU A 1 764 ? 5.431   -8.253  76.716  1.00 49.99  ? 764 LEU A N   1 
ATOM 5720 C CA  . LEU A 1 764 ? 6.566   -7.352  76.863  1.00 49.57  ? 764 LEU A CA  1 
ATOM 5721 C C   . LEU A 1 764 ? 6.223   -6.046  76.160  1.00 48.03  ? 764 LEU A C   1 
ATOM 5722 O O   . LEU A 1 764 ? 6.208   -5.982  74.927  1.00 53.41  ? 764 LEU A O   1 
ATOM 5723 C CB  . LEU A 1 764 ? 7.841   -7.967  76.295  1.00 49.65  ? 764 LEU A CB  1 
ATOM 5724 C CG  . LEU A 1 764 ? 9.096   -7.136  76.558  1.00 49.45  ? 764 LEU A CG  1 
ATOM 5725 C CD1 . LEU A 1 764 ? 9.442   -7.175  78.031  1.00 49.08  ? 764 LEU A CD1 1 
ATOM 5726 C CD2 . LEU A 1 764 ? 10.260  -7.626  75.725  1.00 54.38  ? 764 LEU A CD2 1 
ATOM 5727 N N   . GLU A 1 765 ? 5.953   -5.008  76.945  1.00 58.90  ? 765 GLU A N   1 
ATOM 5728 C CA  . GLU A 1 765 ? 5.582   -3.705  76.416  1.00 53.29  ? 765 GLU A CA  1 
ATOM 5729 C C   . GLU A 1 765 ? 6.814   -2.819  76.317  1.00 56.76  ? 765 GLU A C   1 
ATOM 5730 O O   . GLU A 1 765 ? 7.577   -2.697  77.280  1.00 66.26  ? 765 GLU A O   1 
ATOM 5731 C CB  . GLU A 1 765 ? 4.533   -3.042  77.306  1.00 54.30  ? 765 GLU A CB  1 
ATOM 5732 C CG  . GLU A 1 765 ? 3.151   -2.994  76.704  1.00 63.27  ? 765 GLU A CG  1 
ATOM 5733 C CD  . GLU A 1 765 ? 2.209   -2.103  77.487  1.00 70.59  ? 765 GLU A CD  1 
ATOM 5734 O OE1 . GLU A 1 765 ? 2.611   -0.973  77.834  1.00 67.76  ? 765 GLU A OE1 1 
ATOM 5735 O OE2 . GLU A 1 765 ? 1.066   -2.531  77.752  1.00 72.70  ? 765 GLU A OE2 1 
ATOM 5736 N N   . ALA A 1 766 ? 7.004   -2.201  75.156  1.00 47.16  ? 766 ALA A N   1 
ATOM 5737 C CA  . ALA A 1 766 ? 8.103   -1.267  74.973  1.00 48.69  ? 766 ALA A CA  1 
ATOM 5738 C C   . ALA A 1 766 ? 7.806   -0.355  73.796  1.00 47.22  ? 766 ALA A C   1 
ATOM 5739 O O   . ALA A 1 766 ? 6.995   -0.680  72.927  1.00 49.49  ? 766 ALA A O   1 
ATOM 5740 C CB  . ALA A 1 766 ? 9.429   -1.994  74.751  1.00 56.35  ? 766 ALA A CB  1 
ATOM 5741 N N   . TRP A 1 767 ? 8.478   0.793   73.780  1.00 47.04  ? 767 TRP A N   1 
ATOM 5742 C CA  . TRP A 1 767 ? 8.369   1.722   72.667  1.00 37.16  ? 767 TRP A CA  1 
ATOM 5743 C C   . TRP A 1 767 ? 9.047   1.134   71.440  1.00 43.67  ? 767 TRP A C   1 
ATOM 5744 O O   . TRP A 1 767 ? 10.086  0.475   71.548  1.00 52.03  ? 767 TRP A O   1 
ATOM 5745 C CB  . TRP A 1 767 ? 9.001   3.066   73.026  1.00 46.23  ? 767 TRP A CB  1 
ATOM 5746 C CG  . TRP A 1 767 ? 8.922   4.079   71.926  1.00 40.27  ? 767 TRP A CG  1 
ATOM 5747 C CD1 . TRP A 1 767 ? 7.966   5.033   71.765  1.00 43.36  ? 767 TRP A CD1 1 
ATOM 5748 C CD2 . TRP A 1 767 ? 9.837   4.239   70.834  1.00 47.38  ? 767 TRP A CD2 1 
ATOM 5749 N NE1 . TRP A 1 767 ? 8.224   5.779   70.643  1.00 45.38  ? 767 TRP A NE1 1 
ATOM 5750 C CE2 . TRP A 1 767 ? 9.368   5.311   70.053  1.00 42.03  ? 767 TRP A CE2 1 
ATOM 5751 C CE3 . TRP A 1 767 ? 11.005  3.580   70.442  1.00 41.29  ? 767 TRP A CE3 1 
ATOM 5752 C CZ2 . TRP A 1 767 ? 10.025  5.739   68.903  1.00 43.19  ? 767 TRP A CZ2 1 
ATOM 5753 C CZ3 . TRP A 1 767 ? 11.654  4.005   69.301  1.00 44.55  ? 767 TRP A CZ3 1 
ATOM 5754 C CH2 . TRP A 1 767 ? 11.163  5.074   68.545  1.00 47.31  ? 767 TRP A CH2 1 
ATOM 5755 N N   . ASP A 1 768 ? 8.458   1.368   70.274  1.00 50.69  ? 768 ASP A N   1 
ATOM 5756 C CA  . ASP A 1 768 ? 9.037   0.938   69.014  1.00 45.82  ? 768 ASP A CA  1 
ATOM 5757 C C   . ASP A 1 768 ? 8.585   1.878   67.908  1.00 45.28  ? 768 ASP A C   1 
ATOM 5758 O O   . ASP A 1 768 ? 7.557   2.552   68.013  1.00 61.60  ? 768 ASP A O   1 
ATOM 5759 C CB  . ASP A 1 768 ? 8.646   -0.509  68.688  1.00 42.33  ? 768 ASP A CB  1 
ATOM 5760 C CG  . ASP A 1 768 ? 9.542   -1.130  67.642  1.00 51.02  ? 768 ASP A CG  1 
ATOM 5761 O OD1 . ASP A 1 768 ? 10.439  -0.428  67.136  1.00 54.68  ? 768 ASP A OD1 1 
ATOM 5762 O OD2 . ASP A 1 768 ? 9.353   -2.323  67.329  1.00 64.90  ? 768 ASP A OD2 1 
ATOM 5763 N N   . MET A 1 769 ? 9.376   1.927   66.841  1.00 46.04  ? 769 MET A N   1 
ATOM 5764 C CA  . MET A 1 769 ? 8.997   2.673   65.653  1.00 47.61  ? 769 MET A CA  1 
ATOM 5765 C C   . MET A 1 769 ? 7.758   2.034   65.047  1.00 47.88  ? 769 MET A C   1 
ATOM 5766 O O   . MET A 1 769 ? 7.576   0.816   65.134  1.00 56.26  ? 769 MET A O   1 
ATOM 5767 C CB  . MET A 1 769 ? 10.144  2.696   64.646  1.00 48.62  ? 769 MET A CB  1 
ATOM 5768 C CG  . MET A 1 769 ? 11.481  3.083   65.250  1.00 50.94  ? 769 MET A CG  1 
ATOM 5769 S SD  . MET A 1 769 ? 12.825  3.053   64.053  1.00 74.18  ? 769 MET A SD  1 
ATOM 5770 C CE  . MET A 1 769 ? 14.085  2.191   64.980  1.00 58.35  ? 769 MET A CE  1 
ATOM 5771 N N   . PHE A 1 770 ? 6.898   2.855   64.447  1.00 44.39  ? 770 PHE A N   1 
ATOM 5772 C CA  . PHE A 1 770 ? 5.611   2.371   63.963  1.00 38.02  ? 770 PHE A CA  1 
ATOM 5773 C C   . PHE A 1 770 ? 5.782   1.263   62.933  1.00 50.91  ? 770 PHE A C   1 
ATOM 5774 O O   . PHE A 1 770 ? 6.357   1.480   61.863  1.00 51.33  ? 770 PHE A O   1 
ATOM 5775 C CB  . PHE A 1 770 ? 4.791   3.512   63.370  1.00 41.57  ? 770 PHE A CB  1 
ATOM 5776 C CG  . PHE A 1 770 ? 3.396   3.115   62.999  1.00 42.04  ? 770 PHE A CG  1 
ATOM 5777 C CD1 . PHE A 1 770 ? 2.457   2.852   63.980  1.00 43.57  ? 770 PHE A CD1 1 
ATOM 5778 C CD2 . PHE A 1 770 ? 3.027   2.988   61.675  1.00 43.58  ? 770 PHE A CD2 1 
ATOM 5779 C CE1 . PHE A 1 770 ? 1.173   2.480   63.643  1.00 43.33  ? 770 PHE A CE1 1 
ATOM 5780 C CE2 . PHE A 1 770 ? 1.745   2.617   61.333  1.00 41.47  ? 770 PHE A CE2 1 
ATOM 5781 C CZ  . PHE A 1 770 ? 0.819   2.365   62.317  1.00 45.09  ? 770 PHE A CZ  1 
ATOM 5782 N N   . GLY A 1 771 ? 5.285   0.072   63.254  1.00 49.22  ? 771 GLY A N   1 
ATOM 5783 C CA  . GLY A 1 771 ? 5.385   -1.052  62.349  1.00 43.57  ? 771 GLY A CA  1 
ATOM 5784 C C   . GLY A 1 771 ? 6.767   -1.635  62.203  1.00 48.75  ? 771 GLY A C   1 
ATOM 5785 O O   . GLY A 1 771 ? 7.031   -2.324  61.216  1.00 53.47  ? 771 GLY A O   1 
ATOM 5786 N N   . ASN A 1 772 ? 7.661   -1.387  63.153  1.00 45.20  ? 772 ASN A N   1 
ATOM 5787 C CA  . ASN A 1 772 ? 9.009   -1.925  63.060  1.00 34.26  ? 772 ASN A CA  1 
ATOM 5788 C C   . ASN A 1 772 ? 8.977   -3.441  63.205  1.00 45.63  ? 772 ASN A C   1 
ATOM 5789 O O   . ASN A 1 772 ? 8.440   -3.972  64.181  1.00 58.53  ? 772 ASN A O   1 
ATOM 5790 C CB  . ASN A 1 772 ? 9.900   -1.305  64.132  1.00 43.76  ? 772 ASN A CB  1 
ATOM 5791 C CG  . ASN A 1 772 ? 11.365  -1.596  63.910  1.00 53.76  ? 772 ASN A CG  1 
ATOM 5792 O OD1 . ASN A 1 772 ? 11.755  -2.119  62.867  1.00 58.04  ? 772 ASN A OD1 1 
ATOM 5793 N ND2 . ASN A 1 772 ? 12.188  -1.265  64.894  1.00 46.69  ? 772 ASN A ND2 1 
ATOM 5794 N N   . SER A 1 773 ? 9.548   -4.137  62.224  1.00 44.85  ? 773 SER A N   1 
ATOM 5795 C CA  . SER A 1 773 ? 9.576   -5.593  62.240  1.00 42.39  ? 773 SER A CA  1 
ATOM 5796 C C   . SER A 1 773 ? 10.597  -6.145  63.224  1.00 46.10  ? 773 SER A C   1 
ATOM 5797 O O   . SER A 1 773 ? 10.321  -7.130  63.916  1.00 56.84  ? 773 SER A O   1 
ATOM 5798 C CB  . SER A 1 773 ? 9.870   -6.127  60.837  1.00 48.13  ? 773 SER A CB  1 
ATOM 5799 O OG  . SER A 1 773 ? 9.250   -5.327  59.850  1.00 61.36  ? 773 SER A OG  1 
ATOM 5800 N N   . GLU A 1 774 ? 11.773  -5.532  63.299  1.00 45.83  ? 774 GLU A N   1 
ATOM 5801 C CA  . GLU A 1 774 ? 12.859  -6.012  64.136  1.00 51.88  ? 774 GLU A CA  1 
ATOM 5802 C C   . GLU A 1 774 ? 13.422  -4.866  64.962  1.00 55.54  ? 774 GLU A C   1 
ATOM 5803 O O   . GLU A 1 774 ? 13.421  -3.710  64.531  1.00 66.65  ? 774 GLU A O   1 
ATOM 5804 C CB  . GLU A 1 774 ? 13.984  -6.623  63.295  1.00 50.10  ? 774 GLU A CB  1 
ATOM 5805 C CG  . GLU A 1 774 ? 13.503  -7.514  62.175  1.00 60.43  ? 774 GLU A CG  1 
ATOM 5806 C CD  . GLU A 1 774 ? 14.626  -7.960  61.271  1.00 66.93  ? 774 GLU A CD  1 
ATOM 5807 O OE1 . GLU A 1 774 ? 15.801  -7.712  61.611  1.00 68.51  ? 774 GLU A OE1 1 
ATOM 5808 O OE2 . GLU A 1 774 ? 14.331  -8.546  60.211  1.00 74.39  ? 774 GLU A OE2 1 
ATOM 5809 N N   . ALA A 1 775 ? 13.842  -5.113  66.168  1.00 46.66  ? 775 ALA A N   1 
ATOM 5810 C CA  . ALA A 1 775 ? 14.530  -4.067  66.919  1.00 42.09  ? 775 ALA A CA  1 
ATOM 5811 C C   . ALA A 1 775 ? 15.819  -3.805  66.198  1.00 46.44  ? 775 ALA A C   1 
ATOM 5812 O O   . ALA A 1 775 ? 16.593  -4.718  66.029  1.00 53.92  ? 775 ALA A O   1 
ATOM 5813 C CB  . ALA A 1 775 ? 14.802  -4.547  68.246  1.00 46.82  ? 775 ALA A CB  1 
ATOM 5814 N N   . SER A 1 776 ? 16.046  -2.568  65.855  1.00 50.50  ? 776 SER A N   1 
ATOM 5815 C CA  . SER A 1 776 ? 17.185  -2.188  65.024  1.00 49.30  ? 776 SER A CA  1 
ATOM 5816 C C   . SER A 1 776 ? 18.051  -1.199  65.785  1.00 43.59  ? 776 SER A C   1 
ATOM 5817 O O   . SER A 1 776 ? 17.532  -0.248  66.231  1.00 68.04  ? 776 SER A O   1 
ATOM 5818 C CB  . SER A 1 776 ? 16.589  -1.613  63.855  1.00 47.45  ? 776 SER A CB  1 
ATOM 5819 O OG  . SER A 1 776 ? 15.594  -2.468  63.332  1.00 48.50  ? 776 SER A OG  1 
ATOM 5820 N N   . ILE A 1 777 ? 19.328  -1.446  65.898  1.00 30.00  ? 777 ILE A N   1 
ATOM 5821 C CA  . ILE A 1 777 ? 20.281  -0.581  66.626  1.00 30.00  ? 777 ILE A CA  1 
ATOM 5822 C C   . ILE A 1 777 ? 20.375  0.755   65.890  1.00 30.00  ? 777 ILE A C   1 
ATOM 5823 O O   . ILE A 1 777 ? 19.898  1.770   66.376  1.00 30.00  ? 777 ILE A O   1 
ATOM 5824 C CB  . ILE A 1 777 ? 21.638  -1.290  66.809  1.00 30.00  ? 777 ILE A CB  1 
ATOM 5825 C CG1 . ILE A 1 777 ? 21.699  -2.009  68.131  1.00 30.00  ? 777 ILE A CG1 1 
ATOM 5826 C CG2 . ILE A 1 777 ? 22.812  -0.328  66.666  1.00 30.00  ? 777 ILE A CG2 1 
ATOM 5827 C CD1 . ILE A 1 777 ? 21.252  -3.446  68.041  1.00 30.00  ? 777 ILE A CD1 1 
ATOM 5828 O OXT . ILE A 1 777 ? 20.933  0.779   64.828  1.00 30.00  ? 777 ILE A OXT 1 
ATOM 5829 N N   . TYR B 2 123 ? 5.035   -1.027  -79.954 1.00 67.71  ? 123 TYR B N   1 
ATOM 5830 C CA  . TYR B 2 123 ? 6.315   -0.906  -79.266 1.00 69.96  ? 123 TYR B CA  1 
ATOM 5831 C C   . TYR B 2 123 ? 6.898   -2.279  -78.950 1.00 71.68  ? 123 TYR B C   1 
ATOM 5832 O O   . TYR B 2 123 ? 6.163   -3.246  -78.759 1.00 71.45  ? 123 TYR B O   1 
ATOM 5833 C CB  . TYR B 2 123 ? 6.162   -0.096  -77.979 1.00 69.60  ? 123 TYR B CB  1 
ATOM 5834 C CG  . TYR B 2 123 ? 5.625   1.300   -78.191 1.00 71.77  ? 123 TYR B CG  1 
ATOM 5835 C CD1 . TYR B 2 123 ? 6.214   2.159   -79.109 1.00 74.83  ? 123 TYR B CD1 1 
ATOM 5836 C CD2 . TYR B 2 123 ? 4.532   1.761   -77.471 1.00 69.37  ? 123 TYR B CD2 1 
ATOM 5837 C CE1 . TYR B 2 123 ? 5.728   3.437   -79.305 1.00 75.82  ? 123 TYR B CE1 1 
ATOM 5838 C CE2 . TYR B 2 123 ? 4.038   3.036   -77.661 1.00 71.78  ? 123 TYR B CE2 1 
ATOM 5839 C CZ  . TYR B 2 123 ? 4.640   3.870   -78.578 1.00 74.39  ? 123 TYR B CZ  1 
ATOM 5840 O OH  . TYR B 2 123 ? 4.151   5.141   -78.770 1.00 71.93  ? 123 TYR B OH  1 
ATOM 5841 N N   . ILE B 2 124 ? 8.223   -2.353  -78.897 1.00 67.39  ? 124 ILE B N   1 
ATOM 5842 C CA  . ILE B 2 124 ? 8.927   -3.590  -78.581 1.00 67.31  ? 124 ILE B CA  1 
ATOM 5843 C C   . ILE B 2 124 ? 9.207   -3.602  -77.081 1.00 68.54  ? 124 ILE B C   1 
ATOM 5844 O O   . ILE B 2 124 ? 9.954   -2.736  -76.599 1.00 65.07  ? 124 ILE B O   1 
ATOM 5845 C CB  . ILE B 2 124 ? 10.228  -3.716  -79.382 1.00 68.10  ? 124 ILE B CB  1 
ATOM 5846 C CG1 . ILE B 2 124 ? 9.936   -3.653  -80.883 1.00 70.10  ? 124 ILE B CG1 1 
ATOM 5847 C CG2 . ILE B 2 124 ? 10.949  -5.006  -79.027 1.00 67.75  ? 124 ILE B CG2 1 
ATOM 5848 C CD1 . ILE B 2 124 ? 11.165  -3.430  -81.735 1.00 65.51  ? 124 ILE B CD1 1 
ATOM 5849 N N   . PRO B 2 125 ? 8.645   -4.540  -76.321 1.00 68.94  ? 125 PRO B N   1 
ATOM 5850 C CA  . PRO B 2 125 ? 8.910   -4.572  -74.876 1.00 64.48  ? 125 PRO B CA  1 
ATOM 5851 C C   . PRO B 2 125 ? 10.280  -5.166  -74.590 1.00 68.05  ? 125 PRO B C   1 
ATOM 5852 O O   . PRO B 2 125 ? 10.605  -6.265  -75.045 1.00 70.73  ? 125 PRO B O   1 
ATOM 5853 C CB  . PRO B 2 125 ? 7.785   -5.452  -74.318 1.00 60.42  ? 125 PRO B CB  1 
ATOM 5854 C CG  . PRO B 2 125 ? 7.244   -6.214  -75.478 1.00 63.21  ? 125 PRO B CG  1 
ATOM 5855 C CD  . PRO B 2 125 ? 7.728   -5.606  -76.759 1.00 66.64  ? 125 PRO B CD  1 
ATOM 5856 N N   . PHE B 2 126 ? 11.085  -4.429  -73.828 1.00 64.91  ? 126 PHE B N   1 
ATOM 5857 C CA  . PHE B 2 126 ? 12.413  -4.869  -73.422 1.00 59.02  ? 126 PHE B CA  1 
ATOM 5858 C C   . PHE B 2 126 ? 12.421  -5.028  -71.910 1.00 61.57  ? 126 PHE B C   1 
ATOM 5859 O O   . PHE B 2 126 ? 12.105  -4.083  -71.181 1.00 69.68  ? 126 PHE B O   1 
ATOM 5860 C CB  . PHE B 2 126 ? 13.484  -3.872  -73.870 1.00 56.48  ? 126 PHE B CB  1 
ATOM 5861 C CG  . PHE B 2 126 ? 14.875  -4.248  -73.452 1.00 62.31  ? 126 PHE B CG  1 
ATOM 5862 C CD1 . PHE B 2 126 ? 15.541  -5.290  -74.074 1.00 65.67  ? 126 PHE B CD1 1 
ATOM 5863 C CD2 . PHE B 2 126 ? 15.522  -3.555  -72.443 1.00 62.91  ? 126 PHE B CD2 1 
ATOM 5864 C CE1 . PHE B 2 126 ? 16.823  -5.637  -73.694 1.00 65.53  ? 126 PHE B CE1 1 
ATOM 5865 C CE2 . PHE B 2 126 ? 16.803  -3.898  -72.059 1.00 64.05  ? 126 PHE B CE2 1 
ATOM 5866 C CZ  . PHE B 2 126 ? 17.454  -4.939  -72.684 1.00 65.26  ? 126 PHE B CZ  1 
ATOM 5867 N N   . VAL B 2 127 ? 12.782  -6.219  -71.442 1.00 62.33  ? 127 VAL B N   1 
ATOM 5868 C CA  . VAL B 2 127 ? 12.796  -6.539  -70.021 1.00 63.51  ? 127 VAL B CA  1 
ATOM 5869 C C   . VAL B 2 127 ? 14.226  -6.427  -69.517 1.00 61.07  ? 127 VAL B C   1 
ATOM 5870 O O   . VAL B 2 127 ? 15.131  -7.089  -70.037 1.00 68.93  ? 127 VAL B O   1 
ATOM 5871 C CB  . VAL B 2 127 ? 12.226  -7.944  -69.763 1.00 62.63  ? 127 VAL B CB  1 
ATOM 5872 C CG1 . VAL B 2 127 ? 12.175  -8.226  -68.275 1.00 64.16  ? 127 VAL B CG1 1 
ATOM 5873 C CG2 . VAL B 2 127 ? 10.847  -8.079  -70.386 1.00 63.17  ? 127 VAL B CG2 1 
ATOM 5874 N N   . PHE B 2 128 ? 14.432  -5.590  -68.504 1.00 63.16  ? 128 PHE B N   1 
ATOM 5875 C CA  . PHE B 2 128 ? 15.771  -5.330  -67.997 1.00 66.90  ? 128 PHE B CA  1 
ATOM 5876 C C   . PHE B 2 128 ? 16.223  -6.431  -67.049 1.00 71.39  ? 128 PHE B C   1 
ATOM 5877 O O   . PHE B 2 128 ? 15.594  -6.679  -66.016 1.00 74.75  ? 128 PHE B O   1 
ATOM 5878 C CB  . PHE B 2 128 ? 15.820  -3.980  -67.284 1.00 66.91  ? 128 PHE B CB  1 
ATOM 5879 C CG  . PHE B 2 128 ? 17.163  -3.655  -66.702 1.00 67.85  ? 128 PHE B CG  1 
ATOM 5880 C CD1 . PHE B 2 128 ? 18.269  -3.502  -67.519 1.00 66.98  ? 128 PHE B CD1 1 
ATOM 5881 C CD2 . PHE B 2 128 ? 17.319  -3.500  -65.336 1.00 71.08  ? 128 PHE B CD2 1 
ATOM 5882 C CE1 . PHE B 2 128 ? 19.506  -3.202  -66.984 1.00 73.60  ? 128 PHE B CE1 1 
ATOM 5883 C CE2 . PHE B 2 128 ? 18.553  -3.199  -64.795 1.00 70.25  ? 128 PHE B CE2 1 
ATOM 5884 C CZ  . PHE B 2 128 ? 19.648  -3.050  -65.621 1.00 74.50  ? 128 PHE B CZ  1 
ATOM 5885 N N   . ASN B 2 129 ? 17.333  -7.078  -67.407 1.00 68.54  ? 129 ASN B N   1 
ATOM 5886 C CA  . ASN B 2 129 ? 17.963  -8.130  -66.608 1.00 69.72  ? 129 ASN B CA  1 
ATOM 5887 C C   . ASN B 2 129 ? 16.940  -9.202  -66.228 1.00 70.91  ? 129 ASN B C   1 
ATOM 5888 O O   . ASN B 2 129 ? 16.632  -9.395  -65.049 1.00 75.44  ? 129 ASN B O   1 
ATOM 5889 C CB  . ASN B 2 129 ? 18.650  -7.527  -65.369 1.00 70.85  ? 129 ASN B CB  1 
ATOM 5890 C CG  . ASN B 2 129 ? 19.420  -8.553  -64.525 1.00 76.97  ? 129 ASN B CG  1 
ATOM 5891 O OD1 . ASN B 2 129 ? 19.053  -9.721  -64.408 1.00 77.64  ? 129 ASN B OD1 1 
ATOM 5892 N ND2 . ASN B 2 129 ? 20.509  -8.091  -63.924 1.00 77.04  ? 129 ASN B ND2 1 
ATOM 5893 N N   . ASN B 2 130 ? 16.332  -9.833  -67.236 1.00 78.31  ? 130 ASN B N   1 
ATOM 5894 C CA  . ASN B 2 130 ? 15.404  -10.954 -67.069 1.00 84.90  ? 130 ASN B CA  1 
ATOM 5895 C C   . ASN B 2 130 ? 14.244  -10.644 -66.119 1.00 86.26  ? 130 ASN B C   1 
ATOM 5896 O O   . ASN B 2 130 ? 13.491  -11.544 -65.737 1.00 86.05  ? 130 ASN B O   1 
ATOM 5897 C CB  . ASN B 2 130 ? 16.168  -12.238 -66.674 1.00 85.10  ? 130 ASN B CB  1 
ATOM 5898 C CG  . ASN B 2 130 ? 16.419  -12.403 -65.157 1.00 86.55  ? 130 ASN B CG  1 
ATOM 5899 O OD1 . ASN B 2 130 ? 15.695  -11.906 -64.297 1.00 84.84  ? 130 ASN B OD1 1 
ATOM 5900 N ND2 . ASN B 2 130 ? 17.485  -13.132 -64.843 1.00 88.20  ? 130 ASN B ND2 1 
ATOM 5901 N N   . GLY B 2 131 ? 14.051  -9.374  -65.767 1.00 79.00  ? 131 GLY B N   1 
ATOM 5902 C CA  . GLY B 2 131 ? 12.993  -8.985  -64.860 1.00 74.76  ? 131 GLY B CA  1 
ATOM 5903 C C   . GLY B 2 131 ? 13.413  -8.769  -63.424 1.00 76.11  ? 131 GLY B C   1 
ATOM 5904 O O   . GLY B 2 131 ? 12.552  -8.491  -62.580 1.00 80.07  ? 131 GLY B O   1 
ATOM 5905 N N   . SER B 2 132 ? 14.701  -8.894  -63.111 1.00 71.36  ? 132 SER B N   1 
ATOM 5906 C CA  . SER B 2 132 ? 15.204  -8.699  -61.756 1.00 74.90  ? 132 SER B CA  1 
ATOM 5907 C C   . SER B 2 132 ? 16.467  -7.856  -61.820 1.00 72.49  ? 132 SER B C   1 
ATOM 5908 O O   . SER B 2 132 ? 17.542  -8.372  -62.142 1.00 75.46  ? 132 SER B O   1 
ATOM 5909 C CB  . SER B 2 132 ? 15.485  -10.040 -61.073 1.00 74.38  ? 132 SER B CB  1 
ATOM 5910 O OG  . SER B 2 132 ? 14.304  -10.582 -60.509 1.00 77.63  ? 132 SER B OG  1 
ATOM 5911 N N   . ALA B 2 133 ? 16.339  -6.571  -61.507 1.00 71.53  ? 133 ALA B N   1 
ATOM 5912 C CA  . ALA B 2 133 ? 17.470  -5.657  -61.509 1.00 71.20  ? 133 ALA B CA  1 
ATOM 5913 C C   . ALA B 2 133 ? 18.452  -6.028  -60.405 1.00 70.66  ? 133 ALA B C   1 
ATOM 5914 O O   . ALA B 2 133 ? 18.067  -6.600  -59.381 1.00 73.72  ? 133 ALA B O   1 
ATOM 5915 C CB  . ALA B 2 133 ? 17.000  -4.214  -61.329 1.00 71.41  ? 133 ALA B CB  1 
ATOM 5916 N N   . ALA B 2 134 ? 19.725  -5.701  -60.624 1.00 73.94  ? 134 ALA B N   1 
ATOM 5917 C CA  . ALA B 2 134 ? 20.788  -6.028  -59.684 1.00 71.19  ? 134 ALA B CA  1 
ATOM 5918 C C   . ALA B 2 134 ? 20.869  -5.059  -58.511 1.00 72.22  ? 134 ALA B C   1 
ATOM 5919 O O   . ALA B 2 134 ? 21.623  -5.314  -57.565 1.00 77.32  ? 134 ALA B O   1 
ATOM 5920 C CB  . ALA B 2 134 ? 22.134  -6.078  -60.413 1.00 72.86  ? 134 ALA B CB  1 
ATOM 5921 N N   . GLY B 2 135 ? 20.121  -3.970  -58.546 1.00 67.49  ? 135 GLY B N   1 
ATOM 5922 C CA  . GLY B 2 135 ? 20.152  -2.999  -57.472 1.00 68.58  ? 135 GLY B CA  1 
ATOM 5923 C C   . GLY B 2 135 ? 21.095  -1.850  -57.770 1.00 71.01  ? 135 GLY B C   1 
ATOM 5924 O O   . GLY B 2 135 ? 22.179  -2.024  -58.339 1.00 70.62  ? 135 GLY B O   1 
ATOM 5925 N N   . GLY B 2 136 ? 20.679  -0.649  -57.378 1.00 76.41  ? 136 GLY B N   1 
ATOM 5926 C CA  . GLY B 2 136 ? 21.487  0.539   -57.562 1.00 74.86  ? 136 GLY B CA  1 
ATOM 5927 C C   . GLY B 2 136 ? 21.709  0.924   -59.010 1.00 74.74  ? 136 GLY B C   1 
ATOM 5928 O O   . GLY B 2 136 ? 22.692  1.599   -59.331 1.00 73.77  ? 136 GLY B O   1 
ATOM 5929 N N   . GLU B 2 137 ? 20.806  0.511   -59.896 1.00 74.99  ? 137 GLU B N   1 
ATOM 5930 C CA  . GLU B 2 137 ? 20.940  0.862   -61.303 1.00 71.17  ? 137 GLU B CA  1 
ATOM 5931 C C   . GLU B 2 137 ? 20.200  2.160   -61.597 1.00 70.99  ? 137 GLU B C   1 
ATOM 5932 O O   . GLU B 2 137 ? 18.970  2.224   -61.509 1.00 77.90  ? 137 GLU B O   1 
ATOM 5933 C CB  . GLU B 2 137 ? 20.408  -0.259  -62.194 1.00 69.86  ? 137 GLU B CB  1 
ATOM 5934 C CG  . GLU B 2 137 ? 21.189  -1.555  -62.096 1.00 72.20  ? 137 GLU B CG  1 
ATOM 5935 C CD  . GLU B 2 137 ? 20.342  -2.700  -61.584 1.00 75.96  ? 137 GLU B CD  1 
ATOM 5936 O OE1 . GLU B 2 137 ? 19.705  -2.539  -60.525 1.00 71.97  ? 137 GLU B OE1 1 
ATOM 5937 O OE2 . GLU B 2 137 ? 20.315  -3.763  -62.240 1.00 76.20  ? 137 GLU B OE2 1 
ATOM 5938 N N   . THR B 2 138 ? 20.959  3.199   -61.946 1.00 67.60  ? 138 THR B N   1 
ATOM 5939 C CA  . THR B 2 138 ? 20.393  4.476   -62.349 1.00 69.45  ? 138 THR B CA  1 
ATOM 5940 C C   . THR B 2 138 ? 20.122  4.561   -63.844 1.00 71.90  ? 138 THR B C   1 
ATOM 5941 O O   . THR B 2 138 ? 19.107  5.143   -64.241 1.00 70.57  ? 138 THR B O   1 
ATOM 5942 C CB  . THR B 2 138 ? 21.330  5.623   -61.931 1.00 73.41  ? 138 THR B CB  1 
ATOM 5943 O OG1 . THR B 2 138 ? 21.113  5.938   -60.550 1.00 77.24  ? 138 THR B OG1 1 
ATOM 5944 C CG2 . THR B 2 138 ? 21.103  6.874   -62.771 1.00 73.88  ? 138 THR B CG2 1 
ATOM 5945 N N   . THR B 2 139 ? 20.972  3.958   -64.671 1.00 75.27  ? 139 THR B N   1 
ATOM 5946 C CA  . THR B 2 139 ? 20.864  4.053   -66.117 1.00 76.50  ? 139 THR B CA  1 
ATOM 5947 C C   . THR B 2 139 ? 20.738  2.661   -66.718 1.00 74.67  ? 139 THR B C   1 
ATOM 5948 O O   . THR B 2 139 ? 21.355  1.703   -66.244 1.00 73.71  ? 139 THR B O   1 
ATOM 5949 C CB  . THR B 2 139 ? 22.079  4.772   -66.710 1.00 77.53  ? 139 THR B CB  1 
ATOM 5950 O OG1 . THR B 2 139 ? 23.254  4.410   -65.974 1.00 80.62  ? 139 THR B OG1 1 
ATOM 5951 C CG2 . THR B 2 139 ? 21.891  6.278   -66.626 1.00 75.45  ? 139 THR B CG2 1 
ATOM 5952 N N   . ILE B 2 140 ? 19.927  2.558   -67.768 1.00 68.85  ? 140 ILE B N   1 
ATOM 5953 C CA  . ILE B 2 140 ? 19.684  1.300   -68.465 1.00 72.74  ? 140 ILE B CA  1 
ATOM 5954 C C   . ILE B 2 140 ? 20.003  1.488   -69.941 1.00 75.41  ? 140 ILE B C   1 
ATOM 5955 O O   . ILE B 2 140 ? 19.545  2.451   -70.565 1.00 77.86  ? 140 ILE B O   1 
ATOM 5956 C CB  . ILE B 2 140 ? 18.231  0.816   -68.282 1.00 71.36  ? 140 ILE B CB  1 
ATOM 5957 C CG1 . ILE B 2 140 ? 17.942  0.536   -66.807 1.00 72.73  ? 140 ILE B CG1 1 
ATOM 5958 C CG2 . ILE B 2 140 ? 17.976  -0.425  -69.118 1.00 72.11  ? 140 ILE B CG2 1 
ATOM 5959 C CD1 . ILE B 2 140 ? 16.570  -0.050  -66.557 1.00 72.93  ? 140 ILE B CD1 1 
ATOM 5960 N N   . VAL B 2 141 ? 20.780  0.564   -70.497 1.00 81.70  ? 141 VAL B N   1 
ATOM 5961 C CA  . VAL B 2 141 ? 21.183  0.602   -71.898 1.00 82.30  ? 141 VAL B CA  1 
ATOM 5962 C C   . VAL B 2 141 ? 20.215  -0.258  -72.700 1.00 83.69  ? 141 VAL B C   1 
ATOM 5963 O O   . VAL B 2 141 ? 19.995  -1.430  -72.372 1.00 83.83  ? 141 VAL B O   1 
ATOM 5964 C CB  . VAL B 2 141 ? 22.630  0.122   -72.081 1.00 81.63  ? 141 VAL B CB  1 
ATOM 5965 C CG1 . VAL B 2 141 ? 23.130  0.464   -73.475 1.00 82.78  ? 141 VAL B CG1 1 
ATOM 5966 C CG2 . VAL B 2 141 ? 23.530  0.737   -71.021 1.00 81.65  ? 141 VAL B CG2 1 
ATOM 5967 N N   . VAL B 2 142 ? 19.639  0.322   -73.747 1.00 84.83  ? 142 VAL B N   1 
ATOM 5968 C CA  . VAL B 2 142 ? 18.657  -0.364  -74.585 1.00 85.38  ? 142 VAL B CA  1 
ATOM 5969 C C   . VAL B 2 142 ? 19.333  -0.858  -75.859 1.00 87.49  ? 142 VAL B C   1 
ATOM 5970 O O   . VAL B 2 142 ? 20.398  -0.345  -76.231 1.00 88.52  ? 142 VAL B O   1 
ATOM 5971 C CB  . VAL B 2 142 ? 17.465  0.555   -74.902 1.00 83.30  ? 142 VAL B CB  1 
ATOM 5972 C CG1 . VAL B 2 142 ? 16.971  1.229   -73.634 1.00 83.88  ? 142 VAL B CG1 1 
ATOM 5973 C CG2 . VAL B 2 142 ? 17.853  1.591   -75.945 1.00 81.24  ? 142 VAL B CG2 1 
ATOM 5974 N N   . PRO B 2 143 ? 18.793  -1.863  -76.599 1.00 86.66  ? 143 PRO B N   1 
ATOM 5975 C CA  . PRO B 2 143 ? 19.410  -2.262  -77.859 1.00 85.67  ? 143 PRO B CA  1 
ATOM 5976 C C   . PRO B 2 143 ? 19.424  -1.187  -78.939 1.00 86.90  ? 143 PRO B C   1 
ATOM 5977 O O   . PRO B 2 143 ? 18.727  -0.165  -78.801 1.00 85.05  ? 143 PRO B O   1 
ATOM 5978 C CB  . PRO B 2 143 ? 18.620  -3.500  -78.302 1.00 86.23  ? 143 PRO B CB  1 
ATOM 5979 C CG  . PRO B 2 143 ? 17.296  -3.357  -77.610 1.00 85.61  ? 143 PRO B CG  1 
ATOM 5980 C CD  . PRO B 2 143 ? 17.641  -2.729  -76.276 1.00 84.13  ? 143 PRO B CD  1 
ATOM 5981 N N   . ASP B 2 144 ? 20.177  -1.430  -80.015 1.00 98.15  ? 144 ASP B N   1 
ATOM 5982 C CA  . ASP B 2 144 ? 20.340  -0.417  -81.097 1.00 98.97  ? 144 ASP B CA  1 
ATOM 5983 C C   . ASP B 2 144 ? 18.994  -0.069  -81.736 1.00 97.30  ? 144 ASP B C   1 
ATOM 5984 O O   . ASP B 2 144 ? 18.686  1.134   -81.844 1.00 97.85  ? 144 ASP B O   1 
ATOM 5985 C CB  . ASP B 2 144 ? 21.363  -0.885  -82.117 1.00 99.07  ? 144 ASP B CB  1 
ATOM 5986 C CG  . ASP B 2 144 ? 22.612  -1.517  -81.523 1.00 98.01  ? 144 ASP B CG  1 
ATOM 5987 O OD1 . ASP B 2 144 ? 23.348  -2.185  -82.278 1.00 99.22  ? 144 ASP B OD1 1 
ATOM 5988 O OD2 . ASP B 2 144 ? 22.835  -1.339  -80.308 1.00 96.41  ? 144 ASP B OD2 1 
ATOM 5989 N N   . TYR B 2 145 ? 18.227  -1.080  -82.143 1.00 95.86  ? 145 TYR B N   1 
ATOM 5990 C CA  . TYR B 2 145 ? 16.909  -0.839  -82.772 1.00 95.50  ? 145 TYR B CA  1 
ATOM 5991 C C   . TYR B 2 145 ? 16.210  0.344   -82.100 1.00 96.20  ? 145 TYR B C   1 
ATOM 5992 O O   . TYR B 2 145 ? 15.636  1.185   -82.825 1.00 94.99  ? 145 TYR B O   1 
ATOM 5993 C CB  . TYR B 2 145 ? 16.073  -2.088  -82.669 1.00 30.00  ? 145 TYR B CB  1 
ATOM 5994 N N   . THR B 2 146 ? 16.255  0.416   -80.766 1.00 30.00  ? 146 THR B N   1 
ATOM 5995 C CA  . THR B 2 146 ? 15.519  1.476   -80.035 1.00 30.00  ? 146 THR B CA  1 
ATOM 5996 C C   . THR B 2 146 ? 15.939  2.870   -80.500 1.00 30.00  ? 146 THR B C   1 
ATOM 5997 O O   . THR B 2 146 ? 17.088  3.275   -80.234 1.00 30.00  ? 146 THR B O   1 
ATOM 5998 C CB  . THR B 2 146 ? 15.709  1.315   -78.545 1.00 30.00  ? 146 THR B CB  1 
ATOM 5999 N N   . ILE B 2 147 ? 15.027  3.579   -81.165 1.00 30.00  ? 147 ILE B N   1 
ATOM 6000 C CA  . ILE B 2 147 ? 15.292  4.976   -81.573 1.00 30.00  ? 147 ILE B CA  1 
ATOM 6001 C C   . ILE B 2 147 ? 14.580  5.881   -80.573 1.00 30.00  ? 147 ILE B C   1 
ATOM 6002 O O   . ILE B 2 147 ? 14.701  7.118   -80.672 1.00 30.00  ? 147 ILE B O   1 
ATOM 6003 C CB  . ILE B 2 147 ? 14.775  5.201   -82.969 1.00 30.00  ? 147 ILE B CB  1 
ATOM 6004 N N   . GLY B 2 148 ? 13.849  5.272   -79.638 1.00 30.00  ? 148 GLY B N   1 
ATOM 6005 C CA  . GLY B 2 148 ? 13.099  6.042   -78.630 1.00 30.00  ? 148 GLY B CA  1 
ATOM 6006 C C   . GLY B 2 148 ? 12.542  5.112   -77.575 1.00 30.00  ? 148 GLY B C   1 
ATOM 6007 O O   . GLY B 2 148 ? 12.277  3.941   -77.907 1.00 30.00  ? 148 GLY B O   1 
ATOM 6008 N N   . VAL B 2 149 ? 12.406  5.592   -76.340 1.00 55.87  ? 149 VAL B N   1 
ATOM 6009 C CA  . VAL B 2 149 ? 11.772  4.766   -75.273 1.00 59.53  ? 149 VAL B CA  1 
ATOM 6010 C C   . VAL B 2 149 ? 10.588  5.574   -74.727 1.00 60.00  ? 149 VAL B C   1 
ATOM 6011 O O   . VAL B 2 149 ? 10.810  6.437   -73.868 1.00 60.32  ? 149 VAL B O   1 
ATOM 6012 C CB  . VAL B 2 149 ? 12.772  4.368   -74.174 1.00 59.00  ? 149 VAL B CB  1 
ATOM 6013 C CG1 . VAL B 2 149 ? 12.084  3.686   -73.001 1.00 60.33  ? 149 VAL B CG1 1 
ATOM 6014 C CG2 . VAL B 2 149 ? 13.862  3.460   -74.728 1.00 61.78  ? 149 VAL B CG2 1 
ATOM 6015 N N   . PRO B 2 150 ? 9.357   5.376   -75.240 1.00 58.25  ? 150 PRO B N   1 
ATOM 6016 C CA  . PRO B 2 150 ? 8.229   6.192   -74.807 1.00 56.01  ? 150 PRO B CA  1 
ATOM 6017 C C   . PRO B 2 150 ? 7.703   5.870   -73.426 1.00 60.79  ? 150 PRO B C   1 
ATOM 6018 O O   . PRO B 2 150 ? 7.135   6.764   -72.775 1.00 57.04  ? 150 PRO B O   1 
ATOM 6019 C CB  . PRO B 2 150 ? 7.208   5.827   -75.892 1.00 57.96  ? 150 PRO B CB  1 
ATOM 6020 C CG  . PRO B 2 150 ? 7.525   4.394   -76.233 1.00 57.81  ? 150 PRO B CG  1 
ATOM 6021 C CD  . PRO B 2 150 ? 9.035   4.408   -76.276 1.00 58.40  ? 150 PRO B CD  1 
ATOM 6022 N N   . GLU B 2 151 ? 7.897   4.633   -72.975 1.00 63.08  ? 151 GLU B N   1 
ATOM 6023 C CA  . GLU B 2 151 ? 7.329   4.184   -71.712 1.00 50.12  ? 151 GLU B CA  1 
ATOM 6024 C C   . GLU B 2 151 ? 8.304   3.283   -70.970 1.00 47.08  ? 151 GLU B C   1 
ATOM 6025 O O   . GLU B 2 151 ? 9.084   2.552   -71.585 1.00 63.53  ? 151 GLU B O   1 
ATOM 6026 C CB  . GLU B 2 151 ? 6.014   3.428   -71.935 1.00 47.97  ? 151 GLU B CB  1 
ATOM 6027 C CG  . GLU B 2 151 ? 4.920   4.257   -72.578 1.00 55.93  ? 151 GLU B CG  1 
ATOM 6028 C CD  . GLU B 2 151 ? 3.660   3.456   -72.832 1.00 61.37  ? 151 GLU B CD  1 
ATOM 6029 O OE1 . GLU B 2 151 ? 3.695   2.221   -72.653 1.00 64.43  ? 151 GLU B OE1 1 
ATOM 6030 O OE2 . GLU B 2 151 ? 2.635   4.061   -73.210 1.00 67.71  ? 151 GLU B OE2 1 
ATOM 6031 N N   . ILE B 2 152 ? 8.244   3.345   -69.642 1.00 35.99  ? 152 ILE B N   1 
ATOM 6032 C CA  . ILE B 2 152 ? 8.967   2.443   -68.755 1.00 42.03  ? 152 ILE B CA  1 
ATOM 6033 C C   . ILE B 2 152 ? 7.971   1.893   -67.749 1.00 44.80  ? 152 ILE B C   1 
ATOM 6034 O O   . ILE B 2 152 ? 7.193   2.654   -67.161 1.00 59.32  ? 152 ILE B O   1 
ATOM 6035 C CB  . ILE B 2 152 ? 10.133  3.147   -68.038 1.00 43.43  ? 152 ILE B CB  1 
ATOM 6036 C CG1 . ILE B 2 152 ? 11.208  3.556   -69.041 1.00 44.99  ? 152 ILE B CG1 1 
ATOM 6037 C CG2 . ILE B 2 152 ? 10.733  2.248   -66.975 1.00 47.15  ? 152 ILE B CG2 1 
ATOM 6038 C CD1 . ILE B 2 152 ? 11.786  2.411   -69.801 1.00 52.16  ? 152 ILE B CD1 1 
ATOM 6039 N N   . TYR B 2 153 ? 7.981   0.578   -67.558 1.00 30.68  ? 153 TYR B N   1 
ATOM 6040 C CA  . TYR B 2 153 ? 7.084   -0.082  -66.617 1.00 39.23  ? 153 TYR B CA  1 
ATOM 6041 C C   . TYR B 2 153 ? 7.909   -0.668  -65.478 1.00 41.16  ? 153 TYR B C   1 
ATOM 6042 O O   . TYR B 2 153 ? 8.444   -1.774  -65.596 1.00 55.41  ? 153 TYR B O   1 
ATOM 6043 C CB  . TYR B 2 153 ? 6.262   -1.159  -67.317 1.00 41.46  ? 153 TYR B CB  1 
ATOM 6044 C CG  . TYR B 2 153 ? 5.175   -0.605  -68.206 1.00 40.83  ? 153 TYR B CG  1 
ATOM 6045 C CD1 . TYR B 2 153 ? 3.934   -0.265  -67.686 1.00 40.62  ? 153 TYR B CD1 1 
ATOM 6046 C CD2 . TYR B 2 153 ? 5.390   -0.417  -69.565 1.00 46.68  ? 153 TYR B CD2 1 
ATOM 6047 C CE1 . TYR B 2 153 ? 2.937   0.239   -68.495 1.00 40.65  ? 153 TYR B CE1 1 
ATOM 6048 C CE2 . TYR B 2 153 ? 4.398   0.089   -70.379 1.00 45.45  ? 153 TYR B CE2 1 
ATOM 6049 C CZ  . TYR B 2 153 ? 3.174   0.416   -69.839 1.00 43.08  ? 153 TYR B CZ  1 
ATOM 6050 O OH  . TYR B 2 153 ? 2.181   0.922   -70.646 1.00 49.94  ? 153 TYR B OH  1 
ATOM 6051 N N   . VAL B 2 154 ? 8.004   0.072   -64.379 1.00 38.41  ? 154 VAL B N   1 
ATOM 6052 C CA  . VAL B 2 154 ? 8.706   -0.374  -63.182 1.00 35.20  ? 154 VAL B CA  1 
ATOM 6053 C C   . VAL B 2 154 ? 7.683   -0.998  -62.247 1.00 29.22  ? 154 VAL B C   1 
ATOM 6054 O O   . VAL B 2 154 ? 6.860   -0.288  -61.656 1.00 31.74  ? 154 VAL B O   1 
ATOM 6055 C CB  . VAL B 2 154 ? 9.442   0.785   -62.495 1.00 31.46  ? 154 VAL B CB  1 
ATOM 6056 C CG1 . VAL B 2 154 ? 10.098  0.307   -61.210 1.00 35.23  ? 154 VAL B CG1 1 
ATOM 6057 C CG2 . VAL B 2 154 ? 10.473  1.387   -63.431 1.00 34.00  ? 154 VAL B CG2 1 
ATOM 6058 N N   . GLU B 2 155 ? 7.735   -2.324  -62.106 1.00 37.63  ? 155 GLU B N   1 
ATOM 6059 C CA  . GLU B 2 155 ? 6.793   -3.057  -61.258 1.00 26.36  ? 155 GLU B CA  1 
ATOM 6060 C C   . GLU B 2 155 ? 5.346   -2.751  -61.633 1.00 29.31  ? 155 GLU B C   1 
ATOM 6061 O O   . GLU B 2 155 ? 4.498   -2.535  -60.765 1.00 47.65  ? 155 GLU B O   1 
ATOM 6062 C CB  . GLU B 2 155 ? 7.035   -2.760  -59.778 1.00 33.43  ? 155 GLU B CB  1 
ATOM 6063 C CG  . GLU B 2 155 ? 8.289   -3.359  -59.165 1.00 32.25  ? 155 GLU B CG  1 
ATOM 6064 C CD  . GLU B 2 155 ? 8.523   -4.799  -59.570 1.00 52.57  ? 155 GLU B CD  1 
ATOM 6065 O OE1 . GLU B 2 155 ? 9.675   -5.138  -59.898 1.00 58.28  ? 155 GLU B OE1 1 
ATOM 6066 O OE2 . GLU B 2 155 ? 7.562   -5.595  -59.545 1.00 53.43  ? 155 GLU B OE2 1 
ATOM 6067 N N   . GLY B 2 156 ? 5.054   -2.734  -62.931 1.00 26.71  ? 156 GLY B N   1 
ATOM 6068 C CA  . GLY B 2 156 ? 3.715   -2.472  -63.413 1.00 29.50  ? 156 GLY B CA  1 
ATOM 6069 C C   . GLY B 2 156 ? 3.315   -1.015  -63.435 1.00 40.85  ? 156 GLY B C   1 
ATOM 6070 O O   . GLY B 2 156 ? 2.158   -0.715  -63.750 1.00 50.35  ? 156 GLY B O   1 
ATOM 6071 N N   . PHE B 2 157 ? 4.229   -0.106  -63.114 1.00 35.91  ? 157 PHE B N   1 
ATOM 6072 C CA  . PHE B 2 157 ? 3.957   1.323   -63.094 1.00 25.46  ? 157 PHE B CA  1 
ATOM 6073 C C   . PHE B 2 157 ? 4.492   1.968   -64.362 1.00 29.82  ? 157 PHE B C   1 
ATOM 6074 O O   . PHE B 2 157 ? 5.702   1.972   -64.604 1.00 50.98  ? 157 PHE B O   1 
ATOM 6075 C CB  . PHE B 2 157 ? 4.608   1.985   -61.878 1.00 36.66  ? 157 PHE B CB  1 
ATOM 6076 C CG  . PHE B 2 157 ? 3.920   1.686   -60.586 1.00 30.43  ? 157 PHE B CG  1 
ATOM 6077 C CD1 . PHE B 2 157 ? 2.545   1.739   -60.491 1.00 30.90  ? 157 PHE B CD1 1 
ATOM 6078 C CD2 . PHE B 2 157 ? 4.652   1.346   -59.463 1.00 35.77  ? 157 PHE B CD2 1 
ATOM 6079 C CE1 . PHE B 2 157 ? 1.915   1.467   -59.301 1.00 31.31  ? 157 PHE B CE1 1 
ATOM 6080 C CE2 . PHE B 2 157 ? 4.024   1.069   -58.272 1.00 24.62  ? 157 PHE B CE2 1 
ATOM 6081 C CZ  . PHE B 2 157 ? 2.653   1.126   -58.192 1.00 27.85  ? 157 PHE B CZ  1 
ATOM 6082 N N   . ARG B 2 158 ? 3.591   2.525   -65.166 1.00 39.45  ? 158 ARG B N   1 
ATOM 6083 C CA  . ARG B 2 158 ? 3.998   3.219   -66.379 1.00 39.51  ? 158 ARG B CA  1 
ATOM 6084 C C   . ARG B 2 158 ? 4.673   4.531   -66.007 1.00 34.20  ? 158 ARG B C   1 
ATOM 6085 O O   . ARG B 2 158 ? 4.155   5.291   -65.182 1.00 39.32  ? 158 ARG B O   1 
ATOM 6086 C CB  . ARG B 2 158 ? 2.801   3.476   -67.289 1.00 38.49  ? 158 ARG B CB  1 
ATOM 6087 C CG  . ARG B 2 158 ? 3.199   4.006   -68.654 1.00 35.44  ? 158 ARG B CG  1 
ATOM 6088 C CD  . ARG B 2 158 ? 2.174   4.977   -69.197 1.00 41.99  ? 158 ARG B CD  1 
ATOM 6089 N NE  . ARG B 2 158 ? 2.565   5.511   -70.495 1.00 48.39  ? 158 ARG B NE  1 
ATOM 6090 C CZ  . ARG B 2 158 ? 3.034   6.734   -70.686 1.00 50.22  ? 158 ARG B CZ  1 
ATOM 6091 N NH1 . ARG B 2 158 ? 3.191   7.579   -69.681 1.00 46.01  ? 158 ARG B NH1 1 
ATOM 6092 N NH2 . ARG B 2 158 ? 3.355   7.121   -71.917 1.00 50.93  ? 158 ARG B NH2 1 
ATOM 6093 N N   . GLN B 2 159 ? 5.824   4.797   -66.612 1.00 39.18  ? 159 GLN B N   1 
ATOM 6094 C CA  . GLN B 2 159 ? 6.554   6.040   -66.409 1.00 43.45  ? 159 GLN B CA  1 
ATOM 6095 C C   . GLN B 2 159 ? 6.554   6.832   -67.707 1.00 45.31  ? 159 GLN B C   1 
ATOM 6096 O O   . GLN B 2 159 ? 6.640   6.252   -68.794 1.00 47.67  ? 159 GLN B O   1 
ATOM 6097 C CB  . GLN B 2 159 ? 7.985   5.770   -65.942 1.00 47.13  ? 159 GLN B CB  1 
ATOM 6098 C CG  . GLN B 2 159 ? 8.090   4.684   -64.889 1.00 40.09  ? 159 GLN B CG  1 
ATOM 6099 C CD  . GLN B 2 159 ? 7.492   5.103   -63.564 1.00 45.95  ? 159 GLN B CD  1 
ATOM 6100 O OE1 . GLN B 2 159 ? 7.543   6.273   -63.189 1.00 51.98  ? 159 GLN B OE1 1 
ATOM 6101 N NE2 . GLN B 2 159 ? 6.920   4.146   -62.845 1.00 41.94  ? 159 GLN B NE2 1 
ATOM 6102 N N   . GLN B 2 160 ? 6.439   8.150   -67.590 1.00 55.01  ? 160 GLN B N   1 
ATOM 6103 C CA  . GLN B 2 160 ? 6.414   9.019   -68.753 1.00 54.85  ? 160 GLN B CA  1 
ATOM 6104 C C   . GLN B 2 160 ? 7.794   9.617   -69.002 1.00 59.06  ? 160 GLN B C   1 
ATOM 6105 O O   . GLN B 2 160 ? 8.568   9.855   -68.070 1.00 65.82  ? 160 GLN B O   1 
ATOM 6106 C CB  . GLN B 2 160 ? 5.376   10.127  -68.564 1.00 57.68  ? 160 GLN B CB  1 
ATOM 6107 C CG  . GLN B 2 160 ? 5.328   11.156  -69.681 1.00 63.65  ? 160 GLN B CG  1 
ATOM 6108 C CD  . GLN B 2 160 ? 4.631   10.638  -70.921 1.00 62.42  ? 160 GLN B CD  1 
ATOM 6109 O OE1 . GLN B 2 160 ? 3.968   9.603   -70.885 1.00 57.83  ? 160 GLN B OE1 1 
ATOM 6110 N NE2 . GLN B 2 160 ? 4.781   11.354  -72.027 1.00 65.45  ? 160 GLN B NE2 1 
ATOM 6111 N N   . VAL B 2 161 ? 8.104   9.842   -70.281 1.00 58.25  ? 161 VAL B N   1 
ATOM 6112 C CA  . VAL B 2 161 ? 9.366   10.467  -70.656 1.00 59.63  ? 161 VAL B CA  1 
ATOM 6113 C C   . VAL B 2 161 ? 9.482   11.841  -70.002 1.00 65.63  ? 161 VAL B C   1 
ATOM 6114 O O   . VAL B 2 161 ? 8.582   12.680  -70.079 1.00 66.23  ? 161 VAL B O   1 
ATOM 6115 C CB  . VAL B 2 161 ? 9.499   10.569  -72.186 1.00 64.32  ? 161 VAL B CB  1 
ATOM 6116 C CG1 . VAL B 2 161 ? 9.988   9.260   -72.764 1.00 60.68  ? 161 VAL B CG1 1 
ATOM 6117 C CG2 . VAL B 2 161 ? 8.167   10.958  -72.808 1.00 70.00  ? 161 VAL B CG2 1 
ATOM 6118 N N   . GLY B 2 162 ? 10.615  12.064  -69.344 1.00 67.52  ? 162 GLY B N   1 
ATOM 6119 C CA  . GLY B 2 162 ? 10.883  13.336  -68.705 1.00 64.77  ? 162 GLY B CA  1 
ATOM 6120 C C   . GLY B 2 162 ? 10.414  13.399  -67.267 1.00 66.50  ? 162 GLY B C   1 
ATOM 6121 O O   . GLY B 2 162 ? 10.876  14.246  -66.496 1.00 71.86  ? 162 GLY B O   1 
ATOM 6122 N N   . ARG B 2 163 ? 9.494   12.512  -66.891 1.00 71.08  ? 163 ARG B N   1 
ATOM 6123 C CA  . ARG B 2 163 ? 8.987   12.450  -65.526 1.00 68.18  ? 163 ARG B CA  1 
ATOM 6124 C C   . ARG B 2 163 ? 9.609   11.319  -64.718 1.00 69.99  ? 163 ARG B C   1 
ATOM 6125 O O   . ARG B 2 163 ? 10.227  11.567  -63.679 1.00 68.96  ? 163 ARG B O   1 
ATOM 6126 C CB  . ARG B 2 163 ? 7.462   12.301  -65.538 1.00 67.51  ? 163 ARG B CB  1 
ATOM 6127 C CG  . ARG B 2 163 ? 6.764   13.106  -66.618 1.00 66.33  ? 163 ARG B CG  1 
ATOM 6128 C CD  . ARG B 2 163 ? 5.284   13.275  -66.304 1.00 69.72  ? 163 ARG B CD  1 
ATOM 6129 N NE  . ARG B 2 163 ? 5.034   13.484  -64.881 1.00 71.27  ? 163 ARG B NE  1 
ATOM 6130 C CZ  . ARG B 2 163 ? 5.362   14.579  -64.207 1.00 69.85  ? 163 ARG B CZ  1 
ATOM 6131 N NH1 . ARG B 2 163 ? 5.941   15.611  -64.799 1.00 67.68  ? 163 ARG B NH1 1 
ATOM 6132 N NH2 . ARG B 2 163 ? 5.096   14.642  -62.905 1.00 67.18  ? 163 ARG B NH2 1 
ATOM 6133 N N   . GLY B 2 164 ? 9.460   10.079  -65.175 1.00 56.77  ? 164 GLY B N   1 
ATOM 6134 C CA  . GLY B 2 164 ? 10.017  8.948   -64.465 1.00 55.80  ? 164 GLY B CA  1 
ATOM 6135 C C   . GLY B 2 164 ? 11.332  8.482   -65.047 1.00 58.82  ? 164 GLY B C   1 
ATOM 6136 O O   . GLY B 2 164 ? 12.051  7.693   -64.428 1.00 62.34  ? 164 GLY B O   1 
ATOM 6137 N N   . PHE B 2 165 ? 11.660  8.974   -66.240 1.00 61.78  ? 165 PHE B N   1 
ATOM 6138 C CA  . PHE B 2 165 ? 12.883  8.582   -66.923 1.00 58.15  ? 165 PHE B CA  1 
ATOM 6139 C C   . PHE B 2 165 ? 13.107  9.512   -68.103 1.00 61.58  ? 165 PHE B C   1 
ATOM 6140 O O   . PHE B 2 165 ? 12.158  10.064  -68.667 1.00 60.85  ? 165 PHE B O   1 
ATOM 6141 C CB  . PHE B 2 165 ? 12.823  7.129   -67.408 1.00 54.35  ? 165 PHE B CB  1 
ATOM 6142 C CG  . PHE B 2 165 ? 11.869  6.912   -68.547 1.00 57.79  ? 165 PHE B CG  1 
ATOM 6143 C CD1 . PHE B 2 165 ? 10.504  6.869   -68.326 1.00 55.61  ? 165 PHE B CD1 1 
ATOM 6144 C CD2 . PHE B 2 165 ? 12.339  6.753   -69.839 1.00 60.88  ? 165 PHE B CD2 1 
ATOM 6145 C CE1 . PHE B 2 165 ? 9.628   6.670   -69.372 1.00 60.40  ? 165 PHE B CE1 1 
ATOM 6146 C CE2 . PHE B 2 165 ? 11.465  6.553   -70.888 1.00 57.44  ? 165 PHE B CE2 1 
ATOM 6147 C CZ  . PHE B 2 165 ? 10.108  6.510   -70.653 1.00 61.71  ? 165 PHE B CZ  1 
ATOM 6148 N N   . THR B 2 166 ? 14.374  9.678   -68.469 1.00 70.63  ? 166 THR B N   1 
ATOM 6149 C CA  . THR B 2 166 ? 14.765  10.423  -69.656 1.00 68.09  ? 166 THR B CA  1 
ATOM 6150 C C   . THR B 2 166 ? 15.602  9.522   -70.551 1.00 69.73  ? 166 THR B C   1 
ATOM 6151 O O   . THR B 2 166 ? 16.573  8.912   -70.091 1.00 71.20  ? 166 THR B O   1 
ATOM 6152 C CB  . THR B 2 166 ? 15.553  11.681  -69.287 1.00 68.40  ? 166 THR B CB  1 
ATOM 6153 O OG1 . THR B 2 166 ? 16.627  11.334  -68.405 1.00 70.62  ? 166 THR B OG1 1 
ATOM 6154 C CG2 . THR B 2 166 ? 14.647  12.695  -68.604 1.00 65.16  ? 166 THR B CG2 1 
ATOM 6155 N N   . PHE B 2 167 ? 15.223  9.436   -71.822 1.00 81.87  ? 167 PHE B N   1 
ATOM 6156 C CA  . PHE B 2 167 ? 15.934  8.625   -72.799 1.00 82.83  ? 167 PHE B CA  1 
ATOM 6157 C C   . PHE B 2 167 ? 16.782  9.517   -73.693 1.00 83.81  ? 167 PHE B C   1 
ATOM 6158 O O   . PHE B 2 167 ? 16.270  10.468  -74.294 1.00 84.90  ? 167 PHE B O   1 
ATOM 6159 C CB  . PHE B 2 167 ? 14.959  7.809   -73.649 1.00 84.87  ? 167 PHE B CB  1 
ATOM 6160 C CG  . PHE B 2 167 ? 15.618  7.049   -74.763 1.00 83.78  ? 167 PHE B CG  1 
ATOM 6161 C CD1 . PHE B 2 167 ? 16.443  5.970   -74.494 1.00 82.33  ? 167 PHE B CD1 1 
ATOM 6162 C CD2 . PHE B 2 167 ? 15.409  7.414   -76.083 1.00 83.92  ? 167 PHE B CD2 1 
ATOM 6163 C CE1 . PHE B 2 167 ? 17.049  5.271   -75.519 1.00 83.12  ? 167 PHE B CE1 1 
ATOM 6164 C CE2 . PHE B 2 167 ? 16.013  6.718   -77.112 1.00 84.77  ? 167 PHE B CE2 1 
ATOM 6165 C CZ  . PHE B 2 167 ? 16.833  5.645   -76.829 1.00 83.86  ? 167 PHE B CZ  1 
ATOM 6166 N N   . ASN B 2 168 ? 18.072  9.211   -73.777 1.00 90.29  ? 168 ASN B N   1 
ATOM 6167 C CA  . ASN B 2 168 ? 18.990  9.909   -74.672 1.00 91.53  ? 168 ASN B CA  1 
ATOM 6168 C C   . ASN B 2 168 ? 19.278  8.987   -75.858 1.00 93.85  ? 168 ASN B C   1 
ATOM 6169 O O   . ASN B 2 168 ? 19.558  7.797   -75.688 1.00 92.38  ? 168 ASN B O   1 
ATOM 6170 C CB  . ASN B 2 168 ? 20.242  10.382  -73.922 1.00 92.61  ? 168 ASN B CB  1 
ATOM 6171 C CG  . ASN B 2 168 ? 21.416  9.412   -73.995 1.00 95.13  ? 168 ASN B CG  1 
ATOM 6172 O OD1 . ASN B 2 168 ? 21.261  8.198   -73.870 1.00 96.98  ? 168 ASN B OD1 1 
ATOM 6173 N ND2 . ASN B 2 168 ? 22.609  9.959   -74.194 1.00 90.77  ? 168 ASN B ND2 1 
ATOM 6174 N N   . SER B 2 169 ? 19.118  9.529   -77.067 1.00 102.70 ? 169 SER B N   1 
ATOM 6175 C CA  . SER B 2 169 ? 19.289  8.719   -78.268 1.00 101.36 ? 169 SER B CA  1 
ATOM 6176 C C   . SER B 2 169 ? 20.760  8.551   -78.625 1.00 100.94 ? 169 SER B C   1 
ATOM 6177 O O   . SER B 2 169 ? 21.131  7.606   -79.329 1.00 101.26 ? 169 SER B O   1 
ATOM 6178 C CB  . SER B 2 169 ? 18.522  9.345   -79.433 1.00 101.39 ? 169 SER B CB  1 
ATOM 6179 O OG  . SER B 2 169 ? 18.524  10.759  -79.342 1.00 102.58 ? 169 SER B OG  1 
ATOM 6180 N N   . VAL B 2 170 ? 21.610  9.467   -78.163 1.00 103.01 ? 170 VAL B N   1 
ATOM 6181 C CA  . VAL B 2 170 ? 23.023  9.407   -78.518 1.00 104.82 ? 170 VAL B CA  1 
ATOM 6182 C C   . VAL B 2 170 ? 23.701  8.182   -77.916 1.00 105.44 ? 170 VAL B C   1 
ATOM 6183 O O   . VAL B 2 170 ? 24.403  7.448   -78.619 1.00 105.72 ? 170 VAL B O   1 
ATOM 6184 C CB  . VAL B 2 170 ? 23.731  10.701  -78.085 1.00 103.98 ? 170 VAL B CB  1 
ATOM 6185 C CG1 . VAL B 2 170 ? 25.106  10.793  -78.732 1.00 104.21 ? 170 VAL B CG1 1 
ATOM 6186 C CG2 . VAL B 2 170 ? 22.879  11.906  -78.443 1.00 103.40 ? 170 VAL B CG2 1 
ATOM 6187 N N   . ASN B 2 171 ? 23.497  7.934   -76.624 1.00 98.90  ? 171 ASN B N   1 
ATOM 6188 C CA  . ASN B 2 171 ? 24.167  6.848   -75.924 1.00 98.06  ? 171 ASN B CA  1 
ATOM 6189 C C   . ASN B 2 171 ? 23.290  5.600   -75.872 1.00 97.62  ? 171 ASN B C   1 
ATOM 6190 O O   . ASN B 2 171 ? 23.813  4.498   -75.686 1.00 97.62  ? 171 ASN B O   1 
ATOM 6191 C CB  . ASN B 2 171 ? 24.585  7.391   -74.531 1.00 97.92  ? 171 ASN B CB  1 
ATOM 6192 C CG  . ASN B 2 171 ? 24.744  6.339   -73.408 1.00 101.13 ? 171 ASN B CG  1 
ATOM 6193 O OD1 . ASN B 2 171 ? 24.827  5.136   -73.611 1.00 101.28 ? 171 ASN B OD1 1 
ATOM 6194 N ND2 . ASN B 2 171 ? 24.804  6.850   -72.181 1.00 100.07 ? 171 ASN B ND2 1 
ATOM 6195 N N   . LEU B 2 172 ? 21.999  5.735   -76.188 1.00 93.76  ? 172 LEU B N   1 
ATOM 6196 C CA  . LEU B 2 172 ? 21.028  4.643   -76.097 1.00 95.26  ? 172 LEU B CA  1 
ATOM 6197 C C   . LEU B 2 172 ? 20.839  4.193   -74.655 1.00 96.03  ? 172 LEU B C   1 
ATOM 6198 O O   . LEU B 2 172 ? 20.725  2.998   -74.370 1.00 97.75  ? 172 LEU B O   1 
ATOM 6199 C CB  . LEU B 2 172 ? 21.432  3.455   -76.976 1.00 92.88  ? 172 LEU B CB  1 
ATOM 6200 C CG  . LEU B 2 172 ? 20.638  3.221   -78.257 1.00 94.62  ? 172 LEU B CG  1 
ATOM 6201 C CD1 . LEU B 2 172 ? 20.655  4.458   -79.129 1.00 93.14  ? 172 LEU B CD1 1 
ATOM 6202 C CD2 . LEU B 2 172 ? 21.231  2.044   -79.007 1.00 95.44  ? 172 LEU B CD2 1 
ATOM 6203 N N   . THR B 2 173 ? 20.808  5.152   -73.737 1.00 86.87  ? 173 THR B N   1 
ATOM 6204 C CA  . THR B 2 173 ? 20.717  4.885   -72.313 1.00 86.18  ? 173 THR B CA  1 
ATOM 6205 C C   . THR B 2 173 ? 19.520  5.613   -71.718 1.00 89.97  ? 173 THR B C   1 
ATOM 6206 O O   . THR B 2 173 ? 19.300  6.796   -71.997 1.00 88.35  ? 173 THR B O   1 
ATOM 6207 C CB  . THR B 2 173 ? 22.003  5.315   -71.606 1.00 87.42  ? 173 THR B CB  1 
ATOM 6208 O OG1 . THR B 2 173 ? 22.994  4.290   -71.752 1.00 87.29  ? 173 THR B OG1 1 
ATOM 6209 C CG2 . THR B 2 173 ? 21.757  5.575   -70.141 1.00 86.30  ? 173 THR B CG2 1 
ATOM 6210 N N   . VAL B 2 174 ? 18.751  4.899   -70.900 1.00 75.64  ? 174 VAL B N   1 
ATOM 6211 C CA  . VAL B 2 174 ? 17.588  5.449   -70.211 1.00 71.24  ? 174 VAL B CA  1 
ATOM 6212 C C   . VAL B 2 174 ? 18.025  5.868   -68.815 1.00 70.67  ? 174 VAL B C   1 
ATOM 6213 O O   . VAL B 2 174 ? 18.406  5.021   -67.999 1.00 67.65  ? 174 VAL B O   1 
ATOM 6214 C CB  . VAL B 2 174 ? 16.436  4.435   -70.141 1.00 66.08  ? 174 VAL B CB  1 
ATOM 6215 C CG1 . VAL B 2 174 ? 15.325  4.955   -69.244 1.00 69.00  ? 174 VAL B CG1 1 
ATOM 6216 C CG2 . VAL B 2 174 ? 15.906  4.137   -71.532 1.00 69.70  ? 174 VAL B CG2 1 
ATOM 6217 N N   . THR B 2 175 ? 17.963  7.169   -68.543 1.00 73.38  ? 175 THR B N   1 
ATOM 6218 C CA  . THR B 2 175 ? 18.301  7.698   -67.225 1.00 74.18  ? 175 THR B CA  1 
ATOM 6219 C C   . THR B 2 175 ? 17.044  7.686   -66.365 1.00 75.39  ? 175 THR B C   1 
ATOM 6220 O O   . THR B 2 175 ? 16.070  8.382   -66.664 1.00 75.98  ? 175 THR B O   1 
ATOM 6221 C CB  . THR B 2 175 ? 18.881  9.105   -67.343 1.00 70.70  ? 175 THR B CB  1 
ATOM 6222 O OG1 . THR B 2 175 ? 20.244  9.025   -67.778 1.00 73.57  ? 175 THR B OG1 1 
ATOM 6223 C CG2 . THR B 2 175 ? 18.831  9.822   -66.001 1.00 72.48  ? 175 THR B CG2 1 
ATOM 6224 N N   . LEU B 2 176 ? 17.062  6.890   -65.301 1.00 62.42  ? 176 LEU B N   1 
ATOM 6225 C CA  . LEU B 2 176 ? 15.884  6.704   -64.470 1.00 57.36  ? 176 LEU B CA  1 
ATOM 6226 C C   . LEU B 2 176 ? 15.818  7.756   -63.370 1.00 61.82  ? 176 LEU B C   1 
ATOM 6227 O O   . LEU B 2 176 ? 16.839  8.268   -62.906 1.00 66.10  ? 176 LEU B O   1 
ATOM 6228 C CB  . LEU B 2 176 ? 15.886  5.306   -63.855 1.00 58.30  ? 176 LEU B CB  1 
ATOM 6229 C CG  . LEU B 2 176 ? 15.991  4.161   -64.862 1.00 56.78  ? 176 LEU B CG  1 
ATOM 6230 C CD1 . LEU B 2 176 ? 16.354  2.867   -64.165 1.00 49.49  ? 176 LEU B CD1 1 
ATOM 6231 C CD2 . LEU B 2 176 ? 14.689  4.008   -65.631 1.00 64.88  ? 176 LEU B CD2 1 
ATOM 6232 N N   . ALA B 2 177 ? 14.589  8.077   -62.957 1.00 54.91  ? 177 ALA B N   1 
ATOM 6233 C CA  . ALA B 2 177 ? 14.391  9.017   -61.860 1.00 54.15  ? 177 ALA B CA  1 
ATOM 6234 C C   . ALA B 2 177 ? 14.913  8.469   -60.539 1.00 60.72  ? 177 ALA B C   1 
ATOM 6235 O O   . ALA B 2 177 ? 15.474  9.226   -59.738 1.00 60.10  ? 177 ALA B O   1 
ATOM 6236 C CB  . ALA B 2 177 ? 12.910  9.374   -61.730 1.00 54.14  ? 177 ALA B CB  1 
ATOM 6237 N N   . GLN B 2 178 ? 14.740  7.172   -60.294 1.00 56.98  ? 178 GLN B N   1 
ATOM 6238 C CA  . GLN B 2 178 ? 15.238  6.528   -59.093 1.00 51.48  ? 178 GLN B CA  1 
ATOM 6239 C C   . GLN B 2 178 ? 16.275  5.468   -59.445 1.00 56.01  ? 178 GLN B C   1 
ATOM 6240 O O   . GLN B 2 178 ? 16.223  4.875   -60.526 1.00 65.10  ? 178 GLN B O   1 
ATOM 6241 C CB  . GLN B 2 178 ? 14.112  5.849   -58.305 1.00 54.92  ? 178 GLN B CB  1 
ATOM 6242 C CG  . GLN B 2 178 ? 13.055  6.771   -57.754 1.00 56.54  ? 178 GLN B CG  1 
ATOM 6243 C CD  . GLN B 2 178 ? 12.095  6.034   -56.847 1.00 60.17  ? 178 GLN B CD  1 
ATOM 6244 O OE1 . GLN B 2 178 ? 12.459  5.044   -56.214 1.00 59.38  ? 178 GLN B OE1 1 
ATOM 6245 N NE2 . GLN B 2 178 ? 10.859  6.504   -56.786 1.00 61.91  ? 178 GLN B NE2 1 
ATOM 6246 N N   . PRO B 2 179 ? 17.230  5.207   -58.555 1.00 59.09  ? 179 PRO B N   1 
ATOM 6247 C CA  . PRO B 2 179 ? 18.089  4.032   -58.733 1.00 58.12  ? 179 PRO B CA  1 
ATOM 6248 C C   . PRO B 2 179 ? 17.304  2.760   -58.463 1.00 53.95  ? 179 PRO B C   1 
ATOM 6249 O O   . PRO B 2 179 ? 16.570  2.653   -57.477 1.00 64.03  ? 179 PRO B O   1 
ATOM 6250 C CB  . PRO B 2 179 ? 19.206  4.228   -57.699 1.00 56.36  ? 179 PRO B CB  1 
ATOM 6251 C CG  . PRO B 2 179 ? 18.803  5.365   -56.839 1.00 57.56  ? 179 PRO B CG  1 
ATOM 6252 C CD  . PRO B 2 179 ? 17.564  6.002   -57.362 1.00 57.58  ? 179 PRO B CD  1 
ATOM 6253 N N   . LEU B 2 180 ? 17.456  1.790   -59.359 1.00 58.76  ? 180 LEU B N   1 
ATOM 6254 C CA  . LEU B 2 180 ? 16.712  0.545   -59.241 1.00 62.45  ? 180 LEU B CA  1 
ATOM 6255 C C   . LEU B 2 180 ? 17.180  -0.252  -58.032 1.00 64.51  ? 180 LEU B C   1 
ATOM 6256 O O   . LEU B 2 180 ? 18.360  -0.233  -57.673 1.00 70.36  ? 180 LEU B O   1 
ATOM 6257 C CB  . LEU B 2 180 ? 16.866  -0.293  -60.507 1.00 64.77  ? 180 LEU B CB  1 
ATOM 6258 C CG  . LEU B 2 180 ? 16.110  0.221   -61.731 1.00 65.99  ? 180 LEU B CG  1 
ATOM 6259 C CD1 . LEU B 2 180 ? 16.294  -0.725  -62.905 1.00 68.63  ? 180 LEU B CD1 1 
ATOM 6260 C CD2 . LEU B 2 180 ? 14.639  0.413   -61.407 1.00 58.99  ? 180 LEU B CD2 1 
ATOM 6261 N N   . GLU B 2 181 ? 16.244  -0.952  -57.403 1.00 56.95  ? 181 GLU B N   1 
ATOM 6262 C CA  . GLU B 2 181 ? 16.561  -1.822  -56.283 1.00 55.83  ? 181 GLU B CA  1 
ATOM 6263 C C   . GLU B 2 181 ? 16.702  -3.257  -56.787 1.00 59.18  ? 181 GLU B C   1 
ATOM 6264 O O   . GLU B 2 181 ? 16.382  -3.573  -57.935 1.00 63.52  ? 181 GLU B O   1 
ATOM 6265 C CB  . GLU B 2 181 ? 15.498  -1.691  -55.196 1.00 62.35  ? 181 GLU B CB  1 
ATOM 6266 C CG  . GLU B 2 181 ? 15.246  -0.259  -54.763 1.00 64.96  ? 181 GLU B CG  1 
ATOM 6267 C CD  . GLU B 2 181 ? 15.495  -0.051  -53.285 1.00 70.33  ? 181 GLU B CD  1 
ATOM 6268 O OE1 . GLU B 2 181 ? 14.597  0.476   -52.593 1.00 71.81  ? 181 GLU B OE1 1 
ATOM 6269 O OE2 . GLU B 2 181 ? 16.592  -0.414  -52.814 1.00 67.77  ? 181 GLU B OE2 1 
ATOM 6270 N N   . GLN B 2 182 ? 17.188  -4.144  -55.925 1.00 63.98  ? 182 GLN B N   1 
ATOM 6271 C CA  . GLN B 2 182 ? 17.434  -5.524  -56.312 1.00 64.44  ? 182 GLN B CA  1 
ATOM 6272 C C   . GLN B 2 182 ? 16.107  -6.226  -56.571 1.00 65.65  ? 182 GLN B C   1 
ATOM 6273 O O   . GLN B 2 182 ? 15.192  -6.184  -55.744 1.00 67.06  ? 182 GLN B O   1 
ATOM 6274 C CB  . GLN B 2 182 ? 18.228  -6.236  -55.210 1.00 64.67  ? 182 GLN B CB  1 
ATOM 6275 C CG  . GLN B 2 182 ? 18.902  -7.573  -55.563 1.00 63.91  ? 182 GLN B CG  1 
ATOM 6276 C CD  . GLN B 2 182 ? 17.984  -8.590  -56.208 1.00 71.04  ? 182 GLN B CD  1 
ATOM 6277 O OE1 . GLN B 2 182 ? 17.116  -9.165  -55.553 1.00 71.41  ? 182 GLN B OE1 1 
ATOM 6278 N NE2 . GLN B 2 182 ? 18.181  -8.828  -57.501 1.00 72.46  ? 182 GLN B NE2 1 
ATOM 6279 N N   . GLY B 2 183 ? 16.006  -6.872  -57.732 1.00 65.42  ? 183 GLY B N   1 
ATOM 6280 C CA  . GLY B 2 183 ? 14.829  -7.632  -58.100 1.00 66.56  ? 183 GLY B CA  1 
ATOM 6281 C C   . GLY B 2 183 ? 13.715  -6.835  -58.741 1.00 66.08  ? 183 GLY B C   1 
ATOM 6282 O O   . GLY B 2 183 ? 12.640  -7.396  -58.979 1.00 71.52  ? 183 GLY B O   1 
ATOM 6283 N N   . ASP B 2 184 ? 13.925  -5.553  -59.026 1.00 58.34  ? 184 ASP B N   1 
ATOM 6284 C CA  . ASP B 2 184 ? 12.893  -4.738  -59.648 1.00 60.13  ? 184 ASP B CA  1 
ATOM 6285 C C   . ASP B 2 184 ? 12.629  -5.197  -61.076 1.00 57.94  ? 184 ASP B C   1 
ATOM 6286 O O   . ASP B 2 184 ? 13.558  -5.425  -61.854 1.00 63.09  ? 184 ASP B O   1 
ATOM 6287 C CB  . ASP B 2 184 ? 13.297  -3.264  -59.645 1.00 62.81  ? 184 ASP B CB  1 
ATOM 6288 C CG  . ASP B 2 184 ? 13.185  -2.633  -58.274 1.00 68.89  ? 184 ASP B CG  1 
ATOM 6289 O OD1 . ASP B 2 184 ? 12.484  -3.204  -57.412 1.00 70.23  ? 184 ASP B OD1 1 
ATOM 6290 O OD2 . ASP B 2 184 ? 13.791  -1.564  -58.059 1.00 73.81  ? 184 ASP B OD2 1 
ATOM 6291 N N   . GLU B 2 185 ? 11.348  -5.332  -61.413 1.00 48.05  ? 185 GLU B N   1 
ATOM 6292 C CA  . GLU B 2 185 ? 10.944  -5.667  -62.772 1.00 47.71  ? 185 GLU B CA  1 
ATOM 6293 C C   . GLU B 2 185 ? 10.715  -4.385  -63.559 1.00 48.78  ? 185 GLU B C   1 
ATOM 6294 O O   . GLU B 2 185 ? 9.780   -3.632  -63.271 1.00 54.07  ? 185 GLU B O   1 
ATOM 6295 C CB  . GLU B 2 185 ? 9.679   -6.522  -62.761 1.00 45.50  ? 185 GLU B CB  1 
ATOM 6296 C CG  . GLU B 2 185 ? 9.139   -6.835  -64.144 1.00 49.38  ? 185 GLU B CG  1 
ATOM 6297 C CD  . GLU B 2 185 ? 7.632   -6.697  -64.226 1.00 58.16  ? 185 GLU B CD  1 
ATOM 6298 O OE1 . GLU B 2 185 ? 7.144   -5.551  -64.319 1.00 60.44  ? 185 GLU B OE1 1 
ATOM 6299 O OE2 . GLU B 2 185 ? 6.935   -7.733  -64.199 1.00 57.61  ? 185 GLU B OE2 1 
ATOM 6300 N N   . VAL B 2 186 ? 11.565  -4.138  -64.550 1.00 48.43  ? 186 VAL B N   1 
ATOM 6301 C CA  . VAL B 2 186 ? 11.464  -2.960  -65.400 1.00 48.28  ? 186 VAL B CA  1 
ATOM 6302 C C   . VAL B 2 186 ? 11.278  -3.433  -66.832 1.00 46.11  ? 186 VAL B C   1 
ATOM 6303 O O   . VAL B 2 186 ? 12.158  -4.100  -67.391 1.00 54.90  ? 186 VAL B O   1 
ATOM 6304 C CB  . VAL B 2 186 ? 12.699  -2.057  -65.277 1.00 42.58  ? 186 VAL B CB  1 
ATOM 6305 C CG1 . VAL B 2 186 ? 12.625  -0.922  -66.284 1.00 41.88  ? 186 VAL B CG1 1 
ATOM 6306 C CG2 . VAL B 2 186 ? 12.811  -1.515  -63.866 1.00 49.77  ? 186 VAL B CG2 1 
ATOM 6307 N N   . VAL B 2 187 ? 10.140  -3.091  -67.423 1.00 38.76  ? 187 VAL B N   1 
ATOM 6308 C CA  . VAL B 2 187 ? 9.842   -3.418  -68.811 1.00 40.36  ? 187 VAL B CA  1 
ATOM 6309 C C   . VAL B 2 187 ? 9.981   -2.136  -69.618 1.00 44.97  ? 187 VAL B C   1 
ATOM 6310 O O   . VAL B 2 187 ? 9.213   -1.187  -69.434 1.00 54.92  ? 187 VAL B O   1 
ATOM 6311 C CB  . VAL B 2 187 ? 8.444   -4.029  -68.965 1.00 46.04  ? 187 VAL B CB  1 
ATOM 6312 C CG1 . VAL B 2 187 ? 8.145   -4.288  -70.432 1.00 47.99  ? 187 VAL B CG1 1 
ATOM 6313 C CG2 . VAL B 2 187 ? 8.339   -5.313  -68.160 1.00 51.24  ? 187 VAL B CG2 1 
ATOM 6314 N N   . LEU B 2 188 ? 10.963  -2.107  -70.512 1.00 54.76  ? 188 LEU B N   1 
ATOM 6315 C CA  . LEU B 2 188 ? 11.239  -0.929  -71.318 1.00 48.51  ? 188 LEU B CA  1 
ATOM 6316 C C   . LEU B 2 188 ? 10.552  -1.056  -72.671 1.00 58.63  ? 188 LEU B C   1 
ATOM 6317 O O   . LEU B 2 188 ? 10.750  -2.043  -73.384 1.00 70.31  ? 188 LEU B O   1 
ATOM 6318 C CB  . LEU B 2 188 ? 12.744  -0.742  -71.509 1.00 52.35  ? 188 LEU B CB  1 
ATOM 6319 C CG  . LEU B 2 188 ? 13.607  -0.554  -70.257 1.00 55.43  ? 188 LEU B CG  1 
ATOM 6320 C CD1 . LEU B 2 188 ? 14.081  -1.881  -69.689 1.00 58.92  ? 188 LEU B CD1 1 
ATOM 6321 C CD2 . LEU B 2 188 ? 14.780  0.360   -70.565 1.00 62.56  ? 188 LEU B CD2 1 
ATOM 6322 N N   . MET B 2 189 ? 9.745   -0.059  -73.015 1.00 64.77  ? 189 MET B N   1 
ATOM 6323 C CA  . MET B 2 189 ? 9.111   0.004   -74.325 1.00 63.10  ? 189 MET B CA  1 
ATOM 6324 C C   . MET B 2 189 ? 10.048  0.711   -75.294 1.00 68.34  ? 189 MET B C   1 
ATOM 6325 O O   . MET B 2 189 ? 10.411  1.870   -75.079 1.00 71.23  ? 189 MET B O   1 
ATOM 6326 C CB  . MET B 2 189 ? 7.770   0.727   -74.248 1.00 65.48  ? 189 MET B CB  1 
ATOM 6327 C CG  . MET B 2 189 ? 6.749   0.015   -73.396 1.00 69.74  ? 189 MET B CG  1 
ATOM 6328 S SD  . MET B 2 189 ? 6.558   -1.688  -73.943 1.00 80.15  ? 189 MET B SD  1 
ATOM 6329 C CE  . MET B 2 189 ? 4.779   -1.800  -74.019 1.00 69.60  ? 189 MET B CE  1 
ATOM 6330 N N   . LEU B 2 190 ? 10.471  -0.017  -76.323 1.00 75.75  ? 190 LEU B N   1 
ATOM 6331 C CA  . LEU B 2 190 ? 11.417  0.564   -77.301 1.00 74.82  ? 190 LEU B CA  1 
ATOM 6332 C C   . LEU B 2 190 ? 10.640  0.983   -78.550 1.00 77.50  ? 190 LEU B C   1 
ATOM 6333 O O   . LEU B 2 190 ? 9.719   0.244   -78.950 1.00 76.75  ? 190 LEU B O   1 
ATOM 6334 C CB  . LEU B 2 190 ? 12.478  -0.480  -77.628 1.00 78.65  ? 190 LEU B CB  1 
ATOM 6335 C CG  . LEU B 2 190 ? 12.993  -1.306  -76.449 1.00 76.40  ? 190 LEU B CG  1 
ATOM 6336 C CD1 . LEU B 2 190 ? 13.872  -2.403  -77.007 1.00 79.27  ? 190 LEU B CD1 1 
ATOM 6337 C CD2 . LEU B 2 190 ? 13.765  -0.435  -75.475 1.00 71.14  ? 190 LEU B CD2 1 
ATOM 6338 N N   . SER B 2 191 ? 11.007  2.123   -79.134 1.00 90.81  ? 191 SER B N   1 
ATOM 6339 C CA  . SER B 2 191 ? 10.350  2.590   -80.380 1.00 92.71  ? 191 SER B CA  1 
ATOM 6340 C C   . SER B 2 191 ? 11.367  2.549   -81.527 1.00 96.48  ? 191 SER B C   1 
ATOM 6341 O O   . SER B 2 191 ? 12.000  3.591   -81.794 1.00 95.59  ? 191 SER B O   1 
ATOM 6342 C CB  . SER B 2 191 ? 9.775   3.965   -80.201 1.00 91.76  ? 191 SER B CB  1 
ATOM 6343 O OG  . SER B 2 191 ? 8.630   4.143   -81.023 1.00 91.03  ? 191 SER B OG  1 
# 
