data_4BDV # _entry.id 4BDV # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4BDV PDBE EBI-54271 WWPDB D_1290054271 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1CFG unspecified . PDB 1D7P unspecified 'CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN FACTOR VIII AT 1.5 A RESOLUTION AT 1.5 A' PDB 1IQD unspecified 'HUMAN FACTOR VIII C2 DOMAIN COMPLEXED TO HUMAN MONOCLONALBO2C11 FAB.' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4BDV _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-10-08 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Svensson, L.A.' 1 'Thim, L.' 2 'Olsen, O.H.' 3 'Nicolaisen, E.M.' 4 # _citation.id primary _citation.title ;Evaluation of the Metal Binding Sites in a Recombinant Coagulation Factor Viii Identifies Two Sites with Unique Metal Binding Properties. ; _citation.journal_abbrev Biol.Chem. _citation.journal_volume 394 _citation.page_first 761 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM ? _citation.country GE _citation.journal_id_ISSN 1431-6730 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23435097 _citation.pdbx_database_id_DOI 10.1515/HSZ-2012-0298 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Svensson, L.A.' 1 primary 'Thim, L.' 2 primary 'Olsen, O.H.' 3 primary 'Nicolaisen, E.M.' 4 # _cell.entry_id 4BDV _cell.length_a 133.840 _cell.length_b 133.840 _cell.length_c 355.810 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BDV _symmetry.space_group_name_H-M 'P 41 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 92 # 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 'FACTOR VIIIA HEAVY CHAIN, 92 KDA ISOFORM, B DOMAIN' 87107.391 1 ? ? 'COAGULATION FACTOR VIII, RESIDUES 20-769,1657-1666' 'THE FVIII B-DOMAIN HAS BEEN REPLACED WITH A TRUNCATED, 21 AMINO ACID LONG, B-DOMAIN VARIANT.' 2 polymer man 'FACTOR VIIIA LIGHT CHAIN' 79241.797 1 ? ? 'RESIDUES 1667-2351' ? 3 non-polymer syn 'ZINC ION' 65.409 1 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 6 non-polymer syn 1,2-ETHANEDIOL 62.068 2 ? ? ? ? 7 non-polymer syn 'COPPER (I) ION' 63.546 1 ? ? ? ? 8 non-polymer man BETA-D-MANNOSE 180.156 3 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'COAGULATION FACTOR VIII, ANTIHEMOPHILIC FACTOR, AHF, PROCOAGULANT COMPONENT' 2 'COAGULATION FACTOR VIII, ANTIHEMOPHILIC FACTOR, AHF, PROCOAGULANT COMPONENT' # 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 ;ATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEV YDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLS HVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNR SLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGM EAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVL APDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGI TDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVD QRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYIL SIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYE DSYEDISAYLLSKNNAIEPRSFSQNSRHPSQNPPVLKRHQ ; ;ATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEV YDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLS HVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNR SLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGM EAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVL APDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGI TDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVD QRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYIL SIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYE DSYEDISAYLLSKNNAIEPRSFSQNSRHPSQNPPVLKRHQ ; A ? 2 'polypeptide(L)' no no ;REITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSV PQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFV KPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETK SWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRK KEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWA PKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFF GNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSK ARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQ DSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY ; ;REITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSV PQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFV KPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETK SWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRK KEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWA PKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFF GNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSK ARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQ DSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 THR n 1 3 ARG n 1 4 ARG n 1 5 TYR n 1 6 TYR n 1 7 LEU n 1 8 GLY n 1 9 ALA n 1 10 VAL n 1 11 GLU n 1 12 LEU n 1 13 SER n 1 14 TRP n 1 15 ASP n 1 16 TYR n 1 17 MET n 1 18 GLN n 1 19 SER n 1 20 ASP n 1 21 LEU n 1 22 GLY n 1 23 GLU n 1 24 LEU n 1 25 PRO n 1 26 VAL n 1 27 ASP n 1 28 ALA n 1 29 ARG n 1 30 PHE n 1 31 PRO n 1 32 PRO n 1 33 ARG n 1 34 VAL n 1 35 PRO n 1 36 LYS n 1 37 SER n 1 38 PHE n 1 39 PRO n 1 40 PHE n 1 41 ASN n 1 42 THR n 1 43 SER n 1 44 VAL n 1 45 VAL n 1 46 TYR n 1 47 LYS n 1 48 LYS n 1 49 THR n 1 50 LEU n 1 51 PHE n 1 52 VAL n 1 53 GLU n 1 54 PHE n 1 55 THR n 1 56 ASP n 1 57 HIS n 1 58 LEU n 1 59 PHE n 1 60 ASN n 1 61 ILE n 1 62 ALA n 1 63 LYS n 1 64 PRO n 1 65 ARG n 1 66 PRO n 1 67 PRO n 1 68 TRP n 1 69 MET n 1 70 GLY n 1 71 LEU n 1 72 LEU n 1 73 GLY n 1 74 PRO n 1 75 THR n 1 76 ILE n 1 77 GLN n 1 78 ALA n 1 79 GLU n 1 80 VAL n 1 81 TYR n 1 82 ASP n 1 83 THR n 1 84 VAL n 1 85 VAL n 1 86 ILE n 1 87 THR n 1 88 LEU n 1 89 LYS n 1 90 ASN n 1 91 MET n 1 92 ALA n 1 93 SER n 1 94 HIS n 1 95 PRO n 1 96 VAL n 1 97 SER n 1 98 LEU n 1 99 HIS n 1 100 ALA n 1 101 VAL n 1 102 GLY n 1 103 VAL n 1 104 SER n 1 105 TYR n 1 106 TRP n 1 107 LYS n 1 108 ALA n 1 109 SER n 1 110 GLU n 1 111 GLY n 1 112 ALA n 1 113 GLU n 1 114 TYR n 1 115 ASP n 1 116 ASP n 1 117 GLN n 1 118 THR n 1 119 SER n 1 120 GLN n 1 121 ARG n 1 122 GLU n 1 123 LYS n 1 124 GLU n 1 125 ASP n 1 126 ASP n 1 127 LYS n 1 128 VAL n 1 129 PHE n 1 130 PRO n 1 131 GLY n 1 132 GLY n 1 133 SER n 1 134 HIS n 1 135 THR n 1 136 TYR n 1 137 VAL n 1 138 TRP n 1 139 GLN n 1 140 VAL n 1 141 LEU n 1 142 LYS n 1 143 GLU n 1 144 ASN n 1 145 GLY n 1 146 PRO n 1 147 MET n 1 148 ALA n 1 149 SER n 1 150 ASP n 1 151 PRO n 1 152 LEU n 1 153 CYS n 1 154 LEU n 1 155 THR n 1 156 TYR n 1 157 SER n 1 158 TYR n 1 159 LEU n 1 160 SER n 1 161 HIS n 1 162 VAL n 1 163 ASP n 1 164 LEU n 1 165 VAL n 1 166 LYS n 1 167 ASP n 1 168 LEU n 1 169 ASN n 1 170 SER n 1 171 GLY n 1 172 LEU n 1 173 ILE n 1 174 GLY n 1 175 ALA n 1 176 LEU n 1 177 LEU n 1 178 VAL n 1 179 CYS n 1 180 ARG n 1 181 GLU n 1 182 GLY n 1 183 SER n 1 184 LEU n 1 185 ALA n 1 186 LYS n 1 187 GLU n 1 188 LYS n 1 189 THR n 1 190 GLN n 1 191 THR n 1 192 LEU n 1 193 HIS n 1 194 LYS n 1 195 PHE n 1 196 ILE n 1 197 LEU n 1 198 LEU n 1 199 PHE n 1 200 ALA n 1 201 VAL n 1 202 PHE n 1 203 ASP n 1 204 GLU n 1 205 GLY n 1 206 LYS n 1 207 SER n 1 208 TRP n 1 209 HIS n 1 210 SER n 1 211 GLU n 1 212 THR n 1 213 LYS n 1 214 ASN n 1 215 SER n 1 216 LEU n 1 217 MET n 1 218 GLN n 1 219 ASP n 1 220 ARG n 1 221 ASP n 1 222 ALA n 1 223 ALA n 1 224 SER n 1 225 ALA n 1 226 ARG n 1 227 ALA n 1 228 TRP n 1 229 PRO n 1 230 LYS n 1 231 MET n 1 232 HIS n 1 233 THR n 1 234 VAL n 1 235 ASN n 1 236 GLY n 1 237 TYR n 1 238 VAL n 1 239 ASN n 1 240 ARG n 1 241 SER n 1 242 LEU n 1 243 PRO n 1 244 GLY n 1 245 LEU n 1 246 ILE n 1 247 GLY n 1 248 CYS n 1 249 HIS n 1 250 ARG n 1 251 LYS n 1 252 SER n 1 253 VAL n 1 254 TYR n 1 255 TRP n 1 256 HIS n 1 257 VAL n 1 258 ILE n 1 259 GLY n 1 260 MET n 1 261 GLY n 1 262 THR n 1 263 THR n 1 264 PRO n 1 265 GLU n 1 266 VAL n 1 267 HIS n 1 268 SER n 1 269 ILE n 1 270 PHE n 1 271 LEU n 1 272 GLU n 1 273 GLY n 1 274 HIS n 1 275 THR n 1 276 PHE n 1 277 LEU n 1 278 VAL n 1 279 ARG n 1 280 ASN n 1 281 HIS n 1 282 ARG n 1 283 GLN n 1 284 ALA n 1 285 SER n 1 286 LEU n 1 287 GLU n 1 288 ILE n 1 289 SER n 1 290 PRO n 1 291 ILE n 1 292 THR n 1 293 PHE n 1 294 LEU n 1 295 THR n 1 296 ALA n 1 297 GLN n 1 298 THR n 1 299 LEU n 1 300 LEU n 1 301 MET n 1 302 ASP n 1 303 LEU n 1 304 GLY n 1 305 GLN n 1 306 PHE n 1 307 LEU n 1 308 LEU n 1 309 PHE n 1 310 CYS n 1 311 HIS n 1 312 ILE n 1 313 SER n 1 314 SER n 1 315 HIS n 1 316 GLN n 1 317 HIS n 1 318 ASP n 1 319 GLY n 1 320 MET n 1 321 GLU n 1 322 ALA n 1 323 TYR n 1 324 VAL n 1 325 LYS n 1 326 VAL n 1 327 ASP n 1 328 SER n 1 329 CYS n 1 330 PRO n 1 331 GLU n 1 332 GLU n 1 333 PRO n 1 334 GLN n 1 335 LEU n 1 336 ARG n 1 337 MET n 1 338 LYS n 1 339 ASN n 1 340 ASN n 1 341 GLU n 1 342 GLU n 1 343 ALA n 1 344 GLU n 1 345 ASP n 1 346 TYR n 1 347 ASP n 1 348 ASP n 1 349 ASP n 1 350 LEU n 1 351 THR n 1 352 ASP n 1 353 SER n 1 354 GLU n 1 355 MET n 1 356 ASP n 1 357 VAL n 1 358 VAL n 1 359 ARG n 1 360 PHE n 1 361 ASP n 1 362 ASP n 1 363 ASP n 1 364 ASN n 1 365 SER n 1 366 PRO n 1 367 SER n 1 368 PHE n 1 369 ILE n 1 370 GLN n 1 371 ILE n 1 372 ARG n 1 373 SER n 1 374 VAL n 1 375 ALA n 1 376 LYS n 1 377 LYS n 1 378 HIS n 1 379 PRO n 1 380 LYS n 1 381 THR n 1 382 TRP n 1 383 VAL n 1 384 HIS n 1 385 TYR n 1 386 ILE n 1 387 ALA n 1 388 ALA n 1 389 GLU n 1 390 GLU n 1 391 GLU n 1 392 ASP n 1 393 TRP n 1 394 ASP n 1 395 TYR n 1 396 ALA n 1 397 PRO n 1 398 LEU n 1 399 VAL n 1 400 LEU n 1 401 ALA n 1 402 PRO n 1 403 ASP n 1 404 ASP n 1 405 ARG n 1 406 SER n 1 407 TYR n 1 408 LYS n 1 409 SER n 1 410 GLN n 1 411 TYR n 1 412 LEU n 1 413 ASN n 1 414 ASN n 1 415 GLY n 1 416 PRO n 1 417 GLN n 1 418 ARG n 1 419 ILE n 1 420 GLY n 1 421 ARG n 1 422 LYS n 1 423 TYR n 1 424 LYS n 1 425 LYS n 1 426 VAL n 1 427 ARG n 1 428 PHE n 1 429 MET n 1 430 ALA n 1 431 TYR n 1 432 THR n 1 433 ASP n 1 434 GLU n 1 435 THR n 1 436 PHE n 1 437 LYS n 1 438 THR n 1 439 ARG n 1 440 GLU n 1 441 ALA n 1 442 ILE n 1 443 GLN n 1 444 HIS n 1 445 GLU n 1 446 SER n 1 447 GLY n 1 448 ILE n 1 449 LEU n 1 450 GLY n 1 451 PRO n 1 452 LEU n 1 453 LEU n 1 454 TYR n 1 455 GLY n 1 456 GLU n 1 457 VAL n 1 458 GLY n 1 459 ASP n 1 460 THR n 1 461 LEU n 1 462 LEU n 1 463 ILE n 1 464 ILE n 1 465 PHE n 1 466 LYS n 1 467 ASN n 1 468 GLN n 1 469 ALA n 1 470 SER n 1 471 ARG n 1 472 PRO n 1 473 TYR n 1 474 ASN n 1 475 ILE n 1 476 TYR n 1 477 PRO n 1 478 HIS n 1 479 GLY n 1 480 ILE n 1 481 THR n 1 482 ASP n 1 483 VAL n 1 484 ARG n 1 485 PRO n 1 486 LEU n 1 487 TYR n 1 488 SER n 1 489 ARG n 1 490 ARG n 1 491 LEU n 1 492 PRO n 1 493 LYS n 1 494 GLY n 1 495 VAL n 1 496 LYS n 1 497 HIS n 1 498 LEU n 1 499 LYS n 1 500 ASP n 1 501 PHE n 1 502 PRO n 1 503 ILE n 1 504 LEU n 1 505 PRO n 1 506 GLY n 1 507 GLU n 1 508 ILE n 1 509 PHE n 1 510 LYS n 1 511 TYR n 1 512 LYS n 1 513 TRP n 1 514 THR n 1 515 VAL n 1 516 THR n 1 517 VAL n 1 518 GLU n 1 519 ASP n 1 520 GLY n 1 521 PRO n 1 522 THR n 1 523 LYS n 1 524 SER n 1 525 ASP n 1 526 PRO n 1 527 ARG n 1 528 CYS n 1 529 LEU n 1 530 THR n 1 531 ARG n 1 532 TYR n 1 533 TYR n 1 534 SER n 1 535 SER n 1 536 PHE n 1 537 VAL n 1 538 ASN n 1 539 MET n 1 540 GLU n 1 541 ARG n 1 542 ASP n 1 543 LEU n 1 544 ALA n 1 545 SER n 1 546 GLY n 1 547 LEU n 1 548 ILE n 1 549 GLY n 1 550 PRO n 1 551 LEU n 1 552 LEU n 1 553 ILE n 1 554 CYS n 1 555 TYR n 1 556 LYS n 1 557 GLU n 1 558 SER n 1 559 VAL n 1 560 ASP n 1 561 GLN n 1 562 ARG n 1 563 GLY n 1 564 ASN n 1 565 GLN n 1 566 ILE n 1 567 MET n 1 568 SER n 1 569 ASP n 1 570 LYS n 1 571 ARG n 1 572 ASN n 1 573 VAL n 1 574 ILE n 1 575 LEU n 1 576 PHE n 1 577 SER n 1 578 VAL n 1 579 PHE n 1 580 ASP n 1 581 GLU n 1 582 ASN n 1 583 ARG n 1 584 SER n 1 585 TRP n 1 586 TYR n 1 587 LEU n 1 588 THR n 1 589 GLU n 1 590 ASN n 1 591 ILE n 1 592 GLN n 1 593 ARG n 1 594 PHE n 1 595 LEU n 1 596 PRO n 1 597 ASN n 1 598 PRO n 1 599 ALA n 1 600 GLY n 1 601 VAL n 1 602 GLN n 1 603 LEU n 1 604 GLU n 1 605 ASP n 1 606 PRO n 1 607 GLU n 1 608 PHE n 1 609 GLN n 1 610 ALA n 1 611 SER n 1 612 ASN n 1 613 ILE n 1 614 MET n 1 615 HIS n 1 616 SER n 1 617 ILE n 1 618 ASN n 1 619 GLY n 1 620 TYR n 1 621 VAL n 1 622 PHE n 1 623 ASP n 1 624 SER n 1 625 LEU n 1 626 GLN n 1 627 LEU n 1 628 SER n 1 629 VAL n 1 630 CYS n 1 631 LEU n 1 632 HIS n 1 633 GLU n 1 634 VAL n 1 635 ALA n 1 636 TYR n 1 637 TRP n 1 638 TYR n 1 639 ILE n 1 640 LEU n 1 641 SER n 1 642 ILE n 1 643 GLY n 1 644 ALA n 1 645 GLN n 1 646 THR n 1 647 ASP n 1 648 PHE n 1 649 LEU n 1 650 SER n 1 651 VAL n 1 652 PHE n 1 653 PHE n 1 654 SER n 1 655 GLY n 1 656 TYR n 1 657 THR n 1 658 PHE n 1 659 LYS n 1 660 HIS n 1 661 LYS n 1 662 MET n 1 663 VAL n 1 664 TYR n 1 665 GLU n 1 666 ASP n 1 667 THR n 1 668 LEU n 1 669 THR n 1 670 LEU n 1 671 PHE n 1 672 PRO n 1 673 PHE n 1 674 SER n 1 675 GLY n 1 676 GLU n 1 677 THR n 1 678 VAL n 1 679 PHE n 1 680 MET n 1 681 SER n 1 682 MET n 1 683 GLU n 1 684 ASN n 1 685 PRO n 1 686 GLY n 1 687 LEU n 1 688 TRP n 1 689 ILE n 1 690 LEU n 1 691 GLY n 1 692 CYS n 1 693 HIS n 1 694 ASN n 1 695 SER n 1 696 ASP n 1 697 PHE n 1 698 ARG n 1 699 ASN n 1 700 ARG n 1 701 GLY n 1 702 MET n 1 703 THR n 1 704 ALA n 1 705 LEU n 1 706 LEU n 1 707 LYS n 1 708 VAL n 1 709 SER n 1 710 SER n 1 711 CYS n 1 712 ASP n 1 713 LYS n 1 714 ASN n 1 715 THR n 1 716 GLY n 1 717 ASP n 1 718 TYR n 1 719 TYR n 1 720 GLU n 1 721 ASP n 1 722 SER n 1 723 TYR n 1 724 GLU n 1 725 ASP n 1 726 ILE n 1 727 SER n 1 728 ALA n 1 729 TYR n 1 730 LEU n 1 731 LEU n 1 732 SER n 1 733 LYS n 1 734 ASN n 1 735 ASN n 1 736 ALA n 1 737 ILE n 1 738 GLU n 1 739 PRO n 1 740 ARG n 1 741 SER n 1 742 PHE n 1 743 SER n 1 744 GLN n 1 745 ASN n 1 746 SER n 1 747 ARG n 1 748 HIS n 1 749 PRO n 1 750 SER n 1 751 GLN n 1 752 ASN n 1 753 PRO n 1 754 PRO n 1 755 VAL n 1 756 LEU n 1 757 LYS n 1 758 ARG n 1 759 HIS n 1 760 GLN n 2 1 ARG n 2 2 GLU n 2 3 ILE n 2 4 THR n 2 5 ARG n 2 6 THR n 2 7 THR n 2 8 LEU n 2 9 GLN n 2 10 SER n 2 11 ASP n 2 12 GLN n 2 13 GLU n 2 14 GLU n 2 15 ILE n 2 16 ASP n 2 17 TYR n 2 18 ASP n 2 19 ASP n 2 20 THR n 2 21 ILE n 2 22 SER n 2 23 VAL n 2 24 GLU n 2 25 MET n 2 26 LYS n 2 27 LYS n 2 28 GLU n 2 29 ASP n 2 30 PHE n 2 31 ASP n 2 32 ILE n 2 33 TYR n 2 34 ASP n 2 35 GLU n 2 36 ASP n 2 37 GLU n 2 38 ASN n 2 39 GLN n 2 40 SER n 2 41 PRO n 2 42 ARG n 2 43 SER n 2 44 PHE n 2 45 GLN n 2 46 LYS n 2 47 LYS n 2 48 THR n 2 49 ARG n 2 50 HIS n 2 51 TYR n 2 52 PHE n 2 53 ILE n 2 54 ALA n 2 55 ALA n 2 56 VAL n 2 57 GLU n 2 58 ARG n 2 59 LEU n 2 60 TRP n 2 61 ASP n 2 62 TYR n 2 63 GLY n 2 64 MET n 2 65 SER n 2 66 SER n 2 67 SER n 2 68 PRO n 2 69 HIS n 2 70 VAL n 2 71 LEU n 2 72 ARG n 2 73 ASN n 2 74 ARG n 2 75 ALA n 2 76 GLN n 2 77 SER n 2 78 GLY n 2 79 SER n 2 80 VAL n 2 81 PRO n 2 82 GLN n 2 83 PHE n 2 84 LYS n 2 85 LYS n 2 86 VAL n 2 87 VAL n 2 88 PHE n 2 89 GLN n 2 90 GLU n 2 91 PHE n 2 92 THR n 2 93 ASP n 2 94 GLY n 2 95 SER n 2 96 PHE n 2 97 THR n 2 98 GLN n 2 99 PRO n 2 100 LEU n 2 101 TYR n 2 102 ARG n 2 103 GLY n 2 104 GLU n 2 105 LEU n 2 106 ASN n 2 107 GLU n 2 108 HIS n 2 109 LEU n 2 110 GLY n 2 111 LEU n 2 112 LEU n 2 113 GLY n 2 114 PRO n 2 115 TYR n 2 116 ILE n 2 117 ARG n 2 118 ALA n 2 119 GLU n 2 120 VAL n 2 121 GLU n 2 122 ASP n 2 123 ASN n 2 124 ILE n 2 125 MET n 2 126 VAL n 2 127 THR n 2 128 PHE n 2 129 ARG n 2 130 ASN n 2 131 GLN n 2 132 ALA n 2 133 SER n 2 134 ARG n 2 135 PRO n 2 136 TYR n 2 137 SER n 2 138 PHE n 2 139 TYR n 2 140 SER n 2 141 SER n 2 142 LEU n 2 143 ILE n 2 144 SER n 2 145 TYR n 2 146 GLU n 2 147 GLU n 2 148 ASP n 2 149 GLN n 2 150 ARG n 2 151 GLN n 2 152 GLY n 2 153 ALA n 2 154 GLU n 2 155 PRO n 2 156 ARG n 2 157 LYS n 2 158 ASN n 2 159 PHE n 2 160 VAL n 2 161 LYS n 2 162 PRO n 2 163 ASN n 2 164 GLU n 2 165 THR n 2 166 LYS n 2 167 THR n 2 168 TYR n 2 169 PHE n 2 170 TRP n 2 171 LYS n 2 172 VAL n 2 173 GLN n 2 174 HIS n 2 175 HIS n 2 176 MET n 2 177 ALA n 2 178 PRO n 2 179 THR n 2 180 LYS n 2 181 ASP n 2 182 GLU n 2 183 PHE n 2 184 ASP n 2 185 CYS n 2 186 LYS n 2 187 ALA n 2 188 TRP n 2 189 ALA n 2 190 TYR n 2 191 PHE n 2 192 SER n 2 193 ASP n 2 194 VAL n 2 195 ASP n 2 196 LEU n 2 197 GLU n 2 198 LYS n 2 199 ASP n 2 200 VAL n 2 201 HIS n 2 202 SER n 2 203 GLY n 2 204 LEU n 2 205 ILE n 2 206 GLY n 2 207 PRO n 2 208 LEU n 2 209 LEU n 2 210 VAL n 2 211 CYS n 2 212 HIS n 2 213 THR n 2 214 ASN n 2 215 THR n 2 216 LEU n 2 217 ASN n 2 218 PRO n 2 219 ALA n 2 220 HIS n 2 221 GLY n 2 222 ARG n 2 223 GLN n 2 224 VAL n 2 225 THR n 2 226 VAL n 2 227 GLN n 2 228 GLU n 2 229 PHE n 2 230 ALA n 2 231 LEU n 2 232 PHE n 2 233 PHE n 2 234 THR n 2 235 ILE n 2 236 PHE n 2 237 ASP n 2 238 GLU n 2 239 THR n 2 240 LYS n 2 241 SER n 2 242 TRP n 2 243 TYR n 2 244 PHE n 2 245 THR n 2 246 GLU n 2 247 ASN n 2 248 MET n 2 249 GLU n 2 250 ARG n 2 251 ASN n 2 252 CYS n 2 253 ARG n 2 254 ALA n 2 255 PRO n 2 256 CYS n 2 257 ASN n 2 258 ILE n 2 259 GLN n 2 260 MET n 2 261 GLU n 2 262 ASP n 2 263 PRO n 2 264 THR n 2 265 PHE n 2 266 LYS n 2 267 GLU n 2 268 ASN n 2 269 TYR n 2 270 ARG n 2 271 PHE n 2 272 HIS n 2 273 ALA n 2 274 ILE n 2 275 ASN n 2 276 GLY n 2 277 TYR n 2 278 ILE n 2 279 MET n 2 280 ASP n 2 281 THR n 2 282 LEU n 2 283 PRO n 2 284 GLY n 2 285 LEU n 2 286 VAL n 2 287 MET n 2 288 ALA n 2 289 GLN n 2 290 ASP n 2 291 GLN n 2 292 ARG n 2 293 ILE n 2 294 ARG n 2 295 TRP n 2 296 TYR n 2 297 LEU n 2 298 LEU n 2 299 SER n 2 300 MET n 2 301 GLY n 2 302 SER n 2 303 ASN n 2 304 GLU n 2 305 ASN n 2 306 ILE n 2 307 HIS n 2 308 SER n 2 309 ILE n 2 310 HIS n 2 311 PHE n 2 312 SER n 2 313 GLY n 2 314 HIS n 2 315 VAL n 2 316 PHE n 2 317 THR n 2 318 VAL n 2 319 ARG n 2 320 LYS n 2 321 LYS n 2 322 GLU n 2 323 GLU n 2 324 TYR n 2 325 LYS n 2 326 MET n 2 327 ALA n 2 328 LEU n 2 329 TYR n 2 330 ASN n 2 331 LEU n 2 332 TYR n 2 333 PRO n 2 334 GLY n 2 335 VAL n 2 336 PHE n 2 337 GLU n 2 338 THR n 2 339 VAL n 2 340 GLU n 2 341 MET n 2 342 LEU n 2 343 PRO n 2 344 SER n 2 345 LYS n 2 346 ALA n 2 347 GLY n 2 348 ILE n 2 349 TRP n 2 350 ARG n 2 351 VAL n 2 352 GLU n 2 353 CYS n 2 354 LEU n 2 355 ILE n 2 356 GLY n 2 357 GLU n 2 358 HIS n 2 359 LEU n 2 360 HIS n 2 361 ALA n 2 362 GLY n 2 363 MET n 2 364 SER n 2 365 THR n 2 366 LEU n 2 367 PHE n 2 368 LEU n 2 369 VAL n 2 370 TYR n 2 371 SER n 2 372 ASN n 2 373 LYS n 2 374 CYS n 2 375 GLN n 2 376 THR n 2 377 PRO n 2 378 LEU n 2 379 GLY n 2 380 MET n 2 381 ALA n 2 382 SER n 2 383 GLY n 2 384 HIS n 2 385 ILE n 2 386 ARG n 2 387 ASP n 2 388 PHE n 2 389 GLN n 2 390 ILE n 2 391 THR n 2 392 ALA n 2 393 SER n 2 394 GLY n 2 395 GLN n 2 396 TYR n 2 397 GLY n 2 398 GLN n 2 399 TRP n 2 400 ALA n 2 401 PRO n 2 402 LYS n 2 403 LEU n 2 404 ALA n 2 405 ARG n 2 406 LEU n 2 407 HIS n 2 408 TYR n 2 409 SER n 2 410 GLY n 2 411 SER n 2 412 ILE n 2 413 ASN n 2 414 ALA n 2 415 TRP n 2 416 SER n 2 417 THR n 2 418 LYS n 2 419 GLU n 2 420 PRO n 2 421 PHE n 2 422 SER n 2 423 TRP n 2 424 ILE n 2 425 LYS n 2 426 VAL n 2 427 ASP n 2 428 LEU n 2 429 LEU n 2 430 ALA n 2 431 PRO n 2 432 MET n 2 433 ILE n 2 434 ILE n 2 435 HIS n 2 436 GLY n 2 437 ILE n 2 438 LYS n 2 439 THR n 2 440 GLN n 2 441 GLY n 2 442 ALA n 2 443 ARG n 2 444 GLN n 2 445 LYS n 2 446 PHE n 2 447 SER n 2 448 SER n 2 449 LEU n 2 450 TYR n 2 451 ILE n 2 452 SER n 2 453 GLN n 2 454 PHE n 2 455 ILE n 2 456 ILE n 2 457 MET n 2 458 TYR n 2 459 SER n 2 460 LEU n 2 461 ASP n 2 462 GLY n 2 463 LYS n 2 464 LYS n 2 465 TRP n 2 466 GLN n 2 467 THR n 2 468 TYR n 2 469 ARG n 2 470 GLY n 2 471 ASN n 2 472 SER n 2 473 THR n 2 474 GLY n 2 475 THR n 2 476 LEU n 2 477 MET n 2 478 VAL n 2 479 PHE n 2 480 PHE n 2 481 GLY n 2 482 ASN n 2 483 VAL n 2 484 ASP n 2 485 SER n 2 486 SER n 2 487 GLY n 2 488 ILE n 2 489 LYS n 2 490 HIS n 2 491 ASN n 2 492 ILE n 2 493 PHE n 2 494 ASN n 2 495 PRO n 2 496 PRO n 2 497 ILE n 2 498 ILE n 2 499 ALA n 2 500 ARG n 2 501 TYR n 2 502 ILE n 2 503 ARG n 2 504 LEU n 2 505 HIS n 2 506 PRO n 2 507 THR n 2 508 HIS n 2 509 TYR n 2 510 SER n 2 511 ILE n 2 512 ARG n 2 513 SER n 2 514 THR n 2 515 LEU n 2 516 ARG n 2 517 MET n 2 518 GLU n 2 519 LEU n 2 520 MET n 2 521 GLY n 2 522 CYS n 2 523 ASP n 2 524 LEU n 2 525 ASN n 2 526 SER n 2 527 CYS n 2 528 SER n 2 529 MET n 2 530 PRO n 2 531 LEU n 2 532 GLY n 2 533 MET n 2 534 GLU n 2 535 SER n 2 536 LYS n 2 537 ALA n 2 538 ILE n 2 539 SER n 2 540 ASP n 2 541 ALA n 2 542 GLN n 2 543 ILE n 2 544 THR n 2 545 ALA n 2 546 SER n 2 547 SER n 2 548 TYR n 2 549 PHE n 2 550 THR n 2 551 ASN n 2 552 MET n 2 553 PHE n 2 554 ALA n 2 555 THR n 2 556 TRP n 2 557 SER n 2 558 PRO n 2 559 SER n 2 560 LYS n 2 561 ALA n 2 562 ARG n 2 563 LEU n 2 564 HIS n 2 565 LEU n 2 566 GLN n 2 567 GLY n 2 568 ARG n 2 569 SER n 2 570 ASN n 2 571 ALA n 2 572 TRP n 2 573 ARG n 2 574 PRO n 2 575 GLN n 2 576 VAL n 2 577 ASN n 2 578 ASN n 2 579 PRO n 2 580 LYS n 2 581 GLU n 2 582 TRP n 2 583 LEU n 2 584 GLN n 2 585 VAL n 2 586 ASP n 2 587 PHE n 2 588 GLN n 2 589 LYS n 2 590 THR n 2 591 MET n 2 592 LYS n 2 593 VAL n 2 594 THR n 2 595 GLY n 2 596 VAL n 2 597 THR n 2 598 THR n 2 599 GLN n 2 600 GLY n 2 601 VAL n 2 602 LYS n 2 603 SER n 2 604 LEU n 2 605 LEU n 2 606 THR n 2 607 SER n 2 608 MET n 2 609 TYR n 2 610 VAL n 2 611 LYS n 2 612 GLU n 2 613 PHE n 2 614 LEU n 2 615 ILE n 2 616 SER n 2 617 SER n 2 618 SER n 2 619 GLN n 2 620 ASP n 2 621 GLY n 2 622 HIS n 2 623 GLN n 2 624 TRP n 2 625 THR n 2 626 LEU n 2 627 PHE n 2 628 PHE n 2 629 GLN n 2 630 ASN n 2 631 GLY n 2 632 LYS n 2 633 VAL n 2 634 LYS n 2 635 VAL n 2 636 PHE n 2 637 GLN n 2 638 GLY n 2 639 ASN n 2 640 GLN n 2 641 ASP n 2 642 SER n 2 643 PHE n 2 644 THR n 2 645 PRO n 2 646 VAL n 2 647 VAL n 2 648 ASN n 2 649 SER n 2 650 LEU n 2 651 ASP n 2 652 PRO n 2 653 PRO n 2 654 LEU n 2 655 LEU n 2 656 THR n 2 657 ARG n 2 658 TYR n 2 659 LEU n 2 660 ARG n 2 661 ILE n 2 662 HIS n 2 663 PRO n 2 664 GLN n 2 665 SER n 2 666 TRP n 2 667 VAL n 2 668 HIS n 2 669 GLN n 2 670 ILE n 2 671 ALA n 2 672 LEU n 2 673 ARG n 2 674 MET n 2 675 GLU n 2 676 VAL n 2 677 LEU n 2 678 GLY n 2 679 CYS n 2 680 GLU n 2 681 ALA n 2 682 GLN n 2 683 ASP n 2 684 LEU n 2 685 TYR 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 ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? BLOOD ? ? ? 'CHINESE HAMSTER' 'CRICETULUS GRISEUS' 10029 ? ? ? ? ? ? ? ? CHO ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? BLOOD ? ? ? 'CHINESE HAMSTER' 'CRICETULUS GRISEUS' 10029 ? ? ? ? ? ? ? ? CHO ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP FA8_HUMAN 1 ? ? P00451 ? 2 UNP FA8_HUMAN 2 ? ? P00451 ? # 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 4BDV A 1 ? 750 ? P00451 20 ? 769 ? 1 750 2 1 4BDV A 751 ? 760 ? P00451 1657 ? 1666 ? 751 760 3 2 4BDV B 1 ? 685 ? P00451 1667 ? 2351 ? 1648 2332 # 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CU1 non-polymer . 'COPPER (I) ION' ? 'Cu 1' 63.546 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 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 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4BDV _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 4.8 _exptl_crystal.density_percent_sol 74 _exptl_crystal.description 'DATA USED DURING REFINEMENTS WERE A COMBINATION TWO DATA SETS COLLECTED AT TWO DIFFERENT WAVELENGTHS.' # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '3% PEG550, 0.100 M NACL, 0.100 M TRIS-HCL PH 7.5, 10% ETHANOL' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2009-06-24 _diffrn_detector.details 'TWO MIRRORS' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'DOUBLE CRYSTAL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # loop_ _diffrn_radiation_wavelength.id _diffrn_radiation_wavelength.wavelength _diffrn_radiation_wavelength.wt 1 1.0082 1.0 2 1.2700 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'MAX II BEAMLINE I911-3' _diffrn_source.pdbx_synchrotron_site 'MAX II' _diffrn_source.pdbx_synchrotron_beamline I911-3 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list '1.0082, 1.2700' # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BDV _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.00 _reflns.d_resolution_high 3.98 _reflns.number_obs 28556 _reflns.number_all ? _reflns.percent_possible_obs 99.6 _reflns.pdbx_Rmerge_I_obs 0.20 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 12.45 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 16.6 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 3.98 _reflns_shell.d_res_low 4.08 _reflns_shell.percent_possible_all 99.9 _reflns_shell.Rmerge_I_obs 1.40 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.39 _reflns_shell.pdbx_redundancy 17.1 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BDV _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 26904 _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 20.00 _refine.ls_d_res_high 3.98 _refine.ls_percent_reflns_obs 98.82 _refine.ls_R_factor_obs 0.16626 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16194 _refine.ls_R_factor_R_free 0.24558 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1458 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.962 _refine.correlation_coeff_Fo_to_Fc_free 0.909 _refine.B_iso_mean 160.457 _refine.aniso_B[1][1] -0.02 _refine.aniso_B[2][2] -0.02 _refine.aniso_B[3][3] 0.04 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'U VALUES WITH TLS ADDED. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT.' _refine.pdbx_starting_model 'PDB ENTRY 3CDZ' _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free 0.608 _refine.overall_SU_ML 0.458 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 79.938 _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 ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 9873 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 100 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 9973 _refine_hist.d_res_high 3.98 _refine_hist.d_res_low 20.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.013 0.019 ? 10274 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.096 1.950 ? 13924 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 10.206 5.000 ? 1209 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 40.871 23.460 ? 474 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 24.741 15.000 ? 1702 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 18.173 15.000 ? 53 'X-RAY DIFFRACTION' ? r_chiral_restr 0.149 0.200 ? 1505 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.021 ? 7753 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 3.980 _refine_ls_shell.d_res_low 4.081 _refine_ls_shell.number_reflns_R_work 1928 _refine_ls_shell.R_factor_R_work 0.292 _refine_ls_shell.percent_reflns_obs 99.36 _refine_ls_shell.R_factor_R_free 0.375 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 101 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BDV _struct.title 'CRYSTAL STRUCTURE OF A TRUNCATED B-DOMAIN HUMAN FACTOR VIII' _struct.pdbx_descriptor 'FACTOR VIIIA HEAVY CHAIN, 92 KDA ISOFORM, B DOMAIN, FACTOR VIIIA LIGHT CHAIN' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BDV _struct_keywords.pdbx_keywords 'BLOOD CLOTTING' _struct_keywords.text 'BLOOD CLOTTING, BLOOD COAGULATION, METAL BINDING' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 5 ? G N N 6 ? H N N 7 ? I N N 5 ? J N N 5 ? K N N 8 ? L N N 8 ? M N N 8 ? N N N 6 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 119 ? LYS A 123 ? SER A 119 LYS A 123 5 ? 5 HELX_P HELX_P2 2 LEU A 164 ? LEU A 172 ? LEU A 164 LEU A 172 1 ? 9 HELX_P HELX_P3 3 ILE A 312 ? GLN A 316 ? ILE A 312 GLN A 316 5 ? 5 HELX_P HELX_P4 4 THR A 516 ? GLY A 520 ? THR A 516 GLY A 520 5 ? 5 HELX_P HELX_P5 5 GLU A 540 ? SER A 545 ? GLU A 540 SER A 545 1 ? 6 HELX_P HELX_P6 6 ASN A 582 ? SER A 584 ? ASN A 582 SER A 584 5 ? 3 HELX_P HELX_P7 7 TYR A 586 ? GLN A 592 ? TYR A 586 GLN A 592 1 ? 7 HELX_P HELX_P8 8 ASP A 605 ? SER A 611 ? ASP A 605 SER A 611 1 ? 7 HELX_P HELX_P9 9 ASP A 696 ? ARG A 700 ? ASP A 696 ARG A 700 5 ? 5 HELX_P HELX_P10 10 GLN B 173 ? ALA B 177 ? GLN B 1820 ALA B 1824 5 ? 5 HELX_P HELX_P11 11 GLU B 197 ? SER B 202 ? GLU B 1844 SER B 1849 1 ? 6 HELX_P HELX_P12 12 ILE B 355 ? HIS B 360 ? ILE B 2002 HIS B 2007 1 ? 6 HELX_P HELX_P13 13 SER B 539 ? ALA B 541 ? SER B 2186 ALA B 2188 5 ? 3 HELX_P HELX_P14 14 SER B 557 ? ALA B 561 ? SER B 2204 ALA B 2208 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 153 SG ? ? ? 1_555 A CYS 179 SG ? ? A CYS 153 A CYS 179 1_555 ? ? ? ? ? ? ? 2.038 ? disulf2 disulf ? ? A CYS 248 SG ? ? ? 1_555 A CYS 329 SG ? ? A CYS 248 A CYS 329 1_555 ? ? ? ? ? ? ? 2.058 ? disulf3 disulf ? ? A CYS 528 SG ? ? ? 1_555 A CYS 554 SG ? ? A CYS 528 A CYS 554 1_555 ? ? ? ? ? ? ? 2.060 ? disulf4 disulf ? ? A CYS 630 SG ? ? ? 1_555 A CYS 711 SG ? ? A CYS 630 A CYS 711 1_555 ? ? ? ? ? ? ? 2.051 ? disulf5 disulf ? ? B CYS 185 SG ? ? ? 1_555 B CYS 211 SG ? ? B CYS 1832 B CYS 1858 1_555 ? ? ? ? ? ? ? 2.056 ? disulf6 disulf ? ? B CYS 374 SG ? ? ? 1_555 B CYS 522 SG ? ? B CYS 2021 B CYS 2169 1_555 ? ? ? ? ? ? ? 2.051 ? disulf7 disulf ? ? B CYS 527 SG ? ? ? 1_555 B CYS 679 SG ? ? B CYS 2174 B CYS 2326 1_555 ? ? ? ? ? ? ? 2.032 ? covale1 covale ? ? A ASN 239 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 239 A NAG 1755 1_555 ? ? ? ? ? ? ? 1.463 ? metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 A HIS 267 ND1 ? ? A ZN 800 A HIS 267 1_555 ? ? ? ? ? ? ? 2.158 ? metalc2 metalc ? ? C ZN . ZN ? ? ? 1_555 A CYS 310 SG ? ? A ZN 800 A CYS 310 1_555 ? ? ? ? ? ? ? 2.350 ? metalc3 metalc ? ? C ZN . ZN ? ? ? 1_555 A HIS 315 ND1 ? ? A ZN 800 A HIS 315 1_555 ? ? ? ? ? ? ? 2.155 ? metalc4 metalc ? ? D CA . CA ? ? ? 1_555 A ASP 125 OD1 ? ? A CA 801 A ASP 125 1_555 ? ? ? ? ? ? ? 2.900 ? metalc5 metalc ? ? D CA . CA ? ? ? 1_555 A ASP 125 OD2 ? ? A CA 801 A ASP 125 1_555 ? ? ? ? ? ? ? 2.317 ? metalc6 metalc ? ? D CA . CA ? ? ? 1_555 A LYS 107 O ? ? A CA 801 A LYS 107 1_555 ? ? ? ? ? ? ? 2.314 ? metalc7 metalc ? ? D CA . CA ? ? ? 1_555 A ASP 116 OD2 ? ? A CA 801 A ASP 116 1_555 ? ? ? ? ? ? ? 2.332 ? metalc8 metalc ? ? D CA . CA ? ? ? 1_555 A ASP 126 OD1 ? ? A CA 801 A ASP 126 1_555 ? ? ? ? ? ? ? 2.315 ? covale2 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1755 A NAG 1756 1_555 ? ? ? ? ? ? ? 1.476 ? metalc9 metalc ? ? H CU1 . CU ? ? ? 1_555 B CYS 353 SG ? ? B CU1 1 B CYS 2000 1_555 ? ? ? ? ? ? ? 2.318 ? metalc10 metalc ? ? H CU1 . CU ? ? ? 1_555 B HIS 358 ND1 ? ? B CU1 1 B HIS 2005 1_555 ? ? ? ? ? ? ? 2.117 ? metalc11 metalc ? ? H CU1 . CU ? ? ? 1_555 B HIS 307 ND1 ? ? B CU1 1 B HIS 1954 1_555 ? ? ? ? ? ? ? 2.092 ? covale3 covale ? ? B ASN 471 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 2118 B NAG 2334 1_555 ? ? ? ? ? ? ? 1.437 ? covale4 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? B NAG 2334 B NAG 2335 1_555 ? ? ? ? ? ? ? 1.468 ? covale5 covale ? ? J NAG . O4 ? ? ? 1_555 K BMA . C1 ? ? B NAG 2335 B BMA 2336 1_555 ? ? ? ? ? ? ? 1.479 ? covale6 covale ? ? K BMA . O6 ? ? ? 1_555 M BMA . C1 ? ? B BMA 2336 B BMA 2338 1_555 ? ? ? ? ? ? ? 1.458 ? covale7 covale ? ? K BMA . O3 ? ? ? 1_555 L BMA . C1 ? ? B BMA 2336 B BMA 2337 1_555 ? ? ? ? ? ? ? 1.459 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 2 ? AB ? 2 ? AC ? 2 ? AD ? 2 ? AE ? 4 ? AF ? 2 ? AG ? 2 ? AH ? 2 ? AI ? 3 ? AJ ? 2 ? AK ? 5 ? AL ? 4 ? AM ? 4 ? AN ? 3 ? AO ? 2 ? AP ? 2 ? BA ? 4 ? BB ? 3 ? BC ? 5 ? BD ? 2 ? BE ? 5 ? BF ? 6 ? BG ? 4 ? BH ? 2 ? BI ? 6 ? BJ ? 2 ? BK ? 6 ? BL ? 2 ? BM ? 6 ? BN ? 4 ? BO ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? parallel AB 1 2 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? anti-parallel AE 1 2 ? parallel AE 2 3 ? anti-parallel AE 3 4 ? anti-parallel AF 1 2 ? parallel AG 1 2 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AJ 1 2 ? anti-parallel AK 1 2 ? anti-parallel AK 2 3 ? parallel AK 3 4 ? anti-parallel AK 4 5 ? anti-parallel AL 1 2 ? parallel AL 2 3 ? anti-parallel AL 3 4 ? anti-parallel AM 1 2 ? anti-parallel AM 2 3 ? parallel AM 3 4 ? anti-parallel AN 1 2 ? parallel AN 2 3 ? anti-parallel AO 1 2 ? anti-parallel AP 1 2 ? anti-parallel BA 1 2 ? anti-parallel BA 2 3 ? parallel BA 3 4 ? anti-parallel BB 1 2 ? parallel BB 2 3 ? anti-parallel BC 1 2 ? parallel BC 2 3 ? anti-parallel BC 3 4 ? anti-parallel BC 4 5 ? anti-parallel BD 1 2 ? anti-parallel BE 1 2 ? parallel BE 2 3 ? anti-parallel BE 3 4 ? anti-parallel BE 4 5 ? anti-parallel BF 1 2 ? anti-parallel BF 2 3 ? parallel BF 3 4 ? anti-parallel BF 4 5 ? anti-parallel BF 5 6 ? anti-parallel BG 1 2 ? anti-parallel BG 2 3 ? parallel BG 3 4 ? anti-parallel BH 1 2 ? anti-parallel BI 1 2 ? anti-parallel BI 2 3 ? parallel BI 3 4 ? anti-parallel BI 4 5 ? anti-parallel BI 5 6 ? anti-parallel BJ 1 2 ? anti-parallel BK 1 2 ? anti-parallel BK 2 3 ? parallel BK 3 4 ? anti-parallel BK 4 5 ? anti-parallel BK 5 6 ? anti-parallel BL 1 2 ? anti-parallel BM 1 2 ? anti-parallel BM 2 3 ? parallel BM 3 4 ? anti-parallel BM 4 5 ? anti-parallel BM 5 6 ? anti-parallel BN 1 2 ? anti-parallel BN 2 3 ? parallel BN 3 4 ? anti-parallel BO 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 ARG A 3 ? TYR A 5 ? ARG A 3 TYR A 5 AA 2 THR A 83 ? LEU A 88 ? THR A 83 LEU A 88 AB 1 HIS A 134 ? THR A 135 ? HIS A 134 THR A 135 AB 2 THR A 83 ? LEU A 88 ? THR A 83 LEU A 88 AC 1 TRP A 138 ? GLN A 139 ? TRP A 138 GLN A 139 AC 2 THR A 83 ? LEU A 88 ? THR A 83 LEU A 88 AD 1 VAL A 10 ? GLU A 11 ? VAL A 10 GLU A 11 AD 2 THR A 49 ? LEU A 50 ? THR A 49 LEU A 50 AE 1 GLY A 73 ? GLU A 79 ? GLY A 73 GLU A 79 AE 2 ILE A 173 ? CYS A 179 ? ILE A 173 CYS A 179 AE 3 CYS A 153 ? LEU A 159 ? CYS A 153 LEU A 159 AE 4 HIS A 99 ? VAL A 101 ? HIS A 99 VAL A 101 AF 1 HIS A 193 ? PHE A 195 ? HIS A 193 PHE A 195 AF 2 VAL A 253 ? MET A 260 ? VAL A 253 MET A 260 AG 1 LEU A 198 ? ALA A 200 ? LEU A 198 ALA A 200 AG 2 VAL A 253 ? MET A 260 ? VAL A 253 MET A 260 AH 1 PHE A 293 ? GLN A 297 ? PHE A 293 GLN A 297 AH 2 VAL A 253 ? MET A 260 ? VAL A 253 MET A 260 AI 1 ILE A 269 ? LEU A 271 ? ILE A 269 LEU A 271 AI 2 GLY A 304 ? CYS A 310 ? GLY A 304 CYS A 310 AI 3 GLU A 321 ? VAL A 326 ? GLU A 321 VAL A 326 AJ 1 PHE A 276 ? VAL A 278 ? PHE A 276 VAL A 278 AJ 2 HIS A 281 ? GLN A 283 ? HIS A 281 GLN A 283 AK 1 LYS A 422 ? TYR A 431 ? LYS A 422 TYR A 431 AK 2 THR A 381 ? ASP A 394 ? THR A 381 ASP A 394 AK 3 THR A 460 ? GLN A 468 ? THR A 460 GLN A 468 AK 4 ILE A 508 ? THR A 514 ? ILE A 508 THR A 514 AK 5 ASP A 482 ? PRO A 485 ? ASP A 482 PRO A 485 AL 1 LEU A 453 ? GLU A 456 ? LEU A 453 GLU A 456 AL 2 ILE A 548 ? CYS A 554 ? ILE A 548 CYS A 554 AL 3 LEU A 529 ? SER A 534 ? LEU A 529 SER A 534 AL 4 TYR A 476 ? HIS A 478 ? TYR A 476 HIS A 478 AM 1 ILE A 613 ? ILE A 617 ? ILE A 613 ILE A 617 AM 2 ASN A 572 ? ASP A 580 ? ASN A 572 ASP A 580 AM 3 ALA A 635 ? SER A 641 ? ALA A 635 SER A 641 AM 4 GLY A 675 ? MET A 680 ? GLY A 675 MET A 680 AN 1 GLN A 626 ? VAL A 629 ? GLN A 626 VAL A 629 AN 2 ALA A 704 ? VAL A 708 ? ALA A 704 VAL A 708 AN 3 GLY A 686 ? LEU A 690 ? GLY A 686 LEU A 690 AO 1 LEU A 649 ? SER A 650 ? LEU A 649 SER A 650 AO 2 THR A 669 ? LEU A 670 ? THR A 669 LEU A 670 AP 1 PHE A 658 ? LYS A 659 ? PHE A 658 LYS A 659 AP 2 TYR A 664 ? GLU A 665 ? TYR A 664 GLU A 665 BA 1 LYS B 84 ? GLU B 90 ? LYS B 1731 GLU B 1737 BA 2 THR B 48 ? LEU B 59 ? THR B 1695 LEU B 1706 BA 3 ASN B 123 ? ASN B 130 ? ASN B 1770 ASN B 1777 BA 4 GLU B 164 ? LYS B 171 ? GLU B 1811 LYS B 1818 BB 1 ILE B 116 ? GLU B 119 ? ILE B 1763 GLU B 1766 BB 2 ILE B 205 ? CYS B 211 ? ILE B 1852 CYS B 1858 BB 3 CYS B 185 ? PHE B 191 ? CYS B 1832 PHE B 1838 BC 1 GLN B 227 ? PHE B 233 ? GLN B 1874 PHE B 1880 BC 2 ILE B 293 ? SER B 299 ? ILE B 1940 SER B 1946 BC 3 GLU B 337 ? MET B 341 ? GLU B 1984 MET B 1988 BC 4 PHE B 316 ? VAL B 318 ? PHE B 1963 VAL B 1965 BC 5 TYR B 324 ? MET B 326 ? TYR B 1971 MET B 1973 BD 1 PHE B 236 ? ASP B 237 ? PHE B 1883 ASP B 1884 BD 2 ARG B 270 ? PHE B 271 ? ARG B 1917 PHE B 1918 BE 1 VAL B 286 ? ALA B 288 ? VAL B 1933 ALA B 1935 BE 2 THR B 365 ? TYR B 370 ? THR B 2012 TYR B 2017 BE 3 GLY B 347 ? CYS B 353 ? GLY B 1994 CYS B 2000 BE 4 SER B 308 ? PHE B 311 ? SER B 1955 PHE B 1958 BE 5 LEU B 328 ? ASN B 330 ? LEU B 1975 ASN B 1977 BF 1 THR B 376 ? PRO B 377 ? THR B 2023 PRO B 2024 BF 2 MET B 517 ? CYS B 522 ? MET B 2164 CYS B 2169 BF 3 ILE B 424 ? THR B 439 ? ILE B 2071 THR B 2086 BF 4 HIS B 490 ? TYR B 509 ? HIS B 2137 TYR B 2156 BF 5 SER B 448 ? SER B 459 ? SER B 2095 SER B 2106 BF 6 GLN B 466 ? THR B 467 ? GLN B 2113 THR B 2114 BG 1 THR B 376 ? PRO B 377 ? THR B 2023 PRO B 2024 BG 2 MET B 517 ? CYS B 522 ? MET B 2164 CYS B 2169 BG 3 ILE B 424 ? THR B 439 ? ILE B 2071 THR B 2086 BG 4 ILE B 390 ? ALA B 392 ? ILE B 2037 ALA B 2039 BH 1 GLY B 441 ? ARG B 443 ? GLY B 2088 ARG B 2090 BH 2 SER B 448 ? SER B 459 ? SER B 2095 SER B 2106 BI 1 THR B 376 ? PRO B 377 ? THR B 2023 PRO B 2024 BI 2 MET B 517 ? CYS B 522 ? MET B 2164 CYS B 2169 BI 3 ILE B 424 ? THR B 439 ? ILE B 2071 THR B 2086 BI 4 HIS B 490 ? TYR B 509 ? HIS B 2137 TYR B 2156 BI 5 SER B 448 ? SER B 459 ? SER B 2095 SER B 2106 BI 6 VAL B 478 ? PHE B 480 ? VAL B 2125 PHE B 2127 BJ 1 GLN B 466 ? THR B 467 ? GLN B 2113 THR B 2114 BJ 2 SER B 448 ? SER B 459 ? SER B 2095 SER B 2106 BK 1 THR B 376 ? PRO B 377 ? THR B 2023 PRO B 2024 BK 2 MET B 517 ? CYS B 522 ? MET B 2164 CYS B 2169 BK 3 ILE B 424 ? THR B 439 ? ILE B 2071 THR B 2086 BK 4 HIS B 490 ? TYR B 509 ? HIS B 2137 TYR B 2156 BK 5 SER B 448 ? SER B 459 ? SER B 2095 SER B 2106 BK 6 GLY B 441 ? ARG B 443 ? GLY B 2088 ARG B 2090 BL 1 TRP B 415 ? THR B 417 ? TRP B 2062 THR B 2064 BL 2 SER B 513 ? LEU B 515 ? SER B 2160 LEU B 2162 BM 1 MET B 529 ? PRO B 530 ? MET B 2176 PRO B 2177 BM 2 MET B 674 ? GLU B 680 ? MET B 2321 GLU B 2327 BM 3 LEU B 583 ? THR B 598 ? LEU B 2230 THR B 2245 BM 4 VAL B 646 ? SER B 665 ? VAL B 2293 SER B 2312 BM 5 GLU B 612 ? SER B 618 ? GLU B 2259 SER B 2265 BM 6 VAL B 635 ? GLN B 637 ? VAL B 2282 GLN B 2284 BN 1 MET B 529 ? PRO B 530 ? MET B 2176 PRO B 2177 BN 2 MET B 674 ? GLU B 680 ? MET B 2321 GLU B 2327 BN 3 LEU B 583 ? THR B 598 ? LEU B 2230 THR B 2245 BN 4 ILE B 543 ? ALA B 545 ? ILE B 2190 ALA B 2192 BO 1 GLY B 600 ? LYS B 602 ? GLY B 2247 LYS B 2249 BO 2 SER B 607 ? TYR B 609 ? SER B 2254 TYR B 2256 # 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 AA 1 2 N ARG A 3 ? N ARG A 3 O THR A 83 ? O THR A 83 AB 1 2 N HIS A 134 ? N HIS A 134 O LEU A 88 ? O LEU A 88 AC 1 2 N TRP A 138 ? N TRP A 138 O VAL A 84 ? O VAL A 84 AD 1 2 N VAL A 10 ? N VAL A 10 O LEU A 50 ? O LEU A 50 AE 1 2 N GLY A 73 ? N GLY A 73 O ILE A 173 ? O ILE A 173 AE 2 3 N VAL A 178 ? N VAL A 178 O LEU A 154 ? O LEU A 154 AE 3 4 N LEU A 159 ? N LEU A 159 O HIS A 99 ? O HIS A 99 AF 1 2 N PHE A 195 ? N PHE A 195 O TYR A 254 ? O TYR A 254 AG 1 2 N PHE A 199 ? N PHE A 199 O ILE A 258 ? O ILE A 258 AH 1 2 N ALA A 296 ? N ALA A 296 O TRP A 255 ? O TRP A 255 AI 1 2 N PHE A 270 ? N PHE A 270 O PHE A 309 ? O PHE A 309 AI 2 3 N LEU A 308 ? N LEU A 308 O ALA A 322 ? O ALA A 322 AJ 1 2 N VAL A 278 ? N VAL A 278 O HIS A 281 ? O HIS A 281 AK 1 2 N TYR A 431 ? N TYR A 431 O TYR A 385 ? O TYR A 385 AK 2 3 N TRP A 382 ? N TRP A 382 O THR A 460 ? O THR A 460 AK 3 4 N PHE A 465 ? N PHE A 465 O PHE A 509 ? O PHE A 509 AK 4 5 N THR A 514 ? N THR A 514 O ASP A 482 ? O ASP A 482 AL 1 2 N LEU A 453 ? N LEU A 453 O PRO A 550 ? O PRO A 550 AL 2 3 N ILE A 553 ? N ILE A 553 O LEU A 529 ? O LEU A 529 AL 3 4 N SER A 534 ? N SER A 534 O TYR A 476 ? O TYR A 476 AM 1 2 N SER A 616 ? N SER A 616 O SER A 577 ? O SER A 577 AM 2 3 N ASN A 572 ? N ASN A 572 O TYR A 636 ? O TYR A 636 AM 3 4 N ILE A 639 ? N ILE A 639 O GLU A 676 ? O GLU A 676 AN 1 2 N LEU A 627 ? N LEU A 627 O LEU A 705 ? O LEU A 705 AN 2 3 N VAL A 708 ? N VAL A 708 O GLY A 686 ? O GLY A 686 AO 1 2 N LEU A 649 ? N LEU A 649 O LEU A 670 ? O LEU A 670 AP 1 2 N PHE A 658 ? N PHE A 658 O GLU A 665 ? O GLU A 665 BA 1 2 N GLN B 89 ? N GLN B 1736 O ALA B 54 ? O ALA B 1701 BA 2 3 N ARG B 49 ? N ARG B 1696 O ASN B 123 ? O ASN B 1770 BA 3 4 N ASN B 130 ? N ASN B 1777 O GLU B 164 ? O GLU B 1811 BB 1 2 N ILE B 116 ? N ILE B 1763 O PRO B 207 ? O PRO B 1854 BB 2 3 N VAL B 210 ? N VAL B 1857 O LYS B 186 ? O LYS B 1833 BC 1 2 N PHE B 229 ? N PHE B 1876 O ARG B 294 ? O ARG B 1941 BC 2 3 N LEU B 297 ? N LEU B 1944 O GLU B 337 ? O GLU B 1984 BC 3 4 N GLU B 340 ? N GLU B 1987 O THR B 317 ? O THR B 1964 BC 4 5 N VAL B 318 ? N VAL B 1965 O TYR B 324 ? O TYR B 1971 BD 1 2 N PHE B 236 ? N PHE B 1883 O PHE B 271 ? O PHE B 1918 BE 1 2 N MET B 287 ? N MET B 1934 O LEU B 368 ? O LEU B 2015 BE 2 3 N VAL B 369 ? N VAL B 2016 O GLY B 347 ? O GLY B 1994 BE 3 4 N GLU B 352 ? N GLU B 1999 O HIS B 310 ? O HIS B 1957 BE 4 5 N ILE B 309 ? N ILE B 1956 O TYR B 329 ? O TYR B 1976 BF 1 2 N THR B 376 ? N THR B 2023 O GLY B 521 ? O GLY B 2168 BF 2 3 N CYS B 522 ? N CYS B 2169 O ILE B 433 ? O ILE B 2080 BF 3 4 N ILE B 437 ? N ILE B 2084 O ASN B 491 ? O ASN B 2138 BF 4 5 O HIS B 508 ? O HIS B 2155 N SER B 452 ? N SER B 2099 BF 5 6 N TYR B 458 ? N TYR B 2105 O GLN B 466 ? O GLN B 2113 BG 1 2 N THR B 376 ? N THR B 2023 O GLY B 521 ? O GLY B 2168 BG 2 3 N CYS B 522 ? N CYS B 2169 O ILE B 433 ? O ILE B 2080 BG 3 4 N LYS B 425 ? N LYS B 2072 O THR B 391 ? O THR B 2038 BH 1 2 N ALA B 442 ? N ALA B 2089 O LEU B 449 ? O LEU B 2096 BI 1 2 N THR B 376 ? N THR B 2023 O GLY B 521 ? O GLY B 2168 BI 2 3 N CYS B 522 ? N CYS B 2169 O ILE B 433 ? O ILE B 2080 BI 3 4 N ILE B 437 ? N ILE B 2084 O ASN B 491 ? O ASN B 2138 BI 4 5 O HIS B 508 ? O HIS B 2155 N SER B 452 ? N SER B 2099 BI 5 6 N PHE B 454 ? N PHE B 2101 O PHE B 479 ? O PHE B 2126 BJ 1 2 N GLN B 466 ? N GLN B 2113 O TYR B 458 ? O TYR B 2105 BK 1 2 N THR B 376 ? N THR B 2023 O GLY B 521 ? O GLY B 2168 BK 2 3 N CYS B 522 ? N CYS B 2169 O ILE B 433 ? O ILE B 2080 BK 3 4 N ILE B 437 ? N ILE B 2084 O ASN B 491 ? O ASN B 2138 BK 4 5 O HIS B 508 ? O HIS B 2155 N SER B 452 ? N SER B 2099 BK 5 6 N LEU B 449 ? N LEU B 2096 O ALA B 442 ? O ALA B 2089 BL 1 2 N THR B 417 ? N THR B 2064 O SER B 513 ? O SER B 2160 BM 1 2 N MET B 529 ? N MET B 2176 O GLY B 678 ? O GLY B 2325 BM 2 3 N CYS B 679 ? N CYS B 2326 O LYS B 592 ? O LYS B 2239 BM 3 4 N THR B 598 ? N THR B 2245 O VAL B 646 ? O VAL B 2293 BM 4 5 N GLN B 664 ? N GLN B 2311 O GLU B 612 ? O GLU B 2259 BM 5 6 N PHE B 613 ? N PHE B 2260 O PHE B 636 ? O PHE B 2283 BN 1 2 N MET B 529 ? N MET B 2176 O GLY B 678 ? O GLY B 2325 BN 2 3 N CYS B 679 ? N CYS B 2326 O LYS B 592 ? O LYS B 2239 BN 3 4 N GLN B 584 ? N GLN B 2231 O THR B 544 ? O THR B 2191 BO 1 2 N VAL B 601 ? N VAL B 2248 O MET B 608 ? O MET B 2255 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 800' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 801' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO A 3333' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 B 1' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO B 3333' AC6 Software ? ? ? ? 2 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 239 RESIDUES 1755 TO 1756' AC7 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B2118 RESIDUES 2334 TO 2338' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 HIS A 267 ? HIS A 267 . ? 1_555 ? 2 AC1 5 CYS A 310 ? CYS A 310 . ? 1_555 ? 3 AC1 5 ILE A 312 ? ILE A 312 . ? 1_555 ? 4 AC1 5 HIS A 315 ? HIS A 315 . ? 1_555 ? 5 AC1 5 MET A 320 ? MET A 320 . ? 1_555 ? 6 AC2 5 LYS A 107 ? LYS A 107 . ? 1_555 ? 7 AC2 5 ASP A 116 ? ASP A 116 . ? 1_555 ? 8 AC2 5 GLU A 122 ? GLU A 122 . ? 1_555 ? 9 AC2 5 ASP A 125 ? ASP A 125 . ? 1_555 ? 10 AC2 5 ASP A 126 ? ASP A 126 . ? 1_555 ? 11 AC3 4 THR A 292 ? THR A 292 . ? 1_555 ? 12 AC3 4 PHE A 293 ? PHE A 293 . ? 1_555 ? 13 AC3 4 MET B 326 ? MET B 1973 . ? 1_555 ? 14 AC3 4 ASN B 330 ? ASN B 1977 . ? 1_555 ? 15 AC4 4 HIS B 307 ? HIS B 1954 . ? 1_555 ? 16 AC4 4 CYS B 353 ? CYS B 2000 . ? 1_555 ? 17 AC4 4 ILE B 355 ? ILE B 2002 . ? 1_555 ? 18 AC4 4 HIS B 358 ? HIS B 2005 . ? 1_555 ? 19 AC5 4 HIS B 220 ? HIS B 1867 . ? 1_555 ? 20 AC5 4 ARG B 222 ? ARG B 1869 . ? 1_555 ? 21 AC5 4 SER B 472 ? SER B 2119 . ? 1_555 ? 22 AC5 4 NAG I . ? NAG B 2334 . ? 1_555 ? 23 AC6 2 ASN A 239 ? ASN A 239 . ? 1_555 ? 24 AC6 2 HIS A 317 ? HIS A 317 . ? 1_555 ? 25 AC7 5 VAL B 224 ? VAL B 1871 . ? 1_555 ? 26 AC7 5 GLN B 291 ? GLN B 1938 . ? 1_555 ? 27 AC7 5 ASN B 471 ? ASN B 2118 . ? 1_555 ? 28 AC7 5 ASN B 494 ? ASN B 2141 . ? 1_555 ? 29 AC7 5 EDO N . ? EDO B 3333 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BDV _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4BDV _atom_sites.fract_transf_matrix[1][1] 0.007472 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007472 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.002810 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA CU N O S ZN # 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 . ALA A 1 1 ? -60.521 -44.240 55.051 1.00 156.18 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -59.364 -43.364 54.762 1.00 163.00 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? -59.608 -41.899 55.174 1.00 166.29 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -59.317 -41.007 54.367 1.00 190.92 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? -58.988 -43.461 53.273 1.00 161.03 ? 1 ALA A CB 1 ATOM 6 N N . THR A 1 2 ? -60.116 -41.642 56.398 1.00 150.41 ? 2 THR A N 1 ATOM 7 C CA . THR A 1 2 ? -60.402 -40.246 56.864 1.00 151.95 ? 2 THR A CA 1 ATOM 8 C C . THR A 1 2 ? -61.305 -40.081 58.121 1.00 157.70 ? 2 THR A C 1 ATOM 9 O O . THR A 1 2 ? -62.446 -40.535 58.125 1.00 171.43 ? 2 THR A O 1 ATOM 10 C CB . THR A 1 2 ? -60.918 -39.354 55.689 1.00 156.53 ? 2 THR A CB 1 ATOM 11 O OG1 . THR A 1 2 ? -60.437 -38.014 55.847 1.00 154.56 ? 2 THR A OG1 1 ATOM 12 C CG2 . THR A 1 2 ? -62.475 -39.393 55.486 1.00 150.04 ? 2 THR A CG2 1 ATOM 13 N N . ARG A 1 3 ? -60.834 -39.377 59.156 1.00 160.16 ? 3 ARG A N 1 ATOM 14 C CA . ARG A 1 3 ? -61.411 -39.542 60.514 1.00 159.95 ? 3 ARG A CA 1 ATOM 15 C C . ARG A 1 3 ? -61.545 -38.298 61.423 1.00 161.85 ? 3 ARG A C 1 ATOM 16 O O . ARG A 1 3 ? -60.760 -38.163 62.364 1.00 166.04 ? 3 ARG A O 1 ATOM 17 C CB . ARG A 1 3 ? -60.505 -40.537 61.235 1.00 152.71 ? 3 ARG A CB 1 ATOM 18 C CG . ARG A 1 3 ? -61.198 -41.514 62.147 1.00 149.83 ? 3 ARG A CG 1 ATOM 19 C CD . ARG A 1 3 ? -60.457 -42.845 62.102 1.00 149.13 ? 3 ARG A CD 1 ATOM 20 N NE . ARG A 1 3 ? -60.805 -43.644 60.923 1.00 160.70 ? 3 ARG A NE 1 ATOM 21 C CZ . ARG A 1 3 ? -60.872 -44.976 60.897 1.00 165.60 ? 3 ARG A CZ 1 ATOM 22 N NH1 . ARG A 1 3 ? -60.604 -45.674 61.988 1.00 174.70 ? 3 ARG A NH1 1 ATOM 23 N NH2 . ARG A 1 3 ? -61.211 -45.619 59.781 1.00 167.81 ? 3 ARG A NH2 1 ATOM 24 N N . ARG A 1 4 ? -62.533 -37.424 61.208 1.00 159.82 ? 4 ARG A N 1 ATOM 25 C CA . ARG A 1 4 ? -62.543 -36.129 61.939 1.00 161.98 ? 4 ARG A CA 1 ATOM 26 C C . ARG A 1 4 ? -63.006 -36.134 63.409 1.00 165.52 ? 4 ARG A C 1 ATOM 27 O O . ARG A 1 4 ? -64.081 -36.640 63.739 1.00 165.92 ? 4 ARG A O 1 ATOM 28 C CB . ARG A 1 4 ? -63.269 -35.019 61.167 1.00 165.80 ? 4 ARG A CB 1 ATOM 29 C CG . ARG A 1 4 ? -62.962 -33.617 61.709 1.00 172.44 ? 4 ARG A CG 1 ATOM 30 C CD . ARG A 1 4 ? -63.572 -32.488 60.886 1.00 183.55 ? 4 ARG A CD 1 ATOM 31 N NE . ARG A 1 4 ? -62.817 -32.198 59.662 1.00 190.68 ? 4 ARG A NE 1 ATOM 32 C CZ . ARG A 1 4 ? -63.113 -32.668 58.444 1.00 194.65 ? 4 ARG A CZ 1 ATOM 33 N NH1 . ARG A 1 4 ? -64.167 -33.467 58.271 1.00 204.91 ? 4 ARG A NH1 1 ATOM 34 N NH2 . ARG A 1 4 ? -62.353 -32.345 57.389 1.00 175.05 ? 4 ARG A NH2 1 ATOM 35 N N . TYR A 1 5 ? -62.186 -35.523 64.269 1.00 167.09 ? 5 TYR A N 1 ATOM 36 C CA . TYR A 1 5 ? -62.394 -35.499 65.724 1.00 159.57 ? 5 TYR A CA 1 ATOM 37 C C . TYR A 1 5 ? -62.560 -34.084 66.312 1.00 165.69 ? 5 TYR A C 1 ATOM 38 O O . TYR A 1 5 ? -61.624 -33.263 66.292 1.00 159.35 ? 5 TYR A O 1 ATOM 39 C CB . TYR A 1 5 ? -61.246 -36.233 66.413 1.00 141.42 ? 5 TYR A CB 1 ATOM 40 C CG . TYR A 1 5 ? -61.291 -37.723 66.236 1.00 139.31 ? 5 TYR A CG 1 ATOM 41 C CD1 . TYR A 1 5 ? -62.450 -38.365 65.781 1.00 152.09 ? 5 TYR A CD1 1 ATOM 42 C CD2 . TYR A 1 5 ? -60.196 -38.506 66.564 1.00 142.16 ? 5 TYR A CD2 1 ATOM 43 C CE1 . TYR A 1 5 ? -62.504 -39.749 65.634 1.00 169.36 ? 5 TYR A CE1 1 ATOM 44 C CE2 . TYR A 1 5 ? -60.232 -39.894 66.424 1.00 155.98 ? 5 TYR A CE2 1 ATOM 45 C CZ . TYR A 1 5 ? -61.386 -40.516 65.965 1.00 172.34 ? 5 TYR A CZ 1 ATOM 46 O OH . TYR A 1 5 ? -61.420 -41.898 65.848 1.00 184.88 ? 5 TYR A OH 1 ATOM 47 N N . TYR A 1 6 ? -63.747 -33.816 66.861 1.00 161.31 ? 6 TYR A N 1 ATOM 48 C CA . TYR A 1 6 ? -64.121 -32.443 67.217 1.00 160.65 ? 6 TYR A CA 1 ATOM 49 C C . TYR A 1 6 ? -63.600 -31.908 68.560 1.00 161.46 ? 6 TYR A C 1 ATOM 50 O O . TYR A 1 6 ? -64.141 -30.927 69.096 1.00 162.31 ? 6 TYR A O 1 ATOM 51 C CB . TYR A 1 6 ? -65.630 -32.225 67.035 1.00 161.84 ? 6 TYR A CB 1 ATOM 52 C CG . TYR A 1 6 ? -65.961 -31.658 65.668 1.00 170.25 ? 6 TYR A CG 1 ATOM 53 C CD1 . TYR A 1 6 ? -65.034 -31.745 64.624 1.00 169.46 ? 6 TYR A CD1 1 ATOM 54 C CD2 . TYR A 1 6 ? -67.176 -31.011 65.418 1.00 176.11 ? 6 TYR A CD2 1 ATOM 55 C CE1 . TYR A 1 6 ? -65.305 -31.222 63.374 1.00 175.07 ? 6 TYR A CE1 1 ATOM 56 C CE2 . TYR A 1 6 ? -67.462 -30.486 64.160 1.00 181.56 ? 6 TYR A CE2 1 ATOM 57 C CZ . TYR A 1 6 ? -66.512 -30.599 63.142 1.00 183.80 ? 6 TYR A CZ 1 ATOM 58 O OH . TYR A 1 6 ? -66.736 -30.096 61.881 1.00 196.33 ? 6 TYR A OH 1 ATOM 59 N N . LEU A 1 7 ? -62.505 -32.519 69.029 1.00 148.67 ? 7 LEU A N 1 ATOM 60 C CA . LEU A 1 7 ? -61.899 -32.339 70.362 1.00 142.22 ? 7 LEU A CA 1 ATOM 61 C C . LEU A 1 7 ? -61.851 -30.928 71.016 1.00 151.75 ? 7 LEU A C 1 ATOM 62 O O . LEU A 1 7 ? -61.729 -29.915 70.327 1.00 158.95 ? 7 LEU A O 1 ATOM 63 C CB . LEU A 1 7 ? -60.506 -32.927 70.293 1.00 132.99 ? 7 LEU A CB 1 ATOM 64 C CG . LEU A 1 7 ? -59.906 -33.508 71.566 1.00 144.52 ? 7 LEU A CG 1 ATOM 65 C CD1 . LEU A 1 7 ? -59.137 -34.794 71.277 1.00 152.09 ? 7 LEU A CD1 1 ATOM 66 C CD2 . LEU A 1 7 ? -59.005 -32.489 72.239 1.00 147.04 ? 7 LEU A CD2 1 ATOM 67 N N . GLY A 1 8 ? -61.939 -30.878 72.352 1.00 152.00 ? 8 GLY A N 1 ATOM 68 C CA . GLY A 1 8 ? -61.897 -29.612 73.129 1.00 154.73 ? 8 GLY A CA 1 ATOM 69 C C . GLY A 1 8 ? -61.169 -29.722 74.474 1.00 159.59 ? 8 GLY A C 1 ATOM 70 O O . GLY A 1 8 ? -61.144 -30.799 75.091 1.00 154.74 ? 8 GLY A O 1 ATOM 71 N N . ALA A 1 9 ? -60.577 -28.615 74.937 1.00 161.82 ? 9 ALA A N 1 ATOM 72 C CA . ALA A 1 9 ? -59.588 -28.674 76.040 1.00 164.51 ? 9 ALA A CA 1 ATOM 73 C C . ALA A 1 9 ? -60.063 -28.048 77.320 1.00 168.89 ? 9 ALA A C 1 ATOM 74 O O . ALA A 1 9 ? -59.542 -27.011 77.737 1.00 170.31 ? 9 ALA A O 1 ATOM 75 C CB . ALA A 1 9 ? -58.264 -28.045 75.633 1.00 164.59 ? 9 ALA A CB 1 ATOM 76 N N . VAL A 1 10 ? -61.004 -28.731 77.963 1.00 176.75 ? 10 VAL A N 1 ATOM 77 C CA . VAL A 1 10 ? -61.790 -28.186 79.077 1.00 188.25 ? 10 VAL A CA 1 ATOM 78 C C . VAL A 1 10 ? -61.223 -28.437 80.485 1.00 192.71 ? 10 VAL A C 1 ATOM 79 O O . VAL A 1 10 ? -60.581 -29.453 80.744 1.00 203.46 ? 10 VAL A O 1 ATOM 80 C CB . VAL A 1 10 ? -63.246 -28.697 78.981 1.00 186.01 ? 10 VAL A CB 1 ATOM 81 C CG1 . VAL A 1 10 ? -64.082 -28.303 80.205 1.00 183.53 ? 10 VAL A CG1 1 ATOM 82 C CG2 . VAL A 1 10 ? -63.860 -28.204 77.674 1.00 180.73 ? 10 VAL A CG2 1 ATOM 83 N N . GLU A 1 11 ? -61.461 -27.491 81.386 1.00 191.09 ? 11 GLU A N 1 ATOM 84 C CA . GLU A 1 11 ? -61.102 -27.670 82.775 1.00 189.23 ? 11 GLU A CA 1 ATOM 85 C C . GLU A 1 11 ? -62.341 -28.060 83.557 1.00 195.45 ? 11 GLU A C 1 ATOM 86 O O . GLU A 1 11 ? -63.285 -27.264 83.682 1.00 203.68 ? 11 GLU A O 1 ATOM 87 C CB . GLU A 1 11 ? -60.434 -26.409 83.350 1.00 193.32 ? 11 GLU A CB 1 ATOM 88 C CG . GLU A 1 11 ? -61.028 -25.078 82.898 1.00 199.42 ? 11 GLU A CG 1 ATOM 89 C CD . GLU A 1 11 ? -60.056 -23.914 83.036 1.00 203.46 ? 11 GLU A CD 1 ATOM 90 O OE1 . GLU A 1 11 ? -58.827 -24.136 82.951 1.00 192.40 ? 11 GLU A OE1 1 ATOM 91 O OE2 . GLU A 1 11 ? -60.523 -22.766 83.221 1.00 222.32 ? 11 GLU A OE2 1 ATOM 92 N N . LEU A 1 12 ? -62.352 -29.303 84.043 1.00 185.01 ? 12 LEU A N 1 ATOM 93 C CA . LEU A 1 12 ? -63.353 -29.706 85.027 1.00 185.30 ? 12 LEU A CA 1 ATOM 94 C C . LEU A 1 12 ? -62.723 -30.108 86.391 1.00 171.30 ? 12 LEU A C 1 ATOM 95 O O . LEU A 1 12 ? -61.671 -29.575 86.757 1.00 165.22 ? 12 LEU A O 1 ATOM 96 C CB . LEU A 1 12 ? -64.414 -30.670 84.431 1.00 190.88 ? 12 LEU A CB 1 ATOM 97 C CG . LEU A 1 12 ? -65.622 -29.992 83.700 1.00 207.04 ? 12 LEU A CG 1 ATOM 98 C CD1 . LEU A 1 12 ? -66.003 -30.727 82.408 1.00 184.74 ? 12 LEU A CD1 1 ATOM 99 C CD2 . LEU A 1 12 ? -66.868 -29.681 84.574 1.00 205.17 ? 12 LEU A CD2 1 ATOM 100 N N . SER A 1 13 ? -63.368 -30.999 87.145 1.00 164.45 ? 13 SER A N 1 ATOM 101 C CA . SER A 1 13 ? -63.057 -31.194 88.581 1.00 164.14 ? 13 SER A CA 1 ATOM 102 C C . SER A 1 13 ? -62.927 -32.690 89.055 1.00 163.20 ? 13 SER A C 1 ATOM 103 O O . SER A 1 13 ? -63.891 -33.436 88.930 1.00 169.06 ? 13 SER A O 1 ATOM 104 C CB . SER A 1 13 ? -64.087 -30.384 89.416 1.00 165.17 ? 13 SER A CB 1 ATOM 105 O OG . SER A 1 13 ? -65.201 -29.923 88.645 1.00 155.39 ? 13 SER A OG 1 ATOM 106 N N . TRP A 1 14 ? -61.782 -33.125 89.616 1.00 161.20 ? 14 TRP A N 1 ATOM 107 C CA . TRP A 1 14 ? -61.454 -34.595 89.703 1.00 176.39 ? 14 TRP A CA 1 ATOM 108 C C . TRP A 1 14 ? -61.748 -35.477 90.987 1.00 195.60 ? 14 TRP A C 1 ATOM 109 O O . TRP A 1 14 ? -62.207 -34.937 91.995 1.00 223.25 ? 14 TRP A O 1 ATOM 110 C CB . TRP A 1 14 ? -59.998 -34.808 89.265 1.00 178.81 ? 14 TRP A CB 1 ATOM 111 C CG . TRP A 1 14 ? -59.743 -36.231 88.870 1.00 187.94 ? 14 TRP A CG 1 ATOM 112 C CD1 . TRP A 1 14 ? -58.658 -37.006 89.196 1.00 193.20 ? 14 TRP A CD1 1 ATOM 113 C CD2 . TRP A 1 14 ? -60.630 -37.073 88.114 1.00 177.51 ? 14 TRP A CD2 1 ATOM 114 N NE1 . TRP A 1 14 ? -58.810 -38.271 88.668 1.00 189.70 ? 14 TRP A NE1 1 ATOM 115 C CE2 . TRP A 1 14 ? -60.012 -38.335 88.002 1.00 177.90 ? 14 TRP A CE2 1 ATOM 116 C CE3 . TRP A 1 14 ? -61.891 -36.880 87.527 1.00 160.61 ? 14 TRP A CE3 1 ATOM 117 C CZ2 . TRP A 1 14 ? -60.609 -39.391 87.317 1.00 164.14 ? 14 TRP A CZ2 1 ATOM 118 C CZ3 . TRP A 1 14 ? -62.477 -37.920 86.859 1.00 152.11 ? 14 TRP A CZ3 1 ATOM 119 C CH2 . TRP A 1 14 ? -61.839 -39.159 86.753 1.00 157.88 ? 14 TRP A CH2 1 ATOM 120 N N . ASP A 1 15 ? -61.539 -36.820 90.917 1.00 192.02 ? 15 ASP A N 1 ATOM 121 C CA . ASP A 1 15 ? -61.157 -37.655 92.117 1.00 178.28 ? 15 ASP A CA 1 ATOM 122 C C . ASP A 1 15 ? -61.181 -39.212 92.316 1.00 175.77 ? 15 ASP A C 1 ATOM 123 O O . ASP A 1 15 ? -60.113 -39.896 92.234 1.00 143.48 ? 15 ASP A O 1 ATOM 124 C CB . ASP A 1 15 ? -61.778 -37.073 93.359 1.00 181.27 ? 15 ASP A CB 1 ATOM 125 C CG . ASP A 1 15 ? -60.808 -37.059 94.462 1.00 196.99 ? 15 ASP A CG 1 ATOM 126 O OD1 . ASP A 1 15 ? -59.598 -37.274 94.146 1.00 187.37 ? 15 ASP A OD1 1 ATOM 127 O OD2 . ASP A 1 15 ? -61.240 -36.849 95.616 1.00 219.48 ? 15 ASP A OD2 1 ATOM 128 N N . TYR A 1 16 ? -62.404 -39.701 92.636 1.00 184.75 ? 16 TYR A N 1 ATOM 129 C CA . TYR A 1 16 ? -62.766 -40.949 93.415 1.00 176.35 ? 16 TYR A CA 1 ATOM 130 C C . TYR A 1 16 ? -61.631 -41.775 94.022 1.00 161.78 ? 16 TYR A C 1 ATOM 131 O O . TYR A 1 16 ? -61.690 -42.114 95.212 1.00 153.89 ? 16 TYR A O 1 ATOM 132 C CB . TYR A 1 16 ? -63.821 -41.877 92.725 1.00 174.93 ? 16 TYR A CB 1 ATOM 133 C CG . TYR A 1 16 ? -64.673 -41.242 91.633 1.00 191.93 ? 16 TYR A CG 1 ATOM 134 C CD1 . TYR A 1 16 ? -64.132 -40.246 90.805 1.00 210.08 ? 16 TYR A CD1 1 ATOM 135 C CD2 . TYR A 1 16 ? -65.996 -41.640 91.401 1.00 191.07 ? 16 TYR A CD2 1 ATOM 136 C CE1 . TYR A 1 16 ? -64.855 -39.643 89.789 1.00 209.10 ? 16 TYR A CE1 1 ATOM 137 C CE2 . TYR A 1 16 ? -66.742 -41.043 90.374 1.00 213.51 ? 16 TYR A CE2 1 ATOM 138 C CZ . TYR A 1 16 ? -66.151 -40.030 89.558 1.00 216.90 ? 16 TYR A CZ 1 ATOM 139 O OH . TYR A 1 16 ? -66.793 -39.373 88.510 1.00 206.74 ? 16 TYR A OH 1 ATOM 140 N N . VAL A 1 44 ? -62.326 -36.726 99.625 1.00 189.54 ? 44 VAL A N 1 ATOM 141 C CA . VAL A 1 44 ? -62.869 -35.360 99.603 1.00 211.44 ? 44 VAL A CA 1 ATOM 142 C C . VAL A 1 44 ? -61.915 -34.345 98.851 1.00 212.19 ? 44 VAL A C 1 ATOM 143 O O . VAL A 1 44 ? -61.989 -33.144 99.088 1.00 225.00 ? 44 VAL A O 1 ATOM 144 C CB . VAL A 1 44 ? -63.389 -34.862 101.048 1.00 221.24 ? 44 VAL A CB 1 ATOM 145 C CG1 . VAL A 1 44 ? -64.903 -34.566 101.108 1.00 210.16 ? 44 VAL A CG1 1 ATOM 146 C CG2 . VAL A 1 44 ? -63.006 -35.804 102.198 1.00 215.98 ? 44 VAL A CG2 1 ATOM 147 N N . VAL A 1 45 ? -61.072 -34.804 97.910 1.00 209.75 ? 45 VAL A N 1 ATOM 148 C CA . VAL A 1 45 ? -59.938 -33.958 97.360 1.00 216.08 ? 45 VAL A CA 1 ATOM 149 C C . VAL A 1 45 ? -59.962 -33.449 95.831 1.00 225.82 ? 45 VAL A C 1 ATOM 150 O O . VAL A 1 45 ? -60.951 -33.687 95.130 1.00 227.11 ? 45 VAL A O 1 ATOM 151 C CB . VAL A 1 45 ? -58.540 -34.551 97.812 1.00 205.89 ? 45 VAL A CB 1 ATOM 152 C CG1 . VAL A 1 45 ? -58.467 -34.738 99.326 1.00 200.80 ? 45 VAL A CG1 1 ATOM 153 C CG2 . VAL A 1 45 ? -58.222 -35.885 97.152 1.00 185.97 ? 45 VAL A CG2 1 ATOM 154 N N . TYR A 1 46 ? -58.922 -32.681 95.400 1.00 231.91 ? 46 TYR A N 1 ATOM 155 C CA . TYR A 1 46 ? -58.420 -32.274 93.968 1.00 213.86 ? 46 TYR A CA 1 ATOM 156 C C . TYR A 1 46 ? -59.198 -31.992 92.609 1.00 191.66 ? 46 TYR A C 1 ATOM 157 O O . TYR A 1 46 ? -60.149 -32.693 92.285 1.00 183.96 ? 46 TYR A O 1 ATOM 158 C CB . TYR A 1 46 ? -57.125 -33.027 93.625 1.00 219.51 ? 46 TYR A CB 1 ATOM 159 C CG . TYR A 1 46 ? -56.029 -32.817 94.643 1.00 237.45 ? 46 TYR A CG 1 ATOM 160 C CD1 . TYR A 1 46 ? -55.431 -31.569 94.806 1.00 242.53 ? 46 TYR A CD1 1 ATOM 161 C CD2 . TYR A 1 46 ? -55.605 -33.866 95.464 1.00 251.79 ? 46 TYR A CD2 1 ATOM 162 C CE1 . TYR A 1 46 ? -54.427 -31.373 95.739 1.00 261.59 ? 46 TYR A CE1 1 ATOM 163 C CE2 . TYR A 1 46 ? -54.604 -33.681 96.402 1.00 261.14 ? 46 TYR A CE2 1 ATOM 164 C CZ . TYR A 1 46 ? -54.020 -32.432 96.532 1.00 268.10 ? 46 TYR A CZ 1 ATOM 165 O OH . TYR A 1 46 ? -53.031 -32.243 97.460 1.00 293.05 ? 46 TYR A OH 1 ATOM 166 N N . LYS A 1 47 ? -58.721 -31.040 91.782 1.00 181.21 ? 47 LYS A N 1 ATOM 167 C CA . LYS A 1 47 ? -59.495 -30.555 90.587 1.00 180.70 ? 47 LYS A CA 1 ATOM 168 C C . LYS A 1 47 ? -58.774 -29.713 89.460 1.00 179.79 ? 47 LYS A C 1 ATOM 169 O O . LYS A 1 47 ? -58.472 -28.528 89.672 1.00 168.03 ? 47 LYS A O 1 ATOM 170 C CB . LYS A 1 47 ? -60.736 -29.770 91.068 1.00 192.36 ? 47 LYS A CB 1 ATOM 171 C CG . LYS A 1 47 ? -61.701 -30.518 92.008 1.00 188.37 ? 47 LYS A CG 1 ATOM 172 C CD . LYS A 1 47 ? -61.499 -30.220 93.498 1.00 179.60 ? 47 LYS A CD 1 ATOM 173 C CE . LYS A 1 47 ? -62.122 -31.301 94.371 1.00 166.29 ? 47 LYS A CE 1 ATOM 174 N NZ . LYS A 1 47 ? -61.555 -31.299 95.749 1.00 163.26 ? 47 LYS A NZ 1 ATOM 175 N N . LYS A 1 48 ? -58.598 -30.304 88.257 1.00 183.33 ? 48 LYS A N 1 ATOM 176 C CA . LYS A 1 48 ? -57.798 -29.723 87.108 1.00 182.11 ? 48 LYS A CA 1 ATOM 177 C C . LYS A 1 48 ? -58.361 -29.748 85.611 1.00 184.77 ? 48 LYS A C 1 ATOM 178 O O . LYS A 1 48 ? -59.444 -30.285 85.364 1.00 189.30 ? 48 LYS A O 1 ATOM 179 C CB . LYS A 1 48 ? -56.333 -30.233 87.157 1.00 164.53 ? 48 LYS A CB 1 ATOM 180 C CG . LYS A 1 48 ? -56.056 -31.522 87.925 1.00 154.88 ? 48 LYS A CG 1 ATOM 181 C CD . LYS A 1 48 ? -56.653 -32.782 87.292 1.00 154.86 ? 48 LYS A CD 1 ATOM 182 C CE . LYS A 1 48 ? -55.921 -34.077 87.706 1.00 161.69 ? 48 LYS A CE 1 ATOM 183 N NZ . LYS A 1 48 ? -56.056 -34.632 89.104 1.00 154.39 ? 48 LYS A NZ 1 ATOM 184 N N . THR A 1 49 ? -57.614 -29.164 84.647 1.00 182.89 ? 49 THR A N 1 ATOM 185 C CA . THR A 1 49 ? -57.925 -29.134 83.159 1.00 170.62 ? 49 THR A CA 1 ATOM 186 C C . THR A 1 49 ? -57.496 -30.379 82.338 1.00 159.53 ? 49 THR A C 1 ATOM 187 O O . THR A 1 49 ? -56.362 -30.819 82.467 1.00 152.67 ? 49 THR A O 1 ATOM 188 C CB . THR A 1 49 ? -57.366 -27.843 82.438 1.00 177.85 ? 49 THR A CB 1 ATOM 189 O OG1 . THR A 1 49 ? -56.870 -28.147 81.119 1.00 164.68 ? 49 THR A OG1 1 ATOM 190 C CG2 . THR A 1 49 ? -56.239 -27.182 83.213 1.00 182.80 ? 49 THR A CG2 1 ATOM 191 N N . LEU A 1 50 ? -58.388 -30.910 81.480 1.00 161.42 ? 50 LEU A N 1 ATOM 192 C CA . LEU A 1 50 ? -58.155 -32.166 80.662 1.00 158.09 ? 50 LEU A CA 1 ATOM 193 C C . LEU A 1 50 ? -58.891 -32.271 79.274 1.00 160.35 ? 50 LEU A C 1 ATOM 194 O O . LEU A 1 50 ? -59.755 -31.453 78.953 1.00 166.39 ? 50 LEU A O 1 ATOM 195 C CB . LEU A 1 50 ? -58.359 -33.443 81.522 1.00 141.35 ? 50 LEU A CB 1 ATOM 196 C CG . LEU A 1 50 ? -58.887 -33.223 82.957 1.00 142.25 ? 50 LEU A CG 1 ATOM 197 C CD1 . LEU A 1 50 ? -60.407 -33.326 83.058 1.00 135.56 ? 50 LEU A CD1 1 ATOM 198 C CD2 . LEU A 1 50 ? -58.195 -34.095 83.997 1.00 132.68 ? 50 LEU A CD2 1 ATOM 199 N N . PHE A 1 51 ? -58.547 -33.264 78.451 1.00 154.20 ? 51 PHE A N 1 ATOM 200 C CA . PHE A 1 51 ? -59.124 -33.355 77.091 1.00 147.81 ? 51 PHE A CA 1 ATOM 201 C C . PHE A 1 51 ? -60.592 -33.792 77.080 1.00 138.82 ? 51 PHE A C 1 ATOM 202 O O . PHE A 1 51 ? -61.117 -34.149 78.114 1.00 133.31 ? 51 PHE A O 1 ATOM 203 C CB . PHE A 1 51 ? -58.280 -34.284 76.216 1.00 153.78 ? 51 PHE A CB 1 ATOM 204 C CG . PHE A 1 51 ? -57.005 -33.659 75.713 1.00 154.93 ? 51 PHE A CG 1 ATOM 205 C CD1 . PHE A 1 51 ? -57.040 -32.609 74.791 1.00 152.40 ? 51 PHE A CD1 1 ATOM 206 C CD2 . PHE A 1 51 ? -55.768 -34.121 76.151 1.00 149.21 ? 51 PHE A CD2 1 ATOM 207 C CE1 . PHE A 1 51 ? -55.874 -32.032 74.313 1.00 146.64 ? 51 PHE A CE1 1 ATOM 208 C CE2 . PHE A 1 51 ? -54.595 -33.549 75.675 1.00 144.61 ? 51 PHE A CE2 1 ATOM 209 C CZ . PHE A 1 51 ? -54.649 -32.500 74.762 1.00 148.59 ? 51 PHE A CZ 1 ATOM 210 N N . VAL A 1 52 ? -61.256 -33.750 75.923 1.00 139.23 ? 52 VAL A N 1 ATOM 211 C CA . VAL A 1 52 ? -62.664 -34.218 75.790 1.00 144.23 ? 52 VAL A CA 1 ATOM 212 C C . VAL A 1 52 ? -63.268 -34.167 74.377 1.00 153.46 ? 52 VAL A C 1 ATOM 213 O O . VAL A 1 52 ? -62.689 -33.589 73.457 1.00 159.26 ? 52 VAL A O 1 ATOM 214 C CB . VAL A 1 52 ? -63.634 -33.463 76.708 1.00 142.63 ? 52 VAL A CB 1 ATOM 215 C CG1 . VAL A 1 52 ? -63.286 -31.984 76.771 1.00 144.47 ? 52 VAL A CG1 1 ATOM 216 C CG2 . VAL A 1 52 ? -65.056 -33.652 76.215 1.00 138.48 ? 52 VAL A CG2 1 ATOM 217 N N . GLU A 1 53 ? -64.472 -34.715 74.239 1.00 154.21 ? 53 GLU A N 1 ATOM 218 C CA . GLU A 1 53 ? -64.986 -35.101 72.934 1.00 164.56 ? 53 GLU A CA 1 ATOM 219 C C . GLU A 1 53 ? -65.677 -34.034 72.068 1.00 160.18 ? 53 GLU A C 1 ATOM 220 O O . GLU A 1 53 ? -65.174 -33.722 70.996 1.00 155.38 ? 53 GLU A O 1 ATOM 221 C CB . GLU A 1 53 ? -65.880 -36.327 73.096 1.00 188.53 ? 53 GLU A CB 1 ATOM 222 C CG . GLU A 1 53 ? -65.154 -37.581 73.566 1.00 217.83 ? 53 GLU A CG 1 ATOM 223 C CD . GLU A 1 53 ? -64.666 -38.475 72.419 1.00 228.27 ? 53 GLU A CD 1 ATOM 224 O OE1 . GLU A 1 53 ? -64.739 -38.057 71.227 1.00 205.38 ? 53 GLU A OE1 1 ATOM 225 O OE2 . GLU A 1 53 ? -64.209 -39.612 72.724 1.00 235.13 ? 53 GLU A OE2 1 ATOM 226 N N . PHE A 1 54 ? -66.816 -33.514 72.541 1.00 171.69 ? 54 PHE A N 1 ATOM 227 C CA . PHE A 1 54 ? -67.833 -32.678 71.799 1.00 181.29 ? 54 PHE A CA 1 ATOM 228 C C . PHE A 1 54 ? -68.224 -33.024 70.363 1.00 180.88 ? 54 PHE A C 1 ATOM 229 O O . PHE A 1 54 ? -67.422 -33.547 69.589 1.00 185.96 ? 54 PHE A O 1 ATOM 230 C CB . PHE A 1 54 ? -67.539 -31.186 71.853 1.00 193.52 ? 54 PHE A CB 1 ATOM 231 C CG . PHE A 1 54 ? -66.945 -30.747 73.127 1.00 197.88 ? 54 PHE A CG 1 ATOM 232 C CD1 . PHE A 1 54 ? -67.576 -31.030 74.316 1.00 192.48 ? 54 PHE A CD1 1 ATOM 233 C CD2 . PHE A 1 54 ? -65.731 -30.072 73.136 1.00 208.76 ? 54 PHE A CD2 1 ATOM 234 C CE1 . PHE A 1 54 ? -67.003 -30.642 75.501 1.00 203.30 ? 54 PHE A CE1 1 ATOM 235 C CE2 . PHE A 1 54 ? -65.156 -29.666 74.319 1.00 207.39 ? 54 PHE A CE2 1 ATOM 236 C CZ . PHE A 1 54 ? -65.795 -29.957 75.503 1.00 206.51 ? 54 PHE A CZ 1 ATOM 237 N N . THR A 1 55 ? -69.460 -32.672 70.009 1.00 180.81 ? 55 THR A N 1 ATOM 238 C CA . THR A 1 55 ? -69.959 -32.935 68.658 1.00 185.09 ? 55 THR A CA 1 ATOM 239 C C . THR A 1 55 ? -70.411 -31.684 67.870 1.00 198.71 ? 55 THR A C 1 ATOM 240 O O . THR A 1 55 ? -70.593 -31.734 66.647 1.00 198.13 ? 55 THR A O 1 ATOM 241 C CB . THR A 1 55 ? -71.006 -34.077 68.658 1.00 177.07 ? 55 THR A CB 1 ATOM 242 O OG1 . THR A 1 55 ? -70.674 -35.004 67.615 1.00 159.44 ? 55 THR A OG1 1 ATOM 243 C CG2 . THR A 1 55 ? -72.500 -33.562 68.545 1.00 181.05 ? 55 THR A CG2 1 ATOM 244 N N . ASP A 1 56 ? -70.555 -30.568 68.579 1.00 208.52 ? 56 ASP A N 1 ATOM 245 C CA . ASP A 1 56 ? -70.882 -29.278 67.979 1.00 216.33 ? 56 ASP A CA 1 ATOM 246 C C . ASP A 1 56 ? -70.238 -29.022 66.620 1.00 220.87 ? 56 ASP A C 1 ATOM 247 O O . ASP A 1 56 ? -69.353 -29.748 66.157 1.00 195.13 ? 56 ASP A O 1 ATOM 248 C CB . ASP A 1 56 ? -70.488 -28.126 68.929 1.00 217.78 ? 56 ASP A CB 1 ATOM 249 C CG . ASP A 1 56 ? -68.969 -27.831 68.936 1.00 209.31 ? 56 ASP A CG 1 ATOM 250 O OD1 . ASP A 1 56 ? -68.362 -27.633 67.858 1.00 201.56 ? 56 ASP A OD1 1 ATOM 251 O OD2 . ASP A 1 56 ? -68.376 -27.777 70.036 1.00 197.85 ? 56 ASP A OD2 1 ATOM 252 N N . HIS A 1 57 ? -70.698 -27.950 65.997 1.00 242.18 ? 57 HIS A N 1 ATOM 253 C CA . HIS A 1 57 ? -69.998 -27.371 64.887 1.00 240.38 ? 57 HIS A CA 1 ATOM 254 C C . HIS A 1 57 ? -69.297 -26.129 65.410 1.00 256.25 ? 57 HIS A C 1 ATOM 255 O O . HIS A 1 57 ? -68.115 -25.952 65.133 1.00 242.63 ? 57 HIS A O 1 ATOM 256 C CB . HIS A 1 57 ? -70.961 -27.036 63.757 1.00 247.65 ? 57 HIS A CB 1 ATOM 257 C CG . HIS A 1 57 ? -70.377 -27.240 62.398 1.00 249.01 ? 57 HIS A CG 1 ATOM 258 N ND1 . HIS A 1 57 ? -69.493 -28.259 62.117 1.00 238.81 ? 57 HIS A ND1 1 ATOM 259 C CD2 . HIS A 1 57 ? -70.564 -26.568 61.236 1.00 263.39 ? 57 HIS A CD2 1 ATOM 260 C CE1 . HIS A 1 57 ? -69.147 -28.197 60.843 1.00 250.75 ? 57 HIS A CE1 1 ATOM 261 N NE2 . HIS A 1 57 ? -69.783 -27.182 60.286 1.00 264.54 ? 57 HIS A NE2 1 ATOM 262 N N . LEU A 1 58 ? -70.007 -25.300 66.193 1.00 293.20 ? 58 LEU A N 1 ATOM 263 C CA . LEU A 1 58 ? -69.404 -24.080 66.800 1.00 318.95 ? 58 LEU A CA 1 ATOM 264 C C . LEU A 1 58 ? -68.635 -24.263 68.151 1.00 348.13 ? 58 LEU A C 1 ATOM 265 O O . LEU A 1 58 ? -67.413 -24.089 68.146 1.00 399.87 ? 58 LEU A O 1 ATOM 266 C CB . LEU A 1 58 ? -70.339 -22.820 66.776 1.00 285.85 ? 58 LEU A CB 1 ATOM 267 C CG . LEU A 1 58 ? -70.245 -21.743 65.648 1.00 249.94 ? 58 LEU A CG 1 ATOM 268 C CD1 . LEU A 1 58 ? -71.260 -20.600 65.795 1.00 229.21 ? 58 LEU A CD1 1 ATOM 269 C CD2 . LEU A 1 58 ? -68.831 -21.183 65.486 1.00 229.62 ? 58 LEU A CD2 1 ATOM 270 N N . PHE A 1 59 ? -69.289 -24.621 69.274 1.00 320.67 ? 59 PHE A N 1 ATOM 271 C CA . PHE A 1 59 ? -68.544 -24.772 70.576 1.00 280.17 ? 59 PHE A CA 1 ATOM 272 C C . PHE A 1 59 ? -68.984 -25.881 71.619 1.00 238.13 ? 59 PHE A C 1 ATOM 273 O O . PHE A 1 59 ? -68.147 -26.331 72.415 1.00 203.93 ? 59 PHE A O 1 ATOM 274 C CB . PHE A 1 59 ? -68.312 -23.373 71.270 1.00 298.06 ? 59 PHE A CB 1 ATOM 275 C CG . PHE A 1 59 ? -67.269 -22.459 70.581 1.00 298.89 ? 59 PHE A CG 1 ATOM 276 C CD1 . PHE A 1 59 ? -65.889 -22.681 70.726 1.00 282.69 ? 59 PHE A CD1 1 ATOM 277 C CD2 . PHE A 1 59 ? -67.670 -21.353 69.809 1.00 292.03 ? 59 PHE A CD2 1 ATOM 278 C CE1 . PHE A 1 59 ? -64.951 -21.848 70.100 1.00 261.14 ? 59 PHE A CE1 1 ATOM 279 C CE2 . PHE A 1 59 ? -66.729 -20.522 69.183 1.00 267.28 ? 59 PHE A CE2 1 ATOM 280 C CZ . PHE A 1 59 ? -65.370 -20.768 69.331 1.00 250.35 ? 59 PHE A CZ 1 ATOM 281 N N . ASN A 1 60 ? -70.229 -26.383 71.550 1.00 223.50 ? 60 ASN A N 1 ATOM 282 C CA . ASN A 1 60 ? -70.973 -27.002 72.717 1.00 215.07 ? 60 ASN A CA 1 ATOM 283 C C . ASN A 1 60 ? -70.881 -28.482 73.170 1.00 216.78 ? 60 ASN A C 1 ATOM 284 O O . ASN A 1 60 ? -70.050 -29.267 72.691 1.00 214.79 ? 60 ASN A O 1 ATOM 285 C CB . ASN A 1 60 ? -72.474 -26.689 72.591 1.00 207.82 ? 60 ASN A CB 1 ATOM 286 C CG . ASN A 1 60 ? -73.211 -27.676 71.698 1.00 198.64 ? 60 ASN A CG 1 ATOM 287 O OD1 . ASN A 1 60 ? -73.136 -27.612 70.469 1.00 202.64 ? 60 ASN A OD1 1 ATOM 288 N ND2 . ASN A 1 60 ? -73.937 -28.588 72.316 1.00 188.24 ? 60 ASN A ND2 1 ATOM 289 N N . ILE A 1 61 ? -71.783 -28.826 74.109 1.00 214.83 ? 61 ILE A N 1 ATOM 290 C CA . ILE A 1 61 ? -72.000 -30.196 74.642 1.00 213.43 ? 61 ILE A CA 1 ATOM 291 C C . ILE A 1 61 ? -72.173 -31.213 73.494 1.00 204.95 ? 61 ILE A C 1 ATOM 292 O O . ILE A 1 61 ? -72.874 -30.945 72.505 1.00 191.91 ? 61 ILE A O 1 ATOM 293 C CB . ILE A 1 61 ? -73.195 -30.247 75.710 1.00 216.19 ? 61 ILE A CB 1 ATOM 294 C CG1 . ILE A 1 61 ? -73.079 -31.409 76.759 1.00 203.84 ? 61 ILE A CG1 1 ATOM 295 C CG2 . ILE A 1 61 ? -74.567 -30.237 75.036 1.00 222.02 ? 61 ILE A CG2 1 ATOM 296 C CD1 . ILE A 1 61 ? -74.004 -31.392 77.987 1.00 174.98 ? 61 ILE A CD1 1 ATOM 297 N N . ALA A 1 62 ? -71.483 -32.349 73.612 1.00 200.62 ? 62 ALA A N 1 ATOM 298 C CA . ALA A 1 62 ? -71.855 -33.570 72.876 1.00 219.10 ? 62 ALA A CA 1 ATOM 299 C C . ALA A 1 62 ? -70.742 -34.651 72.773 1.00 228.75 ? 62 ALA A C 1 ATOM 300 O O . ALA A 1 62 ? -69.918 -34.567 71.866 1.00 245.05 ? 62 ALA A O 1 ATOM 301 C CB . ALA A 1 62 ? -72.419 -33.208 71.500 1.00 202.89 ? 62 ALA A CB 1 ATOM 302 N N . LYS A 1 63 ? -70.738 -35.673 73.658 1.00 221.26 ? 63 LYS A N 1 ATOM 303 C CA . LYS A 1 63 ? -69.564 -36.596 73.793 1.00 200.19 ? 63 LYS A CA 1 ATOM 304 C C . LYS A 1 63 ? -69.619 -37.771 74.785 1.00 199.30 ? 63 LYS A C 1 ATOM 305 O O . LYS A 1 63 ? -68.636 -37.974 75.517 1.00 191.60 ? 63 LYS A O 1 ATOM 306 C CB . LYS A 1 63 ? -68.360 -35.778 74.256 1.00 193.32 ? 63 LYS A CB 1 ATOM 307 C CG . LYS A 1 63 ? -68.345 -35.463 75.755 1.00 191.28 ? 63 LYS A CG 1 ATOM 308 C CD . LYS A 1 63 ? -69.633 -34.796 76.267 1.00 181.24 ? 63 LYS A CD 1 ATOM 309 C CE . LYS A 1 63 ? -69.776 -33.354 75.793 1.00 163.84 ? 63 LYS A CE 1 ATOM 310 N NZ . LYS A 1 63 ? -70.676 -32.600 76.680 1.00 157.00 ? 63 LYS A NZ 1 ATOM 311 N N . PRO A 1 64 ? -70.708 -38.565 74.799 1.00 202.27 ? 64 PRO A N 1 ATOM 312 C CA . PRO A 1 64 ? -70.978 -39.433 75.973 1.00 195.43 ? 64 PRO A CA 1 ATOM 313 C C . PRO A 1 64 ? -69.841 -40.416 76.329 1.00 187.94 ? 64 PRO A C 1 ATOM 314 O O . PRO A 1 64 ? -69.716 -41.421 75.642 1.00 183.18 ? 64 PRO A O 1 ATOM 315 C CB . PRO A 1 64 ? -72.243 -40.204 75.551 1.00 189.97 ? 64 PRO A CB 1 ATOM 316 C CG . PRO A 1 64 ? -72.778 -39.483 74.350 1.00 202.69 ? 64 PRO A CG 1 ATOM 317 C CD . PRO A 1 64 ? -71.579 -38.908 73.662 1.00 199.47 ? 64 PRO A CD 1 ATOM 318 N N . ARG A 1 65 ? -69.048 -40.141 77.387 1.00 194.83 ? 65 ARG A N 1 ATOM 319 C CA . ARG A 1 65 ? -67.790 -40.912 77.724 1.00 194.95 ? 65 ARG A CA 1 ATOM 320 C C . ARG A 1 65 ? -67.911 -42.125 78.708 1.00 195.53 ? 65 ARG A C 1 ATOM 321 O O . ARG A 1 65 ? -68.523 -41.988 79.767 1.00 217.83 ? 65 ARG A O 1 ATOM 322 C CB . ARG A 1 65 ? -66.631 -39.959 78.146 1.00 189.41 ? 65 ARG A CB 1 ATOM 323 C CG . ARG A 1 65 ? -66.560 -39.508 79.610 1.00 179.85 ? 65 ARG A CG 1 ATOM 324 C CD . ARG A 1 65 ? -65.133 -39.178 80.044 1.00 171.12 ? 65 ARG A CD 1 ATOM 325 N NE . ARG A 1 65 ? -64.487 -38.234 79.131 1.00 173.95 ? 65 ARG A NE 1 ATOM 326 C CZ . ARG A 1 65 ? -63.539 -38.536 78.238 1.00 180.09 ? 65 ARG A CZ 1 ATOM 327 N NH1 . ARG A 1 65 ? -63.063 -39.778 78.101 1.00 166.68 ? 65 ARG A NH1 1 ATOM 328 N NH2 . ARG A 1 65 ? -63.060 -37.572 77.465 1.00 186.92 ? 65 ARG A NH2 1 ATOM 329 N N . PRO A 1 66 ? -67.304 -43.302 78.372 1.00 185.25 ? 66 PRO A N 1 ATOM 330 C CA . PRO A 1 66 ? -67.585 -44.490 79.175 1.00 175.03 ? 66 PRO A CA 1 ATOM 331 C C . PRO A 1 66 ? -66.778 -44.539 80.478 1.00 167.77 ? 66 PRO A C 1 ATOM 332 O O . PRO A 1 66 ? -65.643 -44.045 80.520 1.00 152.81 ? 66 PRO A O 1 ATOM 333 C CB . PRO A 1 66 ? -67.186 -45.643 78.244 1.00 168.43 ? 66 PRO A CB 1 ATOM 334 C CG . PRO A 1 66 ? -66.065 -45.093 77.449 1.00 170.15 ? 66 PRO A CG 1 ATOM 335 C CD . PRO A 1 66 ? -66.257 -43.588 77.369 1.00 189.16 ? 66 PRO A CD 1 ATOM 336 N N . PRO A 1 67 ? -67.376 -45.133 81.534 1.00 169.14 ? 67 PRO A N 1 ATOM 337 C CA . PRO A 1 67 ? -66.870 -45.344 82.877 1.00 163.92 ? 67 PRO A CA 1 ATOM 338 C C . PRO A 1 67 ? -65.365 -45.112 83.146 1.00 153.73 ? 67 PRO A C 1 ATOM 339 O O . PRO A 1 67 ? -64.989 -44.200 83.878 1.00 141.06 ? 67 PRO A O 1 ATOM 340 C CB . PRO A 1 67 ? -67.245 -46.825 83.121 1.00 173.95 ? 67 PRO A CB 1 ATOM 341 C CG . PRO A 1 67 ? -68.446 -47.086 82.244 1.00 172.65 ? 67 PRO A CG 1 ATOM 342 C CD . PRO A 1 67 ? -68.664 -45.841 81.403 1.00 171.72 ? 67 PRO A CD 1 ATOM 343 N N . TRP A 1 68 ? -64.525 -45.921 82.529 1.00 153.14 ? 68 TRP A N 1 ATOM 344 C CA . TRP A 1 68 ? -63.193 -46.203 83.035 1.00 156.61 ? 68 TRP A CA 1 ATOM 345 C C . TRP A 1 68 ? -62.056 -45.410 82.361 1.00 166.12 ? 68 TRP A C 1 ATOM 346 O O . TRP A 1 68 ? -60.982 -45.261 82.951 1.00 169.39 ? 68 TRP A O 1 ATOM 347 C CB . TRP A 1 68 ? -62.978 -47.682 82.835 1.00 150.56 ? 68 TRP A CB 1 ATOM 348 C CG . TRP A 1 68 ? -63.434 -48.032 81.473 1.00 154.06 ? 68 TRP A CG 1 ATOM 349 C CD1 . TRP A 1 68 ? -64.708 -48.348 81.083 1.00 156.75 ? 68 TRP A CD1 1 ATOM 350 C CD2 . TRP A 1 68 ? -62.639 -48.025 80.287 1.00 150.92 ? 68 TRP A CD2 1 ATOM 351 N NE1 . TRP A 1 68 ? -64.741 -48.564 79.729 1.00 159.24 ? 68 TRP A NE1 1 ATOM 352 C CE2 . TRP A 1 68 ? -63.480 -48.378 79.219 1.00 155.08 ? 68 TRP A CE2 1 ATOM 353 C CE3 . TRP A 1 68 ? -61.286 -47.774 80.027 1.00 143.65 ? 68 TRP A CE3 1 ATOM 354 C CZ2 . TRP A 1 68 ? -63.009 -48.492 77.907 1.00 155.88 ? 68 TRP A CZ2 1 ATOM 355 C CZ3 . TRP A 1 68 ? -60.826 -47.882 78.726 1.00 141.15 ? 68 TRP A CZ3 1 ATOM 356 C CH2 . TRP A 1 68 ? -61.681 -48.239 77.684 1.00 142.67 ? 68 TRP A CH2 1 ATOM 357 N N . MET A 1 69 ? -62.281 -44.935 81.128 1.00 168.95 ? 69 MET A N 1 ATOM 358 C CA . MET A 1 69 ? -61.394 -43.967 80.465 1.00 163.93 ? 69 MET A CA 1 ATOM 359 C C . MET A 1 69 ? -61.302 -42.721 81.349 1.00 175.18 ? 69 MET A C 1 ATOM 360 O O . MET A 1 69 ? -61.452 -41.608 80.841 1.00 216.37 ? 69 MET A O 1 ATOM 361 C CB . MET A 1 69 ? -61.998 -43.511 79.124 1.00 164.96 ? 69 MET A CB 1 ATOM 362 C CG . MET A 1 69 ? -61.498 -44.136 77.831 1.00 164.38 ? 69 MET A CG 1 ATOM 363 S SD . MET A 1 69 ? -62.188 -43.222 76.415 1.00 185.42 ? 69 MET A SD 1 ATOM 364 C CE . MET A 1 69 ? -62.363 -44.530 75.192 1.00 159.69 ? 69 MET A CE 1 ATOM 365 N N . GLY A 1 70 ? -61.065 -42.905 82.652 1.00 153.90 ? 70 GLY A N 1 ATOM 366 C CA . GLY A 1 70 ? -61.241 -41.860 83.672 1.00 142.15 ? 70 GLY A CA 1 ATOM 367 C C . GLY A 1 70 ? -61.244 -40.397 83.239 1.00 146.99 ? 70 GLY A C 1 ATOM 368 O O . GLY A 1 70 ? -62.233 -39.872 82.694 1.00 144.32 ? 70 GLY A O 1 ATOM 369 N N . LEU A 1 71 ? -60.132 -39.728 83.514 1.00 147.40 ? 71 LEU A N 1 ATOM 370 C CA . LEU A 1 71 ? -59.912 -38.367 83.043 1.00 154.02 ? 71 LEU A CA 1 ATOM 371 C C . LEU A 1 71 ? -59.367 -38.374 81.614 1.00 156.83 ? 71 LEU A C 1 ATOM 372 O O . LEU A 1 71 ? -59.338 -37.350 80.927 1.00 168.00 ? 71 LEU A O 1 ATOM 373 C CB . LEU A 1 71 ? -58.949 -37.617 83.981 1.00 150.98 ? 71 LEU A CB 1 ATOM 374 C CG . LEU A 1 71 ? -57.716 -38.229 84.682 1.00 139.59 ? 71 LEU A CG 1 ATOM 375 C CD1 . LEU A 1 71 ? -57.057 -39.388 83.946 1.00 126.90 ? 71 LEU A CD1 1 ATOM 376 C CD2 . LEU A 1 71 ? -56.697 -37.132 84.971 1.00 132.80 ? 71 LEU A CD2 1 ATOM 377 N N . LEU A 1 72 ? -58.928 -39.551 81.188 1.00 160.52 ? 72 LEU A N 1 ATOM 378 C CA . LEU A 1 72 ? -58.306 -39.772 79.892 1.00 159.48 ? 72 LEU A CA 1 ATOM 379 C C . LEU A 1 72 ? -59.043 -39.080 78.740 1.00 163.31 ? 72 LEU A C 1 ATOM 380 O O . LEU A 1 72 ? -60.225 -39.369 78.461 1.00 161.00 ? 72 LEU A O 1 ATOM 381 C CB . LEU A 1 72 ? -58.223 -41.276 79.649 1.00 156.24 ? 72 LEU A CB 1 ATOM 382 C CG . LEU A 1 72 ? -56.940 -41.855 79.089 1.00 149.11 ? 72 LEU A CG 1 ATOM 383 C CD1 . LEU A 1 72 ? -56.617 -43.129 79.856 1.00 148.14 ? 72 LEU A CD1 1 ATOM 384 C CD2 . LEU A 1 72 ? -57.091 -42.107 77.595 1.00 150.45 ? 72 LEU A CD2 1 ATOM 385 N N . GLY A 1 73 ? -58.338 -38.148 78.098 1.00 160.30 ? 73 GLY A N 1 ATOM 386 C CA . GLY A 1 73 ? -58.792 -37.562 76.846 1.00 155.55 ? 73 GLY A CA 1 ATOM 387 C C . GLY A 1 73 ? -59.189 -38.685 75.901 1.00 151.45 ? 73 GLY A C 1 ATOM 388 O O . GLY A 1 73 ? -58.569 -39.758 75.919 1.00 151.38 ? 73 GLY A O 1 ATOM 389 N N . PRO A 1 74 ? -60.214 -38.443 75.062 1.00 140.95 ? 74 PRO A N 1 ATOM 390 C CA . PRO A 1 74 ? -60.862 -39.461 74.221 1.00 128.74 ? 74 PRO A CA 1 ATOM 391 C C . PRO A 1 74 ? -59.835 -40.279 73.458 1.00 125.00 ? 74 PRO A C 1 ATOM 392 O O . PRO A 1 74 ? -58.804 -39.752 73.046 1.00 119.53 ? 74 PRO A O 1 ATOM 393 C CB . PRO A 1 74 ? -61.654 -38.630 73.230 1.00 123.47 ? 74 PRO A CB 1 ATOM 394 C CG . PRO A 1 74 ? -60.978 -37.299 73.214 1.00 124.10 ? 74 PRO A CG 1 ATOM 395 C CD . PRO A 1 74 ? -60.553 -37.079 74.625 1.00 130.69 ? 74 PRO A CD 1 ATOM 396 N N . THR A 1 75 ? -60.100 -41.563 73.278 1.00 131.66 ? 75 THR A N 1 ATOM 397 C CA . THR A 1 75 ? -59.136 -42.418 72.602 1.00 134.80 ? 75 THR A CA 1 ATOM 398 C C . THR A 1 75 ? -59.311 -42.207 71.089 1.00 135.33 ? 75 THR A C 1 ATOM 399 O O . THR A 1 75 ? -60.343 -42.614 70.530 1.00 138.08 ? 75 THR A O 1 ATOM 400 C CB . THR A 1 75 ? -59.295 -43.914 73.010 1.00 142.66 ? 75 THR A CB 1 ATOM 401 O OG1 . THR A 1 75 ? -59.090 -44.082 74.421 1.00 143.06 ? 75 THR A OG1 1 ATOM 402 C CG2 . THR A 1 75 ? -58.279 -44.770 72.304 1.00 153.56 ? 75 THR A CG2 1 ATOM 403 N N . ILE A 1 76 ? -58.337 -41.537 70.447 1.00 135.25 ? 76 ILE A N 1 ATOM 404 C CA . ILE A 1 76 ? -58.348 -41.325 68.970 1.00 130.57 ? 76 ILE A CA 1 ATOM 405 C C . ILE A 1 76 ? -57.690 -42.522 68.268 1.00 132.10 ? 76 ILE A C 1 ATOM 406 O O . ILE A 1 76 ? -56.706 -43.106 68.781 1.00 125.59 ? 76 ILE A O 1 ATOM 407 C CB . ILE A 1 76 ? -57.747 -39.951 68.480 1.00 127.67 ? 76 ILE A CB 1 ATOM 408 C CG1 . ILE A 1 76 ? -56.223 -39.980 68.362 1.00 127.59 ? 76 ILE A CG1 1 ATOM 409 C CG2 . ILE A 1 76 ? -58.224 -38.743 69.291 1.00 121.71 ? 76 ILE A CG2 1 ATOM 410 C CD1 . ILE A 1 76 ? -55.753 -40.096 66.927 1.00 126.36 ? 76 ILE A CD1 1 ATOM 411 N N . GLN A 1 77 ? -58.232 -42.892 67.107 1.00 133.68 ? 77 GLN A N 1 ATOM 412 C CA . GLN A 1 77 ? -57.857 -44.175 66.501 1.00 136.87 ? 77 GLN A CA 1 ATOM 413 C C . GLN A 1 77 ? -57.949 -44.237 64.981 1.00 136.02 ? 77 GLN A C 1 ATOM 414 O O . GLN A 1 77 ? -59.060 -44.213 64.445 1.00 139.52 ? 77 GLN A O 1 ATOM 415 C CB . GLN A 1 77 ? -58.760 -45.256 67.062 1.00 138.58 ? 77 GLN A CB 1 ATOM 416 C CG . GLN A 1 77 ? -58.024 -46.514 67.455 1.00 146.16 ? 77 GLN A CG 1 ATOM 417 C CD . GLN A 1 77 ? -58.989 -47.630 67.762 1.00 164.34 ? 77 GLN A CD 1 ATOM 418 O OE1 . GLN A 1 77 ? -58.963 -48.240 68.848 1.00 169.95 ? 77 GLN A OE1 1 ATOM 419 N NE2 . GLN A 1 77 ? -59.880 -47.892 66.809 1.00 175.51 ? 77 GLN A NE2 1 ATOM 420 N N . ALA A 1 78 ? -56.797 -44.365 64.303 1.00 126.22 ? 78 ALA A N 1 ATOM 421 C CA . ALA A 1 78 ? -56.744 -44.451 62.821 1.00 124.29 ? 78 ALA A CA 1 ATOM 422 C C . ALA A 1 78 ? -55.996 -45.652 62.260 1.00 124.41 ? 78 ALA A C 1 ATOM 423 O O . ALA A 1 78 ? -55.222 -46.323 62.955 1.00 119.11 ? 78 ALA A O 1 ATOM 424 C CB . ALA A 1 78 ? -56.182 -43.178 62.207 1.00 127.21 ? 78 ALA A CB 1 ATOM 425 N N . GLU A 1 79 ? -56.236 -45.898 60.978 1.00 131.44 ? 79 GLU A N 1 ATOM 426 C CA . GLU A 1 79 ? -55.580 -46.976 60.273 1.00 142.23 ? 79 GLU A CA 1 ATOM 427 C C . GLU A 1 79 ? -54.335 -46.495 59.542 1.00 140.54 ? 79 GLU A C 1 ATOM 428 O O . GLU A 1 79 ? -53.899 -45.358 59.698 1.00 134.67 ? 79 GLU A O 1 ATOM 429 C CB . GLU A 1 79 ? -56.521 -47.598 59.255 1.00 158.37 ? 79 GLU A CB 1 ATOM 430 C CG . GLU A 1 79 ? -57.623 -48.463 59.817 1.00 159.74 ? 79 GLU A CG 1 ATOM 431 C CD . GLU A 1 79 ? -58.379 -49.165 58.707 1.00 177.01 ? 79 GLU A CD 1 ATOM 432 O OE1 . GLU A 1 79 ? -58.590 -48.554 57.628 1.00 181.39 ? 79 GLU A OE1 1 ATOM 433 O OE2 . GLU A 1 79 ? -58.743 -50.337 58.907 1.00 181.50 ? 79 GLU A OE2 1 ATOM 434 N N . VAL A 1 80 ? -53.783 -47.388 58.729 1.00 136.63 ? 80 VAL A N 1 ATOM 435 C CA . VAL A 1 80 ? -52.581 -47.114 57.989 1.00 133.61 ? 80 VAL A CA 1 ATOM 436 C C . VAL A 1 80 ? -52.918 -46.658 56.589 1.00 136.32 ? 80 VAL A C 1 ATOM 437 O O . VAL A 1 80 ? -52.463 -47.233 55.621 1.00 138.64 ? 80 VAL A O 1 ATOM 438 C CB . VAL A 1 80 ? -51.636 -48.338 57.911 1.00 141.56 ? 80 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 80 ? -50.502 -48.215 58.916 1.00 142.95 ? 80 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 80 ? -52.393 -49.653 58.059 1.00 137.94 ? 80 VAL A CG2 1 ATOM 441 N N . TYR A 1 81 ? -53.742 -45.636 56.486 1.00 143.22 ? 81 TYR A N 1 ATOM 442 C CA . TYR A 1 81 ? -53.771 -44.806 55.295 1.00 154.43 ? 81 TYR A CA 1 ATOM 443 C C . TYR A 1 81 ? -54.728 -43.682 55.571 1.00 159.96 ? 81 TYR A C 1 ATOM 444 O O . TYR A 1 81 ? -54.797 -42.716 54.810 1.00 168.30 ? 81 TYR A O 1 ATOM 445 C CB . TYR A 1 81 ? -54.134 -45.589 54.026 1.00 163.46 ? 81 TYR A CB 1 ATOM 446 C CG . TYR A 1 81 ? -52.913 -46.143 53.297 1.00 176.00 ? 81 TYR A CG 1 ATOM 447 C CD1 . TYR A 1 81 ? -51.907 -45.287 52.833 1.00 189.84 ? 81 TYR A CD1 1 ATOM 448 C CD2 . TYR A 1 81 ? -52.752 -47.526 53.086 1.00 179.76 ? 81 TYR A CD2 1 ATOM 449 C CE1 . TYR A 1 81 ? -50.790 -45.785 52.174 1.00 203.65 ? 81 TYR A CE1 1 ATOM 450 C CE2 . TYR A 1 81 ? -51.635 -48.035 52.433 1.00 183.45 ? 81 TYR A CE2 1 ATOM 451 C CZ . TYR A 1 81 ? -50.660 -47.154 51.981 1.00 198.20 ? 81 TYR A CZ 1 ATOM 452 O OH . TYR A 1 81 ? -49.550 -47.627 51.335 1.00 206.01 ? 81 TYR A OH 1 ATOM 453 N N . ASP A 1 82 ? -55.431 -43.811 56.697 1.00 156.52 ? 82 ASP A N 1 ATOM 454 C CA . ASP A 1 82 ? -56.409 -42.834 57.147 1.00 156.45 ? 82 ASP A CA 1 ATOM 455 C C . ASP A 1 82 ? -55.751 -41.510 57.398 1.00 157.41 ? 82 ASP A C 1 ATOM 456 O O . ASP A 1 82 ? -54.524 -41.418 57.370 1.00 160.96 ? 82 ASP A O 1 ATOM 457 C CB . ASP A 1 82 ? -57.084 -43.318 58.413 1.00 155.74 ? 82 ASP A CB 1 ATOM 458 C CG . ASP A 1 82 ? -57.827 -44.606 58.200 1.00 175.40 ? 82 ASP A CG 1 ATOM 459 O OD1 . ASP A 1 82 ? -57.666 -45.248 57.129 1.00 179.28 ? 82 ASP A OD1 1 ATOM 460 O OD2 . ASP A 1 82 ? -58.575 -44.985 59.113 1.00 187.73 ? 82 ASP A OD2 1 ATOM 461 N N . THR A 1 83 ? -56.569 -40.478 57.598 1.00 160.67 ? 83 THR A N 1 ATOM 462 C CA . THR A 1 83 ? -56.071 -39.158 57.984 1.00 148.64 ? 83 THR A CA 1 ATOM 463 C C . THR A 1 83 ? -56.931 -38.661 59.127 1.00 139.45 ? 83 THR A C 1 ATOM 464 O O . THR A 1 83 ? -58.137 -38.455 58.963 1.00 145.57 ? 83 THR A O 1 ATOM 465 C CB . THR A 1 83 ? -56.075 -38.129 56.824 1.00 147.93 ? 83 THR A CB 1 ATOM 466 O OG1 . THR A 1 83 ? -55.684 -38.751 55.593 1.00 150.18 ? 83 THR A OG1 1 ATOM 467 C CG2 . THR A 1 83 ? -55.095 -37.024 57.117 1.00 142.64 ? 83 THR A CG2 1 ATOM 468 N N . VAL A 1 84 ? -56.319 -38.503 60.291 1.00 124.74 ? 84 VAL A N 1 ATOM 469 C CA . VAL A 1 84 ? -57.044 -37.977 61.426 1.00 134.50 ? 84 VAL A CA 1 ATOM 470 C C . VAL A 1 84 ? -57.078 -36.457 61.381 1.00 147.57 ? 84 VAL A C 1 ATOM 471 O O . VAL A 1 84 ? -56.080 -35.820 61.027 1.00 159.54 ? 84 VAL A O 1 ATOM 472 C CB . VAL A 1 84 ? -56.457 -38.483 62.745 1.00 130.48 ? 84 VAL A CB 1 ATOM 473 C CG1 . VAL A 1 84 ? -56.458 -37.393 63.813 1.00 134.18 ? 84 VAL A CG1 1 ATOM 474 C CG2 . VAL A 1 84 ? -57.252 -39.685 63.203 1.00 129.84 ? 84 VAL A CG2 1 ATOM 475 N N . VAL A 1 85 ? -58.230 -35.876 61.718 1.00 146.09 ? 85 VAL A N 1 ATOM 476 C CA . VAL A 1 85 ? -58.352 -34.424 61.741 1.00 140.36 ? 85 VAL A CA 1 ATOM 477 C C . VAL A 1 85 ? -59.018 -33.888 62.998 1.00 147.37 ? 85 VAL A C 1 ATOM 478 O O . VAL A 1 85 ? -60.219 -33.566 63.031 1.00 141.61 ? 85 VAL A O 1 ATOM 479 C CB . VAL A 1 85 ? -59.057 -33.873 60.511 1.00 134.96 ? 85 VAL A CB 1 ATOM 480 C CG1 . VAL A 1 85 ? -59.037 -32.366 60.585 1.00 135.97 ? 85 VAL A CG1 1 ATOM 481 C CG2 . VAL A 1 85 ? -58.349 -34.323 59.253 1.00 131.93 ? 85 VAL A CG2 1 ATOM 482 N N . ILE A 1 86 ? -58.194 -33.773 64.026 1.00 154.90 ? 86 ILE A N 1 ATOM 483 C CA . ILE A 1 86 ? -58.618 -33.208 65.283 1.00 166.28 ? 86 ILE A CA 1 ATOM 484 C C . ILE A 1 86 ? -58.726 -31.689 65.177 1.00 166.45 ? 86 ILE A C 1 ATOM 485 O O . ILE A 1 86 ? -57.815 -31.020 64.689 1.00 171.44 ? 86 ILE A O 1 ATOM 486 C CB . ILE A 1 86 ? -57.662 -33.607 66.416 1.00 170.72 ? 86 ILE A CB 1 ATOM 487 C CG1 . ILE A 1 86 ? -57.190 -35.064 66.225 1.00 163.59 ? 86 ILE A CG1 1 ATOM 488 C CG2 . ILE A 1 86 ? -58.327 -33.327 67.757 1.00 191.16 ? 86 ILE A CG2 1 ATOM 489 C CD1 . ILE A 1 86 ? -57.334 -35.971 67.436 1.00 160.58 ? 86 ILE A CD1 1 ATOM 490 N N . THR A 1 87 ? -59.852 -31.154 65.626 1.00 158.40 ? 87 THR A N 1 ATOM 491 C CA . THR A 1 87 ? -60.099 -29.725 65.534 1.00 154.78 ? 87 THR A CA 1 ATOM 492 C C . THR A 1 87 ? -60.162 -29.219 66.969 1.00 150.42 ? 87 THR A C 1 ATOM 493 O O . THR A 1 87 ? -61.215 -29.281 67.584 1.00 154.79 ? 87 THR A O 1 ATOM 494 C CB . THR A 1 87 ? -61.429 -29.473 64.781 1.00 158.64 ? 87 THR A CB 1 ATOM 495 O OG1 . THR A 1 87 ? -61.603 -30.469 63.756 1.00 158.24 ? 87 THR A OG1 1 ATOM 496 C CG2 . THR A 1 87 ? -61.487 -28.067 64.167 1.00 151.83 ? 87 THR A CG2 1 ATOM 497 N N . LEU A 1 88 ? -59.037 -28.757 67.519 1.00 146.15 ? 88 LEU A N 1 ATOM 498 C CA . LEU A 1 88 ? -58.956 -28.451 68.965 1.00 150.20 ? 88 LEU A CA 1 ATOM 499 C C . LEU A 1 88 ? -59.644 -27.155 69.364 1.00 172.88 ? 88 LEU A C 1 ATOM 500 O O . LEU A 1 88 ? -59.512 -26.164 68.642 1.00 199.05 ? 88 LEU A O 1 ATOM 501 C CB . LEU A 1 88 ? -57.510 -28.353 69.429 1.00 138.80 ? 88 LEU A CB 1 ATOM 502 C CG . LEU A 1 88 ? -57.418 -28.026 70.924 1.00 131.84 ? 88 LEU A CG 1 ATOM 503 C CD1 . LEU A 1 88 ? -57.748 -29.257 71.742 1.00 126.00 ? 88 LEU A CD1 1 ATOM 504 C CD2 . LEU A 1 88 ? -56.055 -27.483 71.318 1.00 136.24 ? 88 LEU A CD2 1 ATOM 505 N N . LYS A 1 89 ? -60.313 -27.139 70.531 1.00 177.70 ? 89 LYS A N 1 ATOM 506 C CA . LYS A 1 89 ? -61.139 -25.968 70.959 1.00 179.51 ? 89 LYS A CA 1 ATOM 507 C C . LYS A 1 89 ? -60.623 -25.108 72.136 1.00 172.45 ? 89 LYS A C 1 ATOM 508 O O . LYS A 1 89 ? -61.125 -24.000 72.329 1.00 164.77 ? 89 LYS A O 1 ATOM 509 C CB . LYS A 1 89 ? -62.595 -26.393 71.235 1.00 181.52 ? 89 LYS A CB 1 ATOM 510 C CG . LYS A 1 89 ? -63.698 -25.481 70.670 1.00 170.20 ? 89 LYS A CG 1 ATOM 511 C CD . LYS A 1 89 ? -65.005 -26.275 70.499 1.00 165.57 ? 89 LYS A CD 1 ATOM 512 C CE . LYS A 1 89 ? -64.745 -27.792 70.472 1.00 151.49 ? 89 LYS A CE 1 ATOM 513 N NZ . LYS A 1 89 ? -65.633 -28.612 69.609 1.00 139.90 ? 89 LYS A NZ 1 ATOM 514 N N . ASN A 1 90 ? -59.645 -25.618 72.897 1.00 166.83 ? 90 ASN A N 1 ATOM 515 C CA . ASN A 1 90 ? -59.079 -24.959 74.109 1.00 169.34 ? 90 ASN A CA 1 ATOM 516 C C . ASN A 1 90 ? -60.004 -24.042 74.890 1.00 172.36 ? 90 ASN A C 1 ATOM 517 O O . ASN A 1 90 ? -59.991 -22.827 74.703 1.00 168.35 ? 90 ASN A O 1 ATOM 518 C CB . ASN A 1 90 ? -57.758 -24.218 73.824 1.00 178.41 ? 90 ASN A CB 1 ATOM 519 C CG . ASN A 1 90 ? -57.130 -23.610 75.090 1.00 185.56 ? 90 ASN A CG 1 ATOM 520 O OD1 . ASN A 1 90 ? -57.739 -23.594 76.167 1.00 186.93 ? 90 ASN A OD1 1 ATOM 521 N ND2 . ASN A 1 90 ? -55.901 -23.111 74.960 1.00 187.15 ? 90 ASN A ND2 1 ATOM 522 N N . MET A 1 91 ? -60.764 -24.625 75.805 1.00 181.49 ? 91 MET A N 1 ATOM 523 C CA . MET A 1 91 ? -61.745 -23.865 76.561 1.00 181.75 ? 91 MET A CA 1 ATOM 524 C C . MET A 1 91 ? -61.161 -23.378 77.888 1.00 175.33 ? 91 MET A C 1 ATOM 525 O O . MET A 1 91 ? -61.767 -22.558 78.566 1.00 187.60 ? 91 MET A O 1 ATOM 526 C CB . MET A 1 91 ? -63.031 -24.689 76.741 1.00 193.45 ? 91 MET A CB 1 ATOM 527 C CG . MET A 1 91 ? -63.494 -25.388 75.458 1.00 204.89 ? 91 MET A CG 1 ATOM 528 S SD . MET A 1 91 ? -65.273 -25.545 75.159 1.00 231.33 ? 91 MET A SD 1 ATOM 529 C CE . MET A 1 91 ? -65.846 -23.835 75.262 1.00 232.86 ? 91 MET A CE 1 ATOM 530 N N . ALA A 1 92 ? -59.962 -23.854 78.219 1.00 167.96 ? 92 ALA A N 1 ATOM 531 C CA . ALA A 1 92 ? -59.282 -23.548 79.485 1.00 175.03 ? 92 ALA A CA 1 ATOM 532 C C . ALA A 1 92 ? -58.824 -22.075 79.605 1.00 187.04 ? 92 ALA A C 1 ATOM 533 O O . ALA A 1 92 ? -58.943 -21.303 78.648 1.00 190.79 ? 92 ALA A O 1 ATOM 534 C CB . ALA A 1 92 ? -58.098 -24.505 79.676 1.00 168.37 ? 92 ALA A CB 1 ATOM 535 N N . SER A 1 93 ? -58.326 -21.695 80.789 1.00 194.17 ? 93 SER A N 1 ATOM 536 C CA . SER A 1 93 ? -57.563 -20.444 80.990 1.00 200.13 ? 93 SER A CA 1 ATOM 537 C C . SER A 1 93 ? -56.040 -20.708 80.875 1.00 206.11 ? 93 SER A C 1 ATOM 538 O O . SER A 1 93 ? -55.198 -19.826 81.121 1.00 202.90 ? 93 SER A O 1 ATOM 539 C CB . SER A 1 93 ? -57.920 -19.819 82.339 1.00 200.30 ? 93 SER A CB 1 ATOM 540 O OG . SER A 1 93 ? -57.956 -20.801 83.361 1.00 192.44 ? 93 SER A OG 1 ATOM 541 N N . HIS A 1 94 ? -55.734 -21.949 80.483 1.00 211.19 ? 94 HIS A N 1 ATOM 542 C CA . HIS A 1 94 ? -54.397 -22.492 80.256 1.00 197.01 ? 94 HIS A CA 1 ATOM 543 C C . HIS A 1 94 ? -53.981 -22.237 78.804 1.00 192.98 ? 94 HIS A C 1 ATOM 544 O O . HIS A 1 94 ? -54.807 -22.344 77.892 1.00 185.44 ? 94 HIS A O 1 ATOM 545 C CB . HIS A 1 94 ? -54.449 -24.014 80.485 1.00 182.83 ? 94 HIS A CB 1 ATOM 546 C CG . HIS A 1 94 ? -53.297 -24.555 81.268 1.00 177.76 ? 94 HIS A CG 1 ATOM 547 N ND1 . HIS A 1 94 ? -53.462 -25.451 82.303 1.00 169.13 ? 94 HIS A ND1 1 ATOM 548 C CD2 . HIS A 1 94 ? -51.965 -24.316 81.181 1.00 173.16 ? 94 HIS A CD2 1 ATOM 549 C CE1 . HIS A 1 94 ? -52.282 -25.736 82.824 1.00 169.44 ? 94 HIS A CE1 1 ATOM 550 N NE2 . HIS A 1 94 ? -51.359 -25.066 82.156 1.00 170.75 ? 94 HIS A NE2 1 ATOM 551 N N . PRO A 1 95 ? -52.706 -21.895 78.565 1.00 195.52 ? 95 PRO A N 1 ATOM 552 C CA . PRO A 1 95 ? -52.311 -21.949 77.153 1.00 197.83 ? 95 PRO A CA 1 ATOM 553 C C . PRO A 1 95 ? -51.922 -23.393 76.797 1.00 196.76 ? 95 PRO A C 1 ATOM 554 O O . PRO A 1 95 ? -50.965 -23.913 77.376 1.00 218.88 ? 95 PRO A O 1 ATOM 555 C CB . PRO A 1 95 ? -51.096 -20.998 77.081 1.00 195.32 ? 95 PRO A CB 1 ATOM 556 C CG . PRO A 1 95 ? -50.989 -20.356 78.432 1.00 200.27 ? 95 PRO A CG 1 ATOM 557 C CD . PRO A 1 95 ? -51.669 -21.277 79.405 1.00 195.30 ? 95 PRO A CD 1 ATOM 558 N N . VAL A 1 96 ? -52.663 -24.051 75.896 1.00 179.58 ? 96 VAL A N 1 ATOM 559 C CA . VAL A 1 96 ? -52.401 -25.482 75.596 1.00 171.86 ? 96 VAL A CA 1 ATOM 560 C C . VAL A 1 96 ? -52.386 -25.893 74.120 1.00 168.72 ? 96 VAL A C 1 ATOM 561 O O . VAL A 1 96 ? -52.977 -25.222 73.278 1.00 163.83 ? 96 VAL A O 1 ATOM 562 C CB . VAL A 1 96 ? -53.353 -26.444 76.344 1.00 173.77 ? 96 VAL A CB 1 ATOM 563 C CG1 . VAL A 1 96 ? -53.223 -26.284 77.853 1.00 187.79 ? 96 VAL A CG1 1 ATOM 564 C CG2 . VAL A 1 96 ? -54.792 -26.269 75.881 1.00 181.03 ? 96 VAL A CG2 1 ATOM 565 N N . SER A 1 97 ? -51.728 -27.024 73.840 1.00 169.90 ? 97 SER A N 1 ATOM 566 C CA . SER A 1 97 ? -51.515 -27.533 72.471 1.00 163.42 ? 97 SER A CA 1 ATOM 567 C C . SER A 1 97 ? -52.149 -28.911 72.196 1.00 159.67 ? 97 SER A C 1 ATOM 568 O O . SER A 1 97 ? -53.154 -29.292 72.832 1.00 152.49 ? 97 SER A O 1 ATOM 569 C CB . SER A 1 97 ? -50.010 -27.534 72.111 1.00 152.78 ? 97 SER A CB 1 ATOM 570 O OG . SER A 1 97 ? -49.270 -28.487 72.859 1.00 137.60 ? 97 SER A OG 1 ATOM 571 N N . LEU A 1 98 ? -51.560 -29.630 71.231 1.00 150.24 ? 98 LEU A N 1 ATOM 572 C CA . LEU A 1 98 ? -51.999 -30.967 70.831 1.00 140.64 ? 98 LEU A CA 1 ATOM 573 C C . LEU A 1 98 ? -50.875 -31.704 70.098 1.00 137.65 ? 98 LEU A C 1 ATOM 574 O O . LEU A 1 98 ? -50.849 -31.761 68.866 1.00 139.92 ? 98 LEU A O 1 ATOM 575 C CB . LEU A 1 98 ? -53.236 -30.874 69.931 1.00 136.60 ? 98 LEU A CB 1 ATOM 576 C CG . LEU A 1 98 ? -54.438 -31.822 70.039 1.00 134.70 ? 98 LEU A CG 1 ATOM 577 C CD1 . LEU A 1 98 ? -55.061 -31.966 68.660 1.00 133.32 ? 98 LEU A CD1 1 ATOM 578 C CD2 . LEU A 1 98 ? -54.111 -33.199 70.592 1.00 133.69 ? 98 LEU A CD2 1 ATOM 579 N N . HIS A 1 99 ? -49.952 -32.282 70.860 1.00 142.33 ? 99 HIS A N 1 ATOM 580 C CA . HIS A 1 99 ? -48.792 -32.954 70.272 1.00 150.22 ? 99 HIS A CA 1 ATOM 581 C C . HIS A 1 99 ? -48.916 -34.458 70.178 1.00 151.81 ? 99 HIS A C 1 ATOM 582 O O . HIS A 1 99 ? -48.823 -35.158 71.190 1.00 153.70 ? 99 HIS A O 1 ATOM 583 C CB . HIS A 1 99 ? -47.517 -32.613 71.038 1.00 150.35 ? 99 HIS A CB 1 ATOM 584 C CG . HIS A 1 99 ? -46.294 -33.276 70.490 1.00 142.79 ? 99 HIS A CG 1 ATOM 585 N ND1 . HIS A 1 99 ? -45.140 -33.424 71.225 1.00 145.39 ? 99 HIS A ND1 1 ATOM 586 C CD2 . HIS A 1 99 ? -46.047 -33.837 69.285 1.00 142.49 ? 99 HIS A CD2 1 ATOM 587 C CE1 . HIS A 1 99 ? -44.230 -34.039 70.494 1.00 147.91 ? 99 HIS A CE1 1 ATOM 588 N NE2 . HIS A 1 99 ? -44.758 -34.306 69.313 1.00 154.27 ? 99 HIS A NE2 1 ATOM 589 N N . ALA A 1 100 ? -49.087 -34.947 68.954 1.00 149.77 ? 100 ALA A N 1 ATOM 590 C CA . ALA A 1 100 ? -49.157 -36.380 68.723 1.00 145.64 ? 100 ALA A CA 1 ATOM 591 C C . ALA A 1 100 ? -47.773 -37.008 68.520 1.00 144.84 ? 100 ALA A C 1 ATOM 592 O O . ALA A 1 100 ? -46.849 -36.384 67.982 1.00 153.55 ? 100 ALA A O 1 ATOM 593 C CB . ALA A 1 100 ? -50.072 -36.689 67.556 1.00 139.31 ? 100 ALA A CB 1 ATOM 594 N N . VAL A 1 101 ? -47.653 -38.257 68.961 1.00 131.24 ? 101 VAL A N 1 ATOM 595 C CA . VAL A 1 101 ? -46.398 -38.996 68.948 1.00 116.34 ? 101 VAL A CA 1 ATOM 596 C C . VAL A 1 101 ? -46.617 -40.259 68.141 1.00 110.12 ? 101 VAL A C 1 ATOM 597 O O . VAL A 1 101 ? -47.548 -41.005 68.405 1.00 101.41 ? 101 VAL A O 1 ATOM 598 C CB . VAL A 1 101 ? -45.982 -39.384 70.390 1.00 105.32 ? 101 VAL A CB 1 ATOM 599 C CG1 . VAL A 1 101 ? -44.615 -40.028 70.429 1.00 100.96 ? 101 VAL A CG1 1 ATOM 600 C CG2 . VAL A 1 101 ? -45.956 -38.166 71.280 1.00 108.03 ? 101 VAL A CG2 1 ATOM 601 N N . GLY A 1 102 ? -45.768 -40.512 67.161 1.00 113.38 ? 102 GLY A N 1 ATOM 602 C CA . GLY A 1 102 ? -45.861 -41.790 66.463 1.00 126.82 ? 102 GLY A CA 1 ATOM 603 C C . GLY A 1 102 ? -46.698 -41.752 65.198 1.00 134.01 ? 102 GLY A C 1 ATOM 604 O O . GLY A 1 102 ? -46.934 -42.789 64.538 1.00 129.61 ? 102 GLY A O 1 ATOM 605 N N . VAL A 1 103 ? -47.137 -40.546 64.860 1.00 129.88 ? 103 VAL A N 1 ATOM 606 C CA . VAL A 1 103 ? -47.760 -40.286 63.577 1.00 129.50 ? 103 VAL A CA 1 ATOM 607 C C . VAL A 1 103 ? -47.134 -39.024 63.022 1.00 131.69 ? 103 VAL A C 1 ATOM 608 O O . VAL A 1 103 ? -46.665 -38.188 63.798 1.00 136.85 ? 103 VAL A O 1 ATOM 609 C CB . VAL A 1 103 ? -49.259 -40.099 63.744 1.00 125.94 ? 103 VAL A CB 1 ATOM 610 C CG1 . VAL A 1 103 ? -49.948 -41.453 63.756 1.00 119.98 ? 103 VAL A CG1 1 ATOM 611 C CG2 . VAL A 1 103 ? -49.529 -39.342 65.036 1.00 126.82 ? 103 VAL A CG2 1 ATOM 612 N N . SER A 1 104 ? -47.100 -38.890 61.698 1.00 127.23 ? 104 SER A N 1 ATOM 613 C CA . SER A 1 104 ? -46.499 -37.700 61.115 1.00 136.55 ? 104 SER A CA 1 ATOM 614 C C . SER A 1 104 ? -47.526 -36.652 60.634 1.00 143.64 ? 104 SER A C 1 ATOM 615 O O . SER A 1 104 ? -48.746 -36.886 60.676 1.00 134.16 ? 104 SER A O 1 ATOM 616 C CB . SER A 1 104 ? -45.442 -38.049 60.053 1.00 141.15 ? 104 SER A CB 1 ATOM 617 O OG . SER A 1 104 ? -45.958 -37.993 58.738 1.00 147.78 ? 104 SER A OG 1 ATOM 618 N N . TYR A 1 105 ? -46.996 -35.504 60.200 1.00 149.82 ? 105 TYR A N 1 ATOM 619 C CA . TYR A 1 105 ? -47.740 -34.277 59.896 1.00 144.29 ? 105 TYR A CA 1 ATOM 620 C C . TYR A 1 105 ? -46.759 -33.352 59.239 1.00 143.49 ? 105 TYR A C 1 ATOM 621 O O . TYR A 1 105 ? -45.586 -33.718 59.094 1.00 149.95 ? 105 TYR A O 1 ATOM 622 C CB . TYR A 1 105 ? -48.180 -33.595 61.186 1.00 151.38 ? 105 TYR A CB 1 ATOM 623 C CG . TYR A 1 105 ? -47.318 -33.906 62.414 1.00 153.07 ? 105 TYR A CG 1 ATOM 624 C CD1 . TYR A 1 105 ? -45.974 -33.529 62.482 1.00 150.05 ? 105 TYR A CD1 1 ATOM 625 C CD2 . TYR A 1 105 ? -47.869 -34.576 63.519 1.00 152.75 ? 105 TYR A CD2 1 ATOM 626 C CE1 . TYR A 1 105 ? -45.209 -33.823 63.610 1.00 157.95 ? 105 TYR A CE1 1 ATOM 627 C CE2 . TYR A 1 105 ? -47.117 -34.870 64.650 1.00 152.51 ? 105 TYR A CE2 1 ATOM 628 C CZ . TYR A 1 105 ? -45.786 -34.498 64.700 1.00 156.25 ? 105 TYR A CZ 1 ATOM 629 O OH . TYR A 1 105 ? -45.040 -34.803 65.833 1.00 147.92 ? 105 TYR A OH 1 ATOM 630 N N . TRP A 1 106 ? -47.215 -32.154 58.870 1.00 139.72 ? 106 TRP A N 1 ATOM 631 C CA . TRP A 1 106 ? -46.282 -31.052 58.544 1.00 145.79 ? 106 TRP A CA 1 ATOM 632 C C . TRP A 1 106 ? -46.016 -30.211 59.794 1.00 143.75 ? 106 TRP A C 1 ATOM 633 O O . TRP A 1 106 ? -46.392 -30.636 60.902 1.00 147.32 ? 106 TRP A O 1 ATOM 634 C CB . TRP A 1 106 ? -46.825 -30.153 57.451 1.00 147.35 ? 106 TRP A CB 1 ATOM 635 C CG . TRP A 1 106 ? -47.159 -30.848 56.223 1.00 155.49 ? 106 TRP A CG 1 ATOM 636 C CD1 . TRP A 1 106 ? -48.362 -31.393 55.894 1.00 157.78 ? 106 TRP A CD1 1 ATOM 637 C CD2 . TRP A 1 106 ? -46.291 -31.075 55.118 1.00 169.41 ? 106 TRP A CD2 1 ATOM 638 N NE1 . TRP A 1 106 ? -48.298 -31.948 54.645 1.00 170.79 ? 106 TRP A NE1 1 ATOM 639 C CE2 . TRP A 1 106 ? -47.036 -31.768 54.142 1.00 178.76 ? 106 TRP A CE2 1 ATOM 640 C CE3 . TRP A 1 106 ? -44.948 -30.762 54.855 1.00 184.52 ? 106 TRP A CE3 1 ATOM 641 C CZ2 . TRP A 1 106 ? -46.484 -32.159 52.912 1.00 198.07 ? 106 TRP A CZ2 1 ATOM 642 C CZ3 . TRP A 1 106 ? -44.395 -31.147 53.631 1.00 202.24 ? 106 TRP A CZ3 1 ATOM 643 C CH2 . TRP A 1 106 ? -45.166 -31.840 52.675 1.00 211.13 ? 106 TRP A CH2 1 ATOM 644 N N . LYS A 1 107 ? -45.399 -29.029 59.640 1.00 127.36 ? 107 LYS A N 1 ATOM 645 C CA . LYS A 1 107 ? -45.125 -28.203 60.829 1.00 126.45 ? 107 LYS A CA 1 ATOM 646 C C . LYS A 1 107 ? -46.226 -27.241 61.329 1.00 138.77 ? 107 LYS A C 1 ATOM 647 O O . LYS A 1 107 ? -45.941 -26.323 62.100 1.00 153.01 ? 107 LYS A O 1 ATOM 648 C CB . LYS A 1 107 ? -43.773 -27.520 60.747 1.00 117.90 ? 107 LYS A CB 1 ATOM 649 C CG . LYS A 1 107 ? -42.658 -28.449 61.171 1.00 120.88 ? 107 LYS A CG 1 ATOM 650 C CD . LYS A 1 107 ? -41.499 -27.741 61.860 1.00 129.31 ? 107 LYS A CD 1 ATOM 651 C CE . LYS A 1 107 ? -41.271 -28.252 63.279 1.00 129.73 ? 107 LYS A CE 1 ATOM 652 N NZ . LYS A 1 107 ? -39.919 -27.895 63.802 1.00 129.06 ? 107 LYS A NZ 1 ATOM 653 N N . ALA A 1 108 ? -47.471 -27.461 60.895 1.00 143.39 ? 108 ALA A N 1 ATOM 654 C CA . ALA A 1 108 ? -48.659 -26.754 61.414 1.00 134.32 ? 108 ALA A CA 1 ATOM 655 C C . ALA A 1 108 ? -49.643 -27.782 61.909 1.00 134.86 ? 108 ALA A C 1 ATOM 656 O O . ALA A 1 108 ? -50.849 -27.552 61.933 1.00 137.86 ? 108 ALA A O 1 ATOM 657 C CB . ALA A 1 108 ? -49.305 -25.852 60.371 1.00 134.06 ? 108 ALA A CB 1 ATOM 658 N N . SER A 1 109 ? -49.104 -28.953 62.218 1.00 139.96 ? 109 SER A N 1 ATOM 659 C CA . SER A 1 109 ? -49.609 -29.795 63.289 1.00 154.05 ? 109 SER A CA 1 ATOM 660 C C . SER A 1 109 ? -48.346 -30.107 64.097 1.00 157.80 ? 109 SER A C 1 ATOM 661 O O . SER A 1 109 ? -47.372 -29.354 63.985 1.00 156.42 ? 109 SER A O 1 ATOM 662 C CB . SER A 1 109 ? -50.345 -31.026 62.760 1.00 156.21 ? 109 SER A CB 1 ATOM 663 O OG . SER A 1 109 ? -51.585 -30.662 62.168 1.00 152.38 ? 109 SER A OG 1 ATOM 664 N N . GLU A 1 110 ? -48.337 -31.175 64.899 1.00 161.82 ? 110 GLU A N 1 ATOM 665 C CA . GLU A 1 110 ? -47.228 -31.423 65.845 1.00 168.11 ? 110 GLU A CA 1 ATOM 666 C C . GLU A 1 110 ? -47.482 -30.640 67.119 1.00 173.03 ? 110 GLU A C 1 ATOM 667 O O . GLU A 1 110 ? -47.460 -31.207 68.206 1.00 191.50 ? 110 GLU A O 1 ATOM 668 C CB . GLU A 1 110 ? -45.854 -31.027 65.260 1.00 160.22 ? 110 GLU A CB 1 ATOM 669 C CG . GLU A 1 110 ? -44.695 -30.980 66.256 1.00 141.32 ? 110 GLU A CG 1 ATOM 670 C CD . GLU A 1 110 ? -43.470 -30.271 65.701 1.00 132.90 ? 110 GLU A CD 1 ATOM 671 O OE1 . GLU A 1 110 ? -43.627 -29.240 65.018 1.00 128.09 ? 110 GLU A OE1 1 ATOM 672 O OE2 . GLU A 1 110 ? -42.343 -30.740 65.957 1.00 128.35 ? 110 GLU A OE2 1 ATOM 673 N N . GLY A 1 111 ? -47.692 -29.334 66.975 1.00 159.76 ? 111 GLY A N 1 ATOM 674 C CA . GLY A 1 111 ? -48.151 -28.502 68.073 1.00 154.12 ? 111 GLY A CA 1 ATOM 675 C C . GLY A 1 111 ? -47.125 -28.319 69.164 1.00 156.12 ? 111 GLY A C 1 ATOM 676 O O . GLY A 1 111 ? -47.447 -28.432 70.354 1.00 158.29 ? 111 GLY A O 1 ATOM 677 N N . ALA A 1 112 ? -45.889 -28.031 68.760 1.00 151.91 ? 112 ALA A N 1 ATOM 678 C CA . ALA A 1 112 ? -44.827 -27.740 69.716 1.00 151.14 ? 112 ALA A CA 1 ATOM 679 C C . ALA A 1 112 ? -43.911 -26.618 69.230 1.00 143.84 ? 112 ALA A C 1 ATOM 680 O O . ALA A 1 112 ? -43.634 -26.514 68.029 1.00 125.29 ? 112 ALA A O 1 ATOM 681 C CB . ALA A 1 112 ? -44.040 -29.003 70.009 1.00 161.50 ? 112 ALA A CB 1 ATOM 682 N N . GLU A 1 113 ? -43.445 -25.788 70.165 1.00 149.08 ? 113 GLU A N 1 ATOM 683 C CA . GLU A 1 113 ? -42.698 -24.579 69.804 1.00 169.66 ? 113 GLU A CA 1 ATOM 684 C C . GLU A 1 113 ? -41.196 -24.633 70.101 1.00 177.56 ? 113 GLU A C 1 ATOM 685 O O . GLU A 1 113 ? -40.806 -24.691 71.269 1.00 207.40 ? 113 GLU A O 1 ATOM 686 C CB . GLU A 1 113 ? -43.315 -23.341 70.472 1.00 180.21 ? 113 GLU A CB 1 ATOM 687 C CG . GLU A 1 113 ? -42.544 -22.048 70.211 1.00 192.87 ? 113 GLU A CG 1 ATOM 688 C CD . GLU A 1 113 ? -43.395 -20.799 70.356 1.00 206.35 ? 113 GLU A CD 1 ATOM 689 O OE1 . GLU A 1 113 ? -43.823 -20.499 71.498 1.00 215.68 ? 113 GLU A OE1 1 ATOM 690 O OE2 . GLU A 1 113 ? -43.621 -20.114 69.326 1.00 203.25 ? 113 GLU A OE2 1 ATOM 691 N N . TYR A 1 114 ? -40.376 -24.604 69.040 1.00 167.69 ? 114 TYR A N 1 ATOM 692 C CA . TYR A 1 114 ? -38.901 -24.463 69.120 1.00 156.16 ? 114 TYR A CA 1 ATOM 693 C C . TYR A 1 114 ? -38.384 -23.568 67.989 1.00 154.34 ? 114 TYR A C 1 ATOM 694 O O . TYR A 1 114 ? -38.432 -22.346 68.100 1.00 161.99 ? 114 TYR A O 1 ATOM 695 C CB . TYR A 1 114 ? -38.154 -25.823 69.187 1.00 151.28 ? 114 TYR A CB 1 ATOM 696 C CG . TYR A 1 114 ? -38.680 -26.955 68.289 1.00 157.95 ? 114 TYR A CG 1 ATOM 697 C CD1 . TYR A 1 114 ? -40.030 -27.340 68.293 1.00 154.77 ? 114 TYR A CD1 1 ATOM 698 C CD2 . TYR A 1 114 ? -37.821 -27.658 67.444 1.00 163.03 ? 114 TYR A CD2 1 ATOM 699 C CE1 . TYR A 1 114 ? -40.498 -28.372 67.476 1.00 144.07 ? 114 TYR A CE1 1 ATOM 700 C CE2 . TYR A 1 114 ? -38.290 -28.688 66.624 1.00 149.42 ? 114 TYR A CE2 1 ATOM 701 C CZ . TYR A 1 114 ? -39.623 -29.048 66.653 1.00 137.00 ? 114 TYR A CZ 1 ATOM 702 O OH . TYR A 1 114 ? -40.077 -30.062 65.852 1.00 121.10 ? 114 TYR A OH 1 ATOM 703 N N . ASP A 1 115 ? -37.896 -24.169 66.909 1.00 150.15 ? 115 ASP A N 1 ATOM 704 C CA . ASP A 1 115 ? -37.492 -23.429 65.714 1.00 148.24 ? 115 ASP A CA 1 ATOM 705 C C . ASP A 1 115 ? -38.018 -24.118 64.493 1.00 148.32 ? 115 ASP A C 1 ATOM 706 O O . ASP A 1 115 ? -37.259 -24.665 63.691 1.00 145.35 ? 115 ASP A O 1 ATOM 707 C CB . ASP A 1 115 ? -35.980 -23.315 65.604 1.00 147.53 ? 115 ASP A CB 1 ATOM 708 C CG . ASP A 1 115 ? -35.396 -22.516 66.712 1.00 152.15 ? 115 ASP A CG 1 ATOM 709 O OD1 . ASP A 1 115 ? -35.418 -23.003 67.874 1.00 153.57 ? 115 ASP A OD1 1 ATOM 710 O OD2 . ASP A 1 115 ? -34.926 -21.398 66.417 1.00 151.19 ? 115 ASP A OD2 1 ATOM 711 N N . ASP A 1 116 ? -39.338 -24.112 64.377 1.00 157.02 ? 116 ASP A N 1 ATOM 712 C CA . ASP A 1 116 ? -39.980 -24.410 63.116 1.00 164.50 ? 116 ASP A CA 1 ATOM 713 C C . ASP A 1 116 ? -39.284 -23.525 62.078 1.00 162.75 ? 116 ASP A C 1 ATOM 714 O O . ASP A 1 116 ? -39.035 -23.958 60.958 1.00 165.13 ? 116 ASP A O 1 ATOM 715 C CB . ASP A 1 116 ? -41.482 -24.063 63.153 1.00 172.67 ? 116 ASP A CB 1 ATOM 716 C CG . ASP A 1 116 ? -42.241 -24.732 64.307 1.00 177.36 ? 116 ASP A CG 1 ATOM 717 O OD1 . ASP A 1 116 ? -41.668 -24.882 65.411 1.00 182.16 ? 116 ASP A OD1 1 ATOM 718 O OD2 . ASP A 1 116 ? -43.434 -25.083 64.112 1.00 182.04 ? 116 ASP A OD2 1 ATOM 719 N N . GLN A 1 117 ? -38.938 -22.303 62.484 1.00 155.94 ? 117 GLN A N 1 ATOM 720 C CA . GLN A 1 117 ? -38.496 -21.265 61.570 1.00 159.22 ? 117 GLN A CA 1 ATOM 721 C C . GLN A 1 117 ? -39.638 -20.647 60.797 1.00 173.87 ? 117 GLN A C 1 ATOM 722 O O . GLN A 1 117 ? -39.435 -19.662 60.083 1.00 209.30 ? 117 GLN A O 1 ATOM 723 C CB . GLN A 1 117 ? -37.491 -21.799 60.560 1.00 149.91 ? 117 GLN A CB 1 ATOM 724 C CG . GLN A 1 117 ? -36.129 -21.189 60.709 1.00 157.76 ? 117 GLN A CG 1 ATOM 725 C CD . GLN A 1 117 ? -35.431 -21.674 61.952 1.00 164.97 ? 117 GLN A CD 1 ATOM 726 O OE1 . GLN A 1 117 ? -36.003 -22.410 62.774 1.00 151.97 ? 117 GLN A OE1 1 ATOM 727 N NE2 . GLN A 1 117 ? -34.177 -21.264 62.101 1.00 181.98 ? 117 GLN A NE2 1 ATOM 728 N N . THR A 1 118 ? -40.831 -21.213 60.933 1.00 167.47 ? 118 THR A N 1 ATOM 729 C CA . THR A 1 118 ? -41.911 -20.941 59.988 1.00 165.41 ? 118 THR A CA 1 ATOM 730 C C . THR A 1 118 ? -42.727 -19.714 60.334 1.00 164.33 ? 118 THR A C 1 ATOM 731 O O . THR A 1 118 ? -42.665 -19.235 61.461 1.00 158.40 ? 118 THR A O 1 ATOM 732 C CB . THR A 1 118 ? -42.856 -22.142 59.879 1.00 164.96 ? 118 THR A CB 1 ATOM 733 O OG1 . THR A 1 118 ? -43.229 -22.578 61.196 1.00 164.62 ? 118 THR A OG1 1 ATOM 734 C CG2 . THR A 1 118 ? -42.191 -23.281 59.105 1.00 163.12 ? 118 THR A CG2 1 ATOM 735 N N . SER A 1 119 ? -43.488 -19.222 59.350 1.00 175.42 ? 119 SER A N 1 ATOM 736 C CA . SER A 1 119 ? -44.478 -18.153 59.547 1.00 192.48 ? 119 SER A CA 1 ATOM 737 C C . SER A 1 119 ? -45.610 -18.593 60.485 1.00 184.57 ? 119 SER A C 1 ATOM 738 O O . SER A 1 119 ? -45.726 -19.763 60.836 1.00 176.06 ? 119 SER A O 1 ATOM 739 C CB . SER A 1 119 ? -45.067 -17.705 58.205 1.00 208.17 ? 119 SER A CB 1 ATOM 740 O OG . SER A 1 119 ? -46.161 -18.533 57.833 1.00 217.90 ? 119 SER A OG 1 ATOM 741 N N . GLN A 1 120 ? -46.456 -17.657 60.882 1.00 184.91 ? 120 GLN A N 1 ATOM 742 C CA . GLN A 1 120 ? -47.410 -17.948 61.939 1.00 192.58 ? 120 GLN A CA 1 ATOM 743 C C . GLN A 1 120 ? -48.485 -18.939 61.525 1.00 194.18 ? 120 GLN A C 1 ATOM 744 O O . GLN A 1 120 ? -48.870 -19.779 62.336 1.00 199.25 ? 120 GLN A O 1 ATOM 745 C CB . GLN A 1 120 ? -48.011 -16.667 62.538 1.00 205.41 ? 120 GLN A CB 1 ATOM 746 C CG . GLN A 1 120 ? -47.043 -15.854 63.395 1.00 216.81 ? 120 GLN A CG 1 ATOM 747 C CD . GLN A 1 120 ? -45.760 -15.470 62.655 1.00 231.18 ? 120 GLN A CD 1 ATOM 748 O OE1 . GLN A 1 120 ? -44.787 -16.227 62.643 1.00 228.03 ? 120 GLN A OE1 1 ATOM 749 N NE2 . GLN A 1 120 ? -45.754 -14.287 62.039 1.00 243.08 ? 120 GLN A NE2 1 ATOM 750 N N . ARG A 1 121 ? -48.955 -18.890 60.276 1.00 195.72 ? 121 ARG A N 1 ATOM 751 C CA . ARG A 1 121 ? -49.959 -19.876 59.851 1.00 193.60 ? 121 ARG A CA 1 ATOM 752 C C . ARG A 1 121 ? -49.286 -21.250 59.858 1.00 192.37 ? 121 ARG A C 1 ATOM 753 O O . ARG A 1 121 ? -49.924 -22.283 59.605 1.00 194.80 ? 121 ARG A O 1 ATOM 754 C CB . ARG A 1 121 ? -50.604 -19.535 58.499 1.00 181.84 ? 121 ARG A CB 1 ATOM 755 C CG . ARG A 1 121 ? -52.107 -19.804 58.461 1.00 171.36 ? 121 ARG A CG 1 ATOM 756 C CD . ARG A 1 121 ? -52.656 -19.793 57.048 1.00 172.26 ? 121 ARG A CD 1 ATOM 757 N NE . ARG A 1 121 ? -52.776 -18.444 56.496 1.00 198.04 ? 121 ARG A NE 1 ATOM 758 C CZ . ARG A 1 121 ? -51.893 -17.859 55.677 1.00 220.96 ? 121 ARG A CZ 1 ATOM 759 N NH1 . ARG A 1 121 ? -50.797 -18.504 55.305 1.00 237.39 ? 121 ARG A NH1 1 ATOM 760 N NH2 . ARG A 1 121 ? -52.098 -16.618 55.221 1.00 222.86 ? 121 ARG A NH2 1 ATOM 761 N N . GLU A 1 122 ? -47.991 -21.222 60.188 1.00 183.01 ? 122 GLU A N 1 ATOM 762 C CA . GLU A 1 122 ? -47.176 -22.411 60.419 1.00 170.91 ? 122 GLU A CA 1 ATOM 763 C C . GLU A 1 122 ? -46.691 -22.524 61.880 1.00 152.23 ? 122 GLU A C 1 ATOM 764 O O . GLU A 1 122 ? -46.084 -23.526 62.256 1.00 139.51 ? 122 GLU A O 1 ATOM 765 C CB . GLU A 1 122 ? -45.970 -22.431 59.465 1.00 183.32 ? 122 GLU A CB 1 ATOM 766 C CG . GLU A 1 122 ? -46.266 -22.603 57.976 1.00 194.65 ? 122 GLU A CG 1 ATOM 767 C CD . GLU A 1 122 ? -44.992 -22.664 57.141 1.00 197.84 ? 122 GLU A CD 1 ATOM 768 O OE1 . GLU A 1 122 ? -44.410 -21.591 56.868 1.00 202.96 ? 122 GLU A OE1 1 ATOM 769 O OE2 . GLU A 1 122 ? -44.562 -23.781 56.766 1.00 191.10 ? 122 GLU A OE2 1 ATOM 770 N N . LYS A 1 123 ? -46.940 -21.498 62.693 1.00 146.83 ? 123 LYS A N 1 ATOM 771 C CA . LYS A 1 123 ? -46.680 -21.591 64.145 1.00 149.78 ? 123 LYS A CA 1 ATOM 772 C C . LYS A 1 123 ? -47.918 -21.421 65.051 1.00 154.45 ? 123 LYS A C 1 ATOM 773 O O . LYS A 1 123 ? -47.788 -21.262 66.277 1.00 144.42 ? 123 LYS A O 1 ATOM 774 C CB . LYS A 1 123 ? -45.558 -20.645 64.588 1.00 146.58 ? 123 LYS A CB 1 ATOM 775 C CG . LYS A 1 123 ? -44.183 -21.267 64.524 1.00 139.32 ? 123 LYS A CG 1 ATOM 776 C CD . LYS A 1 123 ? -43.250 -20.665 65.551 1.00 136.10 ? 123 LYS A CD 1 ATOM 777 C CE . LYS A 1 123 ? -41.835 -20.772 65.016 1.00 139.55 ? 123 LYS A CE 1 ATOM 778 N NZ . LYS A 1 123 ? -40.829 -20.987 66.089 1.00 144.77 ? 123 LYS A NZ 1 ATOM 779 N N . GLU A 1 124 ? -49.105 -21.455 64.440 1.00 165.47 ? 124 GLU A N 1 ATOM 780 C CA . GLU A 1 124 ? -50.375 -21.386 65.170 1.00 171.16 ? 124 GLU A CA 1 ATOM 781 C C . GLU A 1 124 ? -50.650 -22.644 65.976 1.00 170.00 ? 124 GLU A C 1 ATOM 782 O O . GLU A 1 124 ? -51.212 -22.570 67.064 1.00 186.85 ? 124 GLU A O 1 ATOM 783 C CB . GLU A 1 124 ? -51.542 -21.117 64.227 1.00 174.16 ? 124 GLU A CB 1 ATOM 784 C CG . GLU A 1 124 ? -52.202 -19.782 64.478 1.00 191.46 ? 124 GLU A CG 1 ATOM 785 C CD . GLU A 1 124 ? -52.634 -19.128 63.194 1.00 210.86 ? 124 GLU A CD 1 ATOM 786 O OE1 . GLU A 1 124 ? -53.107 -19.861 62.291 1.00 217.58 ? 124 GLU A OE1 1 ATOM 787 O OE2 . GLU A 1 124 ? -52.483 -17.886 63.094 1.00 216.60 ? 124 GLU A OE2 1 ATOM 788 N N . ASP A 1 125 ? -50.266 -23.796 65.437 1.00 156.81 ? 125 ASP A N 1 ATOM 789 C CA . ASP A 1 125 ? -50.393 -25.047 66.152 1.00 142.68 ? 125 ASP A CA 1 ATOM 790 C C . ASP A 1 125 ? -49.630 -25.008 67.482 1.00 146.28 ? 125 ASP A C 1 ATOM 791 O O . ASP A 1 125 ? -50.132 -25.508 68.489 1.00 144.73 ? 125 ASP A O 1 ATOM 792 C CB . ASP A 1 125 ? -49.928 -26.220 65.271 1.00 144.37 ? 125 ASP A CB 1 ATOM 793 C CG . ASP A 1 125 ? -48.503 -26.036 64.704 1.00 144.15 ? 125 ASP A CG 1 ATOM 794 O OD1 . ASP A 1 125 ? -48.279 -25.095 63.913 1.00 142.52 ? 125 ASP A OD1 1 ATOM 795 O OD2 . ASP A 1 125 ? -47.610 -26.851 65.035 1.00 146.61 ? 125 ASP A OD2 1 ATOM 796 N N . ASP A 1 126 ? -48.459 -24.351 67.477 1.00 153.53 ? 126 ASP A N 1 ATOM 797 C CA . ASP A 1 126 ? -47.390 -24.459 68.525 1.00 157.88 ? 126 ASP A CA 1 ATOM 798 C C . ASP A 1 126 ? -47.747 -24.160 70.013 1.00 151.76 ? 126 ASP A C 1 ATOM 799 O O . ASP A 1 126 ? -46.981 -24.522 70.936 1.00 138.25 ? 126 ASP A O 1 ATOM 800 C CB . ASP A 1 126 ? -46.156 -23.609 68.121 1.00 161.30 ? 126 ASP A CB 1 ATOM 801 C CG . ASP A 1 126 ? -45.479 -24.087 66.831 1.00 157.20 ? 126 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 126 ? -46.183 -24.326 65.829 1.00 161.64 ? 126 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 126 ? -44.235 -24.204 66.819 1.00 151.82 ? 126 ASP A OD2 1 ATOM 804 N N . LYS A 1 127 ? -48.903 -23.514 70.211 1.00 152.96 ? 127 LYS A N 1 ATOM 805 C CA . LYS A 1 127 ? -49.335 -22.883 71.466 1.00 151.63 ? 127 LYS A CA 1 ATOM 806 C C . LYS A 1 127 ? -50.724 -22.306 71.206 1.00 145.44 ? 127 LYS A C 1 ATOM 807 O O . LYS A 1 127 ? -50.796 -21.171 70.763 1.00 153.79 ? 127 LYS A O 1 ATOM 808 C CB . LYS A 1 127 ? -48.405 -21.687 71.826 1.00 161.76 ? 127 LYS A CB 1 ATOM 809 C CG . LYS A 1 127 ? -47.443 -21.844 73.005 1.00 170.09 ? 127 LYS A CG 1 ATOM 810 C CD . LYS A 1 127 ? -47.201 -20.508 73.707 1.00 183.92 ? 127 LYS A CD 1 ATOM 811 C CE . LYS A 1 127 ? -47.250 -20.655 75.228 1.00 189.51 ? 127 LYS A CE 1 ATOM 812 N NZ . LYS A 1 127 ? -47.909 -19.499 75.919 1.00 186.12 ? 127 LYS A NZ 1 ATOM 813 N N . VAL A 1 128 ? -51.823 -23.027 71.440 1.00 145.33 ? 128 VAL A N 1 ATOM 814 C CA . VAL A 1 128 ? -53.149 -22.361 71.295 1.00 166.86 ? 128 VAL A CA 1 ATOM 815 C C . VAL A 1 128 ? -53.517 -21.579 72.565 1.00 187.78 ? 128 VAL A C 1 ATOM 816 O O . VAL A 1 128 ? -53.570 -22.155 73.665 1.00 201.12 ? 128 VAL A O 1 ATOM 817 C CB . VAL A 1 128 ? -54.331 -23.288 70.901 1.00 162.59 ? 128 VAL A CB 1 ATOM 818 C CG1 . VAL A 1 128 ? -55.282 -22.551 69.971 1.00 153.11 ? 128 VAL A CG1 1 ATOM 819 C CG2 . VAL A 1 128 ? -53.845 -24.557 70.232 1.00 168.94 ? 128 VAL A CG2 1 ATOM 820 N N . PHE A 1 129 ? -53.764 -20.273 72.406 1.00 191.66 ? 129 PHE A N 1 ATOM 821 C CA . PHE A 1 129 ? -54.007 -19.372 73.542 1.00 194.43 ? 129 PHE A CA 1 ATOM 822 C C . PHE A 1 129 ? -55.414 -19.583 74.125 1.00 201.26 ? 129 PHE A C 1 ATOM 823 O O . PHE A 1 129 ? -56.302 -20.040 73.397 1.00 194.65 ? 129 PHE A O 1 ATOM 824 C CB . PHE A 1 129 ? -53.799 -17.902 73.133 1.00 194.43 ? 129 PHE A CB 1 ATOM 825 C CG . PHE A 1 129 ? -52.362 -17.426 73.200 1.00 189.98 ? 129 PHE A CG 1 ATOM 826 C CD1 . PHE A 1 129 ? -51.346 -18.245 73.691 1.00 185.98 ? 129 PHE A CD1 1 ATOM 827 C CD2 . PHE A 1 129 ? -52.038 -16.124 72.807 1.00 198.90 ? 129 PHE A CD2 1 ATOM 828 C CE1 . PHE A 1 129 ? -50.035 -17.795 73.749 1.00 189.23 ? 129 PHE A CE1 1 ATOM 829 C CE2 . PHE A 1 129 ? -50.733 -15.664 72.872 1.00 200.96 ? 129 PHE A CE2 1 ATOM 830 C CZ . PHE A 1 129 ? -49.730 -16.506 73.340 1.00 200.91 ? 129 PHE A CZ 1 ATOM 831 N N . PRO A 1 130 ? -55.621 -19.266 75.436 1.00 206.86 ? 130 PRO A N 1 ATOM 832 C CA . PRO A 1 130 ? -56.942 -19.428 76.073 1.00 202.13 ? 130 PRO A CA 1 ATOM 833 C C . PRO A 1 130 ? -58.077 -18.845 75.221 1.00 195.87 ? 130 PRO A C 1 ATOM 834 O O . PRO A 1 130 ? -57.984 -17.692 74.796 1.00 204.79 ? 130 PRO A O 1 ATOM 835 C CB . PRO A 1 130 ? -56.793 -18.646 77.386 1.00 208.56 ? 130 PRO A CB 1 ATOM 836 C CG . PRO A 1 130 ? -55.345 -18.756 77.721 1.00 208.93 ? 130 PRO A CG 1 ATOM 837 C CD . PRO A 1 130 ? -54.608 -18.786 76.406 1.00 209.83 ? 130 PRO A CD 1 ATOM 838 N N . GLY A 1 131 ? -59.118 -19.644 74.968 1.00 186.17 ? 131 GLY A N 1 ATOM 839 C CA . GLY A 1 131 ? -60.235 -19.270 74.075 1.00 182.73 ? 131 GLY A CA 1 ATOM 840 C C . GLY A 1 131 ? -60.005 -19.619 72.602 1.00 180.03 ? 131 GLY A C 1 ATOM 841 O O . GLY A 1 131 ? -60.859 -19.325 71.733 1.00 167.73 ? 131 GLY A O 1 ATOM 842 N N . GLY A 1 132 ? -58.870 -20.284 72.340 1.00 183.56 ? 132 GLY A N 1 ATOM 843 C CA . GLY A 1 132 ? -58.319 -20.485 70.986 1.00 198.53 ? 132 GLY A CA 1 ATOM 844 C C . GLY A 1 132 ? -58.528 -21.798 70.234 1.00 199.44 ? 132 GLY A C 1 ATOM 845 O O . GLY A 1 132 ? -57.814 -22.795 70.456 1.00 179.70 ? 132 GLY A O 1 ATOM 846 N N . SER A 1 133 ? -59.492 -21.766 69.313 1.00 204.24 ? 133 SER A N 1 ATOM 847 C CA . SER A 1 133 ? -59.757 -22.864 68.398 1.00 192.05 ? 133 SER A CA 1 ATOM 848 C C . SER A 1 133 ? -58.777 -22.841 67.202 1.00 204.63 ? 133 SER A C 1 ATOM 849 O O . SER A 1 133 ? -58.669 -21.845 66.465 1.00 218.31 ? 133 SER A O 1 ATOM 850 C CB . SER A 1 133 ? -61.227 -22.830 67.941 1.00 179.53 ? 133 SER A CB 1 ATOM 851 O OG . SER A 1 133 ? -62.131 -22.964 69.035 1.00 168.54 ? 133 SER A OG 1 ATOM 852 N N . HIS A 1 134 ? -58.027 -23.930 67.055 1.00 203.59 ? 134 HIS A N 1 ATOM 853 C CA . HIS A 1 134 ? -57.256 -24.190 65.839 1.00 197.90 ? 134 HIS A CA 1 ATOM 854 C C . HIS A 1 134 ? -57.119 -25.707 65.574 1.00 184.49 ? 134 HIS A C 1 ATOM 855 O O . HIS A 1 134 ? -56.878 -26.508 66.495 1.00 160.94 ? 134 HIS A O 1 ATOM 856 C CB . HIS A 1 134 ? -55.909 -23.455 65.855 1.00 196.94 ? 134 HIS A CB 1 ATOM 857 C CG . HIS A 1 134 ? -54.831 -24.163 65.097 1.00 197.65 ? 134 HIS A CG 1 ATOM 858 N ND1 . HIS A 1 134 ? -54.197 -25.289 65.582 1.00 189.10 ? 134 HIS A ND1 1 ATOM 859 C CD2 . HIS A 1 134 ? -54.281 -23.914 63.887 1.00 196.89 ? 134 HIS A CD2 1 ATOM 860 C CE1 . HIS A 1 134 ? -53.299 -25.700 64.707 1.00 173.26 ? 134 HIS A CE1 1 ATOM 861 N NE2 . HIS A 1 134 ? -53.330 -24.884 63.670 1.00 186.03 ? 134 HIS A NE2 1 ATOM 862 N N . THR A 1 135 ? -57.285 -26.066 64.298 1.00 182.08 ? 135 THR A N 1 ATOM 863 C CA . THR A 1 135 ? -57.396 -27.448 63.842 1.00 171.15 ? 135 THR A CA 1 ATOM 864 C C . THR A 1 135 ? -56.050 -28.046 63.554 1.00 165.66 ? 135 THR A C 1 ATOM 865 O O . THR A 1 135 ? -55.138 -27.350 63.103 1.00 162.53 ? 135 THR A O 1 ATOM 866 C CB . THR A 1 135 ? -58.128 -27.536 62.500 1.00 176.44 ? 135 THR A CB 1 ATOM 867 O OG1 . THR A 1 135 ? -59.227 -26.625 62.481 1.00 200.50 ? 135 THR A OG1 1 ATOM 868 C CG2 . THR A 1 135 ? -58.630 -28.938 62.277 1.00 175.47 ? 135 THR A CG2 1 ATOM 869 N N . TYR A 1 136 ? -55.954 -29.355 63.775 1.00 160.29 ? 136 TYR A N 1 ATOM 870 C CA . TYR A 1 136 ? -54.757 -30.127 63.458 1.00 155.73 ? 136 TYR A CA 1 ATOM 871 C C . TYR A 1 136 ? -55.067 -31.174 62.398 1.00 151.47 ? 136 TYR A C 1 ATOM 872 O O . TYR A 1 136 ? -56.242 -31.549 62.193 1.00 138.80 ? 136 TYR A O 1 ATOM 873 C CB . TYR A 1 136 ? -54.230 -30.852 64.699 1.00 155.10 ? 136 TYR A CB 1 ATOM 874 C CG . TYR A 1 136 ? -53.638 -29.974 65.766 1.00 155.33 ? 136 TYR A CG 1 ATOM 875 C CD1 . TYR A 1 136 ? -54.446 -29.125 66.537 1.00 158.43 ? 136 TYR A CD1 1 ATOM 876 C CD2 . TYR A 1 136 ? -52.277 -30.012 66.032 1.00 154.30 ? 136 TYR A CD2 1 ATOM 877 C CE1 . TYR A 1 136 ? -53.906 -28.321 67.525 1.00 153.78 ? 136 TYR A CE1 1 ATOM 878 C CE2 . TYR A 1 136 ? -51.729 -29.215 67.024 1.00 161.78 ? 136 TYR A CE2 1 ATOM 879 C CZ . TYR A 1 136 ? -52.546 -28.374 67.763 1.00 156.23 ? 136 TYR A CZ 1 ATOM 880 O OH . TYR A 1 136 ? -51.988 -27.594 68.744 1.00 155.18 ? 136 TYR A OH 1 ATOM 881 N N . VAL A 1 137 ? -54.003 -31.637 61.732 1.00 145.96 ? 137 VAL A N 1 ATOM 882 C CA . VAL A 1 137 ? -54.080 -32.805 60.861 1.00 137.84 ? 137 VAL A CA 1 ATOM 883 C C . VAL A 1 137 ? -52.889 -33.722 60.987 1.00 141.83 ? 137 VAL A C 1 ATOM 884 O O . VAL A 1 137 ? -51.738 -33.313 60.761 1.00 145.61 ? 137 VAL A O 1 ATOM 885 C CB . VAL A 1 137 ? -54.180 -32.458 59.376 1.00 133.43 ? 137 VAL A CB 1 ATOM 886 C CG1 . VAL A 1 137 ? -52.788 -32.335 58.754 1.00 122.82 ? 137 VAL A CG1 1 ATOM 887 C CG2 . VAL A 1 137 ? -54.989 -33.541 58.676 1.00 129.52 ? 137 VAL A CG2 1 ATOM 888 N N . TRP A 1 138 ? -53.202 -34.975 61.296 1.00 145.06 ? 138 TRP A N 1 ATOM 889 C CA . TRP A 1 138 ? -52.244 -36.060 61.266 1.00 143.19 ? 138 TRP A CA 1 ATOM 890 C C . TRP A 1 138 ? -52.576 -37.049 60.128 1.00 145.74 ? 138 TRP A C 1 ATOM 891 O O . TRP A 1 138 ? -53.763 -37.378 59.911 1.00 139.50 ? 138 TRP A O 1 ATOM 892 C CB . TRP A 1 138 ? -52.276 -36.797 62.604 1.00 138.71 ? 138 TRP A CB 1 ATOM 893 C CG . TRP A 1 138 ? -52.129 -35.955 63.839 1.00 135.69 ? 138 TRP A CG 1 ATOM 894 C CD1 . TRP A 1 138 ? -51.308 -34.876 64.022 1.00 147.49 ? 138 TRP A CD1 1 ATOM 895 C CD2 . TRP A 1 138 ? -52.774 -36.176 65.080 1.00 133.80 ? 138 TRP A CD2 1 ATOM 896 N NE1 . TRP A 1 138 ? -51.423 -34.395 65.305 1.00 145.54 ? 138 TRP A NE1 1 ATOM 897 C CE2 . TRP A 1 138 ? -52.319 -35.180 65.975 1.00 141.47 ? 138 TRP A CE2 1 ATOM 898 C CE3 . TRP A 1 138 ? -53.696 -37.116 65.526 1.00 135.06 ? 138 TRP A CE3 1 ATOM 899 C CZ2 . TRP A 1 138 ? -52.762 -35.100 67.285 1.00 148.89 ? 138 TRP A CZ2 1 ATOM 900 C CZ3 . TRP A 1 138 ? -54.136 -37.037 66.817 1.00 154.14 ? 138 TRP A CZ3 1 ATOM 901 C CH2 . TRP A 1 138 ? -53.671 -36.034 67.690 1.00 159.54 ? 138 TRP A CH2 1 ATOM 902 N N . GLN A 1 139 ? -51.544 -37.501 59.399 1.00 139.26 ? 139 GLN A N 1 ATOM 903 C CA . GLN A 1 139 ? -51.674 -38.714 58.564 1.00 138.96 ? 139 GLN A CA 1 ATOM 904 C C . GLN A 1 139 ? -50.854 -39.908 59.090 1.00 131.73 ? 139 GLN A C 1 ATOM 905 O O . GLN A 1 139 ? -50.113 -39.792 60.086 1.00 118.04 ? 139 GLN A O 1 ATOM 906 C CB . GLN A 1 139 ? -51.429 -38.470 57.071 1.00 139.13 ? 139 GLN A CB 1 ATOM 907 C CG . GLN A 1 139 ? -50.217 -37.632 56.769 1.00 154.46 ? 139 GLN A CG 1 ATOM 908 C CD . GLN A 1 139 ? -50.617 -36.258 56.316 1.00 177.60 ? 139 GLN A CD 1 ATOM 909 O OE1 . GLN A 1 139 ? -50.241 -35.245 56.923 1.00 196.93 ? 139 GLN A OE1 1 ATOM 910 N NE2 . GLN A 1 139 ? -51.407 -36.209 55.245 1.00 185.23 ? 139 GLN A NE2 1 ATOM 911 N N . VAL A 1 140 ? -51.021 -41.054 58.427 1.00 130.61 ? 140 VAL A N 1 ATOM 912 C CA . VAL A 1 140 ? -50.533 -42.327 58.947 1.00 141.38 ? 140 VAL A CA 1 ATOM 913 C C . VAL A 1 140 ? -49.913 -43.213 57.864 1.00 153.23 ? 140 VAL A C 1 ATOM 914 O O . VAL A 1 140 ? -50.419 -44.305 57.591 1.00 169.89 ? 140 VAL A O 1 ATOM 915 C CB . VAL A 1 140 ? -51.652 -43.117 59.686 1.00 139.39 ? 140 VAL A CB 1 ATOM 916 C CG1 . VAL A 1 140 ? -51.912 -42.545 61.074 1.00 127.40 ? 140 VAL A CG1 1 ATOM 917 C CG2 . VAL A 1 140 ? -52.934 -43.150 58.865 1.00 144.28 ? 140 VAL A CG2 1 ATOM 918 N N . LEU A 1 141 ? -48.796 -42.759 57.288 1.00 156.73 ? 141 LEU A N 1 ATOM 919 C CA . LEU A 1 141 ? -48.171 -43.399 56.106 1.00 166.25 ? 141 LEU A CA 1 ATOM 920 C C . LEU A 1 141 ? -47.784 -44.865 56.284 1.00 168.32 ? 141 LEU A C 1 ATOM 921 O O . LEU A 1 141 ? -47.663 -45.348 57.428 1.00 158.07 ? 141 LEU A O 1 ATOM 922 C CB . LEU A 1 141 ? -46.955 -42.603 55.637 1.00 158.90 ? 141 LEU A CB 1 ATOM 923 C CG . LEU A 1 141 ? -47.303 -41.136 55.437 1.00 156.83 ? 141 LEU A CG 1 ATOM 924 C CD1 . LEU A 1 141 ? -46.989 -40.311 56.680 1.00 139.71 ? 141 LEU A CD1 1 ATOM 925 C CD2 . LEU A 1 141 ? -46.571 -40.613 54.213 1.00 177.32 ? 141 LEU A CD2 1 ATOM 926 N N . LYS A 1 142 ? -47.586 -45.565 55.156 1.00 164.06 ? 142 LYS A N 1 ATOM 927 C CA . LYS A 1 142 ? -47.203 -46.972 55.215 1.00 157.46 ? 142 LYS A CA 1 ATOM 928 C C . LYS A 1 142 ? -46.095 -47.044 56.259 1.00 153.24 ? 142 LYS A C 1 ATOM 929 O O . LYS A 1 142 ? -46.007 -48.005 57.016 1.00 152.63 ? 142 LYS A O 1 ATOM 930 C CB . LYS A 1 142 ? -46.753 -47.526 53.851 1.00 165.26 ? 142 LYS A CB 1 ATOM 931 C CG . LYS A 1 142 ? -47.016 -49.024 53.682 1.00 177.10 ? 142 LYS A CG 1 ATOM 932 C CD . LYS A 1 142 ? -45.860 -49.793 53.034 1.00 187.75 ? 142 LYS A CD 1 ATOM 933 C CE . LYS A 1 142 ? -46.005 -51.311 53.218 1.00 193.99 ? 142 LYS A CE 1 ATOM 934 N NZ . LYS A 1 142 ? -46.077 -51.816 54.634 1.00 163.17 ? 142 LYS A NZ 1 ATOM 935 N N . GLU A 1 143 ? -45.301 -45.971 56.320 1.00 161.41 ? 143 GLU A N 1 ATOM 936 C CA . GLU A 1 143 ? -44.239 -45.777 57.319 1.00 162.39 ? 143 GLU A CA 1 ATOM 937 C C . GLU A 1 143 ? -44.768 -45.749 58.790 1.00 132.42 ? 143 GLU A C 1 ATOM 938 O O . GLU A 1 143 ? -44.383 -46.587 59.599 1.00 111.95 ? 143 GLU A O 1 ATOM 939 C CB . GLU A 1 143 ? -43.337 -44.559 56.912 1.00 186.13 ? 143 GLU A CB 1 ATOM 940 C CG . GLU A 1 143 ? -42.305 -44.025 57.927 1.00 221.35 ? 143 GLU A CG 1 ATOM 941 C CD . GLU A 1 143 ? -41.037 -44.878 58.127 1.00 240.16 ? 143 GLU A CD 1 ATOM 942 O OE1 . GLU A 1 143 ? -40.895 -45.963 57.508 1.00 253.41 ? 143 GLU A OE1 1 ATOM 943 O OE2 . GLU A 1 143 ? -40.162 -44.454 58.931 1.00 230.18 ? 143 GLU A OE2 1 ATOM 944 N N . ASN A 1 144 ? -45.672 -44.833 59.124 1.00 126.14 ? 144 ASN A N 1 ATOM 945 C CA . ASN A 1 144 ? -46.057 -44.622 60.529 1.00 127.74 ? 144 ASN A CA 1 ATOM 946 C C . ASN A 1 144 ? -46.629 -45.870 61.217 1.00 129.40 ? 144 ASN A C 1 ATOM 947 O O . ASN A 1 144 ? -46.747 -45.904 62.464 1.00 115.70 ? 144 ASN A O 1 ATOM 948 C CB . ASN A 1 144 ? -47.047 -43.453 60.648 1.00 135.51 ? 144 ASN A CB 1 ATOM 949 C CG . ASN A 1 144 ? -46.372 -42.078 60.639 1.00 139.85 ? 144 ASN A CG 1 ATOM 950 O OD1 . ASN A 1 144 ? -45.758 -41.663 61.627 1.00 140.26 ? 144 ASN A OD1 1 ATOM 951 N ND2 . ASN A 1 144 ? -46.528 -41.345 59.534 1.00 138.10 ? 144 ASN A ND2 1 ATOM 952 N N . GLY A 1 145 ? -46.937 -46.882 60.388 1.00 131.96 ? 145 GLY A N 1 ATOM 953 C CA . GLY A 1 145 ? -47.702 -48.088 60.761 1.00 135.90 ? 145 GLY A CA 1 ATOM 954 C C . GLY A 1 145 ? -46.946 -49.266 61.356 1.00 139.47 ? 145 GLY A C 1 ATOM 955 O O . GLY A 1 145 ? -45.727 -49.280 61.310 1.00 148.40 ? 145 GLY A O 1 ATOM 956 N N . PRO A 1 146 ? -47.675 -50.281 61.888 1.00 144.18 ? 146 PRO A N 1 ATOM 957 C CA . PRO A 1 146 ? -47.160 -51.340 62.774 1.00 134.51 ? 146 PRO A CA 1 ATOM 958 C C . PRO A 1 146 ? -46.400 -52.426 62.047 1.00 132.00 ? 146 PRO A C 1 ATOM 959 O O . PRO A 1 146 ? -46.847 -52.941 61.018 1.00 124.15 ? 146 PRO A O 1 ATOM 960 C CB . PRO A 1 146 ? -48.425 -51.934 63.404 1.00 134.18 ? 146 PRO A CB 1 ATOM 961 C CG . PRO A 1 146 ? -49.574 -51.438 62.584 1.00 149.69 ? 146 PRO A CG 1 ATOM 962 C CD . PRO A 1 146 ? -49.038 -50.606 61.444 1.00 157.93 ? 146 PRO A CD 1 ATOM 963 N N . MET A 1 147 ? -45.253 -52.781 62.602 1.00 138.66 ? 147 MET A N 1 ATOM 964 C CA . MET A 1 147 ? -44.319 -53.610 61.874 1.00 151.43 ? 147 MET A CA 1 ATOM 965 C C . MET A 1 147 ? -44.846 -55.012 61.638 1.00 150.24 ? 147 MET A C 1 ATOM 966 O O . MET A 1 147 ? -45.741 -55.483 62.350 1.00 138.82 ? 147 MET A O 1 ATOM 967 C CB . MET A 1 147 ? -42.945 -53.644 62.552 1.00 161.92 ? 147 MET A CB 1 ATOM 968 C CG . MET A 1 147 ? -41.816 -53.902 61.562 1.00 173.88 ? 147 MET A CG 1 ATOM 969 S SD . MET A 1 147 ? -41.905 -52.735 60.189 1.00 181.86 ? 147 MET A SD 1 ATOM 970 C CE . MET A 1 147 ? -41.358 -51.258 61.022 1.00 171.84 ? 147 MET A CE 1 ATOM 971 N N . ALA A 1 148 ? -44.278 -55.650 60.612 1.00 159.78 ? 148 ALA A N 1 ATOM 972 C CA . ALA A 1 148 ? -44.541 -57.036 60.278 1.00 152.10 ? 148 ALA A CA 1 ATOM 973 C C . ALA A 1 148 ? -45.012 -57.784 61.542 1.00 135.38 ? 148 ALA A C 1 ATOM 974 O O . ALA A 1 148 ? -46.190 -58.075 61.684 1.00 131.25 ? 148 ALA A O 1 ATOM 975 C CB . ALA A 1 148 ? -43.302 -57.683 59.621 1.00 149.83 ? 148 ALA A CB 1 ATOM 976 N N . SER A 1 149 ? -44.131 -58.020 62.499 1.00 124.10 ? 149 SER A N 1 ATOM 977 C CA . SER A 1 149 ? -44.506 -58.909 63.569 1.00 124.30 ? 149 SER A CA 1 ATOM 978 C C . SER A 1 149 ? -44.694 -58.272 64.950 1.00 128.11 ? 149 SER A C 1 ATOM 979 O O . SER A 1 149 ? -44.465 -58.901 65.991 1.00 134.96 ? 149 SER A O 1 ATOM 980 C CB . SER A 1 149 ? -43.609 -60.169 63.589 1.00 133.23 ? 149 SER A CB 1 ATOM 981 O OG . SER A 1 149 ? -42.281 -59.918 63.139 1.00 144.70 ? 149 SER A OG 1 ATOM 982 N N . ASP A 1 150 ? -45.142 -57.027 64.986 1.00 131.54 ? 150 ASP A N 1 ATOM 983 C CA . ASP A 1 150 ? -45.598 -56.530 66.279 1.00 147.31 ? 150 ASP A CA 1 ATOM 984 C C . ASP A 1 150 ? -47.129 -56.471 66.322 1.00 152.53 ? 150 ASP A C 1 ATOM 985 O O . ASP A 1 150 ? -47.771 -56.825 65.326 1.00 142.47 ? 150 ASP A O 1 ATOM 986 C CB . ASP A 1 150 ? -44.855 -55.242 66.774 1.00 160.61 ? 150 ASP A CB 1 ATOM 987 C CG . ASP A 1 150 ? -44.888 -54.060 65.785 1.00 162.29 ? 150 ASP A CG 1 ATOM 988 O OD1 . ASP A 1 150 ? -45.695 -54.067 64.827 1.00 173.13 ? 150 ASP A OD1 1 ATOM 989 O OD2 . ASP A 1 150 ? -44.096 -53.099 66.005 1.00 140.72 ? 150 ASP A OD2 1 ATOM 990 N N . PRO A 1 151 ? -47.707 -56.096 67.489 1.00 162.18 ? 151 PRO A N 1 ATOM 991 C CA . PRO A 1 151 ? -49.102 -55.736 67.765 1.00 149.56 ? 151 PRO A CA 1 ATOM 992 C C . PRO A 1 151 ? -50.014 -55.451 66.563 1.00 136.55 ? 151 PRO A C 1 ATOM 993 O O . PRO A 1 151 ? -49.533 -55.212 65.456 1.00 133.24 ? 151 PRO A O 1 ATOM 994 C CB . PRO A 1 151 ? -48.926 -54.454 68.600 1.00 156.41 ? 151 PRO A CB 1 ATOM 995 C CG . PRO A 1 151 ? -47.523 -54.557 69.201 1.00 172.35 ? 151 PRO A CG 1 ATOM 996 C CD . PRO A 1 151 ? -46.916 -55.852 68.709 1.00 168.89 ? 151 PRO A CD 1 ATOM 997 N N . LEU A 1 152 ? -51.326 -55.474 66.782 1.00 133.39 ? 152 LEU A N 1 ATOM 998 C CA . LEU A 1 152 ? -52.265 -55.106 65.715 1.00 136.19 ? 152 LEU A CA 1 ATOM 999 C C . LEU A 1 152 ? -52.517 -53.603 65.645 1.00 137.10 ? 152 LEU A C 1 ATOM 1000 O O . LEU A 1 152 ? -52.802 -53.063 64.562 1.00 128.22 ? 152 LEU A O 1 ATOM 1001 C CB . LEU A 1 152 ? -53.582 -55.840 65.862 1.00 140.93 ? 152 LEU A CB 1 ATOM 1002 C CG . LEU A 1 152 ? -54.041 -56.255 64.469 1.00 145.90 ? 152 LEU A CG 1 ATOM 1003 C CD1 . LEU A 1 152 ? -54.851 -57.534 64.583 1.00 156.62 ? 152 LEU A CD1 1 ATOM 1004 C CD2 . LEU A 1 152 ? -54.793 -55.155 63.714 1.00 147.98 ? 152 LEU A CD2 1 ATOM 1005 N N . CYS A 1 153 ? -52.442 -52.963 66.819 1.00 148.19 ? 153 CYS A N 1 ATOM 1006 C CA . CYS A 1 153 ? -52.309 -51.503 66.974 1.00 143.07 ? 153 CYS A CA 1 ATOM 1007 C C . CYS A 1 153 ? -51.213 -51.098 67.933 1.00 129.25 ? 153 CYS A C 1 ATOM 1008 O O . CYS A 1 153 ? -51.168 -51.518 69.085 1.00 127.84 ? 153 CYS A O 1 ATOM 1009 C CB . CYS A 1 153 ? -53.599 -50.876 67.443 1.00 153.67 ? 153 CYS A CB 1 ATOM 1010 S SG . CYS A 1 153 ? -54.832 -51.050 66.170 1.00 200.87 ? 153 CYS A SG 1 ATOM 1011 N N . LEU A 1 154 ? -50.325 -50.259 67.454 1.00 124.90 ? 154 LEU A N 1 ATOM 1012 C CA . LEU A 1 154 ? -49.263 -49.827 68.293 1.00 127.56 ? 154 LEU A CA 1 ATOM 1013 C C . LEU A 1 154 ? -49.872 -48.832 69.246 1.00 126.51 ? 154 LEU A C 1 ATOM 1014 O O . LEU A 1 154 ? -50.763 -48.039 68.876 1.00 114.47 ? 154 LEU A O 1 ATOM 1015 C CB . LEU A 1 154 ? -48.168 -49.203 67.452 1.00 141.16 ? 154 LEU A CB 1 ATOM 1016 C CG . LEU A 1 154 ? -47.675 -50.120 66.328 1.00 141.50 ? 154 LEU A CG 1 ATOM 1017 C CD1 . LEU A 1 154 ? -46.992 -49.314 65.228 1.00 136.91 ? 154 LEU A CD1 1 ATOM 1018 C CD2 . LEU A 1 154 ? -46.771 -51.217 66.884 1.00 144.84 ? 154 LEU A CD2 1 ATOM 1019 N N . THR A 1 155 ? -49.420 -48.920 70.488 1.00 125.30 ? 155 THR A N 1 ATOM 1020 C CA . THR A 1 155 ? -49.861 -47.992 71.496 1.00 126.11 ? 155 THR A CA 1 ATOM 1021 C C . THR A 1 155 ? -48.928 -46.800 71.520 1.00 134.81 ? 155 THR A C 1 ATOM 1022 O O . THR A 1 155 ? -47.712 -46.947 71.697 1.00 146.86 ? 155 THR A O 1 ATOM 1023 C CB . THR A 1 155 ? -49.996 -48.664 72.870 1.00 121.48 ? 155 THR A CB 1 ATOM 1024 O OG1 . THR A 1 155 ? -51.315 -49.196 72.985 1.00 118.65 ? 155 THR A OG1 1 ATOM 1025 C CG2 . THR A 1 155 ? -49.799 -47.674 73.993 1.00 121.01 ? 155 THR A CG2 1 ATOM 1026 N N . TYR A 1 156 ? -49.526 -45.636 71.270 1.00 133.89 ? 156 TYR A N 1 ATOM 1027 C CA . TYR A 1 156 ? -48.895 -44.334 71.415 1.00 124.64 ? 156 TYR A CA 1 ATOM 1028 C C . TYR A 1 156 ? -49.864 -43.452 72.189 1.00 118.99 ? 156 TYR A C 1 ATOM 1029 O O . TYR A 1 156 ? -50.681 -43.941 72.949 1.00 126.72 ? 156 TYR A O 1 ATOM 1030 C CB . TYR A 1 156 ? -48.661 -43.689 70.050 1.00 131.70 ? 156 TYR A CB 1 ATOM 1031 C CG . TYR A 1 156 ? -47.775 -44.416 69.040 1.00 136.25 ? 156 TYR A CG 1 ATOM 1032 C CD1 . TYR A 1 156 ? -46.492 -44.884 69.367 1.00 139.07 ? 156 TYR A CD1 1 ATOM 1033 C CD2 . TYR A 1 156 ? -48.204 -44.568 67.727 1.00 137.71 ? 156 TYR A CD2 1 ATOM 1034 C CE1 . TYR A 1 156 ? -45.695 -45.514 68.415 1.00 131.72 ? 156 TYR A CE1 1 ATOM 1035 C CE2 . TYR A 1 156 ? -47.415 -45.185 66.774 1.00 136.47 ? 156 TYR A CE2 1 ATOM 1036 C CZ . TYR A 1 156 ? -46.170 -45.653 67.112 1.00 134.92 ? 156 TYR A CZ 1 ATOM 1037 O OH . TYR A 1 156 ? -45.436 -46.257 66.116 1.00 145.13 ? 156 TYR A OH 1 ATOM 1038 N N . SER A 1 157 ? -49.793 -42.148 71.976 1.00 116.03 ? 157 SER A N 1 ATOM 1039 C CA . SER A 1 157 ? -50.691 -41.200 72.635 1.00 124.02 ? 157 SER A CA 1 ATOM 1040 C C . SER A 1 157 ? -50.262 -39.748 72.344 1.00 137.10 ? 157 SER A C 1 ATOM 1041 O O . SER A 1 157 ? -49.196 -39.504 71.767 1.00 136.97 ? 157 SER A O 1 ATOM 1042 C CB . SER A 1 157 ? -50.814 -41.470 74.150 1.00 116.74 ? 157 SER A CB 1 ATOM 1043 O OG . SER A 1 157 ? -49.893 -40.706 74.915 1.00 116.85 ? 157 SER A OG 1 ATOM 1044 N N . TYR A 1 158 ? -51.115 -38.798 72.730 1.00 146.62 ? 158 TYR A N 1 ATOM 1045 C CA . TYR A 1 158 ? -50.924 -37.376 72.433 1.00 130.81 ? 158 TYR A CA 1 ATOM 1046 C C . TYR A 1 158 ? -50.995 -36.574 73.704 1.00 123.53 ? 158 TYR A C 1 ATOM 1047 O O . TYR A 1 158 ? -51.460 -37.072 74.725 1.00 125.01 ? 158 TYR A O 1 ATOM 1048 C CB . TYR A 1 158 ? -51.974 -36.866 71.430 1.00 128.61 ? 158 TYR A CB 1 ATOM 1049 C CG . TYR A 1 158 ? -53.444 -37.054 71.812 1.00 126.46 ? 158 TYR A CG 1 ATOM 1050 C CD1 . TYR A 1 158 ? -54.025 -36.304 72.830 1.00 131.14 ? 158 TYR A CD1 1 ATOM 1051 C CD2 . TYR A 1 158 ? -54.260 -37.952 71.115 1.00 121.48 ? 158 TYR A CD2 1 ATOM 1052 C CE1 . TYR A 1 158 ? -55.363 -36.453 73.155 1.00 136.40 ? 158 TYR A CE1 1 ATOM 1053 C CE2 . TYR A 1 158 ? -55.595 -38.110 71.437 1.00 126.49 ? 158 TYR A CE2 1 ATOM 1054 C CZ . TYR A 1 158 ? -56.142 -37.355 72.455 1.00 136.78 ? 158 TYR A CZ 1 ATOM 1055 O OH . TYR A 1 158 ? -57.469 -37.490 72.793 1.00 147.04 ? 158 TYR A OH 1 ATOM 1056 N N . LEU A 1 159 ? -50.552 -35.328 73.641 1.00 119.94 ? 159 LEU A N 1 ATOM 1057 C CA . LEU A 1 159 ? -50.512 -34.503 74.833 1.00 130.03 ? 159 LEU A CA 1 ATOM 1058 C C . LEU A 1 159 ? -50.253 -33.055 74.511 1.00 138.90 ? 159 LEU A C 1 ATOM 1059 O O . LEU A 1 159 ? -49.924 -32.711 73.378 1.00 143.78 ? 159 LEU A O 1 ATOM 1060 C CB . LEU A 1 159 ? -49.419 -35.000 75.781 1.00 127.86 ? 159 LEU A CB 1 ATOM 1061 C CG . LEU A 1 159 ? -48.029 -35.128 75.171 1.00 121.07 ? 159 LEU A CG 1 ATOM 1062 C CD1 . LEU A 1 159 ? -47.122 -33.989 75.634 1.00 115.93 ? 159 LEU A CD1 1 ATOM 1063 C CD2 . LEU A 1 159 ? -47.487 -36.499 75.558 1.00 123.56 ? 159 LEU A CD2 1 ATOM 1064 N N . SER A 1 160 ? -50.384 -32.217 75.535 1.00 142.25 ? 160 SER A N 1 ATOM 1065 C CA . SER A 1 160 ? -50.025 -30.823 75.433 1.00 138.84 ? 160 SER A CA 1 ATOM 1066 C C . SER A 1 160 ? -48.528 -30.624 75.639 1.00 139.12 ? 160 SER A C 1 ATOM 1067 O O . SER A 1 160 ? -47.946 -30.983 76.674 1.00 128.81 ? 160 SER A O 1 ATOM 1068 C CB . SER A 1 160 ? -50.819 -29.994 76.419 1.00 144.92 ? 160 SER A CB 1 ATOM 1069 O OG . SER A 1 160 ? -50.654 -28.627 76.120 1.00 162.20 ? 160 SER A OG 1 ATOM 1070 N N . HIS A 1 161 ? -47.921 -30.043 74.617 1.00 147.41 ? 161 HIS A N 1 ATOM 1071 C CA . HIS A 1 161 ? -46.494 -29.840 74.575 1.00 158.81 ? 161 HIS A CA 1 ATOM 1072 C C . HIS A 1 161 ? -46.170 -28.336 74.573 1.00 177.71 ? 161 HIS A C 1 ATOM 1073 O O . HIS A 1 161 ? -45.574 -27.790 73.616 1.00 180.63 ? 161 HIS A O 1 ATOM 1074 C CB . HIS A 1 161 ? -45.935 -30.529 73.346 1.00 156.06 ? 161 HIS A CB 1 ATOM 1075 C CG . HIS A 1 161 ? -44.461 -30.726 73.391 1.00 161.16 ? 161 HIS A CG 1 ATOM 1076 N ND1 . HIS A 1 161 ? -43.570 -29.682 73.279 1.00 176.18 ? 161 HIS A ND1 1 ATOM 1077 C CD2 . HIS A 1 161 ? -43.718 -31.848 73.527 1.00 162.82 ? 161 HIS A CD2 1 ATOM 1078 C CE1 . HIS A 1 161 ? -42.337 -30.152 73.350 1.00 182.75 ? 161 HIS A CE1 1 ATOM 1079 N NE2 . HIS A 1 161 ? -42.400 -31.464 73.494 1.00 173.15 ? 161 HIS A NE2 1 ATOM 1080 N N . VAL A 1 162 ? -46.585 -27.678 75.663 1.00 178.56 ? 162 VAL A N 1 ATOM 1081 C CA . VAL A 1 162 ? -46.265 -26.265 75.915 1.00 160.54 ? 162 VAL A CA 1 ATOM 1082 C C . VAL A 1 162 ? -45.649 -25.899 77.270 1.00 157.11 ? 162 VAL A C 1 ATOM 1083 O O . VAL A 1 162 ? -45.034 -24.848 77.360 1.00 173.51 ? 162 VAL A O 1 ATOM 1084 C CB . VAL A 1 162 ? -47.434 -25.302 75.629 1.00 153.02 ? 162 VAL A CB 1 ATOM 1085 C CG1 . VAL A 1 162 ? -47.059 -24.395 74.475 1.00 158.66 ? 162 VAL A CG1 1 ATOM 1086 C CG2 . VAL A 1 162 ? -48.735 -26.049 75.379 1.00 140.01 ? 162 VAL A CG2 1 ATOM 1087 N N . ASP A 1 163 ? -45.833 -26.725 78.305 1.00 148.95 ? 163 ASP A N 1 ATOM 1088 C CA . ASP A 1 163 ? -45.124 -26.588 79.599 1.00 159.71 ? 163 ASP A CA 1 ATOM 1089 C C . ASP A 1 163 ? -44.987 -27.988 80.194 1.00 157.66 ? 163 ASP A C 1 ATOM 1090 O O . ASP A 1 163 ? -44.600 -28.144 81.352 1.00 158.60 ? 163 ASP A O 1 ATOM 1091 C CB . ASP A 1 163 ? -45.864 -25.622 80.571 1.00 189.24 ? 163 ASP A CB 1 ATOM 1092 C CG . ASP A 1 163 ? -45.004 -25.166 81.825 1.00 210.18 ? 163 ASP A CG 1 ATOM 1093 O OD1 . ASP A 1 163 ? -44.019 -25.835 82.233 1.00 208.62 ? 163 ASP A OD1 1 ATOM 1094 O OD2 . ASP A 1 163 ? -45.353 -24.117 82.433 1.00 214.26 ? 163 ASP A OD2 1 ATOM 1095 N N . LEU A 1 164 ? -45.291 -29.000 79.375 1.00 157.55 ? 164 LEU A N 1 ATOM 1096 C CA . LEU A 1 164 ? -45.293 -30.416 79.779 1.00 153.34 ? 164 LEU A CA 1 ATOM 1097 C C . LEU A 1 164 ? -45.677 -30.641 81.226 1.00 170.44 ? 164 LEU A C 1 ATOM 1098 O O . LEU A 1 164 ? -46.803 -31.033 81.523 1.00 196.42 ? 164 LEU A O 1 ATOM 1099 C CB . LEU A 1 164 ? -43.946 -31.067 79.528 1.00 130.05 ? 164 LEU A CB 1 ATOM 1100 C CG . LEU A 1 164 ? -43.913 -31.868 78.253 1.00 118.97 ? 164 LEU A CG 1 ATOM 1101 C CD1 . LEU A 1 164 ? -42.452 -31.945 77.896 1.00 125.36 ? 164 LEU A CD1 1 ATOM 1102 C CD2 . LEU A 1 164 ? -44.487 -33.258 78.452 1.00 113.89 ? 164 LEU A CD2 1 ATOM 1103 N N . VAL A 1 165 ? -44.723 -30.398 82.117 1.00 165.54 ? 165 VAL A N 1 ATOM 1104 C CA . VAL A 1 165 ? -44.946 -30.465 83.551 1.00 170.56 ? 165 VAL A CA 1 ATOM 1105 C C . VAL A 1 165 ? -46.235 -29.745 83.992 1.00 182.34 ? 165 VAL A C 1 ATOM 1106 O O . VAL A 1 165 ? -47.012 -30.286 84.785 1.00 200.34 ? 165 VAL A O 1 ATOM 1107 C CB . VAL A 1 165 ? -43.730 -29.901 84.288 1.00 163.73 ? 165 VAL A CB 1 ATOM 1108 C CG1 . VAL A 1 165 ? -43.667 -30.436 85.714 1.00 168.59 ? 165 VAL A CG1 1 ATOM 1109 C CG2 . VAL A 1 165 ? -42.480 -30.276 83.522 1.00 152.49 ? 165 VAL A CG2 1 ATOM 1110 N N . LYS A 1 166 ? -46.465 -28.540 83.477 1.00 173.45 ? 166 LYS A N 1 ATOM 1111 C CA . LYS A 1 166 ? -47.716 -27.834 83.726 1.00 176.48 ? 166 LYS A CA 1 ATOM 1112 C C . LYS A 1 166 ? -48.877 -28.663 83.161 1.00 179.84 ? 166 LYS A C 1 ATOM 1113 O O . LYS A 1 166 ? -49.844 -28.927 83.876 1.00 197.56 ? 166 LYS A O 1 ATOM 1114 C CB . LYS A 1 166 ? -47.660 -26.442 83.085 1.00 180.39 ? 166 LYS A CB 1 ATOM 1115 C CG . LYS A 1 166 ? -48.744 -25.432 83.436 1.00 166.99 ? 166 LYS A CG 1 ATOM 1116 C CD . LYS A 1 166 ? -48.642 -24.208 82.525 1.00 150.43 ? 166 LYS A CD 1 ATOM 1117 C CE . LYS A 1 166 ? -49.342 -23.052 83.178 1.00 152.19 ? 166 LYS A CE 1 ATOM 1118 N NZ . LYS A 1 166 ? -49.241 -23.223 84.654 1.00 153.82 ? 166 LYS A NZ 1 ATOM 1119 N N . ASP A 1 167 ? -48.739 -29.116 81.907 1.00 174.15 ? 167 ASP A N 1 ATOM 1120 C CA . ASP A 1 167 ? -49.852 -29.679 81.104 1.00 171.31 ? 167 ASP A CA 1 ATOM 1121 C C . ASP A 1 167 ? -50.216 -31.144 81.369 1.00 167.32 ? 167 ASP A C 1 ATOM 1122 O O . ASP A 1 167 ? -51.403 -31.483 81.458 1.00 159.23 ? 167 ASP A O 1 ATOM 1123 C CB . ASP A 1 167 ? -49.585 -29.493 79.604 1.00 170.17 ? 167 ASP A CB 1 ATOM 1124 C CG . ASP A 1 167 ? -49.345 -28.037 79.220 1.00 184.39 ? 167 ASP A CG 1 ATOM 1125 O OD1 . ASP A 1 167 ? -50.178 -27.159 79.559 1.00 185.96 ? 167 ASP A OD1 1 ATOM 1126 O OD2 . ASP A 1 167 ? -48.316 -27.773 78.562 1.00 187.90 ? 167 ASP A OD2 1 ATOM 1127 N N . LEU A 1 168 ? -49.201 -32.007 81.455 1.00 172.58 ? 168 LEU A N 1 ATOM 1128 C CA . LEU A 1 168 ? -49.402 -33.424 81.769 1.00 165.08 ? 168 LEU A CA 1 ATOM 1129 C C . LEU A 1 168 ? -50.112 -33.483 83.098 1.00 157.92 ? 168 LEU A C 1 ATOM 1130 O O . LEU A 1 168 ? -51.246 -33.968 83.176 1.00 148.25 ? 168 LEU A O 1 ATOM 1131 C CB . LEU A 1 168 ? -48.071 -34.202 81.845 1.00 164.51 ? 168 LEU A CB 1 ATOM 1132 C CG . LEU A 1 168 ? -47.182 -34.392 80.598 1.00 177.61 ? 168 LEU A CG 1 ATOM 1133 C CD1 . LEU A 1 168 ? -45.954 -35.256 80.896 1.00 184.93 ? 168 LEU A CD1 1 ATOM 1134 C CD2 . LEU A 1 168 ? -47.946 -34.928 79.386 1.00 167.56 ? 168 LEU A CD2 1 ATOM 1135 N N . ASN A 1 169 ? -49.449 -32.918 84.113 1.00 154.61 ? 169 ASN A N 1 ATOM 1136 C CA . ASN A 1 169 ? -49.865 -32.994 85.515 1.00 154.95 ? 169 ASN A CA 1 ATOM 1137 C C . ASN A 1 169 ? -51.274 -32.502 85.747 1.00 154.59 ? 169 ASN A C 1 ATOM 1138 O O . ASN A 1 169 ? -51.957 -32.999 86.639 1.00 158.34 ? 169 ASN A O 1 ATOM 1139 C CB . ASN A 1 169 ? -48.889 -32.245 86.432 1.00 157.11 ? 169 ASN A CB 1 ATOM 1140 C CG . ASN A 1 169 ? -47.593 -33.009 86.669 1.00 163.20 ? 169 ASN A CG 1 ATOM 1141 O OD1 . ASN A 1 169 ? -47.163 -33.182 87.807 1.00 156.11 ? 169 ASN A OD1 1 ATOM 1142 N ND2 . ASN A 1 169 ? -46.958 -33.464 85.588 1.00 171.58 ? 169 ASN A ND2 1 ATOM 1143 N N . SER A 1 170 ? -51.703 -31.536 84.936 1.00 156.03 ? 170 SER A N 1 ATOM 1144 C CA . SER A 1 170 ? -53.066 -31.006 85.011 1.00 162.49 ? 170 SER A CA 1 ATOM 1145 C C . SER A 1 170 ? -54.103 -31.968 84.398 1.00 165.38 ? 170 SER A C 1 ATOM 1146 O O . SER A 1 170 ? -55.260 -31.994 84.842 1.00 164.46 ? 170 SER A O 1 ATOM 1147 C CB . SER A 1 170 ? -53.155 -29.607 84.376 1.00 162.37 ? 170 SER A CB 1 ATOM 1148 O OG . SER A 1 170 ? -52.546 -28.608 85.188 1.00 157.53 ? 170 SER A OG 1 ATOM 1149 N N . GLY A 1 171 ? -53.696 -32.748 83.387 1.00 162.47 ? 171 GLY A N 1 ATOM 1150 C CA . GLY A 1 171 ? -54.547 -33.833 82.853 1.00 161.70 ? 171 GLY A CA 1 ATOM 1151 C C . GLY A 1 171 ? -54.714 -33.965 81.342 1.00 152.88 ? 171 GLY A C 1 ATOM 1152 O O . GLY A 1 171 ? -55.792 -34.362 80.834 1.00 141.03 ? 171 GLY A O 1 ATOM 1153 N N . LEU A 1 172 ? -53.648 -33.662 80.614 1.00 143.57 ? 172 LEU A N 1 ATOM 1154 C CA . LEU A 1 172 ? -53.773 -33.613 79.171 1.00 143.12 ? 172 LEU A CA 1 ATOM 1155 C C . LEU A 1 172 ? -52.995 -34.751 78.520 1.00 139.07 ? 172 LEU A C 1 ATOM 1156 O O . LEU A 1 172 ? -51.836 -34.597 78.131 1.00 140.11 ? 172 LEU A O 1 ATOM 1157 C CB . LEU A 1 172 ? -53.404 -32.218 78.630 1.00 142.36 ? 172 LEU A CB 1 ATOM 1158 C CG . LEU A 1 172 ? -54.251 -31.019 79.117 1.00 137.64 ? 172 LEU A CG 1 ATOM 1159 C CD1 . LEU A 1 172 ? -53.342 -29.820 79.342 1.00 135.93 ? 172 LEU A CD1 1 ATOM 1160 C CD2 . LEU A 1 172 ? -55.452 -30.657 78.232 1.00 127.91 ? 172 LEU A CD2 1 ATOM 1161 N N . ILE A 1 173 ? -53.652 -35.906 78.448 1.00 138.82 ? 173 ILE A N 1 ATOM 1162 C CA . ILE A 1 173 ? -53.146 -37.069 77.711 1.00 134.47 ? 173 ILE A CA 1 ATOM 1163 C C . ILE A 1 173 ? -54.282 -37.975 77.223 1.00 135.26 ? 173 ILE A C 1 ATOM 1164 O O . ILE A 1 173 ? -55.030 -38.555 78.019 1.00 132.38 ? 173 ILE A O 1 ATOM 1165 C CB . ILE A 1 173 ? -52.057 -37.864 78.486 1.00 128.17 ? 173 ILE A CB 1 ATOM 1166 C CG1 . ILE A 1 173 ? -51.476 -38.975 77.597 1.00 131.54 ? 173 ILE A CG1 1 ATOM 1167 C CG2 . ILE A 1 173 ? -52.592 -38.407 79.804 1.00 117.55 ? 173 ILE A CG2 1 ATOM 1168 C CD1 . ILE A 1 173 ? -50.014 -39.300 77.854 1.00 141.44 ? 173 ILE A CD1 1 ATOM 1169 N N . GLY A 1 174 ? -54.408 -38.067 75.900 1.00 134.35 ? 174 GLY A N 1 ATOM 1170 C CA . GLY A 1 174 ? -55.369 -38.959 75.268 1.00 130.70 ? 174 GLY A CA 1 ATOM 1171 C C . GLY A 1 174 ? -54.640 -40.141 74.676 1.00 126.25 ? 174 GLY A C 1 ATOM 1172 O O . GLY A 1 174 ? -53.446 -40.070 74.410 1.00 118.57 ? 174 GLY A O 1 ATOM 1173 N N . ALA A 1 175 ? -55.356 -41.240 74.491 1.00 131.37 ? 175 ALA A N 1 ATOM 1174 C CA . ALA A 1 175 ? -54.748 -42.449 73.966 1.00 134.12 ? 175 ALA A CA 1 ATOM 1175 C C . ALA A 1 175 ? -54.809 -42.432 72.437 1.00 140.67 ? 175 ALA A C 1 ATOM 1176 O O . ALA A 1 175 ? -55.890 -42.308 71.854 1.00 152.01 ? 175 ALA A O 1 ATOM 1177 C CB . ALA A 1 175 ? -55.455 -43.671 74.531 1.00 128.40 ? 175 ALA A CB 1 ATOM 1178 N N . LEU A 1 176 ? -53.653 -42.533 71.784 1.00 129.46 ? 176 LEU A N 1 ATOM 1179 C CA . LEU A 1 176 ? -53.625 -42.526 70.326 1.00 120.48 ? 176 LEU A CA 1 ATOM 1180 C C . LEU A 1 176 ? -53.223 -43.867 69.765 1.00 116.43 ? 176 LEU A C 1 ATOM 1181 O O . LEU A 1 176 ? -52.102 -44.346 69.987 1.00 115.00 ? 176 LEU A O 1 ATOM 1182 C CB . LEU A 1 176 ? -52.703 -41.434 69.802 1.00 120.88 ? 176 LEU A CB 1 ATOM 1183 C CG . LEU A 1 176 ? -52.030 -41.552 68.429 1.00 123.21 ? 176 LEU A CG 1 ATOM 1184 C CD1 . LEU A 1 176 ? -52.991 -41.612 67.251 1.00 117.57 ? 176 LEU A CD1 1 ATOM 1185 C CD2 . LEU A 1 176 ? -51.084 -40.377 68.265 1.00 135.23 ? 176 LEU A CD2 1 ATOM 1186 N N . LEU A 1 177 ? -54.136 -44.459 69.009 1.00 109.88 ? 177 LEU A N 1 ATOM 1187 C CA . LEU A 1 177 ? -53.880 -45.772 68.469 1.00 110.20 ? 177 LEU A CA 1 ATOM 1188 C C . LEU A 1 177 ? -53.743 -45.802 66.952 1.00 116.99 ? 177 LEU A C 1 ATOM 1189 O O . LEU A 1 177 ? -54.643 -45.342 66.233 1.00 110.94 ? 177 LEU A O 1 ATOM 1190 C CB . LEU A 1 177 ? -54.965 -46.723 68.936 1.00 104.47 ? 177 LEU A CB 1 ATOM 1191 C CG . LEU A 1 177 ? -54.973 -46.943 70.442 1.00 101.64 ? 177 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 177 ? -55.912 -48.086 70.753 1.00 103.02 ? 177 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 177 ? -53.583 -47.257 70.976 1.00 103.72 ? 177 LEU A CD2 1 ATOM 1194 N N . VAL A 1 178 ? -52.612 -46.347 66.480 1.00 122.13 ? 178 VAL A N 1 ATOM 1195 C CA . VAL A 1 178 ? -52.360 -46.560 65.036 1.00 125.89 ? 178 VAL A CA 1 ATOM 1196 C C . VAL A 1 178 ? -52.396 -48.039 64.642 1.00 120.36 ? 178 VAL A C 1 ATOM 1197 O O . VAL A 1 178 ? -51.890 -48.888 65.378 1.00 119.69 ? 178 VAL A O 1 ATOM 1198 C CB . VAL A 1 178 ? -51.025 -45.949 64.578 1.00 130.40 ? 178 VAL A CB 1 ATOM 1199 C CG1 . VAL A 1 178 ? -49.850 -46.841 64.982 1.00 130.22 ? 178 VAL A CG1 1 ATOM 1200 C CG2 . VAL A 1 178 ? -51.054 -45.713 63.069 1.00 132.41 ? 178 VAL A CG2 1 ATOM 1201 N N . CYS A 1 179 ? -52.953 -48.333 63.467 1.00 115.80 ? 179 CYS A N 1 ATOM 1202 C CA . CYS A 1 179 ? -53.548 -49.636 63.241 1.00 127.01 ? 179 CYS A CA 1 ATOM 1203 C C . CYS A 1 179 ? -53.509 -50.169 61.842 1.00 132.81 ? 179 CYS A C 1 ATOM 1204 O O . CYS A 1 179 ? -53.790 -49.431 60.911 1.00 150.05 ? 179 CYS A O 1 ATOM 1205 C CB . CYS A 1 179 ? -54.997 -49.517 63.633 1.00 143.03 ? 179 CYS A CB 1 ATOM 1206 S SG . CYS A 1 179 ? -55.060 -49.181 65.391 1.00 179.52 ? 179 CYS A SG 1 ATOM 1207 N N . ARG A 1 180 ? -53.231 -51.462 61.690 1.00 128.71 ? 180 ARG A N 1 ATOM 1208 C CA . ARG A 1 180 ? -53.220 -52.065 60.363 1.00 141.99 ? 180 ARG A CA 1 ATOM 1209 C C . ARG A 1 180 ? -54.597 -51.936 59.657 1.00 155.05 ? 180 ARG A C 1 ATOM 1210 O O . ARG A 1 180 ? -55.533 -51.366 60.225 1.00 168.10 ? 180 ARG A O 1 ATOM 1211 C CB . ARG A 1 180 ? -52.738 -53.510 60.446 1.00 153.58 ? 180 ARG A CB 1 ATOM 1212 C CG . ARG A 1 180 ? -51.824 -53.923 59.293 1.00 180.07 ? 180 ARG A CG 1 ATOM 1213 C CD . ARG A 1 180 ? -51.405 -55.391 59.360 1.00 189.60 ? 180 ARG A CD 1 ATOM 1214 N NE . ARG A 1 180 ? -50.342 -55.673 60.339 1.00 194.07 ? 180 ARG A NE 1 ATOM 1215 C CZ . ARG A 1 180 ? -50.533 -56.081 61.599 1.00 190.43 ? 180 ARG A CZ 1 ATOM 1216 N NH1 . ARG A 1 180 ? -51.753 -56.255 62.084 1.00 194.28 ? 180 ARG A NH1 1 ATOM 1217 N NH2 . ARG A 1 180 ? -49.495 -56.314 62.390 1.00 191.68 ? 180 ARG A NH2 1 ATOM 1218 N N . GLU A 1 181 ? -54.702 -52.457 58.428 1.00 160.42 ? 181 GLU A N 1 ATOM 1219 C CA . GLU A 1 181 ? -55.929 -52.432 57.586 1.00 163.75 ? 181 GLU A CA 1 ATOM 1220 C C . GLU A 1 181 ? -57.278 -52.907 58.156 1.00 175.62 ? 181 GLU A C 1 ATOM 1221 O O . GLU A 1 181 ? -58.324 -52.562 57.610 1.00 176.92 ? 181 GLU A O 1 ATOM 1222 C CB . GLU A 1 181 ? -55.672 -53.203 56.297 1.00 161.35 ? 181 GLU A CB 1 ATOM 1223 C CG . GLU A 1 181 ? -55.247 -52.310 55.154 1.00 181.22 ? 181 GLU A CG 1 ATOM 1224 C CD . GLU A 1 181 ? -53.950 -51.568 55.423 1.00 190.80 ? 181 GLU A CD 1 ATOM 1225 O OE1 . GLU A 1 181 ? -53.469 -51.607 56.579 1.00 185.08 ? 181 GLU A OE1 1 ATOM 1226 O OE2 . GLU A 1 181 ? -53.408 -50.952 54.469 1.00 202.90 ? 181 GLU A OE2 1 ATOM 1227 N N . GLY A 1 182 ? -57.255 -53.722 59.211 1.00 186.16 ? 182 GLY A N 1 ATOM 1228 C CA . GLY A 1 182 ? -58.477 -54.195 59.870 1.00 168.68 ? 182 GLY A CA 1 ATOM 1229 C C . GLY A 1 182 ? -58.752 -53.356 61.102 1.00 161.61 ? 182 GLY A C 1 ATOM 1230 O O . GLY A 1 182 ? -57.862 -53.186 61.948 1.00 131.05 ? 182 GLY A O 1 ATOM 1231 N N . SER A 1 183 ? -59.985 -52.841 61.192 1.00 180.45 ? 183 SER A N 1 ATOM 1232 C CA . SER A 1 183 ? -60.378 -51.829 62.194 1.00 191.01 ? 183 SER A CA 1 ATOM 1233 C C . SER A 1 183 ? -61.906 -51.627 62.357 1.00 210.25 ? 183 SER A C 1 ATOM 1234 O O . SER A 1 183 ? -62.668 -51.854 61.421 1.00 197.58 ? 183 SER A O 1 ATOM 1235 C CB . SER A 1 183 ? -59.700 -50.488 61.873 1.00 175.89 ? 183 SER A CB 1 ATOM 1236 O OG . SER A 1 183 ? -60.158 -49.449 62.715 1.00 154.61 ? 183 SER A OG 1 ATOM 1237 N N . LEU A 1 184 ? -62.316 -51.167 63.551 1.00 251.17 ? 184 LEU A N 1 ATOM 1238 C CA . LEU A 1 184 ? -63.740 -50.977 63.979 1.00 276.91 ? 184 LEU A CA 1 ATOM 1239 C C . LEU A 1 184 ? -64.511 -49.932 63.125 1.00 306.70 ? 184 LEU A C 1 ATOM 1240 O O . LEU A 1 184 ? -65.739 -49.812 63.247 1.00 353.62 ? 184 LEU A O 1 ATOM 1241 C CB . LEU A 1 184 ? -63.824 -50.674 65.520 1.00 235.64 ? 184 LEU A CB 1 ATOM 1242 C CG . LEU A 1 184 ? -64.979 -50.859 66.554 1.00 204.04 ? 184 LEU A CG 1 ATOM 1243 C CD1 . LEU A 1 184 ? -65.701 -52.207 66.481 1.00 199.58 ? 184 LEU A CD1 1 ATOM 1244 C CD2 . LEU A 1 184 ? -64.500 -50.594 67.988 1.00 172.63 ? 184 LEU A CD2 1 ATOM 1245 N N . ALA A 1 185 ? -63.790 -49.203 62.262 1.00 293.59 ? 185 ALA A N 1 ATOM 1246 C CA . ALA A 1 185 ? -64.392 -48.264 61.294 1.00 281.94 ? 185 ALA A CA 1 ATOM 1247 C C . ALA A 1 185 ? -64.131 -48.672 59.836 1.00 284.17 ? 185 ALA A C 1 ATOM 1248 O O . ALA A 1 185 ? -64.459 -47.928 58.907 1.00 275.98 ? 185 ALA A O 1 ATOM 1249 C CB . ALA A 1 185 ? -63.913 -46.842 61.547 1.00 257.33 ? 185 ALA A CB 1 ATOM 1250 N N . LYS A 1 186 ? -63.522 -49.848 59.669 1.00 289.17 ? 186 LYS A N 1 ATOM 1251 C CA . LYS A 1 186 ? -63.327 -50.541 58.383 1.00 296.76 ? 186 LYS A CA 1 ATOM 1252 C C . LYS A 1 186 ? -62.830 -51.964 58.696 1.00 294.15 ? 186 LYS A C 1 ATOM 1253 O O . LYS A 1 186 ? -61.643 -52.160 58.987 1.00 297.96 ? 186 LYS A O 1 ATOM 1254 C CB . LYS A 1 186 ? -62.327 -49.804 57.468 1.00 282.69 ? 186 LYS A CB 1 ATOM 1255 C CG . LYS A 1 186 ? -62.931 -49.099 56.253 1.00 255.30 ? 186 LYS A CG 1 ATOM 1256 C CD . LYS A 1 186 ? -61.856 -48.659 55.265 1.00 234.36 ? 186 LYS A CD 1 ATOM 1257 C CE . LYS A 1 186 ? -61.037 -47.502 55.820 1.00 228.97 ? 186 LYS A CE 1 ATOM 1258 N NZ . LYS A 1 186 ? -59.691 -47.365 55.193 1.00 227.31 ? 186 LYS A NZ 1 ATOM 1259 N N . GLU A 1 187 ? -63.743 -52.939 58.644 1.00 281.56 ? 187 GLU A N 1 ATOM 1260 C CA . GLU A 1 187 ? -63.512 -54.322 59.110 1.00 260.03 ? 187 GLU A CA 1 ATOM 1261 C C . GLU A 1 187 ? -64.135 -54.436 60.502 1.00 252.41 ? 187 GLU A C 1 ATOM 1262 O O . GLU A 1 187 ? -63.431 -54.501 61.515 1.00 243.38 ? 187 GLU A O 1 ATOM 1263 C CB . GLU A 1 187 ? -62.017 -54.696 59.102 1.00 248.74 ? 187 GLU A CB 1 ATOM 1264 C CG . GLU A 1 187 ? -61.695 -56.179 59.228 1.00 249.46 ? 187 GLU A CG 1 ATOM 1265 C CD . GLU A 1 187 ? -61.608 -56.659 60.669 1.00 247.41 ? 187 GLU A CD 1 ATOM 1266 O OE1 . GLU A 1 187 ? -61.077 -55.924 61.536 1.00 242.93 ? 187 GLU A OE1 1 ATOM 1267 O OE2 . GLU A 1 187 ? -62.068 -57.787 60.937 1.00 239.87 ? 187 GLU A OE2 1 ATOM 1268 N N . LYS A 1 188 ? -65.469 -54.449 60.528 1.00 254.21 ? 188 LYS A N 1 ATOM 1269 C CA . LYS A 1 188 ? -66.266 -54.299 61.761 1.00 252.11 ? 188 LYS A CA 1 ATOM 1270 C C . LYS A 1 188 ? -66.145 -55.448 62.800 1.00 259.88 ? 188 LYS A C 1 ATOM 1271 O O . LYS A 1 188 ? -66.341 -55.205 64.005 1.00 244.16 ? 188 LYS A O 1 ATOM 1272 C CB . LYS A 1 188 ? -67.750 -54.032 61.417 1.00 245.63 ? 188 LYS A CB 1 ATOM 1273 C CG . LYS A 1 188 ? -68.044 -52.855 60.477 1.00 230.13 ? 188 LYS A CG 1 ATOM 1274 C CD . LYS A 1 188 ? -68.271 -51.529 61.197 1.00 220.72 ? 188 LYS A CD 1 ATOM 1275 C CE . LYS A 1 188 ? -69.395 -51.594 62.225 1.00 220.36 ? 188 LYS A CE 1 ATOM 1276 N NZ . LYS A 1 188 ? -68.963 -52.183 63.529 1.00 206.84 ? 188 LYS A NZ 1 ATOM 1277 N N . THR A 1 189 ? -65.816 -56.669 62.333 1.00 270.70 ? 189 THR A N 1 ATOM 1278 C CA . THR A 1 189 ? -65.765 -57.908 63.178 1.00 253.46 ? 189 THR A CA 1 ATOM 1279 C C . THR A 1 189 ? -64.533 -58.061 64.078 1.00 271.81 ? 189 THR A C 1 ATOM 1280 O O . THR A 1 189 ? -64.379 -59.097 64.753 1.00 261.60 ? 189 THR A O 1 ATOM 1281 C CB . THR A 1 189 ? -65.962 -59.236 62.380 1.00 222.55 ? 189 THR A CB 1 ATOM 1282 O OG1 . THR A 1 189 ? -65.945 -60.350 63.287 1.00 184.63 ? 189 THR A OG1 1 ATOM 1283 C CG2 . THR A 1 189 ? -64.863 -59.437 61.338 1.00 210.16 ? 189 THR A CG2 1 ATOM 1284 N N . GLN A 1 190 ? -63.656 -57.053 64.068 1.00 281.52 ? 190 GLN A N 1 ATOM 1285 C CA . GLN A 1 190 ? -62.661 -56.930 65.119 1.00 260.25 ? 190 GLN A CA 1 ATOM 1286 C C . GLN A 1 190 ? -63.505 -56.983 66.393 1.00 257.74 ? 190 GLN A C 1 ATOM 1287 O O . GLN A 1 190 ? -64.340 -56.101 66.668 1.00 240.20 ? 190 GLN A O 1 ATOM 1288 C CB . GLN A 1 190 ? -61.802 -55.655 64.979 1.00 234.15 ? 190 GLN A CB 1 ATOM 1289 C CG . GLN A 1 190 ? -62.398 -54.370 65.547 1.00 242.98 ? 190 GLN A CG 1 ATOM 1290 C CD . GLN A 1 190 ? -62.083 -54.149 67.027 1.00 244.64 ? 190 GLN A CD 1 ATOM 1291 O OE1 . GLN A 1 190 ? -60.947 -54.337 67.465 1.00 235.96 ? 190 GLN A OE1 1 ATOM 1292 N NE2 . GLN A 1 190 ? -63.093 -53.734 67.800 1.00 238.80 ? 190 GLN A NE2 1 ATOM 1293 N N . THR A 1 191 ? -63.344 -58.087 67.109 1.00 246.74 ? 191 THR A N 1 ATOM 1294 C CA . THR A 1 191 ? -64.169 -58.376 68.266 1.00 226.59 ? 191 THR A CA 1 ATOM 1295 C C . THR A 1 191 ? -63.295 -58.628 69.518 1.00 237.31 ? 191 THR A C 1 ATOM 1296 O O . THR A 1 191 ? -63.753 -59.220 70.505 1.00 248.50 ? 191 THR A O 1 ATOM 1297 C CB . THR A 1 191 ? -65.189 -59.499 67.942 1.00 202.31 ? 191 THR A CB 1 ATOM 1298 O OG1 . THR A 1 191 ? -66.080 -59.670 69.047 1.00 190.04 ? 191 THR A OG1 1 ATOM 1299 C CG2 . THR A 1 191 ? -64.495 -60.830 67.579 1.00 187.23 ? 191 THR A CG2 1 ATOM 1300 N N . LEU A 1 192 ? -62.047 -58.134 69.459 1.00 226.05 ? 192 LEU A N 1 ATOM 1301 C CA . LEU A 1 192 ? -61.057 -58.236 70.554 1.00 206.51 ? 192 LEU A CA 1 ATOM 1302 C C . LEU A 1 192 ? -61.426 -57.408 71.796 1.00 206.31 ? 192 LEU A C 1 ATOM 1303 O O . LEU A 1 192 ? -62.042 -56.345 71.685 1.00 201.98 ? 192 LEU A O 1 ATOM 1304 C CB . LEU A 1 192 ? -59.605 -57.942 70.075 1.00 196.23 ? 192 LEU A CB 1 ATOM 1305 C CG . LEU A 1 192 ? -59.133 -56.789 69.157 1.00 212.00 ? 192 LEU A CG 1 ATOM 1306 C CD1 . LEU A 1 192 ? -57.674 -56.353 69.384 1.00 203.44 ? 192 LEU A CD1 1 ATOM 1307 C CD2 . LEU A 1 192 ? -59.352 -57.149 67.693 1.00 225.23 ? 192 LEU A CD2 1 ATOM 1308 N N . HIS A 1 193 ? -61.045 -57.904 72.973 1.00 203.91 ? 193 HIS A N 1 ATOM 1309 C CA . HIS A 1 193 ? -61.432 -57.279 74.235 1.00 181.45 ? 193 HIS A CA 1 ATOM 1310 C C . HIS A 1 193 ? -60.362 -56.352 74.807 1.00 165.17 ? 193 HIS A C 1 ATOM 1311 O O . HIS A 1 193 ? -59.382 -56.831 75.401 1.00 161.49 ? 193 HIS A O 1 ATOM 1312 C CB . HIS A 1 193 ? -61.789 -58.352 75.248 1.00 174.41 ? 193 HIS A CB 1 ATOM 1313 C CG . HIS A 1 193 ? -63.100 -58.107 75.889 1.00 172.80 ? 193 HIS A CG 1 ATOM 1314 N ND1 . HIS A 1 193 ? -63.969 -59.122 76.210 1.00 179.03 ? 193 HIS A ND1 1 ATOM 1315 C CD2 . HIS A 1 193 ? -63.724 -56.949 76.206 1.00 173.34 ? 193 HIS A CD2 1 ATOM 1316 C CE1 . HIS A 1 193 ? -65.063 -58.598 76.736 1.00 198.20 ? 193 HIS A CE1 1 ATOM 1317 N NE2 . HIS A 1 193 ? -64.939 -57.282 76.746 1.00 196.46 ? 193 HIS A NE2 1 ATOM 1318 N N . LYS A 1 194 ? -60.550 -55.036 74.646 1.00 143.94 ? 194 LYS A N 1 ATOM 1319 C CA . LYS A 1 194 ? -59.440 -54.090 74.901 1.00 135.37 ? 194 LYS A CA 1 ATOM 1320 C C . LYS A 1 194 ? -59.671 -52.778 75.690 1.00 134.66 ? 194 LYS A C 1 ATOM 1321 O O . LYS A 1 194 ? -60.508 -51.934 75.346 1.00 140.57 ? 194 LYS A O 1 ATOM 1322 C CB . LYS A 1 194 ? -58.631 -53.825 73.614 1.00 130.74 ? 194 LYS A CB 1 ATOM 1323 C CG . LYS A 1 194 ? -59.249 -52.875 72.601 1.00 136.59 ? 194 LYS A CG 1 ATOM 1324 C CD . LYS A 1 194 ? -58.347 -52.674 71.386 1.00 134.72 ? 194 LYS A CD 1 ATOM 1325 C CE . LYS A 1 194 ? -58.984 -51.705 70.402 1.00 131.13 ? 194 LYS A CE 1 ATOM 1326 N NZ . LYS A 1 194 ? -58.751 -52.258 69.050 1.00 129.13 ? 194 LYS A NZ 1 ATOM 1327 N N . PHE A 1 195 ? -58.865 -52.621 76.735 1.00 128.59 ? 195 PHE A N 1 ATOM 1328 C CA . PHE A 1 195 ? -58.883 -51.449 77.594 1.00 126.85 ? 195 PHE A CA 1 ATOM 1329 C C . PHE A 1 195 ? -57.606 -50.631 77.435 1.00 120.24 ? 195 PHE A C 1 ATOM 1330 O O . PHE A 1 195 ? -56.590 -51.112 76.937 1.00 118.85 ? 195 PHE A O 1 ATOM 1331 C CB . PHE A 1 195 ? -59.064 -51.874 79.060 1.00 137.02 ? 195 PHE A CB 1 ATOM 1332 C CG . PHE A 1 195 ? -60.368 -52.576 79.330 1.00 145.97 ? 195 PHE A CG 1 ATOM 1333 C CD1 . PHE A 1 195 ? -61.521 -51.846 79.633 1.00 153.04 ? 195 PHE A CD1 1 ATOM 1334 C CD2 . PHE A 1 195 ? -60.453 -53.963 79.269 1.00 143.84 ? 195 PHE A CD2 1 ATOM 1335 C CE1 . PHE A 1 195 ? -62.733 -52.487 79.871 1.00 158.80 ? 195 PHE A CE1 1 ATOM 1336 C CE2 . PHE A 1 195 ? -61.660 -54.607 79.506 1.00 152.87 ? 195 PHE A CE2 1 ATOM 1337 C CZ . PHE A 1 195 ? -62.802 -53.869 79.808 1.00 160.31 ? 195 PHE A CZ 1 ATOM 1338 N N . ILE A 1 196 ? -57.666 -49.386 77.879 1.00 121.18 ? 196 ILE A N 1 ATOM 1339 C CA . ILE A 1 196 ? -56.545 -48.459 77.763 1.00 120.78 ? 196 ILE A CA 1 ATOM 1340 C C . ILE A 1 196 ? -56.016 -48.142 79.178 1.00 121.60 ? 196 ILE A C 1 ATOM 1341 O O . ILE A 1 196 ? -56.569 -47.321 79.905 1.00 120.33 ? 196 ILE A O 1 ATOM 1342 C CB . ILE A 1 196 ? -56.945 -47.178 76.943 1.00 121.83 ? 196 ILE A CB 1 ATOM 1343 C CG1 . ILE A 1 196 ? -57.378 -47.524 75.481 1.00 120.22 ? 196 ILE A CG1 1 ATOM 1344 C CG2 . ILE A 1 196 ? -55.840 -46.111 76.987 1.00 108.82 ? 196 ILE A CG2 1 ATOM 1345 C CD1 . ILE A 1 196 ? -58.855 -47.835 75.219 1.00 113.41 ? 196 ILE A CD1 1 ATOM 1346 N N . LEU A 1 197 ? -54.955 -48.823 79.586 1.00 131.50 ? 197 LEU A N 1 ATOM 1347 C CA . LEU A 1 197 ? -54.392 -48.564 80.912 1.00 140.04 ? 197 LEU A CA 1 ATOM 1348 C C . LEU A 1 197 ? -53.387 -47.409 80.943 1.00 136.68 ? 197 LEU A C 1 ATOM 1349 O O . LEU A 1 197 ? -52.341 -47.457 80.301 1.00 144.40 ? 197 LEU A O 1 ATOM 1350 C CB . LEU A 1 197 ? -53.820 -49.845 81.544 1.00 136.14 ? 197 LEU A CB 1 ATOM 1351 C CG . LEU A 1 197 ? -54.859 -50.494 82.461 1.00 136.37 ? 197 LEU A CG 1 ATOM 1352 C CD1 . LEU A 1 197 ? -55.733 -51.477 81.701 1.00 135.73 ? 197 LEU A CD1 1 ATOM 1353 C CD2 . LEU A 1 197 ? -54.201 -51.161 83.650 1.00 127.84 ? 197 LEU A CD2 1 ATOM 1354 N N . LEU A 1 198 ? -53.731 -46.366 81.688 1.00 127.73 ? 198 LEU A N 1 ATOM 1355 C CA . LEU A 1 198 ? -52.843 -45.239 81.898 1.00 123.63 ? 198 LEU A CA 1 ATOM 1356 C C . LEU A 1 198 ? -52.351 -45.220 83.338 1.00 125.85 ? 198 LEU A C 1 ATOM 1357 O O . LEU A 1 198 ? -53.123 -44.930 84.252 1.00 137.88 ? 198 LEU A O 1 ATOM 1358 C CB . LEU A 1 198 ? -53.582 -43.939 81.606 1.00 118.98 ? 198 LEU A CB 1 ATOM 1359 C CG . LEU A 1 198 ? -52.808 -42.625 81.449 1.00 114.25 ? 198 LEU A CG 1 ATOM 1360 C CD1 . LEU A 1 198 ? -53.743 -41.521 81.879 1.00 118.27 ? 198 LEU A CD1 1 ATOM 1361 C CD2 . LEU A 1 198 ? -51.508 -42.526 82.234 1.00 108.46 ? 198 LEU A CD2 1 ATOM 1362 N N . PHE A 1 199 ? -51.067 -45.492 83.538 1.00 120.37 ? 199 PHE A N 1 ATOM 1363 C CA . PHE A 1 199 ? -50.502 -45.486 84.882 1.00 132.89 ? 199 PHE A CA 1 ATOM 1364 C C . PHE A 1 199 ? -49.901 -44.119 85.260 1.00 145.81 ? 199 PHE A C 1 ATOM 1365 O O . PHE A 1 199 ? -48.688 -43.911 85.182 1.00 144.45 ? 199 PHE A O 1 ATOM 1366 C CB . PHE A 1 199 ? -49.486 -46.619 85.032 1.00 129.26 ? 199 PHE A CB 1 ATOM 1367 C CG . PHE A 1 199 ? -50.094 -47.994 84.989 1.00 129.45 ? 199 PHE A CG 1 ATOM 1368 C CD1 . PHE A 1 199 ? -50.371 -48.617 83.776 1.00 133.40 ? 199 PHE A CD1 1 ATOM 1369 C CD2 . PHE A 1 199 ? -50.376 -48.676 86.161 1.00 132.00 ? 199 PHE A CD2 1 ATOM 1370 C CE1 . PHE A 1 199 ? -50.925 -49.892 83.734 1.00 132.35 ? 199 PHE A CE1 1 ATOM 1371 C CE2 . PHE A 1 199 ? -50.934 -49.947 86.125 1.00 132.43 ? 199 PHE A CE2 1 ATOM 1372 C CZ . PHE A 1 199 ? -51.203 -50.558 84.912 1.00 129.43 ? 199 PHE A CZ 1 ATOM 1373 N N . ALA A 1 200 ? -50.762 -43.201 85.704 1.00 158.77 ? 200 ALA A N 1 ATOM 1374 C CA . ALA A 1 200 ? -50.398 -41.782 85.897 1.00 163.20 ? 200 ALA A CA 1 ATOM 1375 C C . ALA A 1 200 ? -49.954 -41.331 87.308 1.00 172.03 ? 200 ALA A C 1 ATOM 1376 O O . ALA A 1 200 ? -50.697 -41.450 88.288 1.00 175.29 ? 200 ALA A O 1 ATOM 1377 C CB . ALA A 1 200 ? -51.527 -40.888 85.401 1.00 155.35 ? 200 ALA A CB 1 ATOM 1378 N N . VAL A 1 201 ? -48.740 -40.791 87.390 1.00 174.62 ? 201 VAL A N 1 ATOM 1379 C CA . VAL A 1 201 ? -48.283 -40.109 88.600 1.00 161.70 ? 201 VAL A CA 1 ATOM 1380 C C . VAL A 1 201 ? -48.583 -38.597 88.451 1.00 158.59 ? 201 VAL A C 1 ATOM 1381 O O . VAL A 1 201 ? -47.771 -37.830 87.921 1.00 150.64 ? 201 VAL A O 1 ATOM 1382 C CB . VAL A 1 201 ? -46.772 -40.365 88.905 1.00 158.36 ? 201 VAL A CB 1 ATOM 1383 C CG1 . VAL A 1 201 ? -46.573 -40.508 90.411 1.00 147.32 ? 201 VAL A CG1 1 ATOM 1384 C CG2 . VAL A 1 201 ? -46.197 -41.575 88.136 1.00 135.22 ? 201 VAL A CG2 1 ATOM 1385 N N . PHE A 1 202 ? -49.768 -38.177 88.885 1.00 160.71 ? 202 PHE A N 1 ATOM 1386 C CA . PHE A 1 202 ? -50.140 -36.756 88.843 1.00 172.06 ? 202 PHE A CA 1 ATOM 1387 C C . PHE A 1 202 ? -49.674 -35.940 90.036 1.00 193.23 ? 202 PHE A C 1 ATOM 1388 O O . PHE A 1 202 ? -50.217 -36.076 91.143 1.00 200.62 ? 202 PHE A O 1 ATOM 1389 C CB . PHE A 1 202 ? -51.642 -36.599 88.737 1.00 168.46 ? 202 PHE A CB 1 ATOM 1390 C CG . PHE A 1 202 ? -52.158 -36.927 87.401 1.00 162.09 ? 202 PHE A CG 1 ATOM 1391 C CD1 . PHE A 1 202 ? -51.583 -36.363 86.284 1.00 159.00 ? 202 PHE A CD1 1 ATOM 1392 C CD2 . PHE A 1 202 ? -53.192 -37.822 87.251 1.00 167.61 ? 202 PHE A CD2 1 ATOM 1393 C CE1 . PHE A 1 202 ? -52.050 -36.672 85.024 1.00 158.78 ? 202 PHE A CE1 1 ATOM 1394 C CE2 . PHE A 1 202 ? -53.667 -38.137 85.995 1.00 157.59 ? 202 PHE A CE2 1 ATOM 1395 C CZ . PHE A 1 202 ? -53.095 -37.560 84.881 1.00 152.10 ? 202 PHE A CZ 1 ATOM 1396 N N . ASP A 1 203 ? -48.684 -35.080 89.805 1.00 194.85 ? 203 ASP A N 1 ATOM 1397 C CA . ASP A 1 203 ? -48.230 -34.145 90.832 1.00 190.41 ? 203 ASP A CA 1 ATOM 1398 C C . ASP A 1 203 ? -49.222 -33.013 90.802 1.00 189.32 ? 203 ASP A C 1 ATOM 1399 O O . ASP A 1 203 ? -49.474 -32.456 89.733 1.00 207.60 ? 203 ASP A O 1 ATOM 1400 C CB . ASP A 1 203 ? -46.824 -33.617 90.521 1.00 191.56 ? 203 ASP A CB 1 ATOM 1401 C CG . ASP A 1 203 ? -46.185 -32.897 91.700 1.00 193.65 ? 203 ASP A CG 1 ATOM 1402 O OD1 . ASP A 1 203 ? -46.916 -32.329 92.543 1.00 190.75 ? 203 ASP A OD1 1 ATOM 1403 O OD2 . ASP A 1 203 ? -44.935 -32.901 91.775 1.00 196.49 ? 203 ASP A OD2 1 ATOM 1404 N N . GLU A 1 204 ? -49.803 -32.686 91.952 1.00 178.83 ? 204 GLU A N 1 ATOM 1405 C CA . GLU A 1 204 ? -50.824 -31.643 91.986 1.00 174.06 ? 204 GLU A CA 1 ATOM 1406 C C . GLU A 1 204 ? -50.275 -30.291 92.412 1.00 181.87 ? 204 GLU A C 1 ATOM 1407 O O . GLU A 1 204 ? -50.920 -29.262 92.219 1.00 180.54 ? 204 GLU A O 1 ATOM 1408 C CB . GLU A 1 204 ? -52.019 -32.051 92.832 1.00 167.51 ? 204 GLU A CB 1 ATOM 1409 C CG . GLU A 1 204 ? -53.336 -31.594 92.226 1.00 171.97 ? 204 GLU A CG 1 ATOM 1410 C CD . GLU A 1 204 ? -53.524 -32.006 90.769 1.00 167.88 ? 204 GLU A CD 1 ATOM 1411 O OE1 . GLU A 1 204 ? -53.678 -33.232 90.520 1.00 164.22 ? 204 GLU A OE1 1 ATOM 1412 O OE2 . GLU A 1 204 ? -53.526 -31.099 89.884 1.00 162.19 ? 204 GLU A OE2 1 ATOM 1413 N N . GLY A 1 205 ? -49.068 -30.307 92.965 1.00 187.54 ? 205 GLY A N 1 ATOM 1414 C CA . GLY A 1 205 ? -48.320 -29.081 93.207 1.00 190.95 ? 205 GLY A CA 1 ATOM 1415 C C . GLY A 1 205 ? -47.342 -28.746 92.092 1.00 179.93 ? 205 GLY A C 1 ATOM 1416 O O . GLY A 1 205 ? -46.241 -28.267 92.354 1.00 187.61 ? 205 GLY A O 1 ATOM 1417 N N . LYS A 1 206 ? -47.746 -29.006 90.852 1.00 167.48 ? 206 LYS A N 1 ATOM 1418 C CA . LYS A 1 206 ? -46.945 -28.720 89.661 1.00 161.43 ? 206 LYS A CA 1 ATOM 1419 C C . LYS A 1 206 ? -47.925 -28.640 88.499 1.00 158.08 ? 206 LYS A C 1 ATOM 1420 O O . LYS A 1 206 ? -47.809 -29.355 87.500 1.00 146.12 ? 206 LYS A O 1 ATOM 1421 C CB . LYS A 1 206 ? -45.894 -29.815 89.428 1.00 158.93 ? 206 LYS A CB 1 ATOM 1422 C CG . LYS A 1 206 ? -44.669 -29.711 90.326 1.00 164.15 ? 206 LYS A CG 1 ATOM 1423 C CD . LYS A 1 206 ? -43.600 -30.736 89.981 1.00 168.80 ? 206 LYS A CD 1 ATOM 1424 C CE . LYS A 1 206 ? -42.347 -30.511 90.818 1.00 172.74 ? 206 LYS A CE 1 ATOM 1425 N NZ . LYS A 1 206 ? -41.609 -29.269 90.433 1.00 175.49 ? 206 LYS A NZ 1 ATOM 1426 N N . SER A 1 207 ? -48.884 -27.733 88.645 1.00 164.76 ? 207 SER A N 1 ATOM 1427 C CA . SER A 1 207 ? -50.146 -27.818 87.940 1.00 167.84 ? 207 SER A CA 1 ATOM 1428 C C . SER A 1 207 ? -50.475 -26.446 87.388 1.00 169.94 ? 207 SER A C 1 ATOM 1429 O O . SER A 1 207 ? -49.982 -25.995 86.340 1.00 151.37 ? 207 SER A O 1 ATOM 1430 C CB . SER A 1 207 ? -51.209 -28.255 88.980 1.00 170.68 ? 207 SER A CB 1 ATOM 1431 O OG . SER A 1 207 ? -52.525 -28.384 88.461 1.00 170.96 ? 207 SER A OG 1 ATOM 1432 N N . TRP A 1 208 ? -51.384 -25.832 88.119 1.00 185.89 ? 208 TRP A N 1 ATOM 1433 C CA . TRP A 1 208 ? -51.552 -24.418 88.192 1.00 198.93 ? 208 TRP A CA 1 ATOM 1434 C C . TRP A 1 208 ? -51.947 -24.239 89.650 1.00 205.77 ? 208 TRP A C 1 ATOM 1435 O O . TRP A 1 208 ? -52.543 -23.224 90.015 1.00 223.25 ? 208 TRP A O 1 ATOM 1436 C CB . TRP A 1 208 ? -52.626 -23.927 87.221 1.00 200.80 ? 208 TRP A CB 1 ATOM 1437 C CG . TRP A 1 208 ? -53.743 -24.901 86.999 1.00 199.12 ? 208 TRP A CG 1 ATOM 1438 C CD1 . TRP A 1 208 ? -53.819 -25.846 86.016 1.00 190.78 ? 208 TRP A CD1 1 ATOM 1439 C CD2 . TRP A 1 208 ? -54.947 -25.023 87.768 1.00 202.90 ? 208 TRP A CD2 1 ATOM 1440 N NE1 . TRP A 1 208 ? -54.997 -26.547 86.125 1.00 186.69 ? 208 TRP A NE1 1 ATOM 1441 C CE2 . TRP A 1 208 ? -55.707 -26.066 87.190 1.00 192.65 ? 208 TRP A CE2 1 ATOM 1442 C CE3 . TRP A 1 208 ? -55.462 -24.345 88.884 1.00 221.87 ? 208 TRP A CE3 1 ATOM 1443 C CZ2 . TRP A 1 208 ? -56.950 -26.458 87.691 1.00 201.64 ? 208 TRP A CZ2 1 ATOM 1444 C CZ3 . TRP A 1 208 ? -56.705 -24.733 89.387 1.00 233.99 ? 208 TRP A CZ3 1 ATOM 1445 C CH2 . TRP A 1 208 ? -57.433 -25.786 88.789 1.00 227.37 ? 208 TRP A CH2 1 ATOM 1446 N N . HIS A 1 209 ? -51.620 -25.257 90.464 1.00 199.71 ? 209 HIS A N 1 ATOM 1447 C CA . HIS A 1 209 ? -51.658 -25.176 91.938 1.00 220.96 ? 209 HIS A CA 1 ATOM 1448 C C . HIS A 1 209 ? -50.736 -24.005 92.329 1.00 236.58 ? 209 HIS A C 1 ATOM 1449 O O . HIS A 1 209 ? -49.543 -24.007 91.978 1.00 244.97 ? 209 HIS A O 1 ATOM 1450 C CB . HIS A 1 209 ? -51.243 -26.540 92.588 1.00 217.68 ? 209 HIS A CB 1 ATOM 1451 C CG . HIS A 1 209 ? -51.399 -26.635 94.101 1.00 214.88 ? 209 HIS A CG 1 ATOM 1452 N ND1 . HIS A 1 209 ? -51.007 -27.753 94.817 1.00 195.84 ? 209 HIS A ND1 1 ATOM 1453 C CD2 . HIS A 1 209 ? -51.878 -25.761 95.024 1.00 212.70 ? 209 HIS A CD2 1 ATOM 1454 C CE1 . HIS A 1 209 ? -51.240 -27.564 96.103 1.00 193.88 ? 209 HIS A CE1 1 ATOM 1455 N NE2 . HIS A 1 209 ? -51.768 -26.364 96.257 1.00 205.22 ? 209 HIS A NE2 1 ATOM 1456 N N . SER A 1 210 ? -51.319 -22.997 92.996 1.00 235.95 ? 210 SER A N 1 ATOM 1457 C CA . SER A 1 210 ? -50.618 -21.777 93.442 1.00 230.34 ? 210 SER A CA 1 ATOM 1458 C C . SER A 1 210 ? -51.295 -21.152 94.668 1.00 237.00 ? 210 SER A C 1 ATOM 1459 O O . SER A 1 210 ? -51.597 -21.838 95.645 1.00 230.79 ? 210 SER A O 1 ATOM 1460 C CB . SER A 1 210 ? -50.513 -20.742 92.306 1.00 221.53 ? 210 SER A CB 1 ATOM 1461 O OG . SER A 1 210 ? -51.714 -20.003 92.146 1.00 219.70 ? 210 SER A OG 1 ATOM 1462 N N . PRO A 1 229 ? -49.925 -31.528 99.109 1.00 222.93 ? 229 PRO A N 1 ATOM 1463 C CA . PRO A 1 229 ? -50.380 -31.721 97.709 1.00 201.46 ? 229 PRO A CA 1 ATOM 1464 C C . PRO A 1 229 ? -49.827 -32.982 96.931 1.00 175.81 ? 229 PRO A C 1 ATOM 1465 O O . PRO A 1 229 ? -48.613 -33.071 96.784 1.00 164.62 ? 229 PRO A O 1 ATOM 1466 C CB . PRO A 1 229 ? -49.953 -30.387 97.049 1.00 202.52 ? 229 PRO A CB 1 ATOM 1467 C CG . PRO A 1 229 ? -49.840 -29.374 98.199 1.00 205.74 ? 229 PRO A CG 1 ATOM 1468 C CD . PRO A 1 229 ? -49.946 -30.101 99.518 1.00 210.45 ? 229 PRO A CD 1 ATOM 1469 N N . LYS A 1 230 ? -50.679 -33.938 96.475 1.00 170.43 ? 230 LYS A N 1 ATOM 1470 C CA . LYS A 1 230 ? -50.271 -35.012 95.427 1.00 187.14 ? 230 LYS A CA 1 ATOM 1471 C C . LYS A 1 230 ? -51.008 -36.422 95.143 1.00 184.71 ? 230 LYS A C 1 ATOM 1472 O O . LYS A 1 230 ? -50.686 -37.417 95.795 1.00 190.90 ? 230 LYS A O 1 ATOM 1473 C CB . LYS A 1 230 ? -48.745 -35.276 95.502 1.00 178.81 ? 230 LYS A CB 1 ATOM 1474 C CG . LYS A 1 230 ? -48.071 -35.546 94.158 1.00 156.78 ? 230 LYS A CG 1 ATOM 1475 C CD . LYS A 1 230 ? -46.708 -36.175 94.366 1.00 150.05 ? 230 LYS A CD 1 ATOM 1476 C CE . LYS A 1 230 ? -46.848 -37.679 94.377 1.00 151.93 ? 230 LYS A CE 1 ATOM 1477 N NZ . LYS A 1 230 ? -48.199 -38.088 94.862 1.00 149.77 ? 230 LYS A NZ 1 ATOM 1478 N N . MET A 1 231 ? -51.904 -36.523 94.134 1.00 178.83 ? 231 MET A N 1 ATOM 1479 C CA . MET A 1 231 ? -52.474 -37.825 93.631 1.00 165.68 ? 231 MET A CA 1 ATOM 1480 C C . MET A 1 231 ? -51.316 -38.661 93.002 1.00 167.24 ? 231 MET A C 1 ATOM 1481 O O . MET A 1 231 ? -50.181 -38.162 92.994 1.00 151.10 ? 231 MET A O 1 ATOM 1482 C CB . MET A 1 231 ? -53.698 -37.633 92.650 1.00 167.62 ? 231 MET A CB 1 ATOM 1483 C CG . MET A 1 231 ? -55.158 -37.662 93.238 1.00 168.79 ? 231 MET A CG 1 ATOM 1484 S SD . MET A 1 231 ? -56.660 -37.774 92.150 1.00 158.20 ? 231 MET A SD 1 ATOM 1485 C CE . MET A 1 231 ? -56.084 -36.908 90.680 1.00 136.65 ? 231 MET A CE 1 ATOM 1486 N N . HIS A 1 232 ? -51.609 -39.890 92.482 1.00 186.41 ? 232 HIS A N 1 ATOM 1487 C CA . HIS A 1 232 ? -50.633 -41.011 92.120 1.00 166.17 ? 232 HIS A CA 1 ATOM 1488 C C . HIS A 1 232 ? -51.318 -42.313 91.557 1.00 143.98 ? 232 HIS A C 1 ATOM 1489 O O . HIS A 1 232 ? -51.183 -43.385 92.138 1.00 129.97 ? 232 HIS A O 1 ATOM 1490 C CB . HIS A 1 232 ? -49.856 -41.383 93.395 1.00 174.35 ? 232 HIS A CB 1 ATOM 1491 C CG . HIS A 1 232 ? -48.522 -42.029 93.170 1.00 165.87 ? 232 HIS A CG 1 ATOM 1492 N ND1 . HIS A 1 232 ? -47.341 -41.446 93.586 1.00 159.56 ? 232 HIS A ND1 1 ATOM 1493 C CD2 . HIS A 1 232 ? -48.187 -43.237 92.661 1.00 156.63 ? 232 HIS A CD2 1 ATOM 1494 C CE1 . HIS A 1 232 ? -46.335 -42.251 93.310 1.00 154.56 ? 232 HIS A CE1 1 ATOM 1495 N NE2 . HIS A 1 232 ? -46.821 -43.344 92.749 1.00 161.90 ? 232 HIS A NE2 1 ATOM 1496 N N . THR A 1 233 ? -52.003 -42.220 90.413 1.00 143.43 ? 233 THR A N 1 ATOM 1497 C CA . THR A 1 233 ? -53.160 -43.113 90.062 1.00 148.48 ? 233 THR A CA 1 ATOM 1498 C C . THR A 1 233 ? -52.990 -44.236 88.992 1.00 152.10 ? 233 THR A C 1 ATOM 1499 O O . THR A 1 233 ? -51.870 -44.595 88.617 1.00 154.90 ? 233 THR A O 1 ATOM 1500 C CB . THR A 1 233 ? -54.398 -42.271 89.611 1.00 147.41 ? 233 THR A CB 1 ATOM 1501 O OG1 . THR A 1 233 ? -54.751 -42.570 88.249 1.00 137.08 ? 233 THR A OG1 1 ATOM 1502 C CG2 . THR A 1 233 ? -54.156 -40.756 89.742 1.00 147.43 ? 233 THR A CG2 1 ATOM 1503 N N . VAL A 1 234 ? -54.137 -44.781 88.541 1.00 147.53 ? 234 VAL A N 1 ATOM 1504 C CA . VAL A 1 234 ? -54.287 -45.674 87.360 1.00 131.26 ? 234 VAL A CA 1 ATOM 1505 C C . VAL A 1 234 ? -55.537 -45.227 86.592 1.00 123.80 ? 234 VAL A C 1 ATOM 1506 O O . VAL A 1 234 ? -56.640 -45.698 86.850 1.00 115.48 ? 234 VAL A O 1 ATOM 1507 C CB . VAL A 1 234 ? -54.414 -47.190 87.742 1.00 129.77 ? 234 VAL A CB 1 ATOM 1508 C CG1 . VAL A 1 234 ? -54.946 -48.049 86.587 1.00 115.48 ? 234 VAL A CG1 1 ATOM 1509 C CG2 . VAL A 1 234 ? -53.090 -47.744 88.262 1.00 125.09 ? 234 VAL A CG2 1 ATOM 1510 N N . ASN A 1 235 ? -55.361 -44.299 85.661 1.00 127.27 ? 235 ASN A N 1 ATOM 1511 C CA . ASN A 1 235 ? -56.475 -43.803 84.857 1.00 140.02 ? 235 ASN A CA 1 ATOM 1512 C C . ASN A 1 235 ? -57.223 -42.629 85.477 1.00 152.08 ? 235 ASN A C 1 ATOM 1513 O O . ASN A 1 235 ? -58.265 -42.210 84.956 1.00 153.60 ? 235 ASN A O 1 ATOM 1514 C CB . ASN A 1 235 ? -57.469 -44.925 84.551 1.00 141.37 ? 235 ASN A CB 1 ATOM 1515 C CG . ASN A 1 235 ? -57.350 -45.428 83.141 1.00 145.12 ? 235 ASN A CG 1 ATOM 1516 O OD1 . ASN A 1 235 ? -58.299 -45.351 82.369 1.00 154.91 ? 235 ASN A OD1 1 ATOM 1517 N ND2 . ASN A 1 235 ? -56.179 -45.927 82.786 1.00 143.78 ? 235 ASN A ND2 1 ATOM 1518 N N . GLY A 1 236 ? -56.687 -42.101 86.576 1.00 156.70 ? 236 GLY A N 1 ATOM 1519 C CA . GLY A 1 236 ? -57.331 -41.012 87.317 1.00 167.31 ? 236 GLY A CA 1 ATOM 1520 C C . GLY A 1 236 ? -58.036 -41.510 88.569 1.00 181.56 ? 236 GLY A C 1 ATOM 1521 O O . GLY A 1 236 ? -58.494 -40.710 89.410 1.00 187.31 ? 236 GLY A O 1 ATOM 1522 N N . TYR A 1 237 ? -58.119 -42.839 88.689 1.00 176.07 ? 237 TYR A N 1 ATOM 1523 C CA . TYR A 1 237 ? -58.706 -43.482 89.867 1.00 167.42 ? 237 TYR A CA 1 ATOM 1524 C C . TYR A 1 237 ? -57.678 -44.041 90.845 1.00 165.09 ? 237 TYR A C 1 ATOM 1525 O O . TYR A 1 237 ? -56.769 -44.811 90.495 1.00 143.54 ? 237 TYR A O 1 ATOM 1526 C CB . TYR A 1 237 ? -59.660 -44.583 89.480 1.00 155.73 ? 237 TYR A CB 1 ATOM 1527 C CG . TYR A 1 237 ? -60.821 -44.143 88.652 1.00 148.95 ? 237 TYR A CG 1 ATOM 1528 C CD1 . TYR A 1 237 ? -61.932 -43.542 89.228 1.00 150.39 ? 237 TYR A CD1 1 ATOM 1529 C CD2 . TYR A 1 237 ? -60.819 -44.362 87.285 1.00 149.63 ? 237 TYR A CD2 1 ATOM 1530 C CE1 . TYR A 1 237 ? -63.011 -43.169 88.451 1.00 149.76 ? 237 TYR A CE1 1 ATOM 1531 C CE2 . TYR A 1 237 ? -61.889 -44.006 86.501 1.00 148.57 ? 237 TYR A CE2 1 ATOM 1532 C CZ . TYR A 1 237 ? -62.976 -43.411 87.085 1.00 148.08 ? 237 TYR A CZ 1 ATOM 1533 O OH . TYR A 1 237 ? -64.012 -43.065 86.267 1.00 151.66 ? 237 TYR A OH 1 ATOM 1534 N N . VAL A 1 238 ? -57.876 -43.648 92.093 1.00 168.74 ? 238 VAL A N 1 ATOM 1535 C CA . VAL A 1 238 ? -56.874 -43.798 93.107 1.00 160.25 ? 238 VAL A CA 1 ATOM 1536 C C . VAL A 1 238 ? -57.351 -44.888 94.031 1.00 161.73 ? 238 VAL A C 1 ATOM 1537 O O . VAL A 1 238 ? -58.510 -45.294 93.950 1.00 157.59 ? 238 VAL A O 1 ATOM 1538 C CB . VAL A 1 238 ? -56.708 -42.484 93.892 1.00 161.60 ? 238 VAL A CB 1 ATOM 1539 C CG1 . VAL A 1 238 ? -55.234 -42.098 93.896 1.00 158.74 ? 238 VAL A CG1 1 ATOM 1540 C CG2 . VAL A 1 238 ? -57.598 -41.356 93.322 1.00 149.23 ? 238 VAL A CG2 1 ATOM 1541 N N . ASN A 1 239 ? -56.464 -45.363 94.898 1.00 166.40 ? 239 ASN A N 1 ATOM 1542 C CA . ASN A 1 239 ? -56.823 -46.354 95.913 1.00 183.47 ? 239 ASN A CA 1 ATOM 1543 C C . ASN A 1 239 ? -57.419 -47.675 95.391 1.00 195.22 ? 239 ASN A C 1 ATOM 1544 O O . ASN A 1 239 ? -56.819 -48.724 95.615 1.00 230.75 ? 239 ASN A O 1 ATOM 1545 C CB . ASN A 1 239 ? -57.584 -45.704 97.085 1.00 193.37 ? 239 ASN A CB 1 ATOM 1546 C CG . ASN A 1 239 ? -56.626 -45.158 98.117 1.00 209.87 ? 239 ASN A CG 1 ATOM 1547 O OD1 . ASN A 1 239 ? -55.438 -45.452 98.008 1.00 207.15 ? 239 ASN A OD1 1 ATOM 1548 N ND2 . ASN A 1 239 ? -57.097 -44.377 99.112 1.00 228.51 ? 239 ASN A ND2 1 ATOM 1549 N N . ARG A 1 240 ? -58.575 -47.633 94.723 1.00 174.60 ? 240 ARG A N 1 ATOM 1550 C CA . ARG A 1 240 ? -59.001 -48.668 93.748 1.00 150.06 ? 240 ARG A CA 1 ATOM 1551 C C . ARG A 1 240 ? -60.444 -48.502 93.339 1.00 144.16 ? 240 ARG A C 1 ATOM 1552 O O . ARG A 1 240 ? -61.221 -49.429 93.445 1.00 147.22 ? 240 ARG A O 1 ATOM 1553 C CB . ARG A 1 240 ? -58.704 -50.125 94.163 1.00 148.95 ? 240 ARG A CB 1 ATOM 1554 C CG . ARG A 1 240 ? -59.088 -50.512 95.585 1.00 169.79 ? 240 ARG A CG 1 ATOM 1555 C CD . ARG A 1 240 ? -59.144 -52.026 95.791 1.00 181.19 ? 240 ARG A CD 1 ATOM 1556 N NE . ARG A 1 240 ? -57.841 -52.686 95.934 1.00 170.53 ? 240 ARG A NE 1 ATOM 1557 C CZ . ARG A 1 240 ? -57.151 -52.761 97.071 1.00 175.47 ? 240 ARG A CZ 1 ATOM 1558 N NH1 . ARG A 1 240 ? -57.623 -52.194 98.182 1.00 190.51 ? 240 ARG A NH1 1 ATOM 1559 N NH2 . ARG A 1 240 ? -55.979 -53.394 97.096 1.00 164.79 ? 240 ARG A NH2 1 ATOM 1560 N N . SER A 1 241 ? -60.803 -47.308 92.882 1.00 142.70 ? 241 SER A N 1 ATOM 1561 C CA . SER A 1 241 ? -62.023 -47.128 92.094 1.00 142.50 ? 241 SER A CA 1 ATOM 1562 C C . SER A 1 241 ? -61.694 -47.518 90.643 1.00 141.51 ? 241 SER A C 1 ATOM 1563 O O . SER A 1 241 ? -60.736 -48.286 90.421 1.00 146.89 ? 241 SER A O 1 ATOM 1564 C CB . SER A 1 241 ? -62.545 -45.696 92.211 1.00 149.66 ? 241 SER A CB 1 ATOM 1565 O OG . SER A 1 241 ? -61.487 -44.750 92.244 1.00 158.89 ? 241 SER A OG 1 ATOM 1566 N N . LEU A 1 242 ? -62.456 -47.014 89.664 1.00 134.63 ? 242 LEU A N 1 ATOM 1567 C CA . LEU A 1 242 ? -62.253 -47.379 88.250 1.00 142.48 ? 242 LEU A CA 1 ATOM 1568 C C . LEU A 1 242 ? -63.121 -48.587 87.988 1.00 155.59 ? 242 LEU A C 1 ATOM 1569 O O . LEU A 1 242 ? -62.749 -49.689 88.379 1.00 186.40 ? 242 LEU A O 1 ATOM 1570 C CB . LEU A 1 242 ? -60.789 -47.808 87.974 1.00 136.09 ? 242 LEU A CB 1 ATOM 1571 C CG . LEU A 1 242 ? -59.927 -47.471 86.733 1.00 129.77 ? 242 LEU A CG 1 ATOM 1572 C CD1 . LEU A 1 242 ? -58.622 -48.260 86.743 1.00 121.76 ? 242 LEU A CD1 1 ATOM 1573 C CD2 . LEU A 1 242 ? -60.633 -47.588 85.385 1.00 122.31 ? 242 LEU A CD2 1 ATOM 1574 N N . PRO A 1 243 ? -64.266 -48.412 87.315 1.00 158.46 ? 243 PRO A N 1 ATOM 1575 C CA . PRO A 1 243 ? -65.163 -49.562 87.183 1.00 168.06 ? 243 PRO A CA 1 ATOM 1576 C C . PRO A 1 243 ? -64.728 -50.508 86.056 1.00 165.75 ? 243 PRO A C 1 ATOM 1577 O O . PRO A 1 243 ? -64.156 -51.561 86.347 1.00 162.17 ? 243 PRO A O 1 ATOM 1578 C CB . PRO A 1 243 ? -66.512 -48.918 86.883 1.00 167.37 ? 243 PRO A CB 1 ATOM 1579 C CG . PRO A 1 243 ? -66.142 -47.635 86.206 1.00 173.30 ? 243 PRO A CG 1 ATOM 1580 C CD . PRO A 1 243 ? -64.694 -47.297 86.465 1.00 156.75 ? 243 PRO A CD 1 ATOM 1581 N N . GLY A 1 244 ? -64.980 -50.122 84.799 1.00 162.74 ? 244 GLY A N 1 ATOM 1582 C CA . GLY A 1 244 ? -64.696 -50.945 83.611 1.00 151.12 ? 244 GLY A CA 1 ATOM 1583 C C . GLY A 1 244 ? -64.204 -52.361 83.871 1.00 139.07 ? 244 GLY A C 1 ATOM 1584 O O . GLY A 1 244 ? -64.944 -53.217 84.335 1.00 141.30 ? 244 GLY A O 1 ATOM 1585 N N . LEU A 1 245 ? -62.943 -52.603 83.557 1.00 133.48 ? 245 LEU A N 1 ATOM 1586 C CA . LEU A 1 245 ? -62.254 -53.869 83.864 1.00 130.66 ? 245 LEU A CA 1 ATOM 1587 C C . LEU A 1 245 ? -63.139 -55.147 84.036 1.00 132.86 ? 245 LEU A C 1 ATOM 1588 O O . LEU A 1 245 ? -63.650 -55.487 85.120 1.00 128.61 ? 245 LEU A O 1 ATOM 1589 C CB . LEU A 1 245 ? -61.190 -53.655 84.967 1.00 115.67 ? 245 LEU A CB 1 ATOM 1590 C CG . LEU A 1 245 ? -60.108 -52.580 84.676 1.00 106.53 ? 245 LEU A CG 1 ATOM 1591 C CD1 . LEU A 1 245 ? -59.157 -52.880 83.527 1.00 98.50 ? 245 LEU A CD1 1 ATOM 1592 C CD2 . LEU A 1 245 ? -60.716 -51.218 84.406 1.00 111.23 ? 245 LEU A CD2 1 ATOM 1593 N N . ILE A 1 246 ? -63.306 -55.812 82.895 1.00 132.46 ? 246 ILE A N 1 ATOM 1594 C CA . ILE A 1 246 ? -64.050 -57.048 82.733 1.00 133.14 ? 246 ILE A CA 1 ATOM 1595 C C . ILE A 1 246 ? -63.482 -57.767 81.534 1.00 133.37 ? 246 ILE A C 1 ATOM 1596 O O . ILE A 1 246 ? -63.205 -57.133 80.515 1.00 141.18 ? 246 ILE A O 1 ATOM 1597 C CB . ILE A 1 246 ? -65.525 -56.780 82.429 1.00 141.21 ? 246 ILE A CB 1 ATOM 1598 C CG1 . ILE A 1 246 ? -65.711 -55.435 81.641 1.00 145.17 ? 246 ILE A CG1 1 ATOM 1599 C CG2 . ILE A 1 246 ? -66.303 -56.872 83.736 1.00 144.31 ? 246 ILE A CG2 1 ATOM 1600 C CD1 . ILE A 1 246 ? -65.983 -55.515 80.132 1.00 135.10 ? 246 ILE A CD1 1 ATOM 1601 N N . GLY A 1 247 ? -63.302 -59.079 81.646 1.00 130.61 ? 247 GLY A N 1 ATOM 1602 C CA . GLY A 1 247 ? -62.803 -59.894 80.525 1.00 128.36 ? 247 GLY A CA 1 ATOM 1603 C C . GLY A 1 247 ? -63.609 -61.159 80.505 1.00 129.87 ? 247 GLY A C 1 ATOM 1604 O O . GLY A 1 247 ? -64.222 -61.492 81.515 1.00 135.25 ? 247 GLY A O 1 ATOM 1605 N N . CYS A 1 248 ? -63.647 -61.870 79.387 1.00 133.81 ? 248 CYS A N 1 ATOM 1606 C CA . CYS A 1 248 ? -64.514 -63.050 79.363 1.00 153.26 ? 248 CYS A CA 1 ATOM 1607 C C . CYS A 1 248 ? -63.757 -64.321 79.766 1.00 145.18 ? 248 CYS A C 1 ATOM 1608 O O . CYS A 1 248 ? -62.587 -64.472 79.418 1.00 157.76 ? 248 CYS A O 1 ATOM 1609 C CB . CYS A 1 248 ? -65.229 -63.179 78.018 1.00 184.25 ? 248 CYS A CB 1 ATOM 1610 S SG . CYS A 1 248 ? -66.127 -61.691 77.483 1.00 225.99 ? 248 CYS A SG 1 ATOM 1611 N N . HIS A 1 249 ? -64.405 -65.219 80.505 1.00 130.84 ? 249 HIS A N 1 ATOM 1612 C CA . HIS A 1 249 ? -63.662 -66.268 81.191 1.00 132.38 ? 249 HIS A CA 1 ATOM 1613 C C . HIS A 1 249 ? -62.671 -67.009 80.280 1.00 134.72 ? 249 HIS A C 1 ATOM 1614 O O . HIS A 1 249 ? -61.480 -67.071 80.572 1.00 133.60 ? 249 HIS A O 1 ATOM 1615 C CB . HIS A 1 249 ? -64.599 -67.228 81.969 1.00 146.45 ? 249 HIS A CB 1 ATOM 1616 C CG . HIS A 1 249 ? -63.916 -68.450 82.537 1.00 151.53 ? 249 HIS A CG 1 ATOM 1617 N ND1 . HIS A 1 249 ? -64.449 -69.720 82.435 1.00 149.79 ? 249 HIS A ND1 1 ATOM 1618 C CD2 . HIS A 1 249 ? -62.744 -68.593 83.208 1.00 150.18 ? 249 HIS A CD2 1 ATOM 1619 C CE1 . HIS A 1 249 ? -63.631 -70.587 83.008 1.00 155.43 ? 249 HIS A CE1 1 ATOM 1620 N NE2 . HIS A 1 249 ? -62.591 -69.929 83.489 1.00 147.63 ? 249 HIS A NE2 1 ATOM 1621 N N . ARG A 1 250 ? -63.140 -67.558 79.171 1.00 144.79 ? 250 ARG A N 1 ATOM 1622 C CA . ARG A 1 250 ? -62.283 -68.473 78.411 1.00 158.58 ? 250 ARG A CA 1 ATOM 1623 C C . ARG A 1 250 ? -61.238 -67.711 77.604 1.00 150.79 ? 250 ARG A C 1 ATOM 1624 O O . ARG A 1 250 ? -60.117 -68.186 77.458 1.00 154.00 ? 250 ARG A O 1 ATOM 1625 C CB . ARG A 1 250 ? -63.106 -69.406 77.495 1.00 190.54 ? 250 ARG A CB 1 ATOM 1626 C CG . ARG A 1 250 ? -64.132 -70.331 78.177 1.00 203.35 ? 250 ARG A CG 1 ATOM 1627 C CD . ARG A 1 250 ? -63.738 -71.806 78.189 1.00 194.23 ? 250 ARG A CD 1 ATOM 1628 N NE . ARG A 1 250 ? -63.074 -72.213 79.427 1.00 189.44 ? 250 ARG A NE 1 ATOM 1629 C CZ . ARG A 1 250 ? -61.763 -72.133 79.670 1.00 192.26 ? 250 ARG A CZ 1 ATOM 1630 N NH1 . ARG A 1 250 ? -60.901 -71.643 78.766 1.00 175.56 ? 250 ARG A NH1 1 ATOM 1631 N NH2 . ARG A 1 250 ? -61.314 -72.549 80.848 1.00 195.43 ? 250 ARG A NH2 1 ATOM 1632 N N . LYS A 1 251 ? -61.618 -66.528 77.114 1.00 144.67 ? 251 LYS A N 1 ATOM 1633 C CA . LYS A 1 251 ? -60.811 -65.737 76.182 1.00 137.46 ? 251 LYS A CA 1 ATOM 1634 C C . LYS A 1 251 ? -59.821 -64.789 76.855 1.00 130.17 ? 251 LYS A C 1 ATOM 1635 O O . LYS A 1 251 ? -59.581 -64.890 78.057 1.00 126.44 ? 251 LYS A O 1 ATOM 1636 C CB . LYS A 1 251 ? -61.708 -64.997 75.172 1.00 153.99 ? 251 LYS A CB 1 ATOM 1637 C CG . LYS A 1 251 ? -62.298 -63.641 75.592 1.00 177.04 ? 251 LYS A CG 1 ATOM 1638 C CD . LYS A 1 251 ? -63.295 -63.125 74.545 1.00 194.14 ? 251 LYS A CD 1 ATOM 1639 C CE . LYS A 1 251 ? -64.432 -64.136 74.345 1.00 208.05 ? 251 LYS A CE 1 ATOM 1640 N NZ . LYS A 1 251 ? -65.136 -64.151 73.029 1.00 211.13 ? 251 LYS A NZ 1 ATOM 1641 N N . SER A 1 252 ? -59.268 -63.867 76.063 1.00 132.91 ? 252 SER A N 1 ATOM 1642 C CA . SER A 1 252 ? -58.120 -63.033 76.445 1.00 133.44 ? 252 SER A CA 1 ATOM 1643 C C . SER A 1 252 ? -58.373 -61.545 76.358 1.00 131.48 ? 252 SER A C 1 ATOM 1644 O O . SER A 1 252 ? -59.335 -61.081 75.715 1.00 132.68 ? 252 SER A O 1 ATOM 1645 C CB . SER A 1 252 ? -56.917 -63.384 75.580 1.00 134.48 ? 252 SER A CB 1 ATOM 1646 O OG . SER A 1 252 ? -57.358 -64.006 74.376 1.00 146.21 ? 252 SER A OG 1 ATOM 1647 N N . VAL A 1 253 ? -57.488 -60.796 77.002 1.00 125.49 ? 253 VAL A N 1 ATOM 1648 C CA . VAL A 1 253 ? -57.743 -59.380 77.194 1.00 134.24 ? 253 VAL A CA 1 ATOM 1649 C C . VAL A 1 253 ? -56.507 -58.564 76.935 1.00 144.99 ? 253 VAL A C 1 ATOM 1650 O O . VAL A 1 253 ? -55.441 -58.914 77.451 1.00 172.30 ? 253 VAL A O 1 ATOM 1651 C CB . VAL A 1 253 ? -58.260 -59.120 78.611 1.00 128.17 ? 253 VAL A CB 1 ATOM 1652 C CG1 . VAL A 1 253 ? -57.993 -57.688 79.039 1.00 113.37 ? 253 VAL A CG1 1 ATOM 1653 C CG2 . VAL A 1 253 ? -59.747 -59.427 78.644 1.00 141.30 ? 253 VAL A CG2 1 ATOM 1654 N N . TYR A 1 254 ? -56.660 -57.483 76.151 1.00 133.35 ? 254 TYR A N 1 ATOM 1655 C CA . TYR A 1 254 ? -55.528 -56.659 75.662 1.00 121.34 ? 254 TYR A CA 1 ATOM 1656 C C . TYR A 1 254 ? -55.447 -55.326 76.321 1.00 112.89 ? 254 TYR A C 1 ATOM 1657 O O . TYR A 1 254 ? -56.466 -54.668 76.458 1.00 121.66 ? 254 TYR A O 1 ATOM 1658 C CB . TYR A 1 254 ? -55.666 -56.386 74.174 1.00 126.41 ? 254 TYR A CB 1 ATOM 1659 C CG . TYR A 1 254 ? -55.465 -57.604 73.347 1.00 135.52 ? 254 TYR A CG 1 ATOM 1660 C CD1 . TYR A 1 254 ? -54.196 -57.974 72.954 1.00 143.46 ? 254 TYR A CD1 1 ATOM 1661 C CD2 . TYR A 1 254 ? -56.541 -58.409 72.983 1.00 139.13 ? 254 TYR A CD2 1 ATOM 1662 C CE1 . TYR A 1 254 ? -53.989 -59.113 72.206 1.00 165.19 ? 254 TYR A CE1 1 ATOM 1663 C CE2 . TYR A 1 254 ? -56.352 -59.546 72.226 1.00 152.02 ? 254 TYR A CE2 1 ATOM 1664 C CZ . TYR A 1 254 ? -55.068 -59.898 71.838 1.00 166.82 ? 254 TYR A CZ 1 ATOM 1665 O OH . TYR A 1 254 ? -54.835 -61.036 71.079 1.00 191.43 ? 254 TYR A OH 1 ATOM 1666 N N . TRP A 1 255 ? -54.247 -54.902 76.701 1.00 110.54 ? 255 TRP A N 1 ATOM 1667 C CA . TRP A 1 255 ? -54.097 -53.581 77.330 1.00 124.29 ? 255 TRP A CA 1 ATOM 1668 C C . TRP A 1 255 ? -53.241 -52.630 76.492 1.00 119.78 ? 255 TRP A C 1 ATOM 1669 O O . TRP A 1 255 ? -52.104 -52.963 76.134 1.00 130.64 ? 255 TRP A O 1 ATOM 1670 C CB . TRP A 1 255 ? -53.477 -53.652 78.747 1.00 134.64 ? 255 TRP A CB 1 ATOM 1671 C CG . TRP A 1 255 ? -53.927 -54.743 79.702 1.00 126.95 ? 255 TRP A CG 1 ATOM 1672 C CD1 . TRP A 1 255 ? -53.151 -55.748 80.207 1.00 121.65 ? 255 TRP A CD1 1 ATOM 1673 C CD2 . TRP A 1 255 ? -55.222 -54.897 80.301 1.00 125.82 ? 255 TRP A CD2 1 ATOM 1674 N NE1 . TRP A 1 255 ? -53.884 -56.525 81.068 1.00 124.33 ? 255 TRP A NE1 1 ATOM 1675 C CE2 . TRP A 1 255 ? -55.159 -56.033 81.140 1.00 126.01 ? 255 TRP A CE2 1 ATOM 1676 C CE3 . TRP A 1 255 ? -56.436 -54.208 80.186 1.00 124.89 ? 255 TRP A CE3 1 ATOM 1677 C CZ2 . TRP A 1 255 ? -56.259 -56.491 81.863 1.00 126.76 ? 255 TRP A CZ2 1 ATOM 1678 C CZ3 . TRP A 1 255 ? -57.525 -54.661 80.902 1.00 127.06 ? 255 TRP A CZ3 1 ATOM 1679 C CH2 . TRP A 1 255 ? -57.430 -55.794 81.732 1.00 129.42 ? 255 TRP A CH2 1 ATOM 1680 N N . HIS A 1 256 ? -53.756 -51.440 76.207 1.00 106.16 ? 256 HIS A N 1 ATOM 1681 C CA . HIS A 1 256 ? -52.917 -50.447 75.568 1.00 108.89 ? 256 HIS A CA 1 ATOM 1682 C C . HIS A 1 256 ? -52.310 -49.602 76.676 1.00 110.33 ? 256 HIS A C 1 ATOM 1683 O O . HIS A 1 256 ? -52.966 -48.697 77.172 1.00 124.41 ? 256 HIS A O 1 ATOM 1684 C CB . HIS A 1 256 ? -53.716 -49.642 74.534 1.00 113.36 ? 256 HIS A CB 1 ATOM 1685 C CG . HIS A 1 256 ? -54.179 -50.470 73.374 1.00 129.84 ? 256 HIS A CG 1 ATOM 1686 N ND1 . HIS A 1 256 ? -53.305 -51.037 72.469 1.00 143.30 ? 256 HIS A ND1 1 ATOM 1687 C CD2 . HIS A 1 256 ? -55.418 -50.866 72.990 1.00 143.57 ? 256 HIS A CD2 1 ATOM 1688 C CE1 . HIS A 1 256 ? -53.984 -51.738 71.575 1.00 155.26 ? 256 HIS A CE1 1 ATOM 1689 N NE2 . HIS A 1 256 ? -55.269 -51.650 71.867 1.00 154.05 ? 256 HIS A NE2 1 ATOM 1690 N N . VAL A 1 257 ? -51.075 -49.920 77.090 1.00 107.21 ? 257 VAL A N 1 ATOM 1691 C CA . VAL A 1 257 ? -50.465 -49.301 78.304 1.00 104.49 ? 257 VAL A CA 1 ATOM 1692 C C . VAL A 1 257 ? -49.709 -47.984 78.057 1.00 106.27 ? 257 VAL A C 1 ATOM 1693 O O . VAL A 1 257 ? -48.833 -47.902 77.194 1.00 114.79 ? 257 VAL A O 1 ATOM 1694 C CB . VAL A 1 257 ? -49.525 -50.266 79.077 1.00 96.33 ? 257 VAL A CB 1 ATOM 1695 C CG1 . VAL A 1 257 ? -49.454 -49.889 80.544 1.00 87.38 ? 257 VAL A CG1 1 ATOM 1696 C CG2 . VAL A 1 257 ? -49.982 -51.703 78.945 1.00 97.37 ? 257 VAL A CG2 1 ATOM 1697 N N . ILE A 1 258 ? -50.052 -46.957 78.824 1.00 103.93 ? 258 ILE A N 1 ATOM 1698 C CA . ILE A 1 258 ? -49.329 -45.694 78.780 1.00 109.98 ? 258 ILE A CA 1 ATOM 1699 C C . ILE A 1 258 ? -48.716 -45.414 80.166 1.00 126.48 ? 258 ILE A C 1 ATOM 1700 O O . ILE A 1 258 ? -49.431 -45.281 81.176 1.00 130.85 ? 258 ILE A O 1 ATOM 1701 C CB . ILE A 1 258 ? -50.221 -44.500 78.305 1.00 104.44 ? 258 ILE A CB 1 ATOM 1702 C CG1 . ILE A 1 258 ? -50.925 -44.808 76.991 1.00 101.91 ? 258 ILE A CG1 1 ATOM 1703 C CG2 . ILE A 1 258 ? -49.414 -43.220 78.102 1.00 100.83 ? 258 ILE A CG2 1 ATOM 1704 C CD1 . ILE A 1 258 ? -51.893 -43.722 76.560 1.00 106.83 ? 258 ILE A CD1 1 ATOM 1705 N N . GLY A 1 259 ? -47.386 -45.352 80.210 1.00 135.60 ? 259 GLY A N 1 ATOM 1706 C CA . GLY A 1 259 ? -46.686 -44.766 81.349 1.00 145.99 ? 259 GLY A CA 1 ATOM 1707 C C . GLY A 1 259 ? -46.665 -43.248 81.235 1.00 164.94 ? 259 GLY A C 1 ATOM 1708 O O . GLY A 1 259 ? -46.296 -42.704 80.188 1.00 185.31 ? 259 GLY A O 1 ATOM 1709 N N . MET A 1 260 ? -47.078 -42.557 82.298 1.00 168.50 ? 260 MET A N 1 ATOM 1710 C CA . MET A 1 260 ? -46.989 -41.095 82.334 1.00 166.63 ? 260 MET A CA 1 ATOM 1711 C C . MET A 1 260 ? -46.532 -40.519 83.686 1.00 158.92 ? 260 MET A C 1 ATOM 1712 O O . MET A 1 260 ? -46.784 -41.073 84.767 1.00 150.49 ? 260 MET A O 1 ATOM 1713 C CB . MET A 1 260 ? -48.297 -40.446 81.870 1.00 185.89 ? 260 MET A CB 1 ATOM 1714 C CG . MET A 1 260 ? -48.108 -39.088 81.208 1.00 210.51 ? 260 MET A CG 1 ATOM 1715 S SD . MET A 1 260 ? -49.310 -37.840 81.730 1.00 249.57 ? 260 MET A SD 1 ATOM 1716 C CE . MET A 1 260 ? -48.788 -37.527 83.418 1.00 235.26 ? 260 MET A CE 1 ATOM 1717 N N . GLY A 1 261 ? -45.844 -39.392 83.589 1.00 157.92 ? 261 GLY A N 1 ATOM 1718 C CA . GLY A 1 261 ? -45.265 -38.717 84.728 1.00 162.76 ? 261 GLY A CA 1 ATOM 1719 C C . GLY A 1 261 ? -44.463 -37.514 84.270 1.00 171.32 ? 261 GLY A C 1 ATOM 1720 O O . GLY A 1 261 ? -44.330 -37.220 83.068 1.00 176.86 ? 261 GLY A O 1 ATOM 1721 N N . THR A 1 262 ? -43.905 -36.825 85.248 1.00 169.58 ? 262 THR A N 1 ATOM 1722 C CA . THR A 1 262 ? -43.209 -35.587 85.001 1.00 160.99 ? 262 THR A CA 1 ATOM 1723 C C . THR A 1 262 ? -41.706 -35.825 85.271 1.00 152.80 ? 262 THR A C 1 ATOM 1724 O O . THR A 1 262 ? -40.823 -35.177 84.710 1.00 139.69 ? 262 THR A O 1 ATOM 1725 C CB . THR A 1 262 ? -43.898 -34.465 85.838 1.00 167.67 ? 262 THR A CB 1 ATOM 1726 O OG1 . THR A 1 262 ? -43.868 -33.221 85.132 1.00 161.10 ? 262 THR A OG1 1 ATOM 1727 C CG2 . THR A 1 262 ? -43.358 -34.338 87.294 1.00 167.67 ? 262 THR A CG2 1 ATOM 1728 N N . THR A 1 263 ? -41.442 -36.845 86.072 1.00 152.88 ? 263 THR A N 1 ATOM 1729 C CA . THR A 1 263 ? -40.133 -37.099 86.626 1.00 157.39 ? 263 THR A CA 1 ATOM 1730 C C . THR A 1 263 ? -39.818 -38.608 86.511 1.00 162.93 ? 263 THR A C 1 ATOM 1731 O O . THR A 1 263 ? -40.742 -39.411 86.373 1.00 184.63 ? 263 THR A O 1 ATOM 1732 C CB . THR A 1 263 ? -40.139 -36.618 88.089 1.00 164.12 ? 263 THR A CB 1 ATOM 1733 O OG1 . THR A 1 263 ? -38.909 -36.967 88.726 1.00 175.65 ? 263 THR A OG1 1 ATOM 1734 C CG2 . THR A 1 263 ? -41.346 -37.198 88.873 1.00 161.41 ? 263 THR A CG2 1 ATOM 1735 N N . PRO A 1 264 ? -38.525 -39.002 86.549 1.00 156.40 ? 264 PRO A N 1 ATOM 1736 C CA . PRO A 1 264 ? -38.097 -40.409 86.435 1.00 156.98 ? 264 PRO A CA 1 ATOM 1737 C C . PRO A 1 264 ? -38.630 -41.487 87.420 1.00 169.47 ? 264 PRO A C 1 ATOM 1738 O O . PRO A 1 264 ? -38.191 -42.638 87.318 1.00 174.58 ? 264 PRO A O 1 ATOM 1739 C CB . PRO A 1 264 ? -36.561 -40.319 86.564 1.00 149.30 ? 264 PRO A CB 1 ATOM 1740 C CG . PRO A 1 264 ? -36.267 -38.942 87.031 1.00 147.36 ? 264 PRO A CG 1 ATOM 1741 C CD . PRO A 1 264 ? -37.363 -38.109 86.441 1.00 155.42 ? 264 PRO A CD 1 ATOM 1742 N N . GLU A 1 265 ? -39.545 -41.169 88.341 1.00 180.89 ? 265 GLU A N 1 ATOM 1743 C CA . GLU A 1 265 ? -39.985 -42.194 89.315 1.00 185.50 ? 265 GLU A CA 1 ATOM 1744 C C . GLU A 1 265 ? -40.814 -43.315 88.682 1.00 171.08 ? 265 GLU A C 1 ATOM 1745 O O . GLU A 1 265 ? -41.889 -43.087 88.106 1.00 158.54 ? 265 GLU A O 1 ATOM 1746 C CB . GLU A 1 265 ? -40.617 -41.603 90.594 1.00 208.27 ? 265 GLU A CB 1 ATOM 1747 C CG . GLU A 1 265 ? -42.121 -41.364 90.586 1.00 220.86 ? 265 GLU A CG 1 ATOM 1748 C CD . GLU A 1 265 ? -42.630 -40.857 91.927 1.00 234.93 ? 265 GLU A CD 1 ATOM 1749 O OE1 . GLU A 1 265 ? -42.116 -39.825 92.423 1.00 240.37 ? 265 GLU A OE1 1 ATOM 1750 O OE2 . GLU A 1 265 ? -43.543 -41.496 92.489 1.00 232.28 ? 265 GLU A OE2 1 ATOM 1751 N N . VAL A 1 266 ? -40.270 -44.526 88.836 1.00 164.92 ? 266 VAL A N 1 ATOM 1752 C CA . VAL A 1 266 ? -40.621 -45.738 88.080 1.00 143.13 ? 266 VAL A CA 1 ATOM 1753 C C . VAL A 1 266 ? -41.646 -46.660 88.778 1.00 147.33 ? 266 VAL A C 1 ATOM 1754 O O . VAL A 1 266 ? -42.108 -46.351 89.876 1.00 168.83 ? 266 VAL A O 1 ATOM 1755 C CB . VAL A 1 266 ? -39.336 -46.525 87.792 1.00 125.03 ? 266 VAL A CB 1 ATOM 1756 C CG1 . VAL A 1 266 ? -39.046 -47.517 88.913 1.00 109.45 ? 266 VAL A CG1 1 ATOM 1757 C CG2 . VAL A 1 266 ? -39.427 -47.188 86.432 1.00 116.86 ? 266 VAL A CG2 1 ATOM 1758 N N . HIS A 1 267 ? -42.000 -47.777 88.138 1.00 133.69 ? 267 HIS A N 1 ATOM 1759 C CA . HIS A 1 267 ? -43.044 -48.687 88.630 1.00 138.54 ? 267 HIS A CA 1 ATOM 1760 C C . HIS A 1 267 ? -42.775 -50.162 88.262 1.00 148.97 ? 267 HIS A C 1 ATOM 1761 O O . HIS A 1 267 ? -41.980 -50.456 87.376 1.00 168.95 ? 267 HIS A O 1 ATOM 1762 C CB . HIS A 1 267 ? -44.423 -48.288 88.071 1.00 131.61 ? 267 HIS A CB 1 ATOM 1763 C CG . HIS A 1 267 ? -44.918 -46.945 88.517 1.00 136.92 ? 267 HIS A CG 1 ATOM 1764 N ND1 . HIS A 1 267 ? -45.701 -46.770 89.637 1.00 149.73 ? 267 HIS A ND1 1 ATOM 1765 C CD2 . HIS A 1 267 ? -44.764 -45.714 87.972 1.00 145.95 ? 267 HIS A CD2 1 ATOM 1766 C CE1 . HIS A 1 267 ? -45.989 -45.486 89.771 1.00 157.38 ? 267 HIS A CE1 1 ATOM 1767 N NE2 . HIS A 1 267 ? -45.434 -44.823 88.772 1.00 146.20 ? 267 HIS A NE2 1 ATOM 1768 N N . SER A 1 268 ? -43.455 -51.082 88.941 1.00 151.42 ? 268 SER A N 1 ATOM 1769 C CA . SER A 1 268 ? -43.463 -52.505 88.591 1.00 142.31 ? 268 SER A CA 1 ATOM 1770 C C . SER A 1 268 ? -44.932 -52.960 88.802 1.00 140.23 ? 268 SER A C 1 ATOM 1771 O O . SER A 1 268 ? -45.353 -53.223 89.931 1.00 155.27 ? 268 SER A O 1 ATOM 1772 C CB . SER A 1 268 ? -42.450 -53.285 89.480 1.00 141.02 ? 268 SER A CB 1 ATOM 1773 O OG . SER A 1 268 ? -41.879 -54.437 88.851 1.00 129.76 ? 268 SER A OG 1 ATOM 1774 N N . ILE A 1 269 ? -45.726 -53.000 87.732 1.00 120.22 ? 269 ILE A N 1 ATOM 1775 C CA . ILE A 1 269 ? -47.146 -53.392 87.831 1.00 115.19 ? 269 ILE A CA 1 ATOM 1776 C C . ILE A 1 269 ? -47.312 -54.909 87.724 1.00 126.51 ? 269 ILE A C 1 ATOM 1777 O O . ILE A 1 269 ? -46.713 -55.534 86.842 1.00 137.26 ? 269 ILE A O 1 ATOM 1778 C CB . ILE A 1 269 ? -48.007 -52.699 86.740 1.00 105.61 ? 269 ILE A CB 1 ATOM 1779 C CG1 . ILE A 1 269 ? -47.960 -51.195 86.922 1.00 106.98 ? 269 ILE A CG1 1 ATOM 1780 C CG2 . ILE A 1 269 ? -49.464 -53.165 86.747 1.00 97.61 ? 269 ILE A CG2 1 ATOM 1781 C CD1 . ILE A 1 269 ? -46.602 -50.597 86.654 1.00 112.24 ? 269 ILE A CD1 1 ATOM 1782 N N . PHE A 1 270 ? -48.115 -55.497 88.618 1.00 129.17 ? 270 PHE A N 1 ATOM 1783 C CA . PHE A 1 270 ? -48.505 -56.922 88.528 1.00 130.39 ? 270 PHE A CA 1 ATOM 1784 C C . PHE A 1 270 ? -50.028 -57.039 88.458 1.00 126.68 ? 270 PHE A C 1 ATOM 1785 O O . PHE A 1 270 ? -50.741 -56.162 88.961 1.00 132.24 ? 270 PHE A O 1 ATOM 1786 C CB . PHE A 1 270 ? -48.015 -57.718 89.752 1.00 139.49 ? 270 PHE A CB 1 ATOM 1787 C CG . PHE A 1 270 ? -46.501 -57.838 89.879 1.00 146.05 ? 270 PHE A CG 1 ATOM 1788 C CD1 . PHE A 1 270 ? -45.701 -56.725 90.201 1.00 145.14 ? 270 PHE A CD1 1 ATOM 1789 C CD2 . PHE A 1 270 ? -45.874 -59.079 89.728 1.00 139.55 ? 270 PHE A CD2 1 ATOM 1790 C CE1 . PHE A 1 270 ? -44.316 -56.841 90.334 1.00 139.91 ? 270 PHE A CE1 1 ATOM 1791 C CE2 . PHE A 1 270 ? -44.495 -59.194 89.863 1.00 140.24 ? 270 PHE A CE2 1 ATOM 1792 C CZ . PHE A 1 270 ? -43.715 -58.075 90.163 1.00 140.67 ? 270 PHE A CZ 1 ATOM 1793 N N . LEU A 1 271 ? -50.537 -58.098 87.834 1.00 110.97 ? 271 LEU A N 1 ATOM 1794 C CA . LEU A 1 271 ? -51.966 -58.362 87.931 1.00 110.71 ? 271 LEU A CA 1 ATOM 1795 C C . LEU A 1 271 ? -52.140 -59.684 88.592 1.00 120.73 ? 271 LEU A C 1 ATOM 1796 O O . LEU A 1 271 ? -51.747 -60.692 88.029 1.00 137.14 ? 271 LEU A O 1 ATOM 1797 C CB . LEU A 1 271 ? -52.652 -58.427 86.571 1.00 104.79 ? 271 LEU A CB 1 ATOM 1798 C CG . LEU A 1 271 ? -54.135 -58.832 86.663 1.00 102.41 ? 271 LEU A CG 1 ATOM 1799 C CD1 . LEU A 1 271 ? -55.038 -57.609 86.687 1.00 95.41 ? 271 LEU A CD1 1 ATOM 1800 C CD2 . LEU A 1 271 ? -54.548 -59.790 85.550 1.00 102.33 ? 271 LEU A CD2 1 ATOM 1801 N N . GLU A 1 272 ? -52.761 -59.674 89.766 1.00 130.42 ? 272 GLU A N 1 ATOM 1802 C CA . GLU A 1 272 ? -53.061 -60.878 90.562 1.00 138.01 ? 272 GLU A CA 1 ATOM 1803 C C . GLU A 1 272 ? -53.219 -62.182 89.765 1.00 133.61 ? 272 GLU A C 1 ATOM 1804 O O . GLU A 1 272 ? -54.045 -62.277 88.843 1.00 131.58 ? 272 GLU A O 1 ATOM 1805 C CB . GLU A 1 272 ? -54.313 -60.628 91.419 1.00 155.41 ? 272 GLU A CB 1 ATOM 1806 C CG . GLU A 1 272 ? -54.335 -61.374 92.750 1.00 181.70 ? 272 GLU A CG 1 ATOM 1807 C CD . GLU A 1 272 ? -55.303 -60.769 93.754 1.00 199.08 ? 272 GLU A CD 1 ATOM 1808 O OE1 . GLU A 1 272 ? -55.611 -59.563 93.631 1.00 193.98 ? 272 GLU A OE1 1 ATOM 1809 O OE2 . GLU A 1 272 ? -55.755 -61.501 94.668 1.00 227.39 ? 272 GLU A OE2 1 ATOM 1810 N N . GLY A 1 273 ? -52.410 -63.176 90.131 1.00 132.55 ? 273 GLY A N 1 ATOM 1811 C CA . GLY A 1 273 ? -52.468 -64.513 89.532 1.00 143.26 ? 273 GLY A CA 1 ATOM 1812 C C . GLY A 1 273 ? -51.918 -64.505 88.129 1.00 147.26 ? 273 GLY A C 1 ATOM 1813 O O . GLY A 1 273 ? -51.097 -65.348 87.761 1.00 176.72 ? 273 GLY A O 1 ATOM 1814 N N . HIS A 1 274 ? -52.338 -63.496 87.376 1.00 139.69 ? 274 HIS A N 1 ATOM 1815 C CA . HIS A 1 274 ? -52.141 -63.426 85.937 1.00 137.00 ? 274 HIS A CA 1 ATOM 1816 C C . HIS A 1 274 ? -50.826 -62.797 85.437 1.00 129.38 ? 274 HIS A C 1 ATOM 1817 O O . HIS A 1 274 ? -50.403 -61.763 85.943 1.00 135.57 ? 274 HIS A O 1 ATOM 1818 C CB . HIS A 1 274 ? -53.376 -62.775 85.317 1.00 133.45 ? 274 HIS A CB 1 ATOM 1819 C CG . HIS A 1 274 ? -54.622 -63.577 85.519 1.00 140.54 ? 274 HIS A CG 1 ATOM 1820 N ND1 . HIS A 1 274 ? -55.859 -62.999 85.712 1.00 138.19 ? 274 HIS A ND1 1 ATOM 1821 C CD2 . HIS A 1 274 ? -54.815 -64.919 85.577 1.00 146.47 ? 274 HIS A CD2 1 ATOM 1822 C CE1 . HIS A 1 274 ? -56.763 -63.953 85.858 1.00 153.16 ? 274 HIS A CE1 1 ATOM 1823 N NE2 . HIS A 1 274 ? -56.155 -65.126 85.784 1.00 155.69 ? 274 HIS A NE2 1 ATOM 1824 N N . THR A 1 275 ? -50.210 -63.442 84.435 1.00 123.56 ? 275 THR A N 1 ATOM 1825 C CA . THR A 1 275 ? -48.960 -63.022 83.763 1.00 109.05 ? 275 THR A CA 1 ATOM 1826 C C . THR A 1 275 ? -49.253 -62.174 82.497 1.00 104.08 ? 275 THR A C 1 ATOM 1827 O O . THR A 1 275 ? -50.400 -62.048 82.059 1.00 103.59 ? 275 THR A O 1 ATOM 1828 C CB . THR A 1 275 ? -48.146 -64.271 83.363 1.00 115.89 ? 275 THR A CB 1 ATOM 1829 O OG1 . THR A 1 275 ? -48.997 -65.152 82.620 1.00 116.64 ? 275 THR A OG1 1 ATOM 1830 C CG2 . THR A 1 275 ? -47.576 -65.050 84.615 1.00 131.46 ? 275 THR A CG2 1 ATOM 1831 N N . PHE A 1 276 ? -48.237 -61.561 81.903 1.00 109.75 ? 276 PHE A N 1 ATOM 1832 C CA . PHE A 1 276 ? -48.485 -60.766 80.670 1.00 120.27 ? 276 PHE A CA 1 ATOM 1833 C C . PHE A 1 276 ? -47.766 -61.245 79.415 1.00 131.35 ? 276 PHE A C 1 ATOM 1834 O O . PHE A 1 276 ? -46.875 -62.126 79.433 1.00 130.33 ? 276 PHE A O 1 ATOM 1835 C CB . PHE A 1 276 ? -48.161 -59.261 80.826 1.00 108.57 ? 276 PHE A CB 1 ATOM 1836 C CG . PHE A 1 276 ? -48.956 -58.581 81.869 1.00 103.02 ? 276 PHE A CG 1 ATOM 1837 C CD1 . PHE A 1 276 ? -50.332 -58.533 81.777 1.00 105.68 ? 276 PHE A CD1 1 ATOM 1838 C CD2 . PHE A 1 276 ? -48.324 -58.020 82.975 1.00 103.62 ? 276 PHE A CD2 1 ATOM 1839 C CE1 . PHE A 1 276 ? -51.065 -57.911 82.769 1.00 113.54 ? 276 PHE A CE1 1 ATOM 1840 C CE2 . PHE A 1 276 ? -49.045 -57.398 83.977 1.00 100.85 ? 276 PHE A CE2 1 ATOM 1841 C CZ . PHE A 1 276 ? -50.419 -57.340 83.870 1.00 109.41 ? 276 PHE A CZ 1 ATOM 1842 N N . LEU A 1 277 ? -48.165 -60.613 78.319 1.00 126.97 ? 277 LEU A N 1 ATOM 1843 C CA . LEU A 1 277 ? -47.435 -60.713 77.095 1.00 123.81 ? 277 LEU A CA 1 ATOM 1844 C C . LEU A 1 277 ? -47.132 -59.353 76.497 1.00 136.23 ? 277 LEU A C 1 ATOM 1845 O O . LEU A 1 277 ? -48.021 -58.582 76.123 1.00 144.17 ? 277 LEU A O 1 ATOM 1846 C CB . LEU A 1 277 ? -48.145 -61.631 76.129 1.00 112.85 ? 277 LEU A CB 1 ATOM 1847 C CG . LEU A 1 277 ? -47.799 -63.011 76.663 1.00 112.20 ? 277 LEU A CG 1 ATOM 1848 C CD1 . LEU A 1 277 ? -49.023 -63.747 77.199 1.00 120.12 ? 277 LEU A CD1 1 ATOM 1849 C CD2 . LEU A 1 277 ? -47.039 -63.810 75.621 1.00 121.35 ? 277 LEU A CD2 1 ATOM 1850 N N . VAL A 1 278 ? -45.841 -59.068 76.464 1.00 139.14 ? 278 VAL A N 1 ATOM 1851 C CA . VAL A 1 278 ? -45.311 -57.962 75.716 1.00 130.96 ? 278 VAL A CA 1 ATOM 1852 C C . VAL A 1 278 ? -44.559 -58.586 74.554 1.00 129.66 ? 278 VAL A C 1 ATOM 1853 O O . VAL A 1 278 ? -44.240 -59.782 74.575 1.00 105.94 ? 278 VAL A O 1 ATOM 1854 C CB . VAL A 1 278 ? -44.369 -57.101 76.576 1.00 135.37 ? 278 VAL A CB 1 ATOM 1855 C CG1 . VAL A 1 278 ? -44.978 -56.896 77.962 1.00 143.03 ? 278 VAL A CG1 1 ATOM 1856 C CG2 . VAL A 1 278 ? -42.955 -57.702 76.643 1.00 130.63 ? 278 VAL A CG2 1 ATOM 1857 N N . ARG A 1 279 ? -44.302 -57.773 73.533 1.00 147.08 ? 279 ARG A N 1 ATOM 1858 C CA . ARG A 1 279 ? -43.530 -58.205 72.392 1.00 152.66 ? 279 ARG A CA 1 ATOM 1859 C C . ARG A 1 279 ? -43.995 -59.628 72.120 1.00 139.10 ? 279 ARG A C 1 ATOM 1860 O O . ARG A 1 279 ? -45.017 -59.826 71.468 1.00 162.04 ? 279 ARG A O 1 ATOM 1861 C CB . ARG A 1 279 ? -42.030 -58.071 72.709 1.00 174.85 ? 279 ARG A CB 1 ATOM 1862 C CG . ARG A 1 279 ? -41.358 -56.897 71.987 1.00 189.10 ? 279 ARG A CG 1 ATOM 1863 C CD . ARG A 1 279 ? -40.524 -55.924 72.832 1.00 179.97 ? 279 ARG A CD 1 ATOM 1864 N NE . ARG A 1 279 ? -41.245 -54.669 73.053 1.00 167.45 ? 279 ARG A NE 1 ATOM 1865 C CZ . ARG A 1 279 ? -41.719 -53.889 72.084 1.00 158.20 ? 279 ARG A CZ 1 ATOM 1866 N NH1 . ARG A 1 279 ? -41.545 -54.226 70.818 1.00 139.26 ? 279 ARG A NH1 1 ATOM 1867 N NH2 . ARG A 1 279 ? -42.379 -52.772 72.380 1.00 168.26 ? 279 ARG A NH2 1 ATOM 1868 N N . ASN A 1 280 ? -43.299 -60.609 72.665 1.00 116.61 ? 280 ASN A N 1 ATOM 1869 C CA . ASN A 1 280 ? -43.878 -61.919 72.751 1.00 121.12 ? 280 ASN A CA 1 ATOM 1870 C C . ASN A 1 280 ? -43.376 -62.739 73.940 1.00 134.32 ? 280 ASN A C 1 ATOM 1871 O O . ASN A 1 280 ? -43.432 -63.978 73.949 1.00 137.69 ? 280 ASN A O 1 ATOM 1872 C CB . ASN A 1 280 ? -43.672 -62.686 71.467 1.00 127.84 ? 280 ASN A CB 1 ATOM 1873 C CG . ASN A 1 280 ? -44.501 -63.936 71.449 1.00 142.69 ? 280 ASN A CG 1 ATOM 1874 O OD1 . ASN A 1 280 ? -45.719 -63.863 71.594 1.00 149.54 ? 280 ASN A OD1 1 ATOM 1875 N ND2 . ASN A 1 280 ? -43.853 -65.093 71.352 1.00 152.16 ? 280 ASN A ND2 1 ATOM 1876 N N . HIS A 1 281 ? -42.885 -62.050 74.957 1.00 141.34 ? 281 HIS A N 1 ATOM 1877 C CA . HIS A 1 281 ? -42.301 -62.745 76.089 1.00 136.17 ? 281 HIS A CA 1 ATOM 1878 C C . HIS A 1 281 ? -43.269 -62.752 77.244 1.00 136.83 ? 281 HIS A C 1 ATOM 1879 O O . HIS A 1 281 ? -43.961 -61.762 77.524 1.00 134.98 ? 281 HIS A O 1 ATOM 1880 C CB . HIS A 1 281 ? -40.972 -62.106 76.515 1.00 143.65 ? 281 HIS A CB 1 ATOM 1881 C CG . HIS A 1 281 ? -40.027 -61.863 75.378 1.00 140.83 ? 281 HIS A CG 1 ATOM 1882 N ND1 . HIS A 1 281 ? -39.075 -62.782 74.992 1.00 135.70 ? 281 HIS A ND1 1 ATOM 1883 C CD2 . HIS A 1 281 ? -39.901 -60.812 74.533 1.00 135.22 ? 281 HIS A CD2 1 ATOM 1884 C CE1 . HIS A 1 281 ? -38.409 -62.312 73.955 1.00 135.98 ? 281 HIS A CE1 1 ATOM 1885 N NE2 . HIS A 1 281 ? -38.894 -61.120 73.653 1.00 133.78 ? 281 HIS A NE2 1 ATOM 1886 N N . ARG A 1 282 ? -43.325 -63.899 77.897 1.00 135.75 ? 282 ARG A N 1 ATOM 1887 C CA . ARG A 1 282 ? -43.904 -63.991 79.211 1.00 132.00 ? 282 ARG A CA 1 ATOM 1888 C C . ARG A 1 282 ? -43.153 -62.979 80.080 1.00 131.63 ? 282 ARG A C 1 ATOM 1889 O O . ARG A 1 282 ? -41.946 -63.096 80.290 1.00 142.45 ? 282 ARG A O 1 ATOM 1890 C CB . ARG A 1 282 ? -43.704 -65.412 79.734 1.00 134.71 ? 282 ARG A CB 1 ATOM 1891 C CG . ARG A 1 282 ? -44.493 -65.748 80.980 1.00 140.90 ? 282 ARG A CG 1 ATOM 1892 C CD . ARG A 1 282 ? -45.970 -65.837 80.666 1.00 143.53 ? 282 ARG A CD 1 ATOM 1893 N NE . ARG A 1 282 ? -46.255 -67.023 79.876 1.00 141.09 ? 282 ARG A NE 1 ATOM 1894 C CZ . ARG A 1 282 ? -47.429 -67.294 79.316 1.00 152.72 ? 282 ARG A CZ 1 ATOM 1895 N NH1 . ARG A 1 282 ? -48.479 -66.467 79.433 1.00 138.37 ? 282 ARG A NH1 1 ATOM 1896 N NH2 . ARG A 1 282 ? -47.547 -68.414 78.625 1.00 179.26 ? 282 ARG A NH2 1 ATOM 1897 N N . GLN A 1 283 ? -43.851 -61.953 80.530 1.00 123.62 ? 283 GLN A N 1 ATOM 1898 C CA . GLN A 1 283 ? -43.299 -61.031 81.503 1.00 124.67 ? 283 GLN A CA 1 ATOM 1899 C C . GLN A 1 283 ? -44.324 -61.153 82.601 1.00 125.96 ? 283 GLN A C 1 ATOM 1900 O O . GLN A 1 283 ? -45.512 -61.171 82.308 1.00 139.81 ? 283 GLN A O 1 ATOM 1901 C CB . GLN A 1 283 ? -43.318 -59.638 80.910 1.00 126.07 ? 283 GLN A CB 1 ATOM 1902 C CG . GLN A 1 283 ? -42.078 -58.824 81.176 1.00 148.08 ? 283 GLN A CG 1 ATOM 1903 C CD . GLN A 1 283 ? -41.882 -57.757 80.113 1.00 169.21 ? 283 GLN A CD 1 ATOM 1904 O OE1 . GLN A 1 283 ? -41.293 -58.024 79.055 1.00 177.75 ? 283 GLN A OE1 1 ATOM 1905 N NE2 . GLN A 1 283 ? -42.377 -56.534 80.383 1.00 163.67 ? 283 GLN A NE2 1 ATOM 1906 N N . ALA A 1 284 ? -43.933 -61.294 83.856 1.00 122.09 ? 284 ALA A N 1 ATOM 1907 C CA . ALA A 1 284 ? -44.999 -61.454 84.857 1.00 123.97 ? 284 ALA A CA 1 ATOM 1908 C C . ALA A 1 284 ? -45.322 -60.142 85.553 1.00 123.11 ? 284 ALA A C 1 ATOM 1909 O O . ALA A 1 284 ? -46.364 -60.014 86.202 1.00 125.58 ? 284 ALA A O 1 ATOM 1910 C CB . ALA A 1 284 ? -44.700 -62.569 85.856 1.00 138.25 ? 284 ALA A CB 1 ATOM 1911 N N . SER A 1 285 ? -44.404 -59.184 85.424 1.00 120.67 ? 285 SER A N 1 ATOM 1912 C CA . SER A 1 285 ? -44.654 -57.785 85.770 1.00 116.73 ? 285 SER A CA 1 ATOM 1913 C C . SER A 1 285 ? -44.756 -57.034 84.459 1.00 120.58 ? 285 SER A C 1 ATOM 1914 O O . SER A 1 285 ? -44.165 -57.467 83.467 1.00 151.25 ? 285 SER A O 1 ATOM 1915 C CB . SER A 1 285 ? -43.530 -57.181 86.664 1.00 115.91 ? 285 SER A CB 1 ATOM 1916 O OG . SER A 1 285 ? -42.290 -57.904 86.673 1.00 113.07 ? 285 SER A OG 1 ATOM 1917 N N . LEU A 1 286 ? -45.529 -55.952 84.407 1.00 114.98 ? 286 LEU A N 1 ATOM 1918 C CA . LEU A 1 286 ? -45.265 -54.944 83.380 1.00 111.00 ? 286 LEU A CA 1 ATOM 1919 C C . LEU A 1 286 ? -44.304 -54.084 84.146 1.00 118.98 ? 286 LEU A C 1 ATOM 1920 O O . LEU A 1 286 ? -44.398 -53.981 85.381 1.00 119.24 ? 286 LEU A O 1 ATOM 1921 C CB . LEU A 1 286 ? -46.489 -54.101 82.990 1.00 104.42 ? 286 LEU A CB 1 ATOM 1922 C CG . LEU A 1 286 ? -47.804 -54.595 82.368 1.00 99.68 ? 286 LEU A CG 1 ATOM 1923 C CD1 . LEU A 1 286 ? -48.777 -53.436 82.186 1.00 90.98 ? 286 LEU A CD1 1 ATOM 1924 C CD2 . LEU A 1 286 ? -47.593 -55.335 81.053 1.00 103.68 ? 286 LEU A CD2 1 ATOM 1925 N N . GLU A 1 287 ? -43.348 -53.496 83.455 1.00 127.43 ? 287 GLU A N 1 ATOM 1926 C CA . GLU A 1 287 ? -42.427 -52.640 84.176 1.00 140.29 ? 287 GLU A CA 1 ATOM 1927 C C . GLU A 1 287 ? -42.491 -51.230 83.595 1.00 137.59 ? 287 GLU A C 1 ATOM 1928 O O . GLU A 1 287 ? -41.878 -50.926 82.577 1.00 166.52 ? 287 GLU A O 1 ATOM 1929 C CB . GLU A 1 287 ? -41.023 -53.265 84.236 1.00 158.52 ? 287 GLU A CB 1 ATOM 1930 C CG . GLU A 1 287 ? -40.822 -54.549 83.419 1.00 193.54 ? 287 GLU A CG 1 ATOM 1931 C CD . GLU A 1 287 ? -40.050 -55.643 84.171 1.00 227.80 ? 287 GLU A CD 1 ATOM 1932 O OE1 . GLU A 1 287 ? -40.212 -55.769 85.412 1.00 251.34 ? 287 GLU A OE1 1 ATOM 1933 O OE2 . GLU A 1 287 ? -39.291 -56.402 83.520 1.00 228.04 ? 287 GLU A OE2 1 ATOM 1934 N N . ILE A 1 288 ? -43.286 -50.377 84.223 1.00 123.41 ? 288 ILE A N 1 ATOM 1935 C CA . ILE A 1 288 ? -43.580 -49.083 83.641 1.00 123.84 ? 288 ILE A CA 1 ATOM 1936 C C . ILE A 1 288 ? -42.538 -48.033 84.008 1.00 138.62 ? 288 ILE A C 1 ATOM 1937 O O . ILE A 1 288 ? -42.293 -47.756 85.182 1.00 152.60 ? 288 ILE A O 1 ATOM 1938 C CB . ILE A 1 288 ? -44.974 -48.586 84.053 1.00 125.18 ? 288 ILE A CB 1 ATOM 1939 C CG1 . ILE A 1 288 ? -46.077 -49.487 83.488 1.00 126.84 ? 288 ILE A CG1 1 ATOM 1940 C CG2 . ILE A 1 288 ? -45.179 -47.157 83.583 1.00 138.64 ? 288 ILE A CG2 1 ATOM 1941 C CD1 . ILE A 1 288 ? -46.323 -49.353 81.996 1.00 132.78 ? 288 ILE A CD1 1 ATOM 1942 N N . SER A 1 289 ? -41.941 -47.433 82.989 1.00 152.91 ? 289 SER A N 1 ATOM 1943 C CA . SER A 1 289 ? -40.945 -46.390 83.194 1.00 162.14 ? 289 SER A CA 1 ATOM 1944 C C . SER A 1 289 ? -41.537 -44.980 83.024 1.00 150.88 ? 289 SER A C 1 ATOM 1945 O O . SER A 1 289 ? -42.712 -44.832 82.690 1.00 134.48 ? 289 SER A O 1 ATOM 1946 C CB . SER A 1 289 ? -39.740 -46.621 82.261 1.00 180.70 ? 289 SER A CB 1 ATOM 1947 O OG . SER A 1 289 ? -40.085 -47.394 81.117 1.00 195.81 ? 289 SER A OG 1 ATOM 1948 N N . PRO A 1 290 ? -40.722 -43.949 83.288 1.00 150.34 ? 290 PRO A N 1 ATOM 1949 C CA . PRO A 1 290 ? -40.905 -42.560 82.964 1.00 144.39 ? 290 PRO A CA 1 ATOM 1950 C C . PRO A 1 290 ? -41.992 -42.302 81.964 1.00 136.78 ? 290 PRO A C 1 ATOM 1951 O O . PRO A 1 290 ? -43.058 -41.885 82.389 1.00 145.33 ? 290 PRO A O 1 ATOM 1952 C CB . PRO A 1 290 ? -39.553 -42.200 82.387 1.00 154.66 ? 290 PRO A CB 1 ATOM 1953 C CG . PRO A 1 290 ? -38.610 -43.059 83.179 1.00 167.90 ? 290 PRO A CG 1 ATOM 1954 C CD . PRO A 1 290 ? -39.409 -44.107 83.912 1.00 160.56 ? 290 PRO A CD 1 ATOM 1955 N N . ILE A 1 291 ? -41.763 -42.536 80.670 1.00 126.01 ? 291 ILE A N 1 ATOM 1956 C CA . ILE A 1 291 ? -42.879 -42.376 79.709 1.00 134.17 ? 291 ILE A CA 1 ATOM 1957 C C . ILE A 1 291 ? -42.961 -43.465 78.620 1.00 133.98 ? 291 ILE A C 1 ATOM 1958 O O . ILE A 1 291 ? -42.344 -43.355 77.568 1.00 144.99 ? 291 ILE A O 1 ATOM 1959 C CB . ILE A 1 291 ? -43.027 -40.913 79.189 1.00 128.10 ? 291 ILE A CB 1 ATOM 1960 C CG1 . ILE A 1 291 ? -44.421 -40.675 78.575 1.00 125.42 ? 291 ILE A CG1 1 ATOM 1961 C CG2 . ILE A 1 291 ? -41.890 -40.532 78.260 1.00 123.08 ? 291 ILE A CG2 1 ATOM 1962 C CD1 . ILE A 1 291 ? -45.056 -39.361 78.998 1.00 124.66 ? 291 ILE A CD1 1 ATOM 1963 N N . THR A 1 292 ? -43.772 -44.489 78.881 1.00 130.38 ? 292 THR A N 1 ATOM 1964 C CA . THR A 1 292 ? -43.638 -45.774 78.199 1.00 133.85 ? 292 THR A CA 1 ATOM 1965 C C . THR A 1 292 ? -44.923 -46.237 77.536 1.00 121.42 ? 292 THR A C 1 ATOM 1966 O O . THR A 1 292 ? -45.899 -46.540 78.224 1.00 106.63 ? 292 THR A O 1 ATOM 1967 C CB . THR A 1 292 ? -43.200 -46.857 79.210 1.00 151.09 ? 292 THR A CB 1 ATOM 1968 O OG1 . THR A 1 292 ? -42.481 -46.239 80.283 1.00 167.26 ? 292 THR A OG1 1 ATOM 1969 C CG2 . THR A 1 292 ? -42.327 -47.940 78.556 1.00 152.78 ? 292 THR A CG2 1 ATOM 1970 N N . PHE A 1 293 ? -44.919 -46.293 76.203 1.00 127.27 ? 293 PHE A N 1 ATOM 1971 C CA . PHE A 1 293 ? -46.042 -46.878 75.467 1.00 131.78 ? 293 PHE A CA 1 ATOM 1972 C C . PHE A 1 293 ? -45.649 -48.266 75.049 1.00 136.29 ? 293 PHE A C 1 ATOM 1973 O O . PHE A 1 293 ? -44.721 -48.473 74.252 1.00 157.39 ? 293 PHE A O 1 ATOM 1974 C CB . PHE A 1 293 ? -46.495 -46.095 74.214 1.00 135.77 ? 293 PHE A CB 1 ATOM 1975 C CG . PHE A 1 293 ? -46.331 -44.609 74.303 1.00 132.37 ? 293 PHE A CG 1 ATOM 1976 C CD1 . PHE A 1 293 ? -46.696 -43.909 75.451 1.00 139.27 ? 293 PHE A CD1 1 ATOM 1977 C CD2 . PHE A 1 293 ? -45.825 -43.910 73.225 1.00 123.39 ? 293 PHE A CD2 1 ATOM 1978 C CE1 . PHE A 1 293 ? -46.529 -42.542 75.533 1.00 139.02 ? 293 PHE A CE1 1 ATOM 1979 C CE2 . PHE A 1 293 ? -45.660 -42.546 73.294 1.00 130.53 ? 293 PHE A CE2 1 ATOM 1980 C CZ . PHE A 1 293 ? -46.014 -41.860 74.448 1.00 144.26 ? 293 PHE A CZ 1 ATOM 1981 N N . LEU A 1 294 ? -46.379 -49.211 75.611 1.00 136.08 ? 294 LEU A N 1 ATOM 1982 C CA . LEU A 1 294 ? -46.241 -50.607 75.291 1.00 134.66 ? 294 LEU A CA 1 ATOM 1983 C C . LEU A 1 294 ? -47.652 -51.151 75.173 1.00 130.97 ? 294 LEU A C 1 ATOM 1984 O O . LEU A 1 294 ? -48.625 -50.547 75.647 1.00 121.80 ? 294 LEU A O 1 ATOM 1985 C CB . LEU A 1 294 ? -45.493 -51.321 76.412 1.00 129.90 ? 294 LEU A CB 1 ATOM 1986 C CG . LEU A 1 294 ? -46.384 -51.829 77.553 1.00 129.06 ? 294 LEU A CG 1 ATOM 1987 C CD1 . LEU A 1 294 ? -46.574 -53.333 77.417 1.00 135.08 ? 294 LEU A CD1 1 ATOM 1988 C CD2 . LEU A 1 294 ? -45.835 -51.479 78.927 1.00 125.57 ? 294 LEU A CD2 1 ATOM 1989 N N . THR A 1 295 ? -47.770 -52.312 74.560 1.00 130.61 ? 295 THR A N 1 ATOM 1990 C CA . THR A 1 295 ? -49.085 -52.852 74.335 1.00 128.80 ? 295 THR A CA 1 ATOM 1991 C C . THR A 1 295 ? -49.082 -54.359 74.668 1.00 128.82 ? 295 THR A C 1 ATOM 1992 O O . THR A 1 295 ? -48.271 -55.132 74.135 1.00 129.80 ? 295 THR A O 1 ATOM 1993 C CB . THR A 1 295 ? -49.598 -52.399 72.937 1.00 131.59 ? 295 THR A CB 1 ATOM 1994 O OG1 . THR A 1 295 ? -50.639 -53.260 72.464 1.00 123.71 ? 295 THR A OG1 1 ATOM 1995 C CG2 . THR A 1 295 ? -48.425 -52.266 71.897 1.00 138.62 ? 295 THR A CG2 1 ATOM 1996 N N . ALA A 1 296 ? -49.951 -54.750 75.607 1.00 124.15 ? 296 ALA A N 1 ATOM 1997 C CA . ALA A 1 296 ? -49.830 -56.054 76.275 1.00 118.32 ? 296 ALA A CA 1 ATOM 1998 C C . ALA A 1 296 ? -51.101 -56.868 76.502 1.00 111.82 ? 296 ALA A C 1 ATOM 1999 O O . ALA A 1 296 ? -52.189 -56.336 76.752 1.00 92.96 ? 296 ALA A O 1 ATOM 2000 C CB . ALA A 1 296 ? -49.072 -55.912 77.591 1.00 123.69 ? 296 ALA A CB 1 ATOM 2001 N N . GLN A 1 297 ? -50.888 -58.182 76.478 1.00 119.14 ? 297 GLN A N 1 ATOM 2002 C CA . GLN A 1 297 ? -51.927 -59.197 76.555 1.00 129.51 ? 297 GLN A CA 1 ATOM 2003 C C . GLN A 1 297 ? -51.998 -60.009 77.877 1.00 139.15 ? 297 GLN A C 1 ATOM 2004 O O . GLN A 1 297 ? -50.964 -60.316 78.485 1.00 143.76 ? 297 GLN A O 1 ATOM 2005 C CB . GLN A 1 297 ? -51.710 -60.144 75.401 1.00 123.83 ? 297 GLN A CB 1 ATOM 2006 C CG . GLN A 1 297 ? -52.744 -61.233 75.351 1.00 143.07 ? 297 GLN A CG 1 ATOM 2007 C CD . GLN A 1 297 ? -52.625 -62.006 74.078 1.00 162.80 ? 297 GLN A CD 1 ATOM 2008 O OE1 . GLN A 1 297 ? -52.048 -61.509 73.090 1.00 155.01 ? 297 GLN A OE1 1 ATOM 2009 N NE2 . GLN A 1 297 ? -53.155 -63.238 74.081 1.00 174.95 ? 297 GLN A NE2 1 ATOM 2010 N N . THR A 1 298 ? -53.213 -60.380 78.302 1.00 138.07 ? 298 THR A N 1 ATOM 2011 C CA . THR A 1 298 ? -53.369 -61.093 79.571 1.00 127.53 ? 298 THR A CA 1 ATOM 2012 C C . THR A 1 298 ? -53.888 -62.506 79.433 1.00 129.59 ? 298 THR A C 1 ATOM 2013 O O . THR A 1 298 ? -53.261 -63.408 79.984 1.00 133.35 ? 298 THR A O 1 ATOM 2014 C CB . THR A 1 298 ? -54.209 -60.322 80.610 1.00 123.07 ? 298 THR A CB 1 ATOM 2015 O OG1 . THR A 1 298 ? -53.856 -58.944 80.563 1.00 126.60 ? 298 THR A OG1 1 ATOM 2016 C CG2 . THR A 1 298 ? -53.918 -60.814 82.015 1.00 111.61 ? 298 THR A CG2 1 ATOM 2017 N N . LEU A 1 299 ? -54.998 -62.730 78.725 1.00 124.97 ? 299 LEU A N 1 ATOM 2018 C CA . LEU A 1 299 ? -55.652 -64.064 78.801 1.00 140.47 ? 299 LEU A CA 1 ATOM 2019 C C . LEU A 1 299 ? -56.029 -64.546 80.224 1.00 144.72 ? 299 LEU A C 1 ATOM 2020 O O . LEU A 1 299 ? -55.191 -65.137 80.945 1.00 144.57 ? 299 LEU A O 1 ATOM 2021 C CB . LEU A 1 299 ? -54.790 -65.168 78.168 1.00 144.02 ? 299 LEU A CB 1 ATOM 2022 C CG . LEU A 1 299 ? -55.005 -66.548 78.838 1.00 133.11 ? 299 LEU A CG 1 ATOM 2023 C CD1 . LEU A 1 299 ? -56.201 -67.267 78.228 1.00 121.65 ? 299 LEU A CD1 1 ATOM 2024 C CD2 . LEU A 1 299 ? -53.747 -67.419 78.851 1.00 136.44 ? 299 LEU A CD2 1 ATOM 2025 N N . LEU A 1 300 ? -57.296 -64.360 80.595 1.00 144.20 ? 300 LEU A N 1 ATOM 2026 C CA . LEU A 1 300 ? -57.745 -64.625 81.966 1.00 134.71 ? 300 LEU A CA 1 ATOM 2027 C C . LEU A 1 300 ? -58.523 -65.893 82.016 1.00 131.86 ? 300 LEU A C 1 ATOM 2028 O O . LEU A 1 300 ? -59.688 -65.900 81.648 1.00 133.49 ? 300 LEU A O 1 ATOM 2029 C CB . LEU A 1 300 ? -58.633 -63.495 82.506 1.00 122.61 ? 300 LEU A CB 1 ATOM 2030 C CG . LEU A 1 300 ? -58.558 -62.242 81.644 1.00 117.36 ? 300 LEU A CG 1 ATOM 2031 C CD1 . LEU A 1 300 ? -59.755 -62.197 80.704 1.00 116.79 ? 300 LEU A CD1 1 ATOM 2032 C CD2 . LEU A 1 300 ? -58.449 -61.001 82.508 1.00 115.93 ? 300 LEU A CD2 1 ATOM 2033 N N . MET A 1 301 ? -57.889 -66.971 82.458 1.00 131.02 ? 301 MET A N 1 ATOM 2034 C CA . MET A 1 301 ? -58.685 -68.072 82.926 1.00 135.48 ? 301 MET A CA 1 ATOM 2035 C C . MET A 1 301 ? -59.114 -67.702 84.307 1.00 142.09 ? 301 MET A C 1 ATOM 2036 O O . MET A 1 301 ? -58.595 -66.735 84.887 1.00 143.52 ? 301 MET A O 1 ATOM 2037 C CB . MET A 1 301 ? -57.918 -69.364 82.978 1.00 134.21 ? 301 MET A CB 1 ATOM 2038 C CG . MET A 1 301 ? -58.352 -70.311 81.890 1.00 140.78 ? 301 MET A CG 1 ATOM 2039 S SD . MET A 1 301 ? -57.376 -70.008 80.420 1.00 153.24 ? 301 MET A SD 1 ATOM 2040 C CE . MET A 1 301 ? -55.788 -69.535 81.152 1.00 137.98 ? 301 MET A CE 1 ATOM 2041 N N . ASP A 1 302 ? -60.071 -68.476 84.818 1.00 146.49 ? 302 ASP A N 1 ATOM 2042 C CA . ASP A 1 302 ? -60.564 -68.338 86.184 1.00 149.86 ? 302 ASP A CA 1 ATOM 2043 C C . ASP A 1 302 ? -61.417 -67.079 86.410 1.00 144.75 ? 302 ASP A C 1 ATOM 2044 O O . ASP A 1 302 ? -60.964 -65.924 86.204 1.00 137.02 ? 302 ASP A O 1 ATOM 2045 C CB . ASP A 1 302 ? -59.399 -68.354 87.185 1.00 157.42 ? 302 ASP A CB 1 ATOM 2046 C CG . ASP A 1 302 ? -58.333 -69.397 86.864 1.00 156.33 ? 302 ASP A CG 1 ATOM 2047 O OD1 . ASP A 1 302 ? -58.511 -70.239 85.945 1.00 157.06 ? 302 ASP A OD1 1 ATOM 2048 O OD2 . ASP A 1 302 ? -57.305 -69.357 87.573 1.00 153.24 ? 302 ASP A OD2 1 ATOM 2049 N N . LEU A 1 303 ? -62.645 -67.313 86.864 1.00 135.97 ? 303 LEU A N 1 ATOM 2050 C CA . LEU A 1 303 ? -63.558 -66.229 87.180 1.00 133.64 ? 303 LEU A CA 1 ATOM 2051 C C . LEU A 1 303 ? -63.159 -65.563 88.477 1.00 135.56 ? 303 LEU A C 1 ATOM 2052 O O . LEU A 1 303 ? -62.682 -66.232 89.386 1.00 140.23 ? 303 LEU A O 1 ATOM 2053 C CB . LEU A 1 303 ? -64.970 -66.765 87.349 1.00 136.96 ? 303 LEU A CB 1 ATOM 2054 C CG . LEU A 1 303 ? -65.780 -67.295 86.170 1.00 139.01 ? 303 LEU A CG 1 ATOM 2055 C CD1 . LEU A 1 303 ? -65.220 -68.604 85.626 1.00 135.08 ? 303 LEU A CD1 1 ATOM 2056 C CD2 . LEU A 1 303 ? -67.234 -67.447 86.628 1.00 149.44 ? 303 LEU A CD2 1 ATOM 2057 N N . GLY A 1 304 ? -63.376 -64.258 88.581 1.00 141.41 ? 304 GLY A N 1 ATOM 2058 C CA . GLY A 1 304 ? -63.203 -63.575 89.856 1.00 148.72 ? 304 GLY A CA 1 ATOM 2059 C C . GLY A 1 304 ? -62.844 -62.117 89.732 1.00 149.27 ? 304 GLY A C 1 ATOM 2060 O O . GLY A 1 304 ? -63.079 -61.499 88.695 1.00 149.58 ? 304 GLY A O 1 ATOM 2061 N N . GLN A 1 305 ? -62.299 -61.571 90.818 1.00 153.05 ? 305 GLN A N 1 ATOM 2062 C CA . GLN A 1 305 ? -61.791 -60.199 90.867 1.00 149.39 ? 305 GLN A CA 1 ATOM 2063 C C . GLN A 1 305 ? -60.327 -60.263 91.139 1.00 137.55 ? 305 GLN A C 1 ATOM 2064 O O . GLN A 1 305 ? -59.871 -61.100 91.906 1.00 146.94 ? 305 GLN A O 1 ATOM 2065 C CB . GLN A 1 305 ? -62.455 -59.369 91.973 1.00 169.15 ? 305 GLN A CB 1 ATOM 2066 C CG . GLN A 1 305 ? -63.367 -58.258 91.457 1.00 181.58 ? 305 GLN A CG 1 ATOM 2067 C CD . GLN A 1 305 ? -63.993 -57.425 92.563 1.00 181.60 ? 305 GLN A CD 1 ATOM 2068 O OE1 . GLN A 1 305 ? -64.785 -57.922 93.365 1.00 191.26 ? 305 GLN A OE1 1 ATOM 2069 N NE2 . GLN A 1 305 ? -63.657 -56.144 92.595 1.00 176.51 ? 305 GLN A NE2 1 ATOM 2070 N N . PHE A 1 306 ? -59.589 -59.371 90.504 1.00 131.80 ? 306 PHE A N 1 ATOM 2071 C CA . PHE A 1 306 ? -58.144 -59.402 90.573 1.00 138.20 ? 306 PHE A CA 1 ATOM 2072 C C . PHE A 1 306 ? -57.606 -57.980 90.619 1.00 137.04 ? 306 PHE A C 1 ATOM 2073 O O . PHE A 1 306 ? -57.958 -57.127 89.794 1.00 135.19 ? 306 PHE A O 1 ATOM 2074 C CB . PHE A 1 306 ? -57.527 -60.149 89.367 1.00 144.47 ? 306 PHE A CB 1 ATOM 2075 C CG . PHE A 1 306 ? -58.070 -61.544 89.136 1.00 143.31 ? 306 PHE A CG 1 ATOM 2076 C CD1 . PHE A 1 306 ? -57.507 -62.635 89.766 1.00 138.26 ? 306 PHE A CD1 1 ATOM 2077 C CD2 . PHE A 1 306 ? -59.127 -61.762 88.246 1.00 151.15 ? 306 PHE A CD2 1 ATOM 2078 C CE1 . PHE A 1 306 ? -58.004 -63.907 89.531 1.00 142.94 ? 306 PHE A CE1 1 ATOM 2079 C CE2 . PHE A 1 306 ? -59.629 -63.033 88.010 1.00 138.32 ? 306 PHE A CE2 1 ATOM 2080 C CZ . PHE A 1 306 ? -59.066 -64.102 88.652 1.00 140.34 ? 306 PHE A CZ 1 ATOM 2081 N N . LEU A 1 307 ? -56.732 -57.739 91.582 1.00 134.77 ? 307 LEU A N 1 ATOM 2082 C CA . LEU A 1 307 ? -56.055 -56.473 91.681 1.00 136.16 ? 307 LEU A CA 1 ATOM 2083 C C . LEU A 1 307 ? -54.910 -56.410 90.694 1.00 144.22 ? 307 LEU A C 1 ATOM 2084 O O . LEU A 1 307 ? -54.120 -57.348 90.599 1.00 155.66 ? 307 LEU A O 1 ATOM 2085 C CB . LEU A 1 307 ? -55.484 -56.336 93.079 1.00 134.12 ? 307 LEU A CB 1 ATOM 2086 C CG . LEU A 1 307 ? -54.414 -55.274 93.262 1.00 134.47 ? 307 LEU A CG 1 ATOM 2087 C CD1 . LEU A 1 307 ? -55.009 -53.895 93.000 1.00 139.69 ? 307 LEU A CD1 1 ATOM 2088 C CD2 . LEU A 1 307 ? -53.806 -55.380 94.656 1.00 140.59 ? 307 LEU A CD2 1 ATOM 2089 N N . LEU A 1 308 ? -54.802 -55.314 89.957 1.00 142.70 ? 308 LEU A N 1 ATOM 2090 C CA . LEU A 1 308 ? -53.492 -54.979 89.426 1.00 136.56 ? 308 LEU A CA 1 ATOM 2091 C C . LEU A 1 308 ? -53.063 -53.683 90.086 1.00 139.59 ? 308 LEU A C 1 ATOM 2092 O O . LEU A 1 308 ? -53.912 -52.915 90.566 1.00 138.44 ? 308 LEU A O 1 ATOM 2093 C CB . LEU A 1 308 ? -53.467 -54.917 87.913 1.00 127.77 ? 308 LEU A CB 1 ATOM 2094 C CG . LEU A 1 308 ? -54.026 -53.674 87.257 1.00 139.33 ? 308 LEU A CG 1 ATOM 2095 C CD1 . LEU A 1 308 ? -53.639 -53.760 85.799 1.00 147.44 ? 308 LEU A CD1 1 ATOM 2096 C CD2 . LEU A 1 308 ? -55.535 -53.536 87.438 1.00 136.47 ? 308 LEU A CD2 1 ATOM 2097 N N . PHE A 1 309 ? -51.749 -53.460 90.124 1.00 139.57 ? 309 PHE A N 1 ATOM 2098 C CA . PHE A 1 309 ? -51.141 -52.463 91.017 1.00 146.77 ? 309 PHE A CA 1 ATOM 2099 C C . PHE A 1 309 ? -49.634 -52.392 90.824 1.00 151.16 ? 309 PHE A C 1 ATOM 2100 O O . PHE A 1 309 ? -49.079 -53.017 89.921 1.00 163.51 ? 309 PHE A O 1 ATOM 2101 C CB . PHE A 1 309 ? -51.351 -52.906 92.438 1.00 143.43 ? 309 PHE A CB 1 ATOM 2102 C CG . PHE A 1 309 ? -50.736 -54.237 92.720 1.00 148.11 ? 309 PHE A CG 1 ATOM 2103 C CD1 . PHE A 1 309 ? -51.286 -55.394 92.183 1.00 146.93 ? 309 PHE A CD1 1 ATOM 2104 C CD2 . PHE A 1 309 ? -49.581 -54.333 93.475 1.00 154.82 ? 309 PHE A CD2 1 ATOM 2105 C CE1 . PHE A 1 309 ? -50.721 -56.627 92.423 1.00 152.04 ? 309 PHE A CE1 1 ATOM 2106 C CE2 . PHE A 1 309 ? -49.010 -55.567 93.727 1.00 158.96 ? 309 PHE A CE2 1 ATOM 2107 C CZ . PHE A 1 309 ? -49.581 -56.715 93.199 1.00 157.61 ? 309 PHE A CZ 1 ATOM 2108 N N . CYS A 1 310 ? -48.965 -51.686 91.726 1.00 140.89 ? 310 CYS A N 1 ATOM 2109 C CA . CYS A 1 310 ? -47.545 -51.457 91.581 1.00 140.75 ? 310 CYS A CA 1 ATOM 2110 C C . CYS A 1 310 ? -46.796 -51.997 92.809 1.00 141.31 ? 310 CYS A C 1 ATOM 2111 O O . CYS A 1 310 ? -47.033 -51.546 93.926 1.00 138.27 ? 310 CYS A O 1 ATOM 2112 C CB . CYS A 1 310 ? -47.353 -49.962 91.343 1.00 148.78 ? 310 CYS A CB 1 ATOM 2113 S SG . CYS A 1 310 ? -45.705 -49.237 91.417 1.00 162.94 ? 310 CYS A SG 1 ATOM 2114 N N . HIS A 1 311 ? -45.919 -52.983 92.591 1.00 145.88 ? 311 HIS A N 1 ATOM 2115 C CA . HIS A 1 311 ? -45.261 -53.743 93.686 1.00 163.26 ? 311 HIS A CA 1 ATOM 2116 C C . HIS A 1 311 ? -44.280 -52.923 94.522 1.00 171.89 ? 311 HIS A C 1 ATOM 2117 O O . HIS A 1 311 ? -44.103 -53.173 95.717 1.00 187.70 ? 311 HIS A O 1 ATOM 2118 C CB . HIS A 1 311 ? -44.522 -54.993 93.154 1.00 163.02 ? 311 HIS A CB 1 ATOM 2119 C CG . HIS A 1 311 ? -44.501 -56.160 94.112 1.00 168.00 ? 311 HIS A CG 1 ATOM 2120 N ND1 . HIS A 1 311 ? -44.230 -56.030 95.459 1.00 165.36 ? 311 HIS A ND1 1 ATOM 2121 C CD2 . HIS A 1 311 ? -44.703 -57.486 93.902 1.00 169.30 ? 311 HIS A CD2 1 ATOM 2122 C CE1 . HIS A 1 311 ? -44.278 -57.218 96.037 1.00 165.27 ? 311 HIS A CE1 1 ATOM 2123 N NE2 . HIS A 1 311 ? -44.561 -58.120 95.114 1.00 165.51 ? 311 HIS A NE2 1 ATOM 2124 N N . ILE A 1 312 ? -43.632 -51.959 93.887 1.00 165.81 ? 312 ILE A N 1 ATOM 2125 C CA . ILE A 1 312 ? -42.555 -51.206 94.514 1.00 160.94 ? 312 ILE A CA 1 ATOM 2126 C C . ILE A 1 312 ? -42.985 -50.607 95.865 1.00 162.68 ? 312 ILE A C 1 ATOM 2127 O O . ILE A 1 312 ? -44.152 -50.245 96.041 1.00 157.08 ? 312 ILE A O 1 ATOM 2128 C CB . ILE A 1 312 ? -42.049 -50.129 93.543 1.00 156.03 ? 312 ILE A CB 1 ATOM 2129 C CG1 . ILE A 1 312 ? -43.177 -49.122 93.272 1.00 138.53 ? 312 ILE A CG1 1 ATOM 2130 C CG2 . ILE A 1 312 ? -41.478 -50.782 92.269 1.00 139.37 ? 312 ILE A CG2 1 ATOM 2131 C CD1 . ILE A 1 312 ? -42.801 -48.032 92.310 1.00 134.28 ? 312 ILE A CD1 1 ATOM 2132 N N . SER A 1 313 ? -42.031 -50.503 96.794 1.00 167.26 ? 313 SER A N 1 ATOM 2133 C CA . SER A 1 313 ? -42.282 -50.225 98.234 1.00 179.02 ? 313 SER A CA 1 ATOM 2134 C C . SER A 1 313 ? -43.043 -48.952 98.677 1.00 180.97 ? 313 SER A C 1 ATOM 2135 O O . SER A 1 313 ? -44.093 -49.032 99.331 1.00 170.09 ? 313 SER A O 1 ATOM 2136 C CB . SER A 1 313 ? -40.966 -50.329 99.019 1.00 181.30 ? 313 SER A CB 1 ATOM 2137 O OG . SER A 1 313 ? -40.526 -51.671 99.082 1.00 180.25 ? 313 SER A OG 1 ATOM 2138 N N . SER A 1 314 ? -42.498 -47.784 98.359 1.00 184.35 ? 314 SER A N 1 ATOM 2139 C CA . SER A 1 314 ? -43.033 -46.526 98.890 1.00 195.44 ? 314 SER A CA 1 ATOM 2140 C C . SER A 1 314 ? -44.286 -46.031 98.171 1.00 194.85 ? 314 SER A C 1 ATOM 2141 O O . SER A 1 314 ? -44.875 -45.019 98.560 1.00 204.63 ? 314 SER A O 1 ATOM 2142 C CB . SER A 1 314 ? -41.946 -45.446 98.913 1.00 201.09 ? 314 SER A CB 1 ATOM 2143 O OG . SER A 1 314 ? -40.830 -45.843 98.133 1.00 193.67 ? 314 SER A OG 1 ATOM 2144 N N . HIS A 1 315 ? -44.689 -46.755 97.132 1.00 185.63 ? 315 HIS A N 1 ATOM 2145 C CA . HIS A 1 315 ? -45.899 -46.449 96.378 1.00 184.66 ? 315 HIS A CA 1 ATOM 2146 C C . HIS A 1 315 ? -47.108 -47.192 96.949 1.00 192.12 ? 315 HIS A C 1 ATOM 2147 O O . HIS A 1 315 ? -48.256 -46.909 96.579 1.00 194.73 ? 315 HIS A O 1 ATOM 2148 C CB . HIS A 1 315 ? -45.712 -46.863 94.923 1.00 178.90 ? 315 HIS A CB 1 ATOM 2149 C CG . HIS A 1 315 ? -44.624 -46.128 94.217 1.00 173.09 ? 315 HIS A CG 1 ATOM 2150 N ND1 . HIS A 1 315 ? -44.779 -45.625 92.944 1.00 181.88 ? 315 HIS A ND1 1 ATOM 2151 C CD2 . HIS A 1 315 ? -43.364 -45.816 94.594 1.00 173.11 ? 315 HIS A CD2 1 ATOM 2152 C CE1 . HIS A 1 315 ? -43.664 -45.023 92.571 1.00 177.44 ? 315 HIS A CE1 1 ATOM 2153 N NE2 . HIS A 1 315 ? -42.789 -45.126 93.554 1.00 177.61 ? 315 HIS A NE2 1 ATOM 2154 N N . GLN A 1 316 ? -46.836 -48.149 97.838 1.00 190.24 ? 316 GLN A N 1 ATOM 2155 C CA . GLN A 1 316 ? -47.852 -49.027 98.424 1.00 194.35 ? 316 GLN A CA 1 ATOM 2156 C C . GLN A 1 316 ? -49.152 -48.298 98.788 1.00 197.56 ? 316 GLN A C 1 ATOM 2157 O O . GLN A 1 316 ? -50.240 -48.701 98.388 1.00 203.01 ? 316 GLN A O 1 ATOM 2158 C CB . GLN A 1 316 ? -47.267 -49.731 99.649 1.00 199.74 ? 316 GLN A CB 1 ATOM 2159 C CG . GLN A 1 316 ? -48.159 -50.784 100.285 1.00 211.01 ? 316 GLN A CG 1 ATOM 2160 C CD . GLN A 1 316 ? -47.559 -51.329 101.568 1.00 225.96 ? 316 GLN A CD 1 ATOM 2161 O OE1 . GLN A 1 316 ? -46.430 -51.821 101.578 1.00 242.86 ? 316 GLN A OE1 1 ATOM 2162 N NE2 . GLN A 1 316 ? -48.311 -51.244 102.660 1.00 227.03 ? 316 GLN A NE2 1 ATOM 2163 N N . HIS A 1 317 ? -49.035 -47.217 99.541 1.00 197.96 ? 317 HIS A N 1 ATOM 2164 C CA . HIS A 1 317 ? -50.204 -46.465 99.922 1.00 197.07 ? 317 HIS A CA 1 ATOM 2165 C C . HIS A 1 317 ? -50.578 -45.473 98.880 1.00 199.26 ? 317 HIS A C 1 ATOM 2166 O O . HIS A 1 317 ? -51.753 -45.207 98.708 1.00 220.00 ? 317 HIS A O 1 ATOM 2167 C CB . HIS A 1 317 ? -49.976 -45.762 101.233 1.00 211.31 ? 317 HIS A CB 1 ATOM 2168 C CG . HIS A 1 317 ? -50.076 -46.680 102.394 1.00 229.46 ? 317 HIS A CG 1 ATOM 2169 N ND1 . HIS A 1 317 ? -49.427 -47.895 102.427 1.00 230.49 ? 317 HIS A ND1 1 ATOM 2170 C CD2 . HIS A 1 317 ? -50.768 -46.585 103.551 1.00 249.86 ? 317 HIS A CD2 1 ATOM 2171 C CE1 . HIS A 1 317 ? -49.702 -48.504 103.565 1.00 252.62 ? 317 HIS A CE1 1 ATOM 2172 N NE2 . HIS A 1 317 ? -50.513 -47.730 104.266 1.00 266.11 ? 317 HIS A NE2 1 ATOM 2173 N N . ASP A 1 318 ? -49.587 -44.928 98.183 1.00 199.77 ? 318 ASP A N 1 ATOM 2174 C CA . ASP A 1 318 ? -49.841 -43.965 97.108 1.00 207.38 ? 318 ASP A CA 1 ATOM 2175 C C . ASP A 1 318 ? -50.936 -44.425 96.100 1.00 202.67 ? 318 ASP A C 1 ATOM 2176 O O . ASP A 1 318 ? -51.361 -43.651 95.226 1.00 204.87 ? 318 ASP A O 1 ATOM 2177 C CB . ASP A 1 318 ? -48.526 -43.564 96.417 1.00 208.36 ? 318 ASP A CB 1 ATOM 2178 C CG . ASP A 1 318 ? -47.649 -42.650 97.284 1.00 198.93 ? 318 ASP A CG 1 ATOM 2179 O OD1 . ASP A 1 318 ? -47.796 -42.639 98.538 1.00 189.48 ? 318 ASP A OD1 1 ATOM 2180 O OD2 . ASP A 1 318 ? -46.804 -41.944 96.684 1.00 186.05 ? 318 ASP A OD2 1 ATOM 2181 N N . GLY A 1 319 ? -51.378 -45.681 96.242 1.00 183.28 ? 319 GLY A N 1 ATOM 2182 C CA . GLY A 1 319 ? -52.656 -46.146 95.701 1.00 162.76 ? 319 GLY A CA 1 ATOM 2183 C C . GLY A 1 319 ? -52.810 -46.089 94.202 1.00 159.49 ? 319 GLY A C 1 ATOM 2184 O O . GLY A 1 319 ? -53.844 -45.632 93.689 1.00 146.85 ? 319 GLY A O 1 ATOM 2185 N N . MET A 1 320 ? -51.766 -46.521 93.498 1.00 162.84 ? 320 MET A N 1 ATOM 2186 C CA . MET A 1 320 ? -51.933 -46.844 92.094 1.00 164.47 ? 320 MET A CA 1 ATOM 2187 C C . MET A 1 320 ? -52.235 -48.341 91.986 1.00 157.72 ? 320 MET A C 1 ATOM 2188 O O . MET A 1 320 ? -51.369 -49.208 92.210 1.00 154.03 ? 320 MET A O 1 ATOM 2189 C CB . MET A 1 320 ? -50.798 -46.308 91.181 1.00 167.52 ? 320 MET A CB 1 ATOM 2190 C CG . MET A 1 320 ? -49.503 -47.102 91.061 1.00 166.67 ? 320 MET A CG 1 ATOM 2191 S SD . MET A 1 320 ? -49.069 -47.562 89.349 1.00 151.94 ? 320 MET A SD 1 ATOM 2192 C CE . MET A 1 320 ? -48.956 -45.999 88.484 1.00 145.43 ? 320 MET A CE 1 ATOM 2193 N N . GLU A 1 321 ? -53.519 -48.603 91.723 1.00 147.61 ? 321 GLU A N 1 ATOM 2194 C CA . GLU A 1 321 ? -54.131 -49.933 91.706 1.00 137.93 ? 321 GLU A CA 1 ATOM 2195 C C . GLU A 1 321 ? -55.630 -49.825 91.461 1.00 138.21 ? 321 GLU A C 1 ATOM 2196 O O . GLU A 1 321 ? -56.271 -48.857 91.867 1.00 142.68 ? 321 GLU A O 1 ATOM 2197 C CB . GLU A 1 321 ? -53.917 -50.661 93.031 1.00 137.67 ? 321 GLU A CB 1 ATOM 2198 C CG . GLU A 1 321 ? -53.588 -49.747 94.204 1.00 156.66 ? 321 GLU A CG 1 ATOM 2199 C CD . GLU A 1 321 ? -53.789 -50.409 95.553 1.00 174.75 ? 321 GLU A CD 1 ATOM 2200 O OE1 . GLU A 1 321 ? -54.731 -51.215 95.704 1.00 175.65 ? 321 GLU A OE1 1 ATOM 2201 O OE2 . GLU A 1 321 ? -53.007 -50.108 96.479 1.00 204.15 ? 321 GLU A OE2 1 ATOM 2202 N N . ALA A 1 322 ? -56.181 -50.813 90.771 1.00 135.70 ? 322 ALA A N 1 ATOM 2203 C CA . ALA A 1 322 ? -57.622 -51.050 90.776 1.00 133.38 ? 322 ALA A CA 1 ATOM 2204 C C . ALA A 1 322 ? -57.891 -52.518 90.419 1.00 134.96 ? 322 ALA A C 1 ATOM 2205 O O . ALA A 1 322 ? -56.960 -53.303 90.080 1.00 111.53 ? 322 ALA A O 1 ATOM 2206 C CB . ALA A 1 322 ? -58.385 -50.077 89.868 1.00 115.86 ? 322 ALA A CB 1 ATOM 2207 N N . TYR A 1 323 ? -59.167 -52.882 90.540 1.00 142.26 ? 323 TYR A N 1 ATOM 2208 C CA . TYR A 1 323 ? -59.619 -54.258 90.350 1.00 146.89 ? 323 TYR A CA 1 ATOM 2209 C C . TYR A 1 323 ? -60.000 -54.557 88.862 1.00 138.90 ? 323 TYR A C 1 ATOM 2210 O O . TYR A 1 323 ? -60.581 -53.706 88.182 1.00 134.47 ? 323 TYR A O 1 ATOM 2211 C CB . TYR A 1 323 ? -60.801 -54.566 91.314 1.00 154.36 ? 323 TYR A CB 1 ATOM 2212 C CG . TYR A 1 323 ? -60.498 -54.919 92.800 1.00 166.23 ? 323 TYR A CG 1 ATOM 2213 C CD1 . TYR A 1 323 ? -59.423 -55.740 93.166 1.00 172.78 ? 323 TYR A CD1 1 ATOM 2214 C CD2 . TYR A 1 323 ? -61.350 -54.483 93.830 1.00 176.63 ? 323 TYR A CD2 1 ATOM 2215 C CE1 . TYR A 1 323 ? -59.183 -56.069 94.500 1.00 176.49 ? 323 TYR A CE1 1 ATOM 2216 C CE2 . TYR A 1 323 ? -61.120 -54.812 95.164 1.00 183.62 ? 323 TYR A CE2 1 ATOM 2217 C CZ . TYR A 1 323 ? -60.033 -55.601 95.491 1.00 188.57 ? 323 TYR A CZ 1 ATOM 2218 O OH . TYR A 1 323 ? -59.800 -55.932 96.806 1.00 212.96 ? 323 TYR A OH 1 ATOM 2219 N N . VAL A 1 324 ? -59.638 -55.748 88.366 1.00 129.70 ? 324 VAL A N 1 ATOM 2220 C CA . VAL A 1 324 ? -60.146 -56.296 87.094 1.00 120.22 ? 324 VAL A CA 1 ATOM 2221 C C . VAL A 1 324 ? -61.009 -57.494 87.391 1.00 126.66 ? 324 VAL A C 1 ATOM 2222 O O . VAL A 1 324 ? -60.551 -58.414 88.059 1.00 130.84 ? 324 VAL A O 1 ATOM 2223 C CB . VAL A 1 324 ? -59.040 -56.931 86.254 1.00 113.24 ? 324 VAL A CB 1 ATOM 2224 C CG1 . VAL A 1 324 ? -59.624 -57.520 84.977 1.00 105.67 ? 324 VAL A CG1 1 ATOM 2225 C CG2 . VAL A 1 324 ? -57.955 -55.927 85.959 1.00 125.39 ? 324 VAL A CG2 1 ATOM 2226 N N . LYS A 1 325 ? -62.234 -57.526 86.886 1.00 133.50 ? 325 LYS A N 1 ATOM 2227 C CA . LYS A 1 325 ? -63.035 -58.720 87.110 1.00 136.88 ? 325 LYS A CA 1 ATOM 2228 C C . LYS A 1 325 ? -63.174 -59.567 85.840 1.00 130.74 ? 325 LYS A C 1 ATOM 2229 O O . LYS A 1 325 ? -62.758 -59.145 84.763 1.00 128.03 ? 325 LYS A O 1 ATOM 2230 C CB . LYS A 1 325 ? -64.338 -58.396 87.872 1.00 149.72 ? 325 LYS A CB 1 ATOM 2231 C CG . LYS A 1 325 ? -65.641 -58.294 87.102 1.00 165.31 ? 325 LYS A CG 1 ATOM 2232 C CD . LYS A 1 325 ? -66.816 -58.248 88.086 1.00 176.89 ? 325 LYS A CD 1 ATOM 2233 C CE . LYS A 1 325 ? -67.100 -59.579 88.795 1.00 175.08 ? 325 LYS A CE 1 ATOM 2234 N NZ . LYS A 1 325 ? -68.095 -60.423 88.072 1.00 176.33 ? 325 LYS A NZ 1 ATOM 2235 N N . VAL A 1 326 ? -63.689 -60.783 85.978 1.00 126.63 ? 326 VAL A N 1 ATOM 2236 C CA . VAL A 1 326 ? -63.732 -61.706 84.851 1.00 127.15 ? 326 VAL A CA 1 ATOM 2237 C C . VAL A 1 326 ? -64.832 -62.761 85.022 1.00 127.31 ? 326 VAL A C 1 ATOM 2238 O O . VAL A 1 326 ? -64.535 -63.880 85.404 1.00 130.65 ? 326 VAL A O 1 ATOM 2239 C CB . VAL A 1 326 ? -62.306 -62.319 84.547 1.00 128.70 ? 326 VAL A CB 1 ATOM 2240 C CG1 . VAL A 1 326 ? -61.586 -62.812 85.792 1.00 126.33 ? 326 VAL A CG1 1 ATOM 2241 C CG2 . VAL A 1 326 ? -62.357 -63.445 83.520 1.00 137.61 ? 326 VAL A CG2 1 ATOM 2242 N N . ASP A 1 327 ? -66.096 -62.427 84.757 1.00 129.89 ? 327 ASP A N 1 ATOM 2243 C CA . ASP A 1 327 ? -67.130 -63.481 84.751 1.00 147.89 ? 327 ASP A CA 1 ATOM 2244 C C . ASP A 1 327 ? -67.478 -63.874 83.295 1.00 136.79 ? 327 ASP A C 1 ATOM 2245 O O . ASP A 1 327 ? -67.069 -63.195 82.386 1.00 130.33 ? 327 ASP A O 1 ATOM 2246 C CB . ASP A 1 327 ? -68.357 -63.146 85.655 1.00 183.18 ? 327 ASP A CB 1 ATOM 2247 C CG . ASP A 1 327 ? -68.643 -64.258 86.765 1.00 223.56 ? 327 ASP A CG 1 ATOM 2248 O OD1 . ASP A 1 327 ? -67.907 -64.326 87.795 1.00 215.26 ? 327 ASP A OD1 1 ATOM 2249 O OD2 . ASP A 1 327 ? -69.610 -65.063 86.613 1.00 239.94 ? 327 ASP A OD2 1 ATOM 2250 N N . SER A 1 328 ? -68.182 -64.989 83.088 1.00 146.23 ? 328 SER A N 1 ATOM 2251 C CA . SER A 1 328 ? -68.419 -65.583 81.756 1.00 155.14 ? 328 SER A CA 1 ATOM 2252 C C . SER A 1 328 ? -69.385 -64.793 80.894 1.00 166.20 ? 328 SER A C 1 ATOM 2253 O O . SER A 1 328 ? -70.556 -64.636 81.246 1.00 178.95 ? 328 SER A O 1 ATOM 2254 C CB . SER A 1 328 ? -68.990 -67.004 81.888 1.00 162.76 ? 328 SER A CB 1 ATOM 2255 O OG . SER A 1 328 ? -68.062 -67.915 82.439 1.00 167.21 ? 328 SER A OG 1 ATOM 2256 N N . CYS A 1 329 ? -68.912 -64.325 79.747 1.00 173.15 ? 329 CYS A N 1 ATOM 2257 C CA . CYS A 1 329 ? -69.797 -63.702 78.783 1.00 184.38 ? 329 CYS A CA 1 ATOM 2258 C C . CYS A 1 329 ? -70.545 -64.815 78.084 1.00 196.12 ? 329 CYS A C 1 ATOM 2259 O O . CYS A 1 329 ? -70.044 -65.939 77.979 1.00 191.07 ? 329 CYS A O 1 ATOM 2260 C CB . CYS A 1 329 ? -69.004 -62.882 77.771 1.00 193.96 ? 329 CYS A CB 1 ATOM 2261 S SG . CYS A 1 329 ? -67.889 -61.682 78.547 1.00 228.16 ? 329 CYS A SG 1 ATOM 2262 N N . PRO A 1 330 ? -71.773 -64.533 77.648 1.00 213.56 ? 330 PRO A N 1 ATOM 2263 C CA . PRO A 1 330 ? -72.315 -65.469 76.688 1.00 224.65 ? 330 PRO A CA 1 ATOM 2264 C C . PRO A 1 330 ? -71.737 -65.109 75.308 1.00 231.93 ? 330 PRO A C 1 ATOM 2265 O O . PRO A 1 330 ? -71.371 -63.946 75.078 1.00 216.75 ? 330 PRO A O 1 ATOM 2266 C CB . PRO A 1 330 ? -73.834 -65.230 76.774 1.00 235.52 ? 330 PRO A CB 1 ATOM 2267 C CG . PRO A 1 330 ? -74.051 -64.381 77.993 1.00 231.34 ? 330 PRO A CG 1 ATOM 2268 C CD . PRO A 1 330 ? -72.788 -63.584 78.131 1.00 224.65 ? 330 PRO A CD 1 ATOM 2269 N N . GLU A 1 331 ? -71.651 -66.108 74.424 1.00 243.10 ? 331 GLU A N 1 ATOM 2270 C CA . GLU A 1 331 ? -71.004 -66.024 73.091 1.00 246.76 ? 331 GLU A CA 1 ATOM 2271 C C . GLU A 1 331 ? -71.979 -65.916 71.895 1.00 262.73 ? 331 GLU A C 1 ATOM 2272 O O . GLU A 1 331 ? -71.756 -65.136 70.958 1.00 238.08 ? 331 GLU A O 1 ATOM 2273 C CB . GLU A 1 331 ? -70.069 -67.230 72.882 1.00 240.40 ? 331 GLU A CB 1 ATOM 2274 C CG . GLU A 1 331 ? -70.349 -68.470 73.746 1.00 244.13 ? 331 GLU A CG 1 ATOM 2275 C CD . GLU A 1 331 ? -71.832 -68.776 73.982 1.00 243.76 ? 331 GLU A CD 1 ATOM 2276 O OE1 . GLU A 1 331 ? -72.533 -69.246 73.052 1.00 236.59 ? 331 GLU A OE1 1 ATOM 2277 O OE2 . GLU A 1 331 ? -72.297 -68.552 75.121 1.00 237.85 ? 331 GLU A OE2 1 ATOM 2278 N N . GLU A 1 332 ? -73.031 -66.738 71.931 1.00 306.12 ? 332 GLU A N 1 ATOM 2279 C CA . GLU A 1 332 ? -74.160 -66.695 70.988 1.00 332.53 ? 332 GLU A CA 1 ATOM 2280 C C . GLU A 1 332 ? -75.441 -67.043 71.783 1.00 341.80 ? 332 GLU A C 1 ATOM 2281 O O . GLU A 1 332 ? -75.913 -68.185 71.721 1.00 350.39 ? 332 GLU A O 1 ATOM 2282 C CB . GLU A 1 332 ? -73.942 -67.687 69.825 1.00 318.62 ? 332 GLU A CB 1 ATOM 2283 C CG . GLU A 1 332 ? -74.883 -67.522 68.631 1.00 298.77 ? 332 GLU A CG 1 ATOM 2284 C CD . GLU A 1 332 ? -74.275 -66.728 67.483 1.00 285.10 ? 332 GLU A CD 1 ATOM 2285 O OE1 . GLU A 1 332 ? -73.367 -65.890 67.714 1.00 267.01 ? 332 GLU A OE1 1 ATOM 2286 O OE2 . GLU A 1 332 ? -74.717 -66.948 66.335 1.00 279.27 ? 332 GLU A OE2 1 ATOM 2287 N N . PRO A 1 333 ? -76.005 -66.058 72.533 1.00 326.32 ? 333 PRO A N 1 ATOM 2288 C CA . PRO A 1 333 ? -77.037 -66.375 73.524 1.00 301.38 ? 333 PRO A CA 1 ATOM 2289 C C . PRO A 1 333 ? -78.414 -66.545 72.902 1.00 300.77 ? 333 PRO A C 1 ATOM 2290 O O . PRO A 1 333 ? -79.159 -67.431 73.314 1.00 320.48 ? 333 PRO A O 1 ATOM 2291 C CB . PRO A 1 333 ? -77.020 -65.153 74.444 1.00 285.06 ? 333 PRO A CB 1 ATOM 2292 C CG . PRO A 1 333 ? -76.620 -64.025 73.551 1.00 292.13 ? 333 PRO A CG 1 ATOM 2293 C CD . PRO A 1 333 ? -75.824 -64.596 72.400 1.00 315.64 ? 333 PRO A CD 1 ATOM 2294 N N . LYS A 1 377 ? -39.829 -88.414 78.198 1.00 178.02 ? 377 LYS A N 1 ATOM 2295 C CA . LYS A 1 377 ? -40.720 -87.511 77.464 1.00 182.82 ? 377 LYS A CA 1 ATOM 2296 C C . LYS A 1 377 ? -41.951 -87.081 78.292 1.00 180.95 ? 377 LYS A C 1 ATOM 2297 O O . LYS A 1 377 ? -42.289 -85.881 78.343 1.00 171.02 ? 377 LYS A O 1 ATOM 2298 C CB . LYS A 1 377 ? -41.116 -88.124 76.104 1.00 183.46 ? 377 LYS A CB 1 ATOM 2299 C CG . LYS A 1 377 ? -41.637 -89.568 76.133 1.00 176.51 ? 377 LYS A CG 1 ATOM 2300 C CD . LYS A 1 377 ? -41.555 -90.280 74.776 1.00 185.16 ? 377 LYS A CD 1 ATOM 2301 C CE . LYS A 1 377 ? -42.200 -89.523 73.610 1.00 185.54 ? 377 LYS A CE 1 ATOM 2302 N NZ . LYS A 1 377 ? -41.519 -88.237 73.243 1.00 176.58 ? 377 LYS A NZ 1 ATOM 2303 N N . HIS A 1 378 ? -42.592 -88.076 78.927 1.00 177.61 ? 378 HIS A N 1 ATOM 2304 C CA . HIS A 1 378 ? -43.714 -87.916 79.868 1.00 161.06 ? 378 HIS A CA 1 ATOM 2305 C C . HIS A 1 378 ? -43.236 -87.226 81.121 1.00 150.73 ? 378 HIS A C 1 ATOM 2306 O O . HIS A 1 378 ? -42.289 -87.698 81.734 1.00 170.82 ? 378 HIS A O 1 ATOM 2307 C CB . HIS A 1 378 ? -44.249 -89.281 80.290 1.00 165.94 ? 378 HIS A CB 1 ATOM 2308 C CG . HIS A 1 378 ? -44.852 -90.061 79.172 1.00 190.39 ? 378 HIS A CG 1 ATOM 2309 N ND1 . HIS A 1 378 ? -46.121 -89.816 78.695 1.00 196.55 ? 378 HIS A ND1 1 ATOM 2310 C CD2 . HIS A 1 378 ? -44.359 -91.078 78.428 1.00 210.27 ? 378 HIS A CD2 1 ATOM 2311 C CE1 . HIS A 1 378 ? -46.387 -90.648 77.704 1.00 210.37 ? 378 HIS A CE1 1 ATOM 2312 N NE2 . HIS A 1 378 ? -45.334 -91.426 77.524 1.00 229.69 ? 378 HIS A NE2 1 ATOM 2313 N N . PRO A 1 379 ? -43.921 -86.152 81.544 1.00 134.24 ? 379 PRO A N 1 ATOM 2314 C CA . PRO A 1 379 ? -43.473 -85.194 82.577 1.00 126.83 ? 379 PRO A CA 1 ATOM 2315 C C . PRO A 1 379 ? -43.099 -85.821 83.918 1.00 124.34 ? 379 PRO A C 1 ATOM 2316 O O . PRO A 1 379 ? -43.589 -86.891 84.252 1.00 129.24 ? 379 PRO A O 1 ATOM 2317 C CB . PRO A 1 379 ? -44.692 -84.294 82.758 1.00 126.15 ? 379 PRO A CB 1 ATOM 2318 C CG . PRO A 1 379 ? -45.844 -85.157 82.361 1.00 126.96 ? 379 PRO A CG 1 ATOM 2319 C CD . PRO A 1 379 ? -45.336 -85.956 81.202 1.00 128.50 ? 379 PRO A CD 1 ATOM 2320 N N . LYS A 1 380 ? -42.250 -85.161 84.691 1.00 125.69 ? 380 LYS A N 1 ATOM 2321 C CA . LYS A 1 380 ? -41.799 -85.750 85.948 1.00 147.11 ? 380 LYS A CA 1 ATOM 2322 C C . LYS A 1 380 ? -42.484 -85.125 87.159 1.00 144.65 ? 380 LYS A C 1 ATOM 2323 O O . LYS A 1 380 ? -43.030 -84.013 87.083 1.00 134.49 ? 380 LYS A O 1 ATOM 2324 C CB . LYS A 1 380 ? -40.280 -85.594 86.086 1.00 180.60 ? 380 LYS A CB 1 ATOM 2325 C CG . LYS A 1 380 ? -39.596 -86.609 87.007 1.00 213.79 ? 380 LYS A CG 1 ATOM 2326 C CD . LYS A 1 380 ? -38.479 -85.971 87.842 1.00 228.66 ? 380 LYS A CD 1 ATOM 2327 C CE . LYS A 1 380 ? -37.250 -85.569 87.028 1.00 214.09 ? 380 LYS A CE 1 ATOM 2328 N NZ . LYS A 1 380 ? -36.441 -86.742 86.597 1.00 222.03 ? 380 LYS A NZ 1 ATOM 2329 N N . THR A 1 381 ? -42.440 -85.848 88.277 1.00 143.29 ? 381 THR A N 1 ATOM 2330 C CA . THR A 1 381 ? -42.773 -85.266 89.581 1.00 136.53 ? 381 THR A CA 1 ATOM 2331 C C . THR A 1 381 ? -41.511 -84.905 90.424 1.00 132.52 ? 381 THR A C 1 ATOM 2332 O O . THR A 1 381 ? -40.856 -85.737 91.064 1.00 128.82 ? 381 THR A O 1 ATOM 2333 C CB . THR A 1 381 ? -43.796 -86.130 90.340 1.00 135.36 ? 381 THR A CB 1 ATOM 2334 O OG1 . THR A 1 381 ? -44.768 -86.626 89.411 1.00 143.30 ? 381 THR A OG1 1 ATOM 2335 C CG2 . THR A 1 381 ? -44.497 -85.316 91.425 1.00 122.10 ? 381 THR A CG2 1 ATOM 2336 N N . TRP A 1 382 ? -41.171 -83.631 90.385 1.00 132.55 ? 382 TRP A N 1 ATOM 2337 C CA . TRP A 1 382 ? -40.010 -83.123 91.069 1.00 138.19 ? 382 TRP A CA 1 ATOM 2338 C C . TRP A 1 382 ? -40.276 -82.989 92.568 1.00 141.92 ? 382 TRP A C 1 ATOM 2339 O O . TRP A 1 382 ? -41.102 -82.168 92.981 1.00 148.28 ? 382 TRP A O 1 ATOM 2340 C CB . TRP A 1 382 ? -39.648 -81.774 90.448 1.00 143.22 ? 382 TRP A CB 1 ATOM 2341 C CG . TRP A 1 382 ? -38.716 -81.913 89.302 1.00 146.69 ? 382 TRP A CG 1 ATOM 2342 C CD1 . TRP A 1 382 ? -38.996 -82.401 88.064 1.00 136.43 ? 382 TRP A CD1 1 ATOM 2343 C CD2 . TRP A 1 382 ? -37.332 -81.576 89.302 1.00 165.47 ? 382 TRP A CD2 1 ATOM 2344 N NE1 . TRP A 1 382 ? -37.873 -82.385 87.288 1.00 137.31 ? 382 TRP A NE1 1 ATOM 2345 C CE2 . TRP A 1 382 ? -36.832 -81.885 88.028 1.00 164.60 ? 382 TRP A CE2 1 ATOM 2346 C CE3 . TRP A 1 382 ? -36.457 -81.033 90.266 1.00 193.80 ? 382 TRP A CE3 1 ATOM 2347 C CZ2 . TRP A 1 382 ? -35.485 -81.672 87.682 1.00 207.28 ? 382 TRP A CZ2 1 ATOM 2348 C CZ3 . TRP A 1 382 ? -35.109 -80.816 89.922 1.00 204.48 ? 382 TRP A CZ3 1 ATOM 2349 C CH2 . TRP A 1 382 ? -34.642 -81.134 88.641 1.00 212.21 ? 382 TRP A CH2 1 ATOM 2350 N N . VAL A 1 383 ? -39.573 -83.777 93.383 1.00 137.10 ? 383 VAL A N 1 ATOM 2351 C CA . VAL A 1 383 ? -39.834 -83.784 94.835 1.00 125.27 ? 383 VAL A CA 1 ATOM 2352 C C . VAL A 1 383 ? -38.695 -83.300 95.724 1.00 122.98 ? 383 VAL A C 1 ATOM 2353 O O . VAL A 1 383 ? -37.594 -83.858 95.668 1.00 134.72 ? 383 VAL A O 1 ATOM 2354 C CB . VAL A 1 383 ? -40.222 -85.188 95.289 1.00 118.92 ? 383 VAL A CB 1 ATOM 2355 C CG1 . VAL A 1 383 ? -40.219 -85.291 96.805 1.00 114.13 ? 383 VAL A CG1 1 ATOM 2356 C CG2 . VAL A 1 383 ? -41.576 -85.534 94.711 1.00 120.26 ? 383 VAL A CG2 1 ATOM 2357 N N . HIS A 1 384 ? -38.956 -82.264 96.529 1.00 114.65 ? 384 HIS A N 1 ATOM 2358 C CA . HIS A 1 384 ? -37.995 -81.863 97.557 1.00 123.84 ? 384 HIS A CA 1 ATOM 2359 C C . HIS A 1 384 ? -38.630 -81.708 98.920 1.00 130.16 ? 384 HIS A C 1 ATOM 2360 O O . HIS A 1 384 ? -39.775 -81.250 99.037 1.00 125.21 ? 384 HIS A O 1 ATOM 2361 C CB . HIS A 1 384 ? -37.249 -80.552 97.259 1.00 125.34 ? 384 HIS A CB 1 ATOM 2362 C CG . HIS A 1 384 ? -37.301 -80.101 95.835 1.00 131.09 ? 384 HIS A CG 1 ATOM 2363 N ND1 . HIS A 1 384 ? -37.419 -80.966 94.770 1.00 138.69 ? 384 HIS A ND1 1 ATOM 2364 C CD2 . HIS A 1 384 ? -37.200 -78.863 95.299 1.00 135.70 ? 384 HIS A CD2 1 ATOM 2365 C CE1 . HIS A 1 384 ? -37.420 -80.278 93.641 1.00 137.49 ? 384 HIS A CE1 1 ATOM 2366 N NE2 . HIS A 1 384 ? -37.282 -78.999 93.933 1.00 134.29 ? 384 HIS A NE2 1 ATOM 2367 N N . TYR A 1 385 ? -37.850 -82.078 99.940 1.00 137.10 ? 385 TYR A N 1 ATOM 2368 C CA . TYR A 1 385 ? -38.126 -81.730 101.334 1.00 135.16 ? 385 TYR A CA 1 ATOM 2369 C C . TYR A 1 385 ? -37.250 -80.548 101.770 1.00 136.82 ? 385 TYR A C 1 ATOM 2370 O O . TYR A 1 385 ? -36.004 -80.642 101.821 1.00 130.59 ? 385 TYR A O 1 ATOM 2371 C CB . TYR A 1 385 ? -37.880 -82.903 102.270 1.00 134.18 ? 385 TYR A CB 1 ATOM 2372 C CG . TYR A 1 385 ? -38.306 -84.247 101.753 1.00 137.74 ? 385 TYR A CG 1 ATOM 2373 C CD1 . TYR A 1 385 ? -37.516 -84.926 100.834 1.00 143.34 ? 385 TYR A CD1 1 ATOM 2374 C CD2 . TYR A 1 385 ? -39.475 -84.866 102.216 1.00 139.14 ? 385 TYR A CD2 1 ATOM 2375 C CE1 . TYR A 1 385 ? -37.882 -86.172 100.363 1.00 157.86 ? 385 TYR A CE1 1 ATOM 2376 C CE2 . TYR A 1 385 ? -39.850 -86.120 101.755 1.00 147.69 ? 385 TYR A CE2 1 ATOM 2377 C CZ . TYR A 1 385 ? -39.043 -86.768 100.824 1.00 159.90 ? 385 TYR A CZ 1 ATOM 2378 O OH . TYR A 1 385 ? -39.362 -88.014 100.324 1.00 174.23 ? 385 TYR A OH 1 ATOM 2379 N N . ILE A 1 386 ? -37.925 -79.444 102.088 1.00 126.93 ? 386 ILE A N 1 ATOM 2380 C CA . ILE A 1 386 ? -37.286 -78.168 102.376 1.00 113.49 ? 386 ILE A CA 1 ATOM 2381 C C . ILE A 1 386 ? -37.686 -77.755 103.777 1.00 110.55 ? 386 ILE A C 1 ATOM 2382 O O . ILE A 1 386 ? -38.797 -78.086 104.243 1.00 101.31 ? 386 ILE A O 1 ATOM 2383 C CB . ILE A 1 386 ? -37.723 -77.098 101.349 1.00 113.80 ? 386 ILE A CB 1 ATOM 2384 C CG1 . ILE A 1 386 ? -37.265 -77.501 99.933 1.00 119.63 ? 386 ILE A CG1 1 ATOM 2385 C CG2 . ILE A 1 386 ? -37.186 -75.720 101.718 1.00 109.01 ? 386 ILE A CG2 1 ATOM 2386 C CD1 . ILE A 1 386 ? -38.100 -76.955 98.790 1.00 116.07 ? 386 ILE A CD1 1 ATOM 2387 N N . ALA A 1 387 ? -36.768 -77.047 104.443 1.00 108.17 ? 387 ALA A N 1 ATOM 2388 C CA . ALA A 1 387 ? -36.975 -76.570 105.822 1.00 111.47 ? 387 ALA A CA 1 ATOM 2389 C C . ALA A 1 387 ? -36.688 -75.092 106.022 1.00 109.75 ? 387 ALA A C 1 ATOM 2390 O O . ALA A 1 387 ? -35.808 -74.541 105.365 1.00 123.78 ? 387 ALA A O 1 ATOM 2391 C CB . ALA A 1 387 ? -36.118 -77.365 106.783 1.00 115.20 ? 387 ALA A CB 1 ATOM 2392 N N . ALA A 1 388 ? -37.428 -74.452 106.926 1.00 104.59 ? 388 ALA A N 1 ATOM 2393 C CA . ALA A 1 388 ? -37.038 -73.145 107.416 1.00 109.43 ? 388 ALA A CA 1 ATOM 2394 C C . ALA A 1 388 ? -36.121 -73.471 108.578 1.00 124.84 ? 388 ALA A C 1 ATOM 2395 O O . ALA A 1 388 ? -36.403 -74.408 109.340 1.00 130.66 ? 388 ALA A O 1 ATOM 2396 C CB . ALA A 1 388 ? -38.241 -72.354 107.867 1.00 108.61 ? 388 ALA A CB 1 ATOM 2397 N N . GLU A 1 389 ? -35.024 -72.716 108.690 1.00 136.76 ? 389 GLU A N 1 ATOM 2398 C CA . GLU A 1 389 ? -33.837 -73.125 109.456 1.00 144.02 ? 389 GLU A CA 1 ATOM 2399 C C . GLU A 1 389 ? -33.130 -71.916 110.014 1.00 143.63 ? 389 GLU A C 1 ATOM 2400 O O . GLU A 1 389 ? -32.699 -71.065 109.241 1.00 161.57 ? 389 GLU A O 1 ATOM 2401 C CB . GLU A 1 389 ? -32.847 -73.830 108.516 1.00 152.78 ? 389 GLU A CB 1 ATOM 2402 C CG . GLU A 1 389 ? -31.744 -74.625 109.201 1.00 164.53 ? 389 GLU A CG 1 ATOM 2403 C CD . GLU A 1 389 ? -32.235 -75.967 109.729 1.00 166.98 ? 389 GLU A CD 1 ATOM 2404 O OE1 . GLU A 1 389 ? -32.771 -76.005 110.857 1.00 161.85 ? 389 GLU A OE1 1 ATOM 2405 O OE2 . GLU A 1 389 ? -32.082 -76.987 109.017 1.00 161.26 ? 389 GLU A OE2 1 ATOM 2406 N N . GLU A 1 390 ? -32.973 -71.843 111.332 1.00 135.46 ? 390 GLU A N 1 ATOM 2407 C CA . GLU A 1 390 ? -32.209 -70.746 111.919 1.00 142.12 ? 390 GLU A CA 1 ATOM 2408 C C . GLU A 1 390 ? -30.712 -71.062 112.046 1.00 155.62 ? 390 GLU A C 1 ATOM 2409 O O . GLU A 1 390 ? -30.263 -71.707 112.994 1.00 176.78 ? 390 GLU A O 1 ATOM 2410 C CB . GLU A 1 390 ? -32.790 -70.320 113.257 1.00 143.77 ? 390 GLU A CB 1 ATOM 2411 C CG . GLU A 1 390 ? -34.153 -69.664 113.175 1.00 152.08 ? 390 GLU A CG 1 ATOM 2412 C CD . GLU A 1 390 ? -34.709 -69.332 114.552 1.00 167.87 ? 390 GLU A CD 1 ATOM 2413 O OE1 . GLU A 1 390 ? -33.974 -68.708 115.349 1.00 183.42 ? 390 GLU A OE1 1 ATOM 2414 O OE2 . GLU A 1 390 ? -35.873 -69.688 114.851 1.00 163.82 ? 390 GLU A OE2 1 ATOM 2415 N N . GLU A 1 391 ? -29.954 -70.601 111.061 1.00 158.66 ? 391 GLU A N 1 ATOM 2416 C CA . GLU A 1 391 ? -28.508 -70.674 111.046 1.00 161.92 ? 391 GLU A CA 1 ATOM 2417 C C . GLU A 1 391 ? -28.022 -69.253 111.423 1.00 163.24 ? 391 GLU A C 1 ATOM 2418 O O . GLU A 1 391 ? -28.802 -68.290 111.425 1.00 153.73 ? 391 GLU A O 1 ATOM 2419 C CB . GLU A 1 391 ? -28.079 -71.052 109.617 1.00 173.39 ? 391 GLU A CB 1 ATOM 2420 C CG . GLU A 1 391 ? -26.899 -72.005 109.454 1.00 193.54 ? 391 GLU A CG 1 ATOM 2421 C CD . GLU A 1 391 ? -26.401 -72.105 108.000 1.00 204.34 ? 391 GLU A CD 1 ATOM 2422 O OE1 . GLU A 1 391 ? -26.132 -71.063 107.347 1.00 191.18 ? 391 GLU A OE1 1 ATOM 2423 O OE2 . GLU A 1 391 ? -26.267 -73.241 107.496 1.00 208.54 ? 391 GLU A OE2 1 ATOM 2424 N N . ASP A 1 392 ? -26.753 -69.110 111.776 1.00 164.45 ? 392 ASP A N 1 ATOM 2425 C CA . ASP A 1 392 ? -26.146 -67.783 111.802 1.00 159.71 ? 392 ASP A CA 1 ATOM 2426 C C . ASP A 1 392 ? -25.556 -67.557 110.418 1.00 162.72 ? 392 ASP A C 1 ATOM 2427 O O . ASP A 1 392 ? -25.290 -68.514 109.695 1.00 176.41 ? 392 ASP A O 1 ATOM 2428 C CB . ASP A 1 392 ? -25.055 -67.705 112.867 1.00 167.25 ? 392 ASP A CB 1 ATOM 2429 C CG . ASP A 1 392 ? -25.612 -67.704 114.279 1.00 174.25 ? 392 ASP A CG 1 ATOM 2430 O OD1 . ASP A 1 392 ? -26.851 -67.675 114.434 1.00 183.58 ? 392 ASP A OD1 1 ATOM 2431 O OD2 . ASP A 1 392 ? -24.809 -67.728 115.237 1.00 172.73 ? 392 ASP A OD2 1 ATOM 2432 N N . TRP A 1 393 ? -25.344 -66.308 110.030 1.00 168.47 ? 393 TRP A N 1 ATOM 2433 C CA . TRP A 1 393 ? -24.805 -66.040 108.690 1.00 167.72 ? 393 TRP A CA 1 ATOM 2434 C C . TRP A 1 393 ? -23.609 -65.099 108.697 1.00 171.81 ? 393 TRP A C 1 ATOM 2435 O O . TRP A 1 393 ? -23.581 -64.127 109.465 1.00 169.93 ? 393 TRP A O 1 ATOM 2436 C CB . TRP A 1 393 ? -25.901 -65.481 107.781 1.00 162.24 ? 393 TRP A CB 1 ATOM 2437 C CG . TRP A 1 393 ? -25.523 -65.396 106.344 1.00 154.35 ? 393 TRP A CG 1 ATOM 2438 C CD1 . TRP A 1 393 ? -25.556 -64.285 105.563 1.00 146.06 ? 393 TRP A CD1 1 ATOM 2439 C CD2 . TRP A 1 393 ? -25.051 -66.468 105.508 1.00 161.38 ? 393 TRP A CD2 1 ATOM 2440 N NE1 . TRP A 1 393 ? -25.142 -64.590 104.289 1.00 150.52 ? 393 TRP A NE1 1 ATOM 2441 C CE2 . TRP A 1 393 ? -24.828 -65.923 104.223 1.00 154.05 ? 393 TRP A CE2 1 ATOM 2442 C CE3 . TRP A 1 393 ? -24.799 -67.835 105.719 1.00 176.73 ? 393 TRP A CE3 1 ATOM 2443 C CZ2 . TRP A 1 393 ? -24.362 -66.694 103.145 1.00 150.68 ? 393 TRP A CZ2 1 ATOM 2444 C CZ3 . TRP A 1 393 ? -24.334 -68.605 104.643 1.00 185.77 ? 393 TRP A CZ3 1 ATOM 2445 C CH2 . TRP A 1 393 ? -24.123 -68.025 103.371 1.00 164.96 ? 393 TRP A CH2 1 ATOM 2446 N N . ASP A 1 394 ? -22.627 -65.387 107.842 1.00 170.84 ? 394 ASP A N 1 ATOM 2447 C CA . ASP A 1 394 ? -21.507 -64.461 107.649 1.00 181.81 ? 394 ASP A CA 1 ATOM 2448 C C . ASP A 1 394 ? -21.517 -63.816 106.268 1.00 187.30 ? 394 ASP A C 1 ATOM 2449 O O . ASP A 1 394 ? -21.206 -64.476 105.272 1.00 206.61 ? 394 ASP A O 1 ATOM 2450 C CB . ASP A 1 394 ? -20.156 -65.129 107.898 1.00 175.16 ? 394 ASP A CB 1 ATOM 2451 C CG . ASP A 1 394 ? -19.034 -64.121 108.004 1.00 175.37 ? 394 ASP A CG 1 ATOM 2452 O OD1 . ASP A 1 394 ? -18.828 -63.356 107.037 1.00 162.48 ? 394 ASP A OD1 1 ATOM 2453 O OD2 . ASP A 1 394 ? -18.373 -64.083 109.064 1.00 188.33 ? 394 ASP A OD2 1 ATOM 2454 N N . TYR A 1 395 ? -21.844 -62.523 106.231 1.00 176.24 ? 395 TYR A N 1 ATOM 2455 C CA . TYR A 1 395 ? -21.996 -61.769 104.984 1.00 163.85 ? 395 TYR A CA 1 ATOM 2456 C C . TYR A 1 395 ? -20.659 -61.533 104.249 1.00 167.48 ? 395 TYR A C 1 ATOM 2457 O O . TYR A 1 395 ? -20.612 -61.399 103.018 1.00 167.33 ? 395 TYR A O 1 ATOM 2458 C CB . TYR A 1 395 ? -22.679 -60.431 105.258 1.00 154.71 ? 395 TYR A CB 1 ATOM 2459 C CG . TYR A 1 395 ? -24.179 -60.451 105.530 1.00 151.36 ? 395 TYR A CG 1 ATOM 2460 C CD1 . TYR A 1 395 ? -25.107 -60.545 104.494 1.00 145.93 ? 395 TYR A CD1 1 ATOM 2461 C CD2 . TYR A 1 395 ? -24.670 -60.300 106.824 1.00 162.81 ? 395 TYR A CD2 1 ATOM 2462 C CE1 . TYR A 1 395 ? -26.483 -60.513 104.745 1.00 148.63 ? 395 TYR A CE1 1 ATOM 2463 C CE2 . TYR A 1 395 ? -26.042 -60.274 107.089 1.00 163.13 ? 395 TYR A CE2 1 ATOM 2464 C CZ . TYR A 1 395 ? -26.953 -60.374 106.053 1.00 153.58 ? 395 TYR A CZ 1 ATOM 2465 O OH . TYR A 1 395 ? -28.315 -60.328 106.338 1.00 137.48 ? 395 TYR A OH 1 ATOM 2466 N N . ALA A 1 396 ? -19.569 -61.481 104.998 1.00 167.99 ? 396 ALA A N 1 ATOM 2467 C CA . ALA A 1 396 ? -18.272 -61.319 104.372 1.00 175.53 ? 396 ALA A CA 1 ATOM 2468 C C . ALA A 1 396 ? -17.266 -62.280 104.994 1.00 178.02 ? 396 ALA A C 1 ATOM 2469 O O . ALA A 1 396 ? -16.522 -61.899 105.899 1.00 183.90 ? 396 ALA A O 1 ATOM 2470 C CB . ALA A 1 396 ? -17.805 -59.875 104.477 1.00 187.03 ? 396 ALA A CB 1 ATOM 2471 N N . PRO A 1 397 ? -17.259 -63.537 104.514 1.00 175.99 ? 397 PRO A N 1 ATOM 2472 C CA . PRO A 1 397 ? -16.445 -64.643 105.007 1.00 181.68 ? 397 PRO A CA 1 ATOM 2473 C C . PRO A 1 397 ? -14.988 -64.297 105.223 1.00 182.76 ? 397 PRO A C 1 ATOM 2474 O O . PRO A 1 397 ? -14.675 -63.433 106.041 1.00 192.78 ? 397 PRO A O 1 ATOM 2475 C CB . PRO A 1 397 ? -16.579 -65.685 103.901 1.00 185.33 ? 397 PRO A CB 1 ATOM 2476 C CG . PRO A 1 397 ? -17.964 -65.480 103.424 1.00 192.23 ? 397 PRO A CG 1 ATOM 2477 C CD . PRO A 1 397 ? -18.162 -63.986 103.440 1.00 181.11 ? 397 PRO A CD 1 ATOM 2478 N N . LEU A 1 398 ? -14.100 -64.967 104.503 1.00 180.06 ? 398 LEU A N 1 ATOM 2479 C CA . LEU A 1 398 ? -12.697 -64.909 104.867 1.00 199.66 ? 398 LEU A CA 1 ATOM 2480 C C . LEU A 1 398 ? -12.159 -63.465 104.976 1.00 205.44 ? 398 LEU A C 1 ATOM 2481 O O . LEU A 1 398 ? -11.161 -63.242 105.666 1.00 222.49 ? 398 LEU A O 1 ATOM 2482 C CB . LEU A 1 398 ? -11.819 -65.819 103.965 1.00 207.10 ? 398 LEU A CB 1 ATOM 2483 C CG . LEU A 1 398 ? -11.400 -67.295 104.262 1.00 207.72 ? 398 LEU A CG 1 ATOM 2484 C CD1 . LEU A 1 398 ? -10.673 -67.505 105.597 1.00 205.33 ? 398 LEU A CD1 1 ATOM 2485 C CD2 . LEU A 1 398 ? -12.531 -68.310 104.107 1.00 200.12 ? 398 LEU A CD2 1 ATOM 2486 N N . VAL A 1 399 ? -12.841 -62.484 104.370 1.00 193.94 ? 399 VAL A N 1 ATOM 2487 C CA . VAL A 1 399 ? -12.223 -61.151 104.197 1.00 198.91 ? 399 VAL A CA 1 ATOM 2488 C C . VAL A 1 399 ? -12.529 -60.038 105.233 1.00 199.74 ? 399 VAL A C 1 ATOM 2489 O O . VAL A 1 399 ? -13.646 -59.507 105.309 1.00 178.89 ? 399 VAL A O 1 ATOM 2490 C CB . VAL A 1 399 ? -12.286 -60.660 102.721 1.00 194.82 ? 399 VAL A CB 1 ATOM 2491 C CG1 . VAL A 1 399 ? -13.710 -60.305 102.306 1.00 175.61 ? 399 VAL A CG1 1 ATOM 2492 C CG2 . VAL A 1 399 ? -11.262 -59.546 102.458 1.00 203.83 ? 399 VAL A CG2 1 ATOM 2493 N N . LEU A 1 400 ? -11.490 -59.729 106.021 1.00 215.35 ? 400 LEU A N 1 ATOM 2494 C CA . LEU A 1 400 ? -11.416 -58.572 106.927 1.00 213.43 ? 400 LEU A CA 1 ATOM 2495 C C . LEU A 1 400 ? -10.683 -57.421 106.242 1.00 204.73 ? 400 LEU A C 1 ATOM 2496 O O . LEU A 1 400 ? -9.839 -57.625 105.351 1.00 191.38 ? 400 LEU A O 1 ATOM 2497 C CB . LEU A 1 400 ? -10.637 -58.912 108.219 1.00 224.31 ? 400 LEU A CB 1 ATOM 2498 C CG . LEU A 1 400 ? -11.179 -59.485 109.544 1.00 227.08 ? 400 LEU A CG 1 ATOM 2499 C CD1 . LEU A 1 400 ? -11.402 -60.993 109.459 1.00 217.98 ? 400 LEU A CD1 1 ATOM 2500 C CD2 . LEU A 1 400 ? -10.238 -59.150 110.708 1.00 223.71 ? 400 LEU A CD2 1 ATOM 2501 N N . ALA A 1 401 ? -11.002 -56.211 106.683 1.00 200.84 ? 401 ALA A N 1 ATOM 2502 C CA . ALA A 1 401 ? -10.243 -55.042 106.302 1.00 213.06 ? 401 ALA A CA 1 ATOM 2503 C C . ALA A 1 401 ? -9.990 -54.210 107.546 1.00 229.36 ? 401 ALA A C 1 ATOM 2504 O O . ALA A 1 401 ? -10.344 -53.028 107.579 1.00 216.29 ? 401 ALA A O 1 ATOM 2505 C CB . ALA A 1 401 ? -10.993 -54.241 105.263 1.00 213.97 ? 401 ALA A CB 1 ATOM 2506 N N . PRO A 1 402 ? -9.341 -54.822 108.563 1.00 260.48 ? 402 PRO A N 1 ATOM 2507 C CA . PRO A 1 402 ? -9.225 -54.298 109.928 1.00 286.56 ? 402 PRO A CA 1 ATOM 2508 C C . PRO A 1 402 ? -9.094 -52.778 110.060 1.00 298.26 ? 402 PRO A C 1 ATOM 2509 O O . PRO A 1 402 ? -8.890 -52.073 109.062 1.00 284.72 ? 402 PRO A O 1 ATOM 2510 C CB . PRO A 1 402 ? -7.979 -55.013 110.468 1.00 286.24 ? 402 PRO A CB 1 ATOM 2511 C CG . PRO A 1 402 ? -8.027 -56.337 109.796 1.00 276.10 ? 402 PRO A CG 1 ATOM 2512 C CD . PRO A 1 402 ? -8.518 -56.040 108.399 1.00 269.00 ? 402 PRO A CD 1 ATOM 2513 N N . ASP A 1 403 ? -9.212 -52.307 111.305 1.00 310.71 ? 403 ASP A N 1 ATOM 2514 C CA . ASP A 1 403 ? -9.320 -50.883 111.667 1.00 306.99 ? 403 ASP A CA 1 ATOM 2515 C C . ASP A 1 403 ? -10.601 -50.231 111.156 1.00 309.01 ? 403 ASP A C 1 ATOM 2516 O O . ASP A 1 403 ? -10.988 -50.412 109.997 1.00 301.23 ? 403 ASP A O 1 ATOM 2517 C CB . ASP A 1 403 ? -8.096 -50.071 111.222 1.00 292.96 ? 403 ASP A CB 1 ATOM 2518 C CG . ASP A 1 403 ? -6.823 -50.511 111.904 1.00 283.09 ? 403 ASP A CG 1 ATOM 2519 O OD1 . ASP A 1 403 ? -6.829 -51.596 112.538 1.00 272.74 ? 403 ASP A OD1 1 ATOM 2520 O OD2 . ASP A 1 403 ? -5.820 -49.767 111.797 1.00 273.39 ? 403 ASP A OD2 1 ATOM 2521 N N . ASP A 1 404 ? -11.246 -49.468 112.040 1.00 307.04 ? 404 ASP A N 1 ATOM 2522 C CA . ASP A 1 404 ? -12.429 -48.672 111.697 1.00 282.94 ? 404 ASP A CA 1 ATOM 2523 C C . ASP A 1 404 ? -12.014 -47.486 110.817 1.00 260.04 ? 404 ASP A C 1 ATOM 2524 O O . ASP A 1 404 ? -12.775 -46.538 110.583 1.00 240.13 ? 404 ASP A O 1 ATOM 2525 C CB . ASP A 1 404 ? -13.166 -48.235 112.970 1.00 292.25 ? 404 ASP A CB 1 ATOM 2526 C CG . ASP A 1 404 ? -13.621 -49.423 113.823 1.00 291.42 ? 404 ASP A CG 1 ATOM 2527 O OD1 . ASP A 1 404 ? -14.276 -50.349 113.278 1.00 270.42 ? 404 ASP A OD1 1 ATOM 2528 O OD2 . ASP A 1 404 ? -13.308 -49.432 115.037 1.00 293.91 ? 404 ASP A OD2 1 ATOM 2529 N N . ARG A 1 405 ? -10.773 -47.577 110.349 1.00 249.69 ? 405 ARG A N 1 ATOM 2530 C CA . ARG A 1 405 ? -10.250 -46.793 109.257 1.00 243.89 ? 405 ARG A CA 1 ATOM 2531 C C . ARG A 1 405 ? -11.325 -46.594 108.189 1.00 233.95 ? 405 ARG A C 1 ATOM 2532 O O . ARG A 1 405 ? -11.760 -45.463 107.938 1.00 223.17 ? 405 ARG A O 1 ATOM 2533 C CB . ARG A 1 405 ? -9.019 -47.519 108.661 1.00 251.66 ? 405 ARG A CB 1 ATOM 2534 C CG . ARG A 1 405 ? -9.317 -48.823 107.897 1.00 241.52 ? 405 ARG A CG 1 ATOM 2535 C CD . ARG A 1 405 ? -8.097 -49.608 107.410 1.00 241.18 ? 405 ARG A CD 1 ATOM 2536 N NE . ARG A 1 405 ? -6.874 -48.801 107.323 1.00 258.90 ? 405 ARG A NE 1 ATOM 2537 C CZ . ARG A 1 405 ? -6.269 -48.424 106.195 1.00 251.37 ? 405 ARG A CZ 1 ATOM 2538 N NH1 . ARG A 1 405 ? -6.761 -48.776 105.009 1.00 242.51 ? 405 ARG A NH1 1 ATOM 2539 N NH2 . ARG A 1 405 ? -5.159 -47.690 106.262 1.00 245.44 ? 405 ARG A NH2 1 ATOM 2540 N N . SER A 1 406 ? -11.789 -47.721 107.639 1.00 237.94 ? 406 SER A N 1 ATOM 2541 C CA . SER A 1 406 ? -12.463 -47.810 106.332 1.00 238.14 ? 406 SER A CA 1 ATOM 2542 C C . SER A 1 406 ? -13.867 -47.196 106.253 1.00 227.81 ? 406 SER A C 1 ATOM 2543 O O . SER A 1 406 ? -14.273 -46.361 107.064 1.00 236.93 ? 406 SER A O 1 ATOM 2544 C CB . SER A 1 406 ? -12.515 -49.285 105.848 1.00 232.21 ? 406 SER A CB 1 ATOM 2545 O OG . SER A 1 406 ? -11.233 -49.894 105.695 1.00 228.14 ? 406 SER A OG 1 ATOM 2546 N N . TYR A 1 407 ? -14.583 -47.619 105.227 1.00 212.64 ? 407 TYR A N 1 ATOM 2547 C CA . TYR A 1 407 ? -15.986 -47.353 105.091 1.00 207.16 ? 407 TYR A CA 1 ATOM 2548 C C . TYR A 1 407 ? -16.694 -48.727 105.038 1.00 191.86 ? 407 TYR A C 1 ATOM 2549 O O . TYR A 1 407 ? -17.908 -48.827 105.249 1.00 167.83 ? 407 TYR A O 1 ATOM 2550 C CB . TYR A 1 407 ? -16.198 -46.478 103.846 1.00 226.63 ? 407 TYR A CB 1 ATOM 2551 C CG . TYR A 1 407 ? -17.626 -46.303 103.399 1.00 244.10 ? 407 TYR A CG 1 ATOM 2552 C CD1 . TYR A 1 407 ? -18.682 -46.370 104.315 1.00 250.09 ? 407 TYR A CD1 1 ATOM 2553 C CD2 . TYR A 1 407 ? -17.927 -46.077 102.054 1.00 239.32 ? 407 TYR A CD2 1 ATOM 2554 C CE1 . TYR A 1 407 ? -19.996 -46.227 103.913 1.00 257.43 ? 407 TYR A CE1 1 ATOM 2555 C CE2 . TYR A 1 407 ? -19.240 -45.922 101.640 1.00 251.87 ? 407 TYR A CE2 1 ATOM 2556 C CZ . TYR A 1 407 ? -20.272 -46.000 102.578 1.00 263.65 ? 407 TYR A CZ 1 ATOM 2557 O OH . TYR A 1 407 ? -21.584 -45.852 102.192 1.00 273.06 ? 407 TYR A OH 1 ATOM 2558 N N . LYS A 1 408 ? -15.909 -49.779 104.773 1.00 191.90 ? 408 LYS A N 1 ATOM 2559 C CA . LYS A 1 408 ? -16.372 -51.173 104.885 1.00 188.20 ? 408 LYS A CA 1 ATOM 2560 C C . LYS A 1 408 ? -16.268 -51.665 106.321 1.00 198.78 ? 408 LYS A C 1 ATOM 2561 O O . LYS A 1 408 ? -17.204 -52.270 106.844 1.00 196.70 ? 408 LYS A O 1 ATOM 2562 C CB . LYS A 1 408 ? -15.673 -52.144 103.896 1.00 179.96 ? 408 LYS A CB 1 ATOM 2563 C CG . LYS A 1 408 ? -14.173 -52.417 104.026 1.00 186.87 ? 408 LYS A CG 1 ATOM 2564 C CD . LYS A 1 408 ? -13.764 -53.613 103.157 1.00 181.43 ? 408 LYS A CD 1 ATOM 2565 C CE . LYS A 1 408 ? -12.373 -53.452 102.537 1.00 184.43 ? 408 LYS A CE 1 ATOM 2566 N NZ . LYS A 1 408 ? -11.921 -54.622 101.717 1.00 175.38 ? 408 LYS A NZ 1 ATOM 2567 N N . SER A 1 409 ? -15.127 -51.406 106.953 1.00 215.03 ? 409 SER A N 1 ATOM 2568 C CA . SER A 1 409 ? -14.989 -51.604 108.388 1.00 231.39 ? 409 SER A CA 1 ATOM 2569 C C . SER A 1 409 ? -15.924 -50.578 109.013 1.00 218.95 ? 409 SER A C 1 ATOM 2570 O O . SER A 1 409 ? -15.567 -49.410 109.174 1.00 232.13 ? 409 SER A O 1 ATOM 2571 C CB . SER A 1 409 ? -13.539 -51.380 108.839 1.00 256.03 ? 409 SER A CB 1 ATOM 2572 O OG . SER A 1 409 ? -12.629 -52.268 108.203 1.00 265.27 ? 409 SER A OG 1 ATOM 2573 N N . GLN A 1 410 ? -17.134 -51.019 109.335 1.00 195.66 ? 410 GLN A N 1 ATOM 2574 C CA . GLN A 1 410 ? -18.229 -50.107 109.574 1.00 189.24 ? 410 GLN A CA 1 ATOM 2575 C C . GLN A 1 410 ? -19.524 -50.818 109.227 1.00 185.42 ? 410 GLN A C 1 ATOM 2576 O O . GLN A 1 410 ? -20.553 -50.530 109.830 1.00 189.60 ? 410 GLN A O 1 ATOM 2577 C CB . GLN A 1 410 ? -18.071 -48.898 108.669 1.00 199.39 ? 410 GLN A CB 1 ATOM 2578 C CG . GLN A 1 410 ? -18.788 -47.642 109.102 1.00 214.61 ? 410 GLN A CG 1 ATOM 2579 C CD . GLN A 1 410 ? -18.719 -46.593 108.020 1.00 226.58 ? 410 GLN A CD 1 ATOM 2580 O OE1 . GLN A 1 410 ? -19.695 -46.362 107.300 1.00 231.01 ? 410 GLN A OE1 1 ATOM 2581 N NE2 . GLN A 1 410 ? -17.548 -45.982 107.863 1.00 226.64 ? 410 GLN A NE2 1 ATOM 2582 N N . TYR A 1 411 ? -19.469 -51.712 108.228 1.00 184.10 ? 411 TYR A N 1 ATOM 2583 C CA . TYR A 1 411 ? -20.564 -52.655 107.874 1.00 178.74 ? 411 TYR A CA 1 ATOM 2584 C C . TYR A 1 411 ? -20.250 -54.023 108.511 1.00 176.86 ? 411 TYR A C 1 ATOM 2585 O O . TYR A 1 411 ? -21.145 -54.727 109.030 1.00 156.84 ? 411 TYR A O 1 ATOM 2586 C CB . TYR A 1 411 ? -20.710 -52.805 106.333 1.00 175.49 ? 411 TYR A CB 1 ATOM 2587 C CG . TYR A 1 411 ? -21.570 -51.753 105.594 1.00 174.85 ? 411 TYR A CG 1 ATOM 2588 C CD1 . TYR A 1 411 ? -21.040 -50.498 105.248 1.00 179.70 ? 411 TYR A CD1 1 ATOM 2589 C CD2 . TYR A 1 411 ? -22.899 -52.030 105.212 1.00 161.50 ? 411 TYR A CD2 1 ATOM 2590 C CE1 . TYR A 1 411 ? -21.807 -49.550 104.584 1.00 168.21 ? 411 TYR A CE1 1 ATOM 2591 C CE2 . TYR A 1 411 ? -23.667 -51.085 104.546 1.00 150.47 ? 411 TYR A CE2 1 ATOM 2592 C CZ . TYR A 1 411 ? -23.112 -49.856 104.240 1.00 158.42 ? 411 TYR A CZ 1 ATOM 2593 O OH . TYR A 1 411 ? -23.847 -48.914 103.585 1.00 162.09 ? 411 TYR A OH 1 ATOM 2594 N N . LEU A 1 412 ? -18.949 -54.341 108.466 1.00 186.34 ? 412 LEU A N 1 ATOM 2595 C CA . LEU A 1 412 ? -18.312 -55.562 108.992 1.00 190.97 ? 412 LEU A CA 1 ATOM 2596 C C . LEU A 1 412 ? -17.685 -55.367 110.400 1.00 198.80 ? 412 LEU A C 1 ATOM 2597 O O . LEU A 1 412 ? -18.391 -55.433 111.418 1.00 194.24 ? 412 LEU A O 1 ATOM 2598 C CB . LEU A 1 412 ? -17.210 -56.025 108.016 1.00 179.44 ? 412 LEU A CB 1 ATOM 2599 C CG . LEU A 1 412 ? -17.409 -56.613 106.612 1.00 164.02 ? 412 LEU A CG 1 ATOM 2600 C CD1 . LEU A 1 412 ? -18.578 -56.005 105.850 1.00 150.85 ? 412 LEU A CD1 1 ATOM 2601 C CD2 . LEU A 1 412 ? -16.105 -56.484 105.825 1.00 163.13 ? 412 LEU A CD2 1 ATOM 2602 N N . ASN A 1 413 ? -16.362 -55.141 110.435 1.00 201.67 ? 413 ASN A N 1 ATOM 2603 C CA . ASN A 1 413 ? -15.586 -54.950 111.672 1.00 210.89 ? 413 ASN A CA 1 ATOM 2604 C C . ASN A 1 413 ? -16.452 -54.444 112.821 1.00 220.29 ? 413 ASN A C 1 ATOM 2605 O O . ASN A 1 413 ? -16.652 -53.232 112.954 1.00 230.97 ? 413 ASN A O 1 ATOM 2606 C CB . ASN A 1 413 ? -14.390 -53.993 111.451 1.00 209.25 ? 413 ASN A CB 1 ATOM 2607 C CG . ASN A 1 413 ? -13.151 -54.691 110.884 1.00 211.11 ? 413 ASN A CG 1 ATOM 2608 O OD1 . ASN A 1 413 ? -12.515 -54.187 109.958 1.00 209.50 ? 413 ASN A OD1 1 ATOM 2609 N ND2 . ASN A 1 413 ? -12.794 -55.839 111.448 1.00 212.41 ? 413 ASN A ND2 1 ATOM 2610 N N . ASN A 1 414 ? -16.966 -55.385 113.624 1.00 215.66 ? 414 ASN A N 1 ATOM 2611 C CA . ASN A 1 414 ? -17.868 -55.117 114.760 1.00 214.27 ? 414 ASN A CA 1 ATOM 2612 C C . ASN A 1 414 ? -17.364 -54.115 115.820 1.00 227.58 ? 414 ASN A C 1 ATOM 2613 O O . ASN A 1 414 ? -16.211 -54.201 116.256 1.00 231.08 ? 414 ASN A O 1 ATOM 2614 C CB . ASN A 1 414 ? -18.218 -56.430 115.447 1.00 204.89 ? 414 ASN A CB 1 ATOM 2615 C CG . ASN A 1 414 ? -18.704 -56.223 116.865 1.00 208.47 ? 414 ASN A CG 1 ATOM 2616 O OD1 . ASN A 1 414 ? -17.932 -56.327 117.823 1.00 204.08 ? 414 ASN A OD1 1 ATOM 2617 N ND2 . ASN A 1 414 ? -19.984 -55.892 117.006 1.00 212.36 ? 414 ASN A ND2 1 ATOM 2618 N N . GLY A 1 415 ? -18.252 -53.211 116.263 1.00 233.70 ? 415 GLY A N 1 ATOM 2619 C CA . GLY A 1 415 ? -17.879 -52.051 117.103 1.00 240.02 ? 415 GLY A CA 1 ATOM 2620 C C . GLY A 1 415 ? -18.754 -51.683 118.302 1.00 242.46 ? 415 GLY A C 1 ATOM 2621 O O . GLY A 1 415 ? -19.643 -52.454 118.677 1.00 240.51 ? 415 GLY A O 1 ATOM 2622 N N . PRO A 1 416 ? -18.521 -50.482 118.898 1.00 247.84 ? 416 PRO A N 1 ATOM 2623 C CA . PRO A 1 416 ? -19.078 -50.118 120.214 1.00 247.74 ? 416 PRO A CA 1 ATOM 2624 C C . PRO A 1 416 ? -20.591 -50.071 120.162 1.00 241.21 ? 416 PRO A C 1 ATOM 2625 O O . PRO A 1 416 ? -21.262 -50.170 121.196 1.00 235.55 ? 416 PRO A O 1 ATOM 2626 C CB . PRO A 1 416 ? -18.521 -48.713 120.451 1.00 252.85 ? 416 PRO A CB 1 ATOM 2627 C CG . PRO A 1 416 ? -18.357 -48.149 119.078 1.00 246.94 ? 416 PRO A CG 1 ATOM 2628 C CD . PRO A 1 416 ? -17.927 -49.310 118.221 1.00 244.24 ? 416 PRO A CD 1 ATOM 2629 N N . GLN A 1 417 ? -21.099 -49.906 118.943 1.00 232.90 ? 417 GLN A N 1 ATOM 2630 C CA . GLN A 1 417 ? -22.515 -49.939 118.652 1.00 225.29 ? 417 GLN A CA 1 ATOM 2631 C C . GLN A 1 417 ? -22.726 -50.299 117.179 1.00 209.85 ? 417 GLN A C 1 ATOM 2632 O O . GLN A 1 417 ? -23.428 -49.590 116.457 1.00 208.89 ? 417 GLN A O 1 ATOM 2633 C CB . GLN A 1 417 ? -23.173 -48.593 118.994 1.00 235.06 ? 417 GLN A CB 1 ATOM 2634 C CG . GLN A 1 417 ? -24.626 -48.700 119.454 1.00 233.00 ? 417 GLN A CG 1 ATOM 2635 C CD . GLN A 1 417 ? -25.392 -47.388 119.365 1.00 235.22 ? 417 GLN A CD 1 ATOM 2636 O OE1 . GLN A 1 417 ? -26.612 -47.375 119.166 1.00 223.94 ? 417 GLN A OE1 1 ATOM 2637 N NE2 . GLN A 1 417 ? -24.679 -46.274 119.509 1.00 253.52 ? 417 GLN A NE2 1 ATOM 2638 N N . ARG A 1 418 ? -22.105 -51.390 116.730 1.00 197.24 ? 418 ARG A N 1 ATOM 2639 C CA . ARG A 1 418 ? -22.385 -51.925 115.391 1.00 192.28 ? 418 ARG A CA 1 ATOM 2640 C C . ARG A 1 418 ? -22.208 -53.458 115.319 1.00 188.91 ? 418 ARG A C 1 ATOM 2641 O O . ARG A 1 418 ? -21.086 -53.959 115.242 1.00 190.01 ? 418 ARG A O 1 ATOM 2642 C CB . ARG A 1 418 ? -21.534 -51.227 114.313 1.00 190.57 ? 418 ARG A CB 1 ATOM 2643 C CG . ARG A 1 418 ? -21.232 -49.742 114.529 1.00 193.88 ? 418 ARG A CG 1 ATOM 2644 C CD . ARG A 1 418 ? -22.105 -48.815 113.689 1.00 193.08 ? 418 ARG A CD 1 ATOM 2645 N NE . ARG A 1 418 ? -21.529 -47.465 113.563 1.00 206.56 ? 418 ARG A NE 1 ATOM 2646 C CZ . ARG A 1 418 ? -20.681 -47.071 112.603 1.00 210.75 ? 418 ARG A CZ 1 ATOM 2647 N NH1 . ARG A 1 418 ? -20.286 -47.921 111.663 1.00 209.13 ? 418 ARG A NH1 1 ATOM 2648 N NH2 . ARG A 1 418 ? -20.219 -45.822 112.575 1.00 211.79 ? 418 ARG A NH2 1 ATOM 2649 N N . ILE A 1 419 ? -23.323 -54.190 115.352 1.00 185.54 ? 419 ILE A N 1 ATOM 2650 C CA . ILE A 1 419 ? -23.330 -55.657 115.206 1.00 179.30 ? 419 ILE A CA 1 ATOM 2651 C C . ILE A 1 419 ? -22.313 -56.112 114.177 1.00 184.76 ? 419 ILE A C 1 ATOM 2652 O O . ILE A 1 419 ? -21.412 -56.889 114.501 1.00 176.94 ? 419 ILE A O 1 ATOM 2653 C CB . ILE A 1 419 ? -24.712 -56.209 114.776 1.00 170.20 ? 419 ILE A CB 1 ATOM 2654 C CG1 . ILE A 1 419 ? -25.581 -55.115 114.143 1.00 168.03 ? 419 ILE A CG1 1 ATOM 2655 C CG2 . ILE A 1 419 ? -25.442 -56.837 115.948 1.00 172.79 ? 419 ILE A CG2 1 ATOM 2656 C CD1 . ILE A 1 419 ? -26.302 -54.217 115.132 1.00 174.24 ? 419 ILE A CD1 1 ATOM 2657 N N . GLY A 1 420 ? -22.481 -55.608 112.948 1.00 198.62 ? 420 GLY A N 1 ATOM 2658 C CA . GLY A 1 420 ? -21.602 -55.871 111.801 1.00 205.31 ? 420 GLY A CA 1 ATOM 2659 C C . GLY A 1 420 ? -21.362 -57.326 111.403 1.00 209.87 ? 420 GLY A C 1 ATOM 2660 O O . GLY A 1 420 ? -21.390 -58.226 112.253 1.00 223.31 ? 420 GLY A O 1 ATOM 2661 N N . ARG A 1 421 ? -21.133 -57.545 110.102 1.00 188.36 ? 421 ARG A N 1 ATOM 2662 C CA . ARG A 1 421 ? -20.630 -58.824 109.524 1.00 173.76 ? 421 ARG A CA 1 ATOM 2663 C C . ARG A 1 421 ? -21.465 -60.096 109.727 1.00 171.15 ? 421 ARG A C 1 ATOM 2664 O O . ARG A 1 421 ? -21.721 -60.821 108.766 1.00 168.05 ? 421 ARG A O 1 ATOM 2665 C CB . ARG A 1 421 ? -19.169 -59.099 109.936 1.00 172.04 ? 421 ARG A CB 1 ATOM 2666 C CG . ARG A 1 421 ? -18.432 -60.120 109.068 1.00 163.16 ? 421 ARG A CG 1 ATOM 2667 C CD . ARG A 1 421 ? -17.092 -60.539 109.665 1.00 173.69 ? 421 ARG A CD 1 ATOM 2668 N NE . ARG A 1 421 ? -16.213 -59.402 109.952 1.00 183.65 ? 421 ARG A NE 1 ATOM 2669 C CZ . ARG A 1 421 ? -15.303 -58.909 109.113 1.00 182.62 ? 421 ARG A CZ 1 ATOM 2670 N NH1 . ARG A 1 421 ? -15.127 -59.451 107.911 1.00 180.44 ? 421 ARG A NH1 1 ATOM 2671 N NH2 . ARG A 1 421 ? -14.561 -57.868 109.479 1.00 180.51 ? 421 ARG A NH2 1 ATOM 2672 N N . LYS A 1 422 ? -21.857 -60.377 110.968 1.00 179.27 ? 422 LYS A N 1 ATOM 2673 C CA . LYS A 1 422 ? -22.449 -61.670 111.330 1.00 177.80 ? 422 LYS A CA 1 ATOM 2674 C C . LYS A 1 422 ? -23.789 -61.491 112.050 1.00 168.34 ? 422 LYS A C 1 ATOM 2675 O O . LYS A 1 422 ? -23.857 -60.822 113.082 1.00 176.98 ? 422 LYS A O 1 ATOM 2676 C CB . LYS A 1 422 ? -21.452 -62.466 112.193 1.00 193.01 ? 422 LYS A CB 1 ATOM 2677 C CG . LYS A 1 422 ? -21.810 -63.926 112.400 1.00 187.72 ? 422 LYS A CG 1 ATOM 2678 C CD . LYS A 1 422 ? -20.705 -64.720 113.088 1.00 187.34 ? 422 LYS A CD 1 ATOM 2679 C CE . LYS A 1 422 ? -21.327 -65.914 113.805 1.00 187.46 ? 422 LYS A CE 1 ATOM 2680 N NZ . LYS A 1 422 ? -20.574 -67.191 113.684 1.00 185.77 ? 422 LYS A NZ 1 ATOM 2681 N N . TYR A 1 423 ? -24.849 -62.072 111.494 1.00 153.31 ? 423 TYR A N 1 ATOM 2682 C CA . TYR A 1 423 ? -26.205 -61.883 112.018 1.00 158.51 ? 423 TYR A CA 1 ATOM 2683 C C . TYR A 1 423 ? -26.920 -63.249 112.082 1.00 161.11 ? 423 TYR A C 1 ATOM 2684 O O . TYR A 1 423 ? -26.515 -64.194 111.397 1.00 163.89 ? 423 TYR A O 1 ATOM 2685 C CB . TYR A 1 423 ? -26.996 -60.874 111.143 1.00 164.18 ? 423 TYR A CB 1 ATOM 2686 C CG . TYR A 1 423 ? -26.489 -59.406 111.098 1.00 177.40 ? 423 TYR A CG 1 ATOM 2687 C CD1 . TYR A 1 423 ? -25.265 -59.072 110.502 1.00 181.05 ? 423 TYR A CD1 1 ATOM 2688 C CD2 . TYR A 1 423 ? -27.255 -58.347 111.618 1.00 179.97 ? 423 TYR A CD2 1 ATOM 2689 C CE1 . TYR A 1 423 ? -24.811 -57.749 110.458 1.00 173.92 ? 423 TYR A CE1 1 ATOM 2690 C CE2 . TYR A 1 423 ? -26.807 -57.019 111.561 1.00 168.39 ? 423 TYR A CE2 1 ATOM 2691 C CZ . TYR A 1 423 ? -25.584 -56.728 110.983 1.00 165.65 ? 423 TYR A CZ 1 ATOM 2692 O OH . TYR A 1 423 ? -25.113 -55.436 110.923 1.00 159.33 ? 423 TYR A OH 1 ATOM 2693 N N . LYS A 1 424 ? -27.956 -63.371 112.915 1.00 163.02 ? 424 LYS A N 1 ATOM 2694 C CA . LYS A 1 424 ? -28.780 -64.591 112.943 1.00 155.76 ? 424 LYS A CA 1 ATOM 2695 C C . LYS A 1 424 ? -29.913 -64.423 111.946 1.00 155.60 ? 424 LYS A C 1 ATOM 2696 O O . LYS A 1 424 ? -30.702 -63.468 112.039 1.00 156.35 ? 424 LYS A O 1 ATOM 2697 C CB . LYS A 1 424 ? -29.333 -64.885 114.348 1.00 153.85 ? 424 LYS A CB 1 ATOM 2698 C CG . LYS A 1 424 ? -30.297 -66.065 114.416 1.00 148.43 ? 424 LYS A CG 1 ATOM 2699 C CD . LYS A 1 424 ? -30.677 -66.441 115.848 1.00 154.00 ? 424 LYS A CD 1 ATOM 2700 C CE . LYS A 1 424 ? -29.872 -67.633 116.364 1.00 158.47 ? 424 LYS A CE 1 ATOM 2701 N NZ . LYS A 1 424 ? -30.259 -68.066 117.739 1.00 157.83 ? 424 LYS A NZ 1 ATOM 2702 N N . LYS A 1 425 ? -29.969 -65.337 110.979 1.00 151.26 ? 425 LYS A N 1 ATOM 2703 C CA . LYS A 1 425 ? -30.999 -65.305 109.934 1.00 147.98 ? 425 LYS A CA 1 ATOM 2704 C C . LYS A 1 425 ? -31.735 -66.637 109.864 1.00 145.55 ? 425 LYS A C 1 ATOM 2705 O O . LYS A 1 425 ? -31.430 -67.557 110.631 1.00 155.59 ? 425 LYS A O 1 ATOM 2706 C CB . LYS A 1 425 ? -30.393 -64.966 108.569 1.00 148.58 ? 425 LYS A CB 1 ATOM 2707 C CG . LYS A 1 425 ? -29.658 -63.638 108.531 1.00 155.47 ? 425 LYS A CG 1 ATOM 2708 C CD . LYS A 1 425 ? -29.536 -63.087 107.122 1.00 154.26 ? 425 LYS A CD 1 ATOM 2709 C CE . LYS A 1 425 ? -30.763 -62.282 106.713 1.00 151.01 ? 425 LYS A CE 1 ATOM 2710 N NZ . LYS A 1 425 ? -31.316 -61.470 107.833 1.00 146.28 ? 425 LYS A NZ 1 ATOM 2711 N N . VAL A 1 426 ? -32.709 -66.734 108.961 1.00 135.70 ? 426 VAL A N 1 ATOM 2712 C CA . VAL A 1 426 ? -33.487 -67.963 108.791 1.00 137.22 ? 426 VAL A CA 1 ATOM 2713 C C . VAL A 1 426 ? -33.618 -68.284 107.307 1.00 139.74 ? 426 VAL A C 1 ATOM 2714 O O . VAL A 1 426 ? -34.418 -67.664 106.618 1.00 160.76 ? 426 VAL A O 1 ATOM 2715 C CB . VAL A 1 426 ? -34.879 -67.899 109.505 1.00 130.83 ? 426 VAL A CB 1 ATOM 2716 C CG1 . VAL A 1 426 ? -35.752 -66.777 108.965 1.00 122.85 ? 426 VAL A CG1 1 ATOM 2717 C CG2 . VAL A 1 426 ? -35.620 -69.226 109.415 1.00 127.88 ? 426 VAL A CG2 1 ATOM 2718 N N . ARG A 1 427 ? -32.829 -69.234 106.812 1.00 137.86 ? 427 ARG A N 1 ATOM 2719 C CA . ARG A 1 427 ? -32.878 -69.576 105.384 1.00 143.32 ? 427 ARG A CA 1 ATOM 2720 C C . ARG A 1 427 ? -33.687 -70.842 105.162 1.00 133.46 ? 427 ARG A C 1 ATOM 2721 O O . ARG A 1 427 ? -34.047 -71.535 106.114 1.00 129.75 ? 427 ARG A O 1 ATOM 2722 C CB . ARG A 1 427 ? -31.475 -69.780 104.802 1.00 149.19 ? 427 ARG A CB 1 ATOM 2723 C CG . ARG A 1 427 ? -30.339 -69.206 105.632 1.00 150.65 ? 427 ARG A CG 1 ATOM 2724 C CD . ARG A 1 427 ? -29.132 -70.124 105.594 1.00 139.89 ? 427 ARG A CD 1 ATOM 2725 N NE . ARG A 1 427 ? -29.013 -70.739 104.280 1.00 141.00 ? 427 ARG A NE 1 ATOM 2726 C CZ . ARG A 1 427 ? -27.964 -71.443 103.871 1.00 157.97 ? 427 ARG A CZ 1 ATOM 2727 N NH1 . ARG A 1 427 ? -26.915 -71.619 104.675 1.00 183.94 ? 427 ARG A NH1 1 ATOM 2728 N NH2 . ARG A 1 427 ? -27.962 -71.969 102.650 1.00 148.01 ? 427 ARG A NH2 1 ATOM 2729 N N . PHE A 1 428 ? -33.982 -71.126 103.901 1.00 119.67 ? 428 PHE A N 1 ATOM 2730 C CA . PHE A 1 428 ? -34.434 -72.443 103.541 1.00 116.40 ? 428 PHE A CA 1 ATOM 2731 C C . PHE A 1 428 ? -33.228 -73.361 103.393 1.00 122.30 ? 428 PHE A C 1 ATOM 2732 O O . PHE A 1 428 ? -32.369 -73.107 102.561 1.00 136.81 ? 428 PHE A O 1 ATOM 2733 C CB . PHE A 1 428 ? -35.163 -72.400 102.214 1.00 117.09 ? 428 PHE A CB 1 ATOM 2734 C CG . PHE A 1 428 ? -36.476 -71.688 102.260 1.00 125.37 ? 428 PHE A CG 1 ATOM 2735 C CD1 . PHE A 1 428 ? -37.569 -72.258 102.879 1.00 132.94 ? 428 PHE A CD1 1 ATOM 2736 C CD2 . PHE A 1 428 ? -36.633 -70.460 101.644 1.00 132.31 ? 428 PHE A CD2 1 ATOM 2737 C CE1 . PHE A 1 428 ? -38.789 -71.604 102.910 1.00 131.24 ? 428 PHE A CE1 1 ATOM 2738 C CE2 . PHE A 1 428 ? -37.855 -69.805 101.660 1.00 123.03 ? 428 PHE A CE2 1 ATOM 2739 C CZ . PHE A 1 428 ? -38.932 -70.376 102.299 1.00 120.31 ? 428 PHE A CZ 1 ATOM 2740 N N . MET A 1 429 ? -33.150 -74.420 104.192 1.00 126.23 ? 429 MET A N 1 ATOM 2741 C CA . MET A 1 429 ? -32.201 -75.503 103.914 1.00 132.94 ? 429 MET A CA 1 ATOM 2742 C C . MET A 1 429 ? -32.920 -76.766 103.375 1.00 132.57 ? 429 MET A C 1 ATOM 2743 O O . MET A 1 429 ? -34.088 -77.037 103.718 1.00 115.00 ? 429 MET A O 1 ATOM 2744 C CB . MET A 1 429 ? -31.332 -75.805 105.143 1.00 151.72 ? 429 MET A CB 1 ATOM 2745 C CG . MET A 1 429 ? -30.314 -74.718 105.498 1.00 175.21 ? 429 MET A CG 1 ATOM 2746 S SD . MET A 1 429 ? -28.796 -75.274 106.345 1.00 215.99 ? 429 MET A SD 1 ATOM 2747 C CE . MET A 1 429 ? -27.767 -75.897 105.000 1.00 172.70 ? 429 MET A CE 1 ATOM 2748 N N . ALA A 1 430 ? -32.234 -77.524 102.518 1.00 137.28 ? 430 ALA A N 1 ATOM 2749 C CA . ALA A 1 430 ? -32.847 -78.705 101.877 1.00 147.32 ? 430 ALA A CA 1 ATOM 2750 C C . ALA A 1 430 ? -32.411 -80.042 102.498 1.00 157.18 ? 430 ALA A C 1 ATOM 2751 O O . ALA A 1 430 ? -31.228 -80.381 102.457 1.00 169.62 ? 430 ALA A O 1 ATOM 2752 C CB . ALA A 1 430 ? -32.543 -78.702 100.384 1.00 149.17 ? 430 ALA A CB 1 ATOM 2753 N N . TYR A 1 431 ? -33.354 -80.810 103.047 1.00 151.78 ? 431 TYR A N 1 ATOM 2754 C CA . TYR A 1 431 ? -33.017 -82.098 103.689 1.00 156.87 ? 431 TYR A CA 1 ATOM 2755 C C . TYR A 1 431 ? -33.213 -83.296 102.766 1.00 160.79 ? 431 TYR A C 1 ATOM 2756 O O . TYR A 1 431 ? -33.712 -83.146 101.653 1.00 179.36 ? 431 TYR A O 1 ATOM 2757 C CB . TYR A 1 431 ? -33.838 -82.311 104.959 1.00 157.60 ? 431 TYR A CB 1 ATOM 2758 C CG . TYR A 1 431 ? -33.314 -81.587 106.165 1.00 162.13 ? 431 TYR A CG 1 ATOM 2759 C CD1 . TYR A 1 431 ? -33.488 -80.211 106.304 1.00 167.84 ? 431 TYR A CD1 1 ATOM 2760 C CD2 . TYR A 1 431 ? -32.647 -82.268 107.170 1.00 172.48 ? 431 TYR A CD2 1 ATOM 2761 C CE1 . TYR A 1 431 ? -33.014 -79.529 107.414 1.00 169.78 ? 431 TYR A CE1 1 ATOM 2762 C CE2 . TYR A 1 431 ? -32.168 -81.596 108.286 1.00 188.22 ? 431 TYR A CE2 1 ATOM 2763 C CZ . TYR A 1 431 ? -32.356 -80.225 108.403 1.00 180.20 ? 431 TYR A CZ 1 ATOM 2764 O OH . TYR A 1 431 ? -31.888 -79.551 109.505 1.00 185.19 ? 431 TYR A OH 1 ATOM 2765 N N . THR A 1 432 ? -32.863 -84.488 103.253 1.00 152.58 ? 432 THR A N 1 ATOM 2766 C CA . THR A 1 432 ? -32.923 -85.706 102.441 1.00 135.56 ? 432 THR A CA 1 ATOM 2767 C C . THR A 1 432 ? -34.218 -86.496 102.397 1.00 126.77 ? 432 THR A C 1 ATOM 2768 O O . THR A 1 432 ? -34.512 -87.080 101.375 1.00 131.54 ? 432 THR A O 1 ATOM 2769 C CB . THR A 1 432 ? -31.793 -86.673 102.776 1.00 143.41 ? 432 THR A CB 1 ATOM 2770 O OG1 . THR A 1 432 ? -31.422 -86.520 104.154 1.00 141.79 ? 432 THR A OG1 1 ATOM 2771 C CG2 . THR A 1 432 ? -30.622 -86.359 101.884 1.00 154.75 ? 432 THR A CG2 1 ATOM 2772 N N . ASP A 1 433 ? -34.991 -86.543 103.472 1.00 122.99 ? 433 ASP A N 1 ATOM 2773 C CA . ASP A 1 433 ? -36.199 -87.380 103.463 1.00 138.37 ? 433 ASP A CA 1 ATOM 2774 C C . ASP A 1 433 ? -37.339 -86.821 104.326 1.00 149.28 ? 433 ASP A C 1 ATOM 2775 O O . ASP A 1 433 ? -37.245 -85.704 104.833 1.00 156.08 ? 433 ASP A O 1 ATOM 2776 C CB . ASP A 1 433 ? -35.826 -88.757 103.970 1.00 144.65 ? 433 ASP A CB 1 ATOM 2777 C CG . ASP A 1 433 ? -35.155 -88.683 105.308 1.00 151.91 ? 433 ASP A CG 1 ATOM 2778 O OD1 . ASP A 1 433 ? -34.526 -87.637 105.562 1.00 160.05 ? 433 ASP A OD1 1 ATOM 2779 O OD2 . ASP A 1 433 ? -35.269 -89.627 106.113 1.00 151.92 ? 433 ASP A OD2 1 ATOM 2780 N N . GLU A 1 434 ? -38.412 -87.601 104.489 1.00 157.40 ? 434 GLU A N 1 ATOM 2781 C CA . GLU A 1 434 ? -39.513 -87.251 105.400 1.00 160.59 ? 434 GLU A CA 1 ATOM 2782 C C . GLU A 1 434 ? -39.021 -86.678 106.758 1.00 155.89 ? 434 GLU A C 1 ATOM 2783 O O . GLU A 1 434 ? -39.439 -85.593 107.154 1.00 139.46 ? 434 GLU A O 1 ATOM 2784 C CB . GLU A 1 434 ? -40.471 -88.448 105.603 1.00 177.11 ? 434 GLU A CB 1 ATOM 2785 C CG . GLU A 1 434 ? -41.652 -88.526 104.638 1.00 181.98 ? 434 GLU A CG 1 ATOM 2786 C CD . GLU A 1 434 ? -42.621 -87.339 104.749 1.00 190.68 ? 434 GLU A CD 1 ATOM 2787 O OE1 . GLU A 1 434 ? -43.276 -87.153 105.816 1.00 185.47 ? 434 GLU A OE1 1 ATOM 2788 O OE2 . GLU A 1 434 ? -42.731 -86.585 103.750 1.00 177.86 ? 434 GLU A OE2 1 ATOM 2789 N N . THR A 1 435 ? -38.140 -87.398 107.460 1.00 159.86 ? 435 THR A N 1 ATOM 2790 C CA . THR A 1 435 ? -37.497 -86.850 108.662 1.00 154.49 ? 435 THR A CA 1 ATOM 2791 C C . THR A 1 435 ? -36.525 -85.774 108.271 1.00 155.84 ? 435 THR A C 1 ATOM 2792 O O . THR A 1 435 ? -35.977 -85.774 107.172 1.00 157.46 ? 435 THR A O 1 ATOM 2793 C CB . THR A 1 435 ? -36.659 -87.865 109.473 1.00 157.12 ? 435 THR A CB 1 ATOM 2794 O OG1 . THR A 1 435 ? -35.488 -87.191 109.983 1.00 154.30 ? 435 THR A OG1 1 ATOM 2795 C CG2 . THR A 1 435 ? -36.224 -89.063 108.627 1.00 136.70 ? 435 THR A CG2 1 ATOM 2796 N N . PHE A 1 436 ? -36.267 -84.873 109.194 1.00 156.85 ? 436 PHE A N 1 ATOM 2797 C CA . PHE A 1 436 ? -35.308 -83.857 108.894 1.00 163.03 ? 436 PHE A CA 1 ATOM 2798 C C . PHE A 1 436 ? -34.124 -83.952 109.851 1.00 170.37 ? 436 PHE A C 1 ATOM 2799 O O . PHE A 1 436 ? -34.016 -83.171 110.797 1.00 194.65 ? 436 PHE A O 1 ATOM 2800 C CB . PHE A 1 436 ? -35.948 -82.452 108.932 1.00 161.41 ? 436 PHE A CB 1 ATOM 2801 C CG . PHE A 1 436 ? -36.958 -82.170 107.827 1.00 153.49 ? 436 PHE A CG 1 ATOM 2802 C CD1 . PHE A 1 436 ? -38.199 -82.793 107.798 1.00 153.70 ? 436 PHE A CD1 1 ATOM 2803 C CD2 . PHE A 1 436 ? -36.692 -81.212 106.853 1.00 147.02 ? 436 PHE A CD2 1 ATOM 2804 C CE1 . PHE A 1 436 ? -39.120 -82.497 106.796 1.00 141.02 ? 436 PHE A CE1 1 ATOM 2805 C CE2 . PHE A 1 436 ? -37.618 -80.908 105.855 1.00 132.46 ? 436 PHE A CE2 1 ATOM 2806 C CZ . PHE A 1 436 ? -38.831 -81.552 105.826 1.00 128.02 ? 436 PHE A CZ 1 ATOM 2807 N N . LYS A 1 437 ? -33.243 -84.916 109.632 1.00 159.61 ? 437 LYS A N 1 ATOM 2808 C CA . LYS A 1 437 ? -31.843 -84.600 109.899 1.00 169.82 ? 437 LYS A CA 1 ATOM 2809 C C . LYS A 1 437 ? -30.929 -85.064 108.783 1.00 162.27 ? 437 LYS A C 1 ATOM 2810 O O . LYS A 1 437 ? -31.143 -86.113 108.189 1.00 140.79 ? 437 LYS A O 1 ATOM 2811 C CB . LYS A 1 437 ? -31.352 -84.884 111.339 1.00 192.21 ? 437 LYS A CB 1 ATOM 2812 C CG . LYS A 1 437 ? -30.842 -86.278 111.688 1.00 213.27 ? 437 LYS A CG 1 ATOM 2813 C CD . LYS A 1 437 ? -30.743 -86.461 113.212 1.00 209.51 ? 437 LYS A CD 1 ATOM 2814 C CE . LYS A 1 437 ? -32.071 -86.891 113.844 1.00 202.40 ? 437 LYS A CE 1 ATOM 2815 N NZ . LYS A 1 437 ? -33.303 -86.328 113.187 1.00 182.36 ? 437 LYS A NZ 1 ATOM 2816 N N . THR A 1 438 ? -29.961 -84.201 108.476 1.00 176.73 ? 438 THR A N 1 ATOM 2817 C CA . THR A 1 438 ? -28.979 -84.352 107.387 1.00 178.13 ? 438 THR A CA 1 ATOM 2818 C C . THR A 1 438 ? -29.471 -83.895 105.981 1.00 158.25 ? 438 THR A C 1 ATOM 2819 O O . THR A 1 438 ? -30.580 -84.238 105.560 1.00 137.38 ? 438 THR A O 1 ATOM 2820 C CB . THR A 1 438 ? -28.295 -85.740 107.398 1.00 198.23 ? 438 THR A CB 1 ATOM 2821 O OG1 . THR A 1 438 ? -29.289 -86.771 107.320 1.00 204.91 ? 438 THR A OG1 1 ATOM 2822 C CG2 . THR A 1 438 ? -27.448 -85.920 108.686 1.00 194.81 ? 438 THR A CG2 1 ATOM 2823 N N . ARG A 1 439 ? -28.614 -83.123 105.293 1.00 160.91 ? 439 ARG A N 1 ATOM 2824 C CA . ARG A 1 439 ? -28.888 -82.465 103.987 1.00 167.11 ? 439 ARG A CA 1 ATOM 2825 C C . ARG A 1 439 ? -27.695 -82.519 102.993 1.00 175.07 ? 439 ARG A C 1 ATOM 2826 O O . ARG A 1 439 ? -26.626 -83.034 103.332 1.00 190.90 ? 439 ARG A O 1 ATOM 2827 C CB . ARG A 1 439 ? -29.199 -80.988 104.201 1.00 159.57 ? 439 ARG A CB 1 ATOM 2828 C CG . ARG A 1 439 ? -29.320 -80.556 105.642 1.00 162.60 ? 439 ARG A CG 1 ATOM 2829 C CD . ARG A 1 439 ? -28.391 -79.384 105.887 1.00 172.15 ? 439 ARG A CD 1 ATOM 2830 N NE . ARG A 1 439 ? -28.786 -78.613 107.062 1.00 188.92 ? 439 ARG A NE 1 ATOM 2831 C CZ . ARG A 1 439 ? -28.604 -78.996 108.325 1.00 194.78 ? 439 ARG A CZ 1 ATOM 2832 N NH1 . ARG A 1 439 ? -28.029 -80.164 108.605 1.00 200.19 ? 439 ARG A NH1 1 ATOM 2833 N NH2 . ARG A 1 439 ? -29.004 -78.204 109.314 1.00 197.00 ? 439 ARG A NH2 1 ATOM 2834 N N . GLU A 1 440 ? -27.884 -81.979 101.778 1.00 169.17 ? 440 GLU A N 1 ATOM 2835 C CA . GLU A 1 440 ? -26.819 -81.867 100.744 1.00 160.53 ? 440 GLU A CA 1 ATOM 2836 C C . GLU A 1 440 ? -26.026 -80.593 100.996 1.00 154.76 ? 440 GLU A C 1 ATOM 2837 O O . GLU A 1 440 ? -26.564 -79.681 101.619 1.00 153.21 ? 440 GLU A O 1 ATOM 2838 C CB . GLU A 1 440 ? -27.387 -81.906 99.307 1.00 168.35 ? 440 GLU A CB 1 ATOM 2839 C CG . GLU A 1 440 ? -28.916 -81.824 99.169 1.00 181.42 ? 440 GLU A CG 1 ATOM 2840 C CD . GLU A 1 440 ? -29.649 -83.105 99.614 1.00 194.22 ? 440 GLU A CD 1 ATOM 2841 O OE1 . GLU A 1 440 ? -29.681 -84.102 98.847 1.00 200.96 ? 440 GLU A OE1 1 ATOM 2842 O OE2 . GLU A 1 440 ? -30.201 -83.127 100.744 1.00 178.49 ? 440 GLU A OE2 1 ATOM 2843 N N . ALA A 1 441 ? -24.772 -80.527 100.521 1.00 168.65 ? 441 ALA A N 1 ATOM 2844 C CA . ALA A 1 441 ? -23.752 -79.528 101.014 1.00 185.26 ? 441 ALA A CA 1 ATOM 2845 C C . ALA A 1 441 ? -23.923 -78.014 100.669 1.00 179.81 ? 441 ALA A C 1 ATOM 2846 O O . ALA A 1 441 ? -24.337 -77.631 99.562 1.00 154.26 ? 441 ALA A O 1 ATOM 2847 C CB . ALA A 1 441 ? -22.303 -80.011 100.760 1.00 169.43 ? 441 ALA A CB 1 ATOM 2848 N N . ILE A 1 442 ? -23.593 -77.174 101.656 1.00 193.29 ? 442 ILE A N 1 ATOM 2849 C CA . ILE A 1 442 ? -23.775 -75.707 101.611 1.00 217.50 ? 442 ILE A CA 1 ATOM 2850 C C . ILE A 1 442 ? -23.077 -75.137 100.336 1.00 230.82 ? 442 ILE A C 1 ATOM 2851 O O . ILE A 1 442 ? -22.200 -75.796 99.758 1.00 229.84 ? 442 ILE A O 1 ATOM 2852 C CB . ILE A 1 442 ? -23.401 -75.058 103.018 1.00 226.02 ? 442 ILE A CB 1 ATOM 2853 C CG1 . ILE A 1 442 ? -23.706 -73.525 103.131 1.00 216.56 ? 442 ILE A CG1 1 ATOM 2854 C CG2 . ILE A 1 442 ? -22.000 -75.501 103.471 1.00 234.77 ? 442 ILE A CG2 1 ATOM 2855 C CD1 . ILE A 1 442 ? -23.670 -72.904 104.536 1.00 170.11 ? 442 ILE A CD1 1 ATOM 2856 N N . GLN A 1 443 ? -23.503 -73.957 99.872 1.00 239.91 ? 443 GLN A N 1 ATOM 2857 C CA . GLN A 1 443 ? -23.059 -73.398 98.578 1.00 210.52 ? 443 GLN A CA 1 ATOM 2858 C C . GLN A 1 443 ? -22.137 -72.187 98.640 1.00 197.77 ? 443 GLN A C 1 ATOM 2859 O O . GLN A 1 443 ? -22.624 -71.053 98.745 1.00 182.34 ? 443 GLN A O 1 ATOM 2860 C CB . GLN A 1 443 ? -24.276 -73.057 97.701 1.00 195.18 ? 443 GLN A CB 1 ATOM 2861 C CG . GLN A 1 443 ? -24.706 -74.216 96.843 1.00 186.44 ? 443 GLN A CG 1 ATOM 2862 C CD . GLN A 1 443 ? -23.532 -75.128 96.588 1.00 204.41 ? 443 GLN A CD 1 ATOM 2863 O OE1 . GLN A 1 443 ? -22.457 -74.684 96.155 1.00 200.62 ? 443 GLN A OE1 1 ATOM 2864 N NE2 . GLN A 1 443 ? -23.708 -76.404 96.902 1.00 215.33 ? 443 GLN A NE2 1 ATOM 2865 N N . HIS A 1 444 ? -20.819 -72.391 98.547 1.00 190.25 ? 444 HIS A N 1 ATOM 2866 C CA . HIS A 1 444 ? -19.966 -71.208 98.503 1.00 211.11 ? 444 HIS A CA 1 ATOM 2867 C C . HIS A 1 444 ? -20.446 -70.444 97.287 1.00 200.14 ? 444 HIS A C 1 ATOM 2868 O O . HIS A 1 444 ? -20.625 -69.223 97.346 1.00 193.47 ? 444 HIS A O 1 ATOM 2869 C CB . HIS A 1 444 ? -18.451 -71.495 98.445 1.00 240.67 ? 444 HIS A CB 1 ATOM 2870 C CG . HIS A 1 444 ? -17.591 -70.324 98.866 1.00 257.64 ? 444 HIS A CG 1 ATOM 2871 N ND1 . HIS A 1 444 ? -16.637 -70.413 99.862 1.00 256.47 ? 444 HIS A ND1 1 ATOM 2872 C CD2 . HIS A 1 444 ? -17.553 -69.037 98.432 1.00 240.46 ? 444 HIS A CD2 1 ATOM 2873 C CE1 . HIS A 1 444 ? -16.049 -69.239 100.019 1.00 238.99 ? 444 HIS A CE1 1 ATOM 2874 N NE2 . HIS A 1 444 ? -16.587 -68.387 99.163 1.00 231.52 ? 444 HIS A NE2 1 ATOM 2875 N N . GLU A 1 445 ? -20.713 -71.190 96.214 1.00 191.32 ? 445 GLU A N 1 ATOM 2876 C CA . GLU A 1 445 ? -21.246 -70.614 94.984 1.00 190.33 ? 445 GLU A CA 1 ATOM 2877 C C . GLU A 1 445 ? -22.556 -69.826 95.248 1.00 183.88 ? 445 GLU A C 1 ATOM 2878 O O . GLU A 1 445 ? -22.534 -68.595 95.258 1.00 175.41 ? 445 GLU A O 1 ATOM 2879 C CB . GLU A 1 445 ? -21.362 -71.679 93.874 1.00 191.14 ? 445 GLU A CB 1 ATOM 2880 C CG . GLU A 1 445 ? -20.016 -72.233 93.373 1.00 194.76 ? 445 GLU A CG 1 ATOM 2881 C CD . GLU A 1 445 ? -19.493 -71.561 92.094 1.00 199.55 ? 445 GLU A CD 1 ATOM 2882 O OE1 . GLU A 1 445 ? -20.325 -71.168 91.245 1.00 209.35 ? 445 GLU A OE1 1 ATOM 2883 O OE2 . GLU A 1 445 ? -18.250 -71.441 91.916 1.00 176.28 ? 445 GLU A OE2 1 ATOM 2884 N N . SER A 1 446 ? -23.668 -70.513 95.512 1.00 184.02 ? 446 SER A N 1 ATOM 2885 C CA . SER A 1 446 ? -24.956 -69.832 95.746 1.00 164.46 ? 446 SER A CA 1 ATOM 2886 C C . SER A 1 446 ? -25.302 -69.682 97.237 1.00 143.82 ? 446 SER A C 1 ATOM 2887 O O . SER A 1 446 ? -26.117 -70.421 97.790 1.00 131.82 ? 446 SER A O 1 ATOM 2888 C CB . SER A 1 446 ? -26.090 -70.504 94.956 1.00 180.57 ? 446 SER A CB 1 ATOM 2889 O OG . SER A 1 446 ? -26.308 -71.832 95.400 1.00 199.03 ? 446 SER A OG 1 ATOM 2890 N N . GLY A 1 447 ? -24.685 -68.684 97.855 1.00 132.56 ? 447 GLY A N 1 ATOM 2891 C CA . GLY A 1 447 ? -24.669 -68.502 99.308 1.00 136.63 ? 447 GLY A CA 1 ATOM 2892 C C . GLY A 1 447 ? -25.895 -68.727 100.171 1.00 126.81 ? 447 GLY A C 1 ATOM 2893 O O . GLY A 1 447 ? -26.172 -69.855 100.559 1.00 126.08 ? 447 GLY A O 1 ATOM 2894 N N . ILE A 1 448 ? -26.595 -67.640 100.497 1.00 125.41 ? 448 ILE A N 1 ATOM 2895 C CA . ILE A 1 448 ? -27.727 -67.659 101.439 1.00 130.08 ? 448 ILE A CA 1 ATOM 2896 C C . ILE A 1 448 ? -28.997 -68.367 100.910 1.00 138.61 ? 448 ILE A C 1 ATOM 2897 O O . ILE A 1 448 ? -29.865 -68.841 101.697 1.00 129.61 ? 448 ILE A O 1 ATOM 2898 C CB . ILE A 1 448 ? -28.083 -66.228 101.935 1.00 126.46 ? 448 ILE A CB 1 ATOM 2899 C CG1 . ILE A 1 448 ? -29.174 -66.322 103.027 1.00 127.32 ? 448 ILE A CG1 1 ATOM 2900 C CG2 . ILE A 1 448 ? -28.477 -65.303 100.762 1.00 107.21 ? 448 ILE A CG2 1 ATOM 2901 C CD1 . ILE A 1 448 ? -28.978 -65.459 104.259 1.00 122.93 ? 448 ILE A CD1 1 ATOM 2902 N N . LEU A 1 449 ? -29.085 -68.433 99.579 1.00 133.29 ? 449 LEU A N 1 ATOM 2903 C CA . LEU A 1 449 ? -30.252 -68.951 98.876 1.00 126.43 ? 449 LEU A CA 1 ATOM 2904 C C . LEU A 1 449 ? -30.559 -70.353 99.323 1.00 131.65 ? 449 LEU A C 1 ATOM 2905 O O . LEU A 1 449 ? -29.645 -71.141 99.541 1.00 141.26 ? 449 LEU A O 1 ATOM 2906 C CB . LEU A 1 449 ? -30.013 -68.960 97.368 1.00 117.37 ? 449 LEU A CB 1 ATOM 2907 C CG . LEU A 1 449 ? -29.579 -67.620 96.785 1.00 126.47 ? 449 LEU A CG 1 ATOM 2908 C CD1 . LEU A 1 449 ? -28.101 -67.396 97.068 1.00 135.39 ? 449 LEU A CD1 1 ATOM 2909 C CD2 . LEU A 1 449 ? -29.868 -67.535 95.292 1.00 127.25 ? 449 LEU A CD2 1 ATOM 2910 N N . GLY A 1 450 ? -31.847 -70.652 99.479 1.00 135.82 ? 450 GLY A N 1 ATOM 2911 C CA . GLY A 1 450 ? -32.319 -72.034 99.596 1.00 131.76 ? 450 GLY A CA 1 ATOM 2912 C C . GLY A 1 450 ? -32.079 -72.786 98.296 1.00 126.21 ? 450 GLY A C 1 ATOM 2913 O O . GLY A 1 450 ? -31.632 -72.195 97.316 1.00 144.04 ? 450 GLY A O 1 ATOM 2914 N N . PRO A 1 451 ? -32.378 -74.088 98.273 1.00 117.83 ? 451 PRO A N 1 ATOM 2915 C CA . PRO A 1 451 ? -32.119 -75.014 97.158 1.00 123.33 ? 451 PRO A CA 1 ATOM 2916 C C . PRO A 1 451 ? -32.798 -74.645 95.828 1.00 121.56 ? 451 PRO A C 1 ATOM 2917 O O . PRO A 1 451 ? -33.796 -73.905 95.815 1.00 114.18 ? 451 PRO A O 1 ATOM 2918 C CB . PRO A 1 451 ? -32.708 -76.317 97.675 1.00 138.52 ? 451 PRO A CB 1 ATOM 2919 C CG . PRO A 1 451 ? -33.788 -75.861 98.610 1.00 129.42 ? 451 PRO A CG 1 ATOM 2920 C CD . PRO A 1 451 ? -33.126 -74.744 99.347 1.00 117.21 ? 451 PRO A CD 1 ATOM 2921 N N . LEU A 1 452 ? -32.274 -75.182 94.725 1.00 116.71 ? 452 LEU A N 1 ATOM 2922 C CA . LEU A 1 452 ? -32.721 -74.752 93.393 1.00 121.18 ? 452 LEU A CA 1 ATOM 2923 C C . LEU A 1 452 ? -33.925 -75.508 92.899 1.00 113.49 ? 452 LEU A C 1 ATOM 2924 O O . LEU A 1 452 ? -33.798 -76.647 92.465 1.00 126.83 ? 452 LEU A O 1 ATOM 2925 C CB . LEU A 1 452 ? -31.607 -74.935 92.354 1.00 133.86 ? 452 LEU A CB 1 ATOM 2926 C CG . LEU A 1 452 ? -31.607 -74.066 91.072 1.00 134.40 ? 452 LEU A CG 1 ATOM 2927 C CD1 . LEU A 1 452 ? -30.946 -74.809 89.903 1.00 123.75 ? 452 LEU A CD1 1 ATOM 2928 C CD2 . LEU A 1 452 ? -32.972 -73.480 90.679 1.00 120.39 ? 452 LEU A CD2 1 ATOM 2929 N N . LEU A 1 453 ? -35.090 -74.882 92.908 1.00 104.40 ? 453 LEU A N 1 ATOM 2930 C CA . LEU A 1 453 ? -36.267 -75.602 92.424 1.00 109.65 ? 453 LEU A CA 1 ATOM 2931 C C . LEU A 1 453 ? -36.389 -75.488 90.916 1.00 113.09 ? 453 LEU A C 1 ATOM 2932 O O . LEU A 1 453 ? -36.279 -74.409 90.351 1.00 126.08 ? 453 LEU A O 1 ATOM 2933 C CB . LEU A 1 453 ? -37.535 -75.132 93.126 1.00 101.17 ? 453 LEU A CB 1 ATOM 2934 C CG . LEU A 1 453 ? -37.612 -75.434 94.624 1.00 101.33 ? 453 LEU A CG 1 ATOM 2935 C CD1 . LEU A 1 453 ? -36.316 -75.137 95.368 1.00 101.76 ? 453 LEU A CD1 1 ATOM 2936 C CD2 . LEU A 1 453 ? -38.762 -74.682 95.273 1.00 103.24 ? 453 LEU A CD2 1 ATOM 2937 N N . TYR A 1 454 ? -36.585 -76.609 90.255 1.00 108.18 ? 454 TYR A N 1 ATOM 2938 C CA . TYR A 1 454 ? -36.672 -76.580 88.821 1.00 111.21 ? 454 TYR A CA 1 ATOM 2939 C C . TYR A 1 454 ? -37.899 -77.383 88.466 1.00 112.91 ? 454 TYR A C 1 ATOM 2940 O O . TYR A 1 454 ? -38.317 -78.230 89.241 1.00 122.17 ? 454 TYR A O 1 ATOM 2941 C CB . TYR A 1 454 ? -35.396 -77.187 88.211 1.00 121.14 ? 454 TYR A CB 1 ATOM 2942 C CG . TYR A 1 454 ? -35.424 -77.405 86.701 1.00 136.09 ? 454 TYR A CG 1 ATOM 2943 C CD1 . TYR A 1 454 ? -35.434 -76.330 85.815 1.00 143.22 ? 454 TYR A CD1 1 ATOM 2944 C CD2 . TYR A 1 454 ? -35.440 -78.690 86.157 1.00 145.35 ? 454 TYR A CD2 1 ATOM 2945 C CE1 . TYR A 1 454 ? -35.465 -76.533 84.433 1.00 157.80 ? 454 TYR A CE1 1 ATOM 2946 C CE2 . TYR A 1 454 ? -35.474 -78.901 84.777 1.00 154.78 ? 454 TYR A CE2 1 ATOM 2947 C CZ . TYR A 1 454 ? -35.483 -77.821 83.913 1.00 157.83 ? 454 TYR A CZ 1 ATOM 2948 O OH . TYR A 1 454 ? -35.516 -78.012 82.539 1.00 151.95 ? 454 TYR A OH 1 ATOM 2949 N N . GLY A 1 455 ? -38.491 -77.091 87.315 1.00 111.01 ? 455 GLY A N 1 ATOM 2950 C CA . GLY A 1 455 ? -39.504 -77.954 86.722 1.00 106.84 ? 455 GLY A CA 1 ATOM 2951 C C . GLY A 1 455 ? -39.946 -77.454 85.361 1.00 111.51 ? 455 GLY A C 1 ATOM 2952 O O . GLY A 1 455 ? -40.215 -76.247 85.172 1.00 105.57 ? 455 GLY A O 1 ATOM 2953 N N . GLU A 1 456 ? -40.019 -78.395 84.420 1.00 114.81 ? 456 GLU A N 1 ATOM 2954 C CA . GLU A 1 456 ? -40.456 -78.137 83.041 1.00 123.33 ? 456 GLU A CA 1 ATOM 2955 C C . GLU A 1 456 ? -41.985 -78.045 82.939 1.00 117.79 ? 456 GLU A C 1 ATOM 2956 O O . GLU A 1 456 ? -42.669 -78.618 83.773 1.00 126.47 ? 456 GLU A O 1 ATOM 2957 C CB . GLU A 1 456 ? -39.979 -79.286 82.155 1.00 137.29 ? 456 GLU A CB 1 ATOM 2958 C CG . GLU A 1 456 ? -38.470 -79.489 82.108 1.00 148.62 ? 456 GLU A CG 1 ATOM 2959 C CD . GLU A 1 456 ? -38.092 -80.769 81.382 1.00 160.98 ? 456 GLU A CD 1 ATOM 2960 O OE1 . GLU A 1 456 ? -38.455 -81.853 81.898 1.00 170.98 ? 456 GLU A OE1 1 ATOM 2961 O OE2 . GLU A 1 456 ? -37.444 -80.696 80.303 1.00 154.72 ? 456 GLU A OE2 1 ATOM 2962 N N . VAL A 1 457 ? -42.536 -77.352 81.931 1.00 109.47 ? 457 VAL A N 1 ATOM 2963 C CA . VAL A 1 457 ? -44.006 -77.359 81.736 1.00 105.68 ? 457 VAL A CA 1 ATOM 2964 C C . VAL A 1 457 ? -44.514 -78.800 81.755 1.00 119.93 ? 457 VAL A C 1 ATOM 2965 O O . VAL A 1 457 ? -43.817 -79.723 81.307 1.00 128.16 ? 457 VAL A O 1 ATOM 2966 C CB . VAL A 1 457 ? -44.504 -76.592 80.486 1.00 99.46 ? 457 VAL A CB 1 ATOM 2967 C CG1 . VAL A 1 457 ? -43.990 -75.176 80.504 1.00 101.59 ? 457 VAL A CG1 1 ATOM 2968 C CG2 . VAL A 1 457 ? -44.038 -77.235 79.199 1.00 112.91 ? 457 VAL A CG2 1 ATOM 2969 N N . GLY A 1 458 ? -45.701 -78.996 82.328 1.00 130.34 ? 458 GLY A N 1 ATOM 2970 C CA . GLY A 1 458 ? -46.291 -80.336 82.487 1.00 121.47 ? 458 GLY A CA 1 ATOM 2971 C C . GLY A 1 458 ? -45.947 -80.972 83.810 1.00 112.21 ? 458 GLY A C 1 ATOM 2972 O O . GLY A 1 458 ? -46.829 -81.538 84.452 1.00 108.70 ? 458 GLY A O 1 ATOM 2973 N N . ASP A 1 459 ? -44.654 -80.862 84.169 1.00 118.65 ? 459 ASP A N 1 ATOM 2974 C CA . ASP A 1 459 ? -44.011 -81.276 85.446 1.00 121.22 ? 459 ASP A CA 1 ATOM 2975 C C . ASP A 1 459 ? -44.683 -80.733 86.680 1.00 112.88 ? 459 ASP A C 1 ATOM 2976 O O . ASP A 1 459 ? -45.284 -79.661 86.663 1.00 107.95 ? 459 ASP A O 1 ATOM 2977 C CB . ASP A 1 459 ? -42.572 -80.740 85.530 1.00 128.68 ? 459 ASP A CB 1 ATOM 2978 C CG . ASP A 1 459 ? -41.511 -81.761 85.172 1.00 140.39 ? 459 ASP A CG 1 ATOM 2979 O OD1 . ASP A 1 459 ? -41.789 -82.728 84.419 1.00 140.29 ? 459 ASP A OD1 1 ATOM 2980 O OD2 . ASP A 1 459 ? -40.367 -81.549 85.646 1.00 147.51 ? 459 ASP A OD2 1 ATOM 2981 N N . THR A 1 460 ? -44.515 -81.449 87.776 1.00 109.07 ? 460 THR A N 1 ATOM 2982 C CA . THR A 1 460 ? -45.157 -81.047 88.990 1.00 112.70 ? 460 THR A CA 1 ATOM 2983 C C . THR A 1 460 ? -44.146 -81.061 90.099 1.00 118.06 ? 460 THR A C 1 ATOM 2984 O O . THR A 1 460 ? -43.507 -82.084 90.315 1.00 136.94 ? 460 THR A O 1 ATOM 2985 C CB . THR A 1 460 ? -46.245 -82.040 89.388 1.00 118.43 ? 460 THR A CB 1 ATOM 2986 O OG1 . THR A 1 460 ? -46.729 -82.779 88.244 1.00 130.03 ? 460 THR A OG1 1 ATOM 2987 C CG2 . THR A 1 460 ? -47.344 -81.290 90.053 1.00 117.04 ? 460 THR A CG2 1 ATOM 2988 N N . LEU A 1 461 ? -43.988 -79.944 90.806 1.00 114.04 ? 461 LEU A N 1 ATOM 2989 C CA . LEU A 1 461 ? -43.163 -79.950 92.017 1.00 108.79 ? 461 LEU A CA 1 ATOM 2990 C C . LEU A 1 461 ? -43.953 -80.437 93.228 1.00 117.65 ? 461 LEU A C 1 ATOM 2991 O O . LEU A 1 461 ? -45.198 -80.484 93.219 1.00 119.42 ? 461 LEU A O 1 ATOM 2992 C CB . LEU A 1 461 ? -42.507 -78.605 92.293 1.00 99.52 ? 461 LEU A CB 1 ATOM 2993 C CG . LEU A 1 461 ? -41.406 -78.304 91.288 1.00 105.78 ? 461 LEU A CG 1 ATOM 2994 C CD1 . LEU A 1 461 ? -41.969 -77.351 90.255 1.00 116.38 ? 461 LEU A CD1 1 ATOM 2995 C CD2 . LEU A 1 461 ? -40.159 -77.681 91.902 1.00 112.91 ? 461 LEU A CD2 1 ATOM 2996 N N . LEU A 1 462 ? -43.215 -80.817 94.266 1.00 115.88 ? 462 LEU A N 1 ATOM 2997 C CA . LEU A 1 462 ? -43.802 -81.533 95.384 1.00 108.69 ? 462 LEU A CA 1 ATOM 2998 C C . LEU A 1 462 ? -43.069 -81.227 96.669 1.00 108.06 ? 462 LEU A C 1 ATOM 2999 O O . LEU A 1 462 ? -42.141 -81.925 97.088 1.00 105.39 ? 462 LEU A O 1 ATOM 3000 C CB . LEU A 1 462 ? -43.776 -83.014 95.101 1.00 104.49 ? 462 LEU A CB 1 ATOM 3001 C CG . LEU A 1 462 ? -45.038 -83.669 95.581 1.00 99.19 ? 462 LEU A CG 1 ATOM 3002 C CD1 . LEU A 1 462 ? -44.843 -85.161 95.397 1.00 101.28 ? 462 LEU A CD1 1 ATOM 3003 C CD2 . LEU A 1 462 ? -45.276 -83.279 97.029 1.00 95.44 ? 462 LEU A CD2 1 ATOM 3004 N N . ILE A 1 463 ? -43.539 -80.172 97.301 1.00 111.69 ? 463 ILE A N 1 ATOM 3005 C CA . ILE A 1 463 ? -42.762 -79.491 98.289 1.00 115.60 ? 463 ILE A CA 1 ATOM 3006 C C . ILE A 1 463 ? -43.261 -79.880 99.646 1.00 115.82 ? 463 ILE A C 1 ATOM 3007 O O . ILE A 1 463 ? -44.278 -79.357 100.105 1.00 121.50 ? 463 ILE A O 1 ATOM 3008 C CB . ILE A 1 463 ? -42.872 -77.965 98.112 1.00 116.09 ? 463 ILE A CB 1 ATOM 3009 C CG1 . ILE A 1 463 ? -42.545 -77.562 96.677 1.00 123.96 ? 463 ILE A CG1 1 ATOM 3010 C CG2 . ILE A 1 463 ? -41.910 -77.255 99.031 1.00 122.74 ? 463 ILE A CG2 1 ATOM 3011 C CD1 . ILE A 1 463 ? -41.194 -78.057 96.205 1.00 139.88 ? 463 ILE A CD1 1 ATOM 3012 N N . ILE A 1 464 ? -42.555 -80.809 100.280 1.00 115.47 ? 464 ILE A N 1 ATOM 3013 C CA . ILE A 1 464 ? -42.783 -81.045 101.693 1.00 113.41 ? 464 ILE A CA 1 ATOM 3014 C C . ILE A 1 464 ? -41.872 -80.173 102.536 1.00 114.74 ? 464 ILE A C 1 ATOM 3015 O O . ILE A 1 464 ? -40.644 -80.326 102.549 1.00 111.31 ? 464 ILE A O 1 ATOM 3016 C CB . ILE A 1 464 ? -42.631 -82.497 102.115 1.00 112.90 ? 464 ILE A CB 1 ATOM 3017 C CG1 . ILE A 1 464 ? -43.370 -83.423 101.147 1.00 118.82 ? 464 ILE A CG1 1 ATOM 3018 C CG2 . ILE A 1 464 ? -43.184 -82.627 103.518 1.00 110.25 ? 464 ILE A CG2 1 ATOM 3019 C CD1 . ILE A 1 464 ? -42.486 -84.064 100.102 1.00 117.50 ? 464 ILE A CD1 1 ATOM 3020 N N . PHE A 1 465 ? -42.513 -79.251 103.240 1.00 115.71 ? 465 PHE A N 1 ATOM 3021 C CA . PHE A 1 465 ? -41.834 -78.188 103.927 1.00 114.02 ? 465 PHE A CA 1 ATOM 3022 C C . PHE A 1 465 ? -42.041 -78.369 105.403 1.00 124.37 ? 465 PHE A C 1 ATOM 3023 O O . PHE A 1 465 ? -43.183 -78.515 105.852 1.00 132.25 ? 465 PHE A O 1 ATOM 3024 C CB . PHE A 1 465 ? -42.452 -76.875 103.509 1.00 109.03 ? 465 PHE A CB 1 ATOM 3025 C CG . PHE A 1 465 ? -42.113 -75.740 104.407 1.00 113.13 ? 465 PHE A CG 1 ATOM 3026 C CD1 . PHE A 1 465 ? -40.908 -75.079 104.280 1.00 113.76 ? 465 PHE A CD1 1 ATOM 3027 C CD2 . PHE A 1 465 ? -43.003 -75.319 105.376 1.00 121.48 ? 465 PHE A CD2 1 ATOM 3028 C CE1 . PHE A 1 465 ? -40.594 -74.007 105.102 1.00 117.16 ? 465 PHE A CE1 1 ATOM 3029 C CE2 . PHE A 1 465 ? -42.692 -74.256 106.208 1.00 125.24 ? 465 PHE A CE2 1 ATOM 3030 C CZ . PHE A 1 465 ? -41.486 -73.594 106.066 1.00 120.89 ? 465 PHE A CZ 1 ATOM 3031 N N . LYS A 1 466 ? -40.944 -78.373 106.154 1.00 123.32 ? 466 LYS A N 1 ATOM 3032 C CA . LYS A 1 466 ? -41.033 -78.364 107.609 1.00 124.03 ? 466 LYS A CA 1 ATOM 3033 C C . LYS A 1 466 ? -40.542 -77.020 108.063 1.00 117.71 ? 466 LYS A C 1 ATOM 3034 O O . LYS A 1 466 ? -39.678 -76.433 107.430 1.00 120.11 ? 466 LYS A O 1 ATOM 3035 C CB . LYS A 1 466 ? -40.186 -79.471 108.255 1.00 128.09 ? 466 LYS A CB 1 ATOM 3036 C CG . LYS A 1 466 ? -40.382 -79.578 109.769 1.00 136.75 ? 466 LYS A CG 1 ATOM 3037 C CD . LYS A 1 466 ? -39.555 -80.665 110.460 1.00 141.20 ? 466 LYS A CD 1 ATOM 3038 C CE . LYS A 1 466 ? -39.668 -80.545 111.987 1.00 148.17 ? 466 LYS A CE 1 ATOM 3039 N NZ . LYS A 1 466 ? -39.251 -81.736 112.789 1.00 149.75 ? 466 LYS A NZ 1 ATOM 3040 N N . ASN A 1 467 ? -41.089 -76.528 109.160 1.00 116.24 ? 467 ASN A N 1 ATOM 3041 C CA . ASN A 1 467 ? -40.537 -75.339 109.766 1.00 120.81 ? 467 ASN A CA 1 ATOM 3042 C C . ASN A 1 467 ? -39.817 -75.674 111.053 1.00 124.31 ? 467 ASN A C 1 ATOM 3043 O O . ASN A 1 467 ? -40.452 -75.974 112.057 1.00 138.49 ? 467 ASN A O 1 ATOM 3044 C CB . ASN A 1 467 ? -41.636 -74.305 110.022 1.00 122.24 ? 467 ASN A CB 1 ATOM 3045 C CG . ASN A 1 467 ? -41.141 -73.097 110.800 1.00 120.01 ? 467 ASN A CG 1 ATOM 3046 O OD1 . ASN A 1 467 ? -39.999 -72.654 110.644 1.00 111.84 ? 467 ASN A OD1 1 ATOM 3047 N ND2 . ASN A 1 467 ? -42.009 -72.554 111.645 1.00 125.43 ? 467 ASN A ND2 1 ATOM 3048 N N . GLN A 1 468 ? -38.496 -75.631 111.032 1.00 123.34 ? 468 GLN A N 1 ATOM 3049 C CA . GLN A 1 468 ? -37.759 -75.674 112.280 1.00 137.80 ? 468 GLN A CA 1 ATOM 3050 C C . GLN A 1 468 ? -37.207 -74.269 112.535 1.00 145.35 ? 468 GLN A C 1 ATOM 3051 O O . GLN A 1 468 ? -36.283 -73.831 111.851 1.00 152.61 ? 468 GLN A O 1 ATOM 3052 C CB . GLN A 1 468 ? -36.646 -76.705 112.203 1.00 146.46 ? 468 GLN A CB 1 ATOM 3053 C CG . GLN A 1 468 ? -37.067 -78.061 111.662 1.00 150.25 ? 468 GLN A CG 1 ATOM 3054 C CD . GLN A 1 468 ? -35.892 -79.018 111.513 1.00 160.07 ? 468 GLN A CD 1 ATOM 3055 O OE1 . GLN A 1 468 ? -35.771 -79.995 112.261 1.00 167.57 ? 468 GLN A OE1 1 ATOM 3056 N NE2 . GLN A 1 468 ? -35.006 -78.731 110.556 1.00 151.52 ? 468 GLN A NE2 1 ATOM 3057 N N . ALA A 1 469 ? -37.782 -73.566 113.512 1.00 150.53 ? 469 ALA A N 1 ATOM 3058 C CA . ALA A 1 469 ? -37.559 -72.117 113.715 1.00 153.63 ? 469 ALA A CA 1 ATOM 3059 C C . ALA A 1 469 ? -38.746 -71.514 114.473 1.00 158.42 ? 469 ALA A C 1 ATOM 3060 O O . ALA A 1 469 ? -39.822 -72.115 114.486 1.00 183.27 ? 469 ALA A O 1 ATOM 3061 C CB . ALA A 1 469 ? -37.380 -71.404 112.380 1.00 153.65 ? 469 ALA A CB 1 ATOM 3062 N N . SER A 1 470 ? -38.583 -70.329 115.067 1.00 144.18 ? 470 SER A N 1 ATOM 3063 C CA . SER A 1 470 ? -39.585 -69.827 116.033 1.00 149.53 ? 470 SER A CA 1 ATOM 3064 C C . SER A 1 470 ? -40.853 -69.098 115.510 1.00 155.96 ? 470 SER A C 1 ATOM 3065 O O . SER A 1 470 ? -41.840 -68.964 116.247 1.00 183.05 ? 470 SER A O 1 ATOM 3066 C CB . SER A 1 470 ? -38.910 -69.029 117.153 1.00 145.81 ? 470 SER A CB 1 ATOM 3067 O OG . SER A 1 470 ? -37.986 -68.111 116.619 1.00 141.19 ? 470 SER A OG 1 ATOM 3068 N N . ARG A 1 471 ? -40.848 -68.639 114.263 1.00 148.70 ? 471 ARG A N 1 ATOM 3069 C CA . ARG A 1 471 ? -42.030 -67.970 113.717 1.00 145.05 ? 471 ARG A CA 1 ATOM 3070 C C . ARG A 1 471 ? -42.728 -68.798 112.665 1.00 144.34 ? 471 ARG A C 1 ATOM 3071 O O . ARG A 1 471 ? -42.082 -69.436 111.830 1.00 144.02 ? 471 ARG A O 1 ATOM 3072 C CB . ARG A 1 471 ? -41.682 -66.615 113.101 1.00 149.56 ? 471 ARG A CB 1 ATOM 3073 C CG . ARG A 1 471 ? -42.801 -65.990 112.262 1.00 160.62 ? 471 ARG A CG 1 ATOM 3074 C CD . ARG A 1 471 ? -42.744 -64.476 112.250 1.00 163.95 ? 471 ARG A CD 1 ATOM 3075 N NE . ARG A 1 471 ? -42.685 -63.958 113.613 1.00 183.75 ? 471 ARG A NE 1 ATOM 3076 C CZ . ARG A 1 471 ? -41.570 -63.867 114.342 1.00 194.18 ? 471 ARG A CZ 1 ATOM 3077 N NH1 . ARG A 1 471 ? -40.407 -64.232 113.824 1.00 193.68 ? 471 ARG A NH1 1 ATOM 3078 N NH2 . ARG A 1 471 ? -41.609 -63.401 115.588 1.00 212.22 ? 471 ARG A NH2 1 ATOM 3079 N N . PRO A 1 472 ? -44.063 -68.780 112.693 1.00 149.03 ? 472 PRO A N 1 ATOM 3080 C CA . PRO A 1 472 ? -44.833 -69.205 111.529 1.00 154.21 ? 472 PRO A CA 1 ATOM 3081 C C . PRO A 1 472 ? -44.245 -68.669 110.199 1.00 151.13 ? 472 PRO A C 1 ATOM 3082 O O . PRO A 1 472 ? -44.322 -67.463 109.939 1.00 168.07 ? 472 PRO A O 1 ATOM 3083 C CB . PRO A 1 472 ? -46.211 -68.592 111.807 1.00 155.75 ? 472 PRO A CB 1 ATOM 3084 C CG . PRO A 1 472 ? -46.312 -68.580 113.307 1.00 157.70 ? 472 PRO A CG 1 ATOM 3085 C CD . PRO A 1 472 ? -44.917 -68.554 113.878 1.00 149.89 ? 472 PRO A CD 1 ATOM 3086 N N . TYR A 1 473 ? -43.637 -69.548 109.395 1.00 131.42 ? 473 TYR A N 1 ATOM 3087 C CA . TYR A 1 473 ? -43.197 -69.195 108.033 1.00 126.19 ? 473 TYR A CA 1 ATOM 3088 C C . TYR A 1 473 ? -43.872 -70.107 107.034 1.00 123.57 ? 473 TYR A C 1 ATOM 3089 O O . TYR A 1 473 ? -44.525 -71.048 107.467 1.00 126.06 ? 473 TYR A O 1 ATOM 3090 C CB . TYR A 1 473 ? -41.691 -69.344 107.899 1.00 121.97 ? 473 TYR A CB 1 ATOM 3091 C CG . TYR A 1 473 ? -40.934 -68.378 108.743 1.00 125.68 ? 473 TYR A CG 1 ATOM 3092 C CD1 . TYR A 1 473 ? -41.232 -67.020 108.707 1.00 133.06 ? 473 TYR A CD1 1 ATOM 3093 C CD2 . TYR A 1 473 ? -39.928 -68.812 109.592 1.00 134.14 ? 473 TYR A CD2 1 ATOM 3094 C CE1 . TYR A 1 473 ? -40.539 -66.113 109.497 1.00 144.98 ? 473 TYR A CE1 1 ATOM 3095 C CE2 . TYR A 1 473 ? -39.221 -67.915 110.385 1.00 144.03 ? 473 TYR A CE2 1 ATOM 3096 C CZ . TYR A 1 473 ? -39.532 -66.562 110.337 1.00 143.39 ? 473 TYR A CZ 1 ATOM 3097 O OH . TYR A 1 473 ? -38.844 -65.662 111.127 1.00 131.91 ? 473 TYR A OH 1 ATOM 3098 N N . ASN A 1 474 ? -43.725 -69.842 105.724 1.00 117.75 ? 474 ASN A N 1 ATOM 3099 C CA . ASN A 1 474 ? -44.193 -70.792 104.676 1.00 121.53 ? 474 ASN A CA 1 ATOM 3100 C C . ASN A 1 474 ? -43.472 -70.775 103.332 1.00 114.32 ? 474 ASN A C 1 ATOM 3101 O O . ASN A 1 474 ? -42.559 -70.004 103.155 1.00 108.61 ? 474 ASN A O 1 ATOM 3102 C CB . ASN A 1 474 ? -45.729 -70.737 104.465 1.00 128.86 ? 474 ASN A CB 1 ATOM 3103 C CG . ASN A 1 474 ? -46.233 -69.390 103.992 1.00 115.12 ? 474 ASN A CG 1 ATOM 3104 O OD1 . ASN A 1 474 ? -45.548 -68.378 104.102 1.00 109.00 ? 474 ASN A OD1 1 ATOM 3105 N ND2 . ASN A 1 474 ? -47.465 -69.379 103.478 1.00 107.49 ? 474 ASN A ND2 1 ATOM 3106 N N . ILE A 1 475 ? -43.867 -71.644 102.399 1.00 120.83 ? 475 ILE A N 1 ATOM 3107 C CA . ILE A 1 475 ? -43.461 -71.442 101.001 1.00 126.09 ? 475 ILE A CA 1 ATOM 3108 C C . ILE A 1 475 ? -44.536 -71.318 99.933 1.00 127.76 ? 475 ILE A C 1 ATOM 3109 O O . ILE A 1 475 ? -45.313 -72.266 99.660 1.00 117.05 ? 475 ILE A O 1 ATOM 3110 C CB . ILE A 1 475 ? -42.395 -72.409 100.453 1.00 129.36 ? 475 ILE A CB 1 ATOM 3111 C CG1 . ILE A 1 475 ? -42.484 -73.784 101.078 1.00 137.30 ? 475 ILE A CG1 1 ATOM 3112 C CG2 . ILE A 1 475 ? -41.007 -71.818 100.593 1.00 124.49 ? 475 ILE A CG2 1 ATOM 3113 C CD1 . ILE A 1 475 ? -41.307 -74.622 100.641 1.00 155.12 ? 475 ILE A CD1 1 ATOM 3114 N N . TYR A 1 476 ? -44.507 -70.150 99.298 1.00 120.89 ? 476 TYR A N 1 ATOM 3115 C CA . TYR A 1 476 ? -45.121 -69.964 97.998 1.00 113.67 ? 476 TYR A CA 1 ATOM 3116 C C . TYR A 1 476 ? -44.085 -69.566 96.939 1.00 110.39 ? 476 TYR A C 1 ATOM 3117 O O . TYR A 1 476 ? -43.074 -68.911 97.241 1.00 95.57 ? 476 TYR A O 1 ATOM 3118 C CB . TYR A 1 476 ? -46.192 -68.913 98.070 1.00 108.20 ? 476 TYR A CB 1 ATOM 3119 C CG . TYR A 1 476 ? -47.368 -69.214 97.212 1.00 112.38 ? 476 TYR A CG 1 ATOM 3120 C CD1 . TYR A 1 476 ? -47.428 -68.776 95.897 1.00 123.70 ? 476 TYR A CD1 1 ATOM 3121 C CD2 . TYR A 1 476 ? -48.446 -69.918 97.721 1.00 123.04 ? 476 TYR A CD2 1 ATOM 3122 C CE1 . TYR A 1 476 ? -48.540 -69.041 95.103 1.00 143.30 ? 476 TYR A CE1 1 ATOM 3123 C CE2 . TYR A 1 476 ? -49.566 -70.187 96.947 1.00 138.29 ? 476 TYR A CE2 1 ATOM 3124 C CZ . TYR A 1 476 ? -49.609 -69.749 95.638 1.00 144.49 ? 476 TYR A CZ 1 ATOM 3125 O OH . TYR A 1 476 ? -50.725 -70.026 94.883 1.00 149.80 ? 476 TYR A OH 1 ATOM 3126 N N . PRO A 1 477 ? -44.312 -70.008 95.695 1.00 111.35 ? 477 PRO A N 1 ATOM 3127 C CA . PRO A 1 477 ? -43.456 -69.536 94.651 1.00 110.97 ? 477 PRO A CA 1 ATOM 3128 C C . PRO A 1 477 ? -44.225 -68.567 93.767 1.00 124.33 ? 477 PRO A C 1 ATOM 3129 O O . PRO A 1 477 ? -45.413 -68.761 93.480 1.00 126.71 ? 477 PRO A O 1 ATOM 3130 C CB . PRO A 1 477 ? -43.116 -70.824 93.891 1.00 104.21 ? 477 PRO A CB 1 ATOM 3131 C CG . PRO A 1 477 ? -44.326 -71.677 94.043 1.00 103.91 ? 477 PRO A CG 1 ATOM 3132 C CD . PRO A 1 477 ? -45.096 -71.178 95.251 1.00 112.85 ? 477 PRO A CD 1 ATOM 3133 N N . HIS A 1 478 ? -43.548 -67.511 93.353 1.00 140.58 ? 478 HIS A N 1 ATOM 3134 C CA . HIS A 1 478 ? -44.100 -66.624 92.350 1.00 148.65 ? 478 HIS A CA 1 ATOM 3135 C C . HIS A 1 478 ? -43.608 -67.061 90.934 1.00 140.77 ? 478 HIS A C 1 ATOM 3136 O O . HIS A 1 478 ? -42.428 -67.402 90.721 1.00 116.23 ? 478 HIS A O 1 ATOM 3137 C CB . HIS A 1 478 ? -43.856 -65.148 92.760 1.00 145.51 ? 478 HIS A CB 1 ATOM 3138 C CG . HIS A 1 478 ? -43.578 -64.223 91.619 1.00 148.08 ? 478 HIS A CG 1 ATOM 3139 N ND1 . HIS A 1 478 ? -42.364 -63.594 91.457 1.00 136.21 ? 478 HIS A ND1 1 ATOM 3140 C CD2 . HIS A 1 478 ? -44.352 -63.822 90.581 1.00 165.52 ? 478 HIS A CD2 1 ATOM 3141 C CE1 . HIS A 1 478 ? -42.397 -62.850 90.365 1.00 141.44 ? 478 HIS A CE1 1 ATOM 3142 N NE2 . HIS A 1 478 ? -43.592 -62.970 89.815 1.00 153.52 ? 478 HIS A NE2 1 ATOM 3143 N N . GLY A 1 479 ? -44.556 -67.107 89.998 1.00 148.15 ? 479 GLY A N 1 ATOM 3144 C CA . GLY A 1 479 ? -44.309 -67.495 88.604 1.00 150.37 ? 479 GLY A CA 1 ATOM 3145 C C . GLY A 1 479 ? -45.330 -68.530 88.190 1.00 148.88 ? 479 GLY A C 1 ATOM 3146 O O . GLY A 1 479 ? -45.968 -68.416 87.105 1.00 147.67 ? 479 GLY A O 1 ATOM 3147 N N . ILE A 1 480 ? -45.457 -69.521 89.089 1.00 132.78 ? 480 ILE A N 1 ATOM 3148 C CA . ILE A 1 480 ? -46.456 -70.601 89.048 1.00 131.23 ? 480 ILE A CA 1 ATOM 3149 C C . ILE A 1 480 ? -47.795 -70.197 89.675 1.00 138.71 ? 480 ILE A C 1 ATOM 3150 O O . ILE A 1 480 ? -47.877 -69.293 90.533 1.00 147.68 ? 480 ILE A O 1 ATOM 3151 C CB . ILE A 1 480 ? -45.992 -71.882 89.777 1.00 122.64 ? 480 ILE A CB 1 ATOM 3152 C CG1 . ILE A 1 480 ? -44.505 -72.139 89.553 1.00 128.98 ? 480 ILE A CG1 1 ATOM 3153 C CG2 . ILE A 1 480 ? -46.825 -73.084 89.343 1.00 112.41 ? 480 ILE A CG2 1 ATOM 3154 C CD1 . ILE A 1 480 ? -43.862 -72.993 90.627 1.00 136.26 ? 480 ILE A CD1 1 ATOM 3155 N N . THR A 1 481 ? -48.825 -70.928 89.258 1.00 128.41 ? 481 THR A N 1 ATOM 3156 C CA . THR A 1 481 ? -50.203 -70.526 89.405 1.00 122.85 ? 481 THR A CA 1 ATOM 3157 C C . THR A 1 481 ? -51.022 -71.632 90.039 1.00 126.11 ? 481 THR A C 1 ATOM 3158 O O . THR A 1 481 ? -52.038 -71.350 90.646 1.00 144.61 ? 481 THR A O 1 ATOM 3159 C CB . THR A 1 481 ? -50.822 -70.242 88.025 1.00 127.19 ? 481 THR A CB 1 ATOM 3160 O OG1 . THR A 1 481 ? -50.703 -71.419 87.214 1.00 131.88 ? 481 THR A OG1 1 ATOM 3161 C CG2 . THR A 1 481 ? -50.135 -69.045 87.310 1.00 132.19 ? 481 THR A CG2 1 ATOM 3162 N N . ASP A 1 482 ? -50.605 -72.886 89.875 1.00 134.35 ? 482 ASP A N 1 ATOM 3163 C CA . ASP A 1 482 ? -51.326 -74.040 90.447 1.00 141.35 ? 482 ASP A CA 1 ATOM 3164 C C . ASP A 1 482 ? -50.653 -74.485 91.754 1.00 138.32 ? 482 ASP A C 1 ATOM 3165 O O . ASP A 1 482 ? -49.770 -75.349 91.731 1.00 158.37 ? 482 ASP A O 1 ATOM 3166 C CB . ASP A 1 482 ? -51.396 -75.200 89.420 1.00 149.31 ? 482 ASP A CB 1 ATOM 3167 C CG . ASP A 1 482 ? -52.344 -76.350 89.842 1.00 162.07 ? 482 ASP A CG 1 ATOM 3168 O OD1 . ASP A 1 482 ? -52.205 -76.893 90.962 1.00 170.10 ? 482 ASP A OD1 1 ATOM 3169 O OD2 . ASP A 1 482 ? -53.211 -76.748 89.026 1.00 167.25 ? 482 ASP A OD2 1 ATOM 3170 N N . VAL A 1 483 ? -51.050 -73.882 92.881 1.00 124.41 ? 483 VAL A N 1 ATOM 3171 C CA . VAL A 1 483 ? -50.523 -74.272 94.207 1.00 120.33 ? 483 VAL A CA 1 ATOM 3172 C C . VAL A 1 483 ? -51.597 -74.593 95.252 1.00 123.51 ? 483 VAL A C 1 ATOM 3173 O O . VAL A 1 483 ? -52.233 -73.700 95.866 1.00 119.38 ? 483 VAL A O 1 ATOM 3174 C CB . VAL A 1 483 ? -49.533 -73.255 94.793 1.00 119.68 ? 483 VAL A CB 1 ATOM 3175 C CG1 . VAL A 1 483 ? -48.815 -73.876 95.981 1.00 122.37 ? 483 VAL A CG1 1 ATOM 3176 C CG2 . VAL A 1 483 ? -48.525 -72.813 93.747 1.00 120.22 ? 483 VAL A CG2 1 ATOM 3177 N N . ARG A 1 484 ? -51.776 -75.897 95.437 1.00 125.08 ? 484 ARG A N 1 ATOM 3178 C CA . ARG A 1 484 ? -52.763 -76.430 96.355 1.00 128.15 ? 484 ARG A CA 1 ATOM 3179 C C . ARG A 1 484 ? -52.022 -77.357 97.266 1.00 115.77 ? 484 ARG A C 1 ATOM 3180 O O . ARG A 1 484 ? -50.979 -77.871 96.890 1.00 104.00 ? 484 ARG A O 1 ATOM 3181 C CB . ARG A 1 484 ? -53.919 -77.163 95.628 1.00 140.69 ? 484 ARG A CB 1 ATOM 3182 C CG . ARG A 1 484 ? -53.548 -78.366 94.757 1.00 136.39 ? 484 ARG A CG 1 ATOM 3183 C CD . ARG A 1 484 ? -54.742 -78.829 93.919 1.00 137.28 ? 484 ARG A CD 1 ATOM 3184 N NE . ARG A 1 484 ? -54.517 -80.089 93.197 1.00 147.55 ? 484 ARG A NE 1 ATOM 3185 C CZ . ARG A 1 484 ? -54.342 -81.284 93.777 1.00 164.73 ? 484 ARG A CZ 1 ATOM 3186 N NH1 . ARG A 1 484 ? -54.340 -81.400 95.098 1.00 177.25 ? 484 ARG A NH1 1 ATOM 3187 N NH2 . ARG A 1 484 ? -54.148 -82.382 93.047 1.00 165.54 ? 484 ARG A NH2 1 ATOM 3188 N N . PRO A 1 485 ? -52.541 -77.540 98.484 1.00 120.19 ? 485 PRO A N 1 ATOM 3189 C CA . PRO A 1 485 ? -52.058 -78.564 99.390 1.00 129.90 ? 485 PRO A CA 1 ATOM 3190 C C . PRO A 1 485 ? -52.227 -79.884 98.665 1.00 134.61 ? 485 PRO A C 1 ATOM 3191 O O . PRO A 1 485 ? -53.035 -79.941 97.727 1.00 139.42 ? 485 PRO A O 1 ATOM 3192 C CB . PRO A 1 485 ? -53.033 -78.482 100.563 1.00 137.51 ? 485 PRO A CB 1 ATOM 3193 C CG . PRO A 1 485 ? -54.236 -77.774 100.031 1.00 132.27 ? 485 PRO A CG 1 ATOM 3194 C CD . PRO A 1 485 ? -53.704 -76.821 99.026 1.00 123.68 ? 485 PRO A CD 1 ATOM 3195 N N . LEU A 1 486 ? -51.510 -80.929 99.086 1.00 127.53 ? 486 LEU A N 1 ATOM 3196 C CA . LEU A 1 486 ? -51.320 -82.099 98.208 1.00 126.15 ? 486 LEU A CA 1 ATOM 3197 C C . LEU A 1 486 ? -52.566 -82.907 97.778 1.00 127.59 ? 486 LEU A C 1 ATOM 3198 O O . LEU A 1 486 ? -52.740 -83.239 96.578 1.00 126.24 ? 486 LEU A O 1 ATOM 3199 C CB . LEU A 1 486 ? -50.187 -83.011 98.704 1.00 116.14 ? 486 LEU A CB 1 ATOM 3200 C CG . LEU A 1 486 ? -49.650 -84.106 97.742 1.00 112.38 ? 486 LEU A CG 1 ATOM 3201 C CD1 . LEU A 1 486 ? -49.143 -83.672 96.363 1.00 104.02 ? 486 LEU A CD1 1 ATOM 3202 C CD2 . LEU A 1 486 ? -48.560 -84.886 98.437 1.00 108.79 ? 486 LEU A CD2 1 ATOM 3203 N N . TYR A 1 487 ? -53.433 -83.233 98.718 1.00 119.28 ? 487 TYR A N 1 ATOM 3204 C CA . TYR A 1 487 ? -54.435 -84.204 98.355 1.00 127.51 ? 487 TYR A CA 1 ATOM 3205 C C . TYR A 1 487 ? -55.853 -83.665 98.111 1.00 142.07 ? 487 TYR A C 1 ATOM 3206 O O . TYR A 1 487 ? -56.732 -84.390 97.613 1.00 153.76 ? 487 TYR A O 1 ATOM 3207 C CB . TYR A 1 487 ? -54.428 -85.320 99.367 1.00 123.51 ? 487 TYR A CB 1 ATOM 3208 C CG . TYR A 1 487 ? -53.142 -86.109 99.428 1.00 127.67 ? 487 TYR A CG 1 ATOM 3209 C CD1 . TYR A 1 487 ? -51.976 -85.573 99.990 1.00 123.62 ? 487 TYR A CD1 1 ATOM 3210 C CD2 . TYR A 1 487 ? -53.100 -87.428 98.965 1.00 142.62 ? 487 TYR A CD2 1 ATOM 3211 C CE1 . TYR A 1 487 ? -50.804 -86.335 100.079 1.00 132.23 ? 487 TYR A CE1 1 ATOM 3212 C CE2 . TYR A 1 487 ? -51.935 -88.197 99.042 1.00 151.89 ? 487 TYR A CE2 1 ATOM 3213 C CZ . TYR A 1 487 ? -50.783 -87.649 99.598 1.00 146.33 ? 487 TYR A CZ 1 ATOM 3214 O OH . TYR A 1 487 ? -49.640 -88.437 99.662 1.00 150.01 ? 487 TYR A OH 1 ATOM 3215 N N . SER A 1 488 ? -56.070 -82.398 98.446 1.00 144.08 ? 488 SER A N 1 ATOM 3216 C CA . SER A 1 488 ? -57.376 -81.764 98.268 1.00 146.88 ? 488 SER A CA 1 ATOM 3217 C C . SER A 1 488 ? -57.105 -80.374 97.717 1.00 137.41 ? 488 SER A C 1 ATOM 3218 O O . SER A 1 488 ? -55.947 -79.949 97.597 1.00 128.21 ? 488 SER A O 1 ATOM 3219 C CB . SER A 1 488 ? -58.107 -81.666 99.631 1.00 159.18 ? 488 SER A CB 1 ATOM 3220 O OG . SER A 1 488 ? -59.526 -81.798 99.563 1.00 145.25 ? 488 SER A OG 1 ATOM 3221 N N . ARG A 1 489 ? -58.159 -79.657 97.370 1.00 131.67 ? 489 ARG A N 1 ATOM 3222 C CA . ARG A 1 489 ? -58.005 -78.234 97.341 1.00 139.04 ? 489 ARG A CA 1 ATOM 3223 C C . ARG A 1 489 ? -58.477 -77.726 98.705 1.00 150.67 ? 489 ARG A C 1 ATOM 3224 O O . ARG A 1 489 ? -57.736 -77.881 99.670 1.00 157.32 ? 489 ARG A O 1 ATOM 3225 C CB . ARG A 1 489 ? -58.679 -77.613 96.134 1.00 149.28 ? 489 ARG A CB 1 ATOM 3226 C CG . ARG A 1 489 ? -57.947 -77.939 94.841 1.00 162.74 ? 489 ARG A CG 1 ATOM 3227 C CD . ARG A 1 489 ? -58.316 -77.007 93.690 1.00 175.19 ? 489 ARG A CD 1 ATOM 3228 N NE . ARG A 1 489 ? -59.668 -77.144 93.081 1.00 180.11 ? 489 ARG A NE 1 ATOM 3229 C CZ . ARG A 1 489 ? -60.559 -78.154 93.178 1.00 163.98 ? 489 ARG A CZ 1 ATOM 3230 N NH1 . ARG A 1 489 ? -60.370 -79.279 93.894 1.00 143.15 ? 489 ARG A NH1 1 ATOM 3231 N NH2 . ARG A 1 489 ? -61.697 -78.012 92.516 1.00 149.51 ? 489 ARG A NH2 1 ATOM 3232 N N . ARG A 1 490 ? -59.687 -77.168 98.812 1.00 162.12 ? 490 ARG A N 1 ATOM 3233 C CA . ARG A 1 490 ? -60.202 -76.605 100.084 1.00 167.50 ? 490 ARG A CA 1 ATOM 3234 C C . ARG A 1 490 ? -59.086 -76.243 101.090 1.00 170.84 ? 490 ARG A C 1 ATOM 3235 O O . ARG A 1 490 ? -58.731 -77.053 101.941 1.00 177.73 ? 490 ARG A O 1 ATOM 3236 C CB . ARG A 1 490 ? -61.207 -77.574 100.714 1.00 169.28 ? 490 ARG A CB 1 ATOM 3237 C CG . ARG A 1 490 ? -60.689 -79.004 100.912 1.00 168.36 ? 490 ARG A CG 1 ATOM 3238 C CD . ARG A 1 490 ? -61.755 -79.970 101.425 1.00 186.93 ? 490 ARG A CD 1 ATOM 3239 N NE . ARG A 1 490 ? -62.507 -79.444 102.573 1.00 189.86 ? 490 ARG A NE 1 ATOM 3240 C CZ . ARG A 1 490 ? -63.688 -78.828 102.490 1.00 184.03 ? 490 ARG A CZ 1 ATOM 3241 N NH1 . ARG A 1 490 ? -64.269 -78.652 101.314 1.00 188.98 ? 490 ARG A NH1 1 ATOM 3242 N NH2 . ARG A 1 490 ? -64.296 -78.380 103.580 1.00 179.56 ? 490 ARG A NH2 1 ATOM 3243 N N . LEU A 1 491 ? -58.530 -75.037 100.980 1.00 170.54 ? 491 LEU A N 1 ATOM 3244 C CA . LEU A 1 491 ? -57.321 -74.649 101.728 1.00 160.99 ? 491 LEU A CA 1 ATOM 3245 C C . LEU A 1 491 ? -57.590 -74.640 103.224 1.00 169.28 ? 491 LEU A C 1 ATOM 3246 O O . LEU A 1 491 ? -58.538 -74.001 103.677 1.00 174.29 ? 491 LEU A O 1 ATOM 3247 C CB . LEU A 1 491 ? -56.807 -73.274 101.284 1.00 176.70 ? 491 LEU A CB 1 ATOM 3248 C CG . LEU A 1 491 ? -57.092 -72.792 99.851 1.00 185.68 ? 491 LEU A CG 1 ATOM 3249 C CD1 . LEU A 1 491 ? -58.207 -71.747 99.830 1.00 169.37 ? 491 LEU A CD1 1 ATOM 3250 C CD2 . LEU A 1 491 ? -55.827 -72.260 99.182 1.00 187.78 ? 491 LEU A CD2 1 ATOM 3251 N N . PRO A 1 492 ? -56.767 -75.360 104.002 1.00 180.00 ? 492 PRO A N 1 ATOM 3252 C CA . PRO A 1 492 ? -57.204 -75.599 105.367 1.00 183.85 ? 492 PRO A CA 1 ATOM 3253 C C . PRO A 1 492 ? -57.574 -74.402 106.234 1.00 165.12 ? 492 PRO A C 1 ATOM 3254 O O . PRO A 1 492 ? -57.208 -73.252 105.953 1.00 131.77 ? 492 PRO A O 1 ATOM 3255 C CB . PRO A 1 492 ? -56.052 -76.426 105.963 1.00 200.41 ? 492 PRO A CB 1 ATOM 3256 C CG . PRO A 1 492 ? -55.579 -77.235 104.803 1.00 201.07 ? 492 PRO A CG 1 ATOM 3257 C CD . PRO A 1 492 ? -55.654 -76.260 103.637 1.00 201.95 ? 492 PRO A CD 1 ATOM 3258 N N . LYS A 1 493 ? -58.337 -74.744 107.271 1.00 185.21 ? 493 LYS A N 1 ATOM 3259 C CA . LYS A 1 493 ? -58.861 -73.862 108.314 1.00 192.79 ? 493 LYS A CA 1 ATOM 3260 C C . LYS A 1 493 ? -59.635 -72.664 107.764 1.00 182.95 ? 493 LYS A C 1 ATOM 3261 O O . LYS A 1 493 ? -60.647 -72.849 107.078 1.00 174.96 ? 493 LYS A O 1 ATOM 3262 C CB . LYS A 1 493 ? -57.790 -73.490 109.378 1.00 198.25 ? 493 LYS A CB 1 ATOM 3263 C CG . LYS A 1 493 ? -57.127 -74.667 110.124 1.00 197.47 ? 493 LYS A CG 1 ATOM 3264 C CD . LYS A 1 493 ? -58.075 -75.530 110.962 1.00 207.33 ? 493 LYS A CD 1 ATOM 3265 C CE . LYS A 1 493 ? -58.312 -74.989 112.372 1.00 215.06 ? 493 LYS A CE 1 ATOM 3266 N NZ . LYS A 1 493 ? -57.240 -75.331 113.350 1.00 203.67 ? 493 LYS A NZ 1 ATOM 3267 N N . GLY A 1 494 ? -59.154 -71.458 108.062 1.00 176.66 ? 494 GLY A N 1 ATOM 3268 C CA . GLY A 1 494 ? -59.903 -70.235 107.820 1.00 165.98 ? 494 GLY A CA 1 ATOM 3269 C C . GLY A 1 494 ? -59.595 -69.555 106.508 1.00 159.55 ? 494 GLY A C 1 ATOM 3270 O O . GLY A 1 494 ? -60.523 -69.028 105.872 1.00 157.42 ? 494 GLY A O 1 ATOM 3271 N N . VAL A 1 495 ? -58.318 -69.625 106.090 1.00 148.79 ? 495 VAL A N 1 ATOM 3272 C CA . VAL A 1 495 ? -57.699 -68.706 105.087 1.00 150.12 ? 495 VAL A CA 1 ATOM 3273 C C . VAL A 1 495 ? -58.138 -68.751 103.636 1.00 144.13 ? 495 VAL A C 1 ATOM 3274 O O . VAL A 1 495 ? -58.036 -69.796 102.988 1.00 132.25 ? 495 VAL A O 1 ATOM 3275 C CB . VAL A 1 495 ? -56.171 -68.814 105.032 1.00 148.04 ? 495 VAL A CB 1 ATOM 3276 C CG1 . VAL A 1 495 ? -55.550 -67.956 106.133 1.00 166.23 ? 495 VAL A CG1 1 ATOM 3277 C CG2 . VAL A 1 495 ? -55.735 -70.282 105.031 1.00 137.66 ? 495 VAL A CG2 1 ATOM 3278 N N . LYS A 1 496 ? -58.542 -67.589 103.117 1.00 143.24 ? 496 LYS A N 1 ATOM 3279 C CA . LYS A 1 496 ? -59.148 -67.530 101.800 1.00 144.02 ? 496 LYS A CA 1 ATOM 3280 C C . LYS A 1 496 ? -58.100 -67.630 100.717 1.00 138.35 ? 496 LYS A C 1 ATOM 3281 O O . LYS A 1 496 ? -58.453 -67.703 99.550 1.00 146.16 ? 496 LYS A O 1 ATOM 3282 C CB . LYS A 1 496 ? -60.060 -66.309 101.616 1.00 158.80 ? 496 LYS A CB 1 ATOM 3283 C CG . LYS A 1 496 ? -61.567 -66.631 101.575 1.00 173.77 ? 496 LYS A CG 1 ATOM 3284 C CD . LYS A 1 496 ? -62.410 -65.440 102.057 1.00 182.31 ? 496 LYS A CD 1 ATOM 3285 C CE . LYS A 1 496 ? -63.232 -64.751 100.964 1.00 176.31 ? 496 LYS A CE 1 ATOM 3286 N NZ . LYS A 1 496 ? -64.655 -65.196 100.967 1.00 176.36 ? 496 LYS A NZ 1 ATOM 3287 N N . HIS A 1 497 ? -56.822 -67.639 101.102 1.00 132.54 ? 497 HIS A N 1 ATOM 3288 C CA . HIS A 1 497 ? -55.733 -68.008 100.178 1.00 127.92 ? 497 HIS A CA 1 ATOM 3289 C C . HIS A 1 497 ? -54.455 -68.442 100.889 1.00 126.79 ? 497 HIS A C 1 ATOM 3290 O O . HIS A 1 497 ? -54.093 -67.914 101.947 1.00 130.04 ? 497 HIS A O 1 ATOM 3291 C CB . HIS A 1 497 ? -55.444 -66.906 99.157 1.00 136.91 ? 497 HIS A CB 1 ATOM 3292 C CG . HIS A 1 497 ? -54.280 -67.188 98.261 1.00 149.36 ? 497 HIS A CG 1 ATOM 3293 N ND1 . HIS A 1 497 ? -54.066 -68.419 97.679 1.00 159.11 ? 497 HIS A ND1 1 ATOM 3294 C CD2 . HIS A 1 497 ? -53.280 -66.385 97.826 1.00 159.26 ? 497 HIS A CD2 1 ATOM 3295 C CE1 . HIS A 1 497 ? -52.972 -68.369 96.941 1.00 172.19 ? 497 HIS A CE1 1 ATOM 3296 N NE2 . HIS A 1 497 ? -52.478 -67.146 97.011 1.00 173.91 ? 497 HIS A NE2 1 ATOM 3297 N N . LEU A 1 498 ? -53.773 -69.384 100.243 1.00 123.00 ? 498 LEU A N 1 ATOM 3298 C CA . LEU A 1 498 ? -52.740 -70.239 100.821 1.00 117.28 ? 498 LEU A CA 1 ATOM 3299 C C . LEU A 1 498 ? -51.420 -69.536 101.142 1.00 119.72 ? 498 LEU A C 1 ATOM 3300 O O . LEU A 1 498 ? -50.651 -69.999 102.018 1.00 119.83 ? 498 LEU A O 1 ATOM 3301 C CB . LEU A 1 498 ? -52.511 -71.375 99.837 1.00 105.29 ? 498 LEU A CB 1 ATOM 3302 C CG . LEU A 1 498 ? -51.596 -72.565 100.055 1.00 101.87 ? 498 LEU A CG 1 ATOM 3303 C CD1 . LEU A 1 498 ? -51.265 -72.946 101.497 1.00 92.74 ? 498 LEU A CD1 1 ATOM 3304 C CD2 . LEU A 1 498 ? -52.287 -73.686 99.303 1.00 112.32 ? 498 LEU A CD2 1 ATOM 3305 N N . LYS A 1 499 ? -51.178 -68.432 100.426 1.00 115.62 ? 499 LYS A N 1 ATOM 3306 C CA . LYS A 1 499 ? -49.991 -67.580 100.580 1.00 120.01 ? 499 LYS A CA 1 ATOM 3307 C C . LYS A 1 499 ? -49.919 -67.017 101.998 1.00 118.43 ? 499 LYS A C 1 ATOM 3308 O O . LYS A 1 499 ? -48.833 -66.756 102.530 1.00 108.11 ? 499 LYS A O 1 ATOM 3309 C CB . LYS A 1 499 ? -50.053 -66.431 99.558 1.00 134.93 ? 499 LYS A CB 1 ATOM 3310 C CG . LYS A 1 499 ? -48.724 -65.929 99.002 1.00 149.38 ? 499 LYS A CG 1 ATOM 3311 C CD . LYS A 1 499 ? -48.950 -65.063 97.759 1.00 176.29 ? 499 LYS A CD 1 ATOM 3312 C CE . LYS A 1 499 ? -47.777 -65.121 96.775 1.00 212.85 ? 499 LYS A CE 1 ATOM 3313 N NZ . LYS A 1 499 ? -48.036 -64.583 95.395 1.00 225.49 ? 499 LYS A NZ 1 ATOM 3314 N N . ASP A 1 500 ? -51.096 -66.844 102.595 1.00 127.07 ? 500 ASP A N 1 ATOM 3315 C CA . ASP A 1 500 ? -51.237 -66.262 103.915 1.00 138.17 ? 500 ASP A CA 1 ATOM 3316 C C . ASP A 1 500 ? -51.245 -67.313 104.999 1.00 142.30 ? 500 ASP A C 1 ATOM 3317 O O . ASP A 1 500 ? -50.966 -66.988 106.144 1.00 155.13 ? 500 ASP A O 1 ATOM 3318 C CB . ASP A 1 500 ? -52.513 -65.425 103.997 1.00 157.36 ? 500 ASP A CB 1 ATOM 3319 C CG . ASP A 1 500 ? -52.489 -64.220 103.059 1.00 183.38 ? 500 ASP A CG 1 ATOM 3320 O OD1 . ASP A 1 500 ? -51.403 -63.664 102.784 1.00 195.34 ? 500 ASP A OD1 1 ATOM 3321 O OD2 . ASP A 1 500 ? -53.569 -63.820 102.586 1.00 205.21 ? 500 ASP A OD2 1 ATOM 3322 N N . PHE A 1 501 ? -51.564 -68.562 104.644 1.00 143.07 ? 501 PHE A N 1 ATOM 3323 C CA . PHE A 1 501 ? -51.590 -69.674 105.609 1.00 140.08 ? 501 PHE A CA 1 ATOM 3324 C C . PHE A 1 501 ? -50.176 -70.086 106.074 1.00 143.97 ? 501 PHE A C 1 ATOM 3325 O O . PHE A 1 501 ? -49.370 -70.591 105.248 1.00 132.54 ? 501 PHE A O 1 ATOM 3326 C CB . PHE A 1 501 ? -52.402 -70.873 105.077 1.00 142.75 ? 501 PHE A CB 1 ATOM 3327 C CG . PHE A 1 501 ? -52.339 -72.105 105.961 1.00 151.76 ? 501 PHE A CG 1 ATOM 3328 C CD1 . PHE A 1 501 ? -52.718 -72.054 107.298 1.00 149.55 ? 501 PHE A CD1 1 ATOM 3329 C CD2 . PHE A 1 501 ? -51.896 -73.325 105.447 1.00 159.34 ? 501 PHE A CD2 1 ATOM 3330 C CE1 . PHE A 1 501 ? -52.637 -73.181 108.103 1.00 152.98 ? 501 PHE A CE1 1 ATOM 3331 C CE2 . PHE A 1 501 ? -51.826 -74.461 106.243 1.00 144.28 ? 501 PHE A CE2 1 ATOM 3332 C CZ . PHE A 1 501 ? -52.194 -74.385 107.573 1.00 152.63 ? 501 PHE A CZ 1 ATOM 3333 N N . PRO A 1 502 ? -49.888 -69.862 107.398 1.00 143.32 ? 502 PRO A N 1 ATOM 3334 C CA . PRO A 1 502 ? -48.606 -70.027 108.112 1.00 136.18 ? 502 PRO A CA 1 ATOM 3335 C C . PRO A 1 502 ? -48.382 -71.399 108.741 1.00 135.61 ? 502 PRO A C 1 ATOM 3336 O O . PRO A 1 502 ? -49.277 -71.977 109.371 1.00 138.61 ? 502 PRO A O 1 ATOM 3337 C CB . PRO A 1 502 ? -48.677 -68.970 109.222 1.00 131.65 ? 502 PRO A CB 1 ATOM 3338 C CG . PRO A 1 502 ? -50.131 -68.717 109.440 1.00 136.41 ? 502 PRO A CG 1 ATOM 3339 C CD . PRO A 1 502 ? -50.924 -69.356 108.323 1.00 138.49 ? 502 PRO A CD 1 ATOM 3340 N N . ILE A 1 503 ? -47.165 -71.895 108.571 1.00 138.04 ? 503 ILE A N 1 ATOM 3341 C CA . ILE A 1 503 ? -46.790 -73.219 109.036 1.00 137.75 ? 503 ILE A CA 1 ATOM 3342 C C . ILE A 1 503 ? -46.206 -73.060 110.415 1.00 136.51 ? 503 ILE A C 1 ATOM 3343 O O . ILE A 1 503 ? -45.159 -72.422 110.578 1.00 137.08 ? 503 ILE A O 1 ATOM 3344 C CB . ILE A 1 503 ? -45.756 -73.882 108.092 1.00 130.33 ? 503 ILE A CB 1 ATOM 3345 C CG1 . ILE A 1 503 ? -46.355 -74.152 106.687 1.00 126.07 ? 503 ILE A CG1 1 ATOM 3346 C CG2 . ILE A 1 503 ? -45.124 -75.122 108.727 1.00 131.16 ? 503 ILE A CG2 1 ATOM 3347 C CD1 . ILE A 1 503 ? -47.876 -74.155 106.555 1.00 116.72 ? 503 ILE A CD1 1 ATOM 3348 N N . LEU A 1 504 ? -46.882 -73.634 111.403 1.00 128.53 ? 504 LEU A N 1 ATOM 3349 C CA . LEU A 1 504 ? -46.480 -73.413 112.775 1.00 135.39 ? 504 LEU A CA 1 ATOM 3350 C C . LEU A 1 504 ? -45.096 -74.009 113.096 1.00 141.92 ? 504 LEU A C 1 ATOM 3351 O O . LEU A 1 504 ? -44.702 -75.003 112.471 1.00 145.67 ? 504 LEU A O 1 ATOM 3352 C CB . LEU A 1 504 ? -47.583 -73.873 113.721 1.00 136.64 ? 504 LEU A CB 1 ATOM 3353 C CG . LEU A 1 504 ? -48.455 -72.664 114.075 1.00 141.48 ? 504 LEU A CG 1 ATOM 3354 C CD1 . LEU A 1 504 ? -49.893 -72.829 113.616 1.00 146.12 ? 504 LEU A CD1 1 ATOM 3355 C CD2 . LEU A 1 504 ? -48.376 -72.319 115.557 1.00 147.32 ? 504 LEU A CD2 1 ATOM 3356 N N . PRO A 1 505 ? -44.339 -73.381 114.038 1.00 142.49 ? 505 PRO A N 1 ATOM 3357 C CA . PRO A 1 505 ? -43.030 -73.903 114.396 1.00 135.80 ? 505 PRO A CA 1 ATOM 3358 C C . PRO A 1 505 ? -43.161 -75.365 114.756 1.00 144.60 ? 505 PRO A C 1 ATOM 3359 O O . PRO A 1 505 ? -43.811 -75.720 115.753 1.00 150.96 ? 505 PRO A O 1 ATOM 3360 C CB . PRO A 1 505 ? -42.647 -73.088 115.638 1.00 142.07 ? 505 PRO A CB 1 ATOM 3361 C CG . PRO A 1 505 ? -43.924 -72.511 116.158 1.00 148.03 ? 505 PRO A CG 1 ATOM 3362 C CD . PRO A 1 505 ? -44.711 -72.248 114.909 1.00 149.22 ? 505 PRO A CD 1 ATOM 3363 N N . GLY A 1 506 ? -42.600 -76.210 113.902 1.00 147.66 ? 506 GLY A N 1 ATOM 3364 C CA . GLY A 1 506 ? -42.527 -77.636 114.184 1.00 154.40 ? 506 GLY A CA 1 ATOM 3365 C C . GLY A 1 506 ? -43.451 -78.531 113.390 1.00 145.07 ? 506 GLY A C 1 ATOM 3366 O O . GLY A 1 506 ? -43.395 -79.748 113.561 1.00 142.51 ? 506 GLY A O 1 ATOM 3367 N N . GLU A 1 507 ? -44.293 -77.936 112.539 1.00 144.31 ? 507 GLU A N 1 ATOM 3368 C CA . GLU A 1 507 ? -45.214 -78.697 111.687 1.00 148.14 ? 507 GLU A CA 1 ATOM 3369 C C . GLU A 1 507 ? -44.643 -78.838 110.283 1.00 140.22 ? 507 GLU A C 1 ATOM 3370 O O . GLU A 1 507 ? -43.756 -78.079 109.882 1.00 130.84 ? 507 GLU A O 1 ATOM 3371 C CB . GLU A 1 507 ? -46.620 -78.071 111.638 1.00 164.00 ? 507 GLU A CB 1 ATOM 3372 C CG . GLU A 1 507 ? -47.160 -77.509 112.964 1.00 210.06 ? 507 GLU A CG 1 ATOM 3373 C CD . GLU A 1 507 ? -47.577 -78.554 114.012 1.00 224.04 ? 507 GLU A CD 1 ATOM 3374 O OE1 . GLU A 1 507 ? -46.699 -79.297 114.495 1.00 243.04 ? 507 GLU A OE1 1 ATOM 3375 O OE2 . GLU A 1 507 ? -48.775 -78.610 114.397 1.00 209.77 ? 507 GLU A OE2 1 ATOM 3376 N N . ILE A 1 508 ? -45.143 -79.841 109.562 1.00 145.94 ? 508 ILE A N 1 ATOM 3377 C CA . ILE A 1 508 ? -44.777 -80.117 108.161 1.00 142.04 ? 508 ILE A CA 1 ATOM 3378 C C . ILE A 1 508 ? -45.996 -79.893 107.265 1.00 145.12 ? 508 ILE A C 1 ATOM 3379 O O . ILE A 1 508 ? -47.136 -80.181 107.675 1.00 157.55 ? 508 ILE A O 1 ATOM 3380 C CB . ILE A 1 508 ? -44.209 -81.558 107.950 1.00 141.13 ? 508 ILE A CB 1 ATOM 3381 C CG1 . ILE A 1 508 ? -45.067 -82.656 108.668 1.00 163.95 ? 508 ILE A CG1 1 ATOM 3382 C CG2 . ILE A 1 508 ? -42.756 -81.598 108.384 1.00 124.97 ? 508 ILE A CG2 1 ATOM 3383 C CD1 . ILE A 1 508 ? -44.776 -84.135 108.353 1.00 154.76 ? 508 ILE A CD1 1 ATOM 3384 N N . PHE A 1 509 ? -45.777 -79.354 106.065 1.00 133.95 ? 509 PHE A N 1 ATOM 3385 C CA . PHE A 1 509 ? -46.884 -79.239 105.117 1.00 133.93 ? 509 PHE A CA 1 ATOM 3386 C C . PHE A 1 509 ? -46.529 -79.638 103.711 1.00 140.82 ? 509 PHE A C 1 ATOM 3387 O O . PHE A 1 509 ? -45.445 -79.313 103.217 1.00 150.75 ? 509 PHE A O 1 ATOM 3388 C CB . PHE A 1 509 ? -47.534 -77.863 105.108 1.00 122.32 ? 509 PHE A CB 1 ATOM 3389 C CG . PHE A 1 509 ? -48.927 -77.869 104.538 1.00 122.43 ? 509 PHE A CG 1 ATOM 3390 C CD1 . PHE A 1 509 ? -49.752 -78.986 104.697 1.00 127.88 ? 509 PHE A CD1 1 ATOM 3391 C CD2 . PHE A 1 509 ? -49.422 -76.758 103.858 1.00 121.09 ? 509 PHE A CD2 1 ATOM 3392 C CE1 . PHE A 1 509 ? -51.033 -78.992 104.176 1.00 136.18 ? 509 PHE A CE1 1 ATOM 3393 C CE2 . PHE A 1 509 ? -50.704 -76.751 103.339 1.00 117.49 ? 509 PHE A CE2 1 ATOM 3394 C CZ . PHE A 1 509 ? -51.509 -77.867 103.505 1.00 131.98 ? 509 PHE A CZ 1 ATOM 3395 N N . LYS A 1 510 ? -47.484 -80.316 103.077 1.00 136.00 ? 510 LYS A N 1 ATOM 3396 C CA . LYS A 1 510 ? -47.303 -80.868 101.749 1.00 125.93 ? 510 LYS A CA 1 ATOM 3397 C C . LYS A 1 510 ? -48.084 -80.092 100.659 1.00 124.41 ? 510 LYS A C 1 ATOM 3398 O O . LYS A 1 510 ? -49.316 -80.028 100.630 1.00 124.97 ? 510 LYS A O 1 ATOM 3399 C CB . LYS A 1 510 ? -47.606 -82.362 101.757 1.00 116.96 ? 510 LYS A CB 1 ATOM 3400 C CG . LYS A 1 510 ? -46.815 -83.156 102.790 1.00 119.24 ? 510 LYS A CG 1 ATOM 3401 C CD . LYS A 1 510 ? -47.637 -84.327 103.359 1.00 136.32 ? 510 LYS A CD 1 ATOM 3402 C CE . LYS A 1 510 ? -46.841 -85.341 104.200 1.00 136.76 ? 510 LYS A CE 1 ATOM 3403 N NZ . LYS A 1 510 ? -45.841 -86.169 103.446 1.00 126.39 ? 510 LYS A NZ 1 ATOM 3404 N N . TYR A 1 511 ? -47.302 -79.528 99.756 1.00 118.05 ? 511 TYR A N 1 ATOM 3405 C CA . TYR A 1 511 ? -47.734 -78.640 98.723 1.00 112.65 ? 511 TYR A CA 1 ATOM 3406 C C . TYR A 1 511 ? -47.489 -79.284 97.322 1.00 119.13 ? 511 TYR A C 1 ATOM 3407 O O . TYR A 1 511 ? -46.410 -79.849 97.081 1.00 115.77 ? 511 TYR A O 1 ATOM 3408 C CB . TYR A 1 511 ? -46.820 -77.436 98.827 1.00 113.59 ? 511 TYR A CB 1 ATOM 3409 C CG . TYR A 1 511 ? -47.026 -76.412 99.924 1.00 114.12 ? 511 TYR A CG 1 ATOM 3410 C CD1 . TYR A 1 511 ? -46.389 -76.511 101.161 1.00 113.10 ? 511 TYR A CD1 1 ATOM 3411 C CD2 . TYR A 1 511 ? -47.752 -75.265 99.657 1.00 120.97 ? 511 TYR A CD2 1 ATOM 3412 C CE1 . TYR A 1 511 ? -46.533 -75.501 102.117 1.00 122.89 ? 511 TYR A CE1 1 ATOM 3413 C CE2 . TYR A 1 511 ? -47.915 -74.266 100.595 1.00 125.63 ? 511 TYR A CE2 1 ATOM 3414 C CZ . TYR A 1 511 ? -47.315 -74.364 101.822 1.00 125.75 ? 511 TYR A CZ 1 ATOM 3415 O OH . TYR A 1 511 ? -47.544 -73.301 102.700 1.00 116.55 ? 511 TYR A OH 1 ATOM 3416 N N . LYS A 1 512 ? -48.464 -79.189 96.402 1.00 130.00 ? 512 LYS A N 1 ATOM 3417 C CA . LYS A 1 512 ? -48.300 -79.588 94.962 1.00 124.70 ? 512 LYS A CA 1 ATOM 3418 C C . LYS A 1 512 ? -48.231 -78.324 94.112 1.00 121.74 ? 512 LYS A C 1 ATOM 3419 O O . LYS A 1 512 ? -49.225 -77.594 94.006 1.00 122.12 ? 512 LYS A O 1 ATOM 3420 C CB . LYS A 1 512 ? -49.453 -80.525 94.468 1.00 123.21 ? 512 LYS A CB 1 ATOM 3421 C CG . LYS A 1 512 ? -49.504 -80.940 92.978 1.00 115.02 ? 512 LYS A CG 1 ATOM 3422 C CD . LYS A 1 512 ? -50.150 -82.336 92.731 1.00 121.26 ? 512 LYS A CD 1 ATOM 3423 C CE . LYS A 1 512 ? -50.397 -82.708 91.238 1.00 125.07 ? 512 LYS A CE 1 ATOM 3424 N NZ . LYS A 1 512 ? -50.224 -84.150 90.805 1.00 110.86 ? 512 LYS A NZ 1 ATOM 3425 N N . TRP A 1 513 ? -47.048 -78.052 93.556 1.00 117.59 ? 513 TRP A N 1 ATOM 3426 C CA . TRP A 1 513 ? -46.876 -76.999 92.553 1.00 117.23 ? 513 TRP A CA 1 ATOM 3427 C C . TRP A 1 513 ? -46.911 -77.626 91.161 1.00 120.37 ? 513 TRP A C 1 ATOM 3428 O O . TRP A 1 513 ? -45.902 -78.129 90.672 1.00 125.99 ? 513 TRP A O 1 ATOM 3429 C CB . TRP A 1 513 ? -45.542 -76.266 92.714 1.00 114.63 ? 513 TRP A CB 1 ATOM 3430 C CG . TRP A 1 513 ? -45.281 -75.558 94.011 1.00 117.42 ? 513 TRP A CG 1 ATOM 3431 C CD1 . TRP A 1 513 ? -46.181 -75.244 94.991 1.00 122.17 ? 513 TRP A CD1 1 ATOM 3432 C CD2 . TRP A 1 513 ? -44.024 -75.026 94.441 1.00 119.45 ? 513 TRP A CD2 1 ATOM 3433 N NE1 . TRP A 1 513 ? -45.556 -74.565 96.019 1.00 124.05 ? 513 TRP A NE1 1 ATOM 3434 C CE2 . TRP A 1 513 ? -44.228 -74.428 95.706 1.00 129.40 ? 513 TRP A CE2 1 ATOM 3435 C CE3 . TRP A 1 513 ? -42.740 -75.004 93.883 1.00 112.84 ? 513 TRP A CE3 1 ATOM 3436 C CZ2 . TRP A 1 513 ? -43.186 -73.822 96.425 1.00 138.38 ? 513 TRP A CZ2 1 ATOM 3437 C CZ3 . TRP A 1 513 ? -41.716 -74.395 94.589 1.00 115.14 ? 513 TRP A CZ3 1 ATOM 3438 C CH2 . TRP A 1 513 ? -41.940 -73.815 95.848 1.00 125.80 ? 513 TRP A CH2 1 ATOM 3439 N N . THR A 1 514 ? -48.068 -77.620 90.520 1.00 121.39 ? 514 THR A N 1 ATOM 3440 C CA . THR A 1 514 ? -48.140 -78.183 89.189 1.00 132.46 ? 514 THR A CA 1 ATOM 3441 C C . THR A 1 514 ? -47.836 -77.045 88.217 1.00 128.87 ? 514 THR A C 1 ATOM 3442 O O . THR A 1 514 ? -48.231 -75.897 88.461 1.00 120.69 ? 514 THR A O 1 ATOM 3443 C CB . THR A 1 514 ? -49.500 -78.880 88.903 1.00 159.35 ? 514 THR A CB 1 ATOM 3444 O OG1 . THR A 1 514 ? -49.984 -79.549 90.080 1.00 168.49 ? 514 THR A OG1 1 ATOM 3445 C CG2 . THR A 1 514 ? -49.366 -79.916 87.772 1.00 172.73 ? 514 THR A CG2 1 ATOM 3446 N N . VAL A 1 515 ? -47.111 -77.379 87.140 1.00 130.31 ? 515 VAL A N 1 ATOM 3447 C CA . VAL A 1 515 ? -46.639 -76.435 86.101 1.00 114.34 ? 515 VAL A CA 1 ATOM 3448 C C . VAL A 1 515 ? -47.383 -76.592 84.776 1.00 113.92 ? 515 VAL A C 1 ATOM 3449 O O . VAL A 1 515 ? -47.695 -77.715 84.365 1.00 128.38 ? 515 VAL A O 1 ATOM 3450 C CB . VAL A 1 515 ? -45.150 -76.658 85.815 1.00 104.99 ? 515 VAL A CB 1 ATOM 3451 C CG1 . VAL A 1 515 ? -44.822 -76.238 84.402 1.00 104.90 ? 515 VAL A CG1 1 ATOM 3452 C CG2 . VAL A 1 515 ? -44.287 -75.910 86.822 1.00 104.75 ? 515 VAL A CG2 1 ATOM 3453 N N . THR A 1 516 ? -47.632 -75.472 84.104 1.00 105.70 ? 516 THR A N 1 ATOM 3454 C CA . THR A 1 516 ? -48.473 -75.444 82.908 1.00 116.57 ? 516 THR A CA 1 ATOM 3455 C C . THR A 1 516 ? -47.874 -74.540 81.907 1.00 121.03 ? 516 THR A C 1 ATOM 3456 O O . THR A 1 516 ? -47.437 -73.455 82.290 1.00 132.41 ? 516 THR A O 1 ATOM 3457 C CB . THR A 1 516 ? -49.750 -74.675 83.196 1.00 126.02 ? 516 THR A CB 1 ATOM 3458 O OG1 . THR A 1 516 ? -49.642 -74.067 84.496 1.00 132.83 ? 516 THR A OG1 1 ATOM 3459 C CG2 . THR A 1 516 ? -50.962 -75.569 83.092 1.00 136.93 ? 516 THR A CG2 1 ATOM 3460 N N . VAL A 1 517 ? -47.920 -74.897 80.623 1.00 120.12 ? 517 VAL A N 1 ATOM 3461 C CA . VAL A 1 517 ? -47.322 -73.988 79.633 1.00 124.28 ? 517 VAL A CA 1 ATOM 3462 C C . VAL A 1 517 ? -47.702 -72.534 79.884 1.00 134.77 ? 517 VAL A C 1 ATOM 3463 O O . VAL A 1 517 ? -46.858 -71.638 79.777 1.00 148.86 ? 517 VAL A O 1 ATOM 3464 C CB . VAL A 1 517 ? -47.642 -74.307 78.172 1.00 109.53 ? 517 VAL A CB 1 ATOM 3465 C CG1 . VAL A 1 517 ? -47.081 -75.663 77.812 1.00 110.91 ? 517 VAL A CG1 1 ATOM 3466 C CG2 . VAL A 1 517 ? -49.133 -74.138 77.895 1.00 103.82 ? 517 VAL A CG2 1 ATOM 3467 N N . GLU A 1 518 ? -48.953 -72.291 80.246 1.00 128.75 ? 518 GLU A N 1 ATOM 3468 C CA . GLU A 1 518 ? -49.383 -70.924 80.291 1.00 136.75 ? 518 GLU A CA 1 ATOM 3469 C C . GLU A 1 518 ? -48.758 -70.090 81.441 1.00 145.51 ? 518 GLU A C 1 ATOM 3470 O O . GLU A 1 518 ? -49.133 -68.933 81.618 1.00 205.91 ? 518 GLU A O 1 ATOM 3471 C CB . GLU A 1 518 ? -50.910 -70.806 80.198 1.00 143.31 ? 518 GLU A CB 1 ATOM 3472 C CG . GLU A 1 518 ? -51.617 -72.050 79.695 1.00 162.36 ? 518 GLU A CG 1 ATOM 3473 C CD . GLU A 1 518 ? -52.289 -72.846 80.818 1.00 187.62 ? 518 GLU A CD 1 ATOM 3474 O OE1 . GLU A 1 518 ? -51.905 -72.729 82.002 1.00 188.89 ? 518 GLU A OE1 1 ATOM 3475 O OE2 . GLU A 1 518 ? -53.234 -73.595 80.519 1.00 197.61 ? 518 GLU A OE2 1 ATOM 3476 N N . ASP A 1 519 ? -47.802 -70.636 82.200 1.00 138.16 ? 519 ASP A N 1 ATOM 3477 C CA . ASP A 1 519 ? -46.987 -69.791 83.120 1.00 150.54 ? 519 ASP A CA 1 ATOM 3478 C C . ASP A 1 519 ? -45.486 -70.038 82.945 1.00 141.55 ? 519 ASP A C 1 ATOM 3479 O O . ASP A 1 519 ? -44.664 -69.623 83.778 1.00 131.84 ? 519 ASP A O 1 ATOM 3480 C CB . ASP A 1 519 ? -47.418 -69.908 84.596 1.00 162.81 ? 519 ASP A CB 1 ATOM 3481 C CG . ASP A 1 519 ? -47.381 -71.352 85.122 1.00 182.59 ? 519 ASP A CG 1 ATOM 3482 O OD1 . ASP A 1 519 ? -46.729 -72.225 84.509 1.00 178.30 ? 519 ASP A OD1 1 ATOM 3483 O OD2 . ASP A 1 519 ? -48.015 -71.624 86.163 1.00 194.03 ? 519 ASP A OD2 1 ATOM 3484 N N . GLY A 1 520 ? -45.170 -70.715 81.839 1.00 131.89 ? 520 GLY A N 1 ATOM 3485 C CA . GLY A 1 520 ? -43.806 -71.009 81.396 1.00 127.36 ? 520 GLY A CA 1 ATOM 3486 C C . GLY A 1 520 ? -43.459 -70.373 80.044 1.00 129.51 ? 520 GLY A C 1 ATOM 3487 O O . GLY A 1 520 ? -44.352 -69.813 79.363 1.00 118.40 ? 520 GLY A O 1 ATOM 3488 N N . PRO A 1 521 ? -42.162 -70.475 79.634 1.00 124.13 ? 521 PRO A N 1 ATOM 3489 C CA . PRO A 1 521 ? -41.594 -69.617 78.577 1.00 113.75 ? 521 PRO A CA 1 ATOM 3490 C C . PRO A 1 521 ? -42.257 -69.876 77.244 1.00 112.02 ? 521 PRO A C 1 ATOM 3491 O O . PRO A 1 521 ? -42.835 -70.939 77.071 1.00 113.40 ? 521 PRO A O 1 ATOM 3492 C CB . PRO A 1 521 ? -40.112 -70.026 78.535 1.00 108.78 ? 521 PRO A CB 1 ATOM 3493 C CG . PRO A 1 521 ? -39.875 -70.909 79.724 1.00 107.21 ? 521 PRO A CG 1 ATOM 3494 C CD . PRO A 1 521 ? -41.204 -71.519 80.054 1.00 116.53 ? 521 PRO A CD 1 ATOM 3495 N N . THR A 1 522 ? -42.221 -68.907 76.333 1.00 117.59 ? 522 THR A N 1 ATOM 3496 C CA . THR A 1 522 ? -42.651 -69.154 74.952 1.00 129.67 ? 522 THR A CA 1 ATOM 3497 C C . THR A 1 522 ? -41.457 -69.248 74.036 1.00 140.71 ? 522 THR A C 1 ATOM 3498 O O . THR A 1 522 ? -40.317 -69.061 74.453 1.00 146.87 ? 522 THR A O 1 ATOM 3499 C CB . THR A 1 522 ? -43.591 -68.080 74.375 1.00 127.72 ? 522 THR A CB 1 ATOM 3500 O OG1 . THR A 1 522 ? -42.893 -66.833 74.239 1.00 122.78 ? 522 THR A OG1 1 ATOM 3501 C CG2 . THR A 1 522 ? -44.809 -67.915 75.243 1.00 134.64 ? 522 THR A CG2 1 ATOM 3502 N N . LYS A 1 523 ? -41.746 -69.525 72.775 1.00 151.27 ? 523 LYS A N 1 ATOM 3503 C CA . LYS A 1 523 ? -40.745 -69.714 71.742 1.00 159.06 ? 523 LYS A CA 1 ATOM 3504 C C . LYS A 1 523 ? -39.791 -68.530 71.674 1.00 144.92 ? 523 LYS A C 1 ATOM 3505 O O . LYS A 1 523 ? -38.594 -68.722 71.490 1.00 156.36 ? 523 LYS A O 1 ATOM 3506 C CB . LYS A 1 523 ? -41.434 -69.934 70.393 1.00 179.73 ? 523 LYS A CB 1 ATOM 3507 C CG . LYS A 1 523 ? -42.638 -70.880 70.438 1.00 197.88 ? 523 LYS A CG 1 ATOM 3508 C CD . LYS A 1 523 ? -43.764 -70.434 71.384 1.00 203.39 ? 523 LYS A CD 1 ATOM 3509 C CE . LYS A 1 523 ? -44.560 -69.241 70.860 1.00 216.76 ? 523 LYS A CE 1 ATOM 3510 N NZ . LYS A 1 523 ? -45.521 -68.705 71.869 1.00 208.21 ? 523 LYS A NZ 1 ATOM 3511 N N . SER A 1 524 ? -40.318 -67.319 71.840 1.00 134.35 ? 524 SER A N 1 ATOM 3512 C CA . SER A 1 524 ? -39.481 -66.117 71.892 1.00 148.79 ? 524 SER A CA 1 ATOM 3513 C C . SER A 1 524 ? -38.671 -66.043 73.189 1.00 154.69 ? 524 SER A C 1 ATOM 3514 O O . SER A 1 524 ? -37.580 -65.446 73.223 1.00 145.09 ? 524 SER A O 1 ATOM 3515 C CB . SER A 1 524 ? -40.329 -64.847 71.745 1.00 157.83 ? 524 SER A CB 1 ATOM 3516 O OG . SER A 1 524 ? -40.228 -64.273 70.447 1.00 177.44 ? 524 SER A OG 1 ATOM 3517 N N . ASP A 1 525 ? -39.217 -66.660 74.243 1.00 159.71 ? 525 ASP A N 1 ATOM 3518 C CA . ASP A 1 525 ? -38.688 -66.549 75.612 1.00 149.58 ? 525 ASP A CA 1 ATOM 3519 C C . ASP A 1 525 ? -37.328 -67.201 75.761 1.00 135.04 ? 525 ASP A C 1 ATOM 3520 O O . ASP A 1 525 ? -37.078 -68.231 75.153 1.00 120.06 ? 525 ASP A O 1 ATOM 3521 C CB . ASP A 1 525 ? -39.682 -67.117 76.641 1.00 145.67 ? 525 ASP A CB 1 ATOM 3522 C CG . ASP A 1 525 ? -40.789 -66.118 77.008 1.00 152.53 ? 525 ASP A CG 1 ATOM 3523 O OD1 . ASP A 1 525 ? -40.557 -65.273 77.900 1.00 151.26 ? 525 ASP A OD1 1 ATOM 3524 O OD2 . ASP A 1 525 ? -41.891 -66.171 76.414 1.00 147.49 ? 525 ASP A OD2 1 ATOM 3525 N N . PRO A 1 526 ? -36.431 -66.576 76.545 1.00 147.39 ? 526 PRO A N 1 ATOM 3526 C CA . PRO A 1 526 ? -35.178 -67.254 76.812 1.00 152.63 ? 526 PRO A CA 1 ATOM 3527 C C . PRO A 1 526 ? -35.573 -68.566 77.459 1.00 134.35 ? 526 PRO A C 1 ATOM 3528 O O . PRO A 1 526 ? -35.903 -68.588 78.634 1.00 116.38 ? 526 PRO A O 1 ATOM 3529 C CB . PRO A 1 526 ? -34.463 -66.307 77.800 1.00 175.46 ? 526 PRO A CB 1 ATOM 3530 C CG . PRO A 1 526 ? -35.519 -65.390 78.346 1.00 165.70 ? 526 PRO A CG 1 ATOM 3531 C CD . PRO A 1 526 ? -36.519 -65.271 77.233 1.00 168.50 ? 526 PRO A CD 1 ATOM 3532 N N . ARG A 1 527 ? -35.574 -69.640 76.677 1.00 145.91 ? 527 ARG A N 1 ATOM 3533 C CA . ARG A 1 527 ? -36.357 -70.843 77.019 1.00 152.13 ? 527 ARG A CA 1 ATOM 3534 C C . ARG A 1 527 ? -35.922 -71.527 78.315 1.00 126.55 ? 527 ARG A C 1 ATOM 3535 O O . ARG A 1 527 ? -35.293 -72.578 78.293 1.00 109.16 ? 527 ARG A O 1 ATOM 3536 C CB . ARG A 1 527 ? -36.437 -71.821 75.827 1.00 181.97 ? 527 ARG A CB 1 ATOM 3537 C CG . ARG A 1 527 ? -37.212 -71.278 74.622 1.00 202.99 ? 527 ARG A CG 1 ATOM 3538 C CD . ARG A 1 527 ? -37.390 -72.282 73.487 1.00 219.56 ? 527 ARG A CD 1 ATOM 3539 N NE . ARG A 1 527 ? -38.063 -73.511 73.916 1.00 248.96 ? 527 ARG A NE 1 ATOM 3540 C CZ . ARG A 1 527 ? -37.575 -74.746 73.777 1.00 278.52 ? 527 ARG A CZ 1 ATOM 3541 N NH1 . ARG A 1 527 ? -36.401 -74.963 73.192 1.00 298.63 ? 527 ARG A NH1 1 ATOM 3542 N NH2 . ARG A 1 527 ? -38.277 -75.782 74.212 1.00 288.67 ? 527 ARG A NH2 1 ATOM 3543 N N . CYS A 1 528 ? -36.299 -70.901 79.432 1.00 121.44 ? 528 CYS A N 1 ATOM 3544 C CA . CYS A 1 528 ? -35.845 -71.257 80.772 1.00 121.92 ? 528 CYS A CA 1 ATOM 3545 C C . CYS A 1 528 ? -35.856 -70.054 81.733 1.00 112.41 ? 528 CYS A C 1 ATOM 3546 O O . CYS A 1 528 ? -34.805 -69.647 82.248 1.00 98.81 ? 528 CYS A O 1 ATOM 3547 C CB . CYS A 1 528 ? -34.435 -71.839 80.709 1.00 138.57 ? 528 CYS A CB 1 ATOM 3548 S SG . CYS A 1 528 ? -34.151 -73.128 81.928 1.00 175.52 ? 528 CYS A SG 1 ATOM 3549 N N . LEU A 1 529 ? -37.041 -69.501 81.991 1.00 111.24 ? 529 LEU A N 1 ATOM 3550 C CA . LEU A 1 529 ? -37.150 -68.215 82.714 1.00 106.41 ? 529 LEU A CA 1 ATOM 3551 C C . LEU A 1 529 ? -36.879 -68.306 84.182 1.00 102.52 ? 529 LEU A C 1 ATOM 3552 O O . LEU A 1 529 ? -37.360 -69.221 84.862 1.00 105.17 ? 529 LEU A O 1 ATOM 3553 C CB . LEU A 1 529 ? -38.508 -67.545 82.506 1.00 99.99 ? 529 LEU A CB 1 ATOM 3554 C CG . LEU A 1 529 ? -39.676 -68.424 82.077 1.00 97.58 ? 529 LEU A CG 1 ATOM 3555 C CD1 . LEU A 1 529 ? -40.167 -69.246 83.247 1.00 106.78 ? 529 LEU A CD1 1 ATOM 3556 C CD2 . LEU A 1 529 ? -40.804 -67.571 81.529 1.00 94.80 ? 529 LEU A CD2 1 ATOM 3557 N N . THR A 1 530 ? -36.119 -67.347 84.678 1.00 97.90 ? 530 THR A N 1 ATOM 3558 C CA . THR A 1 530 ? -35.857 -67.348 86.101 1.00 107.89 ? 530 THR A CA 1 ATOM 3559 C C . THR A 1 530 ? -37.015 -66.729 86.928 1.00 114.55 ? 530 THR A C 1 ATOM 3560 O O . THR A 1 530 ? -37.798 -65.925 86.411 1.00 121.44 ? 530 THR A O 1 ATOM 3561 C CB . THR A 1 530 ? -34.444 -66.826 86.432 1.00 102.97 ? 530 THR A CB 1 ATOM 3562 O OG1 . THR A 1 530 ? -34.514 -65.842 87.473 1.00 111.40 ? 530 THR A OG1 1 ATOM 3563 C CG2 . THR A 1 530 ? -33.815 -66.234 85.221 1.00 96.72 ? 530 THR A CG2 1 ATOM 3564 N N . ARG A 1 531 ? -37.123 -67.167 88.187 1.00 109.42 ? 531 ARG A N 1 ATOM 3565 C CA . ARG A 1 531 ? -38.163 -66.790 89.155 1.00 107.24 ? 531 ARG A CA 1 ATOM 3566 C C . ARG A 1 531 ? -37.664 -67.186 90.551 1.00 122.45 ? 531 ARG A C 1 ATOM 3567 O O . ARG A 1 531 ? -36.519 -67.632 90.698 1.00 133.72 ? 531 ARG A O 1 ATOM 3568 C CB . ARG A 1 531 ? -39.478 -67.515 88.874 1.00 99.95 ? 531 ARG A CB 1 ATOM 3569 C CG . ARG A 1 531 ? -40.053 -67.226 87.508 1.00 110.21 ? 531 ARG A CG 1 ATOM 3570 C CD . ARG A 1 531 ? -40.477 -65.770 87.394 1.00 122.43 ? 531 ARG A CD 1 ATOM 3571 N NE . ARG A 1 531 ? -40.597 -65.289 86.013 1.00 138.13 ? 531 ARG A NE 1 ATOM 3572 C CZ . ARG A 1 531 ? -41.736 -65.184 85.313 1.00 153.85 ? 531 ARG A CZ 1 ATOM 3573 N NH1 . ARG A 1 531 ? -42.938 -65.540 85.804 1.00 139.35 ? 531 ARG A NH1 1 ATOM 3574 N NH2 . ARG A 1 531 ? -41.667 -64.712 84.079 1.00 182.48 ? 531 ARG A NH2 1 ATOM 3575 N N . TYR A 1 532 ? -38.508 -67.039 91.574 1.00 121.83 ? 532 TYR A N 1 ATOM 3576 C CA . TYR A 1 532 ? -38.081 -67.291 92.960 1.00 124.73 ? 532 TYR A CA 1 ATOM 3577 C C . TYR A 1 532 ? -39.212 -67.916 93.790 1.00 127.57 ? 532 TYR A C 1 ATOM 3578 O O . TYR A 1 532 ? -40.333 -68.051 93.293 1.00 128.26 ? 532 TYR A O 1 ATOM 3579 C CB . TYR A 1 532 ? -37.524 -65.995 93.622 1.00 122.26 ? 532 TYR A CB 1 ATOM 3580 C CG . TYR A 1 532 ? -38.560 -64.927 93.867 1.00 117.48 ? 532 TYR A CG 1 ATOM 3581 C CD1 . TYR A 1 532 ? -39.358 -64.950 95.015 1.00 133.52 ? 532 TYR A CD1 1 ATOM 3582 C CD2 . TYR A 1 532 ? -38.760 -63.909 92.948 1.00 118.56 ? 532 TYR A CD2 1 ATOM 3583 C CE1 . TYR A 1 532 ? -40.339 -63.991 95.236 1.00 153.64 ? 532 TYR A CE1 1 ATOM 3584 C CE2 . TYR A 1 532 ? -39.737 -62.940 93.150 1.00 141.98 ? 532 TYR A CE2 1 ATOM 3585 C CZ . TYR A 1 532 ? -40.528 -62.978 94.295 1.00 160.56 ? 532 TYR A CZ 1 ATOM 3586 O OH . TYR A 1 532 ? -41.499 -62.007 94.509 1.00 169.86 ? 532 TYR A OH 1 ATOM 3587 N N . TYR A 1 533 ? -38.897 -68.301 95.037 1.00 129.48 ? 533 TYR A N 1 ATOM 3588 C CA . TYR A 1 533 ? -39.880 -68.733 96.057 1.00 114.42 ? 533 TYR A CA 1 ATOM 3589 C C . TYR A 1 533 ? -39.570 -68.120 97.444 1.00 107.76 ? 533 TYR A C 1 ATOM 3590 O O . TYR A 1 533 ? -38.404 -68.106 97.881 1.00 94.52 ? 533 TYR A O 1 ATOM 3591 C CB . TYR A 1 533 ? -39.966 -70.272 96.124 1.00 114.31 ? 533 TYR A CB 1 ATOM 3592 C CG . TYR A 1 533 ? -38.718 -70.992 96.636 1.00 118.28 ? 533 TYR A CG 1 ATOM 3593 C CD1 . TYR A 1 533 ? -37.466 -70.761 96.065 1.00 110.23 ? 533 TYR A CD1 1 ATOM 3594 C CD2 . TYR A 1 533 ? -38.801 -71.917 97.693 1.00 126.68 ? 533 TYR A CD2 1 ATOM 3595 C CE1 . TYR A 1 533 ? -36.336 -71.415 96.525 1.00 113.32 ? 533 TYR A CE1 1 ATOM 3596 C CE2 . TYR A 1 533 ? -37.670 -72.574 98.168 1.00 124.81 ? 533 TYR A CE2 1 ATOM 3597 C CZ . TYR A 1 533 ? -36.433 -72.312 97.574 1.00 122.71 ? 533 TYR A CZ 1 ATOM 3598 O OH . TYR A 1 533 ? -35.292 -72.956 98.010 1.00 119.26 ? 533 TYR A OH 1 ATOM 3599 N N . SER A 1 534 ? -40.606 -67.599 98.113 1.00 104.66 ? 534 SER A N 1 ATOM 3600 C CA . SER A 1 534 ? -40.459 -67.064 99.480 1.00 109.52 ? 534 SER A CA 1 ATOM 3601 C C . SER A 1 534 ? -41.582 -67.404 100.492 1.00 120.34 ? 534 SER A C 1 ATOM 3602 O O . SER A 1 534 ? -42.427 -68.302 100.249 1.00 109.59 ? 534 SER A O 1 ATOM 3603 C CB . SER A 1 534 ? -40.217 -65.547 99.481 1.00 102.67 ? 534 SER A CB 1 ATOM 3604 O OG . SER A 1 534 ? -39.873 -65.120 100.808 1.00 101.44 ? 534 SER A OG 1 ATOM 3605 N N . SER A 1 535 ? -41.546 -66.675 101.626 1.00 123.19 ? 535 SER A N 1 ATOM 3606 C CA . SER A 1 535 ? -42.452 -66.844 102.775 1.00 117.10 ? 535 SER A CA 1 ATOM 3607 C C . SER A 1 535 ? -43.340 -65.639 102.957 1.00 116.40 ? 535 SER A C 1 ATOM 3608 O O . SER A 1 535 ? -42.864 -64.605 103.405 1.00 112.09 ? 535 SER A O 1 ATOM 3609 C CB . SER A 1 535 ? -41.654 -67.013 104.068 1.00 113.40 ? 535 SER A CB 1 ATOM 3610 O OG . SER A 1 535 ? -42.519 -67.332 105.147 1.00 110.28 ? 535 SER A OG 1 ATOM 3611 N N . PHE A 1 536 ? -44.630 -65.789 102.652 1.00 127.38 ? 536 PHE A N 1 ATOM 3612 C CA . PHE A 1 536 ? -45.576 -64.659 102.645 1.00 133.68 ? 536 PHE A CA 1 ATOM 3613 C C . PHE A 1 536 ? -46.418 -64.530 103.924 1.00 140.01 ? 536 PHE A C 1 ATOM 3614 O O . PHE A 1 536 ? -47.597 -64.192 103.896 1.00 153.47 ? 536 PHE A O 1 ATOM 3615 C CB . PHE A 1 536 ? -46.392 -64.654 101.334 1.00 130.63 ? 536 PHE A CB 1 ATOM 3616 C CG . PHE A 1 536 ? -45.522 -64.525 100.114 1.00 145.63 ? 536 PHE A CG 1 ATOM 3617 C CD1 . PHE A 1 536 ? -45.020 -63.279 99.726 1.00 167.73 ? 536 PHE A CD1 1 ATOM 3618 C CD2 . PHE A 1 536 ? -45.124 -65.649 99.398 1.00 154.53 ? 536 PHE A CD2 1 ATOM 3619 C CE1 . PHE A 1 536 ? -44.166 -63.156 98.627 1.00 181.36 ? 536 PHE A CE1 1 ATOM 3620 C CE2 . PHE A 1 536 ? -44.276 -65.533 98.295 1.00 168.86 ? 536 PHE A CE2 1 ATOM 3621 C CZ . PHE A 1 536 ? -43.794 -64.287 97.909 1.00 172.88 ? 536 PHE A CZ 1 ATOM 3622 N N . VAL A 1 537 ? -45.772 -64.795 105.052 1.00 140.49 ? 537 VAL A N 1 ATOM 3623 C CA . VAL A 1 537 ? -46.363 -64.600 106.360 1.00 141.10 ? 537 VAL A CA 1 ATOM 3624 C C . VAL A 1 537 ? -46.082 -63.159 106.758 1.00 142.51 ? 537 VAL A C 1 ATOM 3625 O O . VAL A 1 537 ? -46.818 -62.578 107.552 1.00 148.05 ? 537 VAL A O 1 ATOM 3626 C CB . VAL A 1 537 ? -45.790 -65.612 107.381 1.00 147.99 ? 537 VAL A CB 1 ATOM 3627 C CG1 . VAL A 1 537 ? -46.023 -65.165 108.834 1.00 155.91 ? 537 VAL A CG1 1 ATOM 3628 C CG2 . VAL A 1 537 ? -46.341 -67.012 107.093 1.00 133.09 ? 537 VAL A CG2 1 ATOM 3629 N N . ASN A 1 538 ? -45.011 -62.598 106.198 1.00 141.65 ? 538 ASN A N 1 ATOM 3630 C CA . ASN A 1 538 ? -44.703 -61.164 106.301 1.00 156.05 ? 538 ASN A CA 1 ATOM 3631 C C . ASN A 1 538 ? -43.800 -60.739 105.147 1.00 153.72 ? 538 ASN A C 1 ATOM 3632 O O . ASN A 1 538 ? -42.578 -60.588 105.311 1.00 133.74 ? 538 ASN A O 1 ATOM 3633 C CB . ASN A 1 538 ? -44.078 -60.799 107.662 1.00 165.75 ? 538 ASN A CB 1 ATOM 3634 C CG . ASN A 1 538 ? -44.034 -59.288 107.910 1.00 166.15 ? 538 ASN A CG 1 ATOM 3635 O OD1 . ASN A 1 538 ? -43.912 -58.500 106.976 1.00 162.85 ? 538 ASN A OD1 1 ATOM 3636 N ND2 . ASN A 1 538 ? -44.125 -58.884 109.180 1.00 164.48 ? 538 ASN A ND2 1 ATOM 3637 N N . MET A 1 539 ? -44.441 -60.507 103.999 1.00 165.76 ? 539 MET A N 1 ATOM 3638 C CA . MET A 1 539 ? -43.790 -60.485 102.675 1.00 165.84 ? 539 MET A CA 1 ATOM 3639 C C . MET A 1 539 ? -42.272 -60.274 102.625 1.00 154.82 ? 539 MET A C 1 ATOM 3640 O O . MET A 1 539 ? -41.572 -60.985 101.889 1.00 126.90 ? 539 MET A O 1 ATOM 3641 C CB . MET A 1 539 ? -44.506 -59.534 101.712 1.00 175.22 ? 539 MET A CB 1 ATOM 3642 C CG . MET A 1 539 ? -43.997 -59.632 100.282 1.00 178.90 ? 539 MET A CG 1 ATOM 3643 S SD . MET A 1 539 ? -44.967 -58.646 99.130 1.00 241.31 ? 539 MET A SD 1 ATOM 3644 C CE . MET A 1 539 ? -44.818 -56.977 99.783 1.00 228.49 ? 539 MET A CE 1 ATOM 3645 N N . GLU A 1 540 ? -41.782 -59.300 103.401 1.00 166.90 ? 540 GLU A N 1 ATOM 3646 C CA . GLU A 1 540 ? -40.369 -58.864 103.338 1.00 182.83 ? 540 GLU A CA 1 ATOM 3647 C C . GLU A 1 540 ? -39.547 -59.078 104.609 1.00 166.52 ? 540 GLU A C 1 ATOM 3648 O O . GLU A 1 540 ? -38.318 -59.165 104.533 1.00 169.46 ? 540 GLU A O 1 ATOM 3649 C CB . GLU A 1 540 ? -40.224 -57.400 102.838 1.00 193.44 ? 540 GLU A CB 1 ATOM 3650 C CG . GLU A 1 540 ? -40.736 -56.328 103.781 1.00 192.84 ? 540 GLU A CG 1 ATOM 3651 C CD . GLU A 1 540 ? -42.061 -56.719 104.393 1.00 207.03 ? 540 GLU A CD 1 ATOM 3652 O OE1 . GLU A 1 540 ? -43.087 -56.673 103.680 1.00 223.97 ? 540 GLU A OE1 1 ATOM 3653 O OE2 . GLU A 1 540 ? -42.064 -57.114 105.576 1.00 212.07 ? 540 GLU A OE2 1 ATOM 3654 N N . ARG A 1 541 ? -40.197 -59.142 105.766 1.00 144.17 ? 541 ARG A N 1 ATOM 3655 C CA . ARG A 1 541 ? -39.455 -59.472 106.972 1.00 136.02 ? 541 ARG A CA 1 ATOM 3656 C C . ARG A 1 541 ? -38.920 -60.876 106.752 1.00 132.91 ? 541 ARG A C 1 ATOM 3657 O O . ARG A 1 541 ? -37.717 -61.108 106.855 1.00 124.08 ? 541 ARG A O 1 ATOM 3658 C CB . ARG A 1 541 ? -40.344 -59.425 108.212 1.00 137.12 ? 541 ARG A CB 1 ATOM 3659 C CG . ARG A 1 541 ? -40.773 -58.046 108.660 1.00 129.46 ? 541 ARG A CG 1 ATOM 3660 C CD . ARG A 1 541 ? -39.671 -57.333 109.410 1.00 132.23 ? 541 ARG A CD 1 ATOM 3661 N NE . ARG A 1 541 ? -39.618 -57.610 110.849 1.00 150.82 ? 541 ARG A NE 1 ATOM 3662 C CZ . ARG A 1 541 ? -40.539 -57.238 111.741 1.00 163.10 ? 541 ARG A CZ 1 ATOM 3663 N NH1 . ARG A 1 541 ? -41.645 -56.614 111.358 1.00 166.50 ? 541 ARG A NH1 1 ATOM 3664 N NH2 . ARG A 1 541 ? -40.368 -57.513 113.029 1.00 173.16 ? 541 ARG A NH2 1 ATOM 3665 N N . ASP A 1 542 ? -39.839 -61.776 106.391 1.00 132.55 ? 542 ASP A N 1 ATOM 3666 C CA . ASP A 1 542 ? -39.564 -63.185 106.119 1.00 140.62 ? 542 ASP A CA 1 ATOM 3667 C C . ASP A 1 542 ? -38.560 -63.386 104.987 1.00 148.22 ? 542 ASP A C 1 ATOM 3668 O O . ASP A 1 542 ? -37.846 -64.384 104.974 1.00 147.50 ? 542 ASP A O 1 ATOM 3669 C CB . ASP A 1 542 ? -40.861 -63.940 105.791 1.00 146.62 ? 542 ASP A CB 1 ATOM 3670 C CG . ASP A 1 542 ? -41.903 -63.870 106.913 1.00 145.37 ? 542 ASP A CG 1 ATOM 3671 O OD1 . ASP A 1 542 ? -41.622 -63.284 107.970 1.00 145.12 ? 542 ASP A OD1 1 ATOM 3672 O OD2 . ASP A 1 542 ? -43.016 -64.405 106.737 1.00 144.64 ? 542 ASP A OD2 1 ATOM 3673 N N . LEU A 1 543 ? -38.524 -62.457 104.030 1.00 155.19 ? 543 LEU A N 1 ATOM 3674 C CA . LEU A 1 543 ? -37.396 -62.382 103.095 1.00 156.70 ? 543 LEU A CA 1 ATOM 3675 C C . LEU A 1 543 ? -36.167 -61.753 103.757 1.00 163.50 ? 543 LEU A C 1 ATOM 3676 O O . LEU A 1 543 ? -35.106 -62.378 103.838 1.00 171.70 ? 543 LEU A O 1 ATOM 3677 C CB . LEU A 1 543 ? -37.733 -61.597 101.822 1.00 139.96 ? 543 LEU A CB 1 ATOM 3678 C CG . LEU A 1 543 ? -36.463 -61.001 101.169 1.00 143.03 ? 543 LEU A CG 1 ATOM 3679 C CD1 . LEU A 1 543 ? -36.363 -61.383 99.709 1.00 149.28 ? 543 LEU A CD1 1 ATOM 3680 C CD2 . LEU A 1 543 ? -36.290 -59.488 101.348 1.00 152.05 ? 543 LEU A CD2 1 ATOM 3681 N N . ALA A 1 544 ? -36.303 -60.510 104.213 1.00 152.85 ? 544 ALA A N 1 ATOM 3682 C CA . ALA A 1 544 ? -35.146 -59.775 104.662 1.00 144.58 ? 544 ALA A CA 1 ATOM 3683 C C . ALA A 1 544 ? -34.604 -60.422 105.928 1.00 143.54 ? 544 ALA A C 1 ATOM 3684 O O . ALA A 1 544 ? -33.513 -60.097 106.370 1.00 169.47 ? 544 ALA A O 1 ATOM 3685 C CB . ALA A 1 544 ? -35.459 -58.294 104.836 1.00 143.18 ? 544 ALA A CB 1 ATOM 3686 N N . SER A 1 545 ? -35.337 -61.386 106.474 1.00 134.79 ? 545 SER A N 1 ATOM 3687 C CA . SER A 1 545 ? -34.793 -62.215 107.551 1.00 140.69 ? 545 SER A CA 1 ATOM 3688 C C . SER A 1 545 ? -33.921 -63.399 107.065 1.00 139.02 ? 545 SER A C 1 ATOM 3689 O O . SER A 1 545 ? -33.109 -63.904 107.843 1.00 143.13 ? 545 SER A O 1 ATOM 3690 C CB . SER A 1 545 ? -35.895 -62.686 108.517 1.00 142.03 ? 545 SER A CB 1 ATOM 3691 O OG . SER A 1 545 ? -36.423 -61.616 109.289 1.00 131.96 ? 545 SER A OG 1 ATOM 3692 N N . GLY A 1 546 ? -34.084 -63.831 105.806 1.00 129.07 ? 546 GLY A N 1 ATOM 3693 C CA . GLY A 1 546 ? -33.221 -64.882 105.191 1.00 135.69 ? 546 GLY A CA 1 ATOM 3694 C C . GLY A 1 546 ? -33.879 -65.872 104.213 1.00 139.07 ? 546 GLY A C 1 ATOM 3695 O O . GLY A 1 546 ? -33.208 -66.676 103.503 1.00 126.16 ? 546 GLY A O 1 ATOM 3696 N N . LEU A 1 547 ? -35.205 -65.825 104.176 1.00 142.80 ? 547 LEU A N 1 ATOM 3697 C CA . LEU A 1 547 ? -35.959 -66.774 103.376 1.00 141.77 ? 547 LEU A CA 1 ATOM 3698 C C . LEU A 1 547 ? -36.125 -66.328 101.924 1.00 125.66 ? 547 LEU A C 1 ATOM 3699 O O . LEU A 1 547 ? -37.147 -65.723 101.565 1.00 121.02 ? 547 LEU A O 1 ATOM 3700 C CB . LEU A 1 547 ? -37.334 -67.113 104.018 1.00 148.53 ? 547 LEU A CB 1 ATOM 3701 C CG . LEU A 1 547 ? -37.648 -68.245 105.046 1.00 147.49 ? 547 LEU A CG 1 ATOM 3702 C CD1 . LEU A 1 547 ? -36.708 -69.454 105.028 1.00 136.51 ? 547 LEU A CD1 1 ATOM 3703 C CD2 . LEU A 1 547 ? -37.800 -67.746 106.479 1.00 142.65 ? 547 LEU A CD2 1 ATOM 3704 N N . ILE A 1 548 ? -35.102 -66.593 101.112 1.00 107.85 ? 548 ILE A N 1 ATOM 3705 C CA . ILE A 1 548 ? -35.366 -66.949 99.718 1.00 112.76 ? 548 ILE A CA 1 ATOM 3706 C C . ILE A 1 548 ? -34.468 -68.050 99.240 1.00 123.89 ? 548 ILE A C 1 ATOM 3707 O O . ILE A 1 548 ? -33.548 -68.492 99.968 1.00 122.45 ? 548 ILE A O 1 ATOM 3708 C CB . ILE A 1 548 ? -35.230 -65.830 98.665 1.00 104.91 ? 548 ILE A CB 1 ATOM 3709 C CG1 . ILE A 1 548 ? -34.157 -64.843 99.045 1.00 106.43 ? 548 ILE A CG1 1 ATOM 3710 C CG2 . ILE A 1 548 ? -36.563 -65.204 98.340 1.00 112.46 ? 548 ILE A CG2 1 ATOM 3711 C CD1 . ILE A 1 548 ? -32.824 -65.263 98.487 1.00 114.33 ? 548 ILE A CD1 1 ATOM 3712 N N . GLY A 1 549 ? -34.795 -68.451 98.001 1.00 127.92 ? 549 GLY A N 1 ATOM 3713 C CA . GLY A 1 549 ? -34.041 -69.342 97.113 1.00 133.95 ? 549 GLY A CA 1 ATOM 3714 C C . GLY A 1 549 ? -34.616 -69.171 95.705 1.00 131.45 ? 549 GLY A C 1 ATOM 3715 O O . GLY A 1 549 ? -35.593 -68.442 95.540 1.00 134.48 ? 549 GLY A O 1 ATOM 3716 N N . PRO A 1 550 ? -34.035 -69.848 94.685 1.00 130.09 ? 550 PRO A N 1 ATOM 3717 C CA . PRO A 1 550 ? -34.429 -69.632 93.292 1.00 122.24 ? 550 PRO A CA 1 ATOM 3718 C C . PRO A 1 550 ? -35.356 -70.700 92.745 1.00 123.47 ? 550 PRO A C 1 ATOM 3719 O O . PRO A 1 550 ? -35.330 -71.851 93.218 1.00 124.11 ? 550 PRO A O 1 ATOM 3720 C CB . PRO A 1 550 ? -33.104 -69.753 92.557 1.00 122.22 ? 550 PRO A CB 1 ATOM 3721 C CG . PRO A 1 550 ? -32.357 -70.787 93.340 1.00 127.00 ? 550 PRO A CG 1 ATOM 3722 C CD . PRO A 1 550 ? -32.882 -70.763 94.760 1.00 131.39 ? 550 PRO A CD 1 ATOM 3723 N N . LEU A 1 551 ? -36.135 -70.313 91.731 1.00 116.58 ? 551 LEU A N 1 ATOM 3724 C CA . LEU A 1 551 ? -37.014 -71.238 91.005 1.00 108.19 ? 551 LEU A CA 1 ATOM 3725 C C . LEU A 1 551 ? -37.007 -71.076 89.486 1.00 104.41 ? 551 LEU A C 1 ATOM 3726 O O . LEU A 1 551 ? -37.306 -70.011 88.956 1.00 112.69 ? 551 LEU A O 1 ATOM 3727 C CB . LEU A 1 551 ? -38.450 -71.147 91.509 1.00 101.34 ? 551 LEU A CB 1 ATOM 3728 C CG . LEU A 1 551 ? -39.483 -71.867 90.632 1.00 104.54 ? 551 LEU A CG 1 ATOM 3729 C CD1 . LEU A 1 551 ? -39.451 -73.396 90.720 1.00 106.21 ? 551 LEU A CD1 1 ATOM 3730 C CD2 . LEU A 1 551 ? -40.857 -71.338 90.986 1.00 114.54 ? 551 LEU A CD2 1 ATOM 3731 N N . LEU A 1 552 ? -36.711 -72.162 88.789 1.00 103.09 ? 552 LEU A N 1 ATOM 3732 C CA . LEU A 1 552 ? -36.667 -72.140 87.337 1.00 103.62 ? 552 LEU A CA 1 ATOM 3733 C C . LEU A 1 552 ? -37.840 -72.874 86.714 1.00 115.84 ? 552 LEU A C 1 ATOM 3734 O O . LEU A 1 552 ? -37.993 -74.087 86.900 1.00 131.36 ? 552 LEU A O 1 ATOM 3735 C CB . LEU A 1 552 ? -35.338 -72.718 86.859 1.00 90.08 ? 552 LEU A CB 1 ATOM 3736 C CG . LEU A 1 552 ? -34.225 -71.818 87.394 1.00 84.29 ? 552 LEU A CG 1 ATOM 3737 C CD1 . LEU A 1 552 ? -32.820 -72.346 87.153 1.00 81.49 ? 552 LEU A CD1 1 ATOM 3738 C CD2 . LEU A 1 552 ? -34.396 -70.447 86.770 1.00 85.41 ? 552 LEU A CD2 1 ATOM 3739 N N . ILE A 1 553 ? -38.688 -72.140 86.003 1.00 109.32 ? 553 ILE A N 1 ATOM 3740 C CA . ILE A 1 553 ? -39.683 -72.799 85.187 1.00 115.21 ? 553 ILE A CA 1 ATOM 3741 C C . ILE A 1 553 ? -39.156 -72.788 83.777 1.00 122.08 ? 553 ILE A C 1 ATOM 3742 O O . ILE A 1 553 ? -38.868 -71.725 83.227 1.00 126.23 ? 553 ILE A O 1 ATOM 3743 C CB . ILE A 1 553 ? -41.009 -72.069 85.219 1.00 118.77 ? 553 ILE A CB 1 ATOM 3744 C CG1 . ILE A 1 553 ? -41.565 -72.088 86.633 1.00 124.50 ? 553 ILE A CG1 1 ATOM 3745 C CG2 . ILE A 1 553 ? -41.973 -72.699 84.222 1.00 123.56 ? 553 ILE A CG2 1 ATOM 3746 C CD1 . ILE A 1 553 ? -42.412 -70.873 86.939 1.00 133.27 ? 553 ILE A CD1 1 ATOM 3747 N N . CYS A 1 554 ? -39.007 -73.966 83.189 1.00 122.43 ? 554 CYS A N 1 ATOM 3748 C CA . CYS A 1 554 ? -38.343 -74.030 81.906 1.00 120.73 ? 554 CYS A CA 1 ATOM 3749 C C . CYS A 1 554 ? -39.131 -74.808 80.920 1.00 115.33 ? 554 CYS A C 1 ATOM 3750 O O . CYS A 1 554 ? -40.049 -75.511 81.301 1.00 108.07 ? 554 CYS A O 1 ATOM 3751 C CB . CYS A 1 554 ? -36.921 -74.532 82.066 1.00 130.95 ? 554 CYS A CB 1 ATOM 3752 S SG . CYS A 1 554 ? -35.940 -73.272 82.939 1.00 157.47 ? 554 CYS A SG 1 ATOM 3753 N N . TYR A 1 555 ? -38.794 -74.644 79.648 1.00 122.15 ? 555 TYR A N 1 ATOM 3754 C CA . TYR A 1 555 ? -39.595 -75.205 78.580 1.00 141.63 ? 555 TYR A CA 1 ATOM 3755 C C . TYR A 1 555 ? -39.361 -76.700 78.430 1.00 149.66 ? 555 TYR A C 1 ATOM 3756 O O . TYR A 1 555 ? -38.321 -77.193 78.848 1.00 167.21 ? 555 TYR A O 1 ATOM 3757 C CB . TYR A 1 555 ? -39.320 -74.489 77.264 1.00 157.09 ? 555 TYR A CB 1 ATOM 3758 C CG . TYR A 1 555 ? -40.526 -74.511 76.352 1.00 185.06 ? 555 TYR A CG 1 ATOM 3759 C CD1 . TYR A 1 555 ? -41.629 -75.330 76.649 1.00 194.79 ? 555 TYR A CD1 1 ATOM 3760 C CD2 . TYR A 1 555 ? -40.571 -73.729 75.195 1.00 183.79 ? 555 TYR A CD2 1 ATOM 3761 C CE1 . TYR A 1 555 ? -42.735 -75.370 75.828 1.00 214.81 ? 555 TYR A CE1 1 ATOM 3762 C CE2 . TYR A 1 555 ? -41.673 -73.764 74.358 1.00 202.28 ? 555 TYR A CE2 1 ATOM 3763 C CZ . TYR A 1 555 ? -42.751 -74.584 74.685 1.00 230.81 ? 555 TYR A CZ 1 ATOM 3764 O OH . TYR A 1 555 ? -43.857 -74.631 73.874 1.00 273.37 ? 555 TYR A OH 1 ATOM 3765 N N . LYS A 1 556 ? -40.322 -77.411 77.830 1.00 155.10 ? 556 LYS A N 1 ATOM 3766 C CA . LYS A 1 556 ? -40.299 -78.886 77.742 1.00 183.51 ? 556 LYS A CA 1 ATOM 3767 C C . LYS A 1 556 ? -39.327 -79.464 76.675 1.00 206.89 ? 556 LYS A C 1 ATOM 3768 O O . LYS A 1 556 ? -39.617 -80.488 76.042 1.00 224.90 ? 556 LYS A O 1 ATOM 3769 C CB . LYS A 1 556 ? -41.741 -79.430 77.561 1.00 183.26 ? 556 LYS A CB 1 ATOM 3770 C CG . LYS A 1 556 ? -41.967 -80.921 77.877 1.00 186.46 ? 556 LYS A CG 1 ATOM 3771 C CD . LYS A 1 556 ? -41.937 -81.236 79.373 1.00 168.49 ? 556 LYS A CD 1 ATOM 3772 C CE . LYS A 1 556 ? -42.057 -82.727 79.665 1.00 163.34 ? 556 LYS A CE 1 ATOM 3773 N NZ . LYS A 1 556 ? -41.639 -83.017 81.068 1.00 150.19 ? 556 LYS A NZ 1 ATOM 3774 N N . GLU A 1 557 ? -38.170 -78.825 76.496 1.00 217.83 ? 557 GLU A N 1 ATOM 3775 C CA . GLU A 1 557 ? -37.192 -79.271 75.494 1.00 228.96 ? 557 GLU A CA 1 ATOM 3776 C C . GLU A 1 557 ? -36.500 -80.562 75.928 1.00 226.86 ? 557 GLU A C 1 ATOM 3777 O O . GLU A 1 557 ? -36.416 -81.512 75.154 1.00 237.39 ? 557 GLU A O 1 ATOM 3778 C CB . GLU A 1 557 ? -36.166 -78.168 75.182 1.00 231.14 ? 557 GLU A CB 1 ATOM 3779 C CG . GLU A 1 557 ? -34.940 -78.149 76.089 1.00 235.38 ? 557 GLU A CG 1 ATOM 3780 C CD . GLU A 1 557 ? -34.681 -76.788 76.711 1.00 226.73 ? 557 GLU A CD 1 ATOM 3781 O OE1 . GLU A 1 557 ? -35.612 -75.950 76.735 1.00 221.68 ? 557 GLU A OE1 1 ATOM 3782 O OE2 . GLU A 1 557 ? -33.550 -76.561 77.198 1.00 222.14 ? 557 GLU A OE2 1 ATOM 3783 N N . ARG A 1 571 ? -25.991 -75.366 87.619 1.00 153.69 ? 571 ARG A N 1 ATOM 3784 C CA . ARG A 1 571 ? -26.527 -74.111 87.043 1.00 155.33 ? 571 ARG A CA 1 ATOM 3785 C C . ARG A 1 571 ? -26.214 -72.828 87.872 1.00 148.58 ? 571 ARG A C 1 ATOM 3786 O O . ARG A 1 571 ? -26.166 -72.847 89.118 1.00 144.45 ? 571 ARG A O 1 ATOM 3787 C CB . ARG A 1 571 ? -28.030 -74.248 86.727 1.00 153.61 ? 571 ARG A CB 1 ATOM 3788 C CG . ARG A 1 571 ? -28.327 -75.150 85.534 1.00 168.59 ? 571 ARG A CG 1 ATOM 3789 C CD . ARG A 1 571 ? -29.745 -75.722 85.538 1.00 177.28 ? 571 ARG A CD 1 ATOM 3790 N NE . ARG A 1 571 ? -29.936 -76.864 86.456 1.00 210.72 ? 571 ARG A NE 1 ATOM 3791 C CZ . ARG A 1 571 ? -30.920 -77.773 86.362 1.00 216.04 ? 571 ARG A CZ 1 ATOM 3792 N NH1 . ARG A 1 571 ? -31.806 -77.692 85.376 1.00 223.58 ? 571 ARG A NH1 1 ATOM 3793 N NH2 . ARG A 1 571 ? -31.028 -78.778 87.244 1.00 185.45 ? 571 ARG A NH2 1 ATOM 3794 N N . ASN A 1 572 ? -26.010 -71.719 87.160 1.00 137.16 ? 572 ASN A N 1 ATOM 3795 C CA . ASN A 1 572 ? -25.463 -70.477 87.738 1.00 140.56 ? 572 ASN A CA 1 ATOM 3796 C C . ASN A 1 572 ? -26.436 -69.398 88.225 1.00 145.38 ? 572 ASN A C 1 ATOM 3797 O O . ASN A 1 572 ? -26.913 -68.574 87.424 1.00 149.10 ? 572 ASN A O 1 ATOM 3798 C CB . ASN A 1 572 ? -24.517 -69.837 86.729 1.00 134.54 ? 572 ASN A CB 1 ATOM 3799 C CG . ASN A 1 572 ? -23.095 -70.215 86.979 1.00 135.05 ? 572 ASN A CG 1 ATOM 3800 O OD1 . ASN A 1 572 ? -22.624 -70.139 88.118 1.00 140.86 ? 572 ASN A OD1 1 ATOM 3801 N ND2 . ASN A 1 572 ? -22.398 -70.644 85.930 1.00 135.12 ? 572 ASN A ND2 1 ATOM 3802 N N . VAL A 1 573 ? -26.693 -69.355 89.531 1.00 131.86 ? 573 VAL A N 1 ATOM 3803 C CA . VAL A 1 573 ? -27.650 -68.367 90.020 1.00 119.20 ? 573 VAL A CA 1 ATOM 3804 C C . VAL A 1 573 ? -27.008 -67.223 90.775 1.00 125.47 ? 573 VAL A C 1 ATOM 3805 O O . VAL A 1 573 ? -26.468 -67.440 91.860 1.00 137.86 ? 573 VAL A O 1 ATOM 3806 C CB . VAL A 1 573 ? -28.741 -69.000 90.889 1.00 111.81 ? 573 VAL A CB 1 ATOM 3807 C CG1 . VAL A 1 573 ? -29.543 -67.925 91.614 1.00 109.82 ? 573 VAL A CG1 1 ATOM 3808 C CG2 . VAL A 1 573 ? -29.659 -69.824 90.017 1.00 106.10 ? 573 VAL A CG2 1 ATOM 3809 N N . ILE A 1 574 ? -27.081 -66.018 90.193 1.00 121.49 ? 574 ILE A N 1 ATOM 3810 C CA . ILE A 1 574 ? -26.685 -64.767 90.864 1.00 113.23 ? 574 ILE A CA 1 ATOM 3811 C C . ILE A 1 574 ? -27.944 -64.092 91.407 1.00 105.50 ? 574 ILE A C 1 ATOM 3812 O O . ILE A 1 574 ? -28.875 -63.818 90.651 1.00 97.87 ? 574 ILE A O 1 ATOM 3813 C CB . ILE A 1 574 ? -25.904 -63.805 89.914 1.00 116.97 ? 574 ILE A CB 1 ATOM 3814 C CG1 . ILE A 1 574 ? -24.400 -64.067 89.917 1.00 127.05 ? 574 ILE A CG1 1 ATOM 3815 C CG2 . ILE A 1 574 ? -25.951 -62.374 90.404 1.00 112.31 ? 574 ILE A CG2 1 ATOM 3816 C CD1 . ILE A 1 574 ? -23.976 -65.518 89.866 1.00 141.04 ? 574 ILE A CD1 1 ATOM 3817 N N . LEU A 1 575 ? -27.976 -63.857 92.719 1.00 105.73 ? 575 LEU A N 1 ATOM 3818 C CA . LEU A 1 575 ? -29.040 -63.060 93.350 1.00 111.64 ? 575 LEU A CA 1 ATOM 3819 C C . LEU A 1 575 ? -28.563 -61.711 93.968 1.00 115.56 ? 575 LEU A C 1 ATOM 3820 O O . LEU A 1 575 ? -27.788 -61.688 94.926 1.00 119.05 ? 575 LEU A O 1 ATOM 3821 C CB . LEU A 1 575 ? -29.800 -63.893 94.393 1.00 103.11 ? 575 LEU A CB 1 ATOM 3822 C CG . LEU A 1 575 ? -30.194 -63.062 95.630 1.00 105.97 ? 575 LEU A CG 1 ATOM 3823 C CD1 . LEU A 1 575 ? -31.429 -62.182 95.475 1.00 94.25 ? 575 LEU A CD1 1 ATOM 3824 C CD2 . LEU A 1 575 ? -30.319 -63.939 96.854 1.00 117.86 ? 575 LEU A CD2 1 ATOM 3825 N N . PHE A 1 576 ? -29.051 -60.593 93.440 1.00 110.60 ? 576 PHE A N 1 ATOM 3826 C CA . PHE A 1 576 ? -28.706 -59.298 93.999 1.00 112.89 ? 576 PHE A CA 1 ATOM 3827 C C . PHE A 1 576 ? -29.659 -58.889 95.109 1.00 121.65 ? 576 PHE A C 1 ATOM 3828 O O . PHE A 1 576 ? -30.726 -58.326 94.854 1.00 125.66 ? 576 PHE A O 1 ATOM 3829 C CB . PHE A 1 576 ? -28.721 -58.251 92.911 1.00 114.68 ? 576 PHE A CB 1 ATOM 3830 C CG . PHE A 1 576 ? -27.540 -58.305 92.007 1.00 122.05 ? 576 PHE A CG 1 ATOM 3831 C CD1 . PHE A 1 576 ? -27.533 -59.145 90.902 1.00 125.36 ? 576 PHE A CD1 1 ATOM 3832 C CD2 . PHE A 1 576 ? -26.433 -57.497 92.244 1.00 128.34 ? 576 PHE A CD2 1 ATOM 3833 C CE1 . PHE A 1 576 ? -26.431 -59.186 90.054 1.00 133.91 ? 576 PHE A CE1 1 ATOM 3834 C CE2 . PHE A 1 576 ? -25.332 -57.532 91.396 1.00 132.94 ? 576 PHE A CE2 1 ATOM 3835 C CZ . PHE A 1 576 ? -25.328 -58.382 90.301 1.00 132.22 ? 576 PHE A CZ 1 ATOM 3836 N N . SER A 1 577 ? -29.272 -59.161 96.346 1.00 130.82 ? 577 SER A N 1 ATOM 3837 C CA . SER A 1 577 ? -30.138 -58.825 97.467 1.00 141.81 ? 577 SER A CA 1 ATOM 3838 C C . SER A 1 577 ? -29.547 -57.869 98.519 1.00 153.49 ? 577 SER A C 1 ATOM 3839 O O . SER A 1 577 ? -28.452 -58.074 99.044 1.00 157.88 ? 577 SER A O 1 ATOM 3840 C CB . SER A 1 577 ? -30.684 -60.094 98.133 1.00 126.24 ? 577 SER A CB 1 ATOM 3841 O OG . SER A 1 577 ? -31.816 -59.794 98.940 1.00 119.09 ? 577 SER A OG 1 ATOM 3842 N N . VAL A 1 578 ? -30.308 -56.816 98.800 1.00 156.33 ? 578 VAL A N 1 ATOM 3843 C CA . VAL A 1 578 ? -30.135 -56.004 100.000 1.00 141.61 ? 578 VAL A CA 1 ATOM 3844 C C . VAL A 1 578 ? -30.971 -56.590 101.176 1.00 134.99 ? 578 VAL A C 1 ATOM 3845 O O . VAL A 1 578 ? -32.214 -56.679 101.153 1.00 124.53 ? 578 VAL A O 1 ATOM 3846 C CB . VAL A 1 578 ? -30.384 -54.485 99.708 1.00 136.98 ? 578 VAL A CB 1 ATOM 3847 C CG1 . VAL A 1 578 ? -31.816 -54.047 100.001 1.00 129.21 ? 578 VAL A CG1 1 ATOM 3848 C CG2 . VAL A 1 578 ? -29.414 -53.607 100.479 1.00 135.91 ? 578 VAL A CG2 1 ATOM 3849 N N . PHE A 1 579 ? -30.269 -57.040 102.199 1.00 133.43 ? 579 PHE A N 1 ATOM 3850 C CA . PHE A 1 579 ? -30.959 -57.484 103.385 1.00 141.27 ? 579 PHE A CA 1 ATOM 3851 C C . PHE A 1 579 ? -30.995 -56.378 104.410 1.00 146.06 ? 579 PHE A C 1 ATOM 3852 O O . PHE A 1 579 ? -29.946 -55.879 104.846 1.00 149.11 ? 579 PHE A O 1 ATOM 3853 C CB . PHE A 1 579 ? -30.294 -58.727 103.948 1.00 143.06 ? 579 PHE A CB 1 ATOM 3854 C CG . PHE A 1 579 ? -30.391 -59.896 103.037 1.00 141.34 ? 579 PHE A CG 1 ATOM 3855 C CD1 . PHE A 1 579 ? -31.610 -60.532 102.844 1.00 134.54 ? 579 PHE A CD1 1 ATOM 3856 C CD2 . PHE A 1 579 ? -29.272 -60.339 102.339 1.00 143.90 ? 579 PHE A CD2 1 ATOM 3857 C CE1 . PHE A 1 579 ? -31.704 -61.609 101.992 1.00 134.32 ? 579 PHE A CE1 1 ATOM 3858 C CE2 . PHE A 1 579 ? -29.353 -61.424 101.483 1.00 139.93 ? 579 PHE A CE2 1 ATOM 3859 C CZ . PHE A 1 579 ? -30.571 -62.060 101.313 1.00 140.10 ? 579 PHE A CZ 1 ATOM 3860 N N . ASP A 1 580 ? -32.204 -55.976 104.783 1.00 139.69 ? 580 ASP A N 1 ATOM 3861 C CA . ASP A 1 580 ? -32.319 -54.984 105.832 1.00 149.04 ? 580 ASP A CA 1 ATOM 3862 C C . ASP A 1 580 ? -32.373 -55.606 107.228 1.00 149.00 ? 580 ASP A C 1 ATOM 3863 O O . ASP A 1 580 ? -33.454 -55.769 107.815 1.00 149.83 ? 580 ASP A O 1 ATOM 3864 C CB . ASP A 1 580 ? -33.511 -54.063 105.607 1.00 159.58 ? 580 ASP A CB 1 ATOM 3865 C CG . ASP A 1 580 ? -33.537 -52.910 106.600 1.00 176.05 ? 580 ASP A CG 1 ATOM 3866 O OD1 . ASP A 1 580 ? -32.606 -52.063 106.593 1.00 166.85 ? 580 ASP A OD1 1 ATOM 3867 O OD2 . ASP A 1 580 ? -34.489 -52.870 107.406 1.00 191.89 ? 580 ASP A OD2 1 ATOM 3868 N N . GLU A 1 581 ? -31.202 -55.941 107.765 1.00 140.80 ? 581 GLU A N 1 ATOM 3869 C CA . GLU A 1 581 ? -31.127 -56.489 109.111 1.00 142.04 ? 581 GLU A CA 1 ATOM 3870 C C . GLU A 1 581 ? -31.779 -55.589 110.146 1.00 153.82 ? 581 GLU A C 1 ATOM 3871 O O . GLU A 1 581 ? -32.130 -56.073 111.215 1.00 168.61 ? 581 GLU A O 1 ATOM 3872 C CB . GLU A 1 581 ? -29.689 -56.790 109.510 1.00 141.13 ? 581 GLU A CB 1 ATOM 3873 C CG . GLU A 1 581 ? -29.187 -58.118 108.987 1.00 141.45 ? 581 GLU A CG 1 ATOM 3874 C CD . GLU A 1 581 ? -29.703 -59.306 109.779 1.00 147.45 ? 581 GLU A CD 1 ATOM 3875 O OE1 . GLU A 1 581 ? -30.237 -59.134 110.910 1.00 148.11 ? 581 GLU A OE1 1 ATOM 3876 O OE2 . GLU A 1 581 ? -29.549 -60.428 109.256 1.00 146.17 ? 581 GLU A OE2 1 ATOM 3877 N N . ASN A 1 582 ? -31.931 -54.297 109.820 1.00 159.85 ? 582 ASN A N 1 ATOM 3878 C CA . ASN A 1 582 ? -32.696 -53.312 110.615 1.00 164.97 ? 582 ASN A CA 1 ATOM 3879 C C . ASN A 1 582 ? -34.113 -53.737 110.983 1.00 178.98 ? 582 ASN A C 1 ATOM 3880 O O . ASN A 1 582 ? -34.634 -53.344 112.045 1.00 187.78 ? 582 ASN A O 1 ATOM 3881 C CB . ASN A 1 582 ? -32.783 -51.986 109.882 1.00 165.21 ? 582 ASN A CB 1 ATOM 3882 C CG . ASN A 1 582 ? -32.014 -50.907 110.570 1.00 177.44 ? 582 ASN A CG 1 ATOM 3883 O OD1 . ASN A 1 582 ? -32.546 -50.209 111.431 1.00 187.27 ? 582 ASN A OD1 1 ATOM 3884 N ND2 . ASN A 1 582 ? -30.746 -50.773 110.215 1.00 185.21 ? 582 ASN A ND2 1 ATOM 3885 N N . ARG A 1 583 ? -34.748 -54.486 110.075 1.00 172.84 ? 583 ARG A N 1 ATOM 3886 C CA . ARG A 1 583 ? -35.899 -55.317 110.437 1.00 165.86 ? 583 ARG A CA 1 ATOM 3887 C C . ARG A 1 583 ? -35.835 -56.750 109.893 1.00 151.76 ? 583 ARG A C 1 ATOM 3888 O O . ARG A 1 583 ? -36.650 -57.170 109.074 1.00 145.34 ? 583 ARG A O 1 ATOM 3889 C CB . ARG A 1 583 ? -37.258 -54.630 110.203 1.00 167.29 ? 583 ARG A CB 1 ATOM 3890 C CG . ARG A 1 583 ? -37.381 -53.818 108.933 1.00 159.36 ? 583 ARG A CG 1 ATOM 3891 C CD . ARG A 1 583 ? -38.616 -52.924 108.989 1.00 172.70 ? 583 ARG A CD 1 ATOM 3892 N NE . ARG A 1 583 ? -39.742 -53.462 108.227 1.00 180.27 ? 583 ARG A NE 1 ATOM 3893 C CZ . ARG A 1 583 ? -39.789 -53.556 106.891 1.00 194.90 ? 583 ARG A CZ 1 ATOM 3894 N NH1 . ARG A 1 583 ? -38.767 -53.163 106.126 1.00 201.57 ? 583 ARG A NH1 1 ATOM 3895 N NH2 . ARG A 1 583 ? -40.868 -54.058 106.304 1.00 196.43 ? 583 ARG A NH2 1 ATOM 3896 N N . SER A 1 584 ? -34.830 -57.486 110.363 1.00 145.02 ? 584 SER A N 1 ATOM 3897 C CA . SER A 1 584 ? -34.946 -58.928 110.528 1.00 145.70 ? 584 SER A CA 1 ATOM 3898 C C . SER A 1 584 ? -36.004 -59.070 111.627 1.00 143.68 ? 584 SER A C 1 ATOM 3899 O O . SER A 1 584 ? -36.336 -58.080 112.296 1.00 139.70 ? 584 SER A O 1 ATOM 3900 C CB . SER A 1 584 ? -33.601 -59.520 110.991 1.00 150.80 ? 584 SER A CB 1 ATOM 3901 O OG . SER A 1 584 ? -33.570 -60.942 110.922 1.00 149.92 ? 584 SER A OG 1 ATOM 3902 N N . TRP A 1 585 ? -36.562 -60.263 111.816 1.00 138.34 ? 585 TRP A N 1 ATOM 3903 C CA . TRP A 1 585 ? -37.331 -60.488 113.034 1.00 147.69 ? 585 TRP A CA 1 ATOM 3904 C C . TRP A 1 585 ? -36.318 -60.699 114.174 1.00 158.81 ? 585 TRP A C 1 ATOM 3905 O O . TRP A 1 585 ? -36.598 -60.501 115.375 1.00 176.93 ? 585 TRP A O 1 ATOM 3906 C CB . TRP A 1 585 ? -38.204 -61.730 112.938 1.00 146.31 ? 585 TRP A CB 1 ATOM 3907 C CG . TRP A 1 585 ? -39.334 -61.789 111.949 1.00 141.93 ? 585 TRP A CG 1 ATOM 3908 C CD1 . TRP A 1 585 ? -39.261 -62.280 110.692 1.00 145.66 ? 585 TRP A CD1 1 ATOM 3909 C CD2 . TRP A 1 585 ? -40.727 -61.474 112.178 1.00 141.84 ? 585 TRP A CD2 1 ATOM 3910 N NE1 . TRP A 1 585 ? -40.499 -62.256 110.101 1.00 156.26 ? 585 TRP A NE1 1 ATOM 3911 C CE2 . TRP A 1 585 ? -41.417 -61.763 110.990 1.00 147.37 ? 585 TRP A CE2 1 ATOM 3912 C CE3 . TRP A 1 585 ? -41.446 -60.951 113.256 1.00 150.40 ? 585 TRP A CE3 1 ATOM 3913 C CZ2 . TRP A 1 585 ? -42.802 -61.553 110.844 1.00 150.70 ? 585 TRP A CZ2 1 ATOM 3914 C CZ3 . TRP A 1 585 ? -42.832 -60.743 113.112 1.00 159.58 ? 585 TRP A CZ3 1 ATOM 3915 C CH2 . TRP A 1 585 ? -43.487 -61.045 111.915 1.00 156.31 ? 585 TRP A CH2 1 ATOM 3916 N N . TYR A 1 586 ? -35.127 -61.112 113.769 1.00 155.64 ? 586 TYR A N 1 ATOM 3917 C CA . TYR A 1 586 ? -34.085 -61.486 114.688 1.00 161.42 ? 586 TYR A CA 1 ATOM 3918 C C . TYR A 1 586 ? -33.280 -60.282 115.135 1.00 168.11 ? 586 TYR A C 1 ATOM 3919 O O . TYR A 1 586 ? -32.574 -60.361 116.124 1.00 173.39 ? 586 TYR A O 1 ATOM 3920 C CB . TYR A 1 586 ? -33.188 -62.531 114.027 1.00 161.16 ? 586 TYR A CB 1 ATOM 3921 C CG . TYR A 1 586 ? -33.955 -63.752 113.543 1.00 161.64 ? 586 TYR A CG 1 ATOM 3922 C CD1 . TYR A 1 586 ? -34.173 -64.850 114.385 1.00 157.00 ? 586 TYR A CD1 1 ATOM 3923 C CD2 . TYR A 1 586 ? -34.478 -63.809 112.245 1.00 163.74 ? 586 TYR A CD2 1 ATOM 3924 C CE1 . TYR A 1 586 ? -34.881 -65.971 113.949 1.00 144.16 ? 586 TYR A CE1 1 ATOM 3925 C CE2 . TYR A 1 586 ? -35.188 -64.927 111.804 1.00 152.97 ? 586 TYR A CE2 1 ATOM 3926 C CZ . TYR A 1 586 ? -35.385 -66.010 112.659 1.00 139.32 ? 586 TYR A CZ 1 ATOM 3927 O OH . TYR A 1 586 ? -36.084 -67.113 112.220 1.00 120.36 ? 586 TYR A OH 1 ATOM 3928 N N . LEU A 1 587 ? -33.419 -59.163 114.426 1.00 178.80 ? 587 LEU A N 1 ATOM 3929 C CA . LEU A 1 587 ? -32.619 -57.950 114.666 1.00 185.12 ? 587 LEU A CA 1 ATOM 3930 C C . LEU A 1 587 ? -32.260 -57.859 116.147 1.00 187.27 ? 587 LEU A C 1 ATOM 3931 O O . LEU A 1 587 ? -31.102 -57.685 116.566 1.00 185.72 ? 587 LEU A O 1 ATOM 3932 C CB . LEU A 1 587 ? -33.433 -56.682 114.255 1.00 191.70 ? 587 LEU A CB 1 ATOM 3933 C CG . LEU A 1 587 ? -34.550 -55.938 115.066 1.00 186.83 ? 587 LEU A CG 1 ATOM 3934 C CD1 . LEU A 1 587 ? -34.642 -54.461 114.682 1.00 171.59 ? 587 LEU A CD1 1 ATOM 3935 C CD2 . LEU A 1 587 ? -35.952 -56.559 115.032 1.00 177.27 ? 587 LEU A CD2 1 ATOM 3936 N N . THR A 1 588 ? -33.347 -57.870 116.889 1.00 185.28 ? 588 THR A N 1 ATOM 3937 C CA . THR A 1 588 ? -33.346 -57.617 118.307 1.00 183.93 ? 588 THR A CA 1 ATOM 3938 C C . THR A 1 588 ? -32.438 -58.628 119.031 1.00 190.02 ? 588 THR A C 1 ATOM 3939 O O . THR A 1 588 ? -31.575 -58.268 119.873 1.00 189.27 ? 588 THR A O 1 ATOM 3940 C CB . THR A 1 588 ? -34.811 -57.590 118.807 1.00 172.91 ? 588 THR A CB 1 ATOM 3941 O OG1 . THR A 1 588 ? -34.849 -57.923 120.197 1.00 175.30 ? 588 THR A OG1 1 ATOM 3942 C CG2 . THR A 1 588 ? -35.740 -58.541 117.968 1.00 153.57 ? 588 THR A CG2 1 ATOM 3943 N N . GLU A 1 589 ? -32.661 -59.884 118.657 1.00 189.39 ? 589 GLU A N 1 ATOM 3944 C CA . GLU A 1 589 ? -31.913 -61.011 119.241 1.00 193.99 ? 589 GLU A CA 1 ATOM 3945 C C . GLU A 1 589 ? -30.425 -60.838 118.963 1.00 191.01 ? 589 GLU A C 1 ATOM 3946 O O . GLU A 1 589 ? -29.598 -61.029 119.866 1.00 187.78 ? 589 GLU A O 1 ATOM 3947 C CB . GLU A 1 589 ? -32.448 -62.374 118.759 1.00 198.32 ? 589 GLU A CB 1 ATOM 3948 C CG . GLU A 1 589 ? -32.166 -63.537 119.714 1.00 209.40 ? 589 GLU A CG 1 ATOM 3949 C CD . GLU A 1 589 ? -32.014 -64.891 119.018 1.00 212.00 ? 589 GLU A CD 1 ATOM 3950 O OE1 . GLU A 1 589 ? -32.911 -65.290 118.245 1.00 196.61 ? 589 GLU A OE1 1 ATOM 3951 O OE2 . GLU A 1 589 ? -30.995 -65.579 119.257 1.00 226.69 ? 589 GLU A OE2 1 ATOM 3952 N N . ASN A 1 590 ? -30.123 -60.474 117.718 1.00 187.99 ? 590 ASN A N 1 ATOM 3953 C CA . ASN A 1 590 ? -28.746 -60.261 117.268 1.00 182.55 ? 590 ASN A CA 1 ATOM 3954 C C . ASN A 1 590 ? -28.076 -59.187 118.124 1.00 196.67 ? 590 ASN A C 1 ATOM 3955 O O . ASN A 1 590 ? -26.934 -59.361 118.587 1.00 206.38 ? 590 ASN A O 1 ATOM 3956 C CB . ASN A 1 590 ? -28.701 -59.855 115.784 1.00 169.50 ? 590 ASN A CB 1 ATOM 3957 C CG . ASN A 1 590 ? -28.922 -61.027 114.846 1.00 156.45 ? 590 ASN A CG 1 ATOM 3958 O OD1 . ASN A 1 590 ? -28.489 -62.140 115.134 1.00 152.51 ? 590 ASN A OD1 1 ATOM 3959 N ND2 . ASN A 1 590 ? -29.594 -60.781 113.713 1.00 142.47 ? 590 ASN A ND2 1 ATOM 3960 N N . ILE A 1 591 ? -28.821 -58.099 118.317 1.00 202.92 ? 591 ILE A N 1 ATOM 3961 C CA . ILE A 1 591 ? -28.349 -56.962 119.107 1.00 201.82 ? 591 ILE A CA 1 ATOM 3962 C C . ILE A 1 591 ? -28.012 -57.399 120.530 1.00 212.21 ? 591 ILE A C 1 ATOM 3963 O O . ILE A 1 591 ? -26.945 -57.036 121.057 1.00 217.10 ? 591 ILE A O 1 ATOM 3964 C CB . ILE A 1 591 ? -29.180 -55.658 119.044 1.00 189.72 ? 591 ILE A CB 1 ATOM 3965 C CG1 . ILE A 1 591 ? -28.511 -54.590 119.926 1.00 189.56 ? 591 ILE A CG1 1 ATOM 3966 C CG2 . ILE A 1 591 ? -30.624 -55.877 119.440 1.00 189.13 ? 591 ILE A CG2 1 ATOM 3967 C CD1 . ILE A 1 591 ? -29.441 -53.798 120.828 1.00 187.35 ? 591 ILE A CD1 1 ATOM 3968 N N . GLN A 1 592 ? -28.902 -58.149 121.178 1.00 212.03 ? 592 GLN A N 1 ATOM 3969 C CA . GLN A 1 592 ? -28.647 -58.580 122.553 1.00 218.04 ? 592 GLN A CA 1 ATOM 3970 C C . GLN A 1 592 ? -27.663 -59.747 122.625 1.00 218.27 ? 592 GLN A C 1 ATOM 3971 O O . GLN A 1 592 ? -27.815 -60.658 123.434 1.00 227.10 ? 592 GLN A O 1 ATOM 3972 C CB . GLN A 1 592 ? -29.953 -58.890 123.295 1.00 221.24 ? 592 GLN A CB 1 ATOM 3973 C CG . GLN A 1 592 ? -30.360 -57.801 124.282 1.00 236.37 ? 592 GLN A CG 1 ATOM 3974 C CD . GLN A 1 592 ? -30.961 -58.356 125.566 1.00 251.10 ? 592 GLN A CD 1 ATOM 3975 O OE1 . GLN A 1 592 ? -31.988 -59.035 125.540 1.00 255.84 ? 592 GLN A OE1 1 ATOM 3976 N NE2 . GLN A 1 592 ? -30.324 -58.062 126.703 1.00 264.43 ? 592 GLN A NE2 1 ATOM 3977 N N . ARG A 1 593 ? -26.638 -59.701 121.784 1.00 214.74 ? 593 ARG A N 1 ATOM 3978 C CA . ARG A 1 593 ? -25.731 -60.824 121.625 1.00 215.01 ? 593 ARG A CA 1 ATOM 3979 C C . ARG A 1 593 ? -24.474 -60.382 120.896 1.00 215.24 ? 593 ARG A C 1 ATOM 3980 O O . ARG A 1 593 ? -23.484 -61.105 120.894 1.00 229.83 ? 593 ARG A O 1 ATOM 3981 C CB . ARG A 1 593 ? -26.416 -61.940 120.826 1.00 217.87 ? 593 ARG A CB 1 ATOM 3982 C CG . ARG A 1 593 ? -25.881 -63.343 121.070 1.00 223.73 ? 593 ARG A CG 1 ATOM 3983 C CD . ARG A 1 593 ? -26.369 -64.307 119.990 1.00 232.33 ? 593 ARG A CD 1 ATOM 3984 N NE . ARG A 1 593 ? -25.406 -64.481 118.895 1.00 226.38 ? 593 ARG A NE 1 ATOM 3985 C CZ . ARG A 1 593 ? -25.642 -65.162 117.773 1.00 210.80 ? 593 ARG A CZ 1 ATOM 3986 N NH1 . ARG A 1 593 ? -26.821 -65.738 117.567 1.00 208.52 ? 593 ARG A NH1 1 ATOM 3987 N NH2 . ARG A 1 593 ? -24.692 -65.264 116.852 1.00 190.83 ? 593 ARG A NH2 1 ATOM 3988 N N . PHE A 1 594 ? -24.513 -59.198 120.284 1.00 208.21 ? 594 PHE A N 1 ATOM 3989 C CA . PHE A 1 594 ? -23.406 -58.716 119.451 1.00 206.16 ? 594 PHE A CA 1 ATOM 3990 C C . PHE A 1 594 ? -22.875 -57.331 119.829 1.00 206.83 ? 594 PHE A C 1 ATOM 3991 O O . PHE A 1 594 ? -22.133 -56.718 119.061 1.00 209.13 ? 594 PHE A O 1 ATOM 3992 C CB . PHE A 1 594 ? -23.842 -58.692 117.984 1.00 210.35 ? 594 PHE A CB 1 ATOM 3993 C CG . PHE A 1 594 ? -23.554 -59.960 117.234 1.00 215.09 ? 594 PHE A CG 1 ATOM 3994 C CD1 . PHE A 1 594 ? -24.338 -61.097 117.427 1.00 210.83 ? 594 PHE A CD1 1 ATOM 3995 C CD2 . PHE A 1 594 ? -22.505 -60.012 116.311 1.00 218.76 ? 594 PHE A CD2 1 ATOM 3996 C CE1 . PHE A 1 594 ? -24.071 -62.265 116.729 1.00 207.11 ? 594 PHE A CE1 1 ATOM 3997 C CE2 . PHE A 1 594 ? -22.232 -61.180 115.613 1.00 214.33 ? 594 PHE A CE2 1 ATOM 3998 C CZ . PHE A 1 594 ? -23.019 -62.308 115.822 1.00 210.56 ? 594 PHE A CZ 1 ATOM 3999 N N . LEU A 1 595 ? -23.224 -56.847 121.014 1.00 205.70 ? 595 LEU A N 1 ATOM 4000 C CA . LEU A 1 595 ? -23.066 -55.436 121.302 1.00 201.59 ? 595 LEU A CA 1 ATOM 4001 C C . LEU A 1 595 ? -22.746 -55.186 122.763 1.00 206.89 ? 595 LEU A C 1 ATOM 4002 O O . LEU A 1 595 ? -23.290 -55.868 123.631 1.00 203.98 ? 595 LEU A O 1 ATOM 4003 C CB . LEU A 1 595 ? -24.379 -54.739 120.953 1.00 200.21 ? 595 LEU A CB 1 ATOM 4004 C CG . LEU A 1 595 ? -24.411 -53.453 120.132 1.00 196.49 ? 595 LEU A CG 1 ATOM 4005 C CD1 . LEU A 1 595 ? -23.673 -52.316 120.839 1.00 200.82 ? 595 LEU A CD1 1 ATOM 4006 C CD2 . LEU A 1 595 ? -23.900 -53.703 118.718 1.00 188.26 ? 595 LEU A CD2 1 ATOM 4007 N N . PRO A 1 596 ? -21.868 -54.201 123.041 1.00 217.81 ? 596 PRO A N 1 ATOM 4008 C CA . PRO A 1 596 ? -21.592 -53.772 124.417 1.00 232.61 ? 596 PRO A CA 1 ATOM 4009 C C . PRO A 1 596 ? -22.879 -53.721 125.231 1.00 236.07 ? 596 PRO A C 1 ATOM 4010 O O . PRO A 1 596 ? -23.780 -52.944 124.891 1.00 227.85 ? 596 PRO A O 1 ATOM 4011 C CB . PRO A 1 596 ? -21.014 -52.369 124.229 1.00 236.68 ? 596 PRO A CB 1 ATOM 4012 C CG . PRO A 1 596 ? -20.340 -52.428 122.894 1.00 231.18 ? 596 PRO A CG 1 ATOM 4013 C CD . PRO A 1 596 ? -20.984 -53.520 122.075 1.00 217.15 ? 596 PRO A CD 1 ATOM 4014 N N . ASN A 1 597 ? -22.951 -54.547 126.286 1.00 247.96 ? 597 ASN A N 1 ATOM 4015 C CA . ASN A 1 597 ? -24.224 -54.882 126.960 1.00 252.07 ? 597 ASN A CA 1 ATOM 4016 C C . ASN A 1 597 ? -25.368 -53.912 126.613 1.00 248.22 ? 597 ASN A C 1 ATOM 4017 O O . ASN A 1 597 ? -25.477 -52.818 127.169 1.00 261.32 ? 597 ASN A O 1 ATOM 4018 C CB . ASN A 1 597 ? -24.090 -55.233 128.475 1.00 259.55 ? 597 ASN A CB 1 ATOM 4019 C CG . ASN A 1 597 ? -23.180 -54.281 129.261 1.00 274.95 ? 597 ASN A CG 1 ATOM 4020 O OD1 . ASN A 1 597 ? -23.146 -53.076 129.014 1.00 290.71 ? 597 ASN A OD1 1 ATOM 4021 N ND2 . ASN A 1 597 ? -22.461 -54.828 130.247 1.00 269.99 ? 597 ASN A ND2 1 ATOM 4022 N N . PRO A 1 598 ? -26.206 -54.330 125.655 1.00 232.09 ? 598 PRO A N 1 ATOM 4023 C CA . PRO A 1 598 ? -27.092 -53.564 124.767 1.00 224.22 ? 598 PRO A CA 1 ATOM 4024 C C . PRO A 1 598 ? -28.096 -52.581 125.397 1.00 223.92 ? 598 PRO A C 1 ATOM 4025 O O . PRO A 1 598 ? -29.260 -52.549 124.976 1.00 218.45 ? 598 PRO A O 1 ATOM 4026 C CB . PRO A 1 598 ? -27.836 -54.668 124.003 1.00 221.59 ? 598 PRO A CB 1 ATOM 4027 C CG . PRO A 1 598 ? -26.913 -55.841 124.049 1.00 217.64 ? 598 PRO A CG 1 ATOM 4028 C CD . PRO A 1 598 ? -26.329 -55.780 125.419 1.00 224.97 ? 598 PRO A CD 1 ATOM 4029 N N . ALA A 1 599 ? -27.648 -51.767 126.356 1.00 227.46 ? 599 ALA A N 1 ATOM 4030 C CA . ALA A 1 599 ? -28.524 -50.777 126.996 1.00 232.50 ? 599 ALA A CA 1 ATOM 4031 C C . ALA A 1 599 ? -28.990 -49.710 125.987 1.00 234.12 ? 599 ALA A C 1 ATOM 4032 O O . ALA A 1 599 ? -30.095 -49.824 125.438 1.00 228.07 ? 599 ALA A O 1 ATOM 4033 C CB . ALA A 1 599 ? -27.866 -50.153 128.233 1.00 230.93 ? 599 ALA A CB 1 ATOM 4034 N N . GLY A 1 600 ? -28.140 -48.710 125.727 1.00 241.66 ? 600 GLY A N 1 ATOM 4035 C CA . GLY A 1 600 ? -28.436 -47.593 124.813 1.00 237.46 ? 600 GLY A CA 1 ATOM 4036 C C . GLY A 1 600 ? -28.758 -48.050 123.404 1.00 231.34 ? 600 GLY A C 1 ATOM 4037 O O . GLY A 1 600 ? -27.910 -47.994 122.508 1.00 218.84 ? 600 GLY A O 1 ATOM 4038 N N . VAL A 1 601 ? -30.005 -48.486 123.228 1.00 237.50 ? 601 VAL A N 1 ATOM 4039 C CA . VAL A 1 601 ? -30.491 -49.146 122.008 1.00 232.82 ? 601 VAL A CA 1 ATOM 4040 C C . VAL A 1 601 ? -30.594 -48.196 120.775 1.00 225.20 ? 601 VAL A C 1 ATOM 4041 O O . VAL A 1 601 ? -29.621 -48.048 120.029 1.00 214.58 ? 601 VAL A O 1 ATOM 4042 C CB . VAL A 1 601 ? -31.778 -50.017 122.283 1.00 235.59 ? 601 VAL A CB 1 ATOM 4043 C CG1 . VAL A 1 601 ? -31.408 -51.423 122.739 1.00 227.62 ? 601 VAL A CG1 1 ATOM 4044 C CG2 . VAL A 1 601 ? -32.702 -49.391 123.330 1.00 234.20 ? 601 VAL A CG2 1 ATOM 4045 N N . GLN A 1 602 ? -31.743 -47.539 120.590 1.00 227.29 ? 602 GLN A N 1 ATOM 4046 C CA . GLN A 1 602 ? -32.039 -46.687 119.413 1.00 227.00 ? 602 GLN A CA 1 ATOM 4047 C C . GLN A 1 602 ? -31.988 -47.408 118.060 1.00 222.17 ? 602 GLN A C 1 ATOM 4048 O O . GLN A 1 602 ? -30.945 -47.409 117.395 1.00 206.93 ? 602 GLN A O 1 ATOM 4049 C CB . GLN A 1 602 ? -31.163 -45.427 119.356 1.00 230.58 ? 602 GLN A CB 1 ATOM 4050 C CG . GLN A 1 602 ? -31.352 -44.465 120.512 1.00 242.18 ? 602 GLN A CG 1 ATOM 4051 C CD . GLN A 1 602 ? -30.189 -44.517 121.480 1.00 258.14 ? 602 GLN A CD 1 ATOM 4052 O OE1 . GLN A 1 602 ? -29.051 -44.243 121.105 1.00 265.46 ? 602 GLN A OE1 1 ATOM 4053 N NE2 . GLN A 1 602 ? -30.466 -44.866 122.732 1.00 267.57 ? 602 GLN A NE2 1 ATOM 4054 N N . LEU A 1 603 ? -33.123 -48.007 117.674 1.00 233.22 ? 603 LEU A N 1 ATOM 4055 C CA . LEU A 1 603 ? -33.344 -48.588 116.333 1.00 244.46 ? 603 LEU A CA 1 ATOM 4056 C C . LEU A 1 603 ? -33.136 -47.495 115.314 1.00 252.16 ? 603 LEU A C 1 ATOM 4057 O O . LEU A 1 603 ? -32.299 -47.626 114.419 1.00 262.68 ? 603 LEU A O 1 ATOM 4058 C CB . LEU A 1 603 ? -34.775 -49.159 116.190 1.00 249.24 ? 603 LEU A CB 1 ATOM 4059 C CG . LEU A 1 603 ? -35.480 -49.698 114.905 1.00 246.40 ? 603 LEU A CG 1 ATOM 4060 C CD1 . LEU A 1 603 ? -35.777 -48.651 113.822 1.00 232.18 ? 603 LEU A CD1 1 ATOM 4061 C CD2 . LEU A 1 603 ? -34.822 -50.947 114.306 1.00 233.04 ? 603 LEU A CD2 1 ATOM 4062 N N . GLU A 1 604 ? -33.923 -46.428 115.454 1.00 253.20 ? 604 GLU A N 1 ATOM 4063 C CA . GLU A 1 604 ? -33.720 -45.220 114.676 1.00 249.31 ? 604 GLU A CA 1 ATOM 4064 C C . GLU A 1 604 ? -32.384 -44.616 115.107 1.00 234.89 ? 604 GLU A C 1 ATOM 4065 O O . GLU A 1 604 ? -32.077 -44.537 116.302 1.00 233.85 ? 604 GLU A O 1 ATOM 4066 C CB . GLU A 1 604 ? -34.900 -44.237 114.823 1.00 261.56 ? 604 GLU A CB 1 ATOM 4067 C CG . GLU A 1 604 ? -34.973 -43.444 116.129 1.00 287.25 ? 604 GLU A CG 1 ATOM 4068 C CD . GLU A 1 604 ? -35.347 -44.287 117.339 1.00 296.58 ? 604 GLU A CD 1 ATOM 4069 O OE1 . GLU A 1 604 ? -36.098 -45.271 117.171 1.00 300.74 ? 604 GLU A OE1 1 ATOM 4070 O OE2 . GLU A 1 604 ? -34.894 -43.960 118.462 1.00 298.12 ? 604 GLU A OE2 1 ATOM 4071 N N . ASP A 1 605 ? -31.573 -44.276 114.111 1.00 217.68 ? 605 ASP A N 1 ATOM 4072 C CA . ASP A 1 605 ? -30.275 -43.644 114.297 1.00 212.16 ? 605 ASP A CA 1 ATOM 4073 C C . ASP A 1 605 ? -29.660 -43.464 112.930 1.00 204.30 ? 605 ASP A C 1 ATOM 4074 O O . ASP A 1 605 ? -29.369 -44.461 112.245 1.00 173.44 ? 605 ASP A O 1 ATOM 4075 C CB . ASP A 1 605 ? -29.322 -44.468 115.177 1.00 216.85 ? 605 ASP A CB 1 ATOM 4076 C CG . ASP A 1 605 ? -27.941 -43.822 115.308 1.00 219.56 ? 605 ASP A CG 1 ATOM 4077 O OD1 . ASP A 1 605 ? -27.808 -42.815 116.033 1.00 223.89 ? 605 ASP A OD1 1 ATOM 4078 O OD2 . ASP A 1 605 ? -26.983 -44.311 114.677 1.00 215.09 ? 605 ASP A OD2 1 ATOM 4079 N N . PRO A 1 606 ? -29.464 -42.188 112.529 1.00 223.74 ? 606 PRO A N 1 ATOM 4080 C CA . PRO A 1 606 ? -28.788 -41.862 111.281 1.00 230.88 ? 606 PRO A CA 1 ATOM 4081 C C . PRO A 1 606 ? -27.764 -42.949 110.839 1.00 225.08 ? 606 PRO A C 1 ATOM 4082 O O . PRO A 1 606 ? -28.153 -43.910 110.161 1.00 212.79 ? 606 PRO A O 1 ATOM 4083 C CB . PRO A 1 606 ? -28.137 -40.494 111.596 1.00 241.94 ? 606 PRO A CB 1 ATOM 4084 C CG . PRO A 1 606 ? -28.991 -39.880 112.683 1.00 231.32 ? 606 PRO A CG 1 ATOM 4085 C CD . PRO A 1 606 ? -29.887 -40.961 113.247 1.00 229.56 ? 606 PRO A CD 1 ATOM 4086 N N . GLU A 1 607 ? -26.500 -42.821 111.252 1.00 232.76 ? 607 GLU A N 1 ATOM 4087 C CA . GLU A 1 607 ? -25.413 -43.690 110.776 1.00 223.74 ? 607 GLU A CA 1 ATOM 4088 C C . GLU A 1 607 ? -25.572 -45.179 111.137 1.00 217.76 ? 607 GLU A C 1 ATOM 4089 O O . GLU A 1 607 ? -25.472 -46.030 110.249 1.00 227.32 ? 607 GLU A O 1 ATOM 4090 C CB . GLU A 1 607 ? -24.016 -43.131 111.157 1.00 225.61 ? 607 GLU A CB 1 ATOM 4091 C CG . GLU A 1 607 ? -23.382 -43.657 112.452 1.00 239.48 ? 607 GLU A CG 1 ATOM 4092 C CD . GLU A 1 607 ? -23.785 -42.899 113.722 1.00 249.79 ? 607 GLU A CD 1 ATOM 4093 O OE1 . GLU A 1 607 ? -23.849 -41.651 113.695 1.00 258.01 ? 607 GLU A OE1 1 ATOM 4094 O OE2 . GLU A 1 607 ? -24.013 -43.548 114.771 1.00 246.17 ? 607 GLU A OE2 1 ATOM 4095 N N . PHE A 1 608 ? -25.839 -45.496 112.406 1.00 203.67 ? 608 PHE A N 1 ATOM 4096 C CA . PHE A 1 608 ? -25.890 -46.896 112.841 1.00 194.62 ? 608 PHE A CA 1 ATOM 4097 C C . PHE A 1 608 ? -26.723 -47.719 111.889 1.00 188.12 ? 608 PHE A C 1 ATOM 4098 O O . PHE A 1 608 ? -26.279 -48.773 111.436 1.00 183.59 ? 608 PHE A O 1 ATOM 4099 C CB . PHE A 1 608 ? -26.441 -47.035 114.264 1.00 204.71 ? 608 PHE A CB 1 ATOM 4100 C CG . PHE A 1 608 ? -27.108 -48.373 114.554 1.00 199.50 ? 608 PHE A CG 1 ATOM 4101 C CD1 . PHE A 1 608 ? -26.351 -49.481 114.946 1.00 190.82 ? 608 PHE A CD1 1 ATOM 4102 C CD2 . PHE A 1 608 ? -28.503 -48.516 114.466 1.00 188.67 ? 608 PHE A CD2 1 ATOM 4103 C CE1 . PHE A 1 608 ? -26.962 -50.693 115.225 1.00 169.73 ? 608 PHE A CE1 1 ATOM 4104 C CE2 . PHE A 1 608 ? -29.114 -49.725 114.744 1.00 165.85 ? 608 PHE A CE2 1 ATOM 4105 C CZ . PHE A 1 608 ? -28.338 -50.809 115.124 1.00 162.73 ? 608 PHE A CZ 1 ATOM 4106 N N . GLN A 1 609 ? -27.922 -47.228 111.585 1.00 184.20 ? 609 GLN A N 1 ATOM 4107 C CA . GLN A 1 609 ? -28.859 -47.974 110.760 1.00 185.47 ? 609 GLN A CA 1 ATOM 4108 C C . GLN A 1 609 ? -28.224 -48.585 109.489 1.00 185.59 ? 609 GLN A C 1 ATOM 4109 O O . GLN A 1 609 ? -28.543 -49.719 109.108 1.00 173.14 ? 609 GLN A O 1 ATOM 4110 C CB . GLN A 1 609 ? -30.091 -47.129 110.454 1.00 187.16 ? 609 GLN A CB 1 ATOM 4111 C CG . GLN A 1 609 ? -31.073 -47.096 111.612 1.00 195.30 ? 609 GLN A CG 1 ATOM 4112 C CD . GLN A 1 609 ? -32.521 -46.984 111.163 1.00 210.97 ? 609 GLN A CD 1 ATOM 4113 O OE1 . GLN A 1 609 ? -32.887 -46.064 110.428 1.00 224.07 ? 609 GLN A OE1 1 ATOM 4114 N NE2 . GLN A 1 609 ? -33.360 -47.919 111.611 1.00 205.94 ? 609 GLN A NE2 1 ATOM 4115 N N . ALA A 1 610 ? -27.304 -47.842 108.872 1.00 189.17 ? 610 ALA A N 1 ATOM 4116 C CA . ALA A 1 610 ? -26.514 -48.338 107.745 1.00 186.37 ? 610 ALA A CA 1 ATOM 4117 C C . ALA A 1 610 ? -25.799 -49.679 108.031 1.00 191.39 ? 610 ALA A C 1 ATOM 4118 O O . ALA A 1 610 ? -25.832 -50.580 107.185 1.00 191.02 ? 610 ALA A O 1 ATOM 4119 C CB . ALA A 1 610 ? -25.530 -47.273 107.270 1.00 179.62 ? 610 ALA A CB 1 ATOM 4120 N N . SER A 1 611 ? -25.195 -49.811 109.224 1.00 196.86 ? 611 SER A N 1 ATOM 4121 C CA . SER A 1 611 ? -24.383 -50.997 109.642 1.00 198.51 ? 611 SER A CA 1 ATOM 4122 C C . SER A 1 611 ? -25.030 -52.363 109.398 1.00 194.71 ? 611 SER A C 1 ATOM 4123 O O . SER A 1 611 ? -24.360 -53.410 109.438 1.00 186.94 ? 611 SER A O 1 ATOM 4124 C CB . SER A 1 611 ? -23.987 -50.894 111.136 1.00 198.03 ? 611 SER A CB 1 ATOM 4125 O OG . SER A 1 611 ? -23.455 -52.118 111.650 1.00 186.21 ? 611 SER A OG 1 ATOM 4126 N N . ASN A 1 612 ? -26.332 -52.325 109.147 1.00 186.88 ? 612 ASN A N 1 ATOM 4127 C CA . ASN A 1 612 ? -27.179 -53.492 109.218 1.00 183.89 ? 612 ASN A CA 1 ATOM 4128 C C . ASN A 1 612 ? -27.920 -53.653 107.910 1.00 180.05 ? 612 ASN A C 1 ATOM 4129 O O . ASN A 1 612 ? -28.789 -54.510 107.759 1.00 189.38 ? 612 ASN A O 1 ATOM 4130 C CB . ASN A 1 612 ? -28.155 -53.314 110.379 1.00 182.40 ? 612 ASN A CB 1 ATOM 4131 C CG . ASN A 1 612 ? -27.560 -52.493 111.510 1.00 184.48 ? 612 ASN A CG 1 ATOM 4132 O OD1 . ASN A 1 612 ? -26.684 -52.958 112.241 1.00 183.60 ? 612 ASN A OD1 1 ATOM 4133 N ND2 . ASN A 1 612 ? -28.015 -51.254 111.640 1.00 186.01 ? 612 ASN A ND2 1 ATOM 4134 N N . ILE A 1 613 ? -27.569 -52.811 106.955 1.00 172.04 ? 613 ILE A N 1 ATOM 4135 C CA . ILE A 1 613 ? -28.145 -52.921 105.641 1.00 159.61 ? 613 ILE A CA 1 ATOM 4136 C C . ILE A 1 613 ? -27.083 -53.508 104.744 1.00 157.37 ? 613 ILE A C 1 ATOM 4137 O O . ILE A 1 613 ? -26.197 -52.807 104.240 1.00 160.88 ? 613 ILE A O 1 ATOM 4138 C CB . ILE A 1 613 ? -28.618 -51.569 105.134 1.00 157.14 ? 613 ILE A CB 1 ATOM 4139 C CG1 . ILE A 1 613 ? -29.533 -50.933 106.187 1.00 161.62 ? 613 ILE A CG1 1 ATOM 4140 C CG2 . ILE A 1 613 ? -29.309 -51.751 103.795 1.00 146.18 ? 613 ILE A CG2 1 ATOM 4141 C CD1 . ILE A 1 613 ? -29.418 -49.426 106.277 1.00 174.61 ? 613 ILE A CD1 1 ATOM 4142 N N . MET A 1 614 ? -27.170 -54.816 104.576 1.00 148.70 ? 614 MET A N 1 ATOM 4143 C CA . MET A 1 614 ? -26.158 -55.541 103.850 1.00 153.85 ? 614 MET A CA 1 ATOM 4144 C C . MET A 1 614 ? -26.514 -55.615 102.382 1.00 163.87 ? 614 MET A C 1 ATOM 4145 O O . MET A 1 614 ? -27.544 -56.194 102.010 1.00 170.02 ? 614 MET A O 1 ATOM 4146 C CB . MET A 1 614 ? -25.994 -56.932 104.436 1.00 149.30 ? 614 MET A CB 1 ATOM 4147 C CG . MET A 1 614 ? -25.499 -56.914 105.864 1.00 154.89 ? 614 MET A CG 1 ATOM 4148 S SD . MET A 1 614 ? -23.976 -55.977 106.018 1.00 163.23 ? 614 MET A SD 1 ATOM 4149 C CE . MET A 1 614 ? -23.864 -55.730 107.793 1.00 161.08 ? 614 MET A CE 1 ATOM 4150 N N . HIS A 1 615 ? -25.655 -55.016 101.559 1.00 163.54 ? 615 HIS A N 1 ATOM 4151 C CA . HIS A 1 615 ? -25.835 -54.994 100.113 1.00 153.71 ? 615 HIS A CA 1 ATOM 4152 C C . HIS A 1 615 ? -25.051 -56.181 99.571 1.00 145.00 ? 615 HIS A C 1 ATOM 4153 O O . HIS A 1 615 ? -23.842 -56.259 99.780 1.00 147.16 ? 615 HIS A O 1 ATOM 4154 C CB . HIS A 1 615 ? -25.335 -53.657 99.556 1.00 157.55 ? 615 HIS A CB 1 ATOM 4155 C CG . HIS A 1 615 ? -26.009 -52.456 100.161 1.00 166.67 ? 615 HIS A CG 1 ATOM 4156 N ND1 . HIS A 1 615 ? -25.819 -52.071 101.473 1.00 169.47 ? 615 HIS A ND1 1 ATOM 4157 C CD2 . HIS A 1 615 ? -26.866 -51.550 99.628 1.00 169.26 ? 615 HIS A CD2 1 ATOM 4158 C CE1 . HIS A 1 615 ? -26.535 -50.988 101.721 1.00 171.61 ? 615 HIS A CE1 1 ATOM 4159 N NE2 . HIS A 1 615 ? -27.179 -50.650 100.618 1.00 168.88 ? 615 HIS A NE2 1 ATOM 4160 N N . SER A 1 616 ? -25.733 -57.125 98.921 1.00 137.22 ? 616 SER A N 1 ATOM 4161 C CA . SER A 1 616 ? -25.136 -58.457 98.690 1.00 137.90 ? 616 SER A CA 1 ATOM 4162 C C . SER A 1 616 ? -25.489 -59.157 97.382 1.00 147.06 ? 616 SER A C 1 ATOM 4163 O O . SER A 1 616 ? -26.638 -59.110 96.929 1.00 168.88 ? 616 SER A O 1 ATOM 4164 C CB . SER A 1 616 ? -25.511 -59.418 99.824 1.00 127.81 ? 616 SER A CB 1 ATOM 4165 O OG . SER A 1 616 ? -26.719 -60.121 99.541 1.00 112.30 ? 616 SER A OG 1 ATOM 4166 N N . ILE A 1 617 ? -24.489 -59.821 96.798 1.00 142.58 ? 617 ILE A N 1 ATOM 4167 C CA . ILE A 1 617 ? -24.722 -60.832 95.766 1.00 128.97 ? 617 ILE A CA 1 ATOM 4168 C C . ILE A 1 617 ? -24.741 -62.159 96.521 1.00 126.92 ? 617 ILE A C 1 ATOM 4169 O O . ILE A 1 617 ? -23.773 -62.538 97.187 1.00 126.78 ? 617 ILE A O 1 ATOM 4170 C CB . ILE A 1 617 ? -23.656 -60.883 94.614 1.00 124.40 ? 617 ILE A CB 1 ATOM 4171 C CG1 . ILE A 1 617 ? -22.735 -59.658 94.575 1.00 125.85 ? 617 ILE A CG1 1 ATOM 4172 C CG2 . ILE A 1 617 ? -24.313 -61.087 93.251 1.00 115.39 ? 617 ILE A CG2 1 ATOM 4173 C CD1 . ILE A 1 617 ? -23.270 -58.474 93.799 1.00 125.92 ? 617 ILE A CD1 1 ATOM 4174 N N . ASN A 1 618 ? -25.874 -62.840 96.447 1.00 127.52 ? 618 ASN A N 1 ATOM 4175 C CA . ASN A 1 618 ? -26.023 -64.150 97.056 1.00 127.36 ? 618 ASN A CA 1 ATOM 4176 C C . ASN A 1 618 ? -25.741 -64.164 98.556 1.00 125.49 ? 618 ASN A C 1 ATOM 4177 O O . ASN A 1 618 ? -25.167 -65.106 99.084 1.00 124.72 ? 618 ASN A O 1 ATOM 4178 C CB . ASN A 1 618 ? -25.175 -65.172 96.297 1.00 124.34 ? 618 ASN A CB 1 ATOM 4179 C CG . ASN A 1 618 ? -25.839 -65.629 95.012 1.00 121.28 ? 618 ASN A CG 1 ATOM 4180 O OD1 . ASN A 1 618 ? -26.700 -64.946 94.448 1.00 106.47 ? 618 ASN A OD1 1 ATOM 4181 N ND2 . ASN A 1 618 ? -25.460 -66.809 94.557 1.00 132.52 ? 618 ASN A ND2 1 ATOM 4182 N N . GLY A 1 619 ? -26.164 -63.105 99.234 1.00 127.79 ? 619 GLY A N 1 ATOM 4183 C CA . GLY A 1 619 ? -25.940 -62.979 100.657 1.00 133.99 ? 619 GLY A CA 1 ATOM 4184 C C . GLY A 1 619 ? -24.486 -62.740 101.027 1.00 143.21 ? 619 GLY A C 1 ATOM 4185 O O . GLY A 1 619 ? -24.165 -62.710 102.218 1.00 149.63 ? 619 GLY A O 1 ATOM 4186 N N . TYR A 1 620 ? -23.612 -62.580 100.025 1.00 139.73 ? 620 TYR A N 1 ATOM 4187 C CA . TYR A 1 620 ? -22.198 -62.228 100.254 1.00 138.41 ? 620 TYR A CA 1 ATOM 4188 C C . TYR A 1 620 ? -21.938 -60.777 99.944 1.00 138.01 ? 620 TYR A C 1 ATOM 4189 O O . TYR A 1 620 ? -22.460 -60.239 98.975 1.00 135.06 ? 620 TYR A O 1 ATOM 4190 C CB . TYR A 1 620 ? -21.284 -63.037 99.367 1.00 140.27 ? 620 TYR A CB 1 ATOM 4191 C CG . TYR A 1 620 ? -21.098 -64.456 99.790 1.00 148.91 ? 620 TYR A CG 1 ATOM 4192 C CD1 . TYR A 1 620 ? -22.175 -65.324 99.881 1.00 148.19 ? 620 TYR A CD1 1 ATOM 4193 C CD2 . TYR A 1 620 ? -19.834 -64.945 100.080 1.00 164.35 ? 620 TYR A CD2 1 ATOM 4194 C CE1 . TYR A 1 620 ? -21.997 -66.638 100.265 1.00 154.67 ? 620 TYR A CE1 1 ATOM 4195 C CE2 . TYR A 1 620 ? -19.648 -66.265 100.446 1.00 169.28 ? 620 TYR A CE2 1 ATOM 4196 C CZ . TYR A 1 620 ? -20.734 -67.096 100.544 1.00 157.21 ? 620 TYR A CZ 1 ATOM 4197 O OH . TYR A 1 620 ? -20.556 -68.389 100.923 1.00 169.99 ? 620 TYR A OH 1 ATOM 4198 N N . VAL A 1 621 ? -21.124 -60.135 100.760 1.00 143.49 ? 621 VAL A N 1 ATOM 4199 C CA . VAL A 1 621 ? -20.832 -58.740 100.508 1.00 151.19 ? 621 VAL A CA 1 ATOM 4200 C C . VAL A 1 621 ? -19.362 -58.620 100.204 1.00 157.33 ? 621 VAL A C 1 ATOM 4201 O O . VAL A 1 621 ? -18.609 -59.598 100.341 1.00 151.38 ? 621 VAL A O 1 ATOM 4202 C CB . VAL A 1 621 ? -21.207 -57.790 101.686 1.00 152.80 ? 621 VAL A CB 1 ATOM 4203 C CG1 . VAL A 1 621 ? -22.713 -57.609 101.810 1.00 135.58 ? 621 VAL A CG1 1 ATOM 4204 C CG2 . VAL A 1 621 ? -20.586 -58.240 103.008 1.00 153.92 ? 621 VAL A CG2 1 ATOM 4205 N N . PHE A 1 622 ? -18.989 -57.417 99.770 1.00 156.43 ? 622 PHE A N 1 ATOM 4206 C CA . PHE A 1 622 ? -17.605 -56.992 99.682 1.00 161.48 ? 622 PHE A CA 1 ATOM 4207 C C . PHE A 1 622 ? -16.685 -58.017 99.064 1.00 168.90 ? 622 PHE A C 1 ATOM 4208 O O . PHE A 1 622 ? -15.985 -58.743 99.776 1.00 168.51 ? 622 PHE A O 1 ATOM 4209 C CB . PHE A 1 622 ? -17.082 -56.596 101.057 1.00 157.94 ? 622 PHE A CB 1 ATOM 4210 C CG . PHE A 1 622 ? -17.404 -55.194 101.424 1.00 157.42 ? 622 PHE A CG 1 ATOM 4211 C CD1 . PHE A 1 622 ? -16.633 -54.150 100.944 1.00 161.06 ? 622 PHE A CD1 1 ATOM 4212 C CD2 . PHE A 1 622 ? -18.490 -54.912 102.229 1.00 157.07 ? 622 PHE A CD2 1 ATOM 4213 C CE1 . PHE A 1 622 ? -16.940 -52.846 101.264 1.00 160.96 ? 622 PHE A CE1 1 ATOM 4214 C CE2 . PHE A 1 622 ? -18.798 -53.610 102.565 1.00 159.01 ? 622 PHE A CE2 1 ATOM 4215 C CZ . PHE A 1 622 ? -18.025 -52.576 102.078 1.00 161.14 ? 622 PHE A CZ 1 ATOM 4216 N N . ASP A 1 623 ? -16.707 -58.073 97.735 1.00 175.50 ? 623 ASP A N 1 ATOM 4217 C CA . ASP A 1 623 ? -15.797 -58.914 96.980 1.00 177.04 ? 623 ASP A CA 1 ATOM 4218 C C . ASP A 1 623 ? -15.468 -60.193 97.770 1.00 174.69 ? 623 ASP A C 1 ATOM 4219 O O . ASP A 1 623 ? -14.339 -60.664 97.788 1.00 188.38 ? 623 ASP A O 1 ATOM 4220 C CB . ASP A 1 623 ? -14.541 -58.104 96.588 1.00 197.80 ? 623 ASP A CB 1 ATOM 4221 C CG . ASP A 1 623 ? -14.752 -57.233 95.328 1.00 216.13 ? 623 ASP A CG 1 ATOM 4222 O OD1 . ASP A 1 623 ? -15.547 -57.642 94.458 1.00 228.14 ? 623 ASP A OD1 1 ATOM 4223 O OD2 . ASP A 1 623 ? -14.116 -56.153 95.189 1.00 227.24 ? 623 ASP A OD2 1 ATOM 4224 N N . SER A 1 624 ? -16.465 -60.720 98.468 1.00 163.87 ? 624 SER A N 1 ATOM 4225 C CA . SER A 1 624 ? -16.356 -62.024 99.066 1.00 158.91 ? 624 SER A CA 1 ATOM 4226 C C . SER A 1 624 ? -17.449 -62.795 98.402 1.00 159.61 ? 624 SER A C 1 ATOM 4227 O O . SER A 1 624 ? -18.527 -62.241 98.164 1.00 161.02 ? 624 SER A O 1 ATOM 4228 C CB . SER A 1 624 ? -16.591 -61.975 100.555 1.00 164.58 ? 624 SER A CB 1 ATOM 4229 O OG . SER A 1 624 ? -16.101 -63.163 101.131 1.00 173.98 ? 624 SER A OG 1 ATOM 4230 N N . LEU A 1 625 ? -17.172 -64.075 98.149 1.00 161.49 ? 625 LEU A N 1 ATOM 4231 C CA . LEU A 1 625 ? -17.798 -64.885 97.084 1.00 158.12 ? 625 LEU A CA 1 ATOM 4232 C C . LEU A 1 625 ? -17.051 -64.644 95.787 1.00 166.27 ? 625 LEU A C 1 ATOM 4233 O O . LEU A 1 625 ? -17.044 -63.538 95.237 1.00 170.24 ? 625 LEU A O 1 ATOM 4234 C CB . LEU A 1 625 ? -19.308 -64.627 96.889 1.00 147.95 ? 625 LEU A CB 1 ATOM 4235 C CG . LEU A 1 625 ? -19.997 -64.538 95.508 1.00 127.00 ? 625 LEU A CG 1 ATOM 4236 C CD1 . LEU A 1 625 ? -19.717 -65.751 94.636 1.00 125.68 ? 625 LEU A CD1 1 ATOM 4237 C CD2 . LEU A 1 625 ? -21.502 -64.316 95.634 1.00 113.54 ? 625 LEU A CD2 1 ATOM 4238 N N . GLN A 1 626 ? -16.402 -65.695 95.321 1.00 170.34 ? 626 GLN A N 1 ATOM 4239 C CA . GLN A 1 626 ? -15.825 -65.707 94.003 1.00 168.54 ? 626 GLN A CA 1 ATOM 4240 C C . GLN A 1 626 ? -16.424 -66.922 93.331 1.00 162.95 ? 626 GLN A C 1 ATOM 4241 O O . GLN A 1 626 ? -16.890 -67.844 93.999 1.00 166.00 ? 626 GLN A O 1 ATOM 4242 C CB . GLN A 1 626 ? -14.303 -65.852 94.068 1.00 181.67 ? 626 GLN A CB 1 ATOM 4243 C CG . GLN A 1 626 ? -13.545 -64.661 94.622 1.00 189.15 ? 626 GLN A CG 1 ATOM 4244 C CD . GLN A 1 626 ? -12.109 -65.018 94.973 1.00 219.30 ? 626 GLN A CD 1 ATOM 4245 O OE1 . GLN A 1 626 ? -11.211 -64.948 94.126 1.00 230.62 ? 626 GLN A OE1 1 ATOM 4246 N NE2 . GLN A 1 626 ? -11.882 -65.400 96.234 1.00 227.35 ? 626 GLN A NE2 1 ATOM 4247 N N . LEU A 1 627 ? -16.409 -66.918 92.007 1.00 155.46 ? 627 LEU A N 1 ATOM 4248 C CA . LEU A 1 627 ? -16.850 -68.054 91.235 1.00 149.66 ? 627 LEU A CA 1 ATOM 4249 C C . LEU A 1 627 ? -15.720 -68.497 90.321 1.00 157.75 ? 627 LEU A C 1 ATOM 4250 O O . LEU A 1 627 ? -15.071 -67.673 89.660 1.00 151.09 ? 627 LEU A O 1 ATOM 4251 C CB . LEU A 1 627 ? -18.047 -67.646 90.397 1.00 141.60 ? 627 LEU A CB 1 ATOM 4252 C CG . LEU A 1 627 ? -19.056 -66.710 91.059 1.00 137.10 ? 627 LEU A CG 1 ATOM 4253 C CD1 . LEU A 1 627 ? -19.350 -65.532 90.138 1.00 134.95 ? 627 LEU A CD1 1 ATOM 4254 C CD2 . LEU A 1 627 ? -20.331 -67.468 91.406 1.00 132.95 ? 627 LEU A CD2 1 ATOM 4255 N N . SER A 1 628 ? -15.462 -69.797 90.292 1.00 167.78 ? 628 SER A N 1 ATOM 4256 C CA . SER A 1 628 ? -14.601 -70.324 89.243 1.00 182.05 ? 628 SER A CA 1 ATOM 4257 C C . SER A 1 628 ? -15.451 -70.825 88.067 1.00 177.57 ? 628 SER A C 1 ATOM 4258 O O . SER A 1 628 ? -16.555 -71.376 88.263 1.00 173.12 ? 628 SER A O 1 ATOM 4259 C CB . SER A 1 628 ? -13.641 -71.410 89.766 1.00 193.77 ? 628 SER A CB 1 ATOM 4260 O OG . SER A 1 628 ? -12.273 -71.033 89.614 1.00 185.60 ? 628 SER A OG 1 ATOM 4261 N N . VAL A 1 629 ? -14.942 -70.577 86.854 1.00 157.11 ? 629 VAL A N 1 ATOM 4262 C CA . VAL A 1 629 ? -15.402 -71.251 85.635 1.00 146.22 ? 629 VAL A CA 1 ATOM 4263 C C . VAL A 1 629 ? -14.253 -71.564 84.699 1.00 149.79 ? 629 VAL A C 1 ATOM 4264 O O . VAL A 1 629 ? -13.243 -70.853 84.679 1.00 148.57 ? 629 VAL A O 1 ATOM 4265 C CB . VAL A 1 629 ? -16.376 -70.412 84.805 1.00 139.88 ? 629 VAL A CB 1 ATOM 4266 C CG1 . VAL A 1 629 ? -17.822 -70.884 85.006 1.00 132.55 ? 629 VAL A CG1 1 ATOM 4267 C CG2 . VAL A 1 629 ? -16.130 -68.928 85.045 1.00 136.60 ? 629 VAL A CG2 1 ATOM 4268 N N . CYS A 1 630 ? -14.439 -72.626 83.915 1.00 153.13 ? 630 CYS A N 1 ATOM 4269 C CA . CYS A 1 630 ? -13.497 -73.031 82.884 1.00 163.66 ? 630 CYS A CA 1 ATOM 4270 C C . CYS A 1 630 ? -13.614 -72.129 81.664 1.00 146.74 ? 630 CYS A C 1 ATOM 4271 O O . CYS A 1 630 ? -14.683 -72.030 81.079 1.00 148.56 ? 630 CYS A O 1 ATOM 4272 C CB . CYS A 1 630 ? -13.776 -74.480 82.464 1.00 198.54 ? 630 CYS A CB 1 ATOM 4273 S SG . CYS A 1 630 ? -13.556 -75.756 83.736 1.00 254.16 ? 630 CYS A SG 1 ATOM 4274 N N . LEU A 1 631 ? -12.535 -71.469 81.264 1.00 140.66 ? 631 LEU A N 1 ATOM 4275 C CA . LEU A 1 631 ? -12.621 -70.667 80.053 1.00 145.02 ? 631 LEU A CA 1 ATOM 4276 C C . LEU A 1 631 ? -12.958 -71.603 78.888 1.00 152.65 ? 631 LEU A C 1 ATOM 4277 O O . LEU A 1 631 ? -12.387 -72.699 78.757 1.00 149.23 ? 631 LEU A O 1 ATOM 4278 C CB . LEU A 1 631 ? -11.356 -69.844 79.806 1.00 142.04 ? 631 LEU A CB 1 ATOM 4279 C CG . LEU A 1 631 ? -10.210 -70.590 79.141 1.00 149.47 ? 631 LEU A CG 1 ATOM 4280 C CD1 . LEU A 1 631 ? -9.935 -70.037 77.750 1.00 150.13 ? 631 LEU A CD1 1 ATOM 4281 C CD2 . LEU A 1 631 ? -8.981 -70.499 80.023 1.00 155.73 ? 631 LEU A CD2 1 ATOM 4282 N N . HIS A 1 632 ? -13.918 -71.152 78.081 1.00 159.90 ? 632 HIS A N 1 ATOM 4283 C CA . HIS A 1 632 ? -14.578 -71.934 77.029 1.00 163.00 ? 632 HIS A CA 1 ATOM 4284 C C . HIS A 1 632 ? -15.881 -72.599 77.494 1.00 161.79 ? 632 HIS A C 1 ATOM 4285 O O . HIS A 1 632 ? -16.840 -72.671 76.725 1.00 160.18 ? 632 HIS A O 1 ATOM 4286 C CB . HIS A 1 632 ? -13.639 -72.943 76.365 1.00 172.51 ? 632 HIS A CB 1 ATOM 4287 C CG . HIS A 1 632 ? -12.504 -72.315 75.621 1.00 176.23 ? 632 HIS A CG 1 ATOM 4288 N ND1 . HIS A 1 632 ? -12.673 -71.230 74.785 1.00 172.30 ? 632 HIS A ND1 1 ATOM 4289 C CD2 . HIS A 1 632 ? -11.189 -72.637 75.569 1.00 180.71 ? 632 HIS A CD2 1 ATOM 4290 C CE1 . HIS A 1 632 ? -11.504 -70.898 74.267 1.00 197.81 ? 632 HIS A CE1 1 ATOM 4291 N NE2 . HIS A 1 632 ? -10.589 -71.737 74.725 1.00 203.97 ? 632 HIS A NE2 1 ATOM 4292 N N . GLU A 1 633 ? -15.924 -73.088 78.735 1.00 169.97 ? 633 GLU A N 1 ATOM 4293 C CA . GLU A 1 633 ? -17.178 -73.625 79.278 1.00 177.76 ? 633 GLU A CA 1 ATOM 4294 C C . GLU A 1 633 ? -18.220 -72.529 79.252 1.00 164.36 ? 633 GLU A C 1 ATOM 4295 O O . GLU A 1 633 ? -18.025 -71.423 79.780 1.00 159.38 ? 633 GLU A O 1 ATOM 4296 C CB . GLU A 1 633 ? -17.037 -74.189 80.699 1.00 203.74 ? 633 GLU A CB 1 ATOM 4297 C CG . GLU A 1 633 ? -18.362 -74.576 81.357 1.00 224.60 ? 633 GLU A CG 1 ATOM 4298 C CD . GLU A 1 633 ? -18.463 -74.094 82.799 1.00 251.07 ? 633 GLU A CD 1 ATOM 4299 O OE1 . GLU A 1 633 ? -17.658 -74.559 83.636 1.00 265.50 ? 633 GLU A OE1 1 ATOM 4300 O OE2 . GLU A 1 633 ? -19.335 -73.240 83.099 1.00 246.31 ? 633 GLU A OE2 1 ATOM 4301 N N . VAL A 1 634 ? -19.330 -72.864 78.622 1.00 151.04 ? 634 VAL A N 1 ATOM 4302 C CA . VAL A 1 634 ? -20.378 -71.915 78.358 1.00 140.87 ? 634 VAL A CA 1 ATOM 4303 C C . VAL A 1 634 ? -21.548 -72.154 79.303 1.00 136.87 ? 634 VAL A C 1 ATOM 4304 O O . VAL A 1 634 ? -21.859 -73.315 79.593 1.00 135.39 ? 634 VAL A O 1 ATOM 4305 C CB . VAL A 1 634 ? -20.827 -72.056 76.913 1.00 138.57 ? 634 VAL A CB 1 ATOM 4306 C CG1 . VAL A 1 634 ? -21.092 -73.523 76.584 1.00 134.87 ? 634 VAL A CG1 1 ATOM 4307 C CG2 . VAL A 1 634 ? -22.031 -71.172 76.662 1.00 136.54 ? 634 VAL A CG2 1 ATOM 4308 N N . ALA A 1 635 ? -22.196 -71.057 79.738 1.00 134.03 ? 635 ALA A N 1 ATOM 4309 C CA . ALA A 1 635 ? -23.116 -71.033 80.904 1.00 126.57 ? 635 ALA A CA 1 ATOM 4310 C C . ALA A 1 635 ? -24.447 -70.259 80.707 1.00 119.49 ? 635 ALA A C 1 ATOM 4311 O O . ALA A 1 635 ? -24.456 -69.239 80.013 1.00 124.52 ? 635 ALA A O 1 ATOM 4312 C CB . ALA A 1 635 ? -22.359 -70.479 82.116 1.00 122.94 ? 635 ALA A CB 1 ATOM 4313 N N . TYR A 1 636 ? -25.555 -70.745 81.294 1.00 109.76 ? 636 TYR A N 1 ATOM 4314 C CA . TYR A 1 636 ? -26.759 -69.905 81.495 1.00 111.96 ? 636 TYR A CA 1 ATOM 4315 C C . TYR A 1 636 ? -26.736 -69.315 82.911 1.00 116.85 ? 636 TYR A C 1 ATOM 4316 O O . TYR A 1 636 ? -26.592 -70.057 83.887 1.00 135.23 ? 636 TYR A O 1 ATOM 4317 C CB . TYR A 1 636 ? -28.064 -70.693 81.404 1.00 109.64 ? 636 TYR A CB 1 ATOM 4318 C CG . TYR A 1 636 ? -28.661 -71.058 80.048 1.00 124.74 ? 636 TYR A CG 1 ATOM 4319 C CD1 . TYR A 1 636 ? -27.952 -70.929 78.850 1.00 128.57 ? 636 TYR A CD1 1 ATOM 4320 C CD2 . TYR A 1 636 ? -29.968 -71.593 79.981 1.00 140.40 ? 636 TYR A CD2 1 ATOM 4321 C CE1 . TYR A 1 636 ? -28.528 -71.327 77.631 1.00 139.25 ? 636 TYR A CE1 1 ATOM 4322 C CE2 . TYR A 1 636 ? -30.549 -71.987 78.771 1.00 144.34 ? 636 TYR A CE2 1 ATOM 4323 C CZ . TYR A 1 636 ? -29.824 -71.851 77.597 1.00 143.69 ? 636 TYR A CZ 1 ATOM 4324 O OH . TYR A 1 636 ? -30.398 -72.256 76.411 1.00 140.91 ? 636 TYR A OH 1 ATOM 4325 N N . TRP A 1 637 ? -26.925 -68.003 83.031 1.00 111.79 ? 637 TRP A N 1 ATOM 4326 C CA . TRP A 1 637 ? -26.957 -67.347 84.333 1.00 110.13 ? 637 TRP A CA 1 ATOM 4327 C C . TRP A 1 637 ? -28.318 -66.769 84.697 1.00 112.31 ? 637 TRP A C 1 ATOM 4328 O O . TRP A 1 637 ? -28.815 -65.829 84.063 1.00 117.90 ? 637 TRP A O 1 ATOM 4329 C CB . TRP A 1 637 ? -25.937 -66.247 84.351 1.00 118.73 ? 637 TRP A CB 1 ATOM 4330 C CG . TRP A 1 637 ? -24.588 -66.755 84.272 1.00 135.30 ? 637 TRP A CG 1 ATOM 4331 C CD1 . TRP A 1 637 ? -24.041 -67.485 83.267 1.00 144.25 ? 637 TRP A CD1 1 ATOM 4332 C CD2 . TRP A 1 637 ? -23.576 -66.581 85.242 1.00 144.64 ? 637 TRP A CD2 1 ATOM 4333 N NE1 . TRP A 1 637 ? -22.733 -67.783 83.554 1.00 147.61 ? 637 TRP A NE1 1 ATOM 4334 C CE2 . TRP A 1 637 ? -22.423 -67.231 84.763 1.00 142.61 ? 637 TRP A CE2 1 ATOM 4335 C CE3 . TRP A 1 637 ? -23.526 -65.934 86.475 1.00 154.41 ? 637 TRP A CE3 1 ATOM 4336 C CZ2 . TRP A 1 637 ? -21.243 -67.249 85.466 1.00 144.23 ? 637 TRP A CZ2 1 ATOM 4337 C CZ3 . TRP A 1 637 ? -22.349 -65.954 87.176 1.00 158.41 ? 637 TRP A CZ3 1 ATOM 4338 C CH2 . TRP A 1 637 ? -21.224 -66.609 86.674 1.00 154.18 ? 637 TRP A CH2 1 ATOM 4339 N N . TYR A 1 638 ? -28.917 -67.330 85.734 1.00 103.61 ? 638 TYR A N 1 ATOM 4340 C CA . TYR A 1 638 ? -30.213 -66.881 86.172 1.00 95.04 ? 638 TYR A CA 1 ATOM 4341 C C . TYR A 1 638 ? -29.974 -65.878 87.256 1.00 99.43 ? 638 TYR A C 1 ATOM 4342 O O . TYR A 1 638 ? -29.608 -66.221 88.376 1.00 105.93 ? 638 TYR A O 1 ATOM 4343 C CB . TYR A 1 638 ? -30.989 -68.050 86.689 1.00 91.15 ? 638 TYR A CB 1 ATOM 4344 C CG . TYR A 1 638 ? -30.874 -69.214 85.766 1.00 106.34 ? 638 TYR A CG 1 ATOM 4345 C CD1 . TYR A 1 638 ? -31.734 -69.338 84.687 1.00 120.85 ? 638 TYR A CD1 1 ATOM 4346 C CD2 . TYR A 1 638 ? -29.882 -70.193 85.942 1.00 111.74 ? 638 TYR A CD2 1 ATOM 4347 C CE1 . TYR A 1 638 ? -31.635 -70.418 83.815 1.00 130.59 ? 638 TYR A CE1 1 ATOM 4348 C CE2 . TYR A 1 638 ? -29.769 -71.280 85.073 1.00 114.99 ? 638 TYR A CE2 1 ATOM 4349 C CZ . TYR A 1 638 ? -30.650 -71.386 84.006 1.00 120.53 ? 638 TYR A CZ 1 ATOM 4350 O OH . TYR A 1 638 ? -30.594 -72.439 83.115 1.00 120.17 ? 638 TYR A OH 1 ATOM 4351 N N . ILE A 1 639 ? -30.144 -64.622 86.887 1.00 100.59 ? 639 ILE A N 1 ATOM 4352 C CA . ILE A 1 639 ? -29.930 -63.504 87.778 1.00 98.90 ? 639 ILE A CA 1 ATOM 4353 C C . ILE A 1 639 ? -31.278 -62.926 88.190 1.00 104.87 ? 639 ILE A C 1 ATOM 4354 O O . ILE A 1 639 ? -32.246 -62.947 87.422 1.00 110.75 ? 639 ILE A O 1 ATOM 4355 C CB . ILE A 1 639 ? -29.129 -62.414 87.053 1.00 95.46 ? 639 ILE A CB 1 ATOM 4356 C CG1 . ILE A 1 639 ? -27.857 -63.008 86.468 1.00 86.94 ? 639 ILE A CG1 1 ATOM 4357 C CG2 . ILE A 1 639 ? -28.848 -61.209 87.953 1.00 96.75 ? 639 ILE A CG2 1 ATOM 4358 C CD1 . ILE A 1 639 ? -27.427 -62.224 85.262 1.00 87.35 ? 639 ILE A CD1 1 ATOM 4359 N N . LEU A 1 640 ? -31.336 -62.396 89.402 1.00 106.71 ? 640 LEU A N 1 ATOM 4360 C CA . LEU A 1 640 ? -32.538 -61.731 89.868 1.00 106.18 ? 640 LEU A CA 1 ATOM 4361 C C . LEU A 1 640 ? -32.233 -60.806 91.036 1.00 110.81 ? 640 LEU A C 1 ATOM 4362 O O . LEU A 1 640 ? -31.508 -61.168 91.961 1.00 113.93 ? 640 LEU A O 1 ATOM 4363 C CB . LEU A 1 640 ? -33.608 -62.760 90.242 1.00 97.58 ? 640 LEU A CB 1 ATOM 4364 C CG . LEU A 1 640 ? -33.391 -63.757 91.378 1.00 91.99 ? 640 LEU A CG 1 ATOM 4365 C CD1 . LEU A 1 640 ? -34.665 -64.561 91.501 1.00 95.35 ? 640 LEU A CD1 1 ATOM 4366 C CD2 . LEU A 1 640 ? -32.203 -64.687 91.172 1.00 91.25 ? 640 LEU A CD2 1 ATOM 4367 N N . SER A 1 641 ? -32.759 -59.591 90.969 1.00 113.80 ? 641 SER A N 1 ATOM 4368 C CA . SER A 1 641 ? -32.780 -58.737 92.137 1.00 116.20 ? 641 SER A CA 1 ATOM 4369 C C . SER A 1 641 ? -34.045 -59.086 92.886 1.00 117.49 ? 641 SER A C 1 ATOM 4370 O O . SER A 1 641 ? -35.104 -59.287 92.275 1.00 116.31 ? 641 SER A O 1 ATOM 4371 C CB . SER A 1 641 ? -32.785 -57.264 91.764 1.00 120.90 ? 641 SER A CB 1 ATOM 4372 O OG . SER A 1 641 ? -32.858 -56.489 92.946 1.00 125.26 ? 641 SER A OG 1 ATOM 4373 N N . ILE A 1 642 ? -33.923 -59.176 94.206 1.00 120.29 ? 642 ILE A N 1 ATOM 4374 C CA . ILE A 1 642 ? -35.018 -59.637 95.050 1.00 122.96 ? 642 ILE A CA 1 ATOM 4375 C C . ILE A 1 642 ? -34.751 -59.223 96.476 1.00 121.43 ? 642 ILE A C 1 ATOM 4376 O O . ILE A 1 642 ? -33.676 -59.490 97.022 1.00 117.38 ? 642 ILE A O 1 ATOM 4377 C CB . ILE A 1 642 ? -35.272 -61.175 94.932 1.00 129.53 ? 642 ILE A CB 1 ATOM 4378 C CG1 . ILE A 1 642 ? -36.614 -61.549 95.534 1.00 125.35 ? 642 ILE A CG1 1 ATOM 4379 C CG2 . ILE A 1 642 ? -34.184 -62.017 95.580 1.00 127.93 ? 642 ILE A CG2 1 ATOM 4380 C CD1 . ILE A 1 642 ? -37.761 -60.833 94.869 1.00 139.62 ? 642 ILE A CD1 1 ATOM 4381 N N . GLY A 1 643 ? -35.726 -58.542 97.063 1.00 126.25 ? 643 GLY A N 1 ATOM 4382 C CA . GLY A 1 643 ? -35.552 -57.953 98.379 1.00 144.17 ? 643 GLY A CA 1 ATOM 4383 C C . GLY A 1 643 ? -34.479 -56.880 98.392 1.00 164.79 ? 643 GLY A C 1 ATOM 4384 O O . GLY A 1 643 ? -34.208 -56.307 99.449 1.00 171.07 ? 643 GLY A O 1 ATOM 4385 N N . ALA A 1 644 ? -33.857 -56.626 97.227 1.00 165.31 ? 644 ALA A N 1 ATOM 4386 C CA . ALA A 1 644 ? -32.914 -55.504 97.045 1.00 139.92 ? 644 ALA A CA 1 ATOM 4387 C C . ALA A 1 644 ? -33.750 -54.239 96.918 1.00 135.06 ? 644 ALA A C 1 ATOM 4388 O O . ALA A 1 644 ? -33.926 -53.688 95.845 1.00 139.07 ? 644 ALA A O 1 ATOM 4389 C CB . ALA A 1 644 ? -31.982 -55.711 95.848 1.00 104.86 ? 644 ALA A CB 1 ATOM 4390 N N . GLN A 1 645 ? -34.271 -53.817 98.057 1.00 130.55 ? 645 GLN A N 1 ATOM 4391 C CA . GLN A 1 645 ? -35.278 -52.787 98.189 1.00 141.77 ? 645 GLN A CA 1 ATOM 4392 C C . GLN A 1 645 ? -35.283 -51.581 97.181 1.00 148.79 ? 645 GLN A C 1 ATOM 4393 O O . GLN A 1 645 ? -34.235 -51.132 96.694 1.00 131.66 ? 645 GLN A O 1 ATOM 4394 C CB . GLN A 1 645 ? -35.241 -52.328 99.659 1.00 155.65 ? 645 GLN A CB 1 ATOM 4395 C CG . GLN A 1 645 ? -35.949 -53.222 100.705 1.00 177.47 ? 645 GLN A CG 1 ATOM 4396 C CD . GLN A 1 645 ? -35.934 -54.748 100.466 1.00 177.75 ? 645 GLN A CD 1 ATOM 4397 O OE1 . GLN A 1 645 ? -35.456 -55.526 101.321 1.00 173.12 ? 645 GLN A OE1 1 ATOM 4398 N NE2 . GLN A 1 645 ? -36.509 -55.186 99.333 1.00 157.77 ? 645 GLN A NE2 1 ATOM 4399 N N . THR A 1 646 ? -36.502 -51.106 96.880 1.00 168.81 ? 646 THR A N 1 ATOM 4400 C CA . THR A 1 646 ? -36.864 -49.850 96.114 1.00 171.53 ? 646 THR A CA 1 ATOM 4401 C C . THR A 1 646 ? -36.385 -49.620 94.675 1.00 154.75 ? 646 THR A C 1 ATOM 4402 O O . THR A 1 646 ? -37.210 -49.369 93.806 1.00 150.46 ? 646 THR A O 1 ATOM 4403 C CB . THR A 1 646 ? -36.714 -48.496 96.899 1.00 173.09 ? 646 THR A CB 1 ATOM 4404 O OG1 . THR A 1 646 ? -35.390 -48.367 97.418 1.00 180.60 ? 646 THR A OG1 1 ATOM 4405 C CG2 . THR A 1 646 ? -37.765 -48.324 98.035 1.00 160.03 ? 646 THR A CG2 1 ATOM 4406 N N . ASP A 1 647 ? -35.083 -49.650 94.424 1.00 143.40 ? 647 ASP A N 1 ATOM 4407 C CA . ASP A 1 647 ? -34.577 -49.197 93.128 1.00 143.96 ? 647 ASP A CA 1 ATOM 4408 C C . ASP A 1 647 ? -34.422 -50.282 92.021 1.00 143.08 ? 647 ASP A C 1 ATOM 4409 O O . ASP A 1 647 ? -34.744 -51.459 92.228 1.00 145.77 ? 647 ASP A O 1 ATOM 4410 C CB . ASP A 1 647 ? -33.272 -48.447 93.342 1.00 156.34 ? 647 ASP A CB 1 ATOM 4411 C CG . ASP A 1 647 ? -33.193 -47.210 92.506 1.00 180.70 ? 647 ASP A CG 1 ATOM 4412 O OD1 . ASP A 1 647 ? -33.500 -47.292 91.293 1.00 176.12 ? 647 ASP A OD1 1 ATOM 4413 O OD2 . ASP A 1 647 ? -32.855 -46.147 93.067 1.00 216.00 ? 647 ASP A OD2 1 ATOM 4414 N N . PHE A 1 648 ? -33.955 -49.884 90.837 1.00 129.57 ? 648 PHE A N 1 ATOM 4415 C CA . PHE A 1 648 ? -33.571 -50.862 89.822 1.00 117.43 ? 648 PHE A CA 1 ATOM 4416 C C . PHE A 1 648 ? -32.067 -51.162 89.876 1.00 122.25 ? 648 PHE A C 1 ATOM 4417 O O . PHE A 1 648 ? -31.275 -50.431 90.484 1.00 129.07 ? 648 PHE A O 1 ATOM 4418 C CB . PHE A 1 648 ? -34.024 -50.420 88.419 1.00 121.94 ? 648 PHE A CB 1 ATOM 4419 C CG . PHE A 1 648 ? -33.208 -49.282 87.789 1.00 138.43 ? 648 PHE A CG 1 ATOM 4420 C CD1 . PHE A 1 648 ? -31.884 -49.479 87.348 1.00 145.81 ? 648 PHE A CD1 1 ATOM 4421 C CD2 . PHE A 1 648 ? -33.791 -48.037 87.552 1.00 136.84 ? 648 PHE A CD2 1 ATOM 4422 C CE1 . PHE A 1 648 ? -31.156 -48.452 86.746 1.00 136.99 ? 648 PHE A CE1 1 ATOM 4423 C CE2 . PHE A 1 648 ? -33.066 -47.016 86.949 1.00 136.67 ? 648 PHE A CE2 1 ATOM 4424 C CZ . PHE A 1 648 ? -31.751 -47.223 86.550 1.00 135.17 ? 648 PHE A CZ 1 ATOM 4425 N N . LEU A 1 649 ? -31.657 -52.240 89.239 1.00 125.14 ? 649 LEU A N 1 ATOM 4426 C CA . LEU A 1 649 ? -30.238 -52.526 89.155 1.00 135.10 ? 649 LEU A CA 1 ATOM 4427 C C . LEU A 1 649 ? -29.690 -52.434 87.746 1.00 146.58 ? 649 LEU A C 1 ATOM 4428 O O . LEU A 1 649 ? -30.441 -52.387 86.780 1.00 171.86 ? 649 LEU A O 1 ATOM 4429 C CB . LEU A 1 649 ? -29.982 -53.908 89.707 1.00 136.33 ? 649 LEU A CB 1 ATOM 4430 C CG . LEU A 1 649 ? -30.087 -53.872 91.216 1.00 138.13 ? 649 LEU A CG 1 ATOM 4431 C CD1 . LEU A 1 649 ? -29.972 -55.287 91.730 1.00 143.78 ? 649 LEU A CD1 1 ATOM 4432 C CD2 . LEU A 1 649 ? -29.003 -52.968 91.800 1.00 141.83 ? 649 LEU A CD2 1 ATOM 4433 N N . SER A 1 650 ? -28.374 -52.399 87.624 1.00 145.75 ? 650 SER A N 1 ATOM 4434 C CA . SER A 1 650 ? -27.752 -52.532 86.319 1.00 149.57 ? 650 SER A CA 1 ATOM 4435 C C . SER A 1 650 ? -26.563 -53.460 86.497 1.00 150.39 ? 650 SER A C 1 ATOM 4436 O O . SER A 1 650 ? -25.442 -53.006 86.716 1.00 183.01 ? 650 SER A O 1 ATOM 4437 C CB . SER A 1 650 ? -27.345 -51.162 85.734 1.00 144.43 ? 650 SER A CB 1 ATOM 4438 O OG . SER A 1 650 ? -28.437 -50.504 85.112 1.00 131.65 ? 650 SER A OG 1 ATOM 4439 N N . VAL A 1 651 ? -26.814 -54.761 86.420 1.00 127.18 ? 651 VAL A N 1 ATOM 4440 C CA . VAL A 1 651 ? -25.766 -55.758 86.657 1.00 129.81 ? 651 VAL A CA 1 ATOM 4441 C C . VAL A 1 651 ? -24.535 -55.700 85.691 1.00 131.66 ? 651 VAL A C 1 ATOM 4442 O O . VAL A 1 651 ? -24.631 -55.230 84.553 1.00 122.19 ? 651 VAL A O 1 ATOM 4443 C CB . VAL A 1 651 ? -26.385 -57.159 86.767 1.00 130.56 ? 651 VAL A CB 1 ATOM 4444 C CG1 . VAL A 1 651 ? -27.689 -57.072 87.542 1.00 120.02 ? 651 VAL A CG1 1 ATOM 4445 C CG2 . VAL A 1 651 ? -26.632 -57.753 85.389 1.00 140.97 ? 651 VAL A CG2 1 ATOM 4446 N N . PHE A 1 652 ? -23.383 -56.176 86.160 1.00 133.14 ? 652 PHE A N 1 ATOM 4447 C CA . PHE A 1 652 ? -22.111 -55.787 85.559 1.00 131.38 ? 652 PHE A CA 1 ATOM 4448 C C . PHE A 1 652 ? -21.423 -56.865 84.723 1.00 129.68 ? 652 PHE A C 1 ATOM 4449 O O . PHE A 1 652 ? -21.616 -56.884 83.516 1.00 127.83 ? 652 PHE A O 1 ATOM 4450 C CB . PHE A 1 652 ? -21.175 -55.201 86.624 1.00 142.27 ? 652 PHE A CB 1 ATOM 4451 C CG . PHE A 1 652 ? -20.100 -54.324 86.069 1.00 165.11 ? 652 PHE A CG 1 ATOM 4452 C CD1 . PHE A 1 652 ? -20.348 -53.491 84.976 1.00 194.16 ? 652 PHE A CD1 1 ATOM 4453 C CD2 . PHE A 1 652 ? -18.824 -54.328 86.627 1.00 174.93 ? 652 PHE A CD2 1 ATOM 4454 C CE1 . PHE A 1 652 ? -19.338 -52.678 84.454 1.00 219.65 ? 652 PHE A CE1 1 ATOM 4455 C CE2 . PHE A 1 652 ? -17.809 -53.514 86.111 1.00 196.22 ? 652 PHE A CE2 1 ATOM 4456 C CZ . PHE A 1 652 ? -18.064 -52.692 85.021 1.00 208.37 ? 652 PHE A CZ 1 ATOM 4457 N N . PHE A 1 653 ? -20.632 -57.743 85.352 1.00 128.59 ? 653 PHE A N 1 ATOM 4458 C CA . PHE A 1 653 ? -19.775 -58.729 84.646 1.00 122.45 ? 653 PHE A CA 1 ATOM 4459 C C . PHE A 1 653 ? -18.636 -58.086 83.894 1.00 117.88 ? 653 PHE A C 1 ATOM 4460 O O . PHE A 1 653 ? -18.763 -57.853 82.697 1.00 105.62 ? 653 PHE A O 1 ATOM 4461 C CB . PHE A 1 653 ? -20.556 -59.527 83.613 1.00 123.73 ? 653 PHE A CB 1 ATOM 4462 C CG . PHE A 1 653 ? -21.261 -60.711 84.166 1.00 131.18 ? 653 PHE A CG 1 ATOM 4463 C CD1 . PHE A 1 653 ? -22.563 -60.606 84.623 1.00 132.00 ? 653 PHE A CD1 1 ATOM 4464 C CD2 . PHE A 1 653 ? -20.637 -61.950 84.202 1.00 137.14 ? 653 PHE A CD2 1 ATOM 4465 C CE1 . PHE A 1 653 ? -23.221 -61.721 85.129 1.00 136.26 ? 653 PHE A CE1 1 ATOM 4466 C CE2 . PHE A 1 653 ? -21.297 -63.070 84.699 1.00 135.02 ? 653 PHE A CE2 1 ATOM 4467 C CZ . PHE A 1 653 ? -22.589 -62.956 85.164 1.00 126.63 ? 653 PHE A CZ 1 ATOM 4468 N N . SER A 1 654 ? -17.523 -57.851 84.586 1.00 125.92 ? 654 SER A N 1 ATOM 4469 C CA . SER A 1 654 ? -16.354 -57.108 84.060 1.00 138.20 ? 654 SER A CA 1 ATOM 4470 C C . SER A 1 654 ? -15.718 -57.737 82.816 1.00 136.52 ? 654 SER A C 1 ATOM 4471 O O . SER A 1 654 ? -15.123 -58.799 82.906 1.00 133.13 ? 654 SER A O 1 ATOM 4472 C CB . SER A 1 654 ? -15.283 -56.974 85.166 1.00 153.73 ? 654 SER A CB 1 ATOM 4473 O OG . SER A 1 654 ? -14.510 -55.776 85.074 1.00 176.06 ? 654 SER A OG 1 ATOM 4474 N N . GLY A 1 655 ? -15.828 -57.075 81.663 1.00 140.73 ? 655 GLY A N 1 ATOM 4475 C CA . GLY A 1 655 ? -15.215 -57.572 80.416 1.00 149.29 ? 655 GLY A CA 1 ATOM 4476 C C . GLY A 1 655 ? -15.955 -58.738 79.768 1.00 149.74 ? 655 GLY A C 1 ATOM 4477 O O . GLY A 1 655 ? -15.357 -59.610 79.125 1.00 156.94 ? 655 GLY A O 1 ATOM 4478 N N . TYR A 1 656 ? -17.272 -58.737 79.920 1.00 140.49 ? 656 TYR A N 1 ATOM 4479 C CA . TYR A 1 656 ? -18.075 -59.840 79.465 1.00 131.01 ? 656 TYR A CA 1 ATOM 4480 C C . TYR A 1 656 ? -19.368 -59.480 78.754 1.00 140.25 ? 656 TYR A C 1 ATOM 4481 O O . TYR A 1 656 ? -20.082 -58.557 79.147 1.00 156.55 ? 656 TYR A O 1 ATOM 4482 C CB . TYR A 1 656 ? -18.342 -60.749 80.634 1.00 119.91 ? 656 TYR A CB 1 ATOM 4483 C CG . TYR A 1 656 ? -17.436 -61.901 80.540 1.00 129.71 ? 656 TYR A CG 1 ATOM 4484 C CD1 . TYR A 1 656 ? -17.256 -62.545 79.318 1.00 144.09 ? 656 TYR A CD1 1 ATOM 4485 C CD2 . TYR A 1 656 ? -16.739 -62.353 81.641 1.00 136.52 ? 656 TYR A CD2 1 ATOM 4486 C CE1 . TYR A 1 656 ? -16.410 -63.631 79.200 1.00 162.71 ? 656 TYR A CE1 1 ATOM 4487 C CE2 . TYR A 1 656 ? -15.881 -63.440 81.538 1.00 154.94 ? 656 TYR A CE2 1 ATOM 4488 C CZ . TYR A 1 656 ? -15.719 -64.079 80.316 1.00 161.38 ? 656 TYR A CZ 1 ATOM 4489 O OH . TYR A 1 656 ? -14.879 -65.169 80.211 1.00 165.45 ? 656 TYR A OH 1 ATOM 4490 N N . THR A 1 657 ? -19.675 -60.216 77.697 1.00 137.91 ? 657 THR A N 1 ATOM 4491 C CA . THR A 1 657 ? -20.924 -59.981 77.004 1.00 126.69 ? 657 THR A CA 1 ATOM 4492 C C . THR A 1 657 ? -21.794 -61.198 77.016 1.00 127.96 ? 657 THR A C 1 ATOM 4493 O O . THR A 1 657 ? -21.354 -62.331 76.681 1.00 129.21 ? 657 THR A O 1 ATOM 4494 C CB . THR A 1 657 ? -20.695 -59.571 75.566 1.00 129.12 ? 657 THR A CB 1 ATOM 4495 O OG1 . THR A 1 657 ? -19.499 -60.212 75.099 1.00 142.83 ? 657 THR A OG1 1 ATOM 4496 C CG2 . THR A 1 657 ? -20.541 -58.089 75.506 1.00 127.91 ? 657 THR A CG2 1 ATOM 4497 N N . PHE A 1 658 ? -23.043 -60.932 77.390 1.00 120.32 ? 658 PHE A N 1 ATOM 4498 C CA . PHE A 1 658 ? -24.069 -61.958 77.519 1.00 121.61 ? 658 PHE A CA 1 ATOM 4499 C C . PHE A 1 658 ? -25.268 -61.824 76.555 1.00 117.78 ? 658 PHE A C 1 ATOM 4500 O O . PHE A 1 658 ? -25.650 -60.728 76.157 1.00 115.20 ? 658 PHE A O 1 ATOM 4501 C CB . PHE A 1 658 ? -24.549 -62.020 78.960 1.00 114.50 ? 658 PHE A CB 1 ATOM 4502 C CG . PHE A 1 658 ? -25.018 -60.714 79.490 1.00 112.66 ? 658 PHE A CG 1 ATOM 4503 C CD1 . PHE A 1 658 ? -26.339 -60.334 79.351 1.00 115.37 ? 658 PHE A CD1 1 ATOM 4504 C CD2 . PHE A 1 658 ? -24.144 -59.871 80.147 1.00 116.01 ? 658 PHE A CD2 1 ATOM 4505 C CE1 . PHE A 1 658 ? -26.778 -59.121 79.849 1.00 124.57 ? 658 PHE A CE1 1 ATOM 4506 C CE2 . PHE A 1 658 ? -24.578 -58.661 80.656 1.00 123.97 ? 658 PHE A CE2 1 ATOM 4507 C CZ . PHE A 1 658 ? -25.895 -58.280 80.500 1.00 124.49 ? 658 PHE A CZ 1 ATOM 4508 N N . LYS A 1 659 ? -25.837 -62.967 76.179 1.00 114.93 ? 659 LYS A N 1 ATOM 4509 C CA . LYS A 1 659 ? -26.968 -63.016 75.288 1.00 108.02 ? 659 LYS A CA 1 ATOM 4510 C C . LYS A 1 659 ? -28.191 -62.952 76.169 1.00 117.50 ? 659 LYS A C 1 ATOM 4511 O O . LYS A 1 659 ? -28.500 -63.905 76.903 1.00 123.08 ? 659 LYS A O 1 ATOM 4512 C CB . LYS A 1 659 ? -26.967 -64.315 74.473 1.00 102.31 ? 659 LYS A CB 1 ATOM 4513 C CG . LYS A 1 659 ? -27.442 -64.178 73.027 1.00 100.34 ? 659 LYS A CG 1 ATOM 4514 C CD . LYS A 1 659 ? -27.352 -65.498 72.255 1.00 103.44 ? 659 LYS A CD 1 ATOM 4515 C CE . LYS A 1 659 ? -27.053 -65.313 70.759 1.00 105.62 ? 659 LYS A CE 1 ATOM 4516 N NZ . LYS A 1 659 ? -25.622 -65.485 70.316 1.00 101.49 ? 659 LYS A NZ 1 ATOM 4517 N N . HIS A 1 660 ? -28.853 -61.799 76.108 1.00 123.49 ? 660 HIS A N 1 ATOM 4518 C CA . HIS A 1 660 ? -30.170 -61.588 76.689 1.00 123.94 ? 660 HIS A CA 1 ATOM 4519 C C . HIS A 1 660 ? -31.199 -61.653 75.558 1.00 133.20 ? 660 HIS A C 1 ATOM 4520 O O . HIS A 1 660 ? -31.182 -60.793 74.662 1.00 120.74 ? 660 HIS A O 1 ATOM 4521 C CB . HIS A 1 660 ? -30.197 -60.230 77.370 1.00 118.91 ? 660 HIS A CB 1 ATOM 4522 C CG . HIS A 1 660 ? -31.344 -60.040 78.304 1.00 124.89 ? 660 HIS A CG 1 ATOM 4523 N ND1 . HIS A 1 660 ? -31.771 -58.793 78.707 1.00 135.63 ? 660 HIS A ND1 1 ATOM 4524 C CD2 . HIS A 1 660 ? -32.162 -60.931 78.910 1.00 134.37 ? 660 HIS A CD2 1 ATOM 4525 C CE1 . HIS A 1 660 ? -32.794 -58.923 79.534 1.00 139.30 ? 660 HIS A CE1 1 ATOM 4526 N NE2 . HIS A 1 660 ? -33.055 -60.210 79.669 1.00 145.75 ? 660 HIS A NE2 1 ATOM 4527 N N . LYS A 1 661 ? -32.043 -62.696 75.580 1.00 143.62 ? 661 LYS A N 1 ATOM 4528 C CA . LYS A 1 661 ? -33.139 -62.911 74.601 1.00 145.59 ? 661 LYS A CA 1 ATOM 4529 C C . LYS A 1 661 ? -32.788 -62.732 73.079 1.00 135.70 ? 661 LYS A C 1 ATOM 4530 O O . LYS A 1 661 ? -33.186 -61.747 72.400 1.00 100.49 ? 661 LYS A O 1 ATOM 4531 C CB . LYS A 1 661 ? -34.400 -62.151 75.042 1.00 159.77 ? 661 LYS A CB 1 ATOM 4532 C CG . LYS A 1 661 ? -34.457 -60.686 74.630 1.00 198.23 ? 661 LYS A CG 1 ATOM 4533 C CD . LYS A 1 661 ? -33.543 -59.787 75.447 1.00 214.45 ? 661 LYS A CD 1 ATOM 4534 C CE . LYS A 1 661 ? -33.006 -58.641 74.595 1.00 235.59 ? 661 LYS A CE 1 ATOM 4535 N NZ . LYS A 1 661 ? -31.648 -58.198 75.031 1.00 234.45 ? 661 LYS A NZ 1 ATOM 4536 N N . MET A 1 662 ? -32.065 -63.742 72.580 1.00 145.94 ? 662 MET A N 1 ATOM 4537 C CA . MET A 1 662 ? -31.311 -63.730 71.302 1.00 153.67 ? 662 MET A CA 1 ATOM 4538 C C . MET A 1 662 ? -30.713 -62.385 70.793 1.00 145.75 ? 662 MET A C 1 ATOM 4539 O O . MET A 1 662 ? -30.807 -62.064 69.604 1.00 155.26 ? 662 MET A O 1 ATOM 4540 C CB . MET A 1 662 ? -32.051 -64.499 70.185 1.00 171.10 ? 662 MET A CB 1 ATOM 4541 C CG . MET A 1 662 ? -31.511 -65.901 69.861 1.00 194.80 ? 662 MET A CG 1 ATOM 4542 S SD . MET A 1 662 ? -30.053 -66.052 68.765 1.00 239.51 ? 662 MET A SD 1 ATOM 4543 C CE . MET A 1 662 ? -30.606 -65.454 67.156 1.00 212.01 ? 662 MET A CE 1 ATOM 4544 N N . VAL A 1 663 ? -30.084 -61.622 71.692 1.00 126.23 ? 663 VAL A N 1 ATOM 4545 C CA . VAL A 1 663 ? -29.256 -60.466 71.322 1.00 115.07 ? 663 VAL A CA 1 ATOM 4546 C C . VAL A 1 663 ? -28.093 -60.359 72.277 1.00 114.35 ? 663 VAL A C 1 ATOM 4547 O O . VAL A 1 663 ? -28.201 -60.790 73.426 1.00 105.48 ? 663 VAL A O 1 ATOM 4548 C CB . VAL A 1 663 ? -29.976 -59.136 71.504 1.00 119.19 ? 663 VAL A CB 1 ATOM 4549 C CG1 . VAL A 1 663 ? -29.416 -58.101 70.534 1.00 113.16 ? 663 VAL A CG1 1 ATOM 4550 C CG2 . VAL A 1 663 ? -31.481 -59.308 71.369 1.00 142.10 ? 663 VAL A CG2 1 ATOM 4551 N N . TYR A 1 664 ? -27.002 -59.740 71.820 1.00 120.25 ? 664 TYR A N 1 ATOM 4552 C CA . TYR A 1 664 ? -25.798 -59.600 72.648 1.00 119.60 ? 664 TYR A CA 1 ATOM 4553 C C . TYR A 1 664 ? -25.773 -58.278 73.473 1.00 114.90 ? 664 TYR A C 1 ATOM 4554 O O . TYR A 1 664 ? -25.957 -57.202 72.907 1.00 114.93 ? 664 TYR A O 1 ATOM 4555 C CB . TYR A 1 664 ? -24.527 -59.884 71.800 1.00 120.64 ? 664 TYR A CB 1 ATOM 4556 C CG . TYR A 1 664 ? -24.178 -61.372 71.797 1.00 127.72 ? 664 TYR A CG 1 ATOM 4557 C CD1 . TYR A 1 664 ? -24.393 -62.148 72.950 1.00 137.29 ? 664 TYR A CD1 1 ATOM 4558 C CD2 . TYR A 1 664 ? -23.645 -62.017 70.672 1.00 131.25 ? 664 TYR A CD2 1 ATOM 4559 C CE1 . TYR A 1 664 ? -24.094 -63.518 72.998 1.00 152.37 ? 664 TYR A CE1 1 ATOM 4560 C CE2 . TYR A 1 664 ? -23.353 -63.406 70.706 1.00 150.23 ? 664 TYR A CE2 1 ATOM 4561 C CZ . TYR A 1 664 ? -23.576 -64.163 71.880 1.00 156.73 ? 664 TYR A CZ 1 ATOM 4562 O OH . TYR A 1 664 ? -23.305 -65.543 71.991 1.00 142.36 ? 664 TYR A OH 1 ATOM 4563 N N . GLU A 1 665 ? -25.619 -58.369 74.805 1.00 111.70 ? 665 GLU A N 1 ATOM 4564 C CA . GLU A 1 665 ? -25.638 -57.176 75.701 1.00 119.58 ? 665 GLU A CA 1 ATOM 4565 C C . GLU A 1 665 ? -24.384 -56.974 76.586 1.00 132.52 ? 665 GLU A C 1 ATOM 4566 O O . GLU A 1 665 ? -23.451 -57.808 76.628 1.00 129.25 ? 665 GLU A O 1 ATOM 4567 C CB . GLU A 1 665 ? -26.928 -57.035 76.573 1.00 116.60 ? 665 GLU A CB 1 ATOM 4568 C CG . GLU A 1 665 ? -28.254 -56.734 75.852 1.00 135.41 ? 665 GLU A CG 1 ATOM 4569 C CD . GLU A 1 665 ? -28.259 -55.466 74.983 1.00 161.57 ? 665 GLU A CD 1 ATOM 4570 O OE1 . GLU A 1 665 ? -27.590 -54.475 75.347 1.00 186.70 ? 665 GLU A OE1 1 ATOM 4571 O OE2 . GLU A 1 665 ? -28.951 -55.440 73.929 1.00 162.58 ? 665 GLU A OE2 1 ATOM 4572 N N . ASP A 1 666 ? -24.426 -55.850 77.307 1.00 142.14 ? 666 ASP A N 1 ATOM 4573 C CA . ASP A 1 666 ? -23.275 -55.164 77.896 1.00 140.40 ? 666 ASP A CA 1 ATOM 4574 C C . ASP A 1 666 ? -23.587 -55.133 79.356 1.00 127.44 ? 666 ASP A C 1 ATOM 4575 O O . ASP A 1 666 ? -22.686 -55.312 80.176 1.00 118.29 ? 666 ASP A O 1 ATOM 4576 C CB . ASP A 1 666 ? -23.211 -53.711 77.334 1.00 165.90 ? 666 ASP A CB 1 ATOM 4577 C CG . ASP A 1 666 ? -22.016 -52.865 77.860 1.00 173.36 ? 666 ASP A CG 1 ATOM 4578 O OD1 . ASP A 1 666 ? -21.415 -53.225 78.896 1.00 186.39 ? 666 ASP A OD1 1 ATOM 4579 O OD2 . ASP A 1 666 ? -21.704 -51.808 77.230 1.00 157.91 ? 666 ASP A OD2 1 ATOM 4580 N N . THR A 1 667 ? -24.876 -54.919 79.658 1.00 121.85 ? 667 THR A N 1 ATOM 4581 C CA . THR A 1 667 ? -25.351 -54.632 81.014 1.00 135.66 ? 667 THR A CA 1 ATOM 4582 C C . THR A 1 667 ? -26.853 -54.749 81.166 1.00 129.43 ? 667 THR A C 1 ATOM 4583 O O . THR A 1 667 ? -27.610 -53.984 80.580 1.00 131.05 ? 667 THR A O 1 ATOM 4584 C CB . THR A 1 667 ? -24.987 -53.210 81.455 1.00 152.57 ? 667 THR A CB 1 ATOM 4585 O OG1 . THR A 1 667 ? -25.044 -52.339 80.317 1.00 165.40 ? 667 THR A OG1 1 ATOM 4586 C CG2 . THR A 1 667 ? -23.585 -53.173 82.092 1.00 171.09 ? 667 THR A CG2 1 ATOM 4587 N N . LEU A 1 668 ? -27.261 -55.683 82.013 1.00 129.53 ? 668 LEU A N 1 ATOM 4588 C CA . LEU A 1 668 ? -28.656 -56.039 82.204 1.00 123.20 ? 668 LEU A CA 1 ATOM 4589 C C . LEU A 1 668 ? -29.289 -55.204 83.276 1.00 124.05 ? 668 LEU A C 1 ATOM 4590 O O . LEU A 1 668 ? -28.639 -54.868 84.268 1.00 127.48 ? 668 LEU A O 1 ATOM 4591 C CB . LEU A 1 668 ? -28.748 -57.508 82.595 1.00 126.12 ? 668 LEU A CB 1 ATOM 4592 C CG . LEU A 1 668 ? -29.895 -58.045 83.444 1.00 130.91 ? 668 LEU A CG 1 ATOM 4593 C CD1 . LEU A 1 668 ? -31.246 -57.965 82.734 1.00 137.69 ? 668 LEU A CD1 1 ATOM 4594 C CD2 . LEU A 1 668 ? -29.548 -59.480 83.810 1.00 139.05 ? 668 LEU A CD2 1 ATOM 4595 N N . THR A 1 669 ? -30.576 -54.923 83.087 1.00 127.96 ? 669 THR A N 1 ATOM 4596 C CA . THR A 1 669 ? -31.339 -54.030 83.977 1.00 133.65 ? 669 THR A CA 1 ATOM 4597 C C . THR A 1 669 ? -32.440 -54.702 84.858 1.00 132.32 ? 669 THR A C 1 ATOM 4598 O O . THR A 1 669 ? -33.408 -55.271 84.353 1.00 144.34 ? 669 THR A O 1 ATOM 4599 C CB . THR A 1 669 ? -31.894 -52.839 83.168 1.00 120.57 ? 669 THR A CB 1 ATOM 4600 O OG1 . THR A 1 669 ? -32.102 -53.261 81.807 1.00 114.25 ? 669 THR A OG1 1 ATOM 4601 C CG2 . THR A 1 669 ? -30.905 -51.649 83.221 1.00 104.93 ? 669 THR A CG2 1 ATOM 4602 N N . LEU A 1 670 ? -32.286 -54.611 86.179 1.00 125.27 ? 670 LEU A N 1 ATOM 4603 C CA . LEU A 1 670 ? -33.119 -55.370 87.108 1.00 120.60 ? 670 LEU A CA 1 ATOM 4604 C C . LEU A 1 670 ? -33.996 -54.610 88.088 1.00 134.94 ? 670 LEU A C 1 ATOM 4605 O O . LEU A 1 670 ? -33.569 -54.127 89.162 1.00 136.73 ? 670 LEU A O 1 ATOM 4606 C CB . LEU A 1 670 ? -32.285 -56.391 87.854 1.00 119.11 ? 670 LEU A CB 1 ATOM 4607 C CG . LEU A 1 670 ? -32.008 -57.568 86.939 1.00 123.79 ? 670 LEU A CG 1 ATOM 4608 C CD1 . LEU A 1 670 ? -31.519 -58.746 87.765 1.00 133.15 ? 670 LEU A CD1 1 ATOM 4609 C CD2 . LEU A 1 670 ? -33.265 -57.924 86.155 1.00 124.99 ? 670 LEU A CD2 1 ATOM 4610 N N . PHE A 1 671 ? -35.253 -54.543 87.689 1.00 132.94 ? 671 PHE A N 1 ATOM 4611 C CA . PHE A 1 671 ? -36.315 -54.023 88.506 1.00 133.16 ? 671 PHE A CA 1 ATOM 4612 C C . PHE A 1 671 ? -36.591 -54.937 89.679 1.00 129.54 ? 671 PHE A C 1 ATOM 4613 O O . PHE A 1 671 ? -36.552 -56.150 89.517 1.00 143.08 ? 671 PHE A O 1 ATOM 4614 C CB . PHE A 1 671 ? -37.573 -53.999 87.656 1.00 142.46 ? 671 PHE A CB 1 ATOM 4615 C CG . PHE A 1 671 ? -37.786 -52.711 86.929 1.00 147.39 ? 671 PHE A CG 1 ATOM 4616 C CD1 . PHE A 1 671 ? -36.712 -51.879 86.624 1.00 147.10 ? 671 PHE A CD1 1 ATOM 4617 C CD2 . PHE A 1 671 ? -39.073 -52.313 86.568 1.00 146.72 ? 671 PHE A CD2 1 ATOM 4618 C CE1 . PHE A 1 671 ? -36.914 -50.677 85.959 1.00 161.14 ? 671 PHE A CE1 1 ATOM 4619 C CE2 . PHE A 1 671 ? -39.280 -51.117 85.901 1.00 152.78 ? 671 PHE A CE2 1 ATOM 4620 C CZ . PHE A 1 671 ? -38.199 -50.297 85.595 1.00 161.98 ? 671 PHE A CZ 1 ATOM 4621 N N . PRO A 1 672 ? -36.915 -54.360 90.844 1.00 121.27 ? 672 PRO A N 1 ATOM 4622 C CA . PRO A 1 672 ? -37.497 -55.039 91.967 1.00 129.17 ? 672 PRO A CA 1 ATOM 4623 C C . PRO A 1 672 ? -37.668 -56.531 91.819 1.00 133.46 ? 672 PRO A C 1 ATOM 4624 O O . PRO A 1 672 ? -36.695 -57.263 91.975 1.00 143.22 ? 672 PRO A O 1 ATOM 4625 C CB . PRO A 1 672 ? -38.848 -54.332 92.083 1.00 139.40 ? 672 PRO A CB 1 ATOM 4626 C CG . PRO A 1 672 ? -38.495 -52.911 91.735 1.00 143.94 ? 672 PRO A CG 1 ATOM 4627 C CD . PRO A 1 672 ? -37.141 -52.928 91.022 1.00 131.82 ? 672 PRO A CD 1 ATOM 4628 N N . PHE A 1 673 ? -38.873 -57.010 91.548 1.00 130.89 ? 673 PHE A N 1 ATOM 4629 C CA . PHE A 1 673 ? -39.045 -58.443 91.694 1.00 128.99 ? 673 PHE A CA 1 ATOM 4630 C C . PHE A 1 673 ? -39.197 -59.160 90.358 1.00 136.08 ? 673 PHE A C 1 ATOM 4631 O O . PHE A 1 673 ? -39.929 -60.136 90.203 1.00 127.20 ? 673 PHE A O 1 ATOM 4632 C CB . PHE A 1 673 ? -40.086 -58.762 92.771 1.00 128.63 ? 673 PHE A CB 1 ATOM 4633 C CG . PHE A 1 673 ? -39.908 -57.947 94.037 1.00 134.39 ? 673 PHE A CG 1 ATOM 4634 C CD1 . PHE A 1 673 ? -38.654 -57.837 94.652 1.00 142.80 ? 673 PHE A CD1 1 ATOM 4635 C CD2 . PHE A 1 673 ? -40.975 -57.257 94.596 1.00 133.83 ? 673 PHE A CD2 1 ATOM 4636 C CE1 . PHE A 1 673 ? -38.473 -57.074 95.804 1.00 143.53 ? 673 PHE A CE1 1 ATOM 4637 C CE2 . PHE A 1 673 ? -40.804 -56.502 95.750 1.00 137.14 ? 673 PHE A CE2 1 ATOM 4638 C CZ . PHE A 1 673 ? -39.552 -56.407 96.355 1.00 141.13 ? 673 PHE A CZ 1 ATOM 4639 N N . SER A 1 674 ? -38.451 -58.646 89.390 1.00 159.69 ? 674 SER A N 1 ATOM 4640 C CA . SER A 1 674 ? -38.141 -59.390 88.180 1.00 166.01 ? 674 SER A CA 1 ATOM 4641 C C . SER A 1 674 ? -36.837 -60.204 88.358 1.00 143.01 ? 674 SER A C 1 ATOM 4642 O O . SER A 1 674 ? -36.010 -59.934 89.248 1.00 114.15 ? 674 SER A O 1 ATOM 4643 C CB . SER A 1 674 ? -38.095 -58.468 86.937 1.00 179.95 ? 674 SER A CB 1 ATOM 4644 O OG . SER A 1 674 ? -37.192 -57.375 87.083 1.00 162.97 ? 674 SER A OG 1 ATOM 4645 N N . GLY A 1 675 ? -36.699 -61.225 87.521 1.00 132.53 ? 675 GLY A N 1 ATOM 4646 C CA . GLY A 1 675 ? -35.501 -62.037 87.455 1.00 128.89 ? 675 GLY A CA 1 ATOM 4647 C C . GLY A 1 675 ? -35.293 -62.390 86.001 1.00 139.89 ? 675 GLY A C 1 ATOM 4648 O O . GLY A 1 675 ? -36.149 -63.022 85.368 1.00 158.08 ? 675 GLY A O 1 ATOM 4649 N N . GLU A 1 676 ? -34.169 -61.958 85.449 1.00 134.20 ? 676 GLU A N 1 ATOM 4650 C CA . GLU A 1 676 ? -33.902 -62.240 84.055 1.00 128.93 ? 676 GLU A CA 1 ATOM 4651 C C . GLU A 1 676 ? -32.743 -63.208 83.848 1.00 118.52 ? 676 GLU A C 1 ATOM 4652 O O . GLU A 1 676 ? -31.778 -63.244 84.608 1.00 105.88 ? 676 GLU A O 1 ATOM 4653 C CB . GLU A 1 676 ? -33.817 -60.961 83.193 1.00 140.14 ? 676 GLU A CB 1 ATOM 4654 C CG . GLU A 1 676 ? -35.120 -60.639 82.467 1.00 148.50 ? 676 GLU A CG 1 ATOM 4655 C CD . GLU A 1 676 ? -35.975 -61.890 82.223 1.00 182.41 ? 676 GLU A CD 1 ATOM 4656 O OE1 . GLU A 1 676 ? -35.547 -62.827 81.486 1.00 173.42 ? 676 GLU A OE1 1 ATOM 4657 O OE2 . GLU A 1 676 ? -37.090 -61.941 82.791 1.00 206.44 ? 676 GLU A OE2 1 ATOM 4658 N N . THR A 1 677 ? -32.866 -63.981 82.784 1.00 125.77 ? 677 THR A N 1 ATOM 4659 C CA . THR A 1 677 ? -32.054 -65.161 82.560 1.00 124.72 ? 677 THR A CA 1 ATOM 4660 C C . THR A 1 677 ? -31.172 -65.009 81.294 1.00 121.23 ? 677 THR A C 1 ATOM 4661 O O . THR A 1 677 ? -31.712 -64.804 80.190 1.00 123.34 ? 677 THR A O 1 ATOM 4662 C CB . THR A 1 677 ? -33.022 -66.360 82.500 1.00 126.54 ? 677 THR A CB 1 ATOM 4663 O OG1 . THR A 1 677 ? -32.385 -67.489 81.906 1.00 111.03 ? 677 THR A OG1 1 ATOM 4664 C CG2 . THR A 1 677 ? -34.326 -65.976 81.735 1.00 127.54 ? 677 THR A CG2 1 ATOM 4665 N N . VAL A 1 678 ? -29.836 -65.087 81.465 1.00 112.22 ? 678 VAL A N 1 ATOM 4666 C CA . VAL A 1 678 ? -28.829 -64.709 80.409 1.00 111.72 ? 678 VAL A CA 1 ATOM 4667 C C . VAL A 1 678 ? -27.814 -65.787 80.000 1.00 105.02 ? 678 VAL A C 1 ATOM 4668 O O . VAL A 1 678 ? -27.766 -66.840 80.602 1.00 113.73 ? 678 VAL A O 1 ATOM 4669 C CB . VAL A 1 678 ? -27.967 -63.496 80.821 1.00 113.14 ? 678 VAL A CB 1 ATOM 4670 C CG1 . VAL A 1 678 ? -28.814 -62.260 81.134 1.00 111.11 ? 678 VAL A CG1 1 ATOM 4671 C CG2 . VAL A 1 678 ? -27.057 -63.882 81.977 1.00 113.88 ? 678 VAL A CG2 1 ATOM 4672 N N . PHE A 1 679 ? -26.957 -65.498 79.024 1.00 100.49 ? 679 PHE A N 1 ATOM 4673 C CA . PHE A 1 679 ? -26.116 -66.549 78.459 1.00 111.03 ? 679 PHE A CA 1 ATOM 4674 C C . PHE A 1 679 ? -24.650 -66.204 78.119 1.00 121.45 ? 679 PHE A C 1 ATOM 4675 O O . PHE A 1 679 ? -24.368 -65.407 77.222 1.00 132.24 ? 679 PHE A O 1 ATOM 4676 C CB . PHE A 1 679 ? -26.837 -67.081 77.245 1.00 117.46 ? 679 PHE A CB 1 ATOM 4677 C CG . PHE A 1 679 ? -26.112 -68.172 76.515 1.00 135.65 ? 679 PHE A CG 1 ATOM 4678 C CD1 . PHE A 1 679 ? -26.139 -69.478 76.983 1.00 125.08 ? 679 PHE A CD1 1 ATOM 4679 C CD2 . PHE A 1 679 ? -25.446 -67.894 75.310 1.00 157.66 ? 679 PHE A CD2 1 ATOM 4680 C CE1 . PHE A 1 679 ? -25.505 -70.484 76.287 1.00 129.65 ? 679 PHE A CE1 1 ATOM 4681 C CE2 . PHE A 1 679 ? -24.801 -68.896 74.605 1.00 163.78 ? 679 PHE A CE2 1 ATOM 4682 C CZ . PHE A 1 679 ? -24.836 -70.193 75.100 1.00 155.31 ? 679 PHE A CZ 1 ATOM 4683 N N . MET A 1 680 ? -23.717 -66.860 78.801 1.00 127.57 ? 680 MET A N 1 ATOM 4684 C CA . MET A 1 680 ? -22.314 -66.470 78.739 1.00 138.20 ? 680 MET A CA 1 ATOM 4685 C C . MET A 1 680 ? -21.490 -67.285 77.778 1.00 154.53 ? 680 MET A C 1 ATOM 4686 O O . MET A 1 680 ? -20.876 -68.278 78.174 1.00 154.55 ? 680 MET A O 1 ATOM 4687 C CB . MET A 1 680 ? -21.678 -66.563 80.121 1.00 143.65 ? 680 MET A CB 1 ATOM 4688 C CG . MET A 1 680 ? -22.363 -65.703 81.166 1.00 150.43 ? 680 MET A CG 1 ATOM 4689 S SD . MET A 1 680 ? -21.729 -64.032 81.315 1.00 147.60 ? 680 MET A SD 1 ATOM 4690 C CE . MET A 1 680 ? -21.272 -63.647 79.622 1.00 156.58 ? 680 MET A CE 1 ATOM 4691 N N . SER A 1 681 ? -21.468 -66.874 76.515 1.00 173.74 ? 681 SER A N 1 ATOM 4692 C CA . SER A 1 681 ? -20.407 -67.337 75.654 1.00 180.85 ? 681 SER A CA 1 ATOM 4693 C C . SER A 1 681 ? -19.214 -66.817 76.445 1.00 174.12 ? 681 SER A C 1 ATOM 4694 O O . SER A 1 681 ? -19.061 -65.590 76.599 1.00 175.24 ? 681 SER A O 1 ATOM 4695 C CB . SER A 1 681 ? -20.520 -66.692 74.280 1.00 192.11 ? 681 SER A CB 1 ATOM 4696 O OG . SER A 1 681 ? -19.513 -67.189 73.422 1.00 207.66 ? 681 SER A OG 1 ATOM 4697 N N . MET A 1 682 ? -18.427 -67.735 77.018 1.00 153.00 ? 682 MET A N 1 ATOM 4698 C CA . MET A 1 682 ? -17.546 -67.357 78.143 1.00 146.51 ? 682 MET A CA 1 ATOM 4699 C C . MET A 1 682 ? -16.077 -67.790 78.128 1.00 150.01 ? 682 MET A C 1 ATOM 4700 O O . MET A 1 682 ? -15.597 -68.444 79.067 1.00 133.58 ? 682 MET A O 1 ATOM 4701 C CB . MET A 1 682 ? -18.158 -67.795 79.457 1.00 138.46 ? 682 MET A CB 1 ATOM 4702 C CG . MET A 1 682 ? -17.199 -67.661 80.615 1.00 136.47 ? 682 MET A CG 1 ATOM 4703 S SD . MET A 1 682 ? -18.148 -67.276 82.074 1.00 153.82 ? 682 MET A SD 1 ATOM 4704 C CE . MET A 1 682 ? -18.690 -65.619 81.691 1.00 137.48 ? 682 MET A CE 1 ATOM 4705 N N . GLU A 1 683 ? -15.358 -67.356 77.098 1.00 159.85 ? 683 GLU A N 1 ATOM 4706 C CA . GLU A 1 683 ? -13.986 -67.780 76.878 1.00 168.38 ? 683 GLU A CA 1 ATOM 4707 C C . GLU A 1 683 ? -12.960 -66.677 77.164 1.00 172.82 ? 683 GLU A C 1 ATOM 4708 O O . GLU A 1 683 ? -11.838 -66.743 76.678 1.00 197.71 ? 683 GLU A O 1 ATOM 4709 C CB . GLU A 1 683 ? -13.830 -68.382 75.461 1.00 178.72 ? 683 GLU A CB 1 ATOM 4710 C CG . GLU A 1 683 ? -13.877 -67.422 74.268 1.00 203.19 ? 683 GLU A CG 1 ATOM 4711 C CD . GLU A 1 683 ? -15.178 -66.626 74.132 1.00 218.22 ? 683 GLU A CD 1 ATOM 4712 O OE1 . GLU A 1 683 ? -15.479 -65.804 75.030 1.00 211.82 ? 683 GLU A OE1 1 ATOM 4713 O OE2 . GLU A 1 683 ? -15.893 -66.801 73.111 1.00 235.88 ? 683 GLU A OE2 1 ATOM 4714 N N . ASN A 1 684 ? -13.325 -65.690 77.981 1.00 170.98 ? 684 ASN A N 1 ATOM 4715 C CA . ASN A 1 684 ? -12.419 -64.567 78.307 1.00 170.14 ? 684 ASN A CA 1 ATOM 4716 C C . ASN A 1 684 ? -11.802 -64.596 79.736 1.00 169.60 ? 684 ASN A C 1 ATOM 4717 O O . ASN A 1 684 ? -12.490 -64.259 80.703 1.00 164.91 ? 684 ASN A O 1 ATOM 4718 C CB . ASN A 1 684 ? -13.144 -63.236 78.061 1.00 161.49 ? 684 ASN A CB 1 ATOM 4719 C CG . ASN A 1 684 ? -12.206 -62.048 78.045 1.00 160.20 ? 684 ASN A CG 1 ATOM 4720 O OD1 . ASN A 1 684 ? -11.011 -62.185 77.775 1.00 159.75 ? 684 ASN A OD1 1 ATOM 4721 N ND2 . ASN A 1 684 ? -12.748 -60.865 78.319 1.00 156.50 ? 684 ASN A ND2 1 ATOM 4722 N N . PRO A 1 685 ? -10.495 -64.957 79.859 1.00 165.09 ? 685 PRO A N 1 ATOM 4723 C CA . PRO A 1 685 ? -9.757 -65.218 81.118 1.00 165.17 ? 685 PRO A CA 1 ATOM 4724 C C . PRO A 1 685 ? -9.497 -63.987 81.990 1.00 178.97 ? 685 PRO A C 1 ATOM 4725 O O . PRO A 1 685 ? -9.678 -62.861 81.530 1.00 197.11 ? 685 PRO A O 1 ATOM 4726 C CB . PRO A 1 685 ? -8.405 -65.693 80.611 1.00 161.93 ? 685 PRO A CB 1 ATOM 4727 C CG . PRO A 1 685 ? -8.217 -64.919 79.357 1.00 159.84 ? 685 PRO A CG 1 ATOM 4728 C CD . PRO A 1 685 ? -9.573 -64.959 78.707 1.00 158.19 ? 685 PRO A CD 1 ATOM 4729 N N . GLY A 1 686 ? -9.034 -64.210 83.223 1.00 183.78 ? 686 GLY A N 1 ATOM 4730 C CA . GLY A 1 686 ? -8.679 -63.122 84.157 1.00 178.65 ? 686 GLY A CA 1 ATOM 4731 C C . GLY A 1 686 ? -9.618 -63.002 85.352 1.00 167.80 ? 686 GLY A C 1 ATOM 4732 O O . GLY A 1 686 ? -10.580 -63.767 85.472 1.00 166.24 ? 686 GLY A O 1 ATOM 4733 N N . LEU A 1 687 ? -9.337 -62.063 86.255 1.00 160.31 ? 687 LEU A N 1 ATOM 4734 C CA . LEU A 1 687 ? -10.275 -61.800 87.344 1.00 156.12 ? 687 LEU A CA 1 ATOM 4735 C C . LEU A 1 687 ? -11.190 -60.675 86.988 1.00 160.04 ? 687 LEU A C 1 ATOM 4736 O O . LEU A 1 687 ? -10.760 -59.526 86.818 1.00 184.54 ? 687 LEU A O 1 ATOM 4737 C CB . LEU A 1 687 ? -9.604 -61.478 88.677 1.00 158.05 ? 687 LEU A CB 1 ATOM 4738 C CG . LEU A 1 687 ? -9.842 -62.432 89.865 1.00 157.97 ? 687 LEU A CG 1 ATOM 4739 C CD1 . LEU A 1 687 ? -10.136 -61.627 91.119 1.00 154.61 ? 687 LEU A CD1 1 ATOM 4740 C CD2 . LEU A 1 687 ? -10.952 -63.448 89.649 1.00 155.34 ? 687 LEU A CD2 1 ATOM 4741 N N . TRP A 1 688 ? -12.465 -61.015 86.900 1.00 151.70 ? 688 TRP A N 1 ATOM 4742 C CA . TRP A 1 688 ? -13.465 -60.055 86.524 1.00 151.06 ? 688 TRP A CA 1 ATOM 4743 C C . TRP A 1 688 ? -14.393 -59.770 87.680 1.00 146.60 ? 688 TRP A C 1 ATOM 4744 O O . TRP A 1 688 ? -14.924 -60.681 88.321 1.00 144.17 ? 688 TRP A O 1 ATOM 4745 C CB . TRP A 1 688 ? -14.196 -60.540 85.286 1.00 153.21 ? 688 TRP A CB 1 ATOM 4746 C CG . TRP A 1 688 ? -13.225 -60.791 84.180 1.00 164.54 ? 688 TRP A CG 1 ATOM 4747 C CD1 . TRP A 1 688 ? -12.829 -62.002 83.704 1.00 170.97 ? 688 TRP A CD1 1 ATOM 4748 C CD2 . TRP A 1 688 ? -12.483 -59.805 83.438 1.00 171.95 ? 688 TRP A CD2 1 ATOM 4749 N NE1 . TRP A 1 688 ? -11.906 -61.837 82.694 1.00 178.01 ? 688 TRP A NE1 1 ATOM 4750 C CE2 . TRP A 1 688 ? -11.676 -60.499 82.513 1.00 175.38 ? 688 TRP A CE2 1 ATOM 4751 C CE3 . TRP A 1 688 ? -12.430 -58.406 83.459 1.00 175.56 ? 688 TRP A CE3 1 ATOM 4752 C CZ2 . TRP A 1 688 ? -10.828 -59.841 81.617 1.00 174.58 ? 688 TRP A CZ2 1 ATOM 4753 C CZ3 . TRP A 1 688 ? -11.584 -57.754 82.562 1.00 180.03 ? 688 TRP A CZ3 1 ATOM 4754 C CH2 . TRP A 1 688 ? -10.799 -58.473 81.661 1.00 175.00 ? 688 TRP A CH2 1 ATOM 4755 N N . ILE A 1 689 ? -14.541 -58.482 87.950 1.00 140.24 ? 689 ILE A N 1 ATOM 4756 C CA . ILE A 1 689 ? -15.312 -57.989 89.071 1.00 136.48 ? 689 ILE A CA 1 ATOM 4757 C C . ILE A 1 689 ? -16.787 -57.909 88.653 1.00 130.17 ? 689 ILE A C 1 ATOM 4758 O O . ILE A 1 689 ? -17.196 -57.001 87.955 1.00 131.10 ? 689 ILE A O 1 ATOM 4759 C CB . ILE A 1 689 ? -14.664 -56.664 89.603 1.00 152.14 ? 689 ILE A CB 1 ATOM 4760 C CG1 . ILE A 1 689 ? -15.579 -55.890 90.586 1.00 157.76 ? 689 ILE A CG1 1 ATOM 4761 C CG2 . ILE A 1 689 ? -14.052 -55.836 88.452 1.00 150.93 ? 689 ILE A CG2 1 ATOM 4762 C CD1 . ILE A 1 689 ? -14.848 -55.055 91.645 1.00 164.83 ? 689 ILE A CD1 1 ATOM 4763 N N . LEU A 1 690 ? -17.569 -58.919 89.018 1.00 137.92 ? 690 LEU A N 1 ATOM 4764 C CA . LEU A 1 690 ? -19.009 -58.906 88.742 1.00 137.31 ? 690 LEU A CA 1 ATOM 4765 C C . LEU A 1 690 ? -19.698 -58.192 89.885 1.00 139.78 ? 690 LEU A C 1 ATOM 4766 O O . LEU A 1 690 ? -19.801 -58.714 91.001 1.00 141.75 ? 690 LEU A O 1 ATOM 4767 C CB . LEU A 1 690 ? -19.585 -60.322 88.567 1.00 137.21 ? 690 LEU A CB 1 ATOM 4768 C CG . LEU A 1 690 ? -21.049 -60.554 88.986 1.00 134.03 ? 690 LEU A CG 1 ATOM 4769 C CD1 . LEU A 1 690 ? -22.020 -59.728 88.139 1.00 130.61 ? 690 LEU A CD1 1 ATOM 4770 C CD2 . LEU A 1 690 ? -21.411 -62.035 88.984 1.00 124.46 ? 690 LEU A CD2 1 ATOM 4771 N N . GLY A 1 691 ? -20.148 -56.982 89.597 1.00 143.51 ? 691 GLY A N 1 ATOM 4772 C CA . GLY A 1 691 ? -20.880 -56.182 90.558 1.00 146.16 ? 691 GLY A CA 1 ATOM 4773 C C . GLY A 1 691 ? -22.077 -55.667 89.816 1.00 148.96 ? 691 GLY A C 1 ATOM 4774 O O . GLY A 1 691 ? -22.733 -56.421 89.085 1.00 153.20 ? 691 GLY A O 1 ATOM 4775 N N . CYS A 1 692 ? -22.358 -54.384 89.993 1.00 145.29 ? 692 CYS A N 1 ATOM 4776 C CA . CYS A 1 692 ? -23.354 -53.719 89.176 1.00 150.74 ? 692 CYS A CA 1 ATOM 4777 C C . CYS A 1 692 ? -22.851 -52.338 88.878 1.00 159.08 ? 692 CYS A C 1 ATOM 4778 O O . CYS A 1 692 ? -22.284 -51.691 89.755 1.00 156.39 ? 692 CYS A O 1 ATOM 4779 C CB . CYS A 1 692 ? -24.730 -53.671 89.857 1.00 144.31 ? 692 CYS A CB 1 ATOM 4780 S SG . CYS A 1 692 ? -24.800 -52.998 91.534 1.00 142.23 ? 692 CYS A SG 1 ATOM 4781 N N . HIS A 1 693 ? -23.027 -51.880 87.641 1.00 180.51 ? 693 HIS A N 1 ATOM 4782 C CA . HIS A 1 693 ? -22.628 -50.505 87.367 1.00 200.07 ? 693 HIS A CA 1 ATOM 4783 C C . HIS A 1 693 ? -23.666 -49.451 87.794 1.00 199.67 ? 693 HIS A C 1 ATOM 4784 O O . HIS A 1 693 ? -23.926 -48.458 87.114 1.00 225.71 ? 693 HIS A O 1 ATOM 4785 C CB . HIS A 1 693 ? -21.796 -50.297 86.056 1.00 217.76 ? 693 HIS A CB 1 ATOM 4786 C CG . HIS A 1 693 ? -22.562 -49.921 84.820 1.00 227.67 ? 693 HIS A CG 1 ATOM 4787 N ND1 . HIS A 1 693 ? -22.203 -50.392 83.573 1.00 230.30 ? 693 HIS A ND1 1 ATOM 4788 C CD2 . HIS A 1 693 ? -23.588 -49.059 84.614 1.00 237.39 ? 693 HIS A CD2 1 ATOM 4789 C CE1 . HIS A 1 693 ? -23.000 -49.868 82.659 1.00 247.61 ? 693 HIS A CE1 1 ATOM 4790 N NE2 . HIS A 1 693 ? -23.852 -49.059 83.265 1.00 254.46 ? 693 HIS A NE2 1 ATOM 4791 N N . ASN A 1 694 ? -24.266 -49.736 88.951 1.00 183.28 ? 694 ASN A N 1 ATOM 4792 C CA . ASN A 1 694 ? -24.674 -48.711 89.888 1.00 183.28 ? 694 ASN A CA 1 ATOM 4793 C C . ASN A 1 694 ? -23.403 -48.546 90.701 1.00 194.11 ? 694 ASN A C 1 ATOM 4794 O O . ASN A 1 694 ? -22.837 -49.542 91.142 1.00 197.32 ? 694 ASN A O 1 ATOM 4795 C CB . ASN A 1 694 ? -25.793 -49.193 90.820 1.00 181.58 ? 694 ASN A CB 1 ATOM 4796 C CG . ASN A 1 694 ? -26.962 -49.837 90.085 1.00 197.13 ? 694 ASN A CG 1 ATOM 4797 O OD1 . ASN A 1 694 ? -26.780 -50.584 89.122 1.00 203.36 ? 694 ASN A OD1 1 ATOM 4798 N ND2 . ASN A 1 694 ? -28.178 -49.575 90.570 1.00 195.57 ? 694 ASN A ND2 1 ATOM 4799 N N . SER A 1 695 ? -22.918 -47.319 90.872 1.00 214.49 ? 695 SER A N 1 ATOM 4800 C CA . SER A 1 695 ? -21.723 -47.100 91.708 1.00 216.66 ? 695 SER A CA 1 ATOM 4801 C C . SER A 1 695 ? -22.032 -46.424 93.057 1.00 217.05 ? 695 SER A C 1 ATOM 4802 O O . SER A 1 695 ? -21.152 -46.228 93.896 1.00 221.00 ? 695 SER A O 1 ATOM 4803 C CB . SER A 1 695 ? -20.591 -46.417 90.928 1.00 208.83 ? 695 SER A CB 1 ATOM 4804 O OG . SER A 1 695 ? -19.764 -47.392 90.301 1.00 188.18 ? 695 SER A OG 1 ATOM 4805 N N . ASP A 1 696 ? -23.299 -46.074 93.240 1.00 212.52 ? 696 ASP A N 1 ATOM 4806 C CA . ASP A 1 696 ? -23.901 -45.926 94.554 1.00 201.93 ? 696 ASP A CA 1 ATOM 4807 C C . ASP A 1 696 ? -23.591 -47.194 95.385 1.00 186.44 ? 696 ASP A C 1 ATOM 4808 O O . ASP A 1 696 ? -22.589 -47.225 96.099 1.00 177.48 ? 696 ASP A O 1 ATOM 4809 C CB . ASP A 1 696 ? -25.416 -45.712 94.395 1.00 218.33 ? 696 ASP A CB 1 ATOM 4810 C CG . ASP A 1 696 ? -25.995 -46.401 93.120 1.00 231.50 ? 696 ASP A CG 1 ATOM 4811 O OD1 . ASP A 1 696 ? -25.380 -46.300 92.031 1.00 228.74 ? 696 ASP A OD1 1 ATOM 4812 O OD2 . ASP A 1 696 ? -27.078 -47.033 93.196 1.00 225.79 ? 696 ASP A OD2 1 ATOM 4813 N N . PHE A 1 697 ? -24.418 -48.239 95.254 1.00 168.86 ? 697 PHE A N 1 ATOM 4814 C CA . PHE A 1 697 ? -24.293 -49.466 96.057 1.00 157.90 ? 697 PHE A CA 1 ATOM 4815 C C . PHE A 1 697 ? -22.863 -49.981 96.093 1.00 157.88 ? 697 PHE A C 1 ATOM 4816 O O . PHE A 1 697 ? -22.264 -50.012 97.151 1.00 162.58 ? 697 PHE A O 1 ATOM 4817 C CB . PHE A 1 697 ? -25.242 -50.610 95.595 1.00 153.77 ? 697 PHE A CB 1 ATOM 4818 C CG . PHE A 1 697 ? -26.704 -50.230 95.541 1.00 162.79 ? 697 PHE A CG 1 ATOM 4819 C CD1 . PHE A 1 697 ? -27.394 -49.846 96.690 1.00 171.95 ? 697 PHE A CD1 1 ATOM 4820 C CD2 . PHE A 1 697 ? -27.403 -50.262 94.328 1.00 174.69 ? 697 PHE A CD2 1 ATOM 4821 C CE1 . PHE A 1 697 ? -28.742 -49.484 96.625 1.00 179.14 ? 697 PHE A CE1 1 ATOM 4822 C CE2 . PHE A 1 697 ? -28.751 -49.895 94.254 1.00 170.38 ? 697 PHE A CE2 1 ATOM 4823 C CZ . PHE A 1 697 ? -29.421 -49.509 95.405 1.00 170.48 ? 697 PHE A CZ 1 ATOM 4824 N N . ARG A 1 698 ? -22.310 -50.321 94.929 1.00 162.10 ? 698 ARG A N 1 ATOM 4825 C CA . ARG A 1 698 ? -21.186 -51.280 94.820 1.00 168.83 ? 698 ARG A CA 1 ATOM 4826 C C . ARG A 1 698 ? -19.886 -50.992 95.598 1.00 177.07 ? 698 ARG A C 1 ATOM 4827 O O . ARG A 1 698 ? -18.849 -51.623 95.346 1.00 184.36 ? 698 ARG A O 1 ATOM 4828 C CB . ARG A 1 698 ? -20.895 -51.656 93.351 1.00 172.19 ? 698 ARG A CB 1 ATOM 4829 C CG . ARG A 1 698 ? -20.081 -50.646 92.556 1.00 181.94 ? 698 ARG A CG 1 ATOM 4830 C CD . ARG A 1 698 ? -19.404 -51.321 91.378 1.00 189.48 ? 698 ARG A CD 1 ATOM 4831 N NE . ARG A 1 698 ? -18.126 -50.693 91.045 1.00 211.26 ? 698 ARG A NE 1 ATOM 4832 C CZ . ARG A 1 698 ? -16.930 -51.114 91.468 1.00 221.95 ? 698 ARG A CZ 1 ATOM 4833 N NH1 . ARG A 1 698 ? -16.811 -52.184 92.265 1.00 198.63 ? 698 ARG A NH1 1 ATOM 4834 N NH2 . ARG A 1 698 ? -15.841 -50.450 91.090 1.00 239.19 ? 698 ARG A NH2 1 ATOM 4835 N N . ASN A 1 699 ? -19.946 -50.055 96.540 1.00 175.25 ? 699 ASN A N 1 ATOM 4836 C CA . ASN A 1 699 ? -18.922 -49.941 97.577 1.00 171.93 ? 699 ASN A CA 1 ATOM 4837 C C . ASN A 1 699 ? -19.567 -49.771 98.948 1.00 172.55 ? 699 ASN A C 1 ATOM 4838 O O . ASN A 1 699 ? -18.986 -49.171 99.849 1.00 185.67 ? 699 ASN A O 1 ATOM 4839 C CB . ASN A 1 699 ? -17.940 -48.807 97.279 1.00 176.47 ? 699 ASN A CB 1 ATOM 4840 C CG . ASN A 1 699 ? -18.618 -47.459 97.167 1.00 175.33 ? 699 ASN A CG 1 ATOM 4841 O OD1 . ASN A 1 699 ? -19.699 -47.337 96.577 1.00 164.01 ? 699 ASN A OD1 1 ATOM 4842 N ND2 . ASN A 1 699 ? -17.982 -46.432 97.730 1.00 181.35 ? 699 ASN A ND2 1 ATOM 4843 N N . ARG A 1 700 ? -20.796 -50.271 99.062 1.00 166.10 ? 700 ARG A N 1 ATOM 4844 C CA . ARG A 1 700 ? -21.470 -50.517 100.332 1.00 164.33 ? 700 ARG A CA 1 ATOM 4845 C C . ARG A 1 700 ? -21.485 -52.060 100.472 1.00 164.05 ? 700 ARG A C 1 ATOM 4846 O O . ARG A 1 700 ? -22.380 -52.647 101.105 1.00 168.65 ? 700 ARG A O 1 ATOM 4847 C CB . ARG A 1 700 ? -22.899 -49.940 100.310 1.00 165.89 ? 700 ARG A CB 1 ATOM 4848 C CG . ARG A 1 700 ? -23.013 -48.423 100.161 1.00 174.54 ? 700 ARG A CG 1 ATOM 4849 C CD . ARG A 1 700 ? -24.425 -47.977 99.766 1.00 186.75 ? 700 ARG A CD 1 ATOM 4850 N NE . ARG A 1 700 ? -24.671 -46.552 100.044 1.00 217.58 ? 700 ARG A NE 1 ATOM 4851 C CZ . ARG A 1 700 ? -24.836 -45.588 99.127 1.00 238.72 ? 700 ARG A CZ 1 ATOM 4852 N NH1 . ARG A 1 700 ? -24.797 -45.854 97.826 1.00 241.79 ? 700 ARG A NH1 1 ATOM 4853 N NH2 . ARG A 1 700 ? -25.050 -44.334 99.517 1.00 243.54 ? 700 ARG A NH2 1 ATOM 4854 N N . GLY A 1 701 ? -20.455 -52.688 99.892 1.00 155.98 ? 701 GLY A N 1 ATOM 4855 C CA . GLY A 1 701 ? -20.458 -54.109 99.538 1.00 144.78 ? 701 GLY A CA 1 ATOM 4856 C C . GLY A 1 701 ? -21.077 -54.168 98.156 1.00 144.14 ? 701 GLY A C 1 ATOM 4857 O O . GLY A 1 701 ? -21.182 -53.141 97.485 1.00 140.71 ? 701 GLY A O 1 ATOM 4858 N N . MET A 1 702 ? -21.502 -55.354 97.732 1.00 146.11 ? 702 MET A N 1 ATOM 4859 C CA . MET A 1 702 ? -22.287 -55.530 96.484 1.00 144.85 ? 702 MET A CA 1 ATOM 4860 C C . MET A 1 702 ? -21.415 -55.771 95.253 1.00 139.43 ? 702 MET A C 1 ATOM 4861 O O . MET A 1 702 ? -21.677 -55.240 94.164 1.00 140.49 ? 702 MET A O 1 ATOM 4862 C CB . MET A 1 702 ? -23.316 -54.396 96.235 1.00 142.30 ? 702 MET A CB 1 ATOM 4863 C CG . MET A 1 702 ? -24.254 -54.646 95.057 1.00 138.82 ? 702 MET A CG 1 ATOM 4864 S SD . MET A 1 702 ? -25.810 -55.445 95.482 1.00 138.21 ? 702 MET A SD 1 ATOM 4865 C CE . MET A 1 702 ? -26.874 -54.023 95.276 1.00 150.56 ? 702 MET A CE 1 ATOM 4866 N N . THR A 1 703 ? -20.370 -56.565 95.427 1.00 129.43 ? 703 THR A N 1 ATOM 4867 C CA . THR A 1 703 ? -19.670 -57.089 94.278 1.00 133.19 ? 703 THR A CA 1 ATOM 4868 C C . THR A 1 703 ? -19.095 -58.441 94.606 1.00 145.82 ? 703 THR A C 1 ATOM 4869 O O . THR A 1 703 ? -18.882 -58.780 95.778 1.00 157.05 ? 703 THR A O 1 ATOM 4870 C CB . THR A 1 703 ? -18.515 -56.195 93.831 1.00 136.76 ? 703 THR A CB 1 ATOM 4871 O OG1 . THR A 1 703 ? -17.677 -55.926 94.958 1.00 150.52 ? 703 THR A OG1 1 ATOM 4872 C CG2 . THR A 1 703 ? -19.022 -54.892 93.228 1.00 141.43 ? 703 THR A CG2 1 ATOM 4873 N N . ALA A 1 704 ? -18.854 -59.203 93.545 1.00 145.99 ? 704 ALA A N 1 ATOM 4874 C CA . ALA A 1 704 ? -18.175 -60.477 93.618 1.00 137.90 ? 704 ALA A CA 1 ATOM 4875 C C . ALA A 1 704 ? -17.103 -60.508 92.527 1.00 137.62 ? 704 ALA A C 1 ATOM 4876 O O . ALA A 1 704 ? -17.051 -59.622 91.669 1.00 134.89 ? 704 ALA A O 1 ATOM 4877 C CB . ALA A 1 704 ? -19.178 -61.592 93.431 1.00 128.90 ? 704 ALA A CB 1 ATOM 4878 N N . LEU A 1 705 ? -16.231 -61.507 92.574 1.00 141.99 ? 705 LEU A N 1 ATOM 4879 C CA . LEU A 1 705 ? -15.226 -61.675 91.530 1.00 148.04 ? 705 LEU A CA 1 ATOM 4880 C C . LEU A 1 705 ? -15.459 -62.988 90.791 1.00 149.28 ? 705 LEU A C 1 ATOM 4881 O O . LEU A 1 705 ? -16.037 -63.923 91.347 1.00 162.66 ? 705 LEU A O 1 ATOM 4882 C CB . LEU A 1 705 ? -13.811 -61.585 92.111 1.00 163.18 ? 705 LEU A CB 1 ATOM 4883 C CG . LEU A 1 705 ? -13.582 -60.299 92.924 1.00 177.47 ? 705 LEU A CG 1 ATOM 4884 C CD1 . LEU A 1 705 ? -13.804 -60.604 94.394 1.00 183.74 ? 705 LEU A CD1 1 ATOM 4885 C CD2 . LEU A 1 705 ? -12.216 -59.645 92.717 1.00 184.20 ? 705 LEU A CD2 1 ATOM 4886 N N . LEU A 1 706 ? -15.025 -63.049 89.535 1.00 140.08 ? 706 LEU A N 1 ATOM 4887 C CA . LEU A 1 706 ? -15.288 -64.198 88.679 1.00 135.59 ? 706 LEU A CA 1 ATOM 4888 C C . LEU A 1 706 ? -14.000 -64.635 87.989 1.00 144.88 ? 706 LEU A C 1 ATOM 4889 O O . LEU A 1 706 ? -13.513 -63.926 87.103 1.00 155.71 ? 706 LEU A O 1 ATOM 4890 C CB . LEU A 1 706 ? -16.319 -63.778 87.642 1.00 130.66 ? 706 LEU A CB 1 ATOM 4891 C CG . LEU A 1 706 ? -16.997 -64.728 86.665 1.00 129.52 ? 706 LEU A CG 1 ATOM 4892 C CD1 . LEU A 1 706 ? -18.068 -63.903 85.988 1.00 133.80 ? 706 LEU A CD1 1 ATOM 4893 C CD2 . LEU A 1 706 ? -16.068 -65.315 85.615 1.00 129.53 ? 706 LEU A CD2 1 ATOM 4894 N N . LYS A 1 707 ? -13.438 -65.779 88.389 1.00 146.77 ? 707 LYS A N 1 ATOM 4895 C CA . LYS A 1 707 ? -12.211 -66.267 87.751 1.00 157.58 ? 707 LYS A CA 1 ATOM 4896 C C . LYS A 1 707 ? -12.536 -67.248 86.633 1.00 162.87 ? 707 LYS A C 1 ATOM 4897 O O . LYS A 1 707 ? -13.337 -68.178 86.812 1.00 161.24 ? 707 LYS A O 1 ATOM 4898 C CB . LYS A 1 707 ? -11.215 -66.872 88.757 1.00 169.17 ? 707 LYS A CB 1 ATOM 4899 C CG . LYS A 1 707 ? -9.806 -67.076 88.184 1.00 183.90 ? 707 LYS A CG 1 ATOM 4900 C CD . LYS A 1 707 ? -8.786 -67.673 89.164 1.00 197.78 ? 707 LYS A CD 1 ATOM 4901 C CE . LYS A 1 707 ? -9.068 -69.124 89.572 1.00 209.16 ? 707 LYS A CE 1 ATOM 4902 N NZ . LYS A 1 707 ? -9.377 -70.082 88.464 1.00 210.28 ? 707 LYS A NZ 1 ATOM 4903 N N . VAL A 1 708 ? -11.911 -67.011 85.480 1.00 160.89 ? 708 VAL A N 1 ATOM 4904 C CA . VAL A 1 708 ? -12.089 -67.834 84.289 1.00 156.19 ? 708 VAL A CA 1 ATOM 4905 C C . VAL A 1 708 ? -10.735 -68.439 83.953 1.00 158.91 ? 708 VAL A C 1 ATOM 4906 O O . VAL A 1 708 ? -9.824 -67.703 83.572 1.00 155.39 ? 708 VAL A O 1 ATOM 4907 C CB . VAL A 1 708 ? -12.550 -66.994 83.075 1.00 146.48 ? 708 VAL A CB 1 ATOM 4908 C CG1 . VAL A 1 708 ? -13.759 -67.628 82.398 1.00 141.88 ? 708 VAL A CG1 1 ATOM 4909 C CG2 . VAL A 1 708 ? -12.890 -65.584 83.505 1.00 142.70 ? 708 VAL A CG2 1 ATOM 4910 N N . SER A 1 709 ? -10.601 -69.762 84.101 1.00 158.96 ? 709 SER A N 1 ATOM 4911 C CA . SER A 1 709 ? -9.350 -70.443 83.752 1.00 166.80 ? 709 SER A CA 1 ATOM 4912 C C . SER A 1 709 ? -9.434 -71.930 83.340 1.00 174.66 ? 709 SER A C 1 ATOM 4913 O O . SER A 1 709 ? -10.420 -72.592 83.634 1.00 185.49 ? 709 SER A O 1 ATOM 4914 C CB . SER A 1 709 ? -8.363 -70.283 84.886 1.00 173.82 ? 709 SER A CB 1 ATOM 4915 O OG . SER A 1 709 ? -7.064 -70.263 84.337 1.00 199.31 ? 709 SER A OG 1 ATOM 4916 N N . SER A 1 710 ? -8.372 -72.443 82.699 1.00 174.32 ? 710 SER A N 1 ATOM 4917 C CA . SER A 1 710 ? -8.315 -73.804 82.085 1.00 176.60 ? 710 SER A CA 1 ATOM 4918 C C . SER A 1 710 ? -8.357 -75.035 83.011 1.00 185.13 ? 710 SER A C 1 ATOM 4919 O O . SER A 1 710 ? -7.531 -75.172 83.912 1.00 200.54 ? 710 SER A O 1 ATOM 4920 C CB . SER A 1 710 ? -7.062 -73.923 81.212 1.00 173.63 ? 710 SER A CB 1 ATOM 4921 O OG . SER A 1 710 ? -6.723 -72.667 80.668 1.00 165.85 ? 710 SER A OG 1 ATOM 4922 N N . CYS A 1 711 ? -9.277 -75.958 82.725 1.00 187.70 ? 711 CYS A N 1 ATOM 4923 C CA . CYS A 1 711 ? -9.464 -77.178 83.521 1.00 201.71 ? 711 CYS A CA 1 ATOM 4924 C C . CYS A 1 711 ? -9.053 -78.444 82.772 1.00 210.99 ? 711 CYS A C 1 ATOM 4925 O O . CYS A 1 711 ? -8.223 -78.376 81.861 1.00 219.78 ? 711 CYS A O 1 ATOM 4926 C CB . CYS A 1 711 ? -10.915 -77.276 83.942 1.00 208.50 ? 711 CYS A CB 1 ATOM 4927 S SG . CYS A 1 711 ? -11.576 -75.635 84.257 1.00 235.89 ? 711 CYS A SG 1 ATOM 4928 N N . ASP A 1 712 ? -9.628 -79.588 83.164 1.00 211.40 ? 712 ASP A N 1 ATOM 4929 C CA . ASP A 1 712 ? -9.317 -80.888 82.538 1.00 223.80 ? 712 ASP A CA 1 ATOM 4930 C C . ASP A 1 712 ? -10.394 -81.999 82.599 1.00 239.11 ? 712 ASP A C 1 ATOM 4931 O O . ASP A 1 712 ? -10.041 -83.189 82.618 1.00 251.74 ? 712 ASP A O 1 ATOM 4932 C CB . ASP A 1 712 ? -7.971 -81.426 83.046 1.00 213.48 ? 712 ASP A CB 1 ATOM 4933 C CG . ASP A 1 712 ? -6.833 -81.113 82.098 1.00 214.62 ? 712 ASP A CG 1 ATOM 4934 O OD1 . ASP A 1 712 ? -6.300 -79.983 82.138 1.00 214.47 ? 712 ASP A OD1 1 ATOM 4935 O OD2 . ASP A 1 712 ? -6.474 -82.000 81.300 1.00 212.71 ? 712 ASP A OD2 1 ATOM 4936 N N . LYS A 1 713 ? -11.680 -81.614 82.596 1.00 238.70 ? 713 LYS A N 1 ATOM 4937 C CA . LYS A 1 713 ? -12.831 -82.555 82.611 1.00 233.60 ? 713 LYS A CA 1 ATOM 4938 C C . LYS A 1 713 ? -12.454 -84.000 82.270 1.00 255.52 ? 713 LYS A C 1 ATOM 4939 O O . LYS A 1 713 ? -13.187 -84.940 82.583 1.00 278.92 ? 713 LYS A O 1 ATOM 4940 C CB . LYS A 1 713 ? -13.944 -82.096 81.650 1.00 219.74 ? 713 LYS A CB 1 ATOM 4941 C CG . LYS A 1 713 ? -14.527 -80.716 81.909 1.00 203.23 ? 713 LYS A CG 1 ATOM 4942 C CD . LYS A 1 713 ? -15.706 -80.764 82.859 1.00 191.54 ? 713 LYS A CD 1 ATOM 4943 C CE . LYS A 1 713 ? -15.263 -80.683 84.307 1.00 182.34 ? 713 LYS A CE 1 ATOM 4944 N NZ . LYS A 1 713 ? -16.468 -80.539 85.160 1.00 176.92 ? 713 LYS A NZ 1 ATOM 4945 N N . LYS B 2 46 ? -9.006 -59.670 55.665 1.00 220.70 ? 1693 LYS B N 1 ATOM 4946 C CA . LYS B 2 46 ? -9.675 -58.711 56.608 1.00 209.92 ? 1693 LYS B CA 1 ATOM 4947 C C . LYS B 2 46 ? -8.662 -57.964 57.512 1.00 192.42 ? 1693 LYS B C 1 ATOM 4948 O O . LYS B 2 46 ? -7.573 -58.467 57.812 1.00 176.12 ? 1693 LYS B O 1 ATOM 4949 C CB . LYS B 2 46 ? -10.820 -59.391 57.407 1.00 216.21 ? 1693 LYS B CB 1 ATOM 4950 C CG . LYS B 2 46 ? -12.119 -59.657 56.621 1.00 212.03 ? 1693 LYS B CG 1 ATOM 4951 C CD . LYS B 2 46 ? -12.072 -60.976 55.842 1.00 215.07 ? 1693 LYS B CD 1 ATOM 4952 C CE . LYS B 2 46 ? -12.735 -60.879 54.469 1.00 201.28 ? 1693 LYS B CE 1 ATOM 4953 N NZ . LYS B 2 46 ? -12.174 -61.834 53.465 1.00 180.74 ? 1693 LYS B NZ 1 ATOM 4954 N N . LYS B 2 47 ? -9.055 -56.768 57.947 1.00 188.48 ? 1694 LYS B N 1 ATOM 4955 C CA . LYS B 2 47 ? -8.125 -55.718 58.392 1.00 187.03 ? 1694 LYS B CA 1 ATOM 4956 C C . LYS B 2 47 ? -7.864 -55.580 59.900 1.00 181.73 ? 1694 LYS B C 1 ATOM 4957 O O . LYS B 2 47 ? -8.632 -56.074 60.728 1.00 180.78 ? 1694 LYS B O 1 ATOM 4958 C CB . LYS B 2 47 ? -8.608 -54.349 57.872 1.00 188.51 ? 1694 LYS B CB 1 ATOM 4959 C CG . LYS B 2 47 ? -8.667 -54.207 56.358 1.00 190.56 ? 1694 LYS B CG 1 ATOM 4960 C CD . LYS B 2 47 ? -8.122 -52.860 55.904 1.00 187.87 ? 1694 LYS B CD 1 ATOM 4961 C CE . LYS B 2 47 ? -7.431 -52.986 54.550 1.00 187.03 ? 1694 LYS B CE 1 ATOM 4962 N NZ . LYS B 2 47 ? -6.497 -51.861 54.267 1.00 185.40 ? 1694 LYS B NZ 1 ATOM 4963 N N . THR B 2 48 ? -6.772 -54.878 60.226 1.00 177.68 ? 1695 THR B N 1 ATOM 4964 C CA . THR B 2 48 ? -6.489 -54.353 61.573 1.00 163.58 ? 1695 THR B CA 1 ATOM 4965 C C . THR B 2 48 ? -6.827 -52.850 61.645 1.00 149.72 ? 1695 THR B C 1 ATOM 4966 O O . THR B 2 48 ? -6.033 -52.005 61.245 1.00 145.42 ? 1695 THR B O 1 ATOM 4967 C CB . THR B 2 48 ? -5.000 -54.548 61.980 1.00 164.92 ? 1695 THR B CB 1 ATOM 4968 O OG1 . THR B 2 48 ? -4.601 -55.911 61.781 1.00 164.55 ? 1695 THR B OG1 1 ATOM 4969 C CG2 . THR B 2 48 ? -4.773 -54.159 63.438 1.00 157.80 ? 1695 THR B CG2 1 ATOM 4970 N N . ARG B 2 49 ? -8.012 -52.522 62.145 1.00 151.33 ? 1696 ARG B N 1 ATOM 4971 C CA . ARG B 2 49 ? -8.316 -51.140 62.501 1.00 156.90 ? 1696 ARG B CA 1 ATOM 4972 C C . ARG B 2 49 ? -7.356 -50.725 63.612 1.00 160.24 ? 1696 ARG B C 1 ATOM 4973 O O . ARG B 2 49 ? -7.030 -51.508 64.509 1.00 159.41 ? 1696 ARG B O 1 ATOM 4974 C CB . ARG B 2 49 ? -9.767 -50.973 62.969 1.00 153.56 ? 1696 ARG B CB 1 ATOM 4975 C CG . ARG B 2 49 ? -10.816 -51.615 62.074 1.00 156.59 ? 1696 ARG B CG 1 ATOM 4976 C CD . ARG B 2 49 ? -11.026 -50.880 60.756 1.00 159.63 ? 1696 ARG B CD 1 ATOM 4977 N NE . ARG B 2 49 ? -12.137 -51.461 59.995 1.00 159.78 ? 1696 ARG B NE 1 ATOM 4978 C CZ . ARG B 2 49 ? -12.042 -52.022 58.788 1.00 166.63 ? 1696 ARG B CZ 1 ATOM 4979 N NH1 . ARG B 2 49 ? -10.881 -52.085 58.141 1.00 175.94 ? 1696 ARG B NH1 1 ATOM 4980 N NH2 . ARG B 2 49 ? -13.129 -52.513 58.214 1.00 164.24 ? 1696 ARG B NH2 1 ATOM 4981 N N . HIS B 2 50 ? -6.897 -49.488 63.534 1.00 162.36 ? 1697 HIS B N 1 ATOM 4982 C CA . HIS B 2 50 ? -5.856 -48.995 64.408 1.00 160.31 ? 1697 HIS B CA 1 ATOM 4983 C C . HIS B 2 50 ? -6.291 -47.599 64.789 1.00 155.98 ? 1697 HIS B C 1 ATOM 4984 O O . HIS B 2 50 ? -6.649 -46.799 63.923 1.00 156.85 ? 1697 HIS B O 1 ATOM 4985 C CB . HIS B 2 50 ? -4.542 -48.946 63.627 1.00 175.35 ? 1697 HIS B CB 1 ATOM 4986 C CG . HIS B 2 50 ? -3.312 -49.037 64.475 1.00 176.34 ? 1697 HIS B CG 1 ATOM 4987 N ND1 . HIS B 2 50 ? -2.201 -49.759 64.087 1.00 178.25 ? 1697 HIS B ND1 1 ATOM 4988 C CD2 . HIS B 2 50 ? -3.009 -48.489 65.676 1.00 170.35 ? 1697 HIS B CD2 1 ATOM 4989 C CE1 . HIS B 2 50 ? -1.269 -49.654 65.017 1.00 181.31 ? 1697 HIS B CE1 1 ATOM 4990 N NE2 . HIS B 2 50 ? -1.734 -48.890 65.992 1.00 176.64 ? 1697 HIS B NE2 1 ATOM 4991 N N . TYR B 2 51 ? -6.294 -47.300 66.078 1.00 159.21 ? 1698 TYR B N 1 ATOM 4992 C CA . TYR B 2 51 ? -6.769 -45.995 66.510 1.00 164.64 ? 1698 TYR B CA 1 ATOM 4993 C C . TYR B 2 51 ? -5.778 -45.319 67.427 1.00 171.11 ? 1698 TYR B C 1 ATOM 4994 O O . TYR B 2 51 ? -5.397 -45.874 68.469 1.00 179.57 ? 1698 TYR B O 1 ATOM 4995 C CB . TYR B 2 51 ? -8.162 -46.095 67.155 1.00 158.37 ? 1698 TYR B CB 1 ATOM 4996 C CG . TYR B 2 51 ? -9.253 -46.347 66.139 1.00 149.16 ? 1698 TYR B CG 1 ATOM 4997 C CD1 . TYR B 2 51 ? -9.816 -45.295 65.423 1.00 150.46 ? 1698 TYR B CD1 1 ATOM 4998 C CD2 . TYR B 2 51 ? -9.693 -47.641 65.860 1.00 146.64 ? 1698 TYR B CD2 1 ATOM 4999 C CE1 . TYR B 2 51 ? -10.804 -45.518 64.470 1.00 149.61 ? 1698 TYR B CE1 1 ATOM 5000 C CE2 . TYR B 2 51 ? -10.680 -47.876 64.908 1.00 140.74 ? 1698 TYR B CE2 1 ATOM 5001 C CZ . TYR B 2 51 ? -11.236 -46.810 64.216 1.00 140.90 ? 1698 TYR B CZ 1 ATOM 5002 O OH . TYR B 2 51 ? -12.217 -47.023 63.265 1.00 131.58 ? 1698 TYR B OH 1 ATOM 5003 N N . PHE B 2 52 ? -5.335 -44.135 67.017 1.00 156.94 ? 1699 PHE B N 1 ATOM 5004 C CA . PHE B 2 52 ? -4.564 -43.310 67.915 1.00 146.63 ? 1699 PHE B CA 1 ATOM 5005 C C . PHE B 2 52 ? -5.534 -42.395 68.614 1.00 138.76 ? 1699 PHE B C 1 ATOM 5006 O O . PHE B 2 52 ? -6.066 -41.442 68.030 1.00 132.35 ? 1699 PHE B O 1 ATOM 5007 C CB . PHE B 2 52 ? -3.439 -42.577 67.202 1.00 151.34 ? 1699 PHE B CB 1 ATOM 5008 C CG . PHE B 2 52 ? -2.340 -43.487 66.736 1.00 160.32 ? 1699 PHE B CG 1 ATOM 5009 C CD1 . PHE B 2 52 ? -2.095 -44.692 67.380 1.00 168.12 ? 1699 PHE B CD1 1 ATOM 5010 C CD2 . PHE B 2 52 ? -1.563 -43.157 65.638 1.00 166.92 ? 1699 PHE B CD2 1 ATOM 5011 C CE1 . PHE B 2 52 ? -1.086 -45.537 66.939 1.00 181.20 ? 1699 PHE B CE1 1 ATOM 5012 C CE2 . PHE B 2 52 ? -0.548 -43.993 65.191 1.00 174.22 ? 1699 PHE B CE2 1 ATOM 5013 C CZ . PHE B 2 52 ? -0.306 -45.185 65.846 1.00 183.80 ? 1699 PHE B CZ 1 ATOM 5014 N N . ILE B 2 53 ? -5.797 -42.765 69.862 1.00 133.14 ? 1700 ILE B N 1 ATOM 5015 C CA . ILE B 2 53 ? -6.743 -42.082 70.721 1.00 132.69 ? 1700 ILE B CA 1 ATOM 5016 C C . ILE B 2 53 ? -5.961 -41.704 71.967 1.00 144.67 ? 1700 ILE B C 1 ATOM 5017 O O . ILE B 2 53 ? -5.053 -42.440 72.374 1.00 147.90 ? 1700 ILE B O 1 ATOM 5018 C CB . ILE B 2 53 ? -7.900 -43.016 71.122 1.00 120.83 ? 1700 ILE B CB 1 ATOM 5019 C CG1 . ILE B 2 53 ? -9.253 -42.407 70.783 1.00 113.87 ? 1700 ILE B CG1 1 ATOM 5020 C CG2 . ILE B 2 53 ? -7.852 -43.348 72.603 1.00 122.22 ? 1700 ILE B CG2 1 ATOM 5021 C CD1 . ILE B 2 53 ? -10.406 -43.332 71.111 1.00 107.98 ? 1700 ILE B CD1 1 ATOM 5022 N N . ALA B 2 54 ? -6.307 -40.556 72.553 1.00 149.88 ? 1701 ALA B N 1 ATOM 5023 C CA . ALA B 2 54 ? -5.692 -40.077 73.795 1.00 148.35 ? 1701 ALA B CA 1 ATOM 5024 C C . ALA B 2 54 ? -6.773 -39.460 74.672 1.00 143.85 ? 1701 ALA B C 1 ATOM 5025 O O . ALA B 2 54 ? -7.906 -39.287 74.212 1.00 134.05 ? 1701 ALA B O 1 ATOM 5026 C CB . ALA B 2 54 ? -4.587 -39.065 73.501 1.00 145.69 ? 1701 ALA B CB 1 ATOM 5027 N N . ALA B 2 55 ? -6.417 -39.149 75.923 1.00 145.39 ? 1702 ALA B N 1 ATOM 5028 C CA . ALA B 2 55 ? -7.318 -38.508 76.889 1.00 142.27 ? 1702 ALA B CA 1 ATOM 5029 C C . ALA B 2 55 ? -6.850 -37.103 77.192 1.00 151.44 ? 1702 ALA B C 1 ATOM 5030 O O . ALA B 2 55 ? -5.783 -36.921 77.778 1.00 162.79 ? 1702 ALA B O 1 ATOM 5031 C CB . ALA B 2 55 ? -7.378 -39.310 78.168 1.00 137.75 ? 1702 ALA B CB 1 ATOM 5032 N N . VAL B 2 56 ? -7.649 -36.114 76.800 1.00 158.48 ? 1703 VAL B N 1 ATOM 5033 C CA . VAL B 2 56 ? -7.230 -34.706 76.867 1.00 168.85 ? 1703 VAL B CA 1 ATOM 5034 C C . VAL B 2 56 ? -8.043 -33.900 77.861 1.00 171.99 ? 1703 VAL B C 1 ATOM 5035 O O . VAL B 2 56 ? -9.179 -34.268 78.153 1.00 182.63 ? 1703 VAL B O 1 ATOM 5036 C CB . VAL B 2 56 ? -7.352 -34.008 75.501 1.00 166.06 ? 1703 VAL B CB 1 ATOM 5037 C CG1 . VAL B 2 56 ? -6.260 -34.508 74.561 1.00 170.46 ? 1703 VAL B CG1 1 ATOM 5038 C CG2 . VAL B 2 56 ? -8.769 -34.161 74.930 1.00 151.86 ? 1703 VAL B CG2 1 ATOM 5039 N N . GLU B 2 57 ? -7.460 -32.807 78.364 1.00 163.17 ? 1704 GLU B N 1 ATOM 5040 C CA . GLU B 2 57 ? -8.174 -31.856 79.219 1.00 159.84 ? 1704 GLU B CA 1 ATOM 5041 C C . GLU B 2 57 ? -8.611 -30.638 78.395 1.00 157.64 ? 1704 GLU B C 1 ATOM 5042 O O . GLU B 2 57 ? -7.817 -30.107 77.622 1.00 156.80 ? 1704 GLU B O 1 ATOM 5043 C CB . GLU B 2 57 ? -7.300 -31.418 80.399 1.00 173.62 ? 1704 GLU B CB 1 ATOM 5044 C CG . GLU B 2 57 ? -7.155 -32.443 81.526 1.00 190.11 ? 1704 GLU B CG 1 ATOM 5045 C CD . GLU B 2 57 ? -6.352 -31.936 82.737 1.00 208.11 ? 1704 GLU B CD 1 ATOM 5046 O OE1 . GLU B 2 57 ? -6.118 -30.709 82.870 1.00 222.71 ? 1704 GLU B OE1 1 ATOM 5047 O OE2 . GLU B 2 57 ? -5.957 -32.773 83.581 1.00 201.23 ? 1704 GLU B OE2 1 ATOM 5048 N N . ARG B 2 58 ? -9.871 -30.215 78.561 1.00 155.58 ? 1705 ARG B N 1 ATOM 5049 C CA . ARG B 2 58 ? -10.472 -29.072 77.837 1.00 152.46 ? 1705 ARG B CA 1 ATOM 5050 C C . ARG B 2 58 ? -11.268 -28.125 78.750 1.00 162.46 ? 1705 ARG B C 1 ATOM 5051 O O . ARG B 2 58 ? -11.492 -28.400 79.932 1.00 174.42 ? 1705 ARG B O 1 ATOM 5052 C CB . ARG B 2 58 ? -11.445 -29.566 76.767 1.00 140.46 ? 1705 ARG B CB 1 ATOM 5053 C CG . ARG B 2 58 ? -10.856 -30.067 75.454 1.00 150.62 ? 1705 ARG B CG 1 ATOM 5054 C CD . ARG B 2 58 ? -11.976 -30.574 74.535 1.00 153.53 ? 1705 ARG B CD 1 ATOM 5055 N NE . ARG B 2 58 ? -13.134 -29.684 74.630 1.00 155.14 ? 1705 ARG B NE 1 ATOM 5056 C CZ . ARG B 2 58 ? -13.525 -28.835 73.687 1.00 166.18 ? 1705 ARG B CZ 1 ATOM 5057 N NH1 . ARG B 2 58 ? -12.886 -28.769 72.524 1.00 180.52 ? 1705 ARG B NH1 1 ATOM 5058 N NH2 . ARG B 2 58 ? -14.568 -28.050 73.908 1.00 165.59 ? 1705 ARG B NH2 1 ATOM 5059 N N . LEU B 2 59 ? -11.693 -27.003 78.181 1.00 163.23 ? 1706 LEU B N 1 ATOM 5060 C CA . LEU B 2 59 ? -12.796 -26.236 78.736 1.00 163.42 ? 1706 LEU B CA 1 ATOM 5061 C C . LEU B 2 59 ? -14.114 -26.752 78.146 1.00 162.46 ? 1706 LEU B C 1 ATOM 5062 O O . LEU B 2 59 ? -14.177 -27.050 76.943 1.00 156.43 ? 1706 LEU B O 1 ATOM 5063 C CB . LEU B 2 59 ? -12.636 -24.736 78.435 1.00 165.30 ? 1706 LEU B CB 1 ATOM 5064 C CG . LEU B 2 59 ? -12.483 -23.837 79.668 1.00 164.06 ? 1706 LEU B CG 1 ATOM 5065 C CD1 . LEU B 2 59 ? -11.208 -24.284 80.379 1.00 162.03 ? 1706 LEU B CD1 1 ATOM 5066 C CD2 . LEU B 2 59 ? -12.550 -22.326 79.370 1.00 157.67 ? 1706 LEU B CD2 1 ATOM 5067 N N . TRP B 2 60 ? -15.150 -26.864 78.992 1.00 164.69 ? 1707 TRP B N 1 ATOM 5068 C CA . TRP B 2 60 ? -16.533 -27.137 78.529 1.00 163.21 ? 1707 TRP B CA 1 ATOM 5069 C C . TRP B 2 60 ? -17.555 -26.108 78.941 1.00 161.91 ? 1707 TRP B C 1 ATOM 5070 O O . TRP B 2 60 ? -17.482 -25.505 80.002 1.00 164.50 ? 1707 TRP B O 1 ATOM 5071 C CB . TRP B 2 60 ? -17.045 -28.487 78.989 1.00 169.67 ? 1707 TRP B CB 1 ATOM 5072 C CG . TRP B 2 60 ? -18.078 -29.137 78.067 1.00 164.44 ? 1707 TRP B CG 1 ATOM 5073 C CD1 . TRP B 2 60 ? -19.199 -29.811 78.454 1.00 168.08 ? 1707 TRP B CD1 1 ATOM 5074 C CD2 . TRP B 2 60 ? -18.045 -29.214 76.630 1.00 152.25 ? 1707 TRP B CD2 1 ATOM 5075 N NE1 . TRP B 2 60 ? -19.863 -30.300 77.357 1.00 158.41 ? 1707 TRP B NE1 1 ATOM 5076 C CE2 . TRP B 2 60 ? -19.176 -29.952 76.227 1.00 147.88 ? 1707 TRP B CE2 1 ATOM 5077 C CE3 . TRP B 2 60 ? -17.172 -28.736 75.652 1.00 147.91 ? 1707 TRP B CE3 1 ATOM 5078 C CZ2 . TRP B 2 60 ? -19.457 -30.221 74.896 1.00 142.02 ? 1707 TRP B CZ2 1 ATOM 5079 C CZ3 . TRP B 2 60 ? -17.459 -28.994 74.338 1.00 151.37 ? 1707 TRP B CZ3 1 ATOM 5080 C CH2 . TRP B 2 60 ? -18.595 -29.731 73.967 1.00 146.56 ? 1707 TRP B CH2 1 ATOM 5081 N N . ASP B 2 61 ? -18.552 -25.967 78.095 1.00 163.10 ? 1708 ASP B N 1 ATOM 5082 C CA . ASP B 2 61 ? -19.363 -24.801 78.104 1.00 179.27 ? 1708 ASP B CA 1 ATOM 5083 C C . ASP B 2 61 ? -20.539 -25.219 77.299 1.00 179.67 ? 1708 ASP B C 1 ATOM 5084 O O . ASP B 2 61 ? -20.523 -26.273 76.649 1.00 174.10 ? 1708 ASP B O 1 ATOM 5085 C CB . ASP B 2 61 ? -18.631 -23.672 77.357 1.00 198.88 ? 1708 ASP B CB 1 ATOM 5086 C CG . ASP B 2 61 ? -18.610 -23.880 75.820 1.00 210.89 ? 1708 ASP B CG 1 ATOM 5087 O OD1 . ASP B 2 61 ? -18.124 -24.926 75.312 1.00 201.12 ? 1708 ASP B OD1 1 ATOM 5088 O OD2 . ASP B 2 61 ? -19.107 -22.982 75.112 1.00 225.81 ? 1708 ASP B OD2 1 ATOM 5089 N N . TYR B 2 62 ? -21.565 -24.389 77.350 1.00 180.75 ? 1709 TYR B N 1 ATOM 5090 C CA . TYR B 2 62 ? -22.637 -24.434 76.383 1.00 170.08 ? 1709 TYR B CA 1 ATOM 5091 C C . TYR B 2 62 ? -23.235 -22.998 76.490 1.00 174.05 ? 1709 TYR B C 1 ATOM 5092 O O . TYR B 2 62 ? -24.440 -22.783 76.676 1.00 163.64 ? 1709 TYR B O 1 ATOM 5093 C CB . TYR B 2 62 ? -23.594 -25.625 76.665 1.00 157.09 ? 1709 TYR B CB 1 ATOM 5094 C CG . TYR B 2 62 ? -23.126 -26.708 77.707 1.00 151.67 ? 1709 TYR B CG 1 ATOM 5095 C CD1 . TYR B 2 62 ? -22.447 -26.362 78.909 1.00 151.14 ? 1709 TYR B CD1 1 ATOM 5096 C CD2 . TYR B 2 62 ? -23.410 -28.063 77.516 1.00 138.93 ? 1709 TYR B CD2 1 ATOM 5097 C CE1 . TYR B 2 62 ? -22.046 -27.331 79.845 1.00 140.25 ? 1709 TYR B CE1 1 ATOM 5098 C CE2 . TYR B 2 62 ? -23.028 -29.034 78.466 1.00 133.35 ? 1709 TYR B CE2 1 ATOM 5099 C CZ . TYR B 2 62 ? -22.339 -28.674 79.634 1.00 130.26 ? 1709 TYR B CZ 1 ATOM 5100 O OH . TYR B 2 62 ? -21.955 -29.650 80.567 1.00 109.95 ? 1709 TYR B OH 1 ATOM 5101 N N . GLY B 2 63 ? -22.317 -22.022 76.417 1.00 183.82 ? 1710 GLY B N 1 ATOM 5102 C CA . GLY B 2 63 ? -22.598 -20.575 76.452 1.00 186.64 ? 1710 GLY B CA 1 ATOM 5103 C C . GLY B 2 63 ? -22.914 -20.093 75.052 1.00 202.25 ? 1710 GLY B C 1 ATOM 5104 O O . GLY B 2 63 ? -22.045 -19.527 74.364 1.00 180.22 ? 1710 GLY B O 1 ATOM 5105 N N . MET B 2 64 ? -24.205 -20.250 74.715 1.00 235.07 ? 1711 MET B N 1 ATOM 5106 C CA . MET B 2 64 ? -24.786 -20.542 73.361 1.00 241.49 ? 1711 MET B CA 1 ATOM 5107 C C . MET B 2 64 ? -24.367 -19.805 72.074 1.00 233.49 ? 1711 MET B C 1 ATOM 5108 O O . MET B 2 64 ? -23.218 -19.887 71.621 1.00 212.71 ? 1711 MET B O 1 ATOM 5109 C CB . MET B 2 64 ? -26.354 -20.681 73.428 1.00 240.90 ? 1711 MET B CB 1 ATOM 5110 C CG . MET B 2 64 ? -27.193 -19.388 73.538 1.00 238.76 ? 1711 MET B CG 1 ATOM 5111 S SD . MET B 2 64 ? -29.019 -19.457 73.454 1.00 219.26 ? 1711 MET B SD 1 ATOM 5112 C CE . MET B 2 64 ? -29.336 -19.854 71.727 1.00 210.92 ? 1711 MET B CE 1 ATOM 5113 N N . SER B 2 65 ? -25.341 -19.102 71.497 1.00 240.86 ? 1712 SER B N 1 ATOM 5114 C CA . SER B 2 65 ? -25.285 -18.603 70.129 1.00 258.67 ? 1712 SER B CA 1 ATOM 5115 C C . SER B 2 65 ? -26.270 -17.436 69.822 1.00 284.36 ? 1712 SER B C 1 ATOM 5116 O O . SER B 2 65 ? -26.310 -16.950 68.686 1.00 302.56 ? 1712 SER B O 1 ATOM 5117 C CB . SER B 2 65 ? -25.506 -19.778 69.162 1.00 235.42 ? 1712 SER B CB 1 ATOM 5118 O OG . SER B 2 65 ? -26.481 -20.673 69.675 1.00 202.78 ? 1712 SER B OG 1 ATOM 5119 N N . SER B 2 66 ? -27.047 -16.985 70.816 1.00 281.13 ? 1713 SER B N 1 ATOM 5120 C CA . SER B 2 66 ? -27.981 -15.854 70.627 1.00 255.67 ? 1713 SER B CA 1 ATOM 5121 C C . SER B 2 66 ? -27.744 -14.685 71.594 1.00 242.99 ? 1713 SER B C 1 ATOM 5122 O O . SER B 2 66 ? -27.356 -14.873 72.749 1.00 228.72 ? 1713 SER B O 1 ATOM 5123 C CB . SER B 2 66 ? -29.451 -16.318 70.671 1.00 255.07 ? 1713 SER B CB 1 ATOM 5124 O OG . SER B 2 66 ? -29.872 -16.673 71.980 1.00 261.70 ? 1713 SER B OG 1 ATOM 5125 N N . SER B 2 79 ? -20.577 -12.566 82.719 1.00 228.12 ? 1726 SER B N 1 ATOM 5126 C CA . SER B 2 79 ? -21.448 -13.656 82.277 1.00 219.33 ? 1726 SER B CA 1 ATOM 5127 C C . SER B 2 79 ? -20.802 -15.100 82.293 1.00 215.77 ? 1726 SER B C 1 ATOM 5128 O O . SER B 2 79 ? -20.176 -15.454 83.295 1.00 218.59 ? 1726 SER B O 1 ATOM 5129 C CB . SER B 2 79 ? -22.153 -13.278 80.959 1.00 213.89 ? 1726 SER B CB 1 ATOM 5130 O OG . SER B 2 79 ? -21.255 -13.229 79.867 1.00 216.22 ? 1726 SER B OG 1 ATOM 5131 N N . VAL B 2 80 ? -20.926 -15.875 81.194 1.00 207.06 ? 1727 VAL B N 1 ATOM 5132 C CA . VAL B 2 80 ? -20.864 -17.405 81.092 1.00 185.14 ? 1727 VAL B CA 1 ATOM 5133 C C . VAL B 2 80 ? -19.725 -18.307 81.712 1.00 183.86 ? 1727 VAL B C 1 ATOM 5134 O O . VAL B 2 80 ? -18.555 -17.964 81.543 1.00 196.33 ? 1727 VAL B O 1 ATOM 5135 C CB . VAL B 2 80 ? -20.986 -17.833 79.593 1.00 172.28 ? 1727 VAL B CB 1 ATOM 5136 C CG1 . VAL B 2 80 ? -22.444 -17.843 79.134 1.00 157.08 ? 1727 VAL B CG1 1 ATOM 5137 C CG2 . VAL B 2 80 ? -20.092 -16.976 78.684 1.00 175.23 ? 1727 VAL B CG2 1 ATOM 5138 N N . PRO B 2 81 ? -20.068 -19.491 82.354 1.00 174.44 ? 1728 PRO B N 1 ATOM 5139 C CA . PRO B 2 81 ? -19.246 -20.573 83.063 1.00 173.99 ? 1728 PRO B CA 1 ATOM 5140 C C . PRO B 2 81 ? -18.072 -21.406 82.416 1.00 181.28 ? 1728 PRO B C 1 ATOM 5141 O O . PRO B 2 81 ? -18.134 -21.848 81.257 1.00 176.20 ? 1728 PRO B O 1 ATOM 5142 C CB . PRO B 2 81 ? -20.316 -21.575 83.530 1.00 161.90 ? 1728 PRO B CB 1 ATOM 5143 C CG . PRO B 2 81 ? -21.522 -21.277 82.712 1.00 158.74 ? 1728 PRO B CG 1 ATOM 5144 C CD . PRO B 2 81 ? -21.502 -19.776 82.555 1.00 167.24 ? 1728 PRO B CD 1 ATOM 5145 N N . GLN B 2 82 ? -17.048 -21.669 83.238 1.00 197.30 ? 1729 GLN B N 1 ATOM 5146 C CA . GLN B 2 82 ? -15.808 -22.386 82.846 1.00 203.17 ? 1729 GLN B CA 1 ATOM 5147 C C . GLN B 2 82 ? -16.062 -23.917 82.751 1.00 192.27 ? 1729 GLN B C 1 ATOM 5148 O O . GLN B 2 82 ? -16.953 -24.328 82.008 1.00 172.47 ? 1729 GLN B O 1 ATOM 5149 C CB . GLN B 2 82 ? -14.651 -22.030 83.839 1.00 217.54 ? 1729 GLN B CB 1 ATOM 5150 C CG . GLN B 2 82 ? -13.214 -21.912 83.269 1.00 212.66 ? 1729 GLN B CG 1 ATOM 5151 C CD . GLN B 2 82 ? -12.113 -21.712 84.338 1.00 205.44 ? 1729 GLN B CD 1 ATOM 5152 O OE1 . GLN B 2 82 ? -10.951 -22.105 84.143 1.00 187.14 ? 1729 GLN B OE1 1 ATOM 5153 N NE2 . GLN B 2 82 ? -12.480 -21.103 85.468 1.00 213.27 ? 1729 GLN B NE2 1 ATOM 5154 N N . PHE B 2 83 ? -15.274 -24.715 83.505 1.00 196.68 ? 1730 PHE B N 1 ATOM 5155 C CA . PHE B 2 83 ? -15.302 -26.211 83.635 1.00 181.92 ? 1730 PHE B CA 1 ATOM 5156 C C . PHE B 2 83 ? -14.181 -27.002 82.922 1.00 177.30 ? 1730 PHE B C 1 ATOM 5157 O O . PHE B 2 83 ? -14.278 -27.311 81.723 1.00 169.20 ? 1730 PHE B O 1 ATOM 5158 C CB . PHE B 2 83 ? -16.643 -26.810 83.234 1.00 182.66 ? 1730 PHE B CB 1 ATOM 5159 C CG . PHE B 2 83 ? -17.753 -26.510 84.179 1.00 181.62 ? 1730 PHE B CG 1 ATOM 5160 C CD1 . PHE B 2 83 ? -17.681 -26.910 85.504 1.00 185.19 ? 1730 PHE B CD1 1 ATOM 5161 C CD2 . PHE B 2 83 ? -18.898 -25.858 83.726 1.00 178.98 ? 1730 PHE B CD2 1 ATOM 5162 C CE1 . PHE B 2 83 ? -18.734 -26.644 86.363 1.00 195.66 ? 1730 PHE B CE1 1 ATOM 5163 C CE2 . PHE B 2 83 ? -19.948 -25.586 84.576 1.00 175.46 ? 1730 PHE B CE2 1 ATOM 5164 C CZ . PHE B 2 83 ? -19.870 -25.983 85.897 1.00 186.79 ? 1730 PHE B CZ 1 ATOM 5165 N N . LYS B 2 84 ? -13.129 -27.350 83.661 1.00 173.21 ? 1731 LYS B N 1 ATOM 5166 C CA . LYS B 2 84 ? -12.091 -28.227 83.126 1.00 166.22 ? 1731 LYS B CA 1 ATOM 5167 C C . LYS B 2 84 ? -12.818 -29.577 83.108 1.00 165.65 ? 1731 LYS B C 1 ATOM 5168 O O . LYS B 2 84 ? -13.118 -30.134 84.174 1.00 177.54 ? 1731 LYS B O 1 ATOM 5169 C CB . LYS B 2 84 ? -10.837 -28.240 84.052 1.00 165.64 ? 1731 LYS B CB 1 ATOM 5170 C CG . LYS B 2 84 ? -9.421 -28.102 83.426 1.00 158.65 ? 1731 LYS B CG 1 ATOM 5171 C CD . LYS B 2 84 ? -8.353 -27.505 84.401 1.00 161.21 ? 1731 LYS B CD 1 ATOM 5172 C CE . LYS B 2 84 ? -7.725 -28.477 85.431 1.00 154.22 ? 1731 LYS B CE 1 ATOM 5173 N NZ . LYS B 2 84 ? -7.397 -27.979 86.815 1.00 146.46 ? 1731 LYS B NZ 1 ATOM 5174 N N . LYS B 2 85 ? -13.208 -30.039 81.916 1.00 152.86 ? 1732 LYS B N 1 ATOM 5175 C CA . LYS B 2 85 ? -13.639 -31.440 81.738 1.00 147.78 ? 1732 LYS B CA 1 ATOM 5176 C C . LYS B 2 85 ? -12.504 -32.200 81.006 1.00 149.05 ? 1732 LYS B C 1 ATOM 5177 O O . LYS B 2 85 ? -11.578 -31.554 80.494 1.00 142.88 ? 1732 LYS B O 1 ATOM 5178 C CB . LYS B 2 85 ? -15.020 -31.555 81.046 1.00 132.46 ? 1732 LYS B CB 1 ATOM 5179 C CG . LYS B 2 85 ? -16.206 -31.821 81.989 1.00 128.23 ? 1732 LYS B CG 1 ATOM 5180 C CD . LYS B 2 85 ? -17.557 -31.746 81.263 1.00 123.32 ? 1732 LYS B CD 1 ATOM 5181 C CE . LYS B 2 85 ? -18.785 -31.957 82.178 1.00 124.42 ? 1732 LYS B CE 1 ATOM 5182 N NZ . LYS B 2 85 ? -20.031 -31.112 81.978 1.00 114.09 ? 1732 LYS B NZ 1 ATOM 5183 N N . VAL B 2 86 ? -12.534 -33.545 81.025 1.00 152.66 ? 1733 VAL B N 1 ATOM 5184 C CA . VAL B 2 86 ? -11.563 -34.403 80.282 1.00 152.87 ? 1733 VAL B CA 1 ATOM 5185 C C . VAL B 2 86 ? -12.319 -35.167 79.197 1.00 149.65 ? 1733 VAL B C 1 ATOM 5186 O O . VAL B 2 86 ? -13.481 -35.494 79.399 1.00 155.88 ? 1733 VAL B O 1 ATOM 5187 C CB . VAL B 2 86 ? -10.848 -35.478 81.152 1.00 150.32 ? 1733 VAL B CB 1 ATOM 5188 C CG1 . VAL B 2 86 ? -9.359 -35.534 80.844 1.00 152.36 ? 1733 VAL B CG1 1 ATOM 5189 C CG2 . VAL B 2 86 ? -11.058 -35.261 82.636 1.00 150.75 ? 1733 VAL B CG2 1 ATOM 5190 N N . VAL B 2 87 ? -11.690 -35.437 78.051 1.00 145.36 ? 1734 VAL B N 1 ATOM 5191 C CA . VAL B 2 87 ? -12.352 -36.219 77.002 1.00 140.35 ? 1734 VAL B CA 1 ATOM 5192 C C . VAL B 2 87 ? -11.385 -37.148 76.346 1.00 145.13 ? 1734 VAL B C 1 ATOM 5193 O O . VAL B 2 87 ? -10.170 -37.009 76.527 1.00 150.25 ? 1734 VAL B O 1 ATOM 5194 C CB . VAL B 2 87 ? -12.921 -35.376 75.847 1.00 132.09 ? 1734 VAL B CB 1 ATOM 5195 C CG1 . VAL B 2 87 ? -13.903 -36.215 75.043 1.00 128.91 ? 1734 VAL B CG1 1 ATOM 5196 C CG2 . VAL B 2 87 ? -13.628 -34.153 76.364 1.00 131.18 ? 1734 VAL B CG2 1 ATOM 5197 N N . PHE B 2 88 ? -11.953 -38.084 75.580 1.00 140.00 ? 1735 PHE B N 1 ATOM 5198 C CA . PHE B 2 88 ? -11.213 -38.858 74.594 1.00 142.98 ? 1735 PHE B CA 1 ATOM 5199 C C . PHE B 2 88 ? -11.010 -38.056 73.317 1.00 148.23 ? 1735 PHE B C 1 ATOM 5200 O O . PHE B 2 88 ? -11.995 -37.586 72.732 1.00 143.47 ? 1735 PHE B O 1 ATOM 5201 C CB . PHE B 2 88 ? -11.956 -40.141 74.270 1.00 133.23 ? 1735 PHE B CB 1 ATOM 5202 C CG . PHE B 2 88 ? -11.852 -41.169 75.338 1.00 133.22 ? 1735 PHE B CG 1 ATOM 5203 C CD1 . PHE B 2 88 ? -10.704 -41.950 75.453 1.00 138.89 ? 1735 PHE B CD1 1 ATOM 5204 C CD2 . PHE B 2 88 ? -12.885 -41.352 76.238 1.00 131.02 ? 1735 PHE B CD2 1 ATOM 5205 C CE1 . PHE B 2 88 ? -10.587 -42.903 76.452 1.00 139.18 ? 1735 PHE B CE1 1 ATOM 5206 C CE2 . PHE B 2 88 ? -12.781 -42.309 77.231 1.00 135.50 ? 1735 PHE B CE2 1 ATOM 5207 C CZ . PHE B 2 88 ? -11.630 -43.080 77.344 1.00 139.49 ? 1735 PHE B CZ 1 ATOM 5208 N N . GLN B 2 89 ? -9.743 -37.910 72.896 1.00 154.27 ? 1736 GLN B N 1 ATOM 5209 C CA . GLN B 2 89 ? -9.376 -37.154 71.678 1.00 157.27 ? 1736 GLN B CA 1 ATOM 5210 C C . GLN B 2 89 ? -8.770 -38.028 70.586 1.00 149.89 ? 1736 GLN B C 1 ATOM 5211 O O . GLN B 2 89 ? -7.855 -38.819 70.832 1.00 134.54 ? 1736 GLN B O 1 ATOM 5212 C CB . GLN B 2 89 ? -8.442 -35.970 71.989 1.00 168.29 ? 1736 GLN B CB 1 ATOM 5213 C CG . GLN B 2 89 ? -8.299 -34.918 70.879 1.00 167.03 ? 1736 GLN B CG 1 ATOM 5214 C CD . GLN B 2 89 ? -9.461 -33.933 70.819 1.00 168.20 ? 1736 GLN B CD 1 ATOM 5215 O OE1 . GLN B 2 89 ? -9.597 -33.035 71.668 1.00 167.01 ? 1736 GLN B OE1 1 ATOM 5216 N NE2 . GLN B 2 89 ? -10.303 -34.091 69.798 1.00 162.07 ? 1736 GLN B NE2 1 ATOM 5217 N N . GLU B 2 90 ? -9.314 -37.862 69.382 1.00 158.63 ? 1737 GLU B N 1 ATOM 5218 C CA . GLU B 2 90 ? -8.878 -38.586 68.201 1.00 172.54 ? 1737 GLU B CA 1 ATOM 5219 C C . GLU B 2 90 ? -7.560 -37.952 67.788 1.00 173.42 ? 1737 GLU B C 1 ATOM 5220 O O . GLU B 2 90 ? -7.522 -36.779 67.401 1.00 182.69 ? 1737 GLU B O 1 ATOM 5221 C CB . GLU B 2 90 ? -9.954 -38.490 67.092 1.00 177.27 ? 1737 GLU B CB 1 ATOM 5222 C CG . GLU B 2 90 ? -9.592 -39.050 65.710 1.00 178.44 ? 1737 GLU B CG 1 ATOM 5223 C CD . GLU B 2 90 ? -9.489 -40.572 65.628 1.00 172.33 ? 1737 GLU B CD 1 ATOM 5224 O OE1 . GLU B 2 90 ? -8.463 -41.139 66.086 1.00 169.59 ? 1737 GLU B OE1 1 ATOM 5225 O OE2 . GLU B 2 90 ? -10.428 -41.199 65.076 1.00 165.92 ? 1737 GLU B OE2 1 ATOM 5226 N N . PHE B 2 91 ? -6.476 -38.710 67.921 1.00 158.31 ? 1738 PHE B N 1 ATOM 5227 C CA . PHE B 2 91 ? -5.178 -38.193 67.520 1.00 157.01 ? 1738 PHE B CA 1 ATOM 5228 C C . PHE B 2 91 ? -4.770 -38.694 66.149 1.00 149.54 ? 1738 PHE B C 1 ATOM 5229 O O . PHE B 2 91 ? -5.642 -39.117 65.394 1.00 140.38 ? 1738 PHE B O 1 ATOM 5230 C CB . PHE B 2 91 ? -4.118 -38.381 68.609 1.00 172.53 ? 1738 PHE B CB 1 ATOM 5231 C CG . PHE B 2 91 ? -4.001 -37.190 69.516 1.00 186.24 ? 1738 PHE B CG 1 ATOM 5232 C CD1 . PHE B 2 91 ? -4.921 -36.985 70.543 1.00 191.39 ? 1738 PHE B CD1 1 ATOM 5233 C CD2 . PHE B 2 91 ? -3.014 -36.234 69.305 1.00 193.18 ? 1738 PHE B CD2 1 ATOM 5234 C CE1 . PHE B 2 91 ? -4.836 -35.869 71.363 1.00 194.22 ? 1738 PHE B CE1 1 ATOM 5235 C CE2 . PHE B 2 91 ? -2.927 -35.113 70.118 1.00 201.84 ? 1738 PHE B CE2 1 ATOM 5236 C CZ . PHE B 2 91 ? -3.840 -34.930 71.149 1.00 199.97 ? 1738 PHE B CZ 1 ATOM 5237 N N . THR B 2 92 ? -3.476 -38.615 65.816 1.00 153.17 ? 1739 THR B N 1 ATOM 5238 C CA . THR B 2 92 ? -3.030 -38.869 64.434 1.00 149.06 ? 1739 THR B CA 1 ATOM 5239 C C . THR B 2 92 ? -1.924 -39.919 64.256 1.00 153.32 ? 1739 THR B C 1 ATOM 5240 O O . THR B 2 92 ? -2.237 -41.062 63.980 1.00 152.78 ? 1739 THR B O 1 ATOM 5241 C CB . THR B 2 92 ? -2.757 -37.573 63.640 1.00 147.38 ? 1739 THR B CB 1 ATOM 5242 O OG1 . THR B 2 92 ? -3.227 -37.743 62.301 1.00 139.90 ? 1739 THR B OG1 1 ATOM 5243 C CG2 . THR B 2 92 ? -1.276 -37.202 63.637 1.00 148.66 ? 1739 THR B CG2 1 ATOM 5244 N N . ASP B 2 93 ? -0.652 -39.550 64.367 1.00 165.71 ? 1740 ASP B N 1 ATOM 5245 C CA . ASP B 2 93 ? 0.390 -40.578 64.338 1.00 181.46 ? 1740 ASP B CA 1 ATOM 5246 C C . ASP B 2 93 ? 0.750 -40.959 65.772 1.00 185.10 ? 1740 ASP B C 1 ATOM 5247 O O . ASP B 2 93 ? 0.218 -40.366 66.722 1.00 183.42 ? 1740 ASP B O 1 ATOM 5248 C CB . ASP B 2 93 ? 1.614 -40.214 63.454 1.00 197.41 ? 1740 ASP B CB 1 ATOM 5249 C CG . ASP B 2 93 ? 2.059 -38.758 63.590 1.00 213.05 ? 1740 ASP B CG 1 ATOM 5250 O OD1 . ASP B 2 93 ? 1.689 -38.111 64.593 1.00 225.83 ? 1740 ASP B OD1 1 ATOM 5251 O OD2 . ASP B 2 93 ? 2.795 -38.269 62.691 1.00 215.36 ? 1740 ASP B OD2 1 ATOM 5252 N N . GLY B 2 94 ? 1.602 -41.973 65.926 1.00 184.58 ? 1741 GLY B N 1 ATOM 5253 C CA . GLY B 2 94 ? 2.059 -42.402 67.246 1.00 184.14 ? 1741 GLY B CA 1 ATOM 5254 C C . GLY B 2 94 ? 2.592 -41.246 68.082 1.00 190.93 ? 1741 GLY B C 1 ATOM 5255 O O . GLY B 2 94 ? 2.490 -41.263 69.308 1.00 192.00 ? 1741 GLY B O 1 ATOM 5256 N N . SER B 2 95 ? 3.146 -40.237 67.406 1.00 194.61 ? 1742 SER B N 1 ATOM 5257 C CA . SER B 2 95 ? 3.692 -39.033 68.038 1.00 189.69 ? 1742 SER B CA 1 ATOM 5258 C C . SER B 2 95 ? 2.643 -38.238 68.813 1.00 186.10 ? 1742 SER B C 1 ATOM 5259 O O . SER B 2 95 ? 2.997 -37.341 69.575 1.00 191.68 ? 1742 SER B O 1 ATOM 5260 C CB . SER B 2 95 ? 4.330 -38.115 66.984 1.00 189.92 ? 1742 SER B CB 1 ATOM 5261 O OG . SER B 2 95 ? 5.210 -38.815 66.118 1.00 193.16 ? 1742 SER B OG 1 ATOM 5262 N N . PHE B 2 96 ? 1.362 -38.567 68.620 1.00 181.98 ? 1743 PHE B N 1 ATOM 5263 C CA . PHE B 2 96 ? 0.254 -37.783 69.174 1.00 174.79 ? 1743 PHE B CA 1 ATOM 5264 C C . PHE B 2 96 ? 0.624 -36.332 68.985 1.00 175.27 ? 1743 PHE B C 1 ATOM 5265 O O . PHE B 2 96 ? 0.635 -35.531 69.924 1.00 173.37 ? 1743 PHE B O 1 ATOM 5266 C CB . PHE B 2 96 ? 0.009 -38.100 70.654 1.00 176.33 ? 1743 PHE B CB 1 ATOM 5267 C CG . PHE B 2 96 ? -0.577 -39.457 70.889 1.00 178.08 ? 1743 PHE B CG 1 ATOM 5268 C CD1 . PHE B 2 96 ? 0.249 -40.571 71.046 1.00 186.00 ? 1743 PHE B CD1 1 ATOM 5269 C CD2 . PHE B 2 96 ? -1.950 -39.629 70.949 1.00 173.29 ? 1743 PHE B CD2 1 ATOM 5270 C CE1 . PHE B 2 96 ? -0.283 -41.835 71.249 1.00 186.36 ? 1743 PHE B CE1 1 ATOM 5271 C CE2 . PHE B 2 96 ? -2.493 -40.889 71.152 1.00 183.26 ? 1743 PHE B CE2 1 ATOM 5272 C CZ . PHE B 2 96 ? -1.660 -41.994 71.300 1.00 190.18 ? 1743 PHE B CZ 1 ATOM 5273 N N . THR B 2 97 ? 0.992 -36.019 67.755 1.00 175.68 ? 1744 THR B N 1 ATOM 5274 C CA . THR B 2 97 ? 1.377 -34.674 67.432 1.00 182.32 ? 1744 THR B CA 1 ATOM 5275 C C . THR B 2 97 ? 0.161 -33.915 66.857 1.00 189.71 ? 1744 THR B C 1 ATOM 5276 O O . THR B 2 97 ? -0.425 -33.114 67.586 1.00 198.45 ? 1744 THR B O 1 ATOM 5277 C CB . THR B 2 97 ? 2.695 -34.616 66.623 1.00 182.48 ? 1744 THR B CB 1 ATOM 5278 O OG1 . THR B 2 97 ? 3.033 -33.257 66.371 1.00 189.72 ? 1744 THR B OG1 1 ATOM 5279 C CG2 . THR B 2 97 ? 2.609 -35.357 65.301 1.00 187.83 ? 1744 THR B CG2 1 ATOM 5280 N N . GLN B 2 98 ? -0.254 -34.186 65.609 1.00 191.21 ? 1745 GLN B N 1 ATOM 5281 C CA . GLN B 2 98 ? -1.541 -33.670 65.095 1.00 181.00 ? 1745 GLN B CA 1 ATOM 5282 C C . GLN B 2 98 ? -2.624 -34.355 65.895 1.00 184.03 ? 1745 GLN B C 1 ATOM 5283 O O . GLN B 2 98 ? -2.490 -35.540 66.201 1.00 203.58 ? 1745 GLN B O 1 ATOM 5284 C CB . GLN B 2 98 ? -1.793 -34.022 63.622 1.00 169.37 ? 1745 GLN B CB 1 ATOM 5285 C CG . GLN B 2 98 ? -0.613 -33.912 62.677 1.00 187.81 ? 1745 GLN B CG 1 ATOM 5286 C CD . GLN B 2 98 ? -0.378 -32.497 62.203 1.00 205.45 ? 1745 GLN B CD 1 ATOM 5287 O OE1 . GLN B 2 98 ? 0.657 -32.191 61.607 1.00 226.58 ? 1745 GLN B OE1 1 ATOM 5288 N NE2 . GLN B 2 98 ? -1.337 -31.619 62.467 1.00 208.38 ? 1745 GLN B NE2 1 ATOM 5289 N N . PRO B 2 99 ? -3.669 -33.615 66.295 1.00 181.01 ? 1746 PRO B N 1 ATOM 5290 C CA . PRO B 2 99 ? -4.923 -34.299 66.611 1.00 178.95 ? 1746 PRO B CA 1 ATOM 5291 C C . PRO B 2 99 ? -5.752 -34.320 65.334 1.00 172.43 ? 1746 PRO B C 1 ATOM 5292 O O . PRO B 2 99 ? -5.565 -33.424 64.505 1.00 182.04 ? 1746 PRO B O 1 ATOM 5293 C CB . PRO B 2 99 ? -5.570 -33.389 67.670 1.00 176.36 ? 1746 PRO B CB 1 ATOM 5294 C CG . PRO B 2 99 ? -4.485 -32.462 68.117 1.00 182.24 ? 1746 PRO B CG 1 ATOM 5295 C CD . PRO B 2 99 ? -3.626 -32.278 66.902 1.00 184.87 ? 1746 PRO B CD 1 ATOM 5296 N N . LEU B 2 100 ? -6.619 -35.321 65.142 1.00 155.79 ? 1747 LEU B N 1 ATOM 5297 C CA . LEU B 2 100 ? -7.478 -35.319 63.946 1.00 156.61 ? 1747 LEU B CA 1 ATOM 5298 C C . LEU B 2 100 ? -8.693 -34.370 64.087 1.00 162.30 ? 1747 LEU B C 1 ATOM 5299 O O . LEU B 2 100 ? -9.691 -34.714 64.735 1.00 179.82 ? 1747 LEU B O 1 ATOM 5300 C CB . LEU B 2 100 ? -7.898 -36.735 63.472 1.00 151.00 ? 1747 LEU B CB 1 ATOM 5301 C CG . LEU B 2 100 ? -8.799 -36.781 62.192 1.00 155.78 ? 1747 LEU B CG 1 ATOM 5302 C CD1 . LEU B 2 100 ? -8.142 -37.388 60.947 1.00 142.09 ? 1747 LEU B CD1 1 ATOM 5303 C CD2 . LEU B 2 100 ? -10.210 -37.354 62.410 1.00 157.60 ? 1747 LEU B CD2 1 ATOM 5304 N N . TYR B 2 101 ? -8.546 -33.171 63.506 1.00 167.40 ? 1748 TYR B N 1 ATOM 5305 C CA . TYR B 2 101 ? -9.617 -32.226 63.126 1.00 171.75 ? 1748 TYR B CA 1 ATOM 5306 C C . TYR B 2 101 ? -10.940 -32.969 62.912 1.00 165.75 ? 1748 TYR B C 1 ATOM 5307 O O . TYR B 2 101 ? -11.021 -33.867 62.069 1.00 168.93 ? 1748 TYR B O 1 ATOM 5308 C CB . TYR B 2 101 ? -9.163 -31.528 61.813 1.00 206.59 ? 1748 TYR B CB 1 ATOM 5309 C CG . TYR B 2 101 ? -9.933 -30.312 61.287 1.00 229.22 ? 1748 TYR B CG 1 ATOM 5310 C CD1 . TYR B 2 101 ? -11.325 -30.213 61.411 1.00 228.74 ? 1748 TYR B CD1 1 ATOM 5311 C CD2 . TYR B 2 101 ? -9.253 -29.273 60.628 1.00 234.96 ? 1748 TYR B CD2 1 ATOM 5312 C CE1 . TYR B 2 101 ? -12.014 -29.116 60.923 1.00 230.48 ? 1748 TYR B CE1 1 ATOM 5313 C CE2 . TYR B 2 101 ? -9.936 -28.174 60.133 1.00 247.14 ? 1748 TYR B CE2 1 ATOM 5314 C CZ . TYR B 2 101 ? -11.319 -28.106 60.288 1.00 250.59 ? 1748 TYR B CZ 1 ATOM 5315 O OH . TYR B 2 101 ? -12.028 -27.031 59.819 1.00 270.19 ? 1748 TYR B OH 1 ATOM 5316 N N . ARG B 2 102 ? -11.973 -32.633 63.681 1.00 170.80 ? 1749 ARG B N 1 ATOM 5317 C CA . ARG B 2 102 ? -13.264 -33.305 63.482 1.00 169.47 ? 1749 ARG B CA 1 ATOM 5318 C C . ARG B 2 102 ? -14.127 -32.560 62.456 1.00 164.05 ? 1749 ARG B C 1 ATOM 5319 O O . ARG B 2 102 ? -14.539 -31.406 62.666 1.00 159.16 ? 1749 ARG B O 1 ATOM 5320 C CB . ARG B 2 102 ? -13.987 -33.617 64.804 1.00 166.40 ? 1749 ARG B CB 1 ATOM 5321 C CG . ARG B 2 102 ? -13.743 -35.040 65.325 1.00 176.88 ? 1749 ARG B CG 1 ATOM 5322 C CD . ARG B 2 102 ? -13.061 -35.096 66.692 1.00 171.54 ? 1749 ARG B CD 1 ATOM 5323 N NE . ARG B 2 102 ? -13.481 -36.268 67.474 1.00 178.95 ? 1749 ARG B NE 1 ATOM 5324 C CZ . ARG B 2 102 ? -14.626 -36.382 68.171 1.00 175.39 ? 1749 ARG B CZ 1 ATOM 5325 N NH1 . ARG B 2 102 ? -15.543 -35.410 68.224 1.00 157.60 ? 1749 ARG B NH1 1 ATOM 5326 N NH2 . ARG B 2 102 ? -14.865 -37.500 68.833 1.00 172.57 ? 1749 ARG B NH2 1 ATOM 5327 N N . GLY B 2 103 ? -14.353 -33.237 61.329 1.00 158.74 ? 1750 GLY B N 1 ATOM 5328 C CA . GLY B 2 103 ? -14.950 -32.630 60.142 1.00 151.05 ? 1750 GLY B CA 1 ATOM 5329 C C . GLY B 2 103 ? -16.416 -32.394 60.353 1.00 147.85 ? 1750 GLY B C 1 ATOM 5330 O O . GLY B 2 103 ? -16.926 -32.666 61.438 1.00 165.72 ? 1750 GLY B O 1 ATOM 5331 N N . GLU B 2 104 ? -17.103 -31.890 59.332 1.00 138.45 ? 1751 GLU B N 1 ATOM 5332 C CA . GLU B 2 104 ? -18.547 -31.746 59.429 1.00 138.29 ? 1751 GLU B CA 1 ATOM 5333 C C . GLU B 2 104 ? -19.162 -33.104 59.718 1.00 146.82 ? 1751 GLU B C 1 ATOM 5334 O O . GLU B 2 104 ? -20.080 -33.211 60.537 1.00 144.23 ? 1751 GLU B O 1 ATOM 5335 C CB . GLU B 2 104 ? -19.138 -31.150 58.166 1.00 133.77 ? 1751 GLU B CB 1 ATOM 5336 C CG . GLU B 2 104 ? -18.954 -29.651 58.077 1.00 145.80 ? 1751 GLU B CG 1 ATOM 5337 C CD . GLU B 2 104 ? -17.666 -29.268 57.378 1.00 155.74 ? 1751 GLU B CD 1 ATOM 5338 O OE1 . GLU B 2 104 ? -17.018 -30.178 56.820 1.00 165.54 ? 1751 GLU B OE1 1 ATOM 5339 O OE2 . GLU B 2 104 ? -17.305 -28.065 57.367 1.00 161.87 ? 1751 GLU B OE2 1 ATOM 5340 N N . LEU B 2 105 ? -18.621 -34.135 59.061 1.00 162.26 ? 1752 LEU B N 1 ATOM 5341 C CA . LEU B 2 105 ? -18.966 -35.543 59.320 1.00 166.00 ? 1752 LEU B CA 1 ATOM 5342 C C . LEU B 2 105 ? -19.441 -35.776 60.757 1.00 166.24 ? 1752 LEU B C 1 ATOM 5343 O O . LEU B 2 105 ? -20.649 -35.882 61.013 1.00 164.08 ? 1752 LEU B O 1 ATOM 5344 C CB . LEU B 2 105 ? -17.769 -36.473 59.021 1.00 154.55 ? 1752 LEU B CB 1 ATOM 5345 C CG . LEU B 2 105 ? -17.237 -36.792 57.616 1.00 137.55 ? 1752 LEU B CG 1 ATOM 5346 C CD1 . LEU B 2 105 ? -18.376 -36.977 56.613 1.00 118.96 ? 1752 LEU B CD1 1 ATOM 5347 C CD2 . LEU B 2 105 ? -16.221 -35.736 57.183 1.00 144.32 ? 1752 LEU B CD2 1 ATOM 5348 N N . ASN B 2 106 ? -18.482 -35.843 61.682 1.00 164.72 ? 1753 ASN B N 1 ATOM 5349 C CA . ASN B 2 106 ? -18.788 -36.060 63.092 1.00 167.26 ? 1753 ASN B CA 1 ATOM 5350 C C . ASN B 2 106 ? -18.722 -34.810 63.971 1.00 158.03 ? 1753 ASN B C 1 ATOM 5351 O O . ASN B 2 106 ? -18.022 -34.758 64.993 1.00 154.10 ? 1753 ASN B O 1 ATOM 5352 C CB . ASN B 2 106 ? -18.015 -37.261 63.696 1.00 174.06 ? 1753 ASN B CB 1 ATOM 5353 C CG . ASN B 2 106 ? -16.722 -37.594 62.964 1.00 168.85 ? 1753 ASN B CG 1 ATOM 5354 O OD1 . ASN B 2 106 ? -16.046 -36.721 62.395 1.00 164.83 ? 1753 ASN B OD1 1 ATOM 5355 N ND2 . ASN B 2 106 ? -16.356 -38.878 63.006 1.00 164.23 ? 1753 ASN B ND2 1 ATOM 5356 N N . GLU B 2 107 ? -19.483 -33.800 63.567 1.00 148.45 ? 1754 GLU B N 1 ATOM 5357 C CA . GLU B 2 107 ? -19.531 -32.568 64.320 1.00 150.35 ? 1754 GLU B CA 1 ATOM 5358 C C . GLU B 2 107 ? -20.338 -32.808 65.568 1.00 144.31 ? 1754 GLU B C 1 ATOM 5359 O O . GLU B 2 107 ? -20.066 -32.242 66.619 1.00 154.30 ? 1754 GLU B O 1 ATOM 5360 C CB . GLU B 2 107 ? -20.170 -31.462 63.503 1.00 154.62 ? 1754 GLU B CB 1 ATOM 5361 C CG . GLU B 2 107 ? -19.864 -30.086 64.052 1.00 170.31 ? 1754 GLU B CG 1 ATOM 5362 C CD . GLU B 2 107 ? -20.704 -29.011 63.411 1.00 192.09 ? 1754 GLU B CD 1 ATOM 5363 O OE1 . GLU B 2 107 ? -20.767 -28.944 62.157 1.00 201.80 ? 1754 GLU B OE1 1 ATOM 5364 O OE2 . GLU B 2 107 ? -21.298 -28.224 64.175 1.00 202.50 ? 1754 GLU B OE2 1 ATOM 5365 N N . HIS B 2 108 ? -21.313 -33.688 65.432 1.00 133.60 ? 1755 HIS B N 1 ATOM 5366 C CA . HIS B 2 108 ? -22.305 -33.939 66.454 1.00 135.50 ? 1755 HIS B CA 1 ATOM 5367 C C . HIS B 2 108 ? -21.831 -34.719 67.681 1.00 134.48 ? 1755 HIS B C 1 ATOM 5368 O O . HIS B 2 108 ? -22.461 -34.633 68.749 1.00 128.73 ? 1755 HIS B O 1 ATOM 5369 C CB . HIS B 2 108 ? -23.420 -34.723 65.816 1.00 142.16 ? 1755 HIS B CB 1 ATOM 5370 C CG . HIS B 2 108 ? -22.948 -35.959 65.130 1.00 136.77 ? 1755 HIS B CG 1 ATOM 5371 N ND1 . HIS B 2 108 ? -23.064 -37.211 65.694 1.00 138.28 ? 1755 HIS B ND1 1 ATOM 5372 C CD2 . HIS B 2 108 ? -22.342 -36.135 63.935 1.00 134.26 ? 1755 HIS B CD2 1 ATOM 5373 C CE1 . HIS B 2 108 ? -22.569 -38.110 64.866 1.00 136.77 ? 1755 HIS B CE1 1 ATOM 5374 N NE2 . HIS B 2 108 ? -22.119 -37.482 63.794 1.00 148.52 ? 1755 HIS B NE2 1 ATOM 5375 N N . LEU B 2 109 ? -20.757 -35.496 67.533 1.00 130.90 ? 1756 LEU B N 1 ATOM 5376 C CA . LEU B 2 109 ? -20.209 -36.266 68.657 1.00 131.81 ? 1756 LEU B CA 1 ATOM 5377 C C . LEU B 2 109 ? -20.080 -35.438 69.928 1.00 139.85 ? 1756 LEU B C 1 ATOM 5378 O O . LEU B 2 109 ? -20.369 -35.913 71.034 1.00 126.31 ? 1756 LEU B O 1 ATOM 5379 C CB . LEU B 2 109 ? -18.865 -36.877 68.288 1.00 129.47 ? 1756 LEU B CB 1 ATOM 5380 C CG . LEU B 2 109 ? -19.011 -38.357 67.936 1.00 126.82 ? 1756 LEU B CG 1 ATOM 5381 C CD1 . LEU B 2 109 ? -20.088 -38.557 66.886 1.00 116.35 ? 1756 LEU B CD1 1 ATOM 5382 C CD2 . LEU B 2 109 ? -17.691 -38.952 67.468 1.00 138.05 ? 1756 LEU B CD2 1 ATOM 5383 N N . GLY B 2 110 ? -19.656 -34.189 69.739 1.00 152.81 ? 1757 GLY B N 1 ATOM 5384 C CA . GLY B 2 110 ? -19.600 -33.210 70.805 1.00 151.07 ? 1757 GLY B CA 1 ATOM 5385 C C . GLY B 2 110 ? -18.635 -33.727 71.827 1.00 152.56 ? 1757 GLY B C 1 ATOM 5386 O O . GLY B 2 110 ? -17.485 -34.030 71.496 1.00 164.52 ? 1757 GLY B O 1 ATOM 5387 N N . LEU B 2 111 ? -19.136 -33.887 73.046 1.00 141.83 ? 1758 LEU B N 1 ATOM 5388 C CA . LEU B 2 111 ? -18.336 -34.295 74.195 1.00 139.81 ? 1758 LEU B CA 1 ATOM 5389 C C . LEU B 2 111 ? -17.783 -35.732 74.123 1.00 133.90 ? 1758 LEU B C 1 ATOM 5390 O O . LEU B 2 111 ? -16.956 -36.137 74.951 1.00 130.34 ? 1758 LEU B O 1 ATOM 5391 C CB . LEU B 2 111 ? -19.182 -34.144 75.447 1.00 148.86 ? 1758 LEU B CB 1 ATOM 5392 C CG . LEU B 2 111 ? -18.589 -33.441 76.662 1.00 160.37 ? 1758 LEU B CG 1 ATOM 5393 C CD1 . LEU B 2 111 ? -19.529 -33.695 77.823 1.00 172.80 ? 1758 LEU B CD1 1 ATOM 5394 C CD2 . LEU B 2 111 ? -17.185 -33.902 77.025 1.00 158.71 ? 1758 LEU B CD2 1 ATOM 5395 N N . LEU B 2 112 ? -18.247 -36.501 73.144 1.00 128.73 ? 1759 LEU B N 1 ATOM 5396 C CA . LEU B 2 112 ? -17.779 -37.866 72.949 1.00 122.01 ? 1759 LEU B CA 1 ATOM 5397 C C . LEU B 2 112 ? -16.403 -37.927 72.311 1.00 128.42 ? 1759 LEU B C 1 ATOM 5398 O O . LEU B 2 112 ? -15.990 -37.019 71.570 1.00 134.42 ? 1759 LEU B O 1 ATOM 5399 C CB . LEU B 2 112 ? -18.748 -38.621 72.054 1.00 116.74 ? 1759 LEU B CB 1 ATOM 5400 C CG . LEU B 2 112 ? -19.777 -39.570 72.649 1.00 121.61 ? 1759 LEU B CG 1 ATOM 5401 C CD1 . LEU B 2 112 ? -20.553 -38.986 73.817 1.00 125.69 ? 1759 LEU B CD1 1 ATOM 5402 C CD2 . LEU B 2 112 ? -20.724 -39.969 71.535 1.00 122.83 ? 1759 LEU B CD2 1 ATOM 5403 N N . GLY B 2 113 ? -15.700 -39.015 72.607 1.00 127.37 ? 1760 GLY B N 1 ATOM 5404 C CA . GLY B 2 113 ? -14.519 -39.420 71.846 1.00 120.36 ? 1760 GLY B CA 1 ATOM 5405 C C . GLY B 2 113 ? -14.986 -40.172 70.614 1.00 114.00 ? 1760 GLY B C 1 ATOM 5406 O O . GLY B 2 113 ? -16.169 -40.496 70.501 1.00 110.45 ? 1760 GLY B O 1 ATOM 5407 N N . PRO B 2 114 ? -14.061 -40.488 69.698 1.00 114.27 ? 1761 PRO B N 1 ATOM 5408 C CA . PRO B 2 114 ? -14.441 -40.762 68.316 1.00 118.08 ? 1761 PRO B CA 1 ATOM 5409 C C . PRO B 2 114 ? -14.997 -42.145 68.078 1.00 116.29 ? 1761 PRO B C 1 ATOM 5410 O O . PRO B 2 114 ? -14.767 -43.072 68.865 1.00 107.33 ? 1761 PRO B O 1 ATOM 5411 C CB . PRO B 2 114 ? -13.122 -40.626 67.573 1.00 126.06 ? 1761 PRO B CB 1 ATOM 5412 C CG . PRO B 2 114 ? -12.129 -41.152 68.566 1.00 125.02 ? 1761 PRO B CG 1 ATOM 5413 C CD . PRO B 2 114 ? -12.645 -40.798 69.940 1.00 117.24 ? 1761 PRO B CD 1 ATOM 5414 N N . TYR B 2 115 ? -15.720 -42.259 66.972 1.00 122.83 ? 1762 TYR B N 1 ATOM 5415 C CA . TYR B 2 115 ? -16.219 -43.525 66.506 1.00 124.51 ? 1762 TYR B CA 1 ATOM 5416 C C . TYR B 2 115 ? -15.038 -44.415 66.256 1.00 124.91 ? 1762 TYR B C 1 ATOM 5417 O O . TYR B 2 115 ? -14.248 -44.128 65.333 1.00 136.65 ? 1762 TYR B O 1 ATOM 5418 C CB . TYR B 2 115 ? -16.925 -43.346 65.169 1.00 132.70 ? 1762 TYR B CB 1 ATOM 5419 C CG . TYR B 2 115 ? -18.291 -42.734 65.245 1.00 125.07 ? 1762 TYR B CG 1 ATOM 5420 C CD1 . TYR B 2 115 ? -19.238 -43.222 66.129 1.00 109.68 ? 1762 TYR B CD1 1 ATOM 5421 C CD2 . TYR B 2 115 ? -18.641 -41.683 64.399 1.00 129.36 ? 1762 TYR B CD2 1 ATOM 5422 C CE1 . TYR B 2 115 ? -20.491 -42.672 66.186 1.00 113.70 ? 1762 TYR B CE1 1 ATOM 5423 C CE2 . TYR B 2 115 ? -19.896 -41.122 64.450 1.00 122.58 ? 1762 TYR B CE2 1 ATOM 5424 C CZ . TYR B 2 115 ? -20.817 -41.624 65.348 1.00 120.83 ? 1762 TYR B CZ 1 ATOM 5425 O OH . TYR B 2 115 ? -22.076 -41.072 65.410 1.00 131.17 ? 1762 TYR B OH 1 ATOM 5426 N N . ILE B 2 116 ? -14.908 -45.457 67.088 1.00 112.83 ? 1763 ILE B N 1 ATOM 5427 C CA . ILE B 2 116 ? -14.010 -46.586 66.809 1.00 113.03 ? 1763 ILE B CA 1 ATOM 5428 C C . ILE B 2 116 ? -14.843 -47.656 66.112 1.00 117.77 ? 1763 ILE B C 1 ATOM 5429 O O . ILE B 2 116 ? -15.656 -48.324 66.754 1.00 128.15 ? 1763 ILE B O 1 ATOM 5430 C CB . ILE B 2 116 ? -13.370 -47.197 68.081 1.00 110.19 ? 1763 ILE B CB 1 ATOM 5431 C CG1 . ILE B 2 116 ? -12.818 -46.124 69.012 1.00 118.21 ? 1763 ILE B CG1 1 ATOM 5432 C CG2 . ILE B 2 116 ? -12.251 -48.160 67.724 1.00 105.71 ? 1763 ILE B CG2 1 ATOM 5433 C CD1 . ILE B 2 116 ? -11.961 -46.678 70.136 1.00 129.19 ? 1763 ILE B CD1 1 ATOM 5434 N N . ARG B 2 117 ? -14.650 -47.807 64.801 1.00 120.34 ? 1764 ARG B N 1 ATOM 5435 C CA . ARG B 2 117 ? -15.435 -48.758 63.996 1.00 123.76 ? 1764 ARG B CA 1 ATOM 5436 C C . ARG B 2 117 ? -14.614 -50.004 63.590 1.00 128.35 ? 1764 ARG B C 1 ATOM 5437 O O . ARG B 2 117 ? -13.380 -49.955 63.563 1.00 145.66 ? 1764 ARG B O 1 ATOM 5438 C CB . ARG B 2 117 ? -16.022 -48.057 62.763 1.00 118.34 ? 1764 ARG B CB 1 ATOM 5439 C CG . ARG B 2 117 ? -16.823 -46.803 63.056 1.00 116.51 ? 1764 ARG B CG 1 ATOM 5440 C CD . ARG B 2 117 ? -16.250 -45.648 62.252 1.00 125.28 ? 1764 ARG B CD 1 ATOM 5441 N NE . ARG B 2 117 ? -17.160 -44.518 62.050 1.00 129.14 ? 1764 ARG B NE 1 ATOM 5442 C CZ . ARG B 2 117 ? -18.376 -44.598 61.515 1.00 126.71 ? 1764 ARG B CZ 1 ATOM 5443 N NH1 . ARG B 2 117 ? -18.895 -45.771 61.147 1.00 122.46 ? 1764 ARG B NH1 1 ATOM 5444 N NH2 . ARG B 2 117 ? -19.087 -43.491 61.373 1.00 132.38 ? 1764 ARG B NH2 1 ATOM 5445 N N . ALA B 2 118 ? -15.299 -51.111 63.285 1.00 120.80 ? 1765 ALA B N 1 ATOM 5446 C CA . ALA B 2 118 ? -14.649 -52.364 62.883 1.00 121.66 ? 1765 ALA B CA 1 ATOM 5447 C C . ALA B 2 118 ? -15.665 -53.368 62.336 1.00 123.97 ? 1765 ALA B C 1 ATOM 5448 O O . ALA B 2 118 ? -16.807 -53.405 62.808 1.00 127.53 ? 1765 ALA B O 1 ATOM 5449 C CB . ALA B 2 118 ? -13.903 -52.969 64.069 1.00 120.95 ? 1765 ALA B CB 1 ATOM 5450 N N . GLU B 2 119 ? -15.263 -54.175 61.348 1.00 124.52 ? 1766 GLU B N 1 ATOM 5451 C CA . GLU B 2 119 ? -16.065 -55.348 60.959 1.00 129.16 ? 1766 GLU B CA 1 ATOM 5452 C C . GLU B 2 119 ? -15.772 -56.524 61.874 1.00 136.15 ? 1766 GLU B C 1 ATOM 5453 O O . GLU B 2 119 ? -14.932 -56.403 62.770 1.00 148.39 ? 1766 GLU B O 1 ATOM 5454 C CB . GLU B 2 119 ? -15.870 -55.715 59.503 1.00 130.78 ? 1766 GLU B CB 1 ATOM 5455 C CG . GLU B 2 119 ? -16.749 -54.866 58.614 1.00 145.33 ? 1766 GLU B CG 1 ATOM 5456 C CD . GLU B 2 119 ? -16.327 -54.892 57.163 1.00 167.69 ? 1766 GLU B CD 1 ATOM 5457 O OE1 . GLU B 2 119 ? -15.830 -55.951 56.707 1.00 190.82 ? 1766 GLU B OE1 1 ATOM 5458 O OE2 . GLU B 2 119 ? -16.497 -53.848 56.486 1.00 165.05 ? 1766 GLU B OE2 1 ATOM 5459 N N . VAL B 2 120 ? -16.457 -57.651 61.687 1.00 129.74 ? 1767 VAL B N 1 ATOM 5460 C CA . VAL B 2 120 ? -16.391 -58.678 62.726 1.00 127.00 ? 1767 VAL B CA 1 ATOM 5461 C C . VAL B 2 120 ? -15.163 -59.526 62.666 1.00 126.93 ? 1767 VAL B C 1 ATOM 5462 O O . VAL B 2 120 ? -14.474 -59.660 63.668 1.00 127.58 ? 1767 VAL B O 1 ATOM 5463 C CB . VAL B 2 120 ? -17.611 -59.589 62.810 1.00 131.67 ? 1767 VAL B CB 1 ATOM 5464 C CG1 . VAL B 2 120 ? -18.877 -58.757 62.649 1.00 142.37 ? 1767 VAL B CG1 1 ATOM 5465 C CG2 . VAL B 2 120 ? -17.502 -60.750 61.821 1.00 135.85 ? 1767 VAL B CG2 1 ATOM 5466 N N . GLU B 2 121 ? -14.864 -60.097 61.512 1.00 133.52 ? 1768 GLU B N 1 ATOM 5467 C CA . GLU B 2 121 ? -13.663 -60.909 61.465 1.00 158.31 ? 1768 GLU B CA 1 ATOM 5468 C C . GLU B 2 121 ? -12.376 -60.098 61.854 1.00 159.17 ? 1768 GLU B C 1 ATOM 5469 O O . GLU B 2 121 ? -11.318 -60.690 62.109 1.00 148.85 ? 1768 GLU B O 1 ATOM 5470 C CB . GLU B 2 121 ? -13.573 -61.674 60.130 1.00 174.91 ? 1768 GLU B CB 1 ATOM 5471 C CG . GLU B 2 121 ? -14.580 -62.832 59.984 1.00 181.53 ? 1768 GLU B CG 1 ATOM 5472 C CD . GLU B 2 121 ? -14.554 -63.893 61.118 1.00 186.75 ? 1768 GLU B CD 1 ATOM 5473 O OE1 . GLU B 2 121 ? -13.465 -64.345 61.567 1.00 176.56 ? 1768 GLU B OE1 1 ATOM 5474 O OE2 . GLU B 2 121 ? -15.654 -64.312 61.559 1.00 181.97 ? 1768 GLU B OE2 1 ATOM 5475 N N . ASP B 2 122 ? -12.535 -58.765 61.985 1.00 166.32 ? 1769 ASP B N 1 ATOM 5476 C CA . ASP B 2 122 ? -11.454 -57.739 62.144 1.00 155.42 ? 1769 ASP B CA 1 ATOM 5477 C C . ASP B 2 122 ? -10.691 -57.705 63.481 1.00 150.61 ? 1769 ASP B C 1 ATOM 5478 O O . ASP B 2 122 ? -11.011 -58.440 64.424 1.00 154.55 ? 1769 ASP B O 1 ATOM 5479 C CB . ASP B 2 122 ? -12.011 -56.316 61.919 1.00 147.60 ? 1769 ASP B CB 1 ATOM 5480 C CG . ASP B 2 122 ? -12.459 -56.049 60.482 1.00 156.54 ? 1769 ASP B CG 1 ATOM 5481 O OD1 . ASP B 2 122 ? -12.770 -56.992 59.712 1.00 174.80 ? 1769 ASP B OD1 1 ATOM 5482 O OD2 . ASP B 2 122 ? -12.525 -54.855 60.130 1.00 154.42 ? 1769 ASP B OD2 1 ATOM 5483 N N . ASN B 2 123 ? -9.683 -56.830 63.537 1.00 136.86 ? 1770 ASN B N 1 ATOM 5484 C CA . ASN B 2 123 ? -8.961 -56.522 64.766 1.00 133.59 ? 1770 ASN B CA 1 ATOM 5485 C C . ASN B 2 123 ? -9.095 -55.070 65.105 1.00 138.38 ? 1770 ASN B C 1 ATOM 5486 O O . ASN B 2 123 ? -9.161 -54.226 64.215 1.00 152.47 ? 1770 ASN B O 1 ATOM 5487 C CB . ASN B 2 123 ? -7.488 -56.835 64.621 1.00 135.85 ? 1770 ASN B CB 1 ATOM 5488 C CG . ASN B 2 123 ? -7.214 -58.307 64.722 1.00 155.69 ? 1770 ASN B CG 1 ATOM 5489 O OD1 . ASN B 2 123 ? -8.109 -59.090 65.065 1.00 157.55 ? 1770 ASN B OD1 1 ATOM 5490 N ND2 . ASN B 2 123 ? -5.979 -58.709 64.416 1.00 173.00 ? 1770 ASN B ND2 1 ATOM 5491 N N . ILE B 2 124 ? -9.147 -54.772 66.396 1.00 134.40 ? 1771 ILE B N 1 ATOM 5492 C CA . ILE B 2 124 ? -9.102 -53.391 66.826 1.00 128.22 ? 1771 ILE B CA 1 ATOM 5493 C C . ILE B 2 124 ? -7.810 -53.177 67.596 1.00 134.54 ? 1771 ILE B C 1 ATOM 5494 O O . ILE B 2 124 ? -7.401 -54.024 68.392 1.00 135.08 ? 1771 ILE B O 1 ATOM 5495 C CB . ILE B 2 124 ? -10.306 -53.018 67.690 1.00 120.82 ? 1771 ILE B CB 1 ATOM 5496 C CG1 . ILE B 2 124 ? -11.576 -53.530 67.043 1.00 121.31 ? 1771 ILE B CG1 1 ATOM 5497 C CG2 . ILE B 2 124 ? -10.391 -51.509 67.839 1.00 123.13 ? 1771 ILE B CG2 1 ATOM 5498 C CD1 . ILE B 2 124 ? -12.789 -53.425 67.930 1.00 132.96 ? 1771 ILE B CD1 1 ATOM 5499 N N . MET B 2 125 ? -7.150 -52.058 67.329 1.00 138.38 ? 1772 MET B N 1 ATOM 5500 C CA . MET B 2 125 ? -6.006 -51.667 68.127 1.00 141.75 ? 1772 MET B CA 1 ATOM 5501 C C . MET B 2 125 ? -6.101 -50.202 68.523 1.00 138.49 ? 1772 MET B C 1 ATOM 5502 O O . MET B 2 125 ? -6.088 -49.289 67.690 1.00 136.29 ? 1772 MET B O 1 ATOM 5503 C CB . MET B 2 125 ? -4.686 -51.976 67.418 1.00 151.12 ? 1772 MET B CB 1 ATOM 5504 C CG . MET B 2 125 ? -3.467 -51.727 68.294 1.00 162.25 ? 1772 MET B CG 1 ATOM 5505 S SD . MET B 2 125 ? -1.915 -52.186 67.508 1.00 177.07 ? 1772 MET B SD 1 ATOM 5506 C CE . MET B 2 125 ? -0.735 -51.061 68.276 1.00 194.99 ? 1772 MET B CE 1 ATOM 5507 N N . VAL B 2 126 ? -6.212 -49.989 69.819 1.00 132.41 ? 1773 VAL B N 1 ATOM 5508 C CA . VAL B 2 126 ? -6.259 -48.657 70.317 1.00 134.75 ? 1773 VAL B CA 1 ATOM 5509 C C . VAL B 2 126 ? -5.009 -48.427 71.154 1.00 149.54 ? 1773 VAL B C 1 ATOM 5510 O O . VAL B 2 126 ? -4.886 -48.940 72.275 1.00 158.62 ? 1773 VAL B O 1 ATOM 5511 C CB . VAL B 2 126 ? -7.537 -48.427 71.120 1.00 132.78 ? 1773 VAL B CB 1 ATOM 5512 C CG1 . VAL B 2 126 ? -7.740 -46.943 71.314 1.00 143.88 ? 1773 VAL B CG1 1 ATOM 5513 C CG2 . VAL B 2 126 ? -8.734 -49.009 70.383 1.00 128.12 ? 1773 VAL B CG2 1 ATOM 5514 N N . THR B 2 127 ? -4.064 -47.697 70.561 1.00 153.44 ? 1774 THR B N 1 ATOM 5515 C CA . THR B 2 127 ? -2.870 -47.204 71.255 1.00 152.26 ? 1774 THR B CA 1 ATOM 5516 C C . THR B 2 127 ? -3.232 -45.866 71.932 1.00 147.26 ? 1774 THR B C 1 ATOM 5517 O O . THR B 2 127 ? -3.465 -44.835 71.269 1.00 132.03 ? 1774 THR B O 1 ATOM 5518 C CB . THR B 2 127 ? -1.650 -47.087 70.303 1.00 156.94 ? 1774 THR B CB 1 ATOM 5519 O OG1 . THR B 2 127 ? -2.043 -47.465 68.977 1.00 156.28 ? 1774 THR B OG1 1 ATOM 5520 C CG2 . THR B 2 127 ? -0.509 -48.008 70.732 1.00 155.71 ? 1774 THR B CG2 1 ATOM 5521 N N . PHE B 2 128 ? -3.293 -45.926 73.264 1.00 148.91 ? 1775 PHE B N 1 ATOM 5522 C CA . PHE B 2 128 ? -3.917 -44.905 74.112 1.00 149.67 ? 1775 PHE B CA 1 ATOM 5523 C C . PHE B 2 128 ? -2.913 -44.131 74.966 1.00 157.30 ? 1775 PHE B C 1 ATOM 5524 O O . PHE B 2 128 ? -2.033 -44.731 75.602 1.00 154.39 ? 1775 PHE B O 1 ATOM 5525 C CB . PHE B 2 128 ? -4.976 -45.567 75.009 1.00 147.73 ? 1775 PHE B CB 1 ATOM 5526 C CG . PHE B 2 128 ? -5.519 -44.673 76.100 1.00 151.16 ? 1775 PHE B CG 1 ATOM 5527 C CD1 . PHE B 2 128 ? -6.085 -43.426 75.803 1.00 149.42 ? 1775 PHE B CD1 1 ATOM 5528 C CD2 . PHE B 2 128 ? -5.501 -45.094 77.429 1.00 151.78 ? 1775 PHE B CD2 1 ATOM 5529 C CE1 . PHE B 2 128 ? -6.593 -42.615 76.810 1.00 147.47 ? 1775 PHE B CE1 1 ATOM 5530 C CE2 . PHE B 2 128 ? -6.016 -44.285 78.438 1.00 150.81 ? 1775 PHE B CE2 1 ATOM 5531 C CZ . PHE B 2 128 ? -6.559 -43.046 78.128 1.00 149.73 ? 1775 PHE B CZ 1 ATOM 5532 N N . ARG B 2 129 ? -3.073 -42.800 74.981 1.00 162.71 ? 1776 ARG B N 1 ATOM 5533 C CA . ARG B 2 129 ? -2.181 -41.881 75.709 1.00 163.03 ? 1776 ARG B CA 1 ATOM 5534 C C . ARG B 2 129 ? -2.905 -40.945 76.664 1.00 157.38 ? 1776 ARG B C 1 ATOM 5535 O O . ARG B 2 129 ? -3.727 -40.125 76.254 1.00 148.47 ? 1776 ARG B O 1 ATOM 5536 C CB . ARG B 2 129 ? -1.345 -41.035 74.749 1.00 166.55 ? 1776 ARG B CB 1 ATOM 5537 C CG . ARG B 2 129 ? -0.147 -40.393 75.421 1.00 171.05 ? 1776 ARG B CG 1 ATOM 5538 C CD . ARG B 2 129 ? 1.084 -41.267 75.282 1.00 172.59 ? 1776 ARG B CD 1 ATOM 5539 N NE . ARG B 2 129 ? 1.814 -40.960 74.058 1.00 177.67 ? 1776 ARG B NE 1 ATOM 5540 C CZ . ARG B 2 129 ? 2.813 -40.079 73.986 1.00 192.52 ? 1776 ARG B CZ 1 ATOM 5541 N NH1 . ARG B 2 129 ? 3.216 -39.425 75.074 1.00 194.39 ? 1776 ARG B NH1 1 ATOM 5542 N NH2 . ARG B 2 129 ? 3.420 -39.850 72.825 1.00 200.83 ? 1776 ARG B NH2 1 ATOM 5543 N N . ASN B 2 130 ? -2.558 -41.064 77.940 1.00 161.71 ? 1777 ASN B N 1 ATOM 5544 C CA . ASN B 2 130 ? -3.134 -40.236 78.979 1.00 165.22 ? 1777 ASN B CA 1 ATOM 5545 C C . ASN B 2 130 ? -2.369 -38.925 79.057 1.00 170.80 ? 1777 ASN B C 1 ATOM 5546 O O . ASN B 2 130 ? -1.443 -38.749 79.861 1.00 174.36 ? 1777 ASN B O 1 ATOM 5547 C CB . ASN B 2 130 ? -3.139 -40.977 80.319 1.00 172.88 ? 1777 ASN B CB 1 ATOM 5548 C CG . ASN B 2 130 ? -3.809 -40.186 81.430 1.00 178.47 ? 1777 ASN B CG 1 ATOM 5549 O OD1 . ASN B 2 130 ? -3.945 -38.963 81.349 1.00 179.37 ? 1777 ASN B OD1 1 ATOM 5550 N ND2 . ASN B 2 130 ? -4.216 -40.884 82.489 1.00 177.76 ? 1777 ASN B ND2 1 ATOM 5551 N N . GLN B 2 131 ? -2.771 -38.008 78.189 1.00 169.16 ? 1778 GLN B N 1 ATOM 5552 C CA . GLN B 2 131 ? -2.206 -36.679 78.159 1.00 163.79 ? 1778 GLN B CA 1 ATOM 5553 C C . GLN B 2 131 ? -2.866 -35.823 79.205 1.00 158.44 ? 1778 GLN B C 1 ATOM 5554 O O . GLN B 2 131 ? -2.892 -34.606 79.075 1.00 159.33 ? 1778 GLN B O 1 ATOM 5555 C CB . GLN B 2 131 ? -2.437 -36.057 76.795 1.00 163.22 ? 1778 GLN B CB 1 ATOM 5556 C CG . GLN B 2 131 ? -1.345 -36.378 75.803 1.00 176.58 ? 1778 GLN B CG 1 ATOM 5557 C CD . GLN B 2 131 ? -1.485 -35.566 74.540 1.00 189.02 ? 1778 GLN B CD 1 ATOM 5558 O OE1 . GLN B 2 131 ? -2.562 -35.022 74.255 1.00 196.42 ? 1778 GLN B OE1 1 ATOM 5559 N NE2 . GLN B 2 131 ? -0.399 -35.471 73.769 1.00 187.71 ? 1778 GLN B NE2 1 ATOM 5560 N N . ALA B 2 132 ? -3.413 -36.451 80.239 1.00 152.40 ? 1779 ALA B N 1 ATOM 5561 C CA . ALA B 2 132 ? -4.150 -35.703 81.239 1.00 156.18 ? 1779 ALA B CA 1 ATOM 5562 C C . ALA B 2 132 ? -3.350 -35.494 82.526 1.00 165.86 ? 1779 ALA B C 1 ATOM 5563 O O . ALA B 2 132 ? -2.130 -35.689 82.552 1.00 165.37 ? 1779 ALA B O 1 ATOM 5564 C CB . ALA B 2 132 ? -5.500 -36.351 81.516 1.00 145.84 ? 1779 ALA B CB 1 ATOM 5565 N N . SER B 2 133 ? -4.059 -35.074 83.572 1.00 171.41 ? 1780 SER B N 1 ATOM 5566 C CA . SER B 2 133 ? -3.504 -34.828 84.894 1.00 175.17 ? 1780 SER B CA 1 ATOM 5567 C C . SER B 2 133 ? -3.536 -36.095 85.789 1.00 186.76 ? 1780 SER B C 1 ATOM 5568 O O . SER B 2 133 ? -2.528 -36.452 86.411 1.00 196.35 ? 1780 SER B O 1 ATOM 5569 C CB . SER B 2 133 ? -4.264 -33.663 85.536 1.00 167.96 ? 1780 SER B CB 1 ATOM 5570 O OG . SER B 2 133 ? -3.979 -33.531 86.911 1.00 172.23 ? 1780 SER B OG 1 ATOM 5571 N N . ARG B 2 134 ? -4.679 -36.781 85.840 1.00 187.71 ? 1781 ARG B N 1 ATOM 5572 C CA . ARG B 2 134 ? -4.849 -37.935 86.731 1.00 184.44 ? 1781 ARG B CA 1 ATOM 5573 C C . ARG B 2 134 ? -4.851 -39.235 85.951 1.00 177.67 ? 1781 ARG B C 1 ATOM 5574 O O . ARG B 2 134 ? -5.079 -39.227 84.740 1.00 169.15 ? 1781 ARG B O 1 ATOM 5575 C CB . ARG B 2 134 ? -6.160 -37.830 87.497 1.00 186.43 ? 1781 ARG B CB 1 ATOM 5576 C CG . ARG B 2 134 ? -6.522 -36.433 87.974 1.00 212.31 ? 1781 ARG B CG 1 ATOM 5577 C CD . ARG B 2 134 ? -5.766 -35.982 89.225 1.00 233.16 ? 1781 ARG B CD 1 ATOM 5578 N NE . ARG B 2 134 ? -6.589 -35.103 90.067 1.00 237.87 ? 1781 ARG B NE 1 ATOM 5579 C CZ . ARG B 2 134 ? -6.848 -33.814 89.827 1.00 231.34 ? 1781 ARG B CZ 1 ATOM 5580 N NH1 . ARG B 2 134 ? -6.351 -33.198 88.757 1.00 226.77 ? 1781 ARG B NH1 1 ATOM 5581 N NH2 . ARG B 2 134 ? -7.620 -33.135 90.667 1.00 230.93 ? 1781 ARG B NH2 1 ATOM 5582 N N . PRO B 2 135 ? -4.615 -40.365 86.643 1.00 177.57 ? 1782 PRO B N 1 ATOM 5583 C CA . PRO B 2 135 ? -4.643 -41.668 85.973 1.00 172.74 ? 1782 PRO B CA 1 ATOM 5584 C C . PRO B 2 135 ? -6.045 -42.010 85.421 1.00 173.36 ? 1782 PRO B C 1 ATOM 5585 O O . PRO B 2 135 ? -7.022 -41.873 86.168 1.00 180.63 ? 1782 PRO B O 1 ATOM 5586 C CB . PRO B 2 135 ? -4.261 -42.635 87.105 1.00 167.78 ? 1782 PRO B CB 1 ATOM 5587 C CG . PRO B 2 135 ? -4.669 -41.935 88.362 1.00 168.34 ? 1782 PRO B CG 1 ATOM 5588 C CD . PRO B 2 135 ? -4.351 -40.495 88.090 1.00 175.33 ? 1782 PRO B CD 1 ATOM 5589 N N . TYR B 2 136 ? -6.144 -42.399 84.135 1.00 166.75 ? 1783 TYR B N 1 ATOM 5590 C CA . TYR B 2 136 ? -7.374 -43.019 83.538 1.00 157.36 ? 1783 TYR B CA 1 ATOM 5591 C C . TYR B 2 136 ? -7.069 -44.297 82.707 1.00 155.53 ? 1783 TYR B C 1 ATOM 5592 O O . TYR B 2 136 ? -5.905 -44.673 82.559 1.00 156.22 ? 1783 TYR B O 1 ATOM 5593 C CB . TYR B 2 136 ? -8.232 -42.031 82.712 1.00 146.80 ? 1783 TYR B CB 1 ATOM 5594 C CG . TYR B 2 136 ? -8.568 -40.705 83.369 1.00 149.33 ? 1783 TYR B CG 1 ATOM 5595 C CD1 . TYR B 2 136 ? -8.792 -40.600 84.744 1.00 162.91 ? 1783 TYR B CD1 1 ATOM 5596 C CD2 . TYR B 2 136 ? -8.695 -39.558 82.605 1.00 149.95 ? 1783 TYR B CD2 1 ATOM 5597 C CE1 . TYR B 2 136 ? -9.084 -39.378 85.341 1.00 168.45 ? 1783 TYR B CE1 1 ATOM 5598 C CE2 . TYR B 2 136 ? -8.994 -38.333 83.184 1.00 157.11 ? 1783 TYR B CE2 1 ATOM 5599 C CZ . TYR B 2 136 ? -9.187 -38.249 84.547 1.00 162.51 ? 1783 TYR B CZ 1 ATOM 5600 O OH . TYR B 2 136 ? -9.494 -37.038 85.100 1.00 159.93 ? 1783 TYR B OH 1 ATOM 5601 N N . SER B 2 137 ? -8.112 -44.954 82.181 1.00 153.67 ? 1784 SER B N 1 ATOM 5602 C CA . SER B 2 137 ? -7.978 -46.244 81.454 1.00 162.45 ? 1784 SER B CA 1 ATOM 5603 C C . SER B 2 137 ? -8.772 -46.232 80.125 1.00 155.89 ? 1784 SER B C 1 ATOM 5604 O O . SER B 2 137 ? -9.354 -45.206 79.758 1.00 138.89 ? 1784 SER B O 1 ATOM 5605 C CB . SER B 2 137 ? -8.395 -47.439 82.362 1.00 169.53 ? 1784 SER B CB 1 ATOM 5606 O OG . SER B 2 137 ? -7.686 -48.660 82.098 1.00 152.96 ? 1784 SER B OG 1 ATOM 5607 N N . PHE B 2 138 ? -8.770 -47.354 79.396 1.00 158.08 ? 1785 PHE B N 1 ATOM 5608 C CA . PHE B 2 138 ? -9.558 -47.444 78.171 1.00 153.14 ? 1785 PHE B CA 1 ATOM 5609 C C . PHE B 2 138 ? -10.860 -48.174 78.413 1.00 153.23 ? 1785 PHE B C 1 ATOM 5610 O O . PHE B 2 138 ? -11.869 -47.542 78.678 1.00 161.02 ? 1785 PHE B O 1 ATOM 5611 C CB . PHE B 2 138 ? -8.791 -48.076 77.016 1.00 153.10 ? 1785 PHE B CB 1 ATOM 5612 C CG . PHE B 2 138 ? -9.535 -48.040 75.703 1.00 156.68 ? 1785 PHE B CG 1 ATOM 5613 C CD1 . PHE B 2 138 ? -10.195 -46.882 75.281 1.00 152.42 ? 1785 PHE B CD1 1 ATOM 5614 C CD2 . PHE B 2 138 ? -9.573 -49.158 74.879 1.00 155.98 ? 1785 PHE B CD2 1 ATOM 5615 C CE1 . PHE B 2 138 ? -10.883 -46.852 74.072 1.00 145.88 ? 1785 PHE B CE1 1 ATOM 5616 C CE2 . PHE B 2 138 ? -10.257 -49.133 73.669 1.00 151.04 ? 1785 PHE B CE2 1 ATOM 5617 C CZ . PHE B 2 138 ? -10.914 -47.981 73.266 1.00 148.83 ? 1785 PHE B CZ 1 ATOM 5618 N N . TYR B 2 139 ? -10.839 -49.496 78.300 1.00 147.91 ? 1786 TYR B N 1 ATOM 5619 C CA . TYR B 2 139 ? -12.005 -50.331 78.629 1.00 153.31 ? 1786 TYR B CA 1 ATOM 5620 C C . TYR B 2 139 ? -13.301 -50.088 77.863 1.00 155.70 ? 1786 TYR B C 1 ATOM 5621 O O . TYR B 2 139 ? -13.920 -49.008 77.929 1.00 143.36 ? 1786 TYR B O 1 ATOM 5622 C CB . TYR B 2 139 ? -12.318 -50.290 80.133 1.00 155.75 ? 1786 TYR B CB 1 ATOM 5623 C CG . TYR B 2 139 ? -13.409 -51.249 80.589 1.00 154.77 ? 1786 TYR B CG 1 ATOM 5624 C CD1 . TYR B 2 139 ? -13.098 -52.555 80.987 1.00 157.04 ? 1786 TYR B CD1 1 ATOM 5625 C CD2 . TYR B 2 139 ? -14.743 -50.841 80.649 1.00 151.06 ? 1786 TYR B CD2 1 ATOM 5626 C CE1 . TYR B 2 139 ? -14.087 -53.425 81.416 1.00 161.79 ? 1786 TYR B CE1 1 ATOM 5627 C CE2 . TYR B 2 139 ? -15.737 -51.710 81.078 1.00 156.58 ? 1786 TYR B CE2 1 ATOM 5628 C CZ . TYR B 2 139 ? -15.406 -52.998 81.460 1.00 155.47 ? 1786 TYR B CZ 1 ATOM 5629 O OH . TYR B 2 139 ? -16.393 -53.857 81.880 1.00 138.75 ? 1786 TYR B OH 1 ATOM 5630 N N . SER B 2 140 ? -13.695 -51.142 77.154 1.00 162.64 ? 1787 SER B N 1 ATOM 5631 C CA . SER B 2 140 ? -15.086 -51.403 76.821 1.00 154.07 ? 1787 SER B CA 1 ATOM 5632 C C . SER B 2 140 ? -15.427 -52.769 77.440 1.00 145.58 ? 1787 SER B C 1 ATOM 5633 O O . SER B 2 140 ? -14.642 -53.331 78.222 1.00 140.58 ? 1787 SER B O 1 ATOM 5634 C CB . SER B 2 140 ? -15.308 -51.388 75.298 1.00 141.51 ? 1787 SER B CB 1 ATOM 5635 O OG . SER B 2 140 ? -15.311 -52.696 74.761 1.00 134.94 ? 1787 SER B OG 1 ATOM 5636 N N . SER B 2 141 ? -16.600 -53.292 77.114 1.00 137.19 ? 1788 SER B N 1 ATOM 5637 C CA . SER B 2 141 ? -16.892 -54.671 77.435 1.00 136.77 ? 1788 SER B CA 1 ATOM 5638 C C . SER B 2 141 ? -15.993 -55.543 76.583 1.00 133.31 ? 1788 SER B C 1 ATOM 5639 O O . SER B 2 141 ? -15.157 -56.257 77.118 1.00 146.92 ? 1788 SER B O 1 ATOM 5640 C CB . SER B 2 141 ? -18.352 -55.005 77.152 1.00 145.81 ? 1788 SER B CB 1 ATOM 5641 O OG . SER B 2 141 ? -19.212 -54.397 78.096 1.00 167.36 ? 1788 SER B OG 1 ATOM 5642 N N . LEU B 2 142 ? -16.133 -55.416 75.262 1.00 124.70 ? 1789 LEU B N 1 ATOM 5643 C CA . LEU B 2 142 ? -15.569 -56.341 74.262 1.00 128.95 ? 1789 LEU B CA 1 ATOM 5644 C C . LEU B 2 142 ? -14.077 -56.620 74.331 1.00 141.74 ? 1789 LEU B C 1 ATOM 5645 O O . LEU B 2 142 ? -13.616 -57.664 73.861 1.00 166.07 ? 1789 LEU B O 1 ATOM 5646 C CB . LEU B 2 142 ? -15.834 -55.822 72.859 1.00 125.07 ? 1789 LEU B CB 1 ATOM 5647 C CG . LEU B 2 142 ? -17.135 -55.102 72.567 1.00 131.11 ? 1789 LEU B CG 1 ATOM 5648 C CD1 . LEU B 2 142 ? -17.114 -54.652 71.114 1.00 134.67 ? 1789 LEU B CD1 1 ATOM 5649 C CD2 . LEU B 2 142 ? -18.321 -56.013 72.855 1.00 139.39 ? 1789 LEU B CD2 1 ATOM 5650 N N . ILE B 2 143 ? -13.343 -55.667 74.894 1.00 138.34 ? 1790 ILE B N 1 ATOM 5651 C CA . ILE B 2 143 ? -11.878 -55.616 74.947 1.00 136.29 ? 1790 ILE B CA 1 ATOM 5652 C C . ILE B 2 143 ? -11.142 -56.875 75.517 1.00 138.79 ? 1790 ILE B C 1 ATOM 5653 O O . ILE B 2 143 ? -10.591 -56.832 76.612 1.00 144.04 ? 1790 ILE B O 1 ATOM 5654 C CB . ILE B 2 143 ? -11.539 -54.311 75.706 1.00 133.93 ? 1790 ILE B CB 1 ATOM 5655 C CG1 . ILE B 2 143 ? -10.221 -53.716 75.250 1.00 133.62 ? 1790 ILE B CG1 1 ATOM 5656 C CG2 . ILE B 2 143 ? -11.710 -54.446 77.227 1.00 137.13 ? 1790 ILE B CG2 1 ATOM 5657 C CD1 . ILE B 2 143 ? -10.219 -52.216 75.439 1.00 132.37 ? 1790 ILE B CD1 1 ATOM 5658 N N . SER B 2 144 ? -11.098 -57.967 74.743 1.00 136.00 ? 1791 SER B N 1 ATOM 5659 C CA . SER B 2 144 ? -10.825 -59.328 75.267 1.00 136.94 ? 1791 SER B CA 1 ATOM 5660 C C . SER B 2 144 ? -9.344 -59.754 75.263 1.00 139.55 ? 1791 SER B C 1 ATOM 5661 O O . SER B 2 144 ? -8.681 -59.616 74.233 1.00 134.30 ? 1791 SER B O 1 ATOM 5662 C CB . SER B 2 144 ? -11.666 -60.367 74.494 1.00 146.16 ? 1791 SER B CB 1 ATOM 5663 O OG . SER B 2 144 ? -13.065 -60.301 74.785 1.00 152.04 ? 1791 SER B OG 1 ATOM 5664 N N . TYR B 2 145 ? -8.870 -60.332 76.390 1.00 149.60 ? 1792 TYR B N 1 ATOM 5665 C CA . TYR B 2 145 ? -7.413 -60.558 76.701 1.00 155.48 ? 1792 TYR B CA 1 ATOM 5666 C C . TYR B 2 145 ? -6.766 -61.917 76.394 1.00 154.82 ? 1792 TYR B C 1 ATOM 5667 O O . TYR B 2 145 ? -7.248 -62.684 75.563 1.00 151.70 ? 1792 TYR B O 1 ATOM 5668 C CB . TYR B 2 145 ? -7.067 -60.151 78.154 1.00 155.15 ? 1792 TYR B CB 1 ATOM 5669 C CG . TYR B 2 145 ? -7.435 -58.722 78.456 1.00 164.93 ? 1792 TYR B CG 1 ATOM 5670 C CD1 . TYR B 2 145 ? -7.240 -57.703 77.499 1.00 167.73 ? 1792 TYR B CD1 1 ATOM 5671 C CD2 . TYR B 2 145 ? -7.997 -58.376 79.673 1.00 177.14 ? 1792 TYR B CD2 1 ATOM 5672 C CE1 . TYR B 2 145 ? -7.599 -56.385 77.754 1.00 163.81 ? 1792 TYR B CE1 1 ATOM 5673 C CE2 . TYR B 2 145 ? -8.358 -57.058 79.942 1.00 189.40 ? 1792 TYR B CE2 1 ATOM 5674 C CZ . TYR B 2 145 ? -8.161 -56.073 78.981 1.00 175.97 ? 1792 TYR B CZ 1 ATOM 5675 O OH . TYR B 2 145 ? -8.528 -54.785 79.266 1.00 173.94 ? 1792 TYR B OH 1 ATOM 5676 N N . GLU B 2 146 ? -5.656 -62.192 77.068 1.00 160.34 ? 1793 GLU B N 1 ATOM 5677 C CA . GLU B 2 146 ? -4.855 -63.356 76.740 1.00 183.67 ? 1793 GLU B CA 1 ATOM 5678 C C . GLU B 2 146 ? -4.883 -64.497 77.793 1.00 196.71 ? 1793 GLU B C 1 ATOM 5679 O O . GLU B 2 146 ? -5.590 -65.494 77.589 1.00 189.22 ? 1793 GLU B O 1 ATOM 5680 C CB . GLU B 2 146 ? -3.433 -62.913 76.350 1.00 198.68 ? 1793 GLU B CB 1 ATOM 5681 C CG . GLU B 2 146 ? -2.501 -64.018 75.853 1.00 235.70 ? 1793 GLU B CG 1 ATOM 5682 C CD . GLU B 2 146 ? -3.221 -65.243 75.297 1.00 251.53 ? 1793 GLU B CD 1 ATOM 5683 O OE1 . GLU B 2 146 ? -4.128 -65.097 74.441 1.00 247.47 ? 1793 GLU B OE1 1 ATOM 5684 O OE2 . GLU B 2 146 ? -2.872 -66.365 75.727 1.00 269.57 ? 1793 GLU B OE2 1 ATOM 5685 N N . GLU B 2 147 ? -4.100 -64.357 78.876 1.00 205.75 ? 1794 GLU B N 1 ATOM 5686 C CA . GLU B 2 147 ? -4.011 -65.330 80.004 1.00 192.26 ? 1794 GLU B CA 1 ATOM 5687 C C . GLU B 2 147 ? -2.597 -65.457 80.636 1.00 187.41 ? 1794 GLU B C 1 ATOM 5688 O O . GLU B 2 147 ? -1.585 -65.264 79.951 1.00 176.81 ? 1794 GLU B O 1 ATOM 5689 C CB . GLU B 2 147 ? -4.533 -66.719 79.598 1.00 185.07 ? 1794 GLU B CB 1 ATOM 5690 C CG . GLU B 2 147 ? -5.047 -67.555 80.767 1.00 192.10 ? 1794 GLU B CG 1 ATOM 5691 C CD . GLU B 2 147 ? -5.431 -68.977 80.374 1.00 193.11 ? 1794 GLU B CD 1 ATOM 5692 O OE1 . GLU B 2 147 ? -5.315 -69.304 79.168 1.00 197.56 ? 1794 GLU B OE1 1 ATOM 5693 O OE2 . GLU B 2 147 ? -5.853 -69.763 81.267 1.00 180.98 ? 1794 GLU B OE2 1 ATOM 5694 N N . ASP B 2 148 ? -2.555 -65.779 81.937 1.00 185.13 ? 1795 ASP B N 1 ATOM 5695 C CA . ASP B 2 148 ? -1.322 -66.123 82.664 1.00 192.57 ? 1795 ASP B CA 1 ATOM 5696 C C . ASP B 2 148 ? -0.137 -66.496 81.750 1.00 204.80 ? 1795 ASP B C 1 ATOM 5697 O O . ASP B 2 148 ? -0.139 -67.519 81.056 1.00 212.71 ? 1795 ASP B O 1 ATOM 5698 C CB . ASP B 2 148 ? -1.596 -67.226 83.708 1.00 196.28 ? 1795 ASP B CB 1 ATOM 5699 C CG . ASP B 2 148 ? -0.424 -68.222 83.864 1.00 215.29 ? 1795 ASP B CG 1 ATOM 5700 O OD1 . ASP B 2 148 ? 0.708 -67.819 84.243 1.00 220.48 ? 1795 ASP B OD1 1 ATOM 5701 O OD2 . ASP B 2 148 ? -0.640 -69.426 83.595 1.00 221.24 ? 1795 ASP B OD2 1 ATOM 5702 N N . PRO B 2 155 ? -1.446 -61.520 89.674 1.00 239.75 ? 1802 PRO B N 1 ATOM 5703 C CA . PRO B 2 155 ? -1.473 -60.066 89.442 1.00 239.30 ? 1802 PRO B CA 1 ATOM 5704 C C . PRO B 2 155 ? -2.410 -59.572 88.279 1.00 237.71 ? 1802 PRO B C 1 ATOM 5705 O O . PRO B 2 155 ? -1.894 -59.234 87.204 1.00 238.24 ? 1802 PRO B O 1 ATOM 5706 C CB . PRO B 2 155 ? 0.014 -59.737 89.144 1.00 231.46 ? 1802 PRO B CB 1 ATOM 5707 C CG . PRO B 2 155 ? 0.801 -61.011 89.348 1.00 228.04 ? 1802 PRO B CG 1 ATOM 5708 C CD . PRO B 2 155 ? -0.096 -62.008 90.019 1.00 229.81 ? 1802 PRO B CD 1 ATOM 5709 N N . ARG B 2 156 ? -3.742 -59.490 88.492 1.00 223.11 ? 1803 ARG B N 1 ATOM 5710 C CA . ARG B 2 156 ? -4.713 -59.247 87.368 1.00 211.96 ? 1803 ARG B CA 1 ATOM 5711 C C . ARG B 2 156 ? -5.333 -57.835 87.189 1.00 210.01 ? 1803 ARG B C 1 ATOM 5712 O O . ARG B 2 156 ? -6.265 -57.491 87.928 1.00 212.08 ? 1803 ARG B O 1 ATOM 5713 C CB . ARG B 2 156 ? -5.860 -60.294 87.378 1.00 197.36 ? 1803 ARG B CB 1 ATOM 5714 C CG . ARG B 2 156 ? -6.235 -60.895 86.008 1.00 190.01 ? 1803 ARG B CG 1 ATOM 5715 C CD . ARG B 2 156 ? -6.737 -59.885 84.962 1.00 196.10 ? 1803 ARG B CD 1 ATOM 5716 N NE . ARG B 2 156 ? -6.436 -60.285 83.569 1.00 191.76 ? 1803 ARG B NE 1 ATOM 5717 C CZ . ARG B 2 156 ? -6.372 -59.454 82.520 1.00 168.58 ? 1803 ARG B CZ 1 ATOM 5718 N NH1 . ARG B 2 156 ? -6.586 -58.156 82.684 1.00 154.66 ? 1803 ARG B NH1 1 ATOM 5719 N NH2 . ARG B 2 156 ? -6.090 -59.924 81.304 1.00 148.12 ? 1803 ARG B NH2 1 ATOM 5720 N N . LYS B 2 157 ? -4.809 -57.062 86.207 1.00 204.23 ? 1804 LYS B N 1 ATOM 5721 C CA . LYS B 2 157 ? -5.453 -55.848 85.536 1.00 204.10 ? 1804 LYS B CA 1 ATOM 5722 C C . LYS B 2 157 ? -4.562 -54.552 85.206 1.00 194.60 ? 1804 LYS B C 1 ATOM 5723 O O . LYS B 2 157 ? -3.365 -54.681 84.908 1.00 179.21 ? 1804 LYS B O 1 ATOM 5724 C CB . LYS B 2 157 ? -6.919 -55.543 86.032 1.00 204.43 ? 1804 LYS B CB 1 ATOM 5725 C CG . LYS B 2 157 ? -8.048 -56.374 85.362 1.00 174.82 ? 1804 LYS B CG 1 ATOM 5726 C CD . LYS B 2 157 ? -9.470 -55.942 85.750 1.00 161.18 ? 1804 LYS B CD 1 ATOM 5727 C CE . LYS B 2 157 ? -9.884 -54.567 85.201 1.00 156.97 ? 1804 LYS B CE 1 ATOM 5728 N NZ . LYS B 2 157 ? -10.050 -54.435 83.712 1.00 137.95 ? 1804 LYS B NZ 1 ATOM 5729 N N . ASN B 2 158 ? -5.153 -53.338 85.215 1.00 189.15 ? 1805 ASN B N 1 ATOM 5730 C CA . ASN B 2 158 ? -4.558 -52.128 84.559 1.00 186.59 ? 1805 ASN B CA 1 ATOM 5731 C C . ASN B 2 158 ? -5.188 -50.750 84.863 1.00 196.67 ? 1805 ASN B C 1 ATOM 5732 O O . ASN B 2 158 ? -6.401 -50.636 85.090 1.00 208.26 ? 1805 ASN B O 1 ATOM 5733 C CB . ASN B 2 158 ? -4.625 -52.253 83.020 1.00 178.17 ? 1805 ASN B CB 1 ATOM 5734 C CG . ASN B 2 158 ? -5.848 -51.519 82.408 1.00 168.02 ? 1805 ASN B CG 1 ATOM 5735 O OD1 . ASN B 2 158 ? -5.700 -50.553 81.667 1.00 163.26 ? 1805 ASN B OD1 1 ATOM 5736 N ND2 . ASN B 2 158 ? -7.053 -51.970 82.742 1.00 161.57 ? 1805 ASN B ND2 1 ATOM 5737 N N . PHE B 2 159 ? -4.342 -49.716 84.825 1.00 194.80 ? 1806 PHE B N 1 ATOM 5738 C CA . PHE B 2 159 ? -4.722 -48.313 84.516 1.00 177.60 ? 1806 PHE B CA 1 ATOM 5739 C C . PHE B 2 159 ? -3.521 -47.571 83.879 1.00 174.36 ? 1806 PHE B C 1 ATOM 5740 O O . PHE B 2 159 ? -2.382 -48.067 83.928 1.00 175.57 ? 1806 PHE B O 1 ATOM 5741 C CB . PHE B 2 159 ? -5.468 -47.544 85.677 1.00 180.34 ? 1806 PHE B CB 1 ATOM 5742 C CG . PHE B 2 159 ? -4.631 -47.170 86.939 1.00 192.41 ? 1806 PHE B CG 1 ATOM 5743 C CD1 . PHE B 2 159 ? -3.320 -46.649 86.873 1.00 191.48 ? 1806 PHE B CD1 1 ATOM 5744 C CD2 . PHE B 2 159 ? -5.228 -47.240 88.219 1.00 186.44 ? 1806 PHE B CD2 1 ATOM 5745 C CE1 . PHE B 2 159 ? -2.622 -46.285 88.037 1.00 180.94 ? 1806 PHE B CE1 1 ATOM 5746 C CE2 . PHE B 2 159 ? -4.528 -46.867 89.374 1.00 182.33 ? 1806 PHE B CE2 1 ATOM 5747 C CZ . PHE B 2 159 ? -3.227 -46.388 89.283 1.00 178.22 ? 1806 PHE B CZ 1 ATOM 5748 N N . VAL B 2 160 ? -3.755 -46.426 83.238 1.00 165.47 ? 1807 VAL B N 1 ATOM 5749 C CA . VAL B 2 160 ? -2.612 -45.648 82.730 1.00 164.17 ? 1807 VAL B CA 1 ATOM 5750 C C . VAL B 2 160 ? -2.387 -44.300 83.372 1.00 165.18 ? 1807 VAL B C 1 ATOM 5751 O O . VAL B 2 160 ? -3.236 -43.401 83.320 1.00 150.23 ? 1807 VAL B O 1 ATOM 5752 C CB . VAL B 2 160 ? -2.552 -45.499 81.205 1.00 161.43 ? 1807 VAL B CB 1 ATOM 5753 C CG1 . VAL B 2 160 ? -1.785 -46.665 80.616 1.00 169.26 ? 1807 VAL B CG1 1 ATOM 5754 C CG2 . VAL B 2 160 ? -3.937 -45.352 80.605 1.00 155.93 ? 1807 VAL B CG2 1 ATOM 5755 N N . LYS B 2 161 ? -1.200 -44.199 83.966 1.00 181.48 ? 1808 LYS B N 1 ATOM 5756 C CA . LYS B 2 161 ? -0.733 -43.012 84.676 1.00 188.00 ? 1808 LYS B CA 1 ATOM 5757 C C . LYS B 2 161 ? -0.684 -41.839 83.684 1.00 182.49 ? 1808 LYS B C 1 ATOM 5758 O O . LYS B 2 161 ? -0.653 -42.071 82.465 1.00 186.17 ? 1808 LYS B O 1 ATOM 5759 C CB . LYS B 2 161 ? 0.650 -43.280 85.330 1.00 190.07 ? 1808 LYS B CB 1 ATOM 5760 C CG . LYS B 2 161 ? 0.765 -44.608 86.082 1.00 180.99 ? 1808 LYS B CG 1 ATOM 5761 C CD . LYS B 2 161 ? 1.959 -44.664 87.022 1.00 179.71 ? 1808 LYS B CD 1 ATOM 5762 C CE . LYS B 2 161 ? 2.000 -46.021 87.710 1.00 180.46 ? 1808 LYS B CE 1 ATOM 5763 N NZ . LYS B 2 161 ? 3.170 -46.179 88.617 1.00 182.12 ? 1808 LYS B NZ 1 ATOM 5764 N N . PRO B 2 162 ? -0.723 -40.583 84.189 1.00 172.49 ? 1809 PRO B N 1 ATOM 5765 C CA . PRO B 2 162 ? -0.535 -39.408 83.326 1.00 163.24 ? 1809 PRO B CA 1 ATOM 5766 C C . PRO B 2 162 ? 0.664 -39.549 82.351 1.00 159.55 ? 1809 PRO B C 1 ATOM 5767 O O . PRO B 2 162 ? 1.498 -40.435 82.552 1.00 156.29 ? 1809 PRO B O 1 ATOM 5768 C CB . PRO B 2 162 ? -0.306 -38.275 84.345 1.00 168.61 ? 1809 PRO B CB 1 ATOM 5769 C CG . PRO B 2 162 ? -0.398 -38.886 85.728 1.00 167.24 ? 1809 PRO B CG 1 ATOM 5770 C CD . PRO B 2 162 ? -1.112 -40.184 85.556 1.00 168.69 ? 1809 PRO B CD 1 ATOM 5771 N N . ASN B 2 163 ? 0.742 -38.716 81.304 1.00 159.99 ? 1810 ASN B N 1 ATOM 5772 C CA . ASN B 2 163 ? 1.923 -38.701 80.398 1.00 174.04 ? 1810 ASN B CA 1 ATOM 5773 C C . ASN B 2 163 ? 2.378 -40.140 80.002 1.00 179.44 ? 1810 ASN B C 1 ATOM 5774 O O . ASN B 2 163 ? 3.564 -40.374 79.735 1.00 188.10 ? 1810 ASN B O 1 ATOM 5775 C CB . ASN B 2 163 ? 3.127 -37.918 81.046 1.00 188.88 ? 1810 ASN B CB 1 ATOM 5776 C CG . ASN B 2 163 ? 3.305 -36.457 80.547 1.00 187.80 ? 1810 ASN B CG 1 ATOM 5777 O OD1 . ASN B 2 163 ? 2.876 -36.106 79.447 1.00 189.30 ? 1810 ASN B OD1 1 ATOM 5778 N ND2 . ASN B 2 163 ? 3.990 -35.612 81.362 1.00 181.11 ? 1810 ASN B ND2 1 ATOM 5779 N N . GLU B 2 164 ? 1.452 -41.103 79.980 1.00 180.33 ? 1811 GLU B N 1 ATOM 5780 C CA . GLU B 2 164 ? 1.807 -42.518 79.732 1.00 187.51 ? 1811 GLU B CA 1 ATOM 5781 C C . GLU B 2 164 ? 1.025 -43.116 78.555 1.00 184.40 ? 1811 GLU B C 1 ATOM 5782 O O . GLU B 2 164 ? -0.072 -42.651 78.239 1.00 178.07 ? 1811 GLU B O 1 ATOM 5783 C CB . GLU B 2 164 ? 1.587 -43.344 81.002 1.00 188.06 ? 1811 GLU B CB 1 ATOM 5784 C CG . GLU B 2 164 ? 2.316 -44.672 81.072 1.00 193.03 ? 1811 GLU B CG 1 ATOM 5785 C CD . GLU B 2 164 ? 2.500 -45.136 82.506 1.00 203.66 ? 1811 GLU B CD 1 ATOM 5786 O OE1 . GLU B 2 164 ? 3.481 -44.678 83.143 1.00 213.19 ? 1811 GLU B OE1 1 ATOM 5787 O OE2 . GLU B 2 164 ? 1.670 -45.951 82.993 1.00 195.36 ? 1811 GLU B OE2 1 ATOM 5788 N N . THR B 2 165 ? 1.599 -44.131 77.904 1.00 185.57 ? 1812 THR B N 1 ATOM 5789 C CA . THR B 2 165 ? 0.967 -44.783 76.750 1.00 180.23 ? 1812 THR B CA 1 ATOM 5790 C C . THR B 2 165 ? 0.641 -46.231 77.073 1.00 190.25 ? 1812 THR B C 1 ATOM 5791 O O . THR B 2 165 ? 1.511 -46.969 77.544 1.00 202.40 ? 1812 THR B O 1 ATOM 5792 C CB . THR B 2 165 ? 1.892 -44.819 75.514 1.00 175.01 ? 1812 THR B CB 1 ATOM 5793 O OG1 . THR B 2 165 ? 2.848 -43.759 75.584 1.00 178.89 ? 1812 THR B OG1 1 ATOM 5794 C CG2 . THR B 2 165 ? 1.092 -44.708 74.222 1.00 162.72 ? 1812 THR B CG2 1 ATOM 5795 N N . LYS B 2 166 ? -0.606 -46.635 76.829 1.00 191.24 ? 1813 LYS B N 1 ATOM 5796 C CA . LYS B 2 166 ? -0.953 -48.064 76.799 1.00 193.75 ? 1813 LYS B CA 1 ATOM 5797 C C . LYS B 2 166 ? -1.537 -48.449 75.449 1.00 192.58 ? 1813 LYS B C 1 ATOM 5798 O O . LYS B 2 166 ? -2.057 -47.614 74.701 1.00 188.28 ? 1813 LYS B O 1 ATOM 5799 C CB . LYS B 2 166 ? -1.909 -48.493 77.929 1.00 183.38 ? 1813 LYS B CB 1 ATOM 5800 C CG . LYS B 2 166 ? -1.757 -49.958 78.356 1.00 171.72 ? 1813 LYS B CG 1 ATOM 5801 C CD . LYS B 2 166 ? -2.770 -50.350 79.423 1.00 164.38 ? 1813 LYS B CD 1 ATOM 5802 C CE . LYS B 2 166 ? -2.179 -51.256 80.498 1.00 165.00 ? 1813 LYS B CE 1 ATOM 5803 N NZ . LYS B 2 166 ? -2.474 -52.697 80.285 1.00 155.81 ? 1813 LYS B NZ 1 ATOM 5804 N N . THR B 2 167 ? -1.434 -49.733 75.153 1.00 188.15 ? 1814 THR B N 1 ATOM 5805 C CA . THR B 2 167 ? -1.941 -50.258 73.923 1.00 174.82 ? 1814 THR B CA 1 ATOM 5806 C C . THR B 2 167 ? -2.839 -51.433 74.239 1.00 178.59 ? 1814 THR B C 1 ATOM 5807 O O . THR B 2 167 ? -2.507 -52.265 75.091 1.00 192.13 ? 1814 THR B O 1 ATOM 5808 C CB . THR B 2 167 ? -0.790 -50.685 73.008 1.00 178.14 ? 1814 THR B CB 1 ATOM 5809 O OG1 . THR B 2 167 ? -1.325 -50.979 71.719 1.00 180.04 ? 1814 THR B OG1 1 ATOM 5810 C CG2 . THR B 2 167 ? 0.016 -51.901 73.587 1.00 170.44 ? 1814 THR B CG2 1 ATOM 5811 N N . TYR B 2 168 ? -3.994 -51.480 73.584 1.00 168.61 ? 1815 TYR B N 1 ATOM 5812 C CA . TYR B 2 168 ? -4.840 -52.662 73.652 1.00 157.95 ? 1815 TYR B CA 1 ATOM 5813 C C . TYR B 2 168 ? -5.226 -53.088 72.247 1.00 153.75 ? 1815 TYR B C 1 ATOM 5814 O O . TYR B 2 168 ? -5.652 -52.260 71.425 1.00 141.17 ? 1815 TYR B O 1 ATOM 5815 C CB . TYR B 2 168 ? -6.111 -52.424 74.441 1.00 158.28 ? 1815 TYR B CB 1 ATOM 5816 C CG . TYR B 2 168 ? -6.062 -51.456 75.599 1.00 168.25 ? 1815 TYR B CG 1 ATOM 5817 C CD1 . TYR B 2 168 ? -6.170 -50.074 75.389 1.00 167.03 ? 1815 TYR B CD1 1 ATOM 5818 C CD2 . TYR B 2 168 ? -5.994 -51.922 76.914 1.00 168.06 ? 1815 TYR B CD2 1 ATOM 5819 C CE1 . TYR B 2 168 ? -6.165 -49.191 76.457 1.00 161.06 ? 1815 TYR B CE1 1 ATOM 5820 C CE2 . TYR B 2 168 ? -6.001 -51.041 77.984 1.00 164.04 ? 1815 TYR B CE2 1 ATOM 5821 C CZ . TYR B 2 168 ? -6.088 -49.685 77.745 1.00 158.74 ? 1815 TYR B CZ 1 ATOM 5822 O OH . TYR B 2 168 ? -6.097 -48.821 78.796 1.00 158.63 ? 1815 TYR B OH 1 ATOM 5823 N N . PHE B 2 169 ? -5.087 -54.390 71.999 1.00 156.48 ? 1816 PHE B N 1 ATOM 5824 C CA . PHE B 2 169 ? -5.288 -55.006 70.682 1.00 155.80 ? 1816 PHE B CA 1 ATOM 5825 C C . PHE B 2 169 ? -5.979 -56.349 70.907 1.00 150.67 ? 1816 PHE B C 1 ATOM 5826 O O . PHE B 2 169 ? -5.546 -57.121 71.767 1.00 159.07 ? 1816 PHE B O 1 ATOM 5827 C CB . PHE B 2 169 ? -3.925 -55.175 69.979 1.00 165.24 ? 1816 PHE B CB 1 ATOM 5828 C CG . PHE B 2 169 ? -3.925 -56.143 68.818 1.00 167.44 ? 1816 PHE B CG 1 ATOM 5829 C CD1 . PHE B 2 169 ? -4.394 -55.756 67.562 1.00 167.88 ? 1816 PHE B CD1 1 ATOM 5830 C CD2 . PHE B 2 169 ? -3.417 -57.432 68.971 1.00 171.94 ? 1816 PHE B CD2 1 ATOM 5831 C CE1 . PHE B 2 169 ? -4.378 -56.643 66.490 1.00 163.38 ? 1816 PHE B CE1 1 ATOM 5832 C CE2 . PHE B 2 169 ? -3.406 -58.326 67.908 1.00 171.89 ? 1816 PHE B CE2 1 ATOM 5833 C CZ . PHE B 2 169 ? -3.883 -57.927 66.666 1.00 167.46 ? 1816 PHE B CZ 1 ATOM 5834 N N . TRP B 2 170 ? -7.055 -56.610 70.158 1.00 142.02 ? 1817 TRP B N 1 ATOM 5835 C CA . TRP B 2 170 ? -7.885 -57.813 70.348 1.00 139.94 ? 1817 TRP B CA 1 ATOM 5836 C C . TRP B 2 170 ? -8.754 -58.154 69.111 1.00 136.86 ? 1817 TRP B C 1 ATOM 5837 O O . TRP B 2 170 ? -9.207 -57.255 68.383 1.00 127.15 ? 1817 TRP B O 1 ATOM 5838 C CB . TRP B 2 170 ? -8.739 -57.669 71.626 1.00 141.86 ? 1817 TRP B CB 1 ATOM 5839 C CG . TRP B 2 170 ? -9.998 -56.858 71.452 1.00 144.83 ? 1817 TRP B CG 1 ATOM 5840 C CD1 . TRP B 2 170 ? -11.248 -57.353 71.263 1.00 157.43 ? 1817 TRP B CD1 1 ATOM 5841 C CD2 . TRP B 2 170 ? -10.134 -55.424 71.437 1.00 133.30 ? 1817 TRP B CD2 1 ATOM 5842 N NE1 . TRP B 2 170 ? -12.152 -56.327 71.128 1.00 153.45 ? 1817 TRP B NE1 1 ATOM 5843 C CE2 . TRP B 2 170 ? -11.491 -55.135 71.228 1.00 130.37 ? 1817 TRP B CE2 1 ATOM 5844 C CE3 . TRP B 2 170 ? -9.248 -54.370 71.574 1.00 133.40 ? 1817 TRP B CE3 1 ATOM 5845 C CZ2 . TRP B 2 170 ? -11.980 -53.841 71.155 1.00 117.91 ? 1817 TRP B CZ2 1 ATOM 5846 C CZ3 . TRP B 2 170 ? -9.748 -53.077 71.502 1.00 133.77 ? 1817 TRP B CZ3 1 ATOM 5847 C CH2 . TRP B 2 170 ? -11.099 -52.830 71.290 1.00 118.30 ? 1817 TRP B CH2 1 ATOM 5848 N N . LYS B 2 171 ? -8.972 -59.449 68.869 1.00 141.37 ? 1818 LYS B N 1 ATOM 5849 C CA . LYS B 2 171 ? -9.796 -59.876 67.728 1.00 151.76 ? 1818 LYS B CA 1 ATOM 5850 C C . LYS B 2 171 ? -11.291 -59.774 68.047 1.00 155.34 ? 1818 LYS B C 1 ATOM 5851 O O . LYS B 2 171 ? -11.764 -60.352 69.041 1.00 170.03 ? 1818 LYS B O 1 ATOM 5852 C CB . LYS B 2 171 ? -9.443 -61.307 67.263 1.00 164.79 ? 1818 LYS B CB 1 ATOM 5853 C CG . LYS B 2 171 ? -10.144 -61.747 65.967 1.00 175.47 ? 1818 LYS B CG 1 ATOM 5854 C CD . LYS B 2 171 ? -9.833 -63.182 65.538 1.00 180.67 ? 1818 LYS B CD 1 ATOM 5855 C CE . LYS B 2 171 ? -10.767 -63.666 64.431 1.00 173.48 ? 1818 LYS B CE 1 ATOM 5856 N NZ . LYS B 2 171 ? -10.190 -64.796 63.652 1.00 171.22 ? 1818 LYS B NZ 1 ATOM 5857 N N . VAL B 2 172 ? -12.028 -59.042 67.206 1.00 140.49 ? 1819 VAL B N 1 ATOM 5858 C CA . VAL B 2 172 ? -13.494 -59.029 67.268 1.00 126.49 ? 1819 VAL B CA 1 ATOM 5859 C C . VAL B 2 172 ? -14.010 -60.456 67.049 1.00 133.70 ? 1819 VAL B C 1 ATOM 5860 O O . VAL B 2 172 ? -13.490 -61.172 66.199 1.00 151.41 ? 1819 VAL B O 1 ATOM 5861 C CB . VAL B 2 172 ? -14.112 -58.112 66.195 1.00 113.07 ? 1819 VAL B CB 1 ATOM 5862 C CG1 . VAL B 2 172 ? -15.508 -57.698 66.606 1.00 112.43 ? 1819 VAL B CG1 1 ATOM 5863 C CG2 . VAL B 2 172 ? -13.268 -56.879 65.966 1.00 107.51 ? 1819 VAL B CG2 1 ATOM 5864 N N . GLN B 2 173 ? -15.004 -60.874 67.824 1.00 132.39 ? 1820 GLN B N 1 ATOM 5865 C CA . GLN B 2 173 ? -15.623 -62.198 67.675 1.00 146.09 ? 1820 GLN B CA 1 ATOM 5866 C C . GLN B 2 173 ? -17.056 -61.969 67.133 1.00 154.83 ? 1820 GLN B C 1 ATOM 5867 O O . GLN B 2 173 ? -17.459 -60.803 67.017 1.00 159.46 ? 1820 GLN B O 1 ATOM 5868 C CB . GLN B 2 173 ? -15.627 -62.895 69.044 1.00 155.73 ? 1820 GLN B CB 1 ATOM 5869 C CG . GLN B 2 173 ? -15.431 -64.400 69.031 1.00 163.04 ? 1820 GLN B CG 1 ATOM 5870 C CD . GLN B 2 173 ? -14.129 -64.801 68.376 1.00 173.31 ? 1820 GLN B CD 1 ATOM 5871 O OE1 . GLN B 2 173 ? -13.048 -64.286 68.705 1.00 169.01 ? 1820 GLN B OE1 1 ATOM 5872 N NE2 . GLN B 2 173 ? -14.225 -65.723 67.433 1.00 181.68 ? 1820 GLN B NE2 1 ATOM 5873 N N . HIS B 2 174 ? -17.816 -63.025 66.781 1.00 157.81 ? 1821 HIS B N 1 ATOM 5874 C CA . HIS B 2 174 ? -19.276 -62.866 66.489 1.00 147.96 ? 1821 HIS B CA 1 ATOM 5875 C C . HIS B 2 174 ? -20.053 -62.551 67.784 1.00 142.04 ? 1821 HIS B C 1 ATOM 5876 O O . HIS B 2 174 ? -21.136 -61.952 67.728 1.00 126.20 ? 1821 HIS B O 1 ATOM 5877 C CB . HIS B 2 174 ? -19.881 -64.074 65.740 1.00 160.72 ? 1821 HIS B CB 1 ATOM 5878 C CG . HIS B 2 174 ? -20.300 -65.220 66.628 1.00 187.10 ? 1821 HIS B CG 1 ATOM 5879 N ND1 . HIS B 2 174 ? -21.603 -65.407 67.047 1.00 192.40 ? 1821 HIS B ND1 1 ATOM 5880 C CD2 . HIS B 2 174 ? -19.594 -66.254 67.152 1.00 202.69 ? 1821 HIS B CD2 1 ATOM 5881 C CE1 . HIS B 2 174 ? -21.679 -66.494 67.798 1.00 187.55 ? 1821 HIS B CE1 1 ATOM 5882 N NE2 . HIS B 2 174 ? -20.473 -67.027 67.878 1.00 196.42 ? 1821 HIS B NE2 1 ATOM 5883 N N . HIS B 2 175 ? -19.450 -62.954 68.925 1.00 145.11 ? 1822 HIS B N 1 ATOM 5884 C CA . HIS B 2 175 ? -19.909 -62.725 70.328 1.00 132.55 ? 1822 HIS B CA 1 ATOM 5885 C C . HIS B 2 175 ? -19.957 -61.227 70.726 1.00 122.59 ? 1822 HIS B C 1 ATOM 5886 O O . HIS B 2 175 ? -20.624 -60.853 71.684 1.00 118.21 ? 1822 HIS B O 1 ATOM 5887 C CB . HIS B 2 175 ? -19.198 -63.730 71.344 1.00 138.63 ? 1822 HIS B CB 1 ATOM 5888 C CG . HIS B 2 175 ? -18.258 -63.117 72.364 1.00 159.56 ? 1822 HIS B CG 1 ATOM 5889 N ND1 . HIS B 2 175 ? -18.647 -62.816 73.658 1.00 170.08 ? 1822 HIS B ND1 1 ATOM 5890 C CD2 . HIS B 2 175 ? -16.928 -62.849 72.313 1.00 167.33 ? 1822 HIS B CD2 1 ATOM 5891 C CE1 . HIS B 2 175 ? -17.615 -62.334 74.335 1.00 167.57 ? 1822 HIS B CE1 1 ATOM 5892 N NE2 . HIS B 2 175 ? -16.560 -62.338 73.541 1.00 165.39 ? 1822 HIS B NE2 1 ATOM 5893 N N . MET B 2 176 ? -19.295 -60.376 69.933 1.00 121.49 ? 1823 MET B N 1 ATOM 5894 C CA . MET B 2 176 ? -19.320 -58.908 70.080 1.00 116.76 ? 1823 MET B CA 1 ATOM 5895 C C . MET B 2 176 ? -19.939 -58.191 68.856 1.00 118.61 ? 1823 MET B C 1 ATOM 5896 O O . MET B 2 176 ? -19.896 -56.965 68.734 1.00 117.04 ? 1823 MET B O 1 ATOM 5897 C CB . MET B 2 176 ? -17.922 -58.358 70.427 1.00 118.43 ? 1823 MET B CB 1 ATOM 5898 C CG . MET B 2 176 ? -16.729 -59.035 69.757 1.00 129.46 ? 1823 MET B CG 1 ATOM 5899 S SD . MET B 2 176 ? -15.104 -58.756 70.537 1.00 148.76 ? 1823 MET B SD 1 ATOM 5900 C CE . MET B 2 176 ? -14.908 -60.106 71.713 1.00 143.41 ? 1823 MET B CE 1 ATOM 5901 N N . ALA B 2 177 ? -20.557 -58.973 67.972 1.00 124.79 ? 1824 ALA B N 1 ATOM 5902 C CA . ALA B 2 177 ? -21.208 -58.462 66.767 1.00 116.61 ? 1824 ALA B CA 1 ATOM 5903 C C . ALA B 2 177 ? -22.727 -58.461 66.885 1.00 115.13 ? 1824 ALA B C 1 ATOM 5904 O O . ALA B 2 177 ? -23.301 -59.000 67.850 1.00 126.37 ? 1824 ALA B O 1 ATOM 5905 C CB . ALA B 2 177 ? -20.805 -59.311 65.573 1.00 122.15 ? 1824 ALA B CB 1 ATOM 5906 N N . PRO B 2 178 ? -23.384 -57.844 65.899 1.00 103.19 ? 1825 PRO B N 1 ATOM 5907 C CA . PRO B 2 178 ? -24.805 -57.953 65.543 1.00 103.55 ? 1825 PRO B CA 1 ATOM 5908 C C . PRO B 2 178 ? -25.236 -59.317 64.977 1.00 104.99 ? 1825 PRO B C 1 ATOM 5909 O O . PRO B 2 178 ? -24.572 -59.822 64.079 1.00 111.22 ? 1825 PRO B O 1 ATOM 5910 C CB . PRO B 2 178 ? -24.951 -56.909 64.434 1.00 96.18 ? 1825 PRO B CB 1 ATOM 5911 C CG . PRO B 2 178 ? -23.564 -56.638 63.988 1.00 96.05 ? 1825 PRO B CG 1 ATOM 5912 C CD . PRO B 2 178 ? -22.771 -56.690 65.243 1.00 93.81 ? 1825 PRO B CD 1 ATOM 5913 N N . THR B 2 179 ? -26.340 -59.884 65.487 1.00 102.97 ? 1826 THR B N 1 ATOM 5914 C CA . THR B 2 179 ? -26.979 -61.092 64.915 1.00 116.80 ? 1826 THR B CA 1 ATOM 5915 C C . THR B 2 179 ? -27.492 -60.746 63.515 1.00 122.30 ? 1826 THR B C 1 ATOM 5916 O O . THR B 2 179 ? -27.922 -59.603 63.291 1.00 127.07 ? 1826 THR B O 1 ATOM 5917 C CB . THR B 2 179 ? -28.244 -61.573 65.721 1.00 125.62 ? 1826 THR B CB 1 ATOM 5918 O OG1 . THR B 2 179 ? -28.428 -60.796 66.906 1.00 131.31 ? 1826 THR B OG1 1 ATOM 5919 C CG2 . THR B 2 179 ? -28.241 -63.120 66.079 1.00 124.94 ? 1826 THR B CG2 1 ATOM 5920 N N . LYS B 2 180 ? -27.467 -61.729 62.597 1.00 122.91 ? 1827 LYS B N 1 ATOM 5921 C CA . LYS B 2 180 ? -28.173 -61.670 61.292 1.00 126.83 ? 1827 LYS B CA 1 ATOM 5922 C C . LYS B 2 180 ? -29.482 -60.869 61.347 1.00 134.58 ? 1827 LYS B C 1 ATOM 5923 O O . LYS B 2 180 ? -29.995 -60.410 60.324 1.00 149.49 ? 1827 LYS B O 1 ATOM 5924 C CB . LYS B 2 180 ? -28.482 -63.086 60.760 1.00 130.63 ? 1827 LYS B CB 1 ATOM 5925 C CG . LYS B 2 180 ? -29.780 -63.730 61.279 1.00 144.48 ? 1827 LYS B CG 1 ATOM 5926 C CD . LYS B 2 180 ? -30.063 -65.120 60.697 1.00 162.76 ? 1827 LYS B CD 1 ATOM 5927 C CE . LYS B 2 180 ? -31.083 -65.946 61.494 1.00 165.75 ? 1827 LYS B CE 1 ATOM 5928 N NZ . LYS B 2 180 ? -31.575 -67.144 60.728 1.00 161.45 ? 1827 LYS B NZ 1 ATOM 5929 N N . ASP B 2 181 ? -30.002 -60.704 62.555 1.00 130.97 ? 1828 ASP B N 1 ATOM 5930 C CA . ASP B 2 181 ? -31.313 -60.172 62.764 1.00 130.00 ? 1828 ASP B CA 1 ATOM 5931 C C . ASP B 2 181 ? -31.218 -58.716 63.177 1.00 130.11 ? 1828 ASP B C 1 ATOM 5932 O O . ASP B 2 181 ? -32.211 -57.982 63.143 1.00 144.06 ? 1828 ASP B O 1 ATOM 5933 C CB . ASP B 2 181 ? -32.022 -61.029 63.809 1.00 141.62 ? 1828 ASP B CB 1 ATOM 5934 C CG . ASP B 2 181 ? -32.127 -62.505 63.382 1.00 172.82 ? 1828 ASP B CG 1 ATOM 5935 O OD1 . ASP B 2 181 ? -32.560 -62.753 62.230 1.00 174.52 ? 1828 ASP B OD1 1 ATOM 5936 O OD2 . ASP B 2 181 ? -31.774 -63.416 64.185 1.00 196.19 ? 1828 ASP B OD2 1 ATOM 5937 N N . GLU B 2 182 ? -30.021 -58.266 63.529 1.00 126.02 ? 1829 GLU B N 1 ATOM 5938 C CA . GLU B 2 182 ? -29.911 -56.920 64.070 1.00 136.76 ? 1829 GLU B CA 1 ATOM 5939 C C . GLU B 2 182 ? -29.944 -55.866 62.970 1.00 139.41 ? 1829 GLU B C 1 ATOM 5940 O O . GLU B 2 182 ? -30.806 -55.903 62.075 1.00 131.76 ? 1829 GLU B O 1 ATOM 5941 C CB . GLU B 2 182 ? -28.697 -56.759 65.014 1.00 143.94 ? 1829 GLU B CB 1 ATOM 5942 C CG . GLU B 2 182 ? -28.551 -57.881 66.049 1.00 154.93 ? 1829 GLU B CG 1 ATOM 5943 C CD . GLU B 2 182 ? -28.213 -57.434 67.478 1.00 157.15 ? 1829 GLU B CD 1 ATOM 5944 O OE1 . GLU B 2 182 ? -28.851 -56.466 67.966 1.00 153.96 ? 1829 GLU B OE1 1 ATOM 5945 O OE2 . GLU B 2 182 ? -27.346 -58.086 68.135 1.00 141.23 ? 1829 GLU B OE2 1 ATOM 5946 N N . PHE B 2 183 ? -29.032 -54.905 63.092 1.00 140.76 ? 1830 PHE B N 1 ATOM 5947 C CA . PHE B 2 183 ? -28.836 -53.858 62.115 1.00 132.59 ? 1830 PHE B CA 1 ATOM 5948 C C . PHE B 2 183 ? -27.412 -53.969 61.651 1.00 134.83 ? 1830 PHE B C 1 ATOM 5949 O O . PHE B 2 183 ? -26.600 -54.543 62.363 1.00 163.22 ? 1830 PHE B O 1 ATOM 5950 C CB . PHE B 2 183 ? -29.166 -52.493 62.716 1.00 125.83 ? 1830 PHE B CB 1 ATOM 5951 C CG . PHE B 2 183 ? -30.634 -52.162 62.634 1.00 147.06 ? 1830 PHE B CG 1 ATOM 5952 C CD1 . PHE B 2 183 ? -31.520 -53.026 61.959 1.00 151.33 ? 1830 PHE B CD1 1 ATOM 5953 C CD2 . PHE B 2 183 ? -31.144 -50.995 63.184 1.00 145.35 ? 1830 PHE B CD2 1 ATOM 5954 C CE1 . PHE B 2 183 ? -32.867 -52.742 61.856 1.00 138.86 ? 1830 PHE B CE1 1 ATOM 5955 C CE2 . PHE B 2 183 ? -32.503 -50.702 63.075 1.00 138.64 ? 1830 PHE B CE2 1 ATOM 5956 C CZ . PHE B 2 183 ? -33.359 -51.567 62.404 1.00 136.40 ? 1830 PHE B CZ 1 ATOM 5957 N N . ASP B 2 184 ? -27.115 -53.462 60.454 1.00 132.44 ? 1831 ASP B N 1 ATOM 5958 C CA . ASP B 2 184 ? -25.780 -53.597 59.827 1.00 133.28 ? 1831 ASP B CA 1 ATOM 5959 C C . ASP B 2 184 ? -24.599 -53.385 60.792 1.00 129.49 ? 1831 ASP B C 1 ATOM 5960 O O . ASP B 2 184 ? -23.526 -53.970 60.627 1.00 123.66 ? 1831 ASP B O 1 ATOM 5961 C CB . ASP B 2 184 ? -25.651 -52.629 58.655 1.00 140.39 ? 1831 ASP B CB 1 ATOM 5962 C CG . ASP B 2 184 ? -26.610 -52.939 57.533 1.00 156.26 ? 1831 ASP B CG 1 ATOM 5963 O OD1 . ASP B 2 184 ? -26.512 -54.063 56.978 1.00 158.60 ? 1831 ASP B OD1 1 ATOM 5964 O OD2 . ASP B 2 184 ? -27.444 -52.049 57.206 1.00 170.95 ? 1831 ASP B OD2 1 ATOM 5965 N N . CYS B 2 185 ? -24.808 -52.529 61.785 1.00 126.30 ? 1832 CYS B N 1 ATOM 5966 C CA . CYS B 2 185 ? -23.883 -52.362 62.878 1.00 121.60 ? 1832 CYS B CA 1 ATOM 5967 C C . CYS B 2 185 ? -24.607 -52.459 64.230 1.00 125.73 ? 1832 CYS B C 1 ATOM 5968 O O . CYS B 2 185 ? -25.846 -52.471 64.327 1.00 134.04 ? 1832 CYS B O 1 ATOM 5969 C CB . CYS B 2 185 ? -23.177 -51.010 62.766 1.00 139.63 ? 1832 CYS B CB 1 ATOM 5970 S SG . CYS B 2 185 ? -22.238 -50.681 61.243 1.00 171.57 ? 1832 CYS B SG 1 ATOM 5971 N N . LYS B 2 186 ? -23.802 -52.534 65.276 1.00 129.36 ? 1833 LYS B N 1 ATOM 5972 C CA . LYS B 2 186 ? -24.262 -52.483 66.646 1.00 121.98 ? 1833 LYS B CA 1 ATOM 5973 C C . LYS B 2 186 ? -23.360 -51.444 67.339 1.00 114.93 ? 1833 LYS B C 1 ATOM 5974 O O . LYS B 2 186 ? -22.157 -51.364 67.063 1.00 104.41 ? 1833 LYS B O 1 ATOM 5975 C CB . LYS B 2 186 ? -24.096 -53.868 67.269 1.00 117.32 ? 1833 LYS B CB 1 ATOM 5976 C CG . LYS B 2 186 ? -25.206 -54.298 68.202 1.00 113.52 ? 1833 LYS B CG 1 ATOM 5977 C CD . LYS B 2 186 ? -24.787 -55.584 68.900 1.00 123.75 ? 1833 LYS B CD 1 ATOM 5978 C CE . LYS B 2 186 ? -25.912 -56.278 69.668 1.00 129.29 ? 1833 LYS B CE 1 ATOM 5979 N NZ . LYS B 2 186 ? -26.546 -55.463 70.749 1.00 137.34 ? 1833 LYS B NZ 1 ATOM 5980 N N . ALA B 2 187 ? -23.916 -50.634 68.225 1.00 111.76 ? 1834 ALA B N 1 ATOM 5981 C CA . ALA B 2 187 ? -23.050 -49.750 68.988 1.00 111.14 ? 1834 ALA B CA 1 ATOM 5982 C C . ALA B 2 187 ? -22.779 -50.300 70.375 1.00 113.88 ? 1834 ALA B C 1 ATOM 5983 O O . ALA B 2 187 ? -23.651 -50.933 70.999 1.00 117.15 ? 1834 ALA B O 1 ATOM 5984 C CB . ALA B 2 187 ? -23.634 -48.364 69.076 1.00 127.35 ? 1834 ALA B CB 1 ATOM 5985 N N . TRP B 2 188 ? -21.558 -50.059 70.840 1.00 108.80 ? 1835 TRP B N 1 ATOM 5986 C CA . TRP B 2 188 ? -21.103 -50.527 72.136 1.00 115.20 ? 1835 TRP B CA 1 ATOM 5987 C C . TRP B 2 188 ? -20.414 -49.356 72.751 1.00 119.03 ? 1835 TRP B C 1 ATOM 5988 O O . TRP B 2 188 ? -19.838 -48.557 72.019 1.00 122.64 ? 1835 TRP B O 1 ATOM 5989 C CB . TRP B 2 188 ? -20.061 -51.604 71.967 1.00 120.61 ? 1835 TRP B CB 1 ATOM 5990 C CG . TRP B 2 188 ? -20.585 -52.927 71.539 1.00 134.86 ? 1835 TRP B CG 1 ATOM 5991 C CD1 . TRP B 2 188 ? -20.562 -53.461 70.272 1.00 150.79 ? 1835 TRP B CD1 1 ATOM 5992 C CD2 . TRP B 2 188 ? -21.179 -53.910 72.372 1.00 129.39 ? 1835 TRP B CD2 1 ATOM 5993 N NE1 . TRP B 2 188 ? -21.113 -54.722 70.275 1.00 138.33 ? 1835 TRP B NE1 1 ATOM 5994 C CE2 . TRP B 2 188 ? -21.493 -55.022 71.554 1.00 128.91 ? 1835 TRP B CE2 1 ATOM 5995 C CE3 . TRP B 2 188 ? -21.471 -53.966 73.731 1.00 135.86 ? 1835 TRP B CE3 1 ATOM 5996 C CZ2 . TRP B 2 188 ? -22.078 -56.168 72.054 1.00 133.04 ? 1835 TRP B CZ2 1 ATOM 5997 C CZ3 . TRP B 2 188 ? -22.054 -55.109 74.226 1.00 150.76 ? 1835 TRP B CZ3 1 ATOM 5998 C CH2 . TRP B 2 188 ? -22.358 -56.196 73.388 1.00 144.46 ? 1835 TRP B CH2 1 ATOM 5999 N N . ALA B 2 189 ? -20.437 -49.282 74.083 1.00 126.32 ? 1836 ALA B N 1 ATOM 6000 C CA . ALA B 2 189 ? -19.854 -48.163 74.831 1.00 129.79 ? 1836 ALA B CA 1 ATOM 6001 C C . ALA B 2 189 ? -18.399 -48.401 75.235 1.00 137.89 ? 1836 ALA B C 1 ATOM 6002 O O . ALA B 2 189 ? -18.012 -49.546 75.484 1.00 157.82 ? 1836 ALA B O 1 ATOM 6003 C CB . ALA B 2 189 ? -20.687 -47.902 76.065 1.00 137.50 ? 1836 ALA B CB 1 ATOM 6004 N N . TYR B 2 190 ? -17.603 -47.328 75.292 1.00 132.03 ? 1837 TYR B N 1 ATOM 6005 C CA . TYR B 2 190 ? -16.253 -47.376 75.891 1.00 136.23 ? 1837 TYR B CA 1 ATOM 6006 C C . TYR B 2 190 ? -16.024 -46.131 76.727 1.00 134.66 ? 1837 TYR B C 1 ATOM 6007 O O . TYR B 2 190 ? -16.505 -45.046 76.370 1.00 131.98 ? 1837 TYR B O 1 ATOM 6008 C CB . TYR B 2 190 ? -15.129 -47.566 74.849 1.00 142.83 ? 1837 TYR B CB 1 ATOM 6009 C CG . TYR B 2 190 ? -14.776 -46.336 74.006 1.00 153.64 ? 1837 TYR B CG 1 ATOM 6010 C CD1 . TYR B 2 190 ? -13.888 -45.353 74.476 1.00 149.34 ? 1837 TYR B CD1 1 ATOM 6011 C CD2 . TYR B 2 190 ? -15.309 -46.170 72.725 1.00 150.29 ? 1837 TYR B CD2 1 ATOM 6012 C CE1 . TYR B 2 190 ? -13.564 -44.245 73.703 1.00 135.77 ? 1837 TYR B CE1 1 ATOM 6013 C CE2 . TYR B 2 190 ? -14.988 -45.066 71.948 1.00 137.08 ? 1837 TYR B CE2 1 ATOM 6014 C CZ . TYR B 2 190 ? -14.119 -44.112 72.439 1.00 135.09 ? 1837 TYR B CZ 1 ATOM 6015 O OH . TYR B 2 190 ? -13.818 -43.033 71.650 1.00 132.69 ? 1837 TYR B OH 1 ATOM 6016 N N . PHE B 2 191 ? -15.293 -46.296 77.831 1.00 136.34 ? 1838 PHE B N 1 ATOM 6017 C CA . PHE B 2 191 ? -15.113 -45.238 78.848 1.00 147.45 ? 1838 PHE B CA 1 ATOM 6018 C C . PHE B 2 191 ? -14.090 -45.685 79.866 1.00 147.42 ? 1838 PHE B C 1 ATOM 6019 O O . PHE B 2 191 ? -13.847 -46.888 79.980 1.00 161.50 ? 1838 PHE B O 1 ATOM 6020 C CB . PHE B 2 191 ? -16.421 -44.984 79.592 1.00 154.88 ? 1838 PHE B CB 1 ATOM 6021 C CG . PHE B 2 191 ? -16.977 -46.203 80.273 1.00 145.44 ? 1838 PHE B CG 1 ATOM 6022 C CD1 . PHE B 2 191 ? -17.732 -47.126 79.560 1.00 132.71 ? 1838 PHE B CD1 1 ATOM 6023 C CD2 . PHE B 2 191 ? -16.754 -46.417 81.623 1.00 147.99 ? 1838 PHE B CD2 1 ATOM 6024 C CE1 . PHE B 2 191 ? -18.247 -48.240 80.171 1.00 128.25 ? 1838 PHE B CE1 1 ATOM 6025 C CE2 . PHE B 2 191 ? -17.269 -47.536 82.243 1.00 150.51 ? 1838 PHE B CE2 1 ATOM 6026 C CZ . PHE B 2 191 ? -18.014 -48.449 81.511 1.00 143.51 ? 1838 PHE B CZ 1 ATOM 6027 N N . SER B 2 192 ? -13.521 -44.749 80.632 1.00 135.35 ? 1839 SER B N 1 ATOM 6028 C CA . SER B 2 192 ? -12.486 -45.146 81.586 1.00 135.97 ? 1839 SER B CA 1 ATOM 6029 C C . SER B 2 192 ? -13.091 -45.717 82.824 1.00 135.51 ? 1839 SER B C 1 ATOM 6030 O O . SER B 2 192 ? -14.079 -45.173 83.350 1.00 119.78 ? 1839 SER B O 1 ATOM 6031 C CB . SER B 2 192 ? -11.558 -44.019 81.994 1.00 147.44 ? 1839 SER B CB 1 ATOM 6032 O OG . SER B 2 192 ? -10.651 -44.502 82.978 1.00 140.91 ? 1839 SER B OG 1 ATOM 6033 N N . ASP B 2 193 ? -12.459 -46.810 83.270 1.00 148.45 ? 1840 ASP B N 1 ATOM 6034 C CA . ASP B 2 193 ? -12.902 -47.606 84.426 1.00 167.00 ? 1840 ASP B CA 1 ATOM 6035 C C . ASP B 2 193 ? -12.008 -47.426 85.658 1.00 165.04 ? 1840 ASP B C 1 ATOM 6036 O O . ASP B 2 193 ? -11.982 -48.255 86.575 1.00 162.98 ? 1840 ASP B O 1 ATOM 6037 C CB . ASP B 2 193 ? -13.189 -49.102 84.063 1.00 180.46 ? 1840 ASP B CB 1 ATOM 6038 C CG . ASP B 2 193 ? -11.925 -49.978 83.918 1.00 190.84 ? 1840 ASP B CG 1 ATOM 6039 O OD1 . ASP B 2 193 ? -10.793 -49.440 83.830 1.00 195.38 ? 1840 ASP B OD1 1 ATOM 6040 O OD2 . ASP B 2 193 ? -12.094 -51.232 83.881 1.00 192.68 ? 1840 ASP B OD2 1 ATOM 6041 N N . VAL B 2 194 ? -11.307 -46.302 85.674 1.00 162.76 ? 1841 VAL B N 1 ATOM 6042 C CA . VAL B 2 194 ? -10.547 -45.909 86.833 1.00 165.23 ? 1841 VAL B CA 1 ATOM 6043 C C . VAL B 2 194 ? -11.506 -45.529 87.946 1.00 158.92 ? 1841 VAL B C 1 ATOM 6044 O O . VAL B 2 194 ? -11.361 -46.008 89.052 1.00 171.90 ? 1841 VAL B O 1 ATOM 6045 C CB . VAL B 2 194 ? -9.533 -44.818 86.484 1.00 177.43 ? 1841 VAL B CB 1 ATOM 6046 C CG1 . VAL B 2 194 ? -9.228 -43.924 87.681 1.00 189.35 ? 1841 VAL B CG1 1 ATOM 6047 C CG2 . VAL B 2 194 ? -8.274 -45.480 85.947 1.00 187.61 ? 1841 VAL B CG2 1 ATOM 6048 N N . ASP B 2 195 ? -12.485 -44.685 87.657 1.00 157.98 ? 1842 ASP B N 1 ATOM 6049 C CA . ASP B 2 195 ? -13.666 -44.598 88.504 1.00 177.54 ? 1842 ASP B CA 1 ATOM 6050 C C . ASP B 2 195 ? -14.827 -44.697 87.553 1.00 190.32 ? 1842 ASP B C 1 ATOM 6051 O O . ASP B 2 195 ? -15.159 -43.722 86.872 1.00 201.67 ? 1842 ASP B O 1 ATOM 6052 C CB . ASP B 2 195 ? -13.729 -43.296 89.316 1.00 188.20 ? 1842 ASP B CB 1 ATOM 6053 C CG . ASP B 2 195 ? -14.823 -43.322 90.397 1.00 197.98 ? 1842 ASP B CG 1 ATOM 6054 O OD1 . ASP B 2 195 ? -16.008 -43.527 90.051 1.00 201.22 ? 1842 ASP B OD1 1 ATOM 6055 O OD2 . ASP B 2 195 ? -14.500 -43.129 91.596 1.00 193.94 ? 1842 ASP B OD2 1 ATOM 6056 N N . LEU B 2 196 ? -15.430 -45.884 87.494 1.00 208.82 ? 1843 LEU B N 1 ATOM 6057 C CA . LEU B 2 196 ? -16.478 -46.186 86.503 1.00 201.67 ? 1843 LEU B CA 1 ATOM 6058 C C . LEU B 2 196 ? -17.553 -45.090 86.506 1.00 184.55 ? 1843 LEU B C 1 ATOM 6059 O O . LEU B 2 196 ? -18.173 -44.830 85.465 1.00 154.56 ? 1843 LEU B O 1 ATOM 6060 C CB . LEU B 2 196 ? -17.065 -47.610 86.698 1.00 205.11 ? 1843 LEU B CB 1 ATOM 6061 C CG . LEU B 2 196 ? -16.079 -48.808 86.776 1.00 205.63 ? 1843 LEU B CG 1 ATOM 6062 C CD1 . LEU B 2 196 ? -15.697 -49.163 88.219 1.00 195.48 ? 1843 LEU B CD1 1 ATOM 6063 C CD2 . LEU B 2 196 ? -16.568 -50.043 86.016 1.00 179.56 ? 1843 LEU B CD2 1 ATOM 6064 N N . GLU B 2 197 ? -17.695 -44.434 87.674 1.00 185.12 ? 1844 GLU B N 1 ATOM 6065 C CA . GLU B 2 197 ? -18.656 -43.349 87.937 1.00 176.40 ? 1844 GLU B CA 1 ATOM 6066 C C . GLU B 2 197 ? -18.114 -41.940 87.659 1.00 171.28 ? 1844 GLU B C 1 ATOM 6067 O O . GLU B 2 197 ? -18.697 -41.213 86.850 1.00 177.17 ? 1844 GLU B O 1 ATOM 6068 C CB . GLU B 2 197 ? -19.191 -43.417 89.378 1.00 176.76 ? 1844 GLU B CB 1 ATOM 6069 C CG . GLU B 2 197 ? -20.642 -42.967 89.501 1.00 186.84 ? 1844 GLU B CG 1 ATOM 6070 C CD . GLU B 2 197 ? -20.881 -41.951 90.609 1.00 202.18 ? 1844 GLU B CD 1 ATOM 6071 O OE1 . GLU B 2 197 ? -20.466 -42.205 91.769 1.00 207.47 ? 1844 GLU B OE1 1 ATOM 6072 O OE2 . GLU B 2 197 ? -21.505 -40.898 90.313 1.00 194.23 ? 1844 GLU B OE2 1 ATOM 6073 N N . LYS B 2 198 ? -17.023 -41.554 88.329 1.00 161.32 ? 1845 LYS B N 1 ATOM 6074 C CA . LYS B 2 198 ? -16.429 -40.211 88.164 1.00 159.10 ? 1845 LYS B CA 1 ATOM 6075 C C . LYS B 2 198 ? -15.831 -39.927 86.760 1.00 162.44 ? 1845 LYS B C 1 ATOM 6076 O O . LYS B 2 198 ? -16.030 -38.834 86.193 1.00 157.09 ? 1845 LYS B O 1 ATOM 6077 C CB . LYS B 2 198 ? -15.405 -39.923 89.271 1.00 155.31 ? 1845 LYS B CB 1 ATOM 6078 C CG . LYS B 2 198 ? -15.898 -38.976 90.365 1.00 157.22 ? 1845 LYS B CG 1 ATOM 6079 C CD . LYS B 2 198 ? -14.765 -38.569 91.307 1.00 161.07 ? 1845 LYS B CD 1 ATOM 6080 C CE . LYS B 2 198 ? -15.188 -37.535 92.340 1.00 159.46 ? 1845 LYS B CE 1 ATOM 6081 N NZ . LYS B 2 198 ? -14.022 -37.199 93.204 1.00 166.73 ? 1845 LYS B NZ 1 ATOM 6082 N N . ASP B 2 199 ? -15.124 -40.917 86.206 1.00 160.23 ? 1846 ASP B N 1 ATOM 6083 C CA . ASP B 2 199 ? -14.525 -40.830 84.860 1.00 151.36 ? 1846 ASP B CA 1 ATOM 6084 C C . ASP B 2 199 ? -15.558 -40.902 83.732 1.00 141.95 ? 1846 ASP B C 1 ATOM 6085 O O . ASP B 2 199 ? -15.293 -41.384 82.625 1.00 140.78 ? 1846 ASP B O 1 ATOM 6086 C CB . ASP B 2 199 ? -13.441 -41.896 84.679 1.00 148.36 ? 1846 ASP B CB 1 ATOM 6087 C CG . ASP B 2 199 ? -12.341 -41.793 85.719 1.00 150.95 ? 1846 ASP B CG 1 ATOM 6088 O OD1 . ASP B 2 199 ? -12.214 -40.742 86.400 1.00 148.45 ? 1846 ASP B OD1 1 ATOM 6089 O OD2 . ASP B 2 199 ? -11.600 -42.784 85.851 1.00 152.60 ? 1846 ASP B OD2 1 ATOM 6090 N N . VAL B 2 200 ? -16.751 -40.439 84.050 1.00 135.49 ? 1847 VAL B N 1 ATOM 6091 C CA . VAL B 2 200 ? -17.746 -40.173 83.058 1.00 139.62 ? 1847 VAL B CA 1 ATOM 6092 C C . VAL B 2 200 ? -18.106 -38.713 83.212 1.00 151.64 ? 1847 VAL B C 1 ATOM 6093 O O . VAL B 2 200 ? -18.015 -37.948 82.258 1.00 161.54 ? 1847 VAL B O 1 ATOM 6094 C CB . VAL B 2 200 ? -18.946 -41.147 83.155 1.00 132.61 ? 1847 VAL B CB 1 ATOM 6095 C CG1 . VAL B 2 200 ? -20.306 -40.432 83.242 1.00 132.10 ? 1847 VAL B CG1 1 ATOM 6096 C CG2 . VAL B 2 200 ? -18.895 -42.083 81.963 1.00 126.40 ? 1847 VAL B CG2 1 ATOM 6097 N N . HIS B 2 201 ? -18.469 -38.316 84.427 1.00 156.09 ? 1848 HIS B N 1 ATOM 6098 C CA . HIS B 2 201 ? -18.871 -36.949 84.664 1.00 154.03 ? 1848 HIS B CA 1 ATOM 6099 C C . HIS B 2 201 ? -17.704 -36.072 84.281 1.00 157.34 ? 1848 HIS B C 1 ATOM 6100 O O . HIS B 2 201 ? -17.885 -35.041 83.621 1.00 163.47 ? 1848 HIS B O 1 ATOM 6101 C CB . HIS B 2 201 ? -19.329 -36.756 86.106 1.00 157.16 ? 1848 HIS B CB 1 ATOM 6102 C CG . HIS B 2 201 ? -20.703 -37.289 86.359 1.00 164.11 ? 1848 HIS B CG 1 ATOM 6103 N ND1 . HIS B 2 201 ? -20.957 -38.632 86.544 1.00 173.99 ? 1848 HIS B ND1 1 ATOM 6104 C CD2 . HIS B 2 201 ? -21.903 -36.667 86.415 1.00 162.48 ? 1848 HIS B CD2 1 ATOM 6105 C CE1 . HIS B 2 201 ? -22.252 -38.815 86.719 1.00 174.27 ? 1848 HIS B CE1 1 ATOM 6106 N NE2 . HIS B 2 201 ? -22.848 -37.638 86.645 1.00 181.12 ? 1848 HIS B NE2 1 ATOM 6107 N N . SER B 2 202 ? -16.502 -36.526 84.634 1.00 156.93 ? 1849 SER B N 1 ATOM 6108 C CA . SER B 2 202 ? -15.282 -35.870 84.181 1.00 164.13 ? 1849 SER B CA 1 ATOM 6109 C C . SER B 2 202 ? -15.360 -35.626 82.659 1.00 164.00 ? 1849 SER B C 1 ATOM 6110 O O . SER B 2 202 ? -15.192 -34.486 82.219 1.00 160.03 ? 1849 SER B O 1 ATOM 6111 C CB . SER B 2 202 ? -14.037 -36.679 84.581 1.00 166.71 ? 1849 SER B CB 1 ATOM 6112 O OG . SER B 2 202 ? -13.888 -36.804 85.993 1.00 155.26 ? 1849 SER B OG 1 ATOM 6113 N N . GLY B 2 203 ? -15.640 -36.683 81.878 1.00 160.35 ? 1850 GLY B N 1 ATOM 6114 C CA . GLY B 2 203 ? -15.976 -36.542 80.440 1.00 161.02 ? 1850 GLY B CA 1 ATOM 6115 C C . GLY B 2 203 ? -15.590 -37.634 79.432 1.00 154.47 ? 1850 GLY B C 1 ATOM 6116 O O . GLY B 2 203 ? -15.533 -37.405 78.208 1.00 155.52 ? 1850 GLY B O 1 ATOM 6117 N N . LEU B 2 204 ? -15.343 -38.836 79.912 1.00 145.65 ? 1851 LEU B N 1 ATOM 6118 C CA . LEU B 2 204 ? -14.772 -39.815 79.018 1.00 150.11 ? 1851 LEU B CA 1 ATOM 6119 C C . LEU B 2 204 ? -15.786 -40.878 78.592 1.00 150.63 ? 1851 LEU B C 1 ATOM 6120 O O . LEU B 2 204 ? -15.963 -41.870 79.302 1.00 162.23 ? 1851 LEU B O 1 ATOM 6121 C CB . LEU B 2 204 ? -13.521 -40.439 79.670 1.00 154.28 ? 1851 LEU B CB 1 ATOM 6122 C CG . LEU B 2 204 ? -12.251 -39.594 79.906 1.00 151.30 ? 1851 LEU B CG 1 ATOM 6123 C CD1 . LEU B 2 204 ? -12.411 -38.652 81.081 1.00 154.25 ? 1851 LEU B CD1 1 ATOM 6124 C CD2 . LEU B 2 204 ? -11.030 -40.460 80.155 1.00 144.65 ? 1851 LEU B CD2 1 ATOM 6125 N N . ILE B 2 205 ? -16.481 -40.658 77.471 1.00 137.91 ? 1852 ILE B N 1 ATOM 6126 C CA . ILE B 2 205 ? -17.165 -41.768 76.771 1.00 136.61 ? 1852 ILE B CA 1 ATOM 6127 C C . ILE B 2 205 ? -17.079 -41.532 75.305 1.00 140.82 ? 1852 ILE B C 1 ATOM 6128 O O . ILE B 2 205 ? -17.109 -40.376 74.846 1.00 137.18 ? 1852 ILE B O 1 ATOM 6129 C CB . ILE B 2 205 ? -18.699 -41.905 76.968 1.00 134.76 ? 1852 ILE B CB 1 ATOM 6130 C CG1 . ILE B 2 205 ? -19.247 -40.921 77.982 1.00 147.06 ? 1852 ILE B CG1 1 ATOM 6131 C CG2 . ILE B 2 205 ? -19.133 -43.363 77.144 1.00 124.67 ? 1852 ILE B CG2 1 ATOM 6132 C CD1 . ILE B 2 205 ? -19.602 -39.616 77.310 1.00 159.31 ? 1852 ILE B CD1 1 ATOM 6133 N N . GLY B 2 206 ? -17.020 -42.656 74.589 1.00 143.71 ? 1853 GLY B N 1 ATOM 6134 C CA . GLY B 2 206 ? -17.148 -42.713 73.138 1.00 138.00 ? 1853 GLY B CA 1 ATOM 6135 C C . GLY B 2 206 ? -17.886 -43.968 72.699 1.00 122.66 ? 1853 GLY B C 1 ATOM 6136 O O . GLY B 2 206 ? -18.107 -44.865 73.518 1.00 121.13 ? 1853 GLY B O 1 ATOM 6137 N N . PRO B 2 207 ? -18.295 -44.022 71.412 1.00 117.27 ? 1854 PRO B N 1 ATOM 6138 C CA . PRO B 2 207 ? -18.917 -45.193 70.812 1.00 116.86 ? 1854 PRO B CA 1 ATOM 6139 C C . PRO B 2 207 ? -17.937 -46.031 69.984 1.00 118.79 ? 1854 PRO B C 1 ATOM 6140 O O . PRO B 2 207 ? -16.974 -45.499 69.421 1.00 125.41 ? 1854 PRO B O 1 ATOM 6141 C CB . PRO B 2 207 ? -20.009 -44.589 69.923 1.00 113.29 ? 1854 PRO B CB 1 ATOM 6142 C CG . PRO B 2 207 ? -19.534 -43.208 69.598 1.00 114.59 ? 1854 PRO B CG 1 ATOM 6143 C CD . PRO B 2 207 ? -18.387 -42.860 70.509 1.00 121.74 ? 1854 PRO B CD 1 ATOM 6144 N N . LEU B 2 208 ? -18.206 -47.333 69.916 1.00 116.25 ? 1855 LEU B N 1 ATOM 6145 C CA . LEU B 2 208 ? -17.293 -48.302 69.327 1.00 114.79 ? 1855 LEU B CA 1 ATOM 6146 C C . LEU B 2 208 ? -18.120 -49.306 68.578 1.00 110.39 ? 1855 LEU B C 1 ATOM 6147 O O . LEU B 2 208 ? -18.638 -50.246 69.162 1.00 118.88 ? 1855 LEU B O 1 ATOM 6148 C CB . LEU B 2 208 ? -16.481 -48.993 70.421 1.00 119.21 ? 1855 LEU B CB 1 ATOM 6149 C CG . LEU B 2 208 ? -15.745 -50.295 70.136 1.00 118.53 ? 1855 LEU B CG 1 ATOM 6150 C CD1 . LEU B 2 208 ? -14.232 -50.110 70.113 1.00 114.22 ? 1855 LEU B CD1 1 ATOM 6151 C CD2 . LEU B 2 208 ? -16.161 -51.201 71.276 1.00 124.94 ? 1855 LEU B CD2 1 ATOM 6152 N N . LEU B 2 209 ? -18.235 -49.092 67.278 1.00 106.46 ? 1856 LEU B N 1 ATOM 6153 C CA . LEU B 2 209 ? -19.227 -49.770 66.463 1.00 107.31 ? 1856 LEU B CA 1 ATOM 6154 C C . LEU B 2 209 ? -18.714 -51.054 65.840 1.00 112.58 ? 1856 LEU B C 1 ATOM 6155 O O . LEU B 2 209 ? -17.697 -51.044 65.154 1.00 131.77 ? 1856 LEU B O 1 ATOM 6156 C CB . LEU B 2 209 ? -19.684 -48.824 65.364 1.00 104.96 ? 1856 LEU B CB 1 ATOM 6157 C CG . LEU B 2 209 ? -20.713 -47.757 65.737 1.00 113.06 ? 1856 LEU B CG 1 ATOM 6158 C CD1 . LEU B 2 209 ? -20.704 -47.415 67.225 1.00 119.12 ? 1856 LEU B CD1 1 ATOM 6159 C CD2 . LEU B 2 209 ? -20.505 -46.510 64.879 1.00 120.95 ? 1856 LEU B CD2 1 ATOM 6160 N N . VAL B 2 210 ? -19.414 -52.159 66.065 1.00 104.99 ? 1857 VAL B N 1 ATOM 6161 C CA . VAL B 2 210 ? -19.081 -53.389 65.363 1.00 103.09 ? 1857 VAL B CA 1 ATOM 6162 C C . VAL B 2 210 ? -20.027 -53.578 64.193 1.00 103.18 ? 1857 VAL B C 1 ATOM 6163 O O . VAL B 2 210 ? -21.237 -53.484 64.348 1.00 111.95 ? 1857 VAL B O 1 ATOM 6164 C CB . VAL B 2 210 ? -19.119 -54.598 66.297 1.00 102.18 ? 1857 VAL B CB 1 ATOM 6165 C CG1 . VAL B 2 210 ? -18.886 -55.881 65.501 1.00 100.38 ? 1857 VAL B CG1 1 ATOM 6166 C CG2 . VAL B 2 210 ? -18.070 -54.408 67.385 1.00 102.70 ? 1857 VAL B CG2 1 ATOM 6167 N N . CYS B 2 211 ? -19.489 -53.841 63.018 1.00 103.10 ? 1858 CYS B N 1 ATOM 6168 C CA . CYS B 2 211 ? -20.345 -53.958 61.856 1.00 109.09 ? 1858 CYS B CA 1 ATOM 6169 C C . CYS B 2 211 ? -20.202 -55.304 61.135 1.00 115.25 ? 1858 CYS B C 1 ATOM 6170 O O . CYS B 2 211 ? -19.247 -56.048 61.376 1.00 113.21 ? 1858 CYS B O 1 ATOM 6171 C CB . CYS B 2 211 ? -20.070 -52.798 60.921 1.00 122.62 ? 1858 CYS B CB 1 ATOM 6172 S SG . CYS B 2 211 ? -20.286 -51.167 61.668 1.00 150.91 ? 1858 CYS B SG 1 ATOM 6173 N N . HIS B 2 212 ? -21.179 -55.614 60.278 1.00 119.81 ? 1859 HIS B N 1 ATOM 6174 C CA . HIS B 2 212 ? -21.205 -56.848 59.480 1.00 129.18 ? 1859 HIS B CA 1 ATOM 6175 C C . HIS B 2 212 ? -20.143 -56.773 58.417 1.00 131.71 ? 1859 HIS B C 1 ATOM 6176 O O . HIS B 2 212 ? -19.771 -55.683 58.016 1.00 129.55 ? 1859 HIS B O 1 ATOM 6177 C CB . HIS B 2 212 ? -22.563 -57.022 58.802 1.00 143.53 ? 1859 HIS B CB 1 ATOM 6178 C CG . HIS B 2 212 ? -23.492 -57.925 59.542 1.00 150.31 ? 1859 HIS B CG 1 ATOM 6179 N ND1 . HIS B 2 212 ? -24.477 -57.449 60.381 1.00 134.02 ? 1859 HIS B ND1 1 ATOM 6180 C CD2 . HIS B 2 212 ? -23.579 -59.276 59.576 1.00 166.11 ? 1859 HIS B CD2 1 ATOM 6181 C CE1 . HIS B 2 212 ? -25.126 -58.469 60.908 1.00 144.88 ? 1859 HIS B CE1 1 ATOM 6182 N NE2 . HIS B 2 212 ? -24.604 -59.588 60.433 1.00 169.45 ? 1859 HIS B NE2 1 ATOM 6183 N N . THR B 2 213 ? -19.655 -57.913 57.938 1.00 137.47 ? 1860 THR B N 1 ATOM 6184 C CA . THR B 2 213 ? -18.547 -57.867 56.975 1.00 146.01 ? 1860 THR B CA 1 ATOM 6185 C C . THR B 2 213 ? -19.028 -57.261 55.645 1.00 143.08 ? 1860 THR B C 1 ATOM 6186 O O . THR B 2 213 ? -20.228 -57.253 55.354 1.00 142.48 ? 1860 THR B O 1 ATOM 6187 C CB . THR B 2 213 ? -17.822 -59.224 56.836 1.00 151.19 ? 1860 THR B CB 1 ATOM 6188 O OG1 . THR B 2 213 ? -18.660 -60.240 57.405 1.00 164.23 ? 1860 THR B OG1 1 ATOM 6189 C CG2 . THR B 2 213 ? -16.398 -59.217 57.553 1.00 141.11 ? 1860 THR B CG2 1 ATOM 6190 N N . ASN B 2 214 ? -18.088 -56.702 54.886 1.00 143.81 ? 1861 ASN B N 1 ATOM 6191 C CA . ASN B 2 214 ? -18.383 -55.906 53.690 1.00 146.39 ? 1861 ASN B CA 1 ATOM 6192 C C . ASN B 2 214 ? -19.366 -54.764 53.871 1.00 144.18 ? 1861 ASN B C 1 ATOM 6193 O O . ASN B 2 214 ? -19.979 -54.284 52.919 1.00 150.09 ? 1861 ASN B O 1 ATOM 6194 C CB . ASN B 2 214 ? -18.815 -56.798 52.552 1.00 152.95 ? 1861 ASN B CB 1 ATOM 6195 C CG . ASN B 2 214 ? -17.644 -57.365 51.821 1.00 168.99 ? 1861 ASN B CG 1 ATOM 6196 O OD1 . ASN B 2 214 ? -16.649 -56.668 51.596 1.00 174.90 ? 1861 ASN B OD1 1 ATOM 6197 N ND2 . ASN B 2 214 ? -17.736 -58.638 51.452 1.00 185.89 ? 1861 ASN B ND2 1 ATOM 6198 N N . THR B 2 215 ? -19.489 -54.314 55.105 1.00 138.70 ? 1862 THR B N 1 ATOM 6199 C CA . THR B 2 215 ? -20.335 -53.199 55.396 1.00 135.10 ? 1862 THR B CA 1 ATOM 6200 C C . THR B 2 215 ? -19.607 -51.852 55.482 1.00 138.49 ? 1862 THR B C 1 ATOM 6201 O O . THR B 2 215 ? -20.162 -50.846 55.050 1.00 149.96 ? 1862 THR B O 1 ATOM 6202 C CB . THR B 2 215 ? -21.078 -53.424 56.695 1.00 140.19 ? 1862 THR B CB 1 ATOM 6203 O OG1 . THR B 2 215 ? -21.979 -52.335 56.888 1.00 174.43 ? 1862 THR B OG1 1 ATOM 6204 C CG2 . THR B 2 215 ? -20.106 -53.464 57.848 1.00 138.72 ? 1862 THR B CG2 1 ATOM 6205 N N . LEU B 2 216 ? -18.402 -51.812 56.059 1.00 135.28 ? 1863 LEU B N 1 ATOM 6206 C CA . LEU B 2 216 ? -17.640 -50.563 56.106 1.00 133.68 ? 1863 LEU B CA 1 ATOM 6207 C C . LEU B 2 216 ? -16.910 -50.405 54.803 1.00 144.30 ? 1863 LEU B C 1 ATOM 6208 O O . LEU B 2 216 ? -16.398 -51.377 54.254 1.00 154.10 ? 1863 LEU B O 1 ATOM 6209 C CB . LEU B 2 216 ? -16.649 -50.545 57.250 1.00 130.79 ? 1863 LEU B CB 1 ATOM 6210 C CG . LEU B 2 216 ? -17.247 -50.823 58.625 1.00 143.29 ? 1863 LEU B CG 1 ATOM 6211 C CD1 . LEU B 2 216 ? -16.109 -51.236 59.549 1.00 152.22 ? 1863 LEU B CD1 1 ATOM 6212 C CD2 . LEU B 2 216 ? -18.084 -49.673 59.204 1.00 134.18 ? 1863 LEU B CD2 1 ATOM 6213 N N . ASN B 2 217 ? -16.874 -49.181 54.301 1.00 153.28 ? 1864 ASN B N 1 ATOM 6214 C CA . ASN B 2 217 ? -16.342 -48.936 52.980 1.00 165.54 ? 1864 ASN B CA 1 ATOM 6215 C C . ASN B 2 217 ? -14.824 -48.789 52.993 1.00 173.40 ? 1864 ASN B C 1 ATOM 6216 O O . ASN B 2 217 ? -14.298 -47.997 53.773 1.00 173.52 ? 1864 ASN B O 1 ATOM 6217 C CB . ASN B 2 217 ? -16.980 -47.694 52.402 1.00 176.12 ? 1864 ASN B CB 1 ATOM 6218 C CG . ASN B 2 217 ? -16.798 -47.612 50.923 1.00 201.07 ? 1864 ASN B CG 1 ATOM 6219 O OD1 . ASN B 2 217 ? -15.933 -46.879 50.436 1.00 208.89 ? 1864 ASN B OD1 1 ATOM 6220 N ND2 . ASN B 2 217 ? -17.577 -48.407 50.189 1.00 217.10 ? 1864 ASN B ND2 1 ATOM 6221 N N . PRO B 2 218 ? -14.112 -49.533 52.116 1.00 180.12 ? 1865 PRO B N 1 ATOM 6222 C CA . PRO B 2 218 ? -12.655 -49.578 52.221 1.00 173.32 ? 1865 PRO B CA 1 ATOM 6223 C C . PRO B 2 218 ? -12.096 -48.175 52.196 1.00 181.36 ? 1865 PRO B C 1 ATOM 6224 O O . PRO B 2 218 ? -12.639 -47.310 51.495 1.00 170.28 ? 1865 PRO B O 1 ATOM 6225 C CB . PRO B 2 218 ? -12.226 -50.336 50.958 1.00 182.21 ? 1865 PRO B CB 1 ATOM 6226 C CG . PRO B 2 218 ? -13.362 -50.186 50.002 1.00 189.91 ? 1865 PRO B CG 1 ATOM 6227 C CD . PRO B 2 218 ? -14.589 -50.171 50.873 1.00 192.29 ? 1865 PRO B CD 1 ATOM 6228 N N . ALA B 2 219 ? -11.039 -47.966 52.983 1.00 202.91 ? 1866 ALA B N 1 ATOM 6229 C CA . ALA B 2 219 ? -10.333 -46.670 53.134 1.00 211.68 ? 1866 ALA B CA 1 ATOM 6230 C C . ALA B 2 219 ? -11.229 -45.455 53.474 1.00 199.41 ? 1866 ALA B C 1 ATOM 6231 O O . ALA B 2 219 ? -10.909 -44.659 54.370 1.00 187.52 ? 1866 ALA B O 1 ATOM 6232 C CB . ALA B 2 219 ? -9.422 -46.383 51.927 1.00 202.31 ? 1866 ALA B CB 1 ATOM 6233 N N . HIS B 2 220 ? -12.365 -45.357 52.788 1.00 186.69 ? 1867 HIS B N 1 ATOM 6234 C CA . HIS B 2 220 ? -13.208 -44.171 52.777 1.00 176.23 ? 1867 HIS B CA 1 ATOM 6235 C C . HIS B 2 220 ? -13.894 -43.830 54.111 1.00 173.75 ? 1867 HIS B C 1 ATOM 6236 O O . HIS B 2 220 ? -14.994 -43.278 54.115 1.00 181.15 ? 1867 HIS B O 1 ATOM 6237 C CB . HIS B 2 220 ? -14.254 -44.336 51.678 1.00 171.99 ? 1867 HIS B CB 1 ATOM 6238 C CG . HIS B 2 220 ? -14.944 -43.065 51.318 1.00 186.92 ? 1867 HIS B CG 1 ATOM 6239 N ND1 . HIS B 2 220 ? -16.102 -42.650 51.938 1.00 189.87 ? 1867 HIS B ND1 1 ATOM 6240 C CD2 . HIS B 2 220 ? -14.629 -42.103 50.418 1.00 201.53 ? 1867 HIS B CD2 1 ATOM 6241 C CE1 . HIS B 2 220 ? -16.478 -41.491 51.428 1.00 207.58 ? 1867 HIS B CE1 1 ATOM 6242 N NE2 . HIS B 2 220 ? -15.604 -41.140 50.500 1.00 213.66 ? 1867 HIS B NE2 1 ATOM 6243 N N . GLY B 2 221 ? -13.237 -44.116 55.236 1.00 163.73 ? 1868 GLY B N 1 ATOM 6244 C CA . GLY B 2 221 ? -13.912 -44.080 56.531 1.00 148.74 ? 1868 GLY B CA 1 ATOM 6245 C C . GLY B 2 221 ? -14.840 -45.285 56.622 1.00 139.11 ? 1868 GLY B C 1 ATOM 6246 O O . GLY B 2 221 ? -14.579 -46.315 56.013 1.00 130.10 ? 1868 GLY B O 1 ATOM 6247 N N . ARG B 2 222 ? -15.942 -45.168 57.351 1.00 140.06 ? 1869 ARG B N 1 ATOM 6248 C CA . ARG B 2 222 ? -16.691 -46.367 57.714 1.00 148.18 ? 1869 ARG B CA 1 ATOM 6249 C C . ARG B 2 222 ? -18.213 -46.279 57.501 1.00 141.94 ? 1869 ARG B C 1 ATOM 6250 O O . ARG B 2 222 ? -18.808 -45.203 57.617 1.00 130.96 ? 1869 ARG B O 1 ATOM 6251 C CB . ARG B 2 222 ? -16.318 -46.780 59.145 1.00 173.25 ? 1869 ARG B CB 1 ATOM 6252 C CG . ARG B 2 222 ? -14.949 -47.472 59.298 1.00 202.62 ? 1869 ARG B CG 1 ATOM 6253 C CD . ARG B 2 222 ? -13.729 -46.560 59.539 1.00 217.81 ? 1869 ARG B CD 1 ATOM 6254 N NE . ARG B 2 222 ? -12.491 -47.328 59.801 1.00 234.81 ? 1869 ARG B NE 1 ATOM 6255 C CZ . ARG B 2 222 ? -11.245 -46.918 59.533 1.00 234.50 ? 1869 ARG B CZ 1 ATOM 6256 N NH1 . ARG B 2 222 ? -11.034 -45.729 58.978 1.00 249.00 ? 1869 ARG B NH1 1 ATOM 6257 N NH2 . ARG B 2 222 ? -10.202 -47.704 59.813 1.00 208.49 ? 1869 ARG B NH2 1 ATOM 6258 N N . GLN B 2 223 ? -18.824 -47.435 57.221 1.00 142.10 ? 1870 GLN B N 1 ATOM 6259 C CA . GLN B 2 223 ? -20.139 -47.544 56.549 1.00 146.36 ? 1870 GLN B CA 1 ATOM 6260 C C . GLN B 2 223 ? -20.108 -46.666 55.313 1.00 140.41 ? 1870 GLN B C 1 ATOM 6261 O O . GLN B 2 223 ? -19.059 -46.572 54.684 1.00 147.56 ? 1870 GLN B O 1 ATOM 6262 C CB . GLN B 2 223 ? -21.340 -47.218 57.460 1.00 164.21 ? 1870 GLN B CB 1 ATOM 6263 C CG . GLN B 2 223 ? -22.728 -47.368 56.787 1.00 176.08 ? 1870 GLN B CG 1 ATOM 6264 C CD . GLN B 2 223 ? -23.376 -48.764 56.889 1.00 165.74 ? 1870 GLN B CD 1 ATOM 6265 O OE1 . GLN B 2 223 ? -24.413 -49.049 56.255 1.00 138.66 ? 1870 GLN B OE1 1 ATOM 6266 N NE2 . GLN B 2 223 ? -22.787 -49.626 57.707 1.00 167.98 ? 1870 GLN B NE2 1 ATOM 6267 N N . VAL B 2 224 ? -21.238 -46.046 54.962 1.00 137.52 ? 1871 VAL B N 1 ATOM 6268 C CA . VAL B 2 224 ? -21.312 -45.059 53.866 1.00 143.11 ? 1871 VAL B CA 1 ATOM 6269 C C . VAL B 2 224 ? -22.733 -44.812 53.326 1.00 131.75 ? 1871 VAL B C 1 ATOM 6270 O O . VAL B 2 224 ? -23.066 -43.692 52.948 1.00 134.83 ? 1871 VAL B O 1 ATOM 6271 C CB . VAL B 2 224 ? -20.297 -45.352 52.705 1.00 149.37 ? 1871 VAL B CB 1 ATOM 6272 C CG1 . VAL B 2 224 ? -20.785 -46.462 51.772 1.00 153.69 ? 1871 VAL B CG1 1 ATOM 6273 C CG2 . VAL B 2 224 ? -19.929 -44.076 51.940 1.00 141.04 ? 1871 VAL B CG2 1 ATOM 6274 N N . THR B 2 225 ? -23.559 -45.851 53.305 1.00 122.68 ? 1872 THR B N 1 ATOM 6275 C CA . THR B 2 225 ? -24.876 -45.794 52.649 1.00 126.69 ? 1872 THR B CA 1 ATOM 6276 C C . THR B 2 225 ? -26.048 -45.368 53.552 1.00 126.83 ? 1872 THR B C 1 ATOM 6277 O O . THR B 2 225 ? -27.223 -45.310 53.132 1.00 119.18 ? 1872 THR B O 1 ATOM 6278 C CB . THR B 2 225 ? -25.202 -47.135 52.002 1.00 128.75 ? 1872 THR B CB 1 ATOM 6279 O OG1 . THR B 2 225 ? -24.668 -48.184 52.819 1.00 126.74 ? 1872 THR B OG1 1 ATOM 6280 C CG2 . THR B 2 225 ? -24.578 -47.190 50.628 1.00 138.82 ? 1872 THR B CG2 1 ATOM 6281 N N . VAL B 2 226 ? -25.714 -45.074 54.798 1.00 120.57 ? 1873 VAL B N 1 ATOM 6282 C CA . VAL B 2 226 ? -26.654 -44.478 55.706 1.00 117.39 ? 1873 VAL B CA 1 ATOM 6283 C C . VAL B 2 226 ? -25.838 -43.480 56.504 1.00 122.80 ? 1873 VAL B C 1 ATOM 6284 O O . VAL B 2 226 ? -24.617 -43.672 56.678 1.00 123.35 ? 1873 VAL B O 1 ATOM 6285 C CB . VAL B 2 226 ? -27.275 -45.529 56.632 1.00 120.27 ? 1873 VAL B CB 1 ATOM 6286 C CG1 . VAL B 2 226 ? -27.131 -46.941 56.036 1.00 119.22 ? 1873 VAL B CG1 1 ATOM 6287 C CG2 . VAL B 2 226 ? -26.666 -45.444 58.031 1.00 123.04 ? 1873 VAL B CG2 1 ATOM 6288 N N . GLN B 2 227 ? -26.488 -42.402 56.943 1.00 123.46 ? 1874 GLN B N 1 ATOM 6289 C CA . GLN B 2 227 ? -25.845 -41.458 57.840 1.00 119.51 ? 1874 GLN B CA 1 ATOM 6290 C C . GLN B 2 227 ? -26.077 -42.011 59.238 1.00 116.37 ? 1874 GLN B C 1 ATOM 6291 O O . GLN B 2 227 ? -27.205 -42.364 59.605 1.00 95.59 ? 1874 GLN B O 1 ATOM 6292 C CB . GLN B 2 227 ? -26.376 -40.035 57.651 1.00 116.80 ? 1874 GLN B CB 1 ATOM 6293 C CG . GLN B 2 227 ? -26.142 -39.471 56.247 1.00 127.13 ? 1874 GLN B CG 1 ATOM 6294 C CD . GLN B 2 227 ? -27.224 -38.477 55.783 1.00 139.31 ? 1874 GLN B CD 1 ATOM 6295 O OE1 . GLN B 2 227 ? -28.392 -38.836 55.598 1.00 135.44 ? 1874 GLN B OE1 1 ATOM 6296 N NE2 . GLN B 2 227 ? -26.824 -37.224 55.566 1.00 146.80 ? 1874 GLN B NE2 1 ATOM 6297 N N . GLU B 2 228 ? -24.967 -42.174 59.959 1.00 129.29 ? 1875 GLU B N 1 ATOM 6298 C CA . GLU B 2 228 ? -24.950 -42.659 61.333 1.00 127.58 ? 1875 GLU B CA 1 ATOM 6299 C C . GLU B 2 228 ? -24.864 -41.424 62.190 1.00 128.85 ? 1875 GLU B C 1 ATOM 6300 O O . GLU B 2 228 ? -24.162 -40.473 61.824 1.00 141.72 ? 1875 GLU B O 1 ATOM 6301 C CB . GLU B 2 228 ? -23.691 -43.480 61.612 1.00 127.06 ? 1875 GLU B CB 1 ATOM 6302 C CG . GLU B 2 228 ? -23.628 -44.853 60.975 1.00 127.83 ? 1875 GLU B CG 1 ATOM 6303 C CD . GLU B 2 228 ? -22.220 -45.415 60.979 1.00 128.20 ? 1875 GLU B CD 1 ATOM 6304 O OE1 . GLU B 2 228 ? -21.284 -44.648 60.682 1.00 128.04 ? 1875 GLU B OE1 1 ATOM 6305 O OE2 . GLU B 2 228 ? -22.049 -46.620 61.264 1.00 129.40 ? 1875 GLU B OE2 1 ATOM 6306 N N . PHE B 2 229 ? -25.557 -41.456 63.326 1.00 117.65 ? 1876 PHE B N 1 ATOM 6307 C CA . PHE B 2 229 ? -25.463 -40.409 64.332 1.00 112.41 ? 1876 PHE B CA 1 ATOM 6308 C C . PHE B 2 229 ? -25.542 -41.024 65.712 1.00 111.67 ? 1876 PHE B C 1 ATOM 6309 O O . PHE B 2 229 ? -26.438 -41.841 65.956 1.00 121.63 ? 1876 PHE B O 1 ATOM 6310 C CB . PHE B 2 229 ? -26.623 -39.444 64.177 1.00 116.24 ? 1876 PHE B CB 1 ATOM 6311 C CG . PHE B 2 229 ? -26.516 -38.557 62.983 1.00 121.67 ? 1876 PHE B CG 1 ATOM 6312 C CD1 . PHE B 2 229 ? -25.334 -37.900 62.690 1.00 133.24 ? 1876 PHE B CD1 1 ATOM 6313 C CD2 . PHE B 2 229 ? -27.604 -38.366 62.152 1.00 126.01 ? 1876 PHE B CD2 1 ATOM 6314 C CE1 . PHE B 2 229 ? -25.235 -37.078 61.575 1.00 153.83 ? 1876 PHE B CE1 1 ATOM 6315 C CE2 . PHE B 2 229 ? -27.521 -37.536 61.045 1.00 133.61 ? 1876 PHE B CE2 1 ATOM 6316 C CZ . PHE B 2 229 ? -26.333 -36.893 60.751 1.00 148.58 ? 1876 PHE B CZ 1 ATOM 6317 N N . ALA B 2 230 ? -24.644 -40.622 66.619 1.00 98.85 ? 1877 ALA B N 1 ATOM 6318 C CA . ALA B 2 230 ? -24.665 -41.159 67.994 1.00 97.76 ? 1877 ALA B CA 1 ATOM 6319 C C . ALA B 2 230 ? -24.962 -40.176 69.151 1.00 105.17 ? 1877 ALA B C 1 ATOM 6320 O O . ALA B 2 230 ? -24.098 -39.414 69.576 1.00 104.39 ? 1877 ALA B O 1 ATOM 6321 C CB . ALA B 2 230 ? -23.422 -41.988 68.281 1.00 87.73 ? 1877 ALA B CB 1 ATOM 6322 N N . LEU B 2 231 ? -26.197 -40.233 69.660 1.00 118.55 ? 1878 LEU B N 1 ATOM 6323 C CA . LEU B 2 231 ? -26.677 -39.391 70.770 1.00 118.58 ? 1878 LEU B CA 1 ATOM 6324 C C . LEU B 2 231 ? -26.546 -40.096 72.131 1.00 124.02 ? 1878 LEU B C 1 ATOM 6325 O O . LEU B 2 231 ? -26.718 -41.314 72.241 1.00 127.37 ? 1878 LEU B O 1 ATOM 6326 C CB . LEU B 2 231 ? -28.126 -38.939 70.517 1.00 115.93 ? 1878 LEU B CB 1 ATOM 6327 C CG . LEU B 2 231 ? -28.432 -38.348 69.128 1.00 126.64 ? 1878 LEU B CG 1 ATOM 6328 C CD1 . LEU B 2 231 ? -29.725 -37.539 69.103 1.00 134.16 ? 1878 LEU B CD1 1 ATOM 6329 C CD2 . LEU B 2 231 ? -27.282 -37.488 68.610 1.00 129.88 ? 1878 LEU B CD2 1 ATOM 6330 N N . PHE B 2 232 ? -26.243 -39.323 73.168 1.00 124.79 ? 1879 PHE B N 1 ATOM 6331 C CA . PHE B 2 232 ? -25.915 -39.876 74.480 1.00 119.41 ? 1879 PHE B CA 1 ATOM 6332 C C . PHE B 2 232 ? -26.472 -38.962 75.564 1.00 120.93 ? 1879 PHE B C 1 ATOM 6333 O O . PHE B 2 232 ? -26.094 -37.799 75.661 1.00 136.54 ? 1879 PHE B O 1 ATOM 6334 C CB . PHE B 2 232 ? -24.394 -40.007 74.575 1.00 122.29 ? 1879 PHE B CB 1 ATOM 6335 C CG . PHE B 2 232 ? -23.855 -39.969 75.968 1.00 121.89 ? 1879 PHE B CG 1 ATOM 6336 C CD1 . PHE B 2 232 ? -23.574 -38.766 76.584 1.00 129.56 ? 1879 PHE B CD1 1 ATOM 6337 C CD2 . PHE B 2 232 ? -23.593 -41.134 76.643 1.00 125.22 ? 1879 PHE B CD2 1 ATOM 6338 C CE1 . PHE B 2 232 ? -23.069 -38.726 77.862 1.00 132.24 ? 1879 PHE B CE1 1 ATOM 6339 C CE2 . PHE B 2 232 ? -23.082 -41.107 77.922 1.00 130.25 ? 1879 PHE B CE2 1 ATOM 6340 C CZ . PHE B 2 232 ? -22.820 -39.902 78.534 1.00 128.55 ? 1879 PHE B CZ 1 ATOM 6341 N N . PHE B 2 233 ? -27.376 -39.473 76.379 1.00 116.30 ? 1880 PHE B N 1 ATOM 6342 C CA . PHE B 2 233 ? -28.112 -38.594 77.272 1.00 126.69 ? 1880 PHE B CA 1 ATOM 6343 C C . PHE B 2 233 ? -27.673 -38.793 78.703 1.00 137.89 ? 1880 PHE B C 1 ATOM 6344 O O . PHE B 2 233 ? -27.718 -39.913 79.216 1.00 145.27 ? 1880 PHE B O 1 ATOM 6345 C CB . PHE B 2 233 ? -29.615 -38.813 77.105 1.00 122.68 ? 1880 PHE B CB 1 ATOM 6346 C CG . PHE B 2 233 ? -30.087 -38.641 75.687 1.00 124.18 ? 1880 PHE B CG 1 ATOM 6347 C CD1 . PHE B 2 233 ? -29.822 -39.614 74.722 1.00 120.98 ? 1880 PHE B CD1 1 ATOM 6348 C CD2 . PHE B 2 233 ? -30.775 -37.495 75.300 1.00 132.44 ? 1880 PHE B CD2 1 ATOM 6349 C CE1 . PHE B 2 233 ? -30.247 -39.459 73.408 1.00 117.82 ? 1880 PHE B CE1 1 ATOM 6350 C CE2 . PHE B 2 233 ? -31.204 -37.332 73.985 1.00 129.34 ? 1880 PHE B CE2 1 ATOM 6351 C CZ . PHE B 2 233 ? -30.935 -38.317 73.040 1.00 124.80 ? 1880 PHE B CZ 1 ATOM 6352 N N . THR B 2 234 ? -27.216 -37.715 79.337 1.00 140.91 ? 1881 THR B N 1 ATOM 6353 C CA . THR B 2 234 ? -26.832 -37.779 80.747 1.00 141.61 ? 1881 THR B CA 1 ATOM 6354 C C . THR B 2 234 ? -27.324 -36.533 81.431 1.00 139.81 ? 1881 THR B C 1 ATOM 6355 O O . THR B 2 234 ? -27.763 -35.585 80.765 1.00 132.35 ? 1881 THR B O 1 ATOM 6356 C CB . THR B 2 234 ? -25.298 -37.926 80.937 1.00 141.30 ? 1881 THR B CB 1 ATOM 6357 O OG1 . THR B 2 234 ? -24.799 -38.802 79.931 1.00 145.86 ? 1881 THR B OG1 1 ATOM 6358 C CG2 . THR B 2 234 ? -24.907 -38.515 82.329 1.00 130.02 ? 1881 THR B CG2 1 ATOM 6359 N N . ILE B 2 235 ? -27.335 -36.612 82.763 1.00 143.16 ? 1882 ILE B N 1 ATOM 6360 C CA . ILE B 2 235 ? -27.218 -35.468 83.658 1.00 143.56 ? 1882 ILE B CA 1 ATOM 6361 C C . ILE B 2 235 ? -25.719 -35.365 83.938 1.00 141.46 ? 1882 ILE B C 1 ATOM 6362 O O . ILE B 2 235 ? -25.099 -36.313 84.414 1.00 142.47 ? 1882 ILE B O 1 ATOM 6363 C CB . ILE B 2 235 ? -28.047 -35.644 84.969 1.00 140.84 ? 1882 ILE B CB 1 ATOM 6364 C CG1 . ILE B 2 235 ? -29.456 -35.085 84.810 1.00 137.76 ? 1882 ILE B CG1 1 ATOM 6365 C CG2 . ILE B 2 235 ? -27.460 -34.866 86.130 1.00 142.94 ? 1882 ILE B CG2 1 ATOM 6366 C CD1 . ILE B 2 235 ? -30.406 -36.008 84.087 1.00 144.40 ? 1882 ILE B CD1 1 ATOM 6367 N N . PHE B 2 236 ? -25.124 -34.239 83.576 1.00 146.00 ? 1883 PHE B N 1 ATOM 6368 C CA . PHE B 2 236 ? -23.746 -33.978 83.946 1.00 155.81 ? 1883 PHE B CA 1 ATOM 6369 C C . PHE B 2 236 ? -23.796 -33.180 85.232 1.00 165.72 ? 1883 PHE B C 1 ATOM 6370 O O . PHE B 2 236 ? -24.405 -32.105 85.303 1.00 175.14 ? 1883 PHE B O 1 ATOM 6371 C CB . PHE B 2 236 ? -22.975 -33.258 82.826 1.00 156.60 ? 1883 PHE B CB 1 ATOM 6372 C CG . PHE B 2 236 ? -22.488 -34.183 81.743 1.00 156.25 ? 1883 PHE B CG 1 ATOM 6373 C CD1 . PHE B 2 236 ? -23.345 -34.590 80.708 1.00 153.86 ? 1883 PHE B CD1 1 ATOM 6374 C CD2 . PHE B 2 236 ? -21.185 -34.679 81.767 1.00 153.41 ? 1883 PHE B CD2 1 ATOM 6375 C CE1 . PHE B 2 236 ? -22.906 -35.451 79.709 1.00 143.05 ? 1883 PHE B CE1 1 ATOM 6376 C CE2 . PHE B 2 236 ? -20.742 -35.546 80.775 1.00 146.53 ? 1883 PHE B CE2 1 ATOM 6377 C CZ . PHE B 2 236 ? -21.603 -35.928 79.745 1.00 144.77 ? 1883 PHE B CZ 1 ATOM 6378 N N . ASP B 2 237 ? -23.190 -33.731 86.269 1.00 165.02 ? 1884 ASP B N 1 ATOM 6379 C CA . ASP B 2 237 ? -23.292 -33.110 87.570 1.00 175.49 ? 1884 ASP B CA 1 ATOM 6380 C C . ASP B 2 237 ? -21.913 -32.838 88.106 1.00 170.54 ? 1884 ASP B C 1 ATOM 6381 O O . ASP B 2 237 ? -21.260 -33.724 88.658 1.00 175.49 ? 1884 ASP B O 1 ATOM 6382 C CB . ASP B 2 237 ? -24.066 -34.018 88.519 1.00 187.00 ? 1884 ASP B CB 1 ATOM 6383 C CG . ASP B 2 237 ? -24.381 -33.351 89.833 1.00 188.07 ? 1884 ASP B CG 1 ATOM 6384 O OD1 . ASP B 2 237 ? -23.437 -32.876 90.503 1.00 189.12 ? 1884 ASP B OD1 1 ATOM 6385 O OD2 . ASP B 2 237 ? -25.578 -33.322 90.193 1.00 185.92 ? 1884 ASP B OD2 1 ATOM 6386 N N . GLU B 2 238 ? -21.471 -31.603 87.963 1.00 156.06 ? 1885 GLU B N 1 ATOM 6387 C CA . GLU B 2 238 ? -20.101 -31.324 88.278 1.00 157.74 ? 1885 GLU B CA 1 ATOM 6388 C C . GLU B 2 238 ? -19.852 -31.174 89.772 1.00 175.64 ? 1885 GLU B C 1 ATOM 6389 O O . GLU B 2 238 ? -19.064 -30.318 90.169 1.00 198.52 ? 1885 GLU B O 1 ATOM 6390 C CB . GLU B 2 238 ? -19.642 -30.111 87.502 1.00 156.68 ? 1885 GLU B CB 1 ATOM 6391 C CG . GLU B 2 238 ? -19.849 -30.274 86.007 1.00 159.49 ? 1885 GLU B CG 1 ATOM 6392 C CD . GLU B 2 238 ? -18.585 -30.649 85.243 1.00 165.68 ? 1885 GLU B CD 1 ATOM 6393 O OE1 . GLU B 2 238 ? -17.655 -31.278 85.806 1.00 166.48 ? 1885 GLU B OE1 1 ATOM 6394 O OE2 . GLU B 2 238 ? -18.526 -30.300 84.046 1.00 165.50 ? 1885 GLU B OE2 1 ATOM 6395 N N . THR B 2 239 ? -20.530 -31.991 90.592 1.00 176.72 ? 1886 THR B N 1 ATOM 6396 C CA . THR B 2 239 ? -20.125 -32.223 91.997 1.00 189.94 ? 1886 THR B CA 1 ATOM 6397 C C . THR B 2 239 ? -19.225 -33.443 91.998 1.00 194.01 ? 1886 THR B C 1 ATOM 6398 O O . THR B 2 239 ? -18.344 -33.600 92.847 1.00 210.60 ? 1886 THR B O 1 ATOM 6399 C CB . THR B 2 239 ? -21.307 -32.498 92.944 1.00 193.21 ? 1886 THR B CB 1 ATOM 6400 O OG1 . THR B 2 239 ? -22.393 -31.641 92.596 1.00 192.32 ? 1886 THR B OG1 1 ATOM 6401 C CG2 . THR B 2 239 ? -20.909 -32.281 94.442 1.00 196.60 ? 1886 THR B CG2 1 ATOM 6402 N N . LYS B 2 240 ? -19.473 -34.310 91.030 1.00 184.57 ? 1887 LYS B N 1 ATOM 6403 C CA . LYS B 2 240 ? -18.529 -35.331 90.650 1.00 187.91 ? 1887 LYS B CA 1 ATOM 6404 C C . LYS B 2 240 ? -17.450 -34.594 89.825 1.00 191.34 ? 1887 LYS B C 1 ATOM 6405 O O . LYS B 2 240 ? -17.300 -33.377 89.976 1.00 193.44 ? 1887 LYS B O 1 ATOM 6406 C CB . LYS B 2 240 ? -19.272 -36.419 89.864 1.00 195.67 ? 1887 LYS B CB 1 ATOM 6407 C CG . LYS B 2 240 ? -20.393 -37.129 90.649 1.00 208.62 ? 1887 LYS B CG 1 ATOM 6408 C CD . LYS B 2 240 ? -21.770 -36.451 90.596 1.00 200.48 ? 1887 LYS B CD 1 ATOM 6409 C CE . LYS B 2 240 ? -22.875 -37.283 91.260 1.00 192.18 ? 1887 LYS B CE 1 ATOM 6410 N NZ . LYS B 2 240 ? -23.274 -36.833 92.629 1.00 187.80 ? 1887 LYS B NZ 1 ATOM 6411 N N . SER B 2 241 ? -16.716 -35.295 88.956 1.00 193.97 ? 1888 SER B N 1 ATOM 6412 C CA . SER B 2 241 ? -15.597 -34.699 88.168 1.00 195.98 ? 1888 SER B CA 1 ATOM 6413 C C . SER B 2 241 ? -14.397 -34.470 89.071 1.00 195.82 ? 1888 SER B C 1 ATOM 6414 O O . SER B 2 241 ? -14.410 -33.538 89.876 1.00 206.70 ? 1888 SER B O 1 ATOM 6415 C CB . SER B 2 241 ? -15.989 -33.370 87.452 1.00 191.21 ? 1888 SER B CB 1 ATOM 6416 O OG . SER B 2 241 ? -14.992 -32.869 86.550 1.00 171.66 ? 1888 SER B OG 1 ATOM 6417 N N . TRP B 2 242 ? -13.376 -35.322 88.942 1.00 185.04 ? 1889 TRP B N 1 ATOM 6418 C CA . TRP B 2 242 ? -12.092 -35.122 89.616 1.00 188.50 ? 1889 TRP B CA 1 ATOM 6419 C C . TRP B 2 242 ? -11.686 -33.623 89.628 1.00 201.08 ? 1889 TRP B C 1 ATOM 6420 O O . TRP B 2 242 ? -10.822 -33.208 90.420 1.00 216.42 ? 1889 TRP B O 1 ATOM 6421 C CB . TRP B 2 242 ? -10.989 -35.947 88.929 1.00 183.16 ? 1889 TRP B CB 1 ATOM 6422 C CG . TRP B 2 242 ? -11.038 -37.436 89.111 1.00 175.95 ? 1889 TRP B CG 1 ATOM 6423 C CD1 . TRP B 2 242 ? -12.135 -38.217 89.072 1.00 177.41 ? 1889 TRP B CD1 1 ATOM 6424 C CD2 . TRP B 2 242 ? -9.921 -38.324 89.303 1.00 176.26 ? 1889 TRP B CD2 1 ATOM 6425 N NE1 . TRP B 2 242 ? -11.791 -39.529 89.257 1.00 181.51 ? 1889 TRP B NE1 1 ATOM 6426 C CE2 . TRP B 2 242 ? -10.433 -39.620 89.399 1.00 178.45 ? 1889 TRP B CE2 1 ATOM 6427 C CE3 . TRP B 2 242 ? -8.544 -38.143 89.418 1.00 174.86 ? 1889 TRP B CE3 1 ATOM 6428 C CZ2 . TRP B 2 242 ? -9.614 -40.740 89.601 1.00 179.07 ? 1889 TRP B CZ2 1 ATOM 6429 C CZ3 . TRP B 2 242 ? -7.729 -39.260 89.615 1.00 175.60 ? 1889 TRP B CZ3 1 ATOM 6430 C CH2 . TRP B 2 242 ? -8.267 -40.535 89.705 1.00 173.55 ? 1889 TRP B CH2 1 ATOM 6431 N N . TYR B 2 243 ? -12.324 -32.823 88.763 1.00 189.81 ? 1890 TYR B N 1 ATOM 6432 C CA . TYR B 2 243 ? -12.003 -31.402 88.606 1.00 181.78 ? 1890 TYR B CA 1 ATOM 6433 C C . TYR B 2 243 ? -12.857 -30.455 89.441 1.00 178.69 ? 1890 TYR B C 1 ATOM 6434 O O . TYR B 2 243 ? -13.707 -29.722 88.932 1.00 173.47 ? 1890 TYR B O 1 ATOM 6435 C CB . TYR B 2 243 ? -11.978 -31.020 87.129 1.00 178.11 ? 1890 TYR B CB 1 ATOM 6436 C CG . TYR B 2 243 ? -10.922 -31.797 86.366 1.00 183.88 ? 1890 TYR B CG 1 ATOM 6437 C CD1 . TYR B 2 243 ? -9.575 -31.793 86.777 1.00 195.54 ? 1890 TYR B CD1 1 ATOM 6438 C CD2 . TYR B 2 243 ? -11.257 -32.548 85.245 1.00 183.29 ? 1890 TYR B CD2 1 ATOM 6439 C CE1 . TYR B 2 243 ? -8.595 -32.510 86.083 1.00 193.27 ? 1890 TYR B CE1 1 ATOM 6440 C CE2 . TYR B 2 243 ? -10.285 -33.263 84.542 1.00 187.02 ? 1890 TYR B CE2 1 ATOM 6441 C CZ . TYR B 2 243 ? -8.958 -33.249 84.957 1.00 188.93 ? 1890 TYR B CZ 1 ATOM 6442 O OH . TYR B 2 243 ? -8.012 -33.976 84.249 1.00 179.22 ? 1890 TYR B OH 1 ATOM 6443 N N . PHE B 2 244 ? -12.610 -30.505 90.746 1.00 187.19 ? 1891 PHE B N 1 ATOM 6444 C CA . PHE B 2 244 ? -13.137 -29.514 91.667 1.00 192.83 ? 1891 PHE B CA 1 ATOM 6445 C C . PHE B 2 244 ? -12.067 -28.556 92.164 1.00 192.66 ? 1891 PHE B C 1 ATOM 6446 O O . PHE B 2 244 ? -11.624 -28.543 93.343 1.00 176.61 ? 1891 PHE B O 1 ATOM 6447 C CB . PHE B 2 244 ? -14.001 -30.103 92.777 1.00 203.28 ? 1891 PHE B CB 1 ATOM 6448 C CG . PHE B 2 244 ? -15.435 -29.640 92.725 1.00 194.97 ? 1891 PHE B CG 1 ATOM 6449 C CD1 . PHE B 2 244 ? -15.765 -28.435 92.103 1.00 190.57 ? 1891 PHE B CD1 1 ATOM 6450 C CD2 . PHE B 2 244 ? -16.451 -30.401 93.303 1.00 188.76 ? 1891 PHE B CD2 1 ATOM 6451 C CE1 . PHE B 2 244 ? -17.074 -27.997 92.061 1.00 188.89 ? 1891 PHE B CE1 1 ATOM 6452 C CE2 . PHE B 2 244 ? -17.765 -29.962 93.268 1.00 186.26 ? 1891 PHE B CE2 1 ATOM 6453 C CZ . PHE B 2 244 ? -18.076 -28.761 92.642 1.00 187.73 ? 1891 PHE B CZ 1 ATOM 6454 N N . THR B 2 245 ? -11.640 -27.822 91.138 1.00 195.06 ? 1892 THR B N 1 ATOM 6455 C CA . THR B 2 245 ? -11.107 -26.471 91.175 1.00 197.13 ? 1892 THR B CA 1 ATOM 6456 C C . THR B 2 245 ? -12.274 -25.508 91.653 1.00 198.97 ? 1892 THR B C 1 ATOM 6457 O O . THR B 2 245 ? -13.050 -25.882 92.567 1.00 190.57 ? 1892 THR B O 1 ATOM 6458 C CB . THR B 2 245 ? -10.487 -26.153 89.765 1.00 182.92 ? 1892 THR B CB 1 ATOM 6459 O OG1 . THR B 2 245 ? -11.399 -26.554 88.738 1.00 168.02 ? 1892 THR B OG1 1 ATOM 6460 C CG2 . THR B 2 245 ? -9.177 -26.950 89.525 1.00 170.82 ? 1892 THR B CG2 1 ATOM 6461 N N . GLU B 2 246 ? -12.371 -24.287 91.095 1.00 195.83 ? 1893 GLU B N 1 ATOM 6462 C CA . GLU B 2 246 ? -13.628 -23.454 91.099 1.00 188.39 ? 1893 GLU B CA 1 ATOM 6463 C C . GLU B 2 246 ? -13.638 -21.948 91.473 1.00 191.44 ? 1893 GLU B C 1 ATOM 6464 O O . GLU B 2 246 ? -12.844 -21.474 92.290 1.00 193.28 ? 1893 GLU B O 1 ATOM 6465 C CB . GLU B 2 246 ? -14.848 -24.208 91.662 1.00 179.66 ? 1893 GLU B CB 1 ATOM 6466 C CG . GLU B 2 246 ? -15.251 -25.344 90.728 1.00 177.04 ? 1893 GLU B CG 1 ATOM 6467 C CD . GLU B 2 246 ? -14.596 -25.255 89.334 1.00 175.63 ? 1893 GLU B CD 1 ATOM 6468 O OE1 . GLU B 2 246 ? -14.409 -24.121 88.830 1.00 176.06 ? 1893 GLU B OE1 1 ATOM 6469 O OE2 . GLU B 2 246 ? -14.250 -26.311 88.737 1.00 170.57 ? 1893 GLU B OE2 1 ATOM 6470 N N . ASN B 2 247 ? -14.587 -21.232 90.860 1.00 185.22 ? 1894 ASN B N 1 ATOM 6471 C CA . ASN B 2 247 ? -14.633 -19.760 90.800 1.00 183.55 ? 1894 ASN B CA 1 ATOM 6472 C C . ASN B 2 247 ? -15.438 -19.093 91.927 1.00 189.41 ? 1894 ASN B C 1 ATOM 6473 O O . ASN B 2 247 ? -15.070 -18.029 92.452 1.00 193.56 ? 1894 ASN B O 1 ATOM 6474 C CB . ASN B 2 247 ? -15.195 -19.347 89.434 1.00 173.15 ? 1894 ASN B CB 1 ATOM 6475 C CG . ASN B 2 247 ? -14.755 -20.290 88.319 1.00 164.29 ? 1894 ASN B CG 1 ATOM 6476 O OD1 . ASN B 2 247 ? -13.555 -20.506 88.133 1.00 163.79 ? 1894 ASN B OD1 1 ATOM 6477 N ND2 . ASN B 2 247 ? -15.720 -20.867 87.582 1.00 150.62 ? 1894 ASN B ND2 1 ATOM 6478 N N . THR B 2 264 ? -19.565 -25.362 100.399 1.00 293.93 ? 1911 THR B N 1 ATOM 6479 C CA . THR B 2 264 ? -20.857 -25.762 99.851 1.00 288.78 ? 1911 THR B CA 1 ATOM 6480 C C . THR B 2 264 ? -21.981 -24.797 100.297 1.00 306.25 ? 1911 THR B C 1 ATOM 6481 O O . THR B 2 264 ? -22.109 -24.484 101.491 1.00 320.64 ? 1911 THR B O 1 ATOM 6482 C CB . THR B 2 264 ? -21.164 -27.266 100.152 1.00 277.19 ? 1911 THR B CB 1 ATOM 6483 O OG1 . THR B 2 264 ? -22.481 -27.614 99.695 1.00 271.49 ? 1911 THR B OG1 1 ATOM 6484 C CG2 . THR B 2 264 ? -21.008 -27.612 101.652 1.00 273.88 ? 1911 THR B CG2 1 ATOM 6485 N N . PHE B 2 265 ? -22.749 -24.295 99.322 1.00 296.76 ? 1912 PHE B N 1 ATOM 6486 C CA . PHE B 2 265 ? -23.955 -23.483 99.585 1.00 288.89 ? 1912 PHE B CA 1 ATOM 6487 C C . PHE B 2 265 ? -25.253 -24.361 99.444 1.00 289.38 ? 1912 PHE B C 1 ATOM 6488 O O . PHE B 2 265 ? -25.706 -24.923 100.451 1.00 304.05 ? 1912 PHE B O 1 ATOM 6489 C CB . PHE B 2 265 ? -23.953 -22.161 98.759 1.00 263.32 ? 1912 PHE B CB 1 ATOM 6490 C CG . PHE B 2 265 ? -22.862 -21.155 99.155 1.00 248.58 ? 1912 PHE B CG 1 ATOM 6491 C CD1 . PHE B 2 265 ? -22.842 -20.563 100.433 1.00 245.95 ? 1912 PHE B CD1 1 ATOM 6492 C CD2 . PHE B 2 265 ? -21.880 -20.761 98.229 1.00 229.15 ? 1912 PHE B CD2 1 ATOM 6493 C CE1 . PHE B 2 265 ? -21.859 -19.636 100.779 1.00 238.42 ? 1912 PHE B CE1 1 ATOM 6494 C CE2 . PHE B 2 265 ? -20.899 -19.834 98.576 1.00 228.71 ? 1912 PHE B CE2 1 ATOM 6495 C CZ . PHE B 2 265 ? -20.889 -19.271 99.850 1.00 234.58 ? 1912 PHE B CZ 1 ATOM 6496 N N . LYS B 2 266 ? -25.844 -24.481 98.241 1.00 274.60 ? 1913 LYS B N 1 ATOM 6497 C CA . LYS B 2 266 ? -26.810 -25.585 97.897 1.00 253.97 ? 1913 LYS B CA 1 ATOM 6498 C C . LYS B 2 266 ? -27.352 -25.640 96.440 1.00 239.17 ? 1913 LYS B C 1 ATOM 6499 O O . LYS B 2 266 ? -28.443 -25.137 96.117 1.00 236.73 ? 1913 LYS B O 1 ATOM 6500 C CB . LYS B 2 266 ? -27.966 -25.767 98.910 1.00 248.29 ? 1913 LYS B CB 1 ATOM 6501 C CG . LYS B 2 266 ? -28.561 -27.179 98.877 1.00 233.06 ? 1913 LYS B CG 1 ATOM 6502 C CD . LYS B 2 266 ? -30.044 -27.230 99.241 1.00 225.47 ? 1913 LYS B CD 1 ATOM 6503 C CE . LYS B 2 266 ? -30.969 -26.889 98.073 1.00 209.24 ? 1913 LYS B CE 1 ATOM 6504 N NZ . LYS B 2 266 ? -30.772 -27.777 96.899 1.00 190.24 ? 1913 LYS B NZ 1 ATOM 6505 N N . GLU B 2 267 ? -26.555 -26.267 95.581 1.00 217.45 ? 1914 GLU B N 1 ATOM 6506 C CA . GLU B 2 267 ? -26.983 -26.758 94.275 1.00 196.99 ? 1914 GLU B CA 1 ATOM 6507 C C . GLU B 2 267 ? -27.100 -25.722 93.145 1.00 192.59 ? 1914 GLU B C 1 ATOM 6508 O O . GLU B 2 267 ? -27.480 -24.551 93.371 1.00 179.41 ? 1914 GLU B O 1 ATOM 6509 C CB . GLU B 2 267 ? -28.261 -27.614 94.393 1.00 195.63 ? 1914 GLU B CB 1 ATOM 6510 C CG . GLU B 2 267 ? -28.350 -28.817 93.445 1.00 190.12 ? 1914 GLU B CG 1 ATOM 6511 C CD . GLU B 2 267 ? -27.892 -28.517 92.013 1.00 184.55 ? 1914 GLU B CD 1 ATOM 6512 O OE1 . GLU B 2 267 ? -26.681 -28.642 91.766 1.00 182.41 ? 1914 GLU B OE1 1 ATOM 6513 O OE2 . GLU B 2 267 ? -28.703 -28.125 91.130 1.00 177.51 ? 1914 GLU B OE2 1 ATOM 6514 N N . ASN B 2 268 ? -26.728 -26.220 91.945 1.00 192.35 ? 1915 ASN B N 1 ATOM 6515 C CA . ASN B 2 268 ? -26.835 -25.585 90.601 1.00 185.97 ? 1915 ASN B CA 1 ATOM 6516 C C . ASN B 2 268 ? -26.432 -26.458 89.353 1.00 160.48 ? 1915 ASN B C 1 ATOM 6517 O O . ASN B 2 268 ? -27.270 -26.644 88.478 1.00 147.10 ? 1915 ASN B O 1 ATOM 6518 C CB . ASN B 2 268 ? -26.127 -24.221 90.576 1.00 208.57 ? 1915 ASN B CB 1 ATOM 6519 C CG . ASN B 2 268 ? -26.413 -23.433 89.314 1.00 212.70 ? 1915 ASN B CG 1 ATOM 6520 O OD1 . ASN B 2 268 ? -26.234 -23.933 88.194 1.00 211.43 ? 1915 ASN B OD1 1 ATOM 6521 N ND2 . ASN B 2 268 ? -26.845 -22.184 89.488 1.00 214.04 ? 1915 ASN B ND2 1 ATOM 6522 N N . TYR B 2 269 ? -25.186 -26.975 89.292 1.00 156.62 ? 1916 TYR B N 1 ATOM 6523 C CA . TYR B 2 269 ? -24.545 -27.576 88.047 1.00 161.54 ? 1916 TYR B CA 1 ATOM 6524 C C . TYR B 2 269 ? -24.984 -28.959 87.489 1.00 153.41 ? 1916 TYR B C 1 ATOM 6525 O O . TYR B 2 269 ? -24.192 -29.930 87.391 1.00 128.76 ? 1916 TYR B O 1 ATOM 6526 C CB . TYR B 2 269 ? -23.004 -27.644 88.124 1.00 169.10 ? 1916 TYR B CB 1 ATOM 6527 C CG . TYR B 2 269 ? -22.288 -26.758 89.102 1.00 171.26 ? 1916 TYR B CG 1 ATOM 6528 C CD1 . TYR B 2 269 ? -22.343 -25.369 88.990 1.00 179.23 ? 1916 TYR B CD1 1 ATOM 6529 C CD2 . TYR B 2 269 ? -21.491 -27.317 90.098 1.00 170.66 ? 1916 TYR B CD2 1 ATOM 6530 C CE1 . TYR B 2 269 ? -21.665 -24.552 89.882 1.00 196.10 ? 1916 TYR B CE1 1 ATOM 6531 C CE2 . TYR B 2 269 ? -20.807 -26.517 90.993 1.00 192.64 ? 1916 TYR B CE2 1 ATOM 6532 C CZ . TYR B 2 269 ? -20.898 -25.132 90.888 1.00 208.06 ? 1916 TYR B CZ 1 ATOM 6533 O OH . TYR B 2 269 ? -20.221 -24.325 91.787 1.00 228.38 ? 1916 TYR B OH 1 ATOM 6534 N N . ARG B 2 270 ? -26.231 -29.024 87.067 1.00 163.66 ? 1917 ARG B N 1 ATOM 6535 C CA . ARG B 2 270 ? -26.767 -30.232 86.491 1.00 160.81 ? 1917 ARG B CA 1 ATOM 6536 C C . ARG B 2 270 ? -27.027 -29.914 85.015 1.00 157.17 ? 1917 ARG B C 1 ATOM 6537 O O . ARG B 2 270 ? -27.760 -28.967 84.665 1.00 163.21 ? 1917 ARG B O 1 ATOM 6538 C CB . ARG B 2 270 ? -28.040 -30.679 87.248 1.00 174.04 ? 1917 ARG B CB 1 ATOM 6539 C CG . ARG B 2 270 ? -28.132 -30.254 88.729 1.00 172.84 ? 1917 ARG B CG 1 ATOM 6540 C CD . ARG B 2 270 ? -29.254 -30.929 89.526 1.00 164.28 ? 1917 ARG B CD 1 ATOM 6541 N NE . ARG B 2 270 ? -28.976 -32.347 89.706 1.00 158.40 ? 1917 ARG B NE 1 ATOM 6542 C CZ . ARG B 2 270 ? -29.590 -33.320 89.040 1.00 161.52 ? 1917 ARG B CZ 1 ATOM 6543 N NH1 . ARG B 2 270 ? -30.559 -33.040 88.176 1.00 163.46 ? 1917 ARG B NH1 1 ATOM 6544 N NH2 . ARG B 2 270 ? -29.244 -34.583 89.248 1.00 165.43 ? 1917 ARG B NH2 1 ATOM 6545 N N . PHE B 2 271 ? -26.371 -30.669 84.148 1.00 151.59 ? 1918 PHE B N 1 ATOM 6546 C CA . PHE B 2 271 ? -26.459 -30.404 82.718 1.00 153.09 ? 1918 PHE B CA 1 ATOM 6547 C C . PHE B 2 271 ? -27.235 -31.530 82.079 1.00 138.23 ? 1918 PHE B C 1 ATOM 6548 O O . PHE B 2 271 ? -26.894 -32.685 82.259 1.00 138.05 ? 1918 PHE B O 1 ATOM 6549 C CB . PHE B 2 271 ? -25.062 -30.203 82.065 1.00 158.95 ? 1918 PHE B CB 1 ATOM 6550 C CG . PHE B 2 271 ? -24.244 -29.064 82.669 1.00 162.32 ? 1918 PHE B CG 1 ATOM 6551 C CD1 . PHE B 2 271 ? -24.873 -27.918 83.207 1.00 159.34 ? 1918 PHE B CD1 1 ATOM 6552 C CD2 . PHE B 2 271 ? -22.843 -29.134 82.693 1.00 153.21 ? 1918 PHE B CD2 1 ATOM 6553 C CE1 . PHE B 2 271 ? -24.130 -26.895 83.765 1.00 153.32 ? 1918 PHE B CE1 1 ATOM 6554 C CE2 . PHE B 2 271 ? -22.095 -28.103 83.241 1.00 150.10 ? 1918 PHE B CE2 1 ATOM 6555 C CZ . PHE B 2 271 ? -22.740 -26.990 83.777 1.00 153.38 ? 1918 PHE B CZ 1 ATOM 6556 N N . HIS B 2 272 ? -28.293 -31.191 81.358 1.00 134.68 ? 1919 HIS B N 1 ATOM 6557 C CA . HIS B 2 272 ? -29.160 -32.202 80.766 1.00 136.96 ? 1919 HIS B CA 1 ATOM 6558 C C . HIS B 2 272 ? -28.779 -32.464 79.335 1.00 131.64 ? 1919 HIS B C 1 ATOM 6559 O O . HIS B 2 272 ? -29.537 -32.266 78.389 1.00 131.31 ? 1919 HIS B O 1 ATOM 6560 C CB . HIS B 2 272 ? -30.619 -31.834 80.965 1.00 140.38 ? 1919 HIS B CB 1 ATOM 6561 C CG . HIS B 2 272 ? -31.040 -31.950 82.388 1.00 144.81 ? 1919 HIS B CG 1 ATOM 6562 N ND1 . HIS B 2 272 ? -30.415 -31.251 83.399 1.00 141.51 ? 1919 HIS B ND1 1 ATOM 6563 C CD2 . HIS B 2 272 ? -31.975 -32.729 82.984 1.00 148.88 ? 1919 HIS B CD2 1 ATOM 6564 C CE1 . HIS B 2 272 ? -30.965 -31.582 84.554 1.00 154.35 ? 1919 HIS B CE1 1 ATOM 6565 N NE2 . HIS B 2 272 ? -31.915 -32.474 84.331 1.00 151.80 ? 1919 HIS B NE2 1 ATOM 6566 N N . ALA B 2 273 ? -27.574 -32.973 79.214 1.00 132.90 ? 1920 ALA B N 1 ATOM 6567 C CA . ALA B 2 273 ? -26.856 -32.890 77.987 1.00 130.92 ? 1920 ALA B CA 1 ATOM 6568 C C . ALA B 2 273 ? -26.930 -34.128 77.130 1.00 120.87 ? 1920 ALA B C 1 ATOM 6569 O O . ALA B 2 273 ? -26.929 -35.275 77.610 1.00 111.11 ? 1920 ALA B O 1 ATOM 6570 C CB . ALA B 2 273 ? -25.421 -32.528 78.280 1.00 150.04 ? 1920 ALA B CB 1 ATOM 6571 N N . ILE B 2 274 ? -26.990 -33.829 75.842 1.00 113.71 ? 1921 ILE B N 1 ATOM 6572 C CA . ILE B 2 274 ? -26.968 -34.778 74.758 1.00 112.64 ? 1921 ILE B CA 1 ATOM 6573 C C . ILE B 2 274 ? -25.608 -34.614 74.074 1.00 118.43 ? 1921 ILE B C 1 ATOM 6574 O O . ILE B 2 274 ? -25.263 -33.537 73.572 1.00 113.11 ? 1921 ILE B O 1 ATOM 6575 C CB . ILE B 2 274 ? -28.135 -34.482 73.790 1.00 108.82 ? 1921 ILE B CB 1 ATOM 6576 C CG1 . ILE B 2 274 ? -29.436 -34.269 74.604 1.00 106.21 ? 1921 ILE B CG1 1 ATOM 6577 C CG2 . ILE B 2 274 ? -28.205 -35.518 72.660 1.00 97.97 ? 1921 ILE B CG2 1 ATOM 6578 C CD1 . ILE B 2 274 ? -30.654 -33.877 73.801 1.00 105.96 ? 1921 ILE B CD1 1 ATOM 6579 N N . ASN B 2 275 ? -24.825 -35.691 74.079 1.00 131.18 ? 1922 ASN B N 1 ATOM 6580 C CA . ASN B 2 275 ? -23.405 -35.629 73.714 1.00 139.54 ? 1922 ASN B CA 1 ATOM 6581 C C . ASN B 2 275 ? -22.804 -34.357 74.300 1.00 140.02 ? 1922 ASN B C 1 ATOM 6582 O O . ASN B 2 275 ? -22.049 -33.620 73.643 1.00 143.36 ? 1922 ASN B O 1 ATOM 6583 C CB . ASN B 2 275 ? -23.205 -35.747 72.198 1.00 139.95 ? 1922 ASN B CB 1 ATOM 6584 C CG . ASN B 2 275 ? -23.776 -37.041 71.637 1.00 133.55 ? 1922 ASN B CG 1 ATOM 6585 O OD1 . ASN B 2 275 ? -24.738 -37.021 70.868 1.00 136.01 ? 1922 ASN B OD1 1 ATOM 6586 N ND2 . ASN B 2 275 ? -23.203 -38.173 72.038 1.00 115.49 ? 1922 ASN B ND2 1 ATOM 6587 N N . GLY B 2 276 ? -23.199 -34.119 75.549 1.00 129.35 ? 1923 GLY B N 1 ATOM 6588 C CA . GLY B 2 276 ? -22.790 -32.967 76.309 1.00 130.82 ? 1923 GLY B CA 1 ATOM 6589 C C . GLY B 2 276 ? -23.282 -31.585 75.900 1.00 131.48 ? 1923 GLY B C 1 ATOM 6590 O O . GLY B 2 276 ? -22.540 -30.633 76.062 1.00 142.01 ? 1923 GLY B O 1 ATOM 6591 N N . TYR B 2 277 ? -24.512 -31.433 75.405 1.00 128.69 ? 1924 TYR B N 1 ATOM 6592 C CA . TYR B 2 277 ? -25.015 -30.079 75.069 1.00 132.66 ? 1924 TYR B CA 1 ATOM 6593 C C . TYR B 2 277 ? -26.391 -29.739 75.620 1.00 129.35 ? 1924 TYR B C 1 ATOM 6594 O O . TYR B 2 277 ? -27.415 -30.172 75.090 1.00 121.03 ? 1924 TYR B O 1 ATOM 6595 C CB . TYR B 2 277 ? -25.026 -29.839 73.561 1.00 142.35 ? 1924 TYR B CB 1 ATOM 6596 C CG . TYR B 2 277 ? -23.701 -29.450 72.938 1.00 153.33 ? 1924 TYR B CG 1 ATOM 6597 C CD1 . TYR B 2 277 ? -22.879 -28.481 73.515 1.00 169.13 ? 1924 TYR B CD1 1 ATOM 6598 C CD2 . TYR B 2 277 ? -23.280 -30.036 71.748 1.00 151.38 ? 1924 TYR B CD2 1 ATOM 6599 C CE1 . TYR B 2 277 ? -21.662 -28.132 72.924 1.00 176.44 ? 1924 TYR B CE1 1 ATOM 6600 C CE2 . TYR B 2 277 ? -22.077 -29.690 71.151 1.00 152.00 ? 1924 TYR B CE2 1 ATOM 6601 C CZ . TYR B 2 277 ? -21.268 -28.744 71.735 1.00 154.93 ? 1924 TYR B CZ 1 ATOM 6602 O OH . TYR B 2 277 ? -20.074 -28.418 71.133 1.00 142.97 ? 1924 TYR B OH 1 ATOM 6603 N N . ILE B 2 278 ? -26.408 -28.917 76.658 1.00 136.13 ? 1925 ILE B N 1 ATOM 6604 C CA . ILE B 2 278 ? -27.646 -28.624 77.388 1.00 145.00 ? 1925 ILE B CA 1 ATOM 6605 C C . ILE B 2 278 ? -28.440 -27.503 76.699 1.00 135.57 ? 1925 ILE B C 1 ATOM 6606 O O . ILE B 2 278 ? -27.866 -26.746 75.941 1.00 136.34 ? 1925 ILE B O 1 ATOM 6607 C CB . ILE B 2 278 ? -27.343 -28.359 78.883 1.00 159.54 ? 1925 ILE B CB 1 ATOM 6608 C CG1 . ILE B 2 278 ? -28.632 -28.181 79.715 1.00 182.54 ? 1925 ILE B CG1 1 ATOM 6609 C CG2 . ILE B 2 278 ? -26.348 -27.227 79.022 1.00 156.56 ? 1925 ILE B CG2 1 ATOM 6610 C CD1 . ILE B 2 278 ? -28.438 -27.973 81.216 1.00 205.62 ? 1925 ILE B CD1 1 ATOM 6611 N N . MET B 2 279 ? -29.748 -27.420 76.958 1.00 133.79 ? 1926 MET B N 1 ATOM 6612 C CA . MET B 2 279 ? -30.705 -26.714 76.090 1.00 140.29 ? 1926 MET B CA 1 ATOM 6613 C C . MET B 2 279 ? -30.433 -27.085 74.635 1.00 147.99 ? 1926 MET B C 1 ATOM 6614 O O . MET B 2 279 ? -30.182 -28.263 74.365 1.00 167.55 ? 1926 MET B O 1 ATOM 6615 C CB . MET B 2 279 ? -30.696 -25.218 76.327 1.00 146.93 ? 1926 MET B CB 1 ATOM 6616 C CG . MET B 2 279 ? -31.204 -24.813 77.707 1.00 165.63 ? 1926 MET B CG 1 ATOM 6617 S SD . MET B 2 279 ? -32.986 -25.014 77.985 1.00 193.33 ? 1926 MET B SD 1 ATOM 6618 C CE . MET B 2 279 ? -33.315 -23.880 79.356 1.00 185.15 ? 1926 MET B CE 1 ATOM 6619 N N . ASP B 2 280 ? -30.438 -26.138 73.697 1.00 141.54 ? 1927 ASP B N 1 ATOM 6620 C CA . ASP B 2 280 ? -30.353 -26.572 72.292 1.00 141.04 ? 1927 ASP B CA 1 ATOM 6621 C C . ASP B 2 280 ? -28.993 -26.747 71.609 1.00 139.99 ? 1927 ASP B C 1 ATOM 6622 O O . ASP B 2 280 ? -28.930 -27.134 70.445 1.00 132.50 ? 1927 ASP B O 1 ATOM 6623 C CB . ASP B 2 280 ? -31.361 -25.847 71.413 1.00 146.40 ? 1927 ASP B CB 1 ATOM 6624 C CG . ASP B 2 280 ? -32.761 -26.357 71.632 1.00 153.66 ? 1927 ASP B CG 1 ATOM 6625 O OD1 . ASP B 2 280 ? -33.134 -26.428 72.823 1.00 171.71 ? 1927 ASP B OD1 1 ATOM 6626 O OD2 . ASP B 2 280 ? -33.474 -26.698 70.653 1.00 143.12 ? 1927 ASP B OD2 1 ATOM 6627 N N . THR B 2 281 ? -27.923 -26.504 72.358 1.00 154.99 ? 1928 THR B N 1 ATOM 6628 C CA . THR B 2 281 ? -26.542 -26.439 71.822 1.00 171.96 ? 1928 THR B CA 1 ATOM 6629 C C . THR B 2 281 ? -26.048 -27.528 70.774 1.00 157.17 ? 1928 THR B C 1 ATOM 6630 O O . THR B 2 281 ? -25.362 -27.188 69.796 1.00 143.50 ? 1928 THR B O 1 ATOM 6631 C CB . THR B 2 281 ? -25.471 -26.128 72.957 1.00 186.32 ? 1928 THR B CB 1 ATOM 6632 O OG1 . THR B 2 281 ? -25.719 -26.894 74.153 1.00 185.38 ? 1928 THR B OG1 1 ATOM 6633 C CG2 . THR B 2 281 ? -25.412 -24.609 73.322 1.00 161.90 ? 1928 THR B CG2 1 ATOM 6634 N N . LEU B 2 282 ? -26.395 -28.804 70.944 1.00 142.81 ? 1929 LEU B N 1 ATOM 6635 C CA . LEU B 2 282 ? -25.797 -29.833 70.079 1.00 138.75 ? 1929 LEU B CA 1 ATOM 6636 C C . LEU B 2 282 ? -25.952 -29.499 68.619 1.00 129.45 ? 1929 LEU B C 1 ATOM 6637 O O . LEU B 2 282 ? -27.053 -29.543 68.101 1.00 124.12 ? 1929 LEU B O 1 ATOM 6638 C CB . LEU B 2 282 ? -26.329 -31.243 70.359 1.00 156.47 ? 1929 LEU B CB 1 ATOM 6639 C CG . LEU B 2 282 ? -25.569 -32.364 69.616 1.00 161.83 ? 1929 LEU B CG 1 ATOM 6640 C CD1 . LEU B 2 282 ? -25.383 -33.628 70.456 1.00 145.68 ? 1929 LEU B CD1 1 ATOM 6641 C CD2 . LEU B 2 282 ? -26.201 -32.662 68.255 1.00 164.43 ? 1929 LEU B CD2 1 ATOM 6642 N N . PRO B 2 283 ? -24.827 -29.257 67.944 1.00 131.94 ? 1930 PRO B N 1 ATOM 6643 C CA . PRO B 2 283 ? -24.736 -28.471 66.748 1.00 143.46 ? 1930 PRO B CA 1 ATOM 6644 C C . PRO B 2 283 ? -24.878 -29.245 65.455 1.00 142.90 ? 1930 PRO B C 1 ATOM 6645 O O . PRO B 2 283 ? -25.245 -28.633 64.442 1.00 159.58 ? 1930 PRO B O 1 ATOM 6646 C CB . PRO B 2 283 ? -23.297 -28.002 66.810 1.00 157.37 ? 1930 PRO B CB 1 ATOM 6647 C CG . PRO B 2 283 ? -22.584 -29.237 67.257 1.00 147.63 ? 1930 PRO B CG 1 ATOM 6648 C CD . PRO B 2 283 ? -23.535 -29.904 68.223 1.00 139.70 ? 1930 PRO B CD 1 ATOM 6649 N N . GLY B 2 284 ? -24.575 -30.547 65.477 1.00 124.56 ? 1931 GLY B N 1 ATOM 6650 C CA . GLY B 2 284 ? -24.278 -31.265 64.241 1.00 123.53 ? 1931 GLY B CA 1 ATOM 6651 C C . GLY B 2 284 ? -25.203 -32.310 63.618 1.00 119.85 ? 1931 GLY B C 1 ATOM 6652 O O . GLY B 2 284 ? -24.751 -33.420 63.353 1.00 129.09 ? 1931 GLY B O 1 ATOM 6653 N N . LEU B 2 285 ? -26.458 -31.976 63.313 1.00 110.65 ? 1932 LEU B N 1 ATOM 6654 C CA . LEU B 2 285 ? -27.357 -32.985 62.738 1.00 109.12 ? 1932 LEU B CA 1 ATOM 6655 C C . LEU B 2 285 ? -27.853 -32.693 61.313 1.00 113.76 ? 1932 LEU B C 1 ATOM 6656 O O . LEU B 2 285 ? -29.042 -32.462 61.080 1.00 117.71 ? 1932 LEU B O 1 ATOM 6657 C CB . LEU B 2 285 ? -28.489 -33.326 63.717 1.00 107.91 ? 1932 LEU B CB 1 ATOM 6658 C CG . LEU B 2 285 ? -28.023 -33.771 65.121 1.00 109.06 ? 1932 LEU B CG 1 ATOM 6659 C CD1 . LEU B 2 285 ? -29.150 -33.946 66.138 1.00 119.72 ? 1932 LEU B CD1 1 ATOM 6660 C CD2 . LEU B 2 285 ? -27.213 -35.053 65.051 1.00 101.31 ? 1932 LEU B CD2 1 ATOM 6661 N N . VAL B 2 286 ? -26.910 -32.723 60.370 1.00 117.26 ? 1933 VAL B N 1 ATOM 6662 C CA . VAL B 2 286 ? -27.175 -32.497 58.946 1.00 130.49 ? 1933 VAL B CA 1 ATOM 6663 C C . VAL B 2 286 ? -27.381 -33.847 58.269 1.00 135.09 ? 1933 VAL B C 1 ATOM 6664 O O . VAL B 2 286 ? -26.471 -34.701 58.271 1.00 142.28 ? 1933 VAL B O 1 ATOM 6665 C CB . VAL B 2 286 ? -26.017 -31.700 58.251 1.00 146.39 ? 1933 VAL B CB 1 ATOM 6666 C CG1 . VAL B 2 286 ? -25.108 -32.584 57.349 1.00 144.06 ? 1933 VAL B CG1 1 ATOM 6667 C CG2 . VAL B 2 286 ? -26.560 -30.454 57.529 1.00 138.53 ? 1933 VAL B CG2 1 ATOM 6668 N N . MET B 2 287 ? -28.572 -34.021 57.683 1.00 128.91 ? 1934 MET B N 1 ATOM 6669 C CA . MET B 2 287 ? -28.985 -35.299 57.076 1.00 122.93 ? 1934 MET B CA 1 ATOM 6670 C C . MET B 2 287 ? -30.078 -35.181 56.005 1.00 125.50 ? 1934 MET B C 1 ATOM 6671 O O . MET B 2 287 ? -30.968 -34.319 56.095 1.00 121.84 ? 1934 MET B O 1 ATOM 6672 C CB . MET B 2 287 ? -29.463 -36.223 58.171 1.00 122.17 ? 1934 MET B CB 1 ATOM 6673 C CG . MET B 2 287 ? -30.131 -35.445 59.285 1.00 130.78 ? 1934 MET B CG 1 ATOM 6674 S SD . MET B 2 287 ? -30.886 -36.534 60.478 1.00 134.77 ? 1934 MET B SD 1 ATOM 6675 C CE . MET B 2 287 ? -32.067 -37.387 59.437 1.00 118.77 ? 1934 MET B CE 1 ATOM 6676 N N . ALA B 2 288 ? -30.011 -36.069 55.008 1.00 125.08 ? 1935 ALA B N 1 ATOM 6677 C CA . ALA B 2 288 ? -30.862 -35.996 53.800 1.00 130.57 ? 1935 ALA B CA 1 ATOM 6678 C C . ALA B 2 288 ? -32.257 -36.589 53.969 1.00 127.13 ? 1935 ALA B C 1 ATOM 6679 O O . ALA B 2 288 ? -32.453 -37.454 54.810 1.00 141.50 ? 1935 ALA B O 1 ATOM 6680 C CB . ALA B 2 288 ? -30.159 -36.677 52.641 1.00 130.70 ? 1935 ALA B CB 1 ATOM 6681 N N . GLN B 2 289 ? -33.218 -36.168 53.156 1.00 117.91 ? 1936 GLN B N 1 ATOM 6682 C CA . GLN B 2 289 ? -34.546 -36.755 53.273 1.00 124.59 ? 1936 GLN B CA 1 ATOM 6683 C C . GLN B 2 289 ? -34.744 -38.085 52.487 1.00 138.35 ? 1936 GLN B C 1 ATOM 6684 O O . GLN B 2 289 ? -35.860 -38.601 52.317 1.00 137.23 ? 1936 GLN B O 1 ATOM 6685 C CB . GLN B 2 289 ? -35.623 -35.712 52.995 1.00 128.61 ? 1936 GLN B CB 1 ATOM 6686 C CG . GLN B 2 289 ? -36.136 -35.640 51.564 1.00 144.95 ? 1936 GLN B CG 1 ATOM 6687 C CD . GLN B 2 289 ? -37.521 -35.018 51.501 1.00 152.03 ? 1936 GLN B CD 1 ATOM 6688 O OE1 . GLN B 2 289 ? -38.427 -35.418 52.239 1.00 157.09 ? 1936 GLN B OE1 1 ATOM 6689 N NE2 . GLN B 2 289 ? -37.689 -34.021 50.635 1.00 158.78 ? 1936 GLN B NE2 1 ATOM 6690 N N . ASP B 2 290 ? -33.646 -38.653 52.019 1.00 159.96 ? 1937 ASP B N 1 ATOM 6691 C CA . ASP B 2 290 ? -33.693 -40.010 51.508 1.00 172.72 ? 1937 ASP B CA 1 ATOM 6692 C C . ASP B 2 290 ? -33.004 -40.850 52.566 1.00 162.52 ? 1937 ASP B C 1 ATOM 6693 O O . ASP B 2 290 ? -33.670 -41.417 53.434 1.00 145.74 ? 1937 ASP B O 1 ATOM 6694 C CB . ASP B 2 290 ? -32.972 -40.156 50.157 1.00 210.73 ? 1937 ASP B CB 1 ATOM 6695 C CG . ASP B 2 290 ? -32.671 -38.816 49.487 1.00 248.86 ? 1937 ASP B CG 1 ATOM 6696 O OD1 . ASP B 2 290 ? -33.488 -37.867 49.584 1.00 270.70 ? 1937 ASP B OD1 1 ATOM 6697 O OD2 . ASP B 2 290 ? -31.600 -38.721 48.848 1.00 265.96 ? 1937 ASP B OD2 1 ATOM 6698 N N . GLN B 2 291 ? -31.666 -40.851 52.521 1.00 153.05 ? 1938 GLN B N 1 ATOM 6699 C CA . GLN B 2 291 ? -30.813 -41.751 53.303 1.00 133.45 ? 1938 GLN B CA 1 ATOM 6700 C C . GLN B 2 291 ? -31.424 -42.077 54.659 1.00 122.74 ? 1938 GLN B C 1 ATOM 6701 O O . GLN B 2 291 ? -31.798 -41.192 55.422 1.00 112.22 ? 1938 GLN B O 1 ATOM 6702 C CB . GLN B 2 291 ? -29.387 -41.205 53.424 1.00 127.01 ? 1938 GLN B CB 1 ATOM 6703 C CG . GLN B 2 291 ? -28.931 -40.476 52.163 1.00 156.53 ? 1938 GLN B CG 1 ATOM 6704 C CD . GLN B 2 291 ? -27.445 -40.630 51.848 1.00 178.11 ? 1938 GLN B CD 1 ATOM 6705 O OE1 . GLN B 2 291 ? -26.792 -41.533 52.364 1.00 199.77 ? 1938 GLN B OE1 1 ATOM 6706 N NE2 . GLN B 2 291 ? -26.908 -39.753 50.980 1.00 167.45 ? 1938 GLN B NE2 1 ATOM 6707 N N . ARG B 2 292 ? -31.594 -43.368 54.910 1.00 122.00 ? 1939 ARG B N 1 ATOM 6708 C CA . ARG B 2 292 ? -32.020 -43.817 56.213 1.00 116.96 ? 1939 ARG B CA 1 ATOM 6709 C C . ARG B 2 292 ? -30.906 -43.517 57.174 1.00 109.75 ? 1939 ARG B C 1 ATOM 6710 O O . ARG B 2 292 ? -29.730 -43.459 56.805 1.00 107.00 ? 1939 ARG B O 1 ATOM 6711 C CB . ARG B 2 292 ? -32.434 -45.309 56.247 1.00 133.36 ? 1939 ARG B CB 1 ATOM 6712 C CG . ARG B 2 292 ? -31.503 -46.373 55.641 1.00 149.51 ? 1939 ARG B CG 1 ATOM 6713 C CD . ARG B 2 292 ? -32.205 -47.731 55.465 1.00 161.56 ? 1939 ARG B CD 1 ATOM 6714 N NE . ARG B 2 292 ? -33.319 -47.908 56.417 1.00 191.89 ? 1939 ARG B NE 1 ATOM 6715 C CZ . ARG B 2 292 ? -34.628 -47.892 56.114 1.00 203.33 ? 1939 ARG B CZ 1 ATOM 6716 N NH1 . ARG B 2 292 ? -35.047 -47.736 54.857 1.00 209.02 ? 1939 ARG B NH1 1 ATOM 6717 N NH2 . ARG B 2 292 ? -35.536 -48.045 57.080 1.00 193.40 ? 1939 ARG B NH2 1 ATOM 6718 N N . ILE B 2 293 ? -31.292 -43.263 58.406 1.00 107.33 ? 1940 ILE B N 1 ATOM 6719 C CA . ILE B 2 293 ? -30.331 -42.966 59.427 1.00 106.86 ? 1940 ILE B CA 1 ATOM 6720 C C . ILE B 2 293 ? -30.450 -44.042 60.469 1.00 112.89 ? 1940 ILE B C 1 ATOM 6721 O O . ILE B 2 293 ? -31.562 -44.444 60.813 1.00 115.59 ? 1940 ILE B O 1 ATOM 6722 C CB . ILE B 2 293 ? -30.630 -41.614 60.076 1.00 101.97 ? 1940 ILE B CB 1 ATOM 6723 C CG1 . ILE B 2 293 ? -30.399 -40.491 59.064 1.00 103.48 ? 1940 ILE B CG1 1 ATOM 6724 C CG2 . ILE B 2 293 ? -29.778 -41.417 61.326 1.00 100.62 ? 1940 ILE B CG2 1 ATOM 6725 C CD1 . ILE B 2 293 ? -31.565 -40.221 58.141 1.00 99.63 ? 1940 ILE B CD1 1 ATOM 6726 N N . ARG B 2 294 ? -29.311 -44.529 60.947 1.00 115.99 ? 1941 ARG B N 1 ATOM 6727 C CA . ARG B 2 294 ? -29.306 -45.264 62.197 1.00 114.03 ? 1941 ARG B CA 1 ATOM 6728 C C . ARG B 2 294 ? -28.695 -44.365 63.281 1.00 116.69 ? 1941 ARG B C 1 ATOM 6729 O O . ARG B 2 294 ? -27.681 -43.678 63.061 1.00 114.01 ? 1941 ARG B O 1 ATOM 6730 C CB . ARG B 2 294 ? -28.616 -46.618 62.066 1.00 103.99 ? 1941 ARG B CB 1 ATOM 6731 C CG . ARG B 2 294 ? -27.116 -46.526 62.084 1.00 109.20 ? 1941 ARG B CG 1 ATOM 6732 C CD . ARG B 2 294 ? -26.517 -47.880 62.353 1.00 114.06 ? 1941 ARG B CD 1 ATOM 6733 N NE . ARG B 2 294 ? -25.726 -48.359 61.229 1.00 112.74 ? 1941 ARG B NE 1 ATOM 6734 C CZ . ARG B 2 294 ? -26.254 -48.933 60.155 1.00 122.78 ? 1941 ARG B CZ 1 ATOM 6735 N NH1 . ARG B 2 294 ? -27.577 -49.092 60.061 1.00 123.71 ? 1941 ARG B NH1 1 ATOM 6736 N NH2 . ARG B 2 294 ? -25.462 -49.348 59.176 1.00 126.26 ? 1941 ARG B NH2 1 ATOM 6737 N N . TRP B 2 295 ? -29.374 -44.316 64.423 1.00 115.28 ? 1942 TRP B N 1 ATOM 6738 C CA . TRP B 2 295 ? -28.936 -43.507 65.531 1.00 110.59 ? 1942 TRP B CA 1 ATOM 6739 C C . TRP B 2 295 ? -28.577 -44.444 66.629 1.00 120.69 ? 1942 TRP B C 1 ATOM 6740 O O . TRP B 2 295 ? -29.339 -45.370 66.957 1.00 128.37 ? 1942 TRP B O 1 ATOM 6741 C CB . TRP B 2 295 ? -30.040 -42.672 66.083 1.00 104.86 ? 1942 TRP B CB 1 ATOM 6742 C CG . TRP B 2 295 ? -30.731 -41.778 65.161 1.00 113.26 ? 1942 TRP B CG 1 ATOM 6743 C CD1 . TRP B 2 295 ? -31.729 -42.094 64.284 1.00 119.09 ? 1942 TRP B CD1 1 ATOM 6744 C CD2 . TRP B 2 295 ? -30.576 -40.379 65.098 1.00 111.80 ? 1942 TRP B CD2 1 ATOM 6745 N NE1 . TRP B 2 295 ? -32.189 -40.966 63.652 1.00 106.97 ? 1942 TRP B NE1 1 ATOM 6746 C CE2 . TRP B 2 295 ? -31.497 -39.897 64.138 1.00 106.57 ? 1942 TRP B CE2 1 ATOM 6747 C CE3 . TRP B 2 295 ? -29.753 -39.477 65.765 1.00 119.93 ? 1942 TRP B CE3 1 ATOM 6748 C CZ2 . TRP B 2 295 ? -31.601 -38.572 63.819 1.00 113.69 ? 1942 TRP B CZ2 1 ATOM 6749 C CZ3 . TRP B 2 295 ? -29.856 -38.155 65.454 1.00 135.22 ? 1942 TRP B CZ3 1 ATOM 6750 C CH2 . TRP B 2 295 ? -30.773 -37.707 64.480 1.00 138.25 ? 1942 TRP B CH2 1 ATOM 6751 N N . TYR B 2 296 ? -27.421 -44.161 67.210 1.00 121.50 ? 1943 TYR B N 1 ATOM 6752 C CA . TYR B 2 296 ? -26.841 -44.945 68.271 1.00 113.85 ? 1943 TYR B CA 1 ATOM 6753 C C . TYR B 2 296 ? -27.165 -44.228 69.571 1.00 110.79 ? 1943 TYR B C 1 ATOM 6754 O O . TYR B 2 296 ? -26.656 -43.147 69.817 1.00 117.59 ? 1943 TYR B O 1 ATOM 6755 C CB . TYR B 2 296 ? -25.331 -45.054 68.039 1.00 108.28 ? 1943 TYR B CB 1 ATOM 6756 C CG . TYR B 2 296 ? -24.951 -45.811 66.770 1.00 117.43 ? 1943 TYR B CG 1 ATOM 6757 C CD1 . TYR B 2 296 ? -25.471 -47.099 66.511 1.00 121.81 ? 1943 TYR B CD1 1 ATOM 6758 C CD2 . TYR B 2 296 ? -24.061 -45.259 65.834 1.00 117.99 ? 1943 TYR B CD2 1 ATOM 6759 C CE1 . TYR B 2 296 ? -25.114 -47.810 65.369 1.00 119.30 ? 1943 TYR B CE1 1 ATOM 6760 C CE2 . TYR B 2 296 ? -23.706 -45.959 64.679 1.00 120.14 ? 1943 TYR B CE2 1 ATOM 6761 C CZ . TYR B 2 296 ? -24.228 -47.238 64.454 1.00 121.69 ? 1943 TYR B CZ 1 ATOM 6762 O OH . TYR B 2 296 ? -23.890 -47.950 63.314 1.00 111.10 ? 1943 TYR B OH 1 ATOM 6763 N N . LEU B 2 297 ? -28.029 -44.819 70.391 1.00 108.01 ? 1944 LEU B N 1 ATOM 6764 C CA . LEU B 2 297 ? -28.526 -44.150 71.594 1.00 109.53 ? 1944 LEU B CA 1 ATOM 6765 C C . LEU B 2 297 ? -27.972 -44.710 72.895 1.00 118.05 ? 1944 LEU B C 1 ATOM 6766 O O . LEU B 2 297 ? -27.978 -45.926 73.101 1.00 134.37 ? 1944 LEU B O 1 ATOM 6767 C CB . LEU B 2 297 ? -30.044 -44.203 71.614 1.00 104.90 ? 1944 LEU B CB 1 ATOM 6768 C CG . LEU B 2 297 ? -30.627 -43.492 70.402 1.00 114.17 ? 1944 LEU B CG 1 ATOM 6769 C CD1 . LEU B 2 297 ? -32.059 -43.939 70.162 1.00 114.92 ? 1944 LEU B CD1 1 ATOM 6770 C CD2 . LEU B 2 297 ? -30.525 -41.976 70.572 1.00 123.91 ? 1944 LEU B CD2 1 ATOM 6771 N N . LEU B 2 298 ? -27.507 -43.829 73.781 1.00 116.95 ? 1945 LEU B N 1 ATOM 6772 C CA . LEU B 2 298 ? -26.949 -44.276 75.056 1.00 121.78 ? 1945 LEU B CA 1 ATOM 6773 C C . LEU B 2 298 ? -27.366 -43.433 76.258 1.00 130.64 ? 1945 LEU B C 1 ATOM 6774 O O . LEU B 2 298 ? -27.408 -42.203 76.158 1.00 143.01 ? 1945 LEU B O 1 ATOM 6775 C CB . LEU B 2 298 ? -25.420 -44.313 74.974 1.00 116.54 ? 1945 LEU B CB 1 ATOM 6776 C CG . LEU B 2 298 ? -24.727 -44.766 76.265 1.00 114.44 ? 1945 LEU B CG 1 ATOM 6777 C CD1 . LEU B 2 298 ? -25.152 -46.194 76.603 1.00 113.19 ? 1945 LEU B CD1 1 ATOM 6778 C CD2 . LEU B 2 298 ? -23.209 -44.607 76.201 1.00 110.68 ? 1945 LEU B CD2 1 ATOM 6779 N N . SER B 2 299 ? -27.659 -44.094 77.385 1.00 128.57 ? 1946 SER B N 1 ATOM 6780 C CA . SER B 2 299 ? -27.753 -43.410 78.690 1.00 135.87 ? 1946 SER B CA 1 ATOM 6781 C C . SER B 2 299 ? -26.592 -43.809 79.617 1.00 134.02 ? 1946 SER B C 1 ATOM 6782 O O . SER B 2 299 ? -25.824 -44.705 79.267 1.00 125.04 ? 1946 SER B O 1 ATOM 6783 C CB . SER B 2 299 ? -29.092 -43.682 79.359 1.00 144.80 ? 1946 SER B CB 1 ATOM 6784 O OG . SER B 2 299 ? -29.153 -43.016 80.607 1.00 166.39 ? 1946 SER B OG 1 ATOM 6785 N N . MET B 2 300 ? -26.451 -43.168 80.785 1.00 137.65 ? 1947 MET B N 1 ATOM 6786 C CA . MET B 2 300 ? -25.258 -43.429 81.606 1.00 153.51 ? 1947 MET B CA 1 ATOM 6787 C C . MET B 2 300 ? -25.221 -42.943 83.068 1.00 162.78 ? 1947 MET B C 1 ATOM 6788 O O . MET B 2 300 ? -25.051 -41.740 83.345 1.00 161.38 ? 1947 MET B O 1 ATOM 6789 C CB . MET B 2 300 ? -24.029 -42.899 80.862 1.00 161.16 ? 1947 MET B CB 1 ATOM 6790 C CG . MET B 2 300 ? -22.722 -43.623 81.138 1.00 168.87 ? 1947 MET B CG 1 ATOM 6791 S SD . MET B 2 300 ? -22.432 -45.082 80.128 1.00 155.72 ? 1947 MET B SD 1 ATOM 6792 C CE . MET B 2 300 ? -22.906 -46.354 81.306 1.00 171.50 ? 1947 MET B CE 1 ATOM 6793 N N . GLY B 2 301 ? -25.334 -43.902 83.990 1.00 167.53 ? 1948 GLY B N 1 ATOM 6794 C CA . GLY B 2 301 ? -25.043 -43.672 85.407 1.00 172.89 ? 1948 GLY B CA 1 ATOM 6795 C C . GLY B 2 301 ? -26.220 -43.593 86.363 1.00 175.11 ? 1948 GLY B C 1 ATOM 6796 O O . GLY B 2 301 ? -26.997 -44.542 86.484 1.00 176.06 ? 1948 GLY B O 1 ATOM 6797 N N . SER B 2 302 ? -26.329 -42.448 87.045 1.00 181.86 ? 1949 SER B N 1 ATOM 6798 C CA . SER B 2 302 ? -27.331 -42.182 88.095 1.00 175.81 ? 1949 SER B CA 1 ATOM 6799 C C . SER B 2 302 ? -28.679 -42.784 87.769 1.00 158.57 ? 1949 SER B C 1 ATOM 6800 O O . SER B 2 302 ? -29.187 -42.600 86.663 1.00 144.54 ? 1949 SER B O 1 ATOM 6801 C CB . SER B 2 302 ? -27.502 -40.670 88.322 1.00 191.96 ? 1949 SER B CB 1 ATOM 6802 O OG . SER B 2 302 ? -26.359 -40.068 88.916 1.00 202.48 ? 1949 SER B OG 1 ATOM 6803 N N . ASN B 2 303 ? -29.260 -43.479 88.741 1.00 153.19 ? 1950 ASN B N 1 ATOM 6804 C CA . ASN B 2 303 ? -30.485 -44.248 88.508 1.00 157.10 ? 1950 ASN B CA 1 ATOM 6805 C C . ASN B 2 303 ? -31.704 -43.400 88.128 1.00 154.54 ? 1950 ASN B C 1 ATOM 6806 O O . ASN B 2 303 ? -32.824 -43.912 87.973 1.00 140.07 ? 1950 ASN B O 1 ATOM 6807 C CB . ASN B 2 303 ? -30.757 -45.176 89.691 1.00 168.61 ? 1950 ASN B CB 1 ATOM 6808 C CG . ASN B 2 303 ? -29.711 -46.275 89.811 1.00 184.55 ? 1950 ASN B CG 1 ATOM 6809 O OD1 . ASN B 2 303 ? -29.048 -46.618 88.824 1.00 193.52 ? 1950 ASN B OD1 1 ATOM 6810 N ND2 . ASN B 2 303 ? -29.554 -46.836 91.018 1.00 185.17 ? 1950 ASN B ND2 1 ATOM 6811 N N . GLU B 2 304 ? -31.449 -42.102 87.959 1.00 160.42 ? 1951 GLU B N 1 ATOM 6812 C CA . GLU B 2 304 ? -32.434 -41.136 87.481 1.00 162.85 ? 1951 GLU B CA 1 ATOM 6813 C C . GLU B 2 304 ? -32.376 -41.076 85.985 1.00 157.68 ? 1951 GLU B C 1 ATOM 6814 O O . GLU B 2 304 ? -33.382 -40.817 85.336 1.00 162.12 ? 1951 GLU B O 1 ATOM 6815 C CB . GLU B 2 304 ? -32.157 -39.729 88.032 1.00 167.46 ? 1951 GLU B CB 1 ATOM 6816 C CG . GLU B 2 304 ? -30.798 -39.139 87.669 1.00 176.43 ? 1951 GLU B CG 1 ATOM 6817 C CD . GLU B 2 304 ? -30.665 -37.665 88.023 1.00 187.90 ? 1951 GLU B CD 1 ATOM 6818 O OE1 . GLU B 2 304 ? -31.675 -37.054 88.437 1.00 184.93 ? 1951 GLU B OE1 1 ATOM 6819 O OE2 . GLU B 2 304 ? -29.546 -37.114 87.877 1.00 192.83 ? 1951 GLU B OE2 1 ATOM 6820 N N . ASN B 2 305 ? -31.176 -41.304 85.458 1.00 155.25 ? 1952 ASN B N 1 ATOM 6821 C CA . ASN B 2 305 ? -30.874 -41.176 84.038 1.00 152.89 ? 1952 ASN B CA 1 ATOM 6822 C C . ASN B 2 305 ? -31.781 -41.988 83.112 1.00 143.81 ? 1952 ASN B C 1 ATOM 6823 O O . ASN B 2 305 ? -31.346 -42.444 82.060 1.00 152.45 ? 1952 ASN B O 1 ATOM 6824 C CB . ASN B 2 305 ? -29.405 -41.557 83.790 1.00 153.66 ? 1952 ASN B CB 1 ATOM 6825 C CG . ASN B 2 305 ? -28.486 -40.354 83.734 1.00 156.83 ? 1952 ASN B CG 1 ATOM 6826 O OD1 . ASN B 2 305 ? -28.860 -39.242 84.114 1.00 154.16 ? 1952 ASN B OD1 1 ATOM 6827 N ND2 . ASN B 2 305 ? -27.271 -40.572 83.245 1.00 158.97 ? 1952 ASN B ND2 1 ATOM 6828 N N . ILE B 2 306 ? -33.039 -42.161 83.486 1.00 132.24 ? 1953 ILE B N 1 ATOM 6829 C CA . ILE B 2 306 ? -33.919 -43.033 82.721 1.00 131.62 ? 1953 ILE B CA 1 ATOM 6830 C C . ILE B 2 306 ? -34.641 -42.267 81.589 1.00 130.39 ? 1953 ILE B C 1 ATOM 6831 O O . ILE B 2 306 ? -35.859 -42.336 81.426 1.00 131.07 ? 1953 ILE B O 1 ATOM 6832 C CB . ILE B 2 306 ? -34.789 -43.942 83.658 1.00 143.35 ? 1953 ILE B CB 1 ATOM 6833 C CG1 . ILE B 2 306 ? -35.843 -44.769 82.869 1.00 151.56 ? 1953 ILE B CG1 1 ATOM 6834 C CG2 . ILE B 2 306 ? -35.307 -43.172 84.878 1.00 135.64 ? 1953 ILE B CG2 1 ATOM 6835 C CD1 . ILE B 2 306 ? -36.456 -45.935 83.634 1.00 150.68 ? 1953 ILE B CD1 1 ATOM 6836 N N . HIS B 2 307 ? -33.830 -41.574 80.786 1.00 132.76 ? 1954 HIS B N 1 ATOM 6837 C CA . HIS B 2 307 ? -34.259 -40.697 79.670 1.00 128.52 ? 1954 HIS B CA 1 ATOM 6838 C C . HIS B 2 307 ? -35.141 -41.323 78.570 1.00 118.42 ? 1954 HIS B C 1 ATOM 6839 O O . HIS B 2 307 ? -34.665 -42.072 77.718 1.00 109.19 ? 1954 HIS B O 1 ATOM 6840 C CB . HIS B 2 307 ? -33.027 -40.001 79.057 1.00 125.11 ? 1954 HIS B CB 1 ATOM 6841 C CG . HIS B 2 307 ? -32.245 -39.206 80.054 1.00 131.51 ? 1954 HIS B CG 1 ATOM 6842 N ND1 . HIS B 2 307 ? -32.371 -37.841 80.179 1.00 142.40 ? 1954 HIS B ND1 1 ATOM 6843 C CD2 . HIS B 2 307 ? -31.371 -39.592 81.014 1.00 129.06 ? 1954 HIS B CD2 1 ATOM 6844 C CE1 . HIS B 2 307 ? -31.572 -37.417 81.144 1.00 135.95 ? 1954 HIS B CE1 1 ATOM 6845 N NE2 . HIS B 2 307 ? -30.967 -38.461 81.678 1.00 127.51 ? 1954 HIS B NE2 1 ATOM 6846 N N . SER B 2 308 ? -36.428 -40.986 78.607 1.00 119.35 ? 1955 SER B N 1 ATOM 6847 C CA . SER B 2 308 ? -37.406 -41.418 77.604 1.00 121.01 ? 1955 SER B CA 1 ATOM 6848 C C . SER B 2 308 ? -37.338 -40.548 76.321 1.00 116.82 ? 1955 SER B C 1 ATOM 6849 O O . SER B 2 308 ? -37.907 -39.451 76.252 1.00 118.25 ? 1955 SER B O 1 ATOM 6850 C CB . SER B 2 308 ? -38.830 -41.413 78.205 1.00 129.62 ? 1955 SER B CB 1 ATOM 6851 O OG . SER B 2 308 ? -39.032 -42.391 79.229 1.00 132.75 ? 1955 SER B OG 1 ATOM 6852 N N . ILE B 2 309 ? -36.660 -41.069 75.301 1.00 111.40 ? 1956 ILE B N 1 ATOM 6853 C CA . ILE B 2 309 ? -36.322 -40.311 74.096 1.00 108.97 ? 1956 ILE B CA 1 ATOM 6854 C C . ILE B 2 309 ? -37.359 -40.307 72.972 1.00 122.35 ? 1956 ILE B C 1 ATOM 6855 O O . ILE B 2 309 ? -37.837 -41.368 72.532 1.00 125.83 ? 1956 ILE B O 1 ATOM 6856 C CB . ILE B 2 309 ? -34.924 -40.707 73.580 1.00 103.88 ? 1956 ILE B CB 1 ATOM 6857 C CG1 . ILE B 2 309 ? -33.958 -39.579 73.863 1.00 105.98 ? 1956 ILE B CG1 1 ATOM 6858 C CG2 . ILE B 2 309 ? -34.908 -41.032 72.095 1.00 104.72 ? 1956 ILE B CG2 1 ATOM 6859 C CD1 . ILE B 2 309 ? -33.779 -39.331 75.345 1.00 123.61 ? 1956 ILE B CD1 1 ATOM 6860 N N . HIS B 2 310 ? -37.679 -39.099 72.508 1.00 129.56 ? 1957 HIS B N 1 ATOM 6861 C CA . HIS B 2 310 ? -38.630 -38.897 71.419 1.00 127.66 ? 1957 HIS B CA 1 ATOM 6862 C C . HIS B 2 310 ? -38.016 -38.188 70.206 1.00 131.35 ? 1957 HIS B C 1 ATOM 6863 O O . HIS B 2 310 ? -37.199 -37.259 70.328 1.00 125.55 ? 1957 HIS B O 1 ATOM 6864 C CB . HIS B 2 310 ? -39.859 -38.142 71.931 1.00 127.36 ? 1957 HIS B CB 1 ATOM 6865 C CG . HIS B 2 310 ? -40.860 -37.818 70.867 1.00 133.08 ? 1957 HIS B CG 1 ATOM 6866 N ND1 . HIS B 2 310 ? -41.453 -36.578 70.759 1.00 129.80 ? 1957 HIS B ND1 1 ATOM 6867 C CD2 . HIS B 2 310 ? -41.362 -38.568 69.855 1.00 141.76 ? 1957 HIS B CD2 1 ATOM 6868 C CE1 . HIS B 2 310 ? -42.282 -36.579 69.730 1.00 140.65 ? 1957 HIS B CE1 1 ATOM 6869 N NE2 . HIS B 2 310 ? -42.245 -37.774 69.163 1.00 151.83 ? 1957 HIS B NE2 1 ATOM 6870 N N . PHE B 2 311 ? -38.421 -38.649 69.030 1.00 132.59 ? 1958 PHE B N 1 ATOM 6871 C CA . PHE B 2 311 ? -38.058 -37.998 67.786 1.00 132.70 ? 1958 PHE B CA 1 ATOM 6872 C C . PHE B 2 311 ? -39.284 -37.393 67.124 1.00 134.81 ? 1958 PHE B C 1 ATOM 6873 O O . PHE B 2 311 ? -40.082 -38.115 66.501 1.00 143.28 ? 1958 PHE B O 1 ATOM 6874 C CB . PHE B 2 311 ? -37.467 -39.023 66.851 1.00 135.50 ? 1958 PHE B CB 1 ATOM 6875 C CG . PHE B 2 311 ? -36.009 -39.246 67.044 1.00 130.97 ? 1958 PHE B CG 1 ATOM 6876 C CD1 . PHE B 2 311 ? -35.095 -38.251 66.718 1.00 128.21 ? 1958 PHE B CD1 1 ATOM 6877 C CD2 . PHE B 2 311 ? -35.545 -40.462 67.513 1.00 125.90 ? 1958 PHE B CD2 1 ATOM 6878 C CE1 . PHE B 2 311 ? -33.743 -38.463 66.857 1.00 122.07 ? 1958 PHE B CE1 1 ATOM 6879 C CE2 . PHE B 2 311 ? -34.196 -40.677 67.666 1.00 123.06 ? 1958 PHE B CE2 1 ATOM 6880 C CZ . PHE B 2 311 ? -33.295 -39.674 67.337 1.00 123.88 ? 1958 PHE B CZ 1 ATOM 6881 N N . SER B 2 312 ? -39.420 -36.072 67.246 1.00 121.88 ? 1959 SER B N 1 ATOM 6882 C CA . SER B 2 312 ? -40.630 -35.369 66.821 1.00 113.90 ? 1959 SER B CA 1 ATOM 6883 C C . SER B 2 312 ? -41.016 -35.752 65.391 1.00 118.61 ? 1959 SER B C 1 ATOM 6884 O O . SER B 2 312 ? -40.159 -35.845 64.509 1.00 107.75 ? 1959 SER B O 1 ATOM 6885 C CB . SER B 2 312 ? -40.440 -33.860 66.970 1.00 109.32 ? 1959 SER B CB 1 ATOM 6886 O OG . SER B 2 312 ? -41.682 -33.199 67.082 1.00 107.29 ? 1959 SER B OG 1 ATOM 6887 N N . GLY B 2 313 ? -42.300 -36.038 65.184 1.00 134.08 ? 1960 GLY B N 1 ATOM 6888 C CA . GLY B 2 313 ? -42.839 -36.345 63.837 1.00 157.91 ? 1960 GLY B CA 1 ATOM 6889 C C . GLY B 2 313 ? -42.143 -37.395 62.978 1.00 149.72 ? 1960 GLY B C 1 ATOM 6890 O O . GLY B 2 313 ? -42.238 -37.385 61.738 1.00 147.25 ? 1960 GLY B O 1 ATOM 6891 N N . HIS B 2 314 ? -41.459 -38.302 63.658 1.00 138.68 ? 1961 HIS B N 1 ATOM 6892 C CA . HIS B 2 314 ? -40.635 -39.301 63.047 1.00 131.42 ? 1961 HIS B CA 1 ATOM 6893 C C . HIS B 2 314 ? -40.847 -40.527 63.938 1.00 133.12 ? 1961 HIS B C 1 ATOM 6894 O O . HIS B 2 314 ? -41.130 -40.365 65.135 1.00 139.06 ? 1961 HIS B O 1 ATOM 6895 C CB . HIS B 2 314 ? -39.173 -38.817 63.075 1.00 131.54 ? 1961 HIS B CB 1 ATOM 6896 C CG . HIS B 2 314 ? -38.852 -37.721 62.082 1.00 150.73 ? 1961 HIS B CG 1 ATOM 6897 N ND1 . HIS B 2 314 ? -37.640 -37.646 61.420 1.00 152.97 ? 1961 HIS B ND1 1 ATOM 6898 C CD2 . HIS B 2 314 ? -39.577 -36.661 61.639 1.00 155.30 ? 1961 HIS B CD2 1 ATOM 6899 C CE1 . HIS B 2 314 ? -37.635 -36.596 60.614 1.00 149.34 ? 1961 HIS B CE1 1 ATOM 6900 N NE2 . HIS B 2 314 ? -38.800 -35.984 60.724 1.00 156.08 ? 1961 HIS B NE2 1 ATOM 6901 N N . VAL B 2 315 ? -40.788 -41.732 63.352 1.00 130.34 ? 1962 VAL B N 1 ATOM 6902 C CA . VAL B 2 315 ? -40.734 -43.025 64.105 1.00 119.01 ? 1962 VAL B CA 1 ATOM 6903 C C . VAL B 2 315 ? -39.399 -43.686 63.823 1.00 118.70 ? 1962 VAL B C 1 ATOM 6904 O O . VAL B 2 315 ? -38.666 -43.192 62.960 1.00 136.87 ? 1962 VAL B O 1 ATOM 6905 C CB . VAL B 2 315 ? -41.783 -44.085 63.653 1.00 111.65 ? 1962 VAL B CB 1 ATOM 6906 C CG1 . VAL B 2 315 ? -43.141 -43.885 64.295 1.00 113.57 ? 1962 VAL B CG1 1 ATOM 6907 C CG2 . VAL B 2 315 ? -41.886 -44.172 62.137 1.00 117.37 ? 1962 VAL B CG2 1 ATOM 6908 N N . PHE B 2 316 ? -39.112 -44.813 64.498 1.00 112.23 ? 1963 PHE B N 1 ATOM 6909 C CA . PHE B 2 316 ? -38.011 -45.750 64.084 1.00 115.95 ? 1963 PHE B CA 1 ATOM 6910 C C . PHE B 2 316 ? -38.331 -47.267 64.051 1.00 112.46 ? 1963 PHE B C 1 ATOM 6911 O O . PHE B 2 316 ? -39.484 -47.705 64.168 1.00 117.80 ? 1963 PHE B O 1 ATOM 6912 C CB . PHE B 2 316 ? -36.754 -45.526 64.921 1.00 107.02 ? 1963 PHE B CB 1 ATOM 6913 C CG . PHE B 2 316 ? -37.054 -45.256 66.334 1.00 109.12 ? 1963 PHE B CG 1 ATOM 6914 C CD1 . PHE B 2 316 ? -37.425 -43.994 66.733 1.00 115.72 ? 1963 PHE B CD1 1 ATOM 6915 C CD2 . PHE B 2 316 ? -37.025 -46.275 67.253 1.00 121.02 ? 1963 PHE B CD2 1 ATOM 6916 C CE1 . PHE B 2 316 ? -37.730 -43.742 68.052 1.00 143.15 ? 1963 PHE B CE1 1 ATOM 6917 C CE2 . PHE B 2 316 ? -37.333 -46.046 68.578 1.00 136.39 ? 1963 PHE B CE2 1 ATOM 6918 C CZ . PHE B 2 316 ? -37.690 -44.773 68.979 1.00 151.21 ? 1963 PHE B CZ 1 ATOM 6919 N N . THR B 2 317 ? -37.294 -48.069 63.869 1.00 104.18 ? 1964 THR B N 1 ATOM 6920 C CA . THR B 2 317 ? -37.447 -49.507 63.951 1.00 104.62 ? 1964 THR B CA 1 ATOM 6921 C C . THR B 2 317 ? -36.415 -49.972 64.972 1.00 106.10 ? 1964 THR B C 1 ATOM 6922 O O . THR B 2 317 ? -35.375 -49.300 65.166 1.00 99.15 ? 1964 THR B O 1 ATOM 6923 C CB . THR B 2 317 ? -37.185 -50.187 62.590 1.00 111.18 ? 1964 THR B CB 1 ATOM 6924 O OG1 . THR B 2 317 ? -37.586 -49.319 61.520 1.00 128.43 ? 1964 THR B OG1 1 ATOM 6925 C CG2 . THR B 2 317 ? -37.927 -51.509 62.482 1.00 103.29 ? 1964 THR B CG2 1 ATOM 6926 N N . VAL B 2 318 ? -36.708 -51.094 65.642 1.00 102.72 ? 1965 VAL B N 1 ATOM 6927 C CA . VAL B 2 318 ? -35.712 -51.735 66.502 1.00 99.81 ? 1965 VAL B CA 1 ATOM 6928 C C . VAL B 2 318 ? -35.358 -53.176 66.119 1.00 111.42 ? 1965 VAL B C 1 ATOM 6929 O O . VAL B 2 318 ? -36.224 -53.995 65.768 1.00 103.63 ? 1965 VAL B O 1 ATOM 6930 C CB . VAL B 2 318 ? -36.067 -51.690 67.992 1.00 92.38 ? 1965 VAL B CB 1 ATOM 6931 C CG1 . VAL B 2 318 ? -34.789 -51.626 68.823 1.00 89.87 ? 1965 VAL B CG1 1 ATOM 6932 C CG2 . VAL B 2 318 ? -36.979 -50.519 68.311 1.00 90.02 ? 1965 VAL B CG2 1 ATOM 6933 N N . ARG B 2 319 ? -34.051 -53.429 66.196 1.00 131.56 ? 1966 ARG B N 1 ATOM 6934 C CA . ARG B 2 319 ? -33.402 -54.717 65.985 1.00 141.92 ? 1966 ARG B CA 1 ATOM 6935 C C . ARG B 2 319 ? -34.007 -55.821 66.870 1.00 136.54 ? 1966 ARG B C 1 ATOM 6936 O O . ARG B 2 319 ? -34.983 -56.435 66.463 1.00 138.86 ? 1966 ARG B O 1 ATOM 6937 C CB . ARG B 2 319 ? -31.886 -54.560 66.217 1.00 164.41 ? 1966 ARG B CB 1 ATOM 6938 C CG . ARG B 2 319 ? -31.535 -53.480 67.240 1.00 178.68 ? 1966 ARG B CG 1 ATOM 6939 C CD . ARG B 2 319 ? -30.077 -53.485 67.658 1.00 199.08 ? 1966 ARG B CD 1 ATOM 6940 N NE . ARG B 2 319 ? -29.967 -53.658 69.111 1.00 231.31 ? 1966 ARG B NE 1 ATOM 6941 C CZ . ARG B 2 319 ? -28.977 -53.188 69.872 1.00 253.75 ? 1966 ARG B CZ 1 ATOM 6942 N NH1 . ARG B 2 319 ? -27.987 -52.479 69.335 1.00 274.08 ? 1966 ARG B NH1 1 ATOM 6943 N NH2 . ARG B 2 319 ? -28.983 -53.418 71.183 1.00 231.67 ? 1966 ARG B NH2 1 ATOM 6944 N N . LYS B 2 320 ? -33.453 -56.041 68.069 1.00 126.00 ? 1967 LYS B N 1 ATOM 6945 C CA . LYS B 2 320 ? -33.779 -57.197 68.958 1.00 132.99 ? 1967 LYS B CA 1 ATOM 6946 C C . LYS B 2 320 ? -34.193 -58.511 68.252 1.00 134.53 ? 1967 LYS B C 1 ATOM 6947 O O . LYS B 2 320 ? -33.587 -58.902 67.260 1.00 125.67 ? 1967 LYS B O 1 ATOM 6948 C CB . LYS B 2 320 ? -34.755 -56.822 70.097 1.00 139.30 ? 1967 LYS B CB 1 ATOM 6949 C CG . LYS B 2 320 ? -34.534 -55.449 70.728 1.00 149.82 ? 1967 LYS B CG 1 ATOM 6950 C CD . LYS B 2 320 ? -33.070 -55.083 70.958 1.00 155.78 ? 1967 LYS B CD 1 ATOM 6951 C CE . LYS B 2 320 ? -32.579 -55.529 72.326 1.00 165.61 ? 1967 LYS B CE 1 ATOM 6952 N NZ . LYS B 2 320 ? -33.241 -54.771 73.423 1.00 172.48 ? 1967 LYS B NZ 1 ATOM 6953 N N . LYS B 2 321 ? -35.194 -59.216 68.767 1.00 145.81 ? 1968 LYS B N 1 ATOM 6954 C CA . LYS B 2 321 ? -35.621 -60.459 68.104 1.00 153.07 ? 1968 LYS B CA 1 ATOM 6955 C C . LYS B 2 321 ? -36.035 -60.288 66.601 1.00 134.76 ? 1968 LYS B C 1 ATOM 6956 O O . LYS B 2 321 ? -35.257 -60.646 65.736 1.00 122.41 ? 1968 LYS B O 1 ATOM 6957 C CB . LYS B 2 321 ? -36.648 -61.218 68.966 1.00 174.34 ? 1968 LYS B CB 1 ATOM 6958 C CG . LYS B 2 321 ? -36.049 -61.930 70.182 1.00 178.85 ? 1968 LYS B CG 1 ATOM 6959 C CD . LYS B 2 321 ? -35.434 -63.279 69.804 1.00 185.54 ? 1968 LYS B CD 1 ATOM 6960 C CE . LYS B 2 321 ? -35.427 -64.263 70.970 1.00 179.22 ? 1968 LYS B CE 1 ATOM 6961 N NZ . LYS B 2 321 ? -34.867 -65.598 70.611 1.00 162.21 ? 1968 LYS B NZ 1 ATOM 6962 N N . GLU B 2 322 ? -37.224 -59.743 66.309 1.00 130.78 ? 1969 GLU B N 1 ATOM 6963 C CA . GLU B 2 322 ? -37.637 -59.314 64.946 1.00 132.81 ? 1969 GLU B CA 1 ATOM 6964 C C . GLU B 2 322 ? -37.766 -57.786 64.921 1.00 140.66 ? 1969 GLU B C 1 ATOM 6965 O O . GLU B 2 322 ? -37.576 -57.136 65.946 1.00 143.47 ? 1969 GLU B O 1 ATOM 6966 C CB . GLU B 2 322 ? -38.986 -59.907 64.565 1.00 133.69 ? 1969 GLU B CB 1 ATOM 6967 C CG . GLU B 2 322 ? -39.297 -61.209 65.261 1.00 153.30 ? 1969 GLU B CG 1 ATOM 6968 C CD . GLU B 2 322 ? -39.445 -62.334 64.286 1.00 177.96 ? 1969 GLU B CD 1 ATOM 6969 O OE1 . GLU B 2 322 ? -40.580 -62.502 63.792 1.00 193.36 ? 1969 GLU B OE1 1 ATOM 6970 O OE2 . GLU B 2 322 ? -38.437 -63.035 64.020 1.00 197.61 ? 1969 GLU B OE2 1 ATOM 6971 N N . GLU B 2 323 ? -38.108 -57.193 63.777 1.00 148.29 ? 1970 GLU B N 1 ATOM 6972 C CA . GLU B 2 323 ? -38.152 -55.722 63.726 1.00 144.41 ? 1970 GLU B CA 1 ATOM 6973 C C . GLU B 2 323 ? -39.471 -55.158 64.243 1.00 132.86 ? 1970 GLU B C 1 ATOM 6974 O O . GLU B 2 323 ? -40.542 -55.568 63.793 1.00 126.10 ? 1970 GLU B O 1 ATOM 6975 C CB . GLU B 2 323 ? -37.743 -55.155 62.344 1.00 159.63 ? 1970 GLU B CB 1 ATOM 6976 C CG . GLU B 2 323 ? -36.233 -54.863 62.248 1.00 169.41 ? 1970 GLU B CG 1 ATOM 6977 C CD . GLU B 2 323 ? -35.742 -54.334 60.895 1.00 162.09 ? 1970 GLU B CD 1 ATOM 6978 O OE1 . GLU B 2 323 ? -36.576 -53.783 60.116 1.00 141.07 ? 1970 GLU B OE1 1 ATOM 6979 O OE2 . GLU B 2 323 ? -34.503 -54.471 60.634 1.00 141.42 ? 1970 GLU B OE2 1 ATOM 6980 N N . TYR B 2 324 ? -39.361 -54.244 65.210 1.00 124.84 ? 1971 TYR B N 1 ATOM 6981 C CA . TYR B 2 324 ? -40.500 -53.567 65.847 1.00 127.94 ? 1971 TYR B CA 1 ATOM 6982 C C . TYR B 2 324 ? -40.496 -52.069 65.541 1.00 131.54 ? 1971 TYR B C 1 ATOM 6983 O O . TYR B 2 324 ? -39.433 -51.436 65.593 1.00 130.08 ? 1971 TYR B O 1 ATOM 6984 C CB . TYR B 2 324 ? -40.402 -53.717 67.361 1.00 130.45 ? 1971 TYR B CB 1 ATOM 6985 C CG . TYR B 2 324 ? -40.468 -55.137 67.867 1.00 137.17 ? 1971 TYR B CG 1 ATOM 6986 C CD1 . TYR B 2 324 ? -39.327 -55.939 67.941 1.00 125.05 ? 1971 TYR B CD1 1 ATOM 6987 C CD2 . TYR B 2 324 ? -41.679 -55.677 68.290 1.00 157.37 ? 1971 TYR B CD2 1 ATOM 6988 C CE1 . TYR B 2 324 ? -39.396 -57.243 68.413 1.00 127.54 ? 1971 TYR B CE1 1 ATOM 6989 C CE2 . TYR B 2 324 ? -41.763 -56.981 68.757 1.00 160.21 ? 1971 TYR B CE2 1 ATOM 6990 C CZ . TYR B 2 324 ? -40.619 -57.765 68.816 1.00 145.68 ? 1971 TYR B CZ 1 ATOM 6991 O OH . TYR B 2 324 ? -40.738 -59.063 69.288 1.00 153.47 ? 1971 TYR B OH 1 ATOM 6992 N N . LYS B 2 325 ? -41.668 -51.494 65.254 1.00 124.52 ? 1972 LYS B N 1 ATOM 6993 C CA . LYS B 2 325 ? -41.753 -50.047 65.006 1.00 113.54 ? 1972 LYS B CA 1 ATOM 6994 C C . LYS B 2 325 ? -42.206 -49.259 66.233 1.00 108.99 ? 1972 LYS B C 1 ATOM 6995 O O . LYS B 2 325 ? -43.257 -49.539 66.785 1.00 109.39 ? 1972 LYS B O 1 ATOM 6996 C CB . LYS B 2 325 ? -42.664 -49.739 63.834 1.00 110.63 ? 1972 LYS B CB 1 ATOM 6997 C CG . LYS B 2 325 ? -42.817 -48.248 63.600 1.00 113.32 ? 1972 LYS B CG 1 ATOM 6998 C CD . LYS B 2 325 ? -43.138 -47.950 62.151 1.00 122.66 ? 1972 LYS B CD 1 ATOM 6999 C CE . LYS B 2 325 ? -41.942 -48.216 61.254 1.00 133.59 ? 1972 LYS B CE 1 ATOM 7000 N NZ . LYS B 2 325 ? -42.298 -48.811 59.930 1.00 147.91 ? 1972 LYS B NZ 1 ATOM 7001 N N . MET B 2 326 ? -41.409 -48.264 66.626 1.00 107.75 ? 1973 MET B N 1 ATOM 7002 C CA . MET B 2 326 ? -41.578 -47.510 67.880 1.00 114.51 ? 1973 MET B CA 1 ATOM 7003 C C . MET B 2 326 ? -41.416 -46.006 67.676 1.00 117.88 ? 1973 MET B C 1 ATOM 7004 O O . MET B 2 326 ? -40.733 -45.586 66.732 1.00 116.80 ? 1973 MET B O 1 ATOM 7005 C CB . MET B 2 326 ? -40.498 -47.900 68.881 1.00 120.49 ? 1973 MET B CB 1 ATOM 7006 C CG . MET B 2 326 ? -40.322 -49.376 69.171 1.00 125.21 ? 1973 MET B CG 1 ATOM 7007 S SD . MET B 2 326 ? -39.636 -49.489 70.832 1.00 137.05 ? 1973 MET B SD 1 ATOM 7008 C CE . MET B 2 326 ? -41.169 -49.542 71.780 1.00 144.62 ? 1973 MET B CE 1 ATOM 7009 N N . ALA B 2 327 ? -41.988 -45.198 68.581 1.00 119.96 ? 1974 ALA B N 1 ATOM 7010 C CA . ALA B 2 327 ? -41.849 -43.725 68.482 1.00 120.79 ? 1974 ALA B CA 1 ATOM 7011 C C . ALA B 2 327 ? -41.109 -43.093 69.655 1.00 116.37 ? 1974 ALA B C 1 ATOM 7012 O O . ALA B 2 327 ? -40.653 -41.919 69.580 1.00 109.40 ? 1974 ALA B O 1 ATOM 7013 C CB . ALA B 2 327 ? -43.195 -43.047 68.270 1.00 119.93 ? 1974 ALA B CB 1 ATOM 7014 N N . LEU B 2 328 ? -40.995 -43.880 70.723 1.00 107.95 ? 1975 LEU B N 1 ATOM 7015 C CA . LEU B 2 328 ? -40.309 -43.449 71.916 1.00 115.50 ? 1975 LEU B CA 1 ATOM 7016 C C . LEU B 2 328 ? -39.535 -44.628 72.425 1.00 118.68 ? 1975 LEU B C 1 ATOM 7017 O O . LEU B 2 328 ? -40.106 -45.708 72.551 1.00 136.96 ? 1975 LEU B O 1 ATOM 7018 C CB . LEU B 2 328 ? -41.326 -43.031 72.975 1.00 124.97 ? 1975 LEU B CB 1 ATOM 7019 C CG . LEU B 2 328 ? -40.927 -41.921 73.957 1.00 128.28 ? 1975 LEU B CG 1 ATOM 7020 C CD1 . LEU B 2 328 ? -42.149 -41.357 74.663 1.00 130.54 ? 1975 LEU B CD1 1 ATOM 7021 C CD2 . LEU B 2 328 ? -39.912 -42.403 74.976 1.00 127.12 ? 1975 LEU B CD2 1 ATOM 7022 N N . TYR B 2 329 ? -38.250 -44.426 72.722 1.00 117.70 ? 1976 TYR B N 1 ATOM 7023 C CA . TYR B 2 329 ? -37.407 -45.489 73.305 1.00 129.74 ? 1976 TYR B CA 1 ATOM 7024 C C . TYR B 2 329 ? -36.744 -45.003 74.602 1.00 128.79 ? 1976 TYR B C 1 ATOM 7025 O O . TYR B 2 329 ? -36.045 -43.992 74.593 1.00 135.67 ? 1976 TYR B O 1 ATOM 7026 C CB . TYR B 2 329 ? -36.354 -45.996 72.288 1.00 132.78 ? 1976 TYR B CB 1 ATOM 7027 C CG . TYR B 2 329 ? -35.730 -47.353 72.606 1.00 134.08 ? 1976 TYR B CG 1 ATOM 7028 C CD1 . TYR B 2 329 ? -34.753 -47.481 73.607 1.00 141.21 ? 1976 TYR B CD1 1 ATOM 7029 C CD2 . TYR B 2 329 ? -36.100 -48.497 71.900 1.00 132.11 ? 1976 TYR B CD2 1 ATOM 7030 C CE1 . TYR B 2 329 ? -34.178 -48.709 73.914 1.00 152.80 ? 1976 TYR B CE1 1 ATOM 7031 C CE2 . TYR B 2 329 ? -35.527 -49.732 72.199 1.00 153.42 ? 1976 TYR B CE2 1 ATOM 7032 C CZ . TYR B 2 329 ? -34.571 -49.836 73.210 1.00 158.86 ? 1976 TYR B CZ 1 ATOM 7033 O OH . TYR B 2 329 ? -34.000 -51.056 73.521 1.00 153.23 ? 1976 TYR B OH 1 ATOM 7034 N N . ASN B 2 330 ? -36.977 -45.720 75.706 1.00 123.55 ? 1977 ASN B N 1 ATOM 7035 C CA . ASN B 2 330 ? -36.436 -45.359 77.022 1.00 116.88 ? 1977 ASN B CA 1 ATOM 7036 C C . ASN B 2 330 ? -35.047 -45.933 77.200 1.00 120.85 ? 1977 ASN B C 1 ATOM 7037 O O . ASN B 2 330 ? -34.810 -47.112 76.940 1.00 133.21 ? 1977 ASN B O 1 ATOM 7038 C CB . ASN B 2 330 ? -37.333 -45.868 78.149 1.00 115.51 ? 1977 ASN B CB 1 ATOM 7039 C CG . ASN B 2 330 ? -38.820 -45.750 77.830 1.00 120.63 ? 1977 ASN B CG 1 ATOM 7040 O OD1 . ASN B 2 330 ? -39.553 -45.049 78.536 1.00 133.16 ? 1977 ASN B OD1 1 ATOM 7041 N ND2 . ASN B 2 330 ? -39.279 -46.446 76.781 1.00 107.44 ? 1977 ASN B ND2 1 ATOM 7042 N N . LEU B 2 331 ? -34.118 -45.100 77.634 1.00 125.07 ? 1978 LEU B N 1 ATOM 7043 C CA . LEU B 2 331 ? -32.756 -45.565 77.854 1.00 127.66 ? 1978 LEU B CA 1 ATOM 7044 C C . LEU B 2 331 ? -32.564 -45.915 79.304 1.00 133.17 ? 1978 LEU B C 1 ATOM 7045 O O . LEU B 2 331 ? -32.953 -45.168 80.194 1.00 141.59 ? 1978 LEU B O 1 ATOM 7046 C CB . LEU B 2 331 ? -31.740 -44.503 77.439 1.00 122.85 ? 1978 LEU B CB 1 ATOM 7047 C CG . LEU B 2 331 ? -31.133 -44.615 76.046 1.00 123.03 ? 1978 LEU B CG 1 ATOM 7048 C CD1 . LEU B 2 331 ? -32.043 -45.391 75.113 1.00 135.34 ? 1978 LEU B CD1 1 ATOM 7049 C CD2 . LEU B 2 331 ? -30.855 -43.240 75.472 1.00 121.98 ? 1978 LEU B CD2 1 ATOM 7050 N N . TYR B 2 332 ? -31.981 -47.068 79.550 1.00 133.51 ? 1979 TYR B N 1 ATOM 7051 C CA . TYR B 2 332 ? -31.562 -47.361 80.892 1.00 138.87 ? 1979 TYR B CA 1 ATOM 7052 C C . TYR B 2 332 ? -30.080 -47.125 80.895 1.00 135.74 ? 1979 TYR B C 1 ATOM 7053 O O . TYR B 2 332 ? -29.492 -47.004 79.825 1.00 144.38 ? 1979 TYR B O 1 ATOM 7054 C CB . TYR B 2 332 ? -31.962 -48.783 81.259 1.00 155.69 ? 1979 TYR B CB 1 ATOM 7055 C CG . TYR B 2 332 ? -33.460 -48.887 81.395 1.00 169.92 ? 1979 TYR B CG 1 ATOM 7056 C CD1 . TYR B 2 332 ? -34.102 -48.425 82.553 1.00 178.08 ? 1979 TYR B CD1 1 ATOM 7057 C CD2 . TYR B 2 332 ? -34.247 -49.393 80.359 1.00 163.74 ? 1979 TYR B CD2 1 ATOM 7058 C CE1 . TYR B 2 332 ? -35.481 -48.486 82.687 1.00 168.92 ? 1979 TYR B CE1 1 ATOM 7059 C CE2 . TYR B 2 332 ? -35.629 -49.459 80.492 1.00 169.16 ? 1979 TYR B CE2 1 ATOM 7060 C CZ . TYR B 2 332 ? -36.239 -48.998 81.654 1.00 163.73 ? 1979 TYR B CZ 1 ATOM 7061 O OH . TYR B 2 332 ? -37.604 -49.052 81.798 1.00 151.29 ? 1979 TYR B OH 1 ATOM 7062 N N . PRO B 2 333 ? -29.469 -47.005 82.077 1.00 139.19 ? 1980 PRO B N 1 ATOM 7063 C CA . PRO B 2 333 ? -28.014 -46.827 82.080 1.00 146.72 ? 1980 PRO B CA 1 ATOM 7064 C C . PRO B 2 333 ? -27.286 -48.017 81.436 1.00 141.85 ? 1980 PRO B C 1 ATOM 7065 O O . PRO B 2 333 ? -27.550 -49.166 81.796 1.00 153.81 ? 1980 PRO B O 1 ATOM 7066 C CB . PRO B 2 333 ? -27.669 -46.725 83.574 1.00 162.57 ? 1980 PRO B CB 1 ATOM 7067 C CG . PRO B 2 333 ? -28.948 -46.353 84.251 1.00 162.58 ? 1980 PRO B CG 1 ATOM 7068 C CD . PRO B 2 333 ? -30.045 -46.968 83.432 1.00 149.48 ? 1980 PRO B CD 1 ATOM 7069 N N . GLY B 2 334 ? -26.411 -47.738 80.470 1.00 136.90 ? 1981 GLY B N 1 ATOM 7070 C CA . GLY B 2 334 ? -25.543 -48.759 79.862 1.00 142.18 ? 1981 GLY B CA 1 ATOM 7071 C C . GLY B 2 334 ? -26.033 -49.450 78.598 1.00 146.23 ? 1981 GLY B C 1 ATOM 7072 O O . GLY B 2 334 ? -25.254 -50.131 77.918 1.00 154.88 ? 1981 GLY B O 1 ATOM 7073 N N . VAL B 2 335 ? -27.315 -49.275 78.277 1.00 141.84 ? 1982 VAL B N 1 ATOM 7074 C CA . VAL B 2 335 ? -27.936 -49.981 77.151 1.00 137.15 ? 1982 VAL B CA 1 ATOM 7075 C C . VAL B 2 335 ? -27.815 -49.225 75.827 1.00 140.43 ? 1982 VAL B C 1 ATOM 7076 O O . VAL B 2 335 ? -28.682 -48.424 75.449 1.00 136.26 ? 1982 VAL B O 1 ATOM 7077 C CB . VAL B 2 335 ? -29.394 -50.430 77.456 1.00 136.28 ? 1982 VAL B CB 1 ATOM 7078 C CG1 . VAL B 2 335 ? -29.412 -51.271 78.717 1.00 136.58 ? 1982 VAL B CG1 1 ATOM 7079 C CG2 . VAL B 2 335 ? -30.375 -49.259 77.579 1.00 136.62 ? 1982 VAL B CG2 1 ATOM 7080 N N . PHE B 2 336 ? -26.717 -49.481 75.129 1.00 143.85 ? 1983 PHE B N 1 ATOM 7081 C CA . PHE B 2 336 ? -26.473 -48.815 73.862 1.00 141.74 ? 1983 PHE B CA 1 ATOM 7082 C C . PHE B 2 336 ? -27.402 -49.422 72.820 1.00 142.27 ? 1983 PHE B C 1 ATOM 7083 O O . PHE B 2 336 ? -27.386 -50.635 72.570 1.00 147.86 ? 1983 PHE B O 1 ATOM 7084 C CB . PHE B 2 336 ? -25.005 -48.934 73.450 1.00 138.36 ? 1983 PHE B CB 1 ATOM 7085 C CG . PHE B 2 336 ? -24.396 -47.644 72.943 1.00 124.76 ? 1983 PHE B CG 1 ATOM 7086 C CD1 . PHE B 2 336 ? -25.014 -46.894 71.948 1.00 119.27 ? 1983 PHE B CD1 1 ATOM 7087 C CD2 . PHE B 2 336 ? -23.187 -47.184 73.458 1.00 118.33 ? 1983 PHE B CD2 1 ATOM 7088 C CE1 . PHE B 2 336 ? -24.435 -45.719 71.483 1.00 112.54 ? 1983 PHE B CE1 1 ATOM 7089 C CE2 . PHE B 2 336 ? -22.609 -46.012 72.994 1.00 108.90 ? 1983 PHE B CE2 1 ATOM 7090 C CZ . PHE B 2 336 ? -23.231 -45.282 72.004 1.00 106.22 ? 1983 PHE B CZ 1 ATOM 7091 N N . GLU B 2 337 ? -28.222 -48.560 72.235 1.00 139.61 ? 1984 GLU B N 1 ATOM 7092 C CA . GLU B 2 337 ? -29.339 -48.999 71.424 1.00 141.99 ? 1984 GLU B CA 1 ATOM 7093 C C . GLU B 2 337 ? -29.350 -48.441 69.991 1.00 135.56 ? 1984 GLU B C 1 ATOM 7094 O O . GLU B 2 337 ? -29.274 -47.234 69.765 1.00 138.23 ? 1984 GLU B O 1 ATOM 7095 C CB . GLU B 2 337 ? -30.656 -48.728 72.163 1.00 138.82 ? 1984 GLU B CB 1 ATOM 7096 C CG . GLU B 2 337 ? -31.819 -49.537 71.627 1.00 158.62 ? 1984 GLU B CG 1 ATOM 7097 C CD . GLU B 2 337 ? -31.473 -51.003 71.414 1.00 184.67 ? 1984 GLU B CD 1 ATOM 7098 O OE1 . GLU B 2 337 ? -30.734 -51.578 72.246 1.00 206.23 ? 1984 GLU B OE1 1 ATOM 7099 O OE2 . GLU B 2 337 ? -31.938 -51.583 70.407 1.00 191.59 ? 1984 GLU B OE2 1 ATOM 7100 N N . THR B 2 338 ? -29.465 -49.348 69.033 1.00 126.44 ? 1985 THR B N 1 ATOM 7101 C CA . THR B 2 338 ? -29.366 -49.018 67.629 1.00 121.92 ? 1985 THR B CA 1 ATOM 7102 C C . THR B 2 338 ? -30.772 -49.018 67.008 1.00 115.41 ? 1985 THR B C 1 ATOM 7103 O O . THR B 2 338 ? -31.461 -50.050 67.020 1.00 104.24 ? 1985 THR B O 1 ATOM 7104 C CB . THR B 2 338 ? -28.404 -50.021 66.936 1.00 130.12 ? 1985 THR B CB 1 ATOM 7105 O OG1 . THR B 2 338 ? -27.115 -49.966 67.570 1.00 118.85 ? 1985 THR B OG1 1 ATOM 7106 C CG2 . THR B 2 338 ? -28.250 -49.734 65.452 1.00 134.33 ? 1985 THR B CG2 1 ATOM 7107 N N . VAL B 2 339 ? -31.190 -47.851 66.496 1.00 114.89 ? 1986 VAL B N 1 ATOM 7108 C CA . VAL B 2 339 ? -32.456 -47.696 65.728 1.00 122.60 ? 1986 VAL B CA 1 ATOM 7109 C C . VAL B 2 339 ? -32.296 -46.983 64.387 1.00 130.47 ? 1986 VAL B C 1 ATOM 7110 O O . VAL B 2 339 ? -31.487 -46.057 64.283 1.00 126.17 ? 1986 VAL B O 1 ATOM 7111 C CB . VAL B 2 339 ? -33.513 -46.897 66.490 1.00 117.91 ? 1986 VAL B CB 1 ATOM 7112 C CG1 . VAL B 2 339 ? -34.139 -47.762 67.563 1.00 122.12 ? 1986 VAL B CG1 1 ATOM 7113 C CG2 . VAL B 2 339 ? -32.899 -45.625 67.062 1.00 117.48 ? 1986 VAL B CG2 1 ATOM 7114 N N . GLU B 2 340 ? -33.093 -47.406 63.392 1.00 137.26 ? 1987 GLU B N 1 ATOM 7115 C CA . GLU B 2 340 ? -33.055 -46.887 62.002 1.00 136.68 ? 1987 GLU B CA 1 ATOM 7116 C C . GLU B 2 340 ? -34.348 -46.099 61.672 1.00 129.99 ? 1987 GLU B C 1 ATOM 7117 O O . GLU B 2 340 ? -35.433 -46.487 62.106 1.00 126.94 ? 1987 GLU B O 1 ATOM 7118 C CB . GLU B 2 340 ? -32.798 -48.031 60.959 1.00 140.36 ? 1987 GLU B CB 1 ATOM 7119 C CG . GLU B 2 340 ? -31.319 -48.372 60.648 1.00 142.18 ? 1987 GLU B CG 1 ATOM 7120 C CD . GLU B 2 340 ? -31.081 -49.403 59.512 1.00 151.35 ? 1987 GLU B CD 1 ATOM 7121 O OE1 . GLU B 2 340 ? -31.968 -49.636 58.663 1.00 161.59 ? 1987 GLU B OE1 1 ATOM 7122 O OE2 . GLU B 2 340 ? -29.974 -49.989 59.436 1.00 139.61 ? 1987 GLU B OE2 1 ATOM 7123 N N . MET B 2 341 ? -34.225 -44.991 60.927 1.00 125.47 ? 1988 MET B N 1 ATOM 7124 C CA . MET B 2 341 ? -35.388 -44.207 60.459 1.00 123.88 ? 1988 MET B CA 1 ATOM 7125 C C . MET B 2 341 ? -35.171 -43.498 59.126 1.00 129.38 ? 1988 MET B C 1 ATOM 7126 O O . MET B 2 341 ? -34.061 -43.062 58.795 1.00 128.40 ? 1988 MET B O 1 ATOM 7127 C CB . MET B 2 341 ? -35.793 -43.157 61.485 1.00 124.63 ? 1988 MET B CB 1 ATOM 7128 C CG . MET B 2 341 ? -35.732 -41.714 61.001 1.00 118.47 ? 1988 MET B CG 1 ATOM 7129 S SD . MET B 2 341 ? -34.901 -40.632 62.174 1.00 124.62 ? 1988 MET B SD 1 ATOM 7130 C CE . MET B 2 341 ? -35.945 -40.764 63.623 1.00 119.43 ? 1988 MET B CE 1 ATOM 7131 N N . LEU B 2 342 ? -36.276 -43.343 58.407 1.00 131.25 ? 1989 LEU B N 1 ATOM 7132 C CA . LEU B 2 342 ? -36.319 -42.784 57.067 1.00 131.08 ? 1989 LEU B CA 1 ATOM 7133 C C . LEU B 2 342 ? -37.168 -41.520 57.204 1.00 135.08 ? 1989 LEU B C 1 ATOM 7134 O O . LEU B 2 342 ? -38.351 -41.624 57.533 1.00 165.92 ? 1989 LEU B O 1 ATOM 7135 C CB . LEU B 2 342 ? -36.996 -43.834 56.184 1.00 136.82 ? 1989 LEU B CB 1 ATOM 7136 C CG . LEU B 2 342 ? -37.247 -43.860 54.671 1.00 156.75 ? 1989 LEU B CG 1 ATOM 7137 C CD1 . LEU B 2 342 ? -37.300 -45.317 54.177 1.00 152.90 ? 1989 LEU B CD1 1 ATOM 7138 C CD2 . LEU B 2 342 ? -38.509 -43.082 54.275 1.00 166.49 ? 1989 LEU B CD2 1 ATOM 7139 N N . PRO B 2 343 ? -36.571 -40.321 57.000 1.00 124.93 ? 1990 PRO B N 1 ATOM 7140 C CA . PRO B 2 343 ? -37.221 -39.083 57.477 1.00 127.44 ? 1990 PRO B CA 1 ATOM 7141 C C . PRO B 2 343 ? -38.281 -38.368 56.626 1.00 144.74 ? 1990 PRO B C 1 ATOM 7142 O O . PRO B 2 343 ? -37.969 -37.572 55.747 1.00 128.90 ? 1990 PRO B O 1 ATOM 7143 C CB . PRO B 2 343 ? -36.048 -38.153 57.783 1.00 118.18 ? 1990 PRO B CB 1 ATOM 7144 C CG . PRO B 2 343 ? -34.865 -39.051 57.832 1.00 121.42 ? 1990 PRO B CG 1 ATOM 7145 C CD . PRO B 2 343 ? -35.138 -40.102 56.801 1.00 123.42 ? 1990 PRO B CD 1 ATOM 7146 N N . SER B 2 344 ? -39.535 -38.709 56.934 1.00 196.34 ? 1991 SER B N 1 ATOM 7147 C CA . SER B 2 344 ? -40.736 -37.859 56.792 1.00 215.65 ? 1991 SER B CA 1 ATOM 7148 C C . SER B 2 344 ? -40.647 -36.764 55.718 1.00 203.23 ? 1991 SER B C 1 ATOM 7149 O O . SER B 2 344 ? -40.412 -37.043 54.520 1.00 155.64 ? 1991 SER B O 1 ATOM 7150 C CB . SER B 2 344 ? -41.086 -37.248 58.190 1.00 226.36 ? 1991 SER B CB 1 ATOM 7151 O OG . SER B 2 344 ? -42.444 -36.820 58.347 1.00 201.81 ? 1991 SER B OG 1 ATOM 7152 N N . LYS B 2 345 ? -40.869 -35.534 56.197 1.00 204.74 ? 1992 LYS B N 1 ATOM 7153 C CA . LYS B 2 345 ? -40.832 -34.299 55.430 1.00 178.97 ? 1992 LYS B CA 1 ATOM 7154 C C . LYS B 2 345 ? -39.586 -33.548 55.868 1.00 163.12 ? 1992 LYS B C 1 ATOM 7155 O O . LYS B 2 345 ? -39.075 -33.732 56.995 1.00 139.55 ? 1992 LYS B O 1 ATOM 7156 C CB . LYS B 2 345 ? -42.091 -33.437 55.681 1.00 170.29 ? 1992 LYS B CB 1 ATOM 7157 C CG . LYS B 2 345 ? -43.393 -34.217 55.920 1.00 173.71 ? 1992 LYS B CG 1 ATOM 7158 C CD . LYS B 2 345 ? -43.973 -34.838 54.642 1.00 171.80 ? 1992 LYS B CD 1 ATOM 7159 C CE . LYS B 2 345 ? -44.935 -35.996 54.909 1.00 151.23 ? 1992 LYS B CE 1 ATOM 7160 N NZ . LYS B 2 345 ? -46.116 -35.634 55.739 1.00 134.51 ? 1992 LYS B NZ 1 ATOM 7161 N N . ALA B 2 346 ? -39.099 -32.720 54.952 1.00 160.01 ? 1993 ALA B N 1 ATOM 7162 C CA . ALA B 2 346 ? -37.862 -31.988 55.140 1.00 154.20 ? 1993 ALA B CA 1 ATOM 7163 C C . ALA B 2 346 ? -38.102 -30.820 56.069 1.00 147.61 ? 1993 ALA B C 1 ATOM 7164 O O . ALA B 2 346 ? -39.231 -30.342 56.195 1.00 148.48 ? 1993 ALA B O 1 ATOM 7165 C CB . ALA B 2 346 ? -37.324 -31.506 53.801 1.00 159.96 ? 1993 ALA B CB 1 ATOM 7166 N N . GLY B 2 347 ? -37.037 -30.364 56.716 1.00 140.04 ? 1994 GLY B N 1 ATOM 7167 C CA . GLY B 2 347 ? -37.138 -29.247 57.639 1.00 147.85 ? 1994 GLY B CA 1 ATOM 7168 C C . GLY B 2 347 ? -36.262 -29.367 58.872 1.00 148.86 ? 1994 GLY B C 1 ATOM 7169 O O . GLY B 2 347 ? -35.343 -30.196 58.932 1.00 148.46 ? 1994 GLY B O 1 ATOM 7170 N N . ILE B 2 348 ? -36.558 -28.524 59.856 1.00 140.72 ? 1995 ILE B N 1 ATOM 7171 C CA . ILE B 2 348 ? -35.755 -28.419 61.059 1.00 129.66 ? 1995 ILE B CA 1 ATOM 7172 C C . ILE B 2 348 ? -36.591 -28.881 62.258 1.00 132.37 ? 1995 ILE B C 1 ATOM 7173 O O . ILE B 2 348 ? -37.523 -28.184 62.683 1.00 137.10 ? 1995 ILE B O 1 ATOM 7174 C CB . ILE B 2 348 ? -35.206 -26.985 61.201 1.00 123.64 ? 1995 ILE B CB 1 ATOM 7175 C CG1 . ILE B 2 348 ? -34.769 -26.710 62.642 1.00 132.78 ? 1995 ILE B CG1 1 ATOM 7176 C CG2 . ILE B 2 348 ? -36.233 -25.979 60.699 1.00 115.03 ? 1995 ILE B CG2 1 ATOM 7177 C CD1 . ILE B 2 348 ? -33.751 -25.597 62.795 1.00 150.23 ? 1995 ILE B CD1 1 ATOM 7178 N N . TRP B 2 349 ? -36.259 -30.070 62.774 1.00 123.63 ? 1996 TRP B N 1 ATOM 7179 C CA . TRP B 2 349 ? -37.062 -30.756 63.802 1.00 122.49 ? 1996 TRP B CA 1 ATOM 7180 C C . TRP B 2 349 ? -36.308 -30.943 65.122 1.00 122.29 ? 1996 TRP B C 1 ATOM 7181 O O . TRP B 2 349 ? -35.130 -30.603 65.192 1.00 125.39 ? 1996 TRP B O 1 ATOM 7182 C CB . TRP B 2 349 ? -37.453 -32.131 63.309 1.00 115.99 ? 1996 TRP B CB 1 ATOM 7183 C CG . TRP B 2 349 ? -38.277 -32.192 62.090 1.00 123.08 ? 1996 TRP B CG 1 ATOM 7184 C CD1 . TRP B 2 349 ? -37.844 -32.434 60.824 1.00 134.93 ? 1996 TRP B CD1 1 ATOM 7185 C CD2 . TRP B 2 349 ? -39.691 -32.083 62.013 1.00 125.37 ? 1996 TRP B CD2 1 ATOM 7186 N NE1 . TRP B 2 349 ? -38.902 -32.469 59.953 1.00 134.07 ? 1996 TRP B NE1 1 ATOM 7187 C CE2 . TRP B 2 349 ? -40.051 -32.253 60.663 1.00 130.22 ? 1996 TRP B CE2 1 ATOM 7188 C CE3 . TRP B 2 349 ? -40.693 -31.853 62.953 1.00 136.33 ? 1996 TRP B CE3 1 ATOM 7189 C CZ2 . TRP B 2 349 ? -41.369 -32.203 60.231 1.00 139.82 ? 1996 TRP B CZ2 1 ATOM 7190 C CZ3 . TRP B 2 349 ? -42.007 -31.798 62.521 1.00 146.63 ? 1996 TRP B CZ3 1 ATOM 7191 C CH2 . TRP B 2 349 ? -42.333 -31.976 61.172 1.00 143.66 ? 1996 TRP B CH2 1 ATOM 7192 N N . ARG B 2 350 ? -36.969 -31.492 66.157 1.00 121.19 ? 1997 ARG B N 1 ATOM 7193 C CA . ARG B 2 350 ? -36.273 -31.791 67.428 1.00 121.71 ? 1997 ARG B CA 1 ATOM 7194 C C . ARG B 2 350 ? -36.293 -33.221 67.975 1.00 120.22 ? 1997 ARG B C 1 ATOM 7195 O O . ARG B 2 350 ? -37.167 -34.043 67.673 1.00 107.18 ? 1997 ARG B O 1 ATOM 7196 C CB . ARG B 2 350 ? -36.571 -30.764 68.552 1.00 131.89 ? 1997 ARG B CB 1 ATOM 7197 C CG . ARG B 2 350 ? -37.918 -30.867 69.259 1.00 141.34 ? 1997 ARG B CG 1 ATOM 7198 C CD . ARG B 2 350 ? -37.828 -30.541 70.762 1.00 159.51 ? 1997 ARG B CD 1 ATOM 7199 N NE . ARG B 2 350 ? -37.617 -29.125 71.136 1.00 173.69 ? 1997 ARG B NE 1 ATOM 7200 C CZ . ARG B 2 350 ? -37.956 -28.573 72.318 1.00 186.93 ? 1997 ARG B CZ 1 ATOM 7201 N NH1 . ARG B 2 350 ? -38.546 -29.272 73.283 1.00 191.78 ? 1997 ARG B NH1 1 ATOM 7202 N NH2 . ARG B 2 350 ? -37.703 -27.298 72.554 1.00 192.54 ? 1997 ARG B NH2 1 ATOM 7203 N N . VAL B 2 351 ? -35.262 -33.491 68.770 1.00 132.27 ? 1998 VAL B N 1 ATOM 7204 C CA . VAL B 2 351 ? -35.143 -34.696 69.573 1.00 137.54 ? 1998 VAL B CA 1 ATOM 7205 C C . VAL B 2 351 ? -34.954 -34.295 71.048 1.00 142.81 ? 1998 VAL B C 1 ATOM 7206 O O . VAL B 2 351 ? -34.043 -33.533 71.392 1.00 150.31 ? 1998 VAL B O 1 ATOM 7207 C CB . VAL B 2 351 ? -34.018 -35.634 69.069 1.00 136.63 ? 1998 VAL B CB 1 ATOM 7208 C CG1 . VAL B 2 351 ? -32.645 -34.936 68.966 1.00 126.43 ? 1998 VAL B CG1 1 ATOM 7209 C CG2 . VAL B 2 351 ? -33.962 -36.861 69.957 1.00 139.68 ? 1998 VAL B CG2 1 ATOM 7210 N N . GLU B 2 352 ? -35.833 -34.816 71.901 1.00 138.22 ? 1999 GLU B N 1 ATOM 7211 C CA . GLU B 2 352 ? -36.016 -34.332 73.268 1.00 133.04 ? 1999 GLU B CA 1 ATOM 7212 C C . GLU B 2 352 ? -36.354 -35.519 74.170 1.00 131.36 ? 1999 GLU B C 1 ATOM 7213 O O . GLU B 2 352 ? -37.021 -36.462 73.727 1.00 135.09 ? 1999 GLU B O 1 ATOM 7214 C CB . GLU B 2 352 ? -37.186 -33.349 73.291 1.00 131.68 ? 1999 GLU B CB 1 ATOM 7215 C CG . GLU B 2 352 ? -38.540 -34.032 73.073 1.00 147.23 ? 1999 GLU B CG 1 ATOM 7216 C CD . GLU B 2 352 ? -39.684 -33.097 72.698 1.00 161.19 ? 1999 GLU B CD 1 ATOM 7217 O OE1 . GLU B 2 352 ? -39.569 -31.874 72.918 1.00 167.06 ? 1999 GLU B OE1 1 ATOM 7218 O OE2 . GLU B 2 352 ? -40.721 -33.595 72.190 1.00 163.67 ? 1999 GLU B OE2 1 ATOM 7219 N N . CYS B 2 353 ? -35.917 -35.481 75.428 1.00 122.95 ? 2000 CYS B N 1 ATOM 7220 C CA . CYS B 2 353 ? -36.388 -36.481 76.394 1.00 116.30 ? 2000 CYS B CA 1 ATOM 7221 C C . CYS B 2 353 ? -37.754 -36.076 76.920 1.00 115.63 ? 2000 CYS B C 1 ATOM 7222 O O . CYS B 2 353 ? -37.879 -35.116 77.663 1.00 133.39 ? 2000 CYS B O 1 ATOM 7223 C CB . CYS B 2 353 ? -35.424 -36.674 77.566 1.00 112.13 ? 2000 CYS B CB 1 ATOM 7224 S SG . CYS B 2 353 ? -36.254 -37.407 79.004 1.00 115.90 ? 2000 CYS B SG 1 ATOM 7225 N N . LEU B 2 354 ? -38.777 -36.825 76.567 1.00 109.79 ? 2001 LEU B N 1 ATOM 7226 C CA . LEU B 2 354 ? -40.144 -36.397 76.821 1.00 117.35 ? 2001 LEU B CA 1 ATOM 7227 C C . LEU B 2 354 ? -40.609 -36.302 78.308 1.00 128.89 ? 2001 LEU B C 1 ATOM 7228 O O . LEU B 2 354 ? -41.799 -36.019 78.618 1.00 131.21 ? 2001 LEU B O 1 ATOM 7229 C CB . LEU B 2 354 ? -41.052 -37.325 76.048 1.00 116.66 ? 2001 LEU B CB 1 ATOM 7230 C CG . LEU B 2 354 ? -41.966 -36.652 75.052 1.00 116.67 ? 2001 LEU B CG 1 ATOM 7231 C CD1 . LEU B 2 354 ? -42.753 -37.769 74.398 1.00 125.35 ? 2001 LEU B CD1 1 ATOM 7232 C CD2 . LEU B 2 354 ? -42.887 -35.656 75.732 1.00 118.33 ? 2001 LEU B CD2 1 ATOM 7233 N N . ILE B 2 355 ? -39.693 -36.538 79.238 1.00 128.93 ? 2002 ILE B N 1 ATOM 7234 C CA . ILE B 2 355 ? -40.102 -36.475 80.623 1.00 135.05 ? 2002 ILE B CA 1 ATOM 7235 C C . ILE B 2 355 ? -39.929 -35.084 81.135 1.00 138.94 ? 2002 ILE B C 1 ATOM 7236 O O . ILE B 2 355 ? -38.817 -34.639 81.437 1.00 126.71 ? 2002 ILE B O 1 ATOM 7237 C CB . ILE B 2 355 ? -39.426 -37.515 81.520 1.00 140.24 ? 2002 ILE B CB 1 ATOM 7238 C CG1 . ILE B 2 355 ? -37.911 -37.498 81.355 1.00 127.96 ? 2002 ILE B CG1 1 ATOM 7239 C CG2 . ILE B 2 355 ? -40.014 -38.887 81.224 1.00 152.14 ? 2002 ILE B CG2 1 ATOM 7240 C CD1 . ILE B 2 355 ? -37.212 -38.306 82.419 1.00 128.94 ? 2002 ILE B CD1 1 ATOM 7241 N N . GLY B 2 356 ? -41.073 -34.410 81.193 1.00 153.96 ? 2003 GLY B N 1 ATOM 7242 C CA . GLY B 2 356 ? -41.187 -32.998 81.550 1.00 162.32 ? 2003 GLY B CA 1 ATOM 7243 C C . GLY B 2 356 ? -39.953 -32.335 82.130 1.00 156.24 ? 2003 GLY B C 1 ATOM 7244 O O . GLY B 2 356 ? -39.153 -31.761 81.397 1.00 153.82 ? 2003 GLY B O 1 ATOM 7245 N N . GLU B 2 357 ? -39.803 -32.426 83.450 1.00 157.02 ? 2004 GLU B N 1 ATOM 7246 C CA . GLU B 2 357 ? -38.746 -31.720 84.177 1.00 155.57 ? 2004 GLU B CA 1 ATOM 7247 C C . GLU B 2 357 ? -37.432 -31.819 83.411 1.00 147.31 ? 2004 GLU B C 1 ATOM 7248 O O . GLU B 2 357 ? -36.845 -30.797 83.059 1.00 142.99 ? 2004 GLU B O 1 ATOM 7249 C CB . GLU B 2 357 ? -38.632 -32.234 85.629 1.00 169.21 ? 2004 GLU B CB 1 ATOM 7250 C CG . GLU B 2 357 ? -39.550 -31.528 86.643 1.00 180.50 ? 2004 GLU B CG 1 ATOM 7251 C CD . GLU B 2 357 ? -40.153 -32.458 87.705 1.00 190.20 ? 2004 GLU B CD 1 ATOM 7252 O OE1 . GLU B 2 357 ? -39.587 -33.547 87.969 1.00 187.84 ? 2004 GLU B OE1 1 ATOM 7253 O OE2 . GLU B 2 357 ? -41.208 -32.100 88.284 1.00 192.91 ? 2004 GLU B OE2 1 ATOM 7254 N N . HIS B 2 358 ? -37.030 -33.051 83.101 1.00 142.04 ? 2005 HIS B N 1 ATOM 7255 C CA . HIS B 2 358 ? -35.841 -33.359 82.306 1.00 136.60 ? 2005 HIS B CA 1 ATOM 7256 C C . HIS B 2 358 ? -35.657 -32.560 81.010 1.00 130.02 ? 2005 HIS B C 1 ATOM 7257 O O . HIS B 2 358 ? -34.533 -32.428 80.500 1.00 120.12 ? 2005 HIS B O 1 ATOM 7258 C CB . HIS B 2 358 ? -35.877 -34.832 81.955 1.00 144.40 ? 2005 HIS B CB 1 ATOM 7259 C CG . HIS B 2 358 ? -35.051 -35.681 82.859 1.00 161.51 ? 2005 HIS B CG 1 ATOM 7260 N ND1 . HIS B 2 358 ? -34.392 -36.813 82.413 1.00 173.61 ? 2005 HIS B ND1 1 ATOM 7261 C CD2 . HIS B 2 358 ? -34.748 -35.548 84.174 1.00 164.75 ? 2005 HIS B CD2 1 ATOM 7262 C CE1 . HIS B 2 358 ? -33.738 -37.350 83.433 1.00 177.14 ? 2005 HIS B CE1 1 ATOM 7263 N NE2 . HIS B 2 358 ? -33.935 -36.602 84.508 1.00 175.27 ? 2005 HIS B NE2 1 ATOM 7264 N N . LEU B 2 359 ? -36.768 -32.051 80.482 1.00 126.47 ? 2006 LEU B N 1 ATOM 7265 C CA . LEU B 2 359 ? -36.784 -31.312 79.229 1.00 119.25 ? 2006 LEU B CA 1 ATOM 7266 C C . LEU B 2 359 ? -36.565 -29.822 79.455 1.00 127.29 ? 2006 LEU B C 1 ATOM 7267 O O . LEU B 2 359 ? -35.691 -29.219 78.842 1.00 130.14 ? 2006 LEU B O 1 ATOM 7268 C CB . LEU B 2 359 ? -38.124 -31.514 78.529 1.00 109.49 ? 2006 LEU B CB 1 ATOM 7269 C CG . LEU B 2 359 ? -38.110 -31.672 77.015 1.00 103.88 ? 2006 LEU B CG 1 ATOM 7270 C CD1 . LEU B 2 359 ? -39.196 -30.788 76.410 1.00 102.68 ? 2006 LEU B CD1 1 ATOM 7271 C CD2 . LEU B 2 359 ? -36.731 -31.383 76.419 1.00 102.53 ? 2006 LEU B CD2 1 ATOM 7272 N N . HIS B 2 360 ? -37.374 -29.233 80.327 1.00 135.99 ? 2007 HIS B N 1 ATOM 7273 C CA . HIS B 2 360 ? -37.294 -27.810 80.610 1.00 152.53 ? 2007 HIS B CA 1 ATOM 7274 C C . HIS B 2 360 ? -36.152 -27.649 81.572 1.00 151.72 ? 2007 HIS B C 1 ATOM 7275 O O . HIS B 2 360 ? -36.223 -26.914 82.568 1.00 169.79 ? 2007 HIS B O 1 ATOM 7276 C CB . HIS B 2 360 ? -38.600 -27.307 81.214 1.00 179.51 ? 2007 HIS B CB 1 ATOM 7277 C CG . HIS B 2 360 ? -39.808 -27.615 80.381 1.00 193.65 ? 2007 HIS B CG 1 ATOM 7278 N ND1 . HIS B 2 360 ? -40.997 -26.931 80.517 1.00 201.91 ? 2007 HIS B ND1 1 ATOM 7279 C CD2 . HIS B 2 360 ? -40.010 -28.531 79.402 1.00 192.88 ? 2007 HIS B CD2 1 ATOM 7280 C CE1 . HIS B 2 360 ? -41.881 -27.419 79.664 1.00 191.97 ? 2007 HIS B CE1 1 ATOM 7281 N NE2 . HIS B 2 360 ? -41.308 -28.391 78.977 1.00 191.43 ? 2007 HIS B NE2 1 ATOM 7282 N N . ALA B 2 361 ? -35.103 -28.386 81.240 1.00 140.74 ? 2008 ALA B N 1 ATOM 7283 C CA . ALA B 2 361 ? -33.852 -28.422 81.958 1.00 148.79 ? 2008 ALA B CA 1 ATOM 7284 C C . ALA B 2 361 ? -32.770 -28.557 80.917 1.00 146.66 ? 2008 ALA B C 1 ATOM 7285 O O . ALA B 2 361 ? -31.573 -28.595 81.253 1.00 140.91 ? 2008 ALA B O 1 ATOM 7286 C CB . ALA B 2 361 ? -33.823 -29.626 82.871 1.00 163.24 ? 2008 ALA B CB 1 ATOM 7287 N N . GLY B 2 362 ? -33.233 -28.678 79.665 1.00 148.23 ? 2009 GLY B N 1 ATOM 7288 C CA . GLY B 2 362 ? -32.412 -28.739 78.454 1.00 140.55 ? 2009 GLY B CA 1 ATOM 7289 C C . GLY B 2 362 ? -32.269 -30.125 77.868 1.00 133.04 ? 2009 GLY B C 1 ATOM 7290 O O . GLY B 2 362 ? -31.355 -30.854 78.222 1.00 133.17 ? 2009 GLY B O 1 ATOM 7291 N N . MET B 2 363 ? -33.167 -30.521 76.984 1.00 128.04 ? 2010 MET B N 1 ATOM 7292 C CA . MET B 2 363 ? -32.899 -31.749 76.269 1.00 133.29 ? 2010 MET B CA 1 ATOM 7293 C C . MET B 2 363 ? -33.041 -31.509 74.789 1.00 137.78 ? 2010 MET B C 1 ATOM 7294 O O . MET B 2 363 ? -32.244 -32.020 74.007 1.00 130.69 ? 2010 MET B O 1 ATOM 7295 C CB . MET B 2 363 ? -33.723 -32.932 76.794 1.00 132.01 ? 2010 MET B CB 1 ATOM 7296 C CG . MET B 2 363 ? -33.088 -33.613 78.015 1.00 131.93 ? 2010 MET B CG 1 ATOM 7297 S SD . MET B 2 363 ? -32.170 -35.151 77.715 1.00 129.65 ? 2010 MET B SD 1 ATOM 7298 C CE . MET B 2 363 ? -30.865 -35.091 78.952 1.00 116.66 ? 2010 MET B CE 1 ATOM 7299 N N . SER B 2 364 ? -34.012 -30.677 74.420 1.00 153.06 ? 2011 SER B N 1 ATOM 7300 C CA . SER B 2 364 ? -34.210 -30.283 73.018 1.00 168.83 ? 2011 SER B CA 1 ATOM 7301 C C . SER B 2 364 ? -32.887 -30.130 72.290 1.00 167.14 ? 2011 SER B C 1 ATOM 7302 O O . SER B 2 364 ? -31.925 -29.567 72.811 1.00 186.98 ? 2011 SER B O 1 ATOM 7303 C CB . SER B 2 364 ? -34.998 -28.971 72.901 1.00 174.43 ? 2011 SER B CB 1 ATOM 7304 O OG . SER B 2 364 ? -35.155 -28.558 71.536 1.00 160.55 ? 2011 SER B OG 1 ATOM 7305 N N . THR B 2 365 ? -32.849 -30.643 71.077 1.00 147.45 ? 2012 THR B N 1 ATOM 7306 C CA . THR B 2 365 ? -31.675 -30.536 70.266 1.00 136.46 ? 2012 THR B CA 1 ATOM 7307 C C . THR B 2 365 ? -32.181 -30.791 68.903 1.00 132.73 ? 2012 THR B C 1 ATOM 7308 O O . THR B 2 365 ? -33.091 -31.596 68.724 1.00 143.40 ? 2012 THR B O 1 ATOM 7309 C CB . THR B 2 365 ? -30.642 -31.575 70.679 1.00 135.74 ? 2012 THR B CB 1 ATOM 7310 O OG1 . THR B 2 365 ? -29.801 -30.969 71.664 1.00 139.91 ? 2012 THR B OG1 1 ATOM 7311 C CG2 . THR B 2 365 ? -29.807 -32.048 69.484 1.00 131.02 ? 2012 THR B CG2 1 ATOM 7312 N N . LEU B 2 366 ? -31.616 -30.092 67.937 1.00 120.61 ? 2013 LEU B N 1 ATOM 7313 C CA . LEU B 2 366 ? -32.232 -30.064 66.631 1.00 118.91 ? 2013 LEU B CA 1 ATOM 7314 C C . LEU B 2 366 ? -31.508 -30.847 65.535 1.00 120.53 ? 2013 LEU B C 1 ATOM 7315 O O . LEU B 2 366 ? -30.325 -31.162 65.658 1.00 125.28 ? 2013 LEU B O 1 ATOM 7316 C CB . LEU B 2 366 ? -32.460 -28.626 66.220 1.00 118.28 ? 2013 LEU B CB 1 ATOM 7317 C CG . LEU B 2 366 ? -33.669 -27.974 66.874 1.00 120.82 ? 2013 LEU B CG 1 ATOM 7318 C CD1 . LEU B 2 366 ? -33.682 -28.046 68.401 1.00 115.89 ? 2013 LEU B CD1 1 ATOM 7319 C CD2 . LEU B 2 366 ? -33.691 -26.537 66.381 1.00 135.46 ? 2013 LEU B CD2 1 ATOM 7320 N N . PHE B 2 367 ? -32.250 -31.165 64.474 1.00 122.10 ? 2014 PHE B N 1 ATOM 7321 C CA . PHE B 2 367 ? -31.700 -31.782 63.266 1.00 124.82 ? 2014 PHE B CA 1 ATOM 7322 C C . PHE B 2 367 ? -32.392 -31.245 62.002 1.00 135.55 ? 2014 PHE B C 1 ATOM 7323 O O . PHE B 2 367 ? -33.620 -31.026 61.977 1.00 132.42 ? 2014 PHE B O 1 ATOM 7324 C CB . PHE B 2 367 ? -31.726 -33.325 63.341 1.00 115.66 ? 2014 PHE B CB 1 ATOM 7325 C CG . PHE B 2 367 ? -33.113 -33.932 63.484 1.00 121.12 ? 2014 PHE B CG 1 ATOM 7326 C CD1 . PHE B 2 367 ? -33.933 -33.633 64.578 1.00 118.30 ? 2014 PHE B CD1 1 ATOM 7327 C CD2 . PHE B 2 367 ? -33.593 -34.838 62.526 1.00 121.25 ? 2014 PHE B CD2 1 ATOM 7328 C CE1 . PHE B 2 367 ? -35.196 -34.206 64.693 1.00 113.42 ? 2014 PHE B CE1 1 ATOM 7329 C CE2 . PHE B 2 367 ? -34.858 -35.416 62.641 1.00 108.05 ? 2014 PHE B CE2 1 ATOM 7330 C CZ . PHE B 2 367 ? -35.657 -35.093 63.722 1.00 108.30 ? 2014 PHE B CZ 1 ATOM 7331 N N . LEU B 2 368 ? -31.591 -30.994 60.969 1.00 137.58 ? 2015 LEU B N 1 ATOM 7332 C CA . LEU B 2 368 ? -32.147 -30.589 59.698 1.00 130.64 ? 2015 LEU B CA 1 ATOM 7333 C C . LEU B 2 368 ? -32.119 -31.744 58.748 1.00 128.54 ? 2015 LEU B C 1 ATOM 7334 O O . LEU B 2 368 ? -31.053 -32.298 58.445 1.00 122.69 ? 2015 LEU B O 1 ATOM 7335 C CB . LEU B 2 368 ? -31.407 -29.411 59.067 1.00 133.47 ? 2015 LEU B CB 1 ATOM 7336 C CG . LEU B 2 368 ? -32.014 -28.969 57.717 1.00 142.67 ? 2015 LEU B CG 1 ATOM 7337 C CD1 . LEU B 2 368 ? -33.249 -28.104 57.888 1.00 146.82 ? 2015 LEU B CD1 1 ATOM 7338 C CD2 . LEU B 2 368 ? -31.015 -28.254 56.818 1.00 155.93 ? 2015 LEU B CD2 1 ATOM 7339 N N . VAL B 2 369 ? -33.319 -32.092 58.301 1.00 131.89 ? 2016 VAL B N 1 ATOM 7340 C CA . VAL B 2 369 ? -33.511 -32.884 57.098 1.00 137.84 ? 2016 VAL B CA 1 ATOM 7341 C C . VAL B 2 369 ? -33.784 -31.961 55.902 1.00 129.73 ? 2016 VAL B C 1 ATOM 7342 O O . VAL B 2 369 ? -34.824 -31.295 55.800 1.00 116.32 ? 2016 VAL B O 1 ATOM 7343 C CB . VAL B 2 369 ? -34.589 -33.974 57.279 1.00 153.13 ? 2016 VAL B CB 1 ATOM 7344 C CG1 . VAL B 2 369 ? -34.074 -35.041 58.223 1.00 154.60 ? 2016 VAL B CG1 1 ATOM 7345 C CG2 . VAL B 2 369 ? -35.896 -33.404 57.819 1.00 165.92 ? 2016 VAL B CG2 1 ATOM 7346 N N . TYR B 2 370 ? -32.795 -31.881 55.029 1.00 126.10 ? 2017 TYR B N 1 ATOM 7347 C CA . TYR B 2 370 ? -32.914 -31.051 53.855 1.00 133.45 ? 2017 TYR B CA 1 ATOM 7348 C C . TYR B 2 370 ? -33.292 -31.981 52.770 1.00 141.84 ? 2017 TYR B C 1 ATOM 7349 O O . TYR B 2 370 ? -33.067 -33.197 52.883 1.00 149.05 ? 2017 TYR B O 1 ATOM 7350 C CB . TYR B 2 370 ? -31.590 -30.401 53.475 1.00 130.82 ? 2017 TYR B CB 1 ATOM 7351 C CG . TYR B 2 370 ? -30.445 -31.376 53.295 1.00 124.59 ? 2017 TYR B CG 1 ATOM 7352 C CD1 . TYR B 2 370 ? -29.907 -32.047 54.382 1.00 121.67 ? 2017 TYR B CD1 1 ATOM 7353 C CD2 . TYR B 2 370 ? -29.887 -31.615 52.042 1.00 132.52 ? 2017 TYR B CD2 1 ATOM 7354 C CE1 . TYR B 2 370 ? -28.847 -32.930 54.233 1.00 131.57 ? 2017 TYR B CE1 1 ATOM 7355 C CE2 . TYR B 2 370 ? -28.821 -32.510 51.878 1.00 133.97 ? 2017 TYR B CE2 1 ATOM 7356 C CZ . TYR B 2 370 ? -28.301 -33.172 52.986 1.00 131.95 ? 2017 TYR B CZ 1 ATOM 7357 O OH . TYR B 2 370 ? -27.246 -34.074 52.877 1.00 129.34 ? 2017 TYR B OH 1 ATOM 7358 N N . SER B 2 371 ? -33.886 -31.410 51.730 1.00 137.23 ? 2018 SER B N 1 ATOM 7359 C CA . SER B 2 371 ? -34.062 -32.115 50.485 1.00 136.30 ? 2018 SER B CA 1 ATOM 7360 C C . SER B 2 371 ? -32.851 -31.704 49.724 1.00 134.59 ? 2018 SER B C 1 ATOM 7361 O O . SER B 2 371 ? -32.337 -30.588 49.956 1.00 125.64 ? 2018 SER B O 1 ATOM 7362 C CB . SER B 2 371 ? -35.308 -31.634 49.748 1.00 137.62 ? 2018 SER B CB 1 ATOM 7363 O OG . SER B 2 371 ? -35.299 -32.129 48.422 1.00 139.07 ? 2018 SER B OG 1 ATOM 7364 N N . ASN B 2 372 ? -32.368 -32.610 48.867 1.00 143.74 ? 2019 ASN B N 1 ATOM 7365 C CA . ASN B 2 372 ? -31.386 -32.223 47.848 1.00 157.68 ? 2019 ASN B CA 1 ATOM 7366 C C . ASN B 2 372 ? -31.906 -32.359 46.428 1.00 159.34 ? 2019 ASN B C 1 ATOM 7367 O O . ASN B 2 372 ? -31.154 -32.176 45.464 1.00 169.67 ? 2019 ASN B O 1 ATOM 7368 C CB . ASN B 2 372 ? -29.988 -32.837 48.038 1.00 161.02 ? 2019 ASN B CB 1 ATOM 7369 C CG . ASN B 2 372 ? -30.013 -34.336 48.143 1.00 185.05 ? 2019 ASN B CG 1 ATOM 7370 O OD1 . ASN B 2 372 ? -31.082 -34.970 48.108 1.00 188.61 ? 2019 ASN B OD1 1 ATOM 7371 N ND2 . ASN B 2 372 ? -28.823 -34.923 48.286 1.00 200.45 ? 2019 ASN B ND2 1 ATOM 7372 N N . LYS B 2 373 ? -33.201 -32.661 46.309 1.00 158.20 ? 2020 LYS B N 1 ATOM 7373 C CA . LYS B 2 373 ? -33.924 -32.334 45.080 1.00 158.97 ? 2020 LYS B CA 1 ATOM 7374 C C . LYS B 2 373 ? -34.220 -30.827 45.058 1.00 154.67 ? 2020 LYS B C 1 ATOM 7375 O O . LYS B 2 373 ? -34.957 -30.347 44.209 1.00 162.41 ? 2020 LYS B O 1 ATOM 7376 C CB . LYS B 2 373 ? -35.180 -33.198 44.879 1.00 161.89 ? 2020 LYS B CB 1 ATOM 7377 C CG . LYS B 2 373 ? -34.847 -34.616 44.425 1.00 177.57 ? 2020 LYS B CG 1 ATOM 7378 C CD . LYS B 2 373 ? -35.945 -35.281 43.601 1.00 190.90 ? 2020 LYS B CD 1 ATOM 7379 C CE . LYS B 2 373 ? -35.443 -36.585 42.974 1.00 196.78 ? 2020 LYS B CE 1 ATOM 7380 N NZ . LYS B 2 373 ? -36.350 -37.193 41.950 1.00 195.19 ? 2020 LYS B NZ 1 ATOM 7381 N N . CYS B 2 374 ? -33.625 -30.101 46.007 1.00 149.68 ? 2021 CYS B N 1 ATOM 7382 C CA . CYS B 2 374 ? -33.532 -28.647 45.986 1.00 145.58 ? 2021 CYS B CA 1 ATOM 7383 C C . CYS B 2 374 ? -32.069 -28.217 45.965 1.00 144.23 ? 2021 CYS B C 1 ATOM 7384 O O . CYS B 2 374 ? -31.512 -27.856 47.006 1.00 143.44 ? 2021 CYS B O 1 ATOM 7385 C CB . CYS B 2 374 ? -34.197 -28.020 47.217 1.00 161.74 ? 2021 CYS B CB 1 ATOM 7386 S SG . CYS B 2 374 ? -34.069 -26.208 47.217 1.00 211.19 ? 2021 CYS B SG 1 ATOM 7387 N N . GLN B 2 375 ? -31.429 -28.309 44.804 1.00 150.20 ? 2022 GLN B N 1 ATOM 7388 C CA . GLN B 2 375 ? -30.238 -27.500 44.526 1.00 154.10 ? 2022 GLN B CA 1 ATOM 7389 C C . GLN B 2 375 ? -30.780 -26.354 43.647 1.00 154.45 ? 2022 GLN B C 1 ATOM 7390 O O . GLN B 2 375 ? -31.663 -26.588 42.807 1.00 163.01 ? 2022 GLN B O 1 ATOM 7391 C CB . GLN B 2 375 ? -29.121 -28.313 43.814 1.00 162.67 ? 2022 GLN B CB 1 ATOM 7392 C CG . GLN B 2 375 ? -27.983 -28.852 44.699 1.00 155.78 ? 2022 GLN B CG 1 ATOM 7393 C CD . GLN B 2 375 ? -26.676 -29.195 43.946 1.00 159.03 ? 2022 GLN B CD 1 ATOM 7394 O OE1 . GLN B 2 375 ? -26.267 -28.506 43.003 1.00 157.22 ? 2022 GLN B OE1 1 ATOM 7395 N NE2 . GLN B 2 375 ? -26.006 -30.258 44.388 1.00 153.06 ? 2022 GLN B NE2 1 ATOM 7396 N N . THR B 2 376 ? -30.306 -25.122 43.862 1.00 138.21 ? 2023 THR B N 1 ATOM 7397 C CA . THR B 2 376 ? -30.740 -23.965 43.044 1.00 135.82 ? 2023 THR B CA 1 ATOM 7398 C C . THR B 2 376 ? -29.767 -22.777 43.108 1.00 135.55 ? 2023 THR B C 1 ATOM 7399 O O . THR B 2 376 ? -29.047 -22.617 44.101 1.00 141.68 ? 2023 THR B O 1 ATOM 7400 C CB . THR B 2 376 ? -32.178 -23.503 43.382 1.00 140.28 ? 2023 THR B CB 1 ATOM 7401 O OG1 . THR B 2 376 ? -32.668 -22.637 42.346 1.00 144.49 ? 2023 THR B OG1 1 ATOM 7402 C CG2 . THR B 2 376 ? -32.231 -22.780 44.726 1.00 141.54 ? 2023 THR B CG2 1 ATOM 7403 N N . PRO B 2 377 ? -29.751 -21.929 42.057 1.00 134.70 ? 2024 PRO B N 1 ATOM 7404 C CA . PRO B 2 377 ? -28.666 -20.961 42.008 1.00 133.46 ? 2024 PRO B CA 1 ATOM 7405 C C . PRO B 2 377 ? -28.885 -19.905 43.076 1.00 139.34 ? 2024 PRO B C 1 ATOM 7406 O O . PRO B 2 377 ? -29.997 -19.399 43.199 1.00 157.30 ? 2024 PRO B O 1 ATOM 7407 C CB . PRO B 2 377 ? -28.818 -20.357 40.611 1.00 140.08 ? 2024 PRO B CB 1 ATOM 7408 C CG . PRO B 2 377 ? -30.281 -20.440 40.323 1.00 134.78 ? 2024 PRO B CG 1 ATOM 7409 C CD . PRO B 2 377 ? -30.764 -21.680 41.008 1.00 134.24 ? 2024 PRO B CD 1 ATOM 7410 N N . LEU B 2 378 ? -27.854 -19.576 43.848 1.00 131.29 ? 2025 LEU B N 1 ATOM 7411 C CA . LEU B 2 378 ? -28.009 -18.556 44.895 1.00 126.70 ? 2025 LEU B CA 1 ATOM 7412 C C . LEU B 2 378 ? -28.041 -17.122 44.406 1.00 138.69 ? 2025 LEU B C 1 ATOM 7413 O O . LEU B 2 378 ? -28.245 -16.207 45.208 1.00 131.71 ? 2025 LEU B O 1 ATOM 7414 C CB . LEU B 2 378 ? -26.975 -18.742 45.969 1.00 114.55 ? 2025 LEU B CB 1 ATOM 7415 C CG . LEU B 2 378 ? -27.363 -20.113 46.478 1.00 117.25 ? 2025 LEU B CG 1 ATOM 7416 C CD1 . LEU B 2 378 ? -26.288 -20.548 47.444 1.00 132.26 ? 2025 LEU B CD1 1 ATOM 7417 C CD2 . LEU B 2 378 ? -28.761 -20.124 47.101 1.00 108.37 ? 2025 LEU B CD2 1 ATOM 7418 N N . GLY B 2 379 ? -27.847 -16.954 43.092 1.00 156.45 ? 2026 GLY B N 1 ATOM 7419 C CA . GLY B 2 379 ? -28.084 -15.705 42.370 1.00 152.03 ? 2026 GLY B CA 1 ATOM 7420 C C . GLY B 2 379 ? -26.864 -14.819 42.203 1.00 150.21 ? 2026 GLY B C 1 ATOM 7421 O O . GLY B 2 379 ? -26.977 -13.593 42.295 1.00 164.03 ? 2026 GLY B O 1 ATOM 7422 N N . MET B 2 380 ? -25.697 -15.423 41.985 1.00 127.96 ? 2027 MET B N 1 ATOM 7423 C CA . MET B 2 380 ? -24.537 -14.659 41.532 1.00 119.21 ? 2027 MET B CA 1 ATOM 7424 C C . MET B 2 380 ? -24.513 -14.626 40.022 1.00 122.36 ? 2027 MET B C 1 ATOM 7425 O O . MET B 2 380 ? -23.716 -13.923 39.387 1.00 104.51 ? 2027 MET B O 1 ATOM 7426 C CB . MET B 2 380 ? -23.262 -15.203 42.120 1.00 110.53 ? 2027 MET B CB 1 ATOM 7427 C CG . MET B 2 380 ? -22.918 -14.356 43.318 1.00 120.60 ? 2027 MET B CG 1 ATOM 7428 S SD . MET B 2 380 ? -21.634 -15.018 44.360 1.00 130.17 ? 2027 MET B SD 1 ATOM 7429 C CE . MET B 2 380 ? -20.179 -14.580 43.404 1.00 130.09 ? 2027 MET B CE 1 ATOM 7430 N N . ALA B 2 381 ? -25.443 -15.405 39.478 1.00 141.26 ? 2028 ALA B N 1 ATOM 7431 C CA . ALA B 2 381 ? -25.749 -15.472 38.062 1.00 154.88 ? 2028 ALA B CA 1 ATOM 7432 C C . ALA B 2 381 ? -26.311 -14.120 37.611 1.00 160.34 ? 2028 ALA B C 1 ATOM 7433 O O . ALA B 2 381 ? -25.609 -13.327 36.964 1.00 144.58 ? 2028 ALA B O 1 ATOM 7434 C CB . ALA B 2 381 ? -26.753 -16.607 37.802 1.00 155.54 ? 2028 ALA B CB 1 ATOM 7435 N N . SER B 2 382 ? -27.586 -13.894 37.942 1.00 170.65 ? 2029 SER B N 1 ATOM 7436 C CA . SER B 2 382 ? -28.212 -12.588 37.887 1.00 163.57 ? 2029 SER B CA 1 ATOM 7437 C C . SER B 2 382 ? -27.682 -11.867 39.107 1.00 168.05 ? 2029 SER B C 1 ATOM 7438 O O . SER B 2 382 ? -27.282 -12.496 40.086 1.00 154.59 ? 2029 SER B O 1 ATOM 7439 C CB . SER B 2 382 ? -29.721 -12.725 38.021 1.00 166.15 ? 2029 SER B CB 1 ATOM 7440 O OG . SER B 2 382 ? -30.069 -13.147 39.339 1.00 179.40 ? 2029 SER B OG 1 ATOM 7441 N N . GLY B 2 383 ? -27.685 -10.545 39.062 1.00 192.91 ? 2030 GLY B N 1 ATOM 7442 C CA . GLY B 2 383 ? -27.209 -9.764 40.193 1.00 216.39 ? 2030 GLY B CA 1 ATOM 7443 C C . GLY B 2 383 ? -28.138 -9.825 41.393 1.00 223.51 ? 2030 GLY B C 1 ATOM 7444 O O . GLY B 2 383 ? -28.258 -8.838 42.126 1.00 253.05 ? 2030 GLY B O 1 ATOM 7445 N N . HIS B 2 384 ? -28.794 -10.971 41.599 1.00 198.33 ? 2031 HIS B N 1 ATOM 7446 C CA . HIS B 2 384 ? -29.700 -11.120 42.729 1.00 177.13 ? 2031 HIS B CA 1 ATOM 7447 C C . HIS B 2 384 ? -28.930 -11.108 44.064 1.00 170.82 ? 2031 HIS B C 1 ATOM 7448 O O . HIS B 2 384 ? -29.484 -10.749 45.113 1.00 183.21 ? 2031 HIS B O 1 ATOM 7449 C CB . HIS B 2 384 ? -30.606 -12.342 42.590 1.00 168.76 ? 2031 HIS B CB 1 ATOM 7450 C CG . HIS B 2 384 ? -31.457 -12.574 43.797 1.00 178.09 ? 2031 HIS B CG 1 ATOM 7451 N ND1 . HIS B 2 384 ? -31.053 -13.364 44.853 1.00 182.87 ? 2031 HIS B ND1 1 ATOM 7452 C CD2 . HIS B 2 384 ? -32.659 -12.065 44.150 1.00 179.59 ? 2031 HIS B CD2 1 ATOM 7453 C CE1 . HIS B 2 384 ? -31.982 -13.357 45.792 1.00 170.23 ? 2031 HIS B CE1 1 ATOM 7454 N NE2 . HIS B 2 384 ? -32.966 -12.575 45.390 1.00 174.47 ? 2031 HIS B NE2 1 ATOM 7455 N N . ILE B 2 385 ? -27.656 -11.489 44.018 1.00 150.89 ? 2032 ILE B N 1 ATOM 7456 C CA . ILE B 2 385 ? -26.729 -11.182 45.102 1.00 149.11 ? 2032 ILE B CA 1 ATOM 7457 C C . ILE B 2 385 ? -26.134 -9.813 44.748 1.00 161.03 ? 2032 ILE B C 1 ATOM 7458 O O . ILE B 2 385 ? -25.236 -9.745 43.915 1.00 167.31 ? 2032 ILE B O 1 ATOM 7459 C CB . ILE B 2 385 ? -25.619 -12.250 45.204 1.00 137.27 ? 2032 ILE B CB 1 ATOM 7460 C CG1 . ILE B 2 385 ? -26.211 -13.599 45.570 1.00 133.41 ? 2032 ILE B CG1 1 ATOM 7461 C CG2 . ILE B 2 385 ? -24.582 -11.881 46.249 1.00 139.01 ? 2032 ILE B CG2 1 ATOM 7462 C CD1 . ILE B 2 385 ? -25.182 -14.700 45.673 1.00 137.78 ? 2032 ILE B CD1 1 ATOM 7463 N N . ARG B 2 386 ? -26.638 -8.730 45.350 1.00 175.76 ? 2033 ARG B N 1 ATOM 7464 C CA . ARG B 2 386 ? -26.260 -7.362 44.920 1.00 193.72 ? 2033 ARG B CA 1 ATOM 7465 C C . ARG B 2 386 ? -24.777 -7.048 45.049 1.00 198.60 ? 2033 ARG B C 1 ATOM 7466 O O . ARG B 2 386 ? -24.057 -7.719 45.793 1.00 180.57 ? 2033 ARG B O 1 ATOM 7467 C CB . ARG B 2 386 ? -27.100 -6.277 45.602 1.00 206.20 ? 2033 ARG B CB 1 ATOM 7468 C CG . ARG B 2 386 ? -28.174 -5.693 44.700 1.00 214.08 ? 2033 ARG B CG 1 ATOM 7469 C CD . ARG B 2 386 ? -29.329 -5.178 45.536 1.00 222.38 ? 2033 ARG B CD 1 ATOM 7470 N NE . ARG B 2 386 ? -30.627 -5.732 45.132 1.00 233.68 ? 2033 ARG B NE 1 ATOM 7471 C CZ . ARG B 2 386 ? -31.103 -6.929 45.495 1.00 227.85 ? 2033 ARG B CZ 1 ATOM 7472 N NH1 . ARG B 2 386 ? -30.393 -7.750 46.267 1.00 212.12 ? 2033 ARG B NH1 1 ATOM 7473 N NH2 . ARG B 2 386 ? -32.303 -7.313 45.075 1.00 232.13 ? 2033 ARG B NH2 1 ATOM 7474 N N . ASP B 2 387 ? -24.345 -6.013 44.326 1.00 210.58 ? 2034 ASP B N 1 ATOM 7475 C CA . ASP B 2 387 ? -22.920 -5.740 44.111 1.00 203.55 ? 2034 ASP B CA 1 ATOM 7476 C C . ASP B 2 387 ? -22.035 -5.658 45.363 1.00 192.95 ? 2034 ASP B C 1 ATOM 7477 O O . ASP B 2 387 ? -20.857 -6.022 45.301 1.00 180.83 ? 2034 ASP B O 1 ATOM 7478 C CB . ASP B 2 387 ? -22.723 -4.540 43.182 1.00 218.10 ? 2034 ASP B CB 1 ATOM 7479 C CG . ASP B 2 387 ? -22.474 -4.960 41.739 1.00 222.35 ? 2034 ASP B CG 1 ATOM 7480 O OD1 . ASP B 2 387 ? -22.692 -6.140 41.399 1.00 217.65 ? 2034 ASP B OD1 1 ATOM 7481 O OD2 . ASP B 2 387 ? -22.045 -4.111 40.936 1.00 244.95 ? 2034 ASP B OD2 1 ATOM 7482 N N . PHE B 2 388 ? -22.596 -5.205 46.487 1.00 180.75 ? 2035 PHE B N 1 ATOM 7483 C CA . PHE B 2 388 ? -21.923 -5.357 47.779 1.00 168.16 ? 2035 PHE B CA 1 ATOM 7484 C C . PHE B 2 388 ? -21.971 -6.851 48.186 1.00 162.36 ? 2035 PHE B C 1 ATOM 7485 O O . PHE B 2 388 ? -22.053 -7.715 47.306 1.00 152.24 ? 2035 PHE B O 1 ATOM 7486 C CB . PHE B 2 388 ? -22.523 -4.405 48.828 1.00 165.83 ? 2035 PHE B CB 1 ATOM 7487 C CG . PHE B 2 388 ? -23.728 -4.951 49.526 1.00 166.26 ? 2035 PHE B CG 1 ATOM 7488 C CD1 . PHE B 2 388 ? -24.923 -5.137 48.844 1.00 170.69 ? 2035 PHE B CD1 1 ATOM 7489 C CD2 . PHE B 2 388 ? -23.665 -5.300 50.868 1.00 168.24 ? 2035 PHE B CD2 1 ATOM 7490 C CE1 . PHE B 2 388 ? -26.034 -5.658 49.494 1.00 171.45 ? 2035 PHE B CE1 1 ATOM 7491 C CE2 . PHE B 2 388 ? -24.769 -5.824 51.524 1.00 169.96 ? 2035 PHE B CE2 1 ATOM 7492 C CZ . PHE B 2 388 ? -25.957 -6.000 50.836 1.00 167.63 ? 2035 PHE B CZ 1 ATOM 7493 N N . GLN B 2 389 ? -21.898 -7.161 49.487 1.00 163.28 ? 2036 GLN B N 1 ATOM 7494 C CA . GLN B 2 389 ? -21.909 -8.559 50.015 1.00 158.73 ? 2036 GLN B CA 1 ATOM 7495 C C . GLN B 2 389 ? -20.916 -9.570 49.338 1.00 148.17 ? 2036 GLN B C 1 ATOM 7496 O O . GLN B 2 389 ? -21.008 -10.784 49.523 1.00 137.39 ? 2036 GLN B O 1 ATOM 7497 C CB . GLN B 2 389 ? -23.360 -9.124 50.177 1.00 160.57 ? 2036 GLN B CB 1 ATOM 7498 C CG . GLN B 2 389 ? -24.264 -9.099 48.927 1.00 164.33 ? 2036 GLN B CG 1 ATOM 7499 C CD . GLN B 2 389 ? -25.579 -9.895 49.036 1.00 157.87 ? 2036 GLN B CD 1 ATOM 7500 O OE1 . GLN B 2 389 ? -26.615 -9.478 48.512 1.00 166.03 ? 2036 GLN B OE1 1 ATOM 7501 N NE2 . GLN B 2 389 ? -25.533 -11.048 49.683 1.00 144.27 ? 2036 GLN B NE2 1 ATOM 7502 N N . ILE B 2 390 ? -19.960 -9.053 48.571 1.00 147.41 ? 2037 ILE B N 1 ATOM 7503 C CA . ILE B 2 390 ? -18.854 -9.848 48.024 1.00 143.15 ? 2037 ILE B CA 1 ATOM 7504 C C . ILE B 2 390 ? -17.536 -9.110 48.354 1.00 151.52 ? 2037 ILE B C 1 ATOM 7505 O O . ILE B 2 390 ? -17.297 -7.989 47.872 1.00 155.04 ? 2037 ILE B O 1 ATOM 7506 C CB . ILE B 2 390 ? -19.007 -10.079 46.488 1.00 141.16 ? 2037 ILE B CB 1 ATOM 7507 C CG1 . ILE B 2 390 ? -20.375 -10.693 46.142 1.00 130.53 ? 2037 ILE B CG1 1 ATOM 7508 C CG2 . ILE B 2 390 ? -17.861 -10.921 45.920 1.00 136.36 ? 2037 ILE B CG2 1 ATOM 7509 C CD1 . ILE B 2 390 ? -20.648 -10.794 44.654 1.00 123.11 ? 2037 ILE B CD1 1 ATOM 7510 N N . THR B 2 391 ? -16.696 -9.713 49.194 1.00 151.81 ? 2038 THR B N 1 ATOM 7511 C CA . THR B 2 391 ? -15.426 -9.075 49.577 1.00 159.10 ? 2038 THR B CA 1 ATOM 7512 C C . THR B 2 391 ? -14.201 -9.860 49.092 1.00 151.45 ? 2038 THR B C 1 ATOM 7513 O O . THR B 2 391 ? -14.295 -11.038 48.708 1.00 128.56 ? 2038 THR B O 1 ATOM 7514 C CB . THR B 2 391 ? -15.294 -8.831 51.110 1.00 172.95 ? 2038 THR B CB 1 ATOM 7515 O OG1 . THR B 2 391 ? -16.568 -8.963 51.768 1.00 157.98 ? 2038 THR B OG1 1 ATOM 7516 C CG2 . THR B 2 391 ? -14.656 -7.439 51.393 1.00 183.60 ? 2038 THR B CG2 1 ATOM 7517 N N . ALA B 2 392 ? -13.055 -9.182 49.118 1.00 154.98 ? 2039 ALA B N 1 ATOM 7518 C CA . ALA B 2 392 ? -11.781 -9.782 48.748 1.00 156.39 ? 2039 ALA B CA 1 ATOM 7519 C C . ALA B 2 392 ? -10.744 -9.522 49.813 1.00 152.48 ? 2039 ALA B C 1 ATOM 7520 O O . ALA B 2 392 ? -10.939 -8.670 50.668 1.00 152.66 ? 2039 ALA B O 1 ATOM 7521 C CB . ALA B 2 392 ? -11.297 -9.220 47.422 1.00 168.79 ? 2039 ALA B CB 1 ATOM 7522 N N . SER B 2 393 ? -9.643 -10.266 49.748 1.00 158.30 ? 2040 SER B N 1 ATOM 7523 C CA . SER B 2 393 ? -8.478 -10.017 50.585 1.00 176.56 ? 2040 SER B CA 1 ATOM 7524 C C . SER B 2 393 ? -7.880 -8.744 50.056 1.00 182.69 ? 2040 SER B C 1 ATOM 7525 O O . SER B 2 393 ? -7.328 -7.937 50.801 1.00 213.81 ? 2040 SER B O 1 ATOM 7526 C CB . SER B 2 393 ? -7.447 -11.145 50.459 1.00 189.23 ? 2040 SER B CB 1 ATOM 7527 O OG . SER B 2 393 ? -6.712 -11.048 49.245 1.00 188.85 ? 2040 SER B OG 1 ATOM 7528 N N . GLY B 2 394 ? -7.998 -8.592 48.745 1.00 166.71 ? 2041 GLY B N 1 ATOM 7529 C CA . GLY B 2 394 ? -7.523 -7.430 48.045 1.00 171.55 ? 2041 GLY B CA 1 ATOM 7530 C C . GLY B 2 394 ? -7.839 -7.707 46.606 1.00 170.99 ? 2041 GLY B C 1 ATOM 7531 O O . GLY B 2 394 ? -8.527 -8.685 46.280 1.00 151.15 ? 2041 GLY B O 1 ATOM 7532 N N . GLN B 2 395 ? -7.336 -6.844 45.739 1.00 187.03 ? 2042 GLN B N 1 ATOM 7533 C CA . GLN B 2 395 ? -7.512 -7.045 44.318 1.00 189.96 ? 2042 GLN B CA 1 ATOM 7534 C C . GLN B 2 395 ? -6.362 -6.441 43.534 1.00 198.54 ? 2042 GLN B C 1 ATOM 7535 O O . GLN B 2 395 ? -5.542 -5.677 44.079 1.00 204.16 ? 2042 GLN B O 1 ATOM 7536 C CB . GLN B 2 395 ? -8.845 -6.472 43.858 1.00 182.08 ? 2042 GLN B CB 1 ATOM 7537 C CG . GLN B 2 395 ? -9.062 -5.046 44.311 1.00 191.08 ? 2042 GLN B CG 1 ATOM 7538 C CD . GLN B 2 395 ? -10.443 -4.580 43.962 1.00 195.17 ? 2042 GLN B CD 1 ATOM 7539 O OE1 . GLN B 2 395 ? -10.640 -3.928 42.942 1.00 201.22 ? 2042 GLN B OE1 1 ATOM 7540 N NE2 . GLN B 2 395 ? -11.420 -4.945 44.784 1.00 193.31 ? 2042 GLN B NE2 1 ATOM 7541 N N . TYR B 2 396 ? -6.317 -6.816 42.257 1.00 189.25 ? 2043 TYR B N 1 ATOM 7542 C CA . TYR B 2 396 ? -5.367 -6.285 41.299 1.00 187.19 ? 2043 TYR B CA 1 ATOM 7543 C C . TYR B 2 396 ? -5.994 -5.150 40.470 1.00 184.83 ? 2043 TYR B C 1 ATOM 7544 O O . TYR B 2 396 ? -6.742 -5.401 39.527 1.00 167.14 ? 2043 TYR B O 1 ATOM 7545 C CB . TYR B 2 396 ? -4.840 -7.413 40.407 1.00 183.18 ? 2043 TYR B CB 1 ATOM 7546 C CG . TYR B 2 396 ? -4.056 -6.930 39.217 1.00 192.98 ? 2043 TYR B CG 1 ATOM 7547 C CD1 . TYR B 2 396 ? -2.774 -6.401 39.373 1.00 213.34 ? 2043 TYR B CD1 1 ATOM 7548 C CD2 . TYR B 2 396 ? -4.591 -6.995 37.936 1.00 190.60 ? 2043 TYR B CD2 1 ATOM 7549 C CE1 . TYR B 2 396 ? -2.044 -5.943 38.284 1.00 230.34 ? 2043 TYR B CE1 1 ATOM 7550 C CE2 . TYR B 2 396 ? -3.871 -6.543 36.841 1.00 218.30 ? 2043 TYR B CE2 1 ATOM 7551 C CZ . TYR B 2 396 ? -2.597 -6.021 37.018 1.00 232.77 ? 2043 TYR B CZ 1 ATOM 7552 O OH . TYR B 2 396 ? -1.876 -5.572 35.932 1.00 246.74 ? 2043 TYR B OH 1 ATOM 7553 N N . GLY B 2 397 ? -5.672 -3.908 40.848 1.00 201.96 ? 2044 GLY B N 1 ATOM 7554 C CA . GLY B 2 397 ? -6.158 -2.678 40.192 1.00 222.15 ? 2044 GLY B CA 1 ATOM 7555 C C . GLY B 2 397 ? -7.661 -2.552 40.309 1.00 230.91 ? 2044 GLY B C 1 ATOM 7556 O O . GLY B 2 397 ? -8.219 -2.743 41.393 1.00 245.19 ? 2044 GLY B O 1 ATOM 7557 N N . GLN B 2 398 ? -8.319 -2.206 39.203 1.00 229.48 ? 2045 GLN B N 1 ATOM 7558 C CA . GLN B 2 398 ? -9.696 -2.647 39.016 1.00 227.01 ? 2045 GLN B CA 1 ATOM 7559 C C . GLN B 2 398 ? -9.603 -4.074 38.439 1.00 206.47 ? 2045 GLN B C 1 ATOM 7560 O O . GLN B 2 398 ? -8.597 -4.421 37.827 1.00 201.94 ? 2045 GLN B O 1 ATOM 7561 C CB . GLN B 2 398 ? -10.500 -1.703 38.119 1.00 227.87 ? 2045 GLN B CB 1 ATOM 7562 C CG . GLN B 2 398 ? -11.998 -1.859 38.350 1.00 236.84 ? 2045 GLN B CG 1 ATOM 7563 C CD . GLN B 2 398 ? -12.790 -1.992 37.065 1.00 236.92 ? 2045 GLN B CD 1 ATOM 7564 O OE1 . GLN B 2 398 ? -12.905 -1.033 36.306 1.00 244.12 ? 2045 GLN B OE1 1 ATOM 7565 N NE2 . GLN B 2 398 ? -13.350 -3.181 36.818 1.00 216.51 ? 2045 GLN B NE2 1 ATOM 7566 N N . TRP B 2 399 ? -10.628 -4.896 38.640 1.00 184.14 ? 2046 TRP B N 1 ATOM 7567 C CA . TRP B 2 399 ? -10.537 -6.338 38.409 1.00 171.68 ? 2046 TRP B CA 1 ATOM 7568 C C . TRP B 2 399 ? -10.976 -6.893 39.745 1.00 159.22 ? 2046 TRP B C 1 ATOM 7569 O O . TRP B 2 399 ? -10.399 -7.829 40.303 1.00 142.22 ? 2046 TRP B O 1 ATOM 7570 C CB . TRP B 2 399 ? -9.098 -6.779 38.053 1.00 182.31 ? 2046 TRP B CB 1 ATOM 7571 C CG . TRP B 2 399 ? -8.978 -7.719 36.851 1.00 186.53 ? 2046 TRP B CG 1 ATOM 7572 C CD1 . TRP B 2 399 ? -8.314 -8.923 36.794 1.00 189.55 ? 2046 TRP B CD1 1 ATOM 7573 C CD2 . TRP B 2 399 ? -9.543 -7.523 35.556 1.00 180.79 ? 2046 TRP B CD2 1 ATOM 7574 N NE1 . TRP B 2 399 ? -8.440 -9.487 35.544 1.00 173.10 ? 2046 TRP B NE1 1 ATOM 7575 C CE2 . TRP B 2 399 ? -9.190 -8.649 34.767 1.00 177.09 ? 2046 TRP B CE2 1 ATOM 7576 C CE3 . TRP B 2 399 ? -10.329 -6.512 34.987 1.00 177.01 ? 2046 TRP B CE3 1 ATOM 7577 C CZ2 . TRP B 2 399 ? -9.587 -8.783 33.453 1.00 184.65 ? 2046 TRP B CZ2 1 ATOM 7578 C CZ3 . TRP B 2 399 ? -10.716 -6.640 33.685 1.00 181.73 ? 2046 TRP B CZ3 1 ATOM 7579 C CH2 . TRP B 2 399 ? -10.341 -7.767 32.924 1.00 195.31 ? 2046 TRP B CH2 1 ATOM 7580 N N . ALA B 2 400 ? -12.016 -6.256 40.254 1.00 165.85 ? 2047 ALA B N 1 ATOM 7581 C CA . ALA B 2 400 ? -12.511 -6.493 41.591 1.00 184.47 ? 2047 ALA B CA 1 ATOM 7582 C C . ALA B 2 400 ? -13.404 -7.741 41.687 1.00 178.79 ? 2047 ALA B C 1 ATOM 7583 O O . ALA B 2 400 ? -13.848 -8.280 40.655 1.00 165.55 ? 2047 ALA B O 1 ATOM 7584 C CB . ALA B 2 400 ? -13.274 -5.259 42.074 1.00 197.68 ? 2047 ALA B CB 1 ATOM 7585 N N . PRO B 2 401 ? -13.644 -8.213 42.935 1.00 167.77 ? 2048 PRO B N 1 ATOM 7586 C CA . PRO B 2 401 ? -14.814 -9.024 43.214 1.00 148.79 ? 2048 PRO B CA 1 ATOM 7587 C C . PRO B 2 401 ? -15.997 -8.076 43.220 1.00 147.78 ? 2048 PRO B C 1 ATOM 7588 O O . PRO B 2 401 ? -15.847 -6.866 43.495 1.00 143.43 ? 2048 PRO B O 1 ATOM 7589 C CB . PRO B 2 401 ? -14.549 -9.544 44.613 1.00 148.03 ? 2048 PRO B CB 1 ATOM 7590 C CG . PRO B 2 401 ? -13.739 -8.467 45.245 1.00 156.07 ? 2048 PRO B CG 1 ATOM 7591 C CD . PRO B 2 401 ? -12.839 -7.982 44.153 1.00 161.89 ? 2048 PRO B CD 1 ATOM 7592 N N . LYS B 2 402 ? -17.166 -8.631 42.948 1.00 143.57 ? 2049 LYS B N 1 ATOM 7593 C CA . LYS B 2 402 ? -18.265 -7.867 42.387 1.00 153.38 ? 2049 LYS B CA 1 ATOM 7594 C C . LYS B 2 402 ? -18.266 -8.321 40.950 1.00 152.49 ? 2049 LYS B C 1 ATOM 7595 O O . LYS B 2 402 ? -19.158 -9.059 40.556 1.00 149.40 ? 2049 LYS B O 1 ATOM 7596 C CB . LYS B 2 402 ? -18.061 -6.340 42.457 1.00 152.44 ? 2049 LYS B CB 1 ATOM 7597 C CG . LYS B 2 402 ? -19.068 -5.573 41.616 1.00 149.59 ? 2049 LYS B CG 1 ATOM 7598 C CD . LYS B 2 402 ? -18.555 -4.211 41.214 1.00 157.47 ? 2049 LYS B CD 1 ATOM 7599 C CE . LYS B 2 402 ? -19.268 -3.728 39.958 1.00 167.95 ? 2049 LYS B CE 1 ATOM 7600 N NZ . LYS B 2 402 ? -19.230 -2.240 39.791 1.00 180.24 ? 2049 LYS B NZ 1 ATOM 7601 N N . LEU B 2 403 ? -17.246 -7.912 40.185 1.00 155.33 ? 2050 LEU B N 1 ATOM 7602 C CA . LEU B 2 403 ? -17.022 -8.423 38.827 1.00 160.01 ? 2050 LEU B CA 1 ATOM 7603 C C . LEU B 2 403 ? -16.832 -9.959 38.842 1.00 166.26 ? 2050 LEU B C 1 ATOM 7604 O O . LEU B 2 403 ? -16.640 -10.579 37.781 1.00 162.37 ? 2050 LEU B O 1 ATOM 7605 C CB . LEU B 2 403 ? -15.821 -7.729 38.151 1.00 160.02 ? 2050 LEU B CB 1 ATOM 7606 C CG . LEU B 2 403 ? -15.765 -6.238 37.736 1.00 172.20 ? 2050 LEU B CG 1 ATOM 7607 C CD1 . LEU B 2 403 ? -14.392 -5.895 37.158 1.00 173.33 ? 2050 LEU B CD1 1 ATOM 7608 C CD2 . LEU B 2 403 ? -16.849 -5.786 36.758 1.00 173.39 ? 2050 LEU B CD2 1 ATOM 7609 N N . ALA B 2 404 ? -16.935 -10.545 40.049 1.00 166.59 ? 2051 ALA B N 1 ATOM 7610 C CA . ALA B 2 404 ? -16.698 -11.978 40.341 1.00 149.30 ? 2051 ALA B CA 1 ATOM 7611 C C . ALA B 2 404 ? -17.848 -12.964 39.992 1.00 132.36 ? 2051 ALA B C 1 ATOM 7612 O O . ALA B 2 404 ? -17.723 -14.167 40.206 1.00 118.08 ? 2051 ALA B O 1 ATOM 7613 C CB . ALA B 2 404 ? -16.272 -12.141 41.805 1.00 141.97 ? 2051 ALA B CB 1 ATOM 7614 N N . ARG B 2 405 ? -18.952 -12.459 39.445 1.00 132.95 ? 2052 ARG B N 1 ATOM 7615 C CA . ARG B 2 405 ? -20.129 -13.291 39.134 1.00 132.40 ? 2052 ARG B CA 1 ATOM 7616 C C . ARG B 2 405 ? -19.826 -14.204 37.979 1.00 128.47 ? 2052 ARG B C 1 ATOM 7617 O O . ARG B 2 405 ? -19.070 -13.846 37.084 1.00 125.53 ? 2052 ARG B O 1 ATOM 7618 C CB . ARG B 2 405 ? -21.374 -12.454 38.769 1.00 146.12 ? 2052 ARG B CB 1 ATOM 7619 C CG . ARG B 2 405 ? -21.247 -10.946 38.995 1.00 164.60 ? 2052 ARG B CG 1 ATOM 7620 C CD . ARG B 2 405 ? -22.567 -10.176 39.093 1.00 152.26 ? 2052 ARG B CD 1 ATOM 7621 N NE . ARG B 2 405 ? -22.564 -9.487 40.372 1.00 140.60 ? 2052 ARG B NE 1 ATOM 7622 C CZ . ARG B 2 405 ? -22.950 -10.053 41.511 1.00 135.71 ? 2052 ARG B CZ 1 ATOM 7623 N NH1 . ARG B 2 405 ? -23.424 -11.297 41.514 1.00 127.73 ? 2052 ARG B NH1 1 ATOM 7624 N NH2 . ARG B 2 405 ? -22.881 -9.369 42.645 1.00 141.29 ? 2052 ARG B NH2 1 ATOM 7625 N N . LEU B 2 406 ? -20.441 -15.379 37.996 1.00 140.97 ? 2053 LEU B N 1 ATOM 7626 C CA . LEU B 2 406 ? -20.268 -16.348 36.926 1.00 142.71 ? 2053 LEU B CA 1 ATOM 7627 C C . LEU B 2 406 ? -20.813 -15.791 35.632 1.00 144.80 ? 2053 LEU B C 1 ATOM 7628 O O . LEU B 2 406 ? -21.891 -15.194 35.604 1.00 139.01 ? 2053 LEU B O 1 ATOM 7629 C CB . LEU B 2 406 ? -20.944 -17.684 37.248 1.00 134.51 ? 2053 LEU B CB 1 ATOM 7630 C CG . LEU B 2 406 ? -20.187 -18.873 36.656 1.00 130.23 ? 2053 LEU B CG 1 ATOM 7631 C CD1 . LEU B 2 406 ? -20.290 -20.091 37.558 1.00 125.50 ? 2053 LEU B CD1 1 ATOM 7632 C CD2 . LEU B 2 406 ? -20.644 -19.183 35.240 1.00 125.38 ? 2053 LEU B CD2 1 ATOM 7633 N N . HIS B 2 407 ? -20.020 -15.983 34.582 1.00 153.27 ? 2054 HIS B N 1 ATOM 7634 C CA . HIS B 2 407 ? -20.338 -15.606 33.206 1.00 157.21 ? 2054 HIS B CA 1 ATOM 7635 C C . HIS B 2 407 ? -20.206 -14.155 32.827 1.00 153.70 ? 2054 HIS B C 1 ATOM 7636 O O . HIS B 2 407 ? -20.522 -13.804 31.687 1.00 153.49 ? 2054 HIS B O 1 ATOM 7637 C CB . HIS B 2 407 ? -21.708 -16.114 32.792 1.00 162.38 ? 2054 HIS B CB 1 ATOM 7638 C CG . HIS B 2 407 ? -21.679 -17.526 32.344 1.00 165.07 ? 2054 HIS B CG 1 ATOM 7639 N ND1 . HIS B 2 407 ? -22.410 -18.514 32.962 1.00 155.73 ? 2054 HIS B ND1 1 ATOM 7640 C CD2 . HIS B 2 407 ? -20.963 -18.129 31.368 1.00 171.75 ? 2054 HIS B CD2 1 ATOM 7641 C CE1 . HIS B 2 407 ? -22.165 -19.666 32.368 1.00 165.16 ? 2054 HIS B CE1 1 ATOM 7642 N NE2 . HIS B 2 407 ? -21.291 -19.460 31.398 1.00 185.21 ? 2054 HIS B NE2 1 ATOM 7643 N N . TYR B 2 408 ? -19.740 -13.315 33.751 1.00 147.83 ? 2055 TYR B N 1 ATOM 7644 C CA . TYR B 2 408 ? -19.590 -11.904 33.435 1.00 153.98 ? 2055 TYR B CA 1 ATOM 7645 C C . TYR B 2 408 ? -18.788 -11.755 32.131 1.00 175.21 ? 2055 TYR B C 1 ATOM 7646 O O . TYR B 2 408 ? -17.713 -12.346 31.974 1.00 186.67 ? 2055 TYR B O 1 ATOM 7647 C CB . TYR B 2 408 ? -18.999 -11.103 34.600 1.00 138.55 ? 2055 TYR B CB 1 ATOM 7648 C CG . TYR B 2 408 ? -19.532 -9.704 34.613 1.00 141.38 ? 2055 TYR B CG 1 ATOM 7649 C CD1 . TYR B 2 408 ? -20.904 -9.476 34.637 1.00 154.81 ? 2055 TYR B CD1 1 ATOM 7650 C CD2 . TYR B 2 408 ? -18.681 -8.606 34.568 1.00 156.58 ? 2055 TYR B CD2 1 ATOM 7651 C CE1 . TYR B 2 408 ? -21.428 -8.193 34.638 1.00 189.41 ? 2055 TYR B CE1 1 ATOM 7652 C CE2 . TYR B 2 408 ? -19.189 -7.307 34.556 1.00 188.14 ? 2055 TYR B CE2 1 ATOM 7653 C CZ . TYR B 2 408 ? -20.567 -7.106 34.597 1.00 200.98 ? 2055 TYR B CZ 1 ATOM 7654 O OH . TYR B 2 408 ? -21.104 -5.833 34.599 1.00 200.96 ? 2055 TYR B OH 1 ATOM 7655 N N . SER B 2 409 ? -19.357 -11.016 31.180 1.00 181.17 ? 2056 SER B N 1 ATOM 7656 C CA . SER B 2 409 ? -18.787 -10.883 29.841 1.00 180.10 ? 2056 SER B CA 1 ATOM 7657 C C . SER B 2 409 ? -17.966 -9.614 29.729 1.00 188.38 ? 2056 SER B C 1 ATOM 7658 O O . SER B 2 409 ? -17.749 -8.917 30.717 1.00 196.37 ? 2056 SER B O 1 ATOM 7659 C CB . SER B 2 409 ? -19.900 -10.857 28.810 1.00 187.16 ? 2056 SER B CB 1 ATOM 7660 O OG . SER B 2 409 ? -20.886 -9.929 29.217 1.00 201.82 ? 2056 SER B OG 1 ATOM 7661 N N . GLY B 2 410 ? -17.530 -9.300 28.516 1.00 204.02 ? 2057 GLY B N 1 ATOM 7662 C CA . GLY B 2 410 ? -16.465 -8.324 28.327 1.00 222.80 ? 2057 GLY B CA 1 ATOM 7663 C C . GLY B 2 410 ? -15.168 -8.992 28.755 1.00 231.78 ? 2057 GLY B C 1 ATOM 7664 O O . GLY B 2 410 ? -15.185 -10.051 29.399 1.00 243.87 ? 2057 GLY B O 1 ATOM 7665 N N . SER B 2 411 ? -14.035 -8.410 28.383 1.00 225.02 ? 2058 SER B N 1 ATOM 7666 C CA . SER B 2 411 ? -12.786 -8.914 28.911 1.00 216.79 ? 2058 SER B CA 1 ATOM 7667 C C . SER B 2 411 ? -12.475 -8.103 30.157 1.00 220.11 ? 2058 SER B C 1 ATOM 7668 O O . SER B 2 411 ? -11.627 -8.504 30.942 1.00 239.01 ? 2058 SER B O 1 ATOM 7669 C CB . SER B 2 411 ? -11.654 -8.863 27.892 1.00 213.54 ? 2058 SER B CB 1 ATOM 7670 O OG . SER B 2 411 ? -10.712 -7.875 28.246 1.00 225.04 ? 2058 SER B OG 1 ATOM 7671 N N . ILE B 2 412 ? -13.171 -6.972 30.328 1.00 211.65 ? 2059 ILE B N 1 ATOM 7672 C CA . ILE B 2 412 ? -13.266 -6.297 31.638 1.00 216.89 ? 2059 ILE B CA 1 ATOM 7673 C C . ILE B 2 412 ? -14.194 -7.071 32.616 1.00 217.53 ? 2059 ILE B C 1 ATOM 7674 O O . ILE B 2 412 ? -15.354 -6.690 32.837 1.00 225.34 ? 2059 ILE B O 1 ATOM 7675 C CB . ILE B 2 412 ? -13.604 -4.767 31.507 1.00 216.75 ? 2059 ILE B CB 1 ATOM 7676 C CG1 . ILE B 2 412 ? -13.877 -4.101 32.900 1.00 210.11 ? 2059 ILE B CG1 1 ATOM 7677 C CG2 . ILE B 2 412 ? -14.609 -4.485 30.370 1.00 209.03 ? 2059 ILE B CG2 1 ATOM 7678 C CD1 . ILE B 2 412 ? -15.274 -4.184 33.516 1.00 188.68 ? 2059 ILE B CD1 1 ATOM 7679 N N . ASN B 2 413 ? -13.675 -8.165 33.190 1.00 203.87 ? 2060 ASN B N 1 ATOM 7680 C CA . ASN B 2 413 ? -14.492 -9.089 34.006 1.00 186.57 ? 2060 ASN B CA 1 ATOM 7681 C C . ASN B 2 413 ? -13.748 -10.013 35.002 1.00 176.11 ? 2060 ASN B C 1 ATOM 7682 O O . ASN B 2 413 ? -12.565 -10.352 34.796 1.00 169.52 ? 2060 ASN B O 1 ATOM 7683 C CB . ASN B 2 413 ? -15.376 -9.942 33.097 1.00 186.78 ? 2060 ASN B CB 1 ATOM 7684 C CG . ASN B 2 413 ? -14.916 -11.380 33.024 1.00 190.50 ? 2060 ASN B CG 1 ATOM 7685 O OD1 . ASN B 2 413 ? -15.336 -12.209 33.834 1.00 179.34 ? 2060 ASN B OD1 1 ATOM 7686 N ND2 . ASN B 2 413 ? -14.047 -11.686 32.056 1.00 203.56 ? 2060 ASN B ND2 1 ATOM 7687 N N . ALA B 2 414 ? -14.489 -10.418 36.050 1.00 158.81 ? 2061 ALA B N 1 ATOM 7688 C CA . ALA B 2 414 ? -14.057 -11.312 37.157 1.00 144.72 ? 2061 ALA B CA 1 ATOM 7689 C C . ALA B 2 414 ? -12.971 -10.823 38.130 1.00 145.41 ? 2061 ALA B C 1 ATOM 7690 O O . ALA B 2 414 ? -12.027 -10.142 37.745 1.00 151.16 ? 2061 ALA B O 1 ATOM 7691 C CB . ALA B 2 414 ? -13.719 -12.702 36.644 1.00 142.04 ? 2061 ALA B CB 1 ATOM 7692 N N . TRP B 2 415 ? -13.117 -11.195 39.397 1.00 142.26 ? 2062 TRP B N 1 ATOM 7693 C CA . TRP B 2 415 ? -12.109 -10.918 40.419 1.00 140.60 ? 2062 TRP B CA 1 ATOM 7694 C C . TRP B 2 415 ? -10.702 -11.467 40.041 1.00 133.97 ? 2062 TRP B C 1 ATOM 7695 O O . TRP B 2 415 ? -10.608 -12.437 39.294 1.00 134.70 ? 2062 TRP B O 1 ATOM 7696 C CB . TRP B 2 415 ? -12.600 -11.469 41.776 1.00 135.81 ? 2062 TRP B CB 1 ATOM 7697 C CG . TRP B 2 415 ? -11.583 -11.304 42.857 1.00 146.39 ? 2062 TRP B CG 1 ATOM 7698 C CD1 . TRP B 2 415 ? -10.915 -10.147 43.203 1.00 156.98 ? 2062 TRP B CD1 1 ATOM 7699 C CD2 . TRP B 2 415 ? -11.080 -12.321 43.716 1.00 138.53 ? 2062 TRP B CD2 1 ATOM 7700 N NE1 . TRP B 2 415 ? -10.040 -10.388 44.234 1.00 150.12 ? 2062 TRP B NE1 1 ATOM 7701 C CE2 . TRP B 2 415 ? -10.114 -11.715 44.566 1.00 141.48 ? 2062 TRP B CE2 1 ATOM 7702 C CE3 . TRP B 2 415 ? -11.359 -13.678 43.869 1.00 128.22 ? 2062 TRP B CE3 1 ATOM 7703 C CZ2 . TRP B 2 415 ? -9.425 -12.427 45.541 1.00 132.92 ? 2062 TRP B CZ2 1 ATOM 7704 C CZ3 . TRP B 2 415 ? -10.676 -14.378 44.840 1.00 132.45 ? 2062 TRP B CZ3 1 ATOM 7705 C CH2 . TRP B 2 415 ? -9.719 -13.750 45.668 1.00 130.26 ? 2062 TRP B CH2 1 ATOM 7706 N N . SER B 2 416 ? -9.629 -10.823 40.518 1.00 129.61 ? 2063 SER B N 1 ATOM 7707 C CA . SER B 2 416 ? -8.252 -11.373 40.439 1.00 132.30 ? 2063 SER B CA 1 ATOM 7708 C C . SER B 2 416 ? -7.183 -10.572 41.220 1.00 143.60 ? 2063 SER B C 1 ATOM 7709 O O . SER B 2 416 ? -7.157 -9.338 41.156 1.00 147.93 ? 2063 SER B O 1 ATOM 7710 C CB . SER B 2 416 ? -7.804 -11.530 38.978 1.00 133.63 ? 2063 SER B CB 1 ATOM 7711 O OG . SER B 2 416 ? -6.598 -12.275 38.855 1.00 130.33 ? 2063 SER B OG 1 ATOM 7712 N N . THR B 2 417 ? -6.313 -11.277 41.953 1.00 147.63 ? 2064 THR B N 1 ATOM 7713 C CA . THR B 2 417 ? -5.139 -10.660 42.592 1.00 157.67 ? 2064 THR B CA 1 ATOM 7714 C C . THR B 2 417 ? -3.930 -11.433 42.214 1.00 169.05 ? 2064 THR B C 1 ATOM 7715 O O . THR B 2 417 ? -3.993 -12.658 42.098 1.00 174.74 ? 2064 THR B O 1 ATOM 7716 C CB . THR B 2 417 ? -5.099 -10.833 44.109 1.00 159.10 ? 2064 THR B CB 1 ATOM 7717 O OG1 . THR B 2 417 ? -6.308 -11.443 44.578 1.00 168.16 ? 2064 THR B OG1 1 ATOM 7718 C CG2 . THR B 2 417 ? -4.827 -9.507 44.773 1.00 165.90 ? 2064 THR B CG2 1 ATOM 7719 N N . LYS B 2 418 ? -2.807 -10.748 42.069 1.00 183.40 ? 2065 LYS B N 1 ATOM 7720 C CA . LYS B 2 418 ? -1.570 -11.495 42.003 1.00 199.05 ? 2065 LYS B CA 1 ATOM 7721 C C . LYS B 2 418 ? -0.950 -11.537 43.389 1.00 206.42 ? 2065 LYS B C 1 ATOM 7722 O O . LYS B 2 418 ? 0.118 -12.122 43.565 1.00 223.81 ? 2065 LYS B O 1 ATOM 7723 C CB . LYS B 2 418 ? -0.602 -10.997 40.917 1.00 206.76 ? 2065 LYS B CB 1 ATOM 7724 C CG . LYS B 2 418 ? -0.100 -9.571 41.075 1.00 219.05 ? 2065 LYS B CG 1 ATOM 7725 C CD . LYS B 2 418 ? 1.158 -9.317 40.247 1.00 222.19 ? 2065 LYS B CD 1 ATOM 7726 C CE . LYS B 2 418 ? 0.892 -9.385 38.751 1.00 221.51 ? 2065 LYS B CE 1 ATOM 7727 N NZ . LYS B 2 418 ? 1.853 -8.530 38.003 1.00 231.67 ? 2065 LYS B NZ 1 ATOM 7728 N N . GLU B 2 419 ? -1.633 -10.947 44.373 1.00 200.24 ? 2066 GLU B N 1 ATOM 7729 C CA . GLU B 2 419 ? -1.187 -11.066 45.759 1.00 209.13 ? 2066 GLU B CA 1 ATOM 7730 C C . GLU B 2 419 ? -1.205 -12.551 46.182 1.00 206.55 ? 2066 GLU B C 1 ATOM 7731 O O . GLU B 2 419 ? -2.098 -13.302 45.760 1.00 194.42 ? 2066 GLU B O 1 ATOM 7732 C CB . GLU B 2 419 ? -2.004 -10.173 46.698 1.00 218.50 ? 2066 GLU B CB 1 ATOM 7733 C CG . GLU B 2 419 ? -3.242 -10.833 47.286 1.00 220.04 ? 2066 GLU B CG 1 ATOM 7734 C CD . GLU B 2 419 ? -3.720 -10.160 48.555 1.00 231.10 ? 2066 GLU B CD 1 ATOM 7735 O OE1 . GLU B 2 419 ? -3.562 -8.919 48.670 1.00 246.37 ? 2066 GLU B OE1 1 ATOM 7736 O OE2 . GLU B 2 419 ? -4.244 -10.882 49.436 1.00 213.32 ? 2066 GLU B OE2 1 ATOM 7737 N N . PRO B 2 420 ? -0.202 -12.977 46.992 1.00 212.12 ? 2067 PRO B N 1 ATOM 7738 C CA . PRO B 2 420 ? 0.102 -14.397 47.274 1.00 200.09 ? 2067 PRO B CA 1 ATOM 7739 C C . PRO B 2 420 ? -1.086 -15.269 47.716 1.00 178.52 ? 2067 PRO B C 1 ATOM 7740 O O . PRO B 2 420 ? -1.637 -15.994 46.872 1.00 156.52 ? 2067 PRO B O 1 ATOM 7741 C CB . PRO B 2 420 ? 1.184 -14.312 48.361 1.00 214.82 ? 2067 PRO B CB 1 ATOM 7742 C CG . PRO B 2 420 ? 1.857 -13.003 48.110 1.00 226.01 ? 2067 PRO B CG 1 ATOM 7743 C CD . PRO B 2 420 ? 0.746 -12.080 47.689 1.00 224.24 ? 2067 PRO B CD 1 ATOM 7744 N N . PHE B 2 421 ? -1.451 -15.197 49.008 1.00 174.16 ? 2068 PHE B N 1 ATOM 7745 C CA . PHE B 2 421 ? -2.615 -15.914 49.589 1.00 169.58 ? 2068 PHE B CA 1 ATOM 7746 C C . PHE B 2 421 ? -3.852 -15.021 49.775 1.00 165.50 ? 2068 PHE B C 1 ATOM 7747 O O . PHE B 2 421 ? -4.057 -14.389 50.811 1.00 163.14 ? 2068 PHE B O 1 ATOM 7748 C CB . PHE B 2 421 ? -2.274 -16.611 50.919 1.00 168.03 ? 2068 PHE B CB 1 ATOM 7749 C CG . PHE B 2 421 ? -0.892 -17.187 50.971 1.00 182.80 ? 2068 PHE B CG 1 ATOM 7750 C CD1 . PHE B 2 421 ? -0.445 -18.068 49.990 1.00 188.40 ? 2068 PHE B CD1 1 ATOM 7751 C CD2 . PHE B 2 421 ? -0.032 -16.858 52.015 1.00 199.88 ? 2068 PHE B CD2 1 ATOM 7752 C CE1 . PHE B 2 421 ? 0.839 -18.594 50.043 1.00 208.12 ? 2068 PHE B CE1 1 ATOM 7753 C CE2 . PHE B 2 421 ? 1.255 -17.385 52.080 1.00 213.17 ? 2068 PHE B CE2 1 ATOM 7754 C CZ . PHE B 2 421 ? 1.691 -18.254 51.091 1.00 216.89 ? 2068 PHE B CZ 1 ATOM 7755 N N . SER B 2 422 ? -4.682 -14.982 48.750 1.00 165.05 ? 2069 SER B N 1 ATOM 7756 C CA . SER B 2 422 ? -5.877 -14.177 48.781 1.00 160.07 ? 2069 SER B CA 1 ATOM 7757 C C . SER B 2 422 ? -7.061 -14.986 49.307 1.00 150.85 ? 2069 SER B C 1 ATOM 7758 O O . SER B 2 422 ? -6.899 -16.127 49.779 1.00 148.86 ? 2069 SER B O 1 ATOM 7759 C CB . SER B 2 422 ? -6.168 -13.636 47.376 1.00 171.80 ? 2069 SER B CB 1 ATOM 7760 O OG . SER B 2 422 ? -6.126 -14.668 46.399 1.00 177.45 ? 2069 SER B OG 1 ATOM 7761 N N . TRP B 2 423 ? -8.239 -14.363 49.225 1.00 138.12 ? 2070 TRP B N 1 ATOM 7762 C CA . TRP B 2 423 ? -9.526 -14.951 49.577 1.00 122.59 ? 2070 TRP B CA 1 ATOM 7763 C C . TRP B 2 423 ? -10.687 -14.089 49.069 1.00 115.84 ? 2070 TRP B C 1 ATOM 7764 O O . TRP B 2 423 ? -10.510 -12.934 48.743 1.00 123.75 ? 2070 TRP B O 1 ATOM 7765 C CB . TRP B 2 423 ? -9.628 -15.174 51.091 1.00 129.38 ? 2070 TRP B CB 1 ATOM 7766 C CG . TRP B 2 423 ? -9.564 -13.942 51.971 1.00 140.54 ? 2070 TRP B CG 1 ATOM 7767 C CD1 . TRP B 2 423 ? -8.503 -13.531 52.756 1.00 150.67 ? 2070 TRP B CD1 1 ATOM 7768 C CD2 . TRP B 2 423 ? -10.618 -12.996 52.200 1.00 144.66 ? 2070 TRP B CD2 1 ATOM 7769 N NE1 . TRP B 2 423 ? -8.832 -12.376 53.437 1.00 158.00 ? 2070 TRP B NE1 1 ATOM 7770 C CE2 . TRP B 2 423 ? -10.124 -12.030 53.115 1.00 159.47 ? 2070 TRP B CE2 1 ATOM 7771 C CE3 . TRP B 2 423 ? -11.930 -12.863 51.715 1.00 134.40 ? 2070 TRP B CE3 1 ATOM 7772 C CZ2 . TRP B 2 423 ? -10.906 -10.945 53.550 1.00 165.67 ? 2070 TRP B CZ2 1 ATOM 7773 C CZ3 . TRP B 2 423 ? -12.698 -11.788 52.141 1.00 137.97 ? 2070 TRP B CZ3 1 ATOM 7774 C CH2 . TRP B 2 423 ? -12.187 -10.844 53.053 1.00 151.74 ? 2070 TRP B CH2 1 ATOM 7775 N N . ILE B 2 424 ? -11.877 -14.658 48.997 1.00 111.45 ? 2071 ILE B N 1 ATOM 7776 C CA . ILE B 2 424 ? -13.068 -13.909 48.622 1.00 106.33 ? 2071 ILE B CA 1 ATOM 7777 C C . ILE B 2 424 ? -14.254 -14.436 49.451 1.00 108.80 ? 2071 ILE B C 1 ATOM 7778 O O . ILE B 2 424 ? -14.332 -15.626 49.769 1.00 105.66 ? 2071 ILE B O 1 ATOM 7779 C CB . ILE B 2 424 ? -13.295 -13.954 47.096 1.00 99.60 ? 2071 ILE B CB 1 ATOM 7780 C CG1 . ILE B 2 424 ? -14.431 -13.041 46.689 1.00 104.32 ? 2071 ILE B CG1 1 ATOM 7781 C CG2 . ILE B 2 424 ? -13.555 -15.367 46.597 1.00 91.49 ? 2071 ILE B CG2 1 ATOM 7782 C CD1 . ILE B 2 424 ? -14.703 -13.098 45.200 1.00 124.36 ? 2071 ILE B CD1 1 ATOM 7783 N N . LYS B 2 425 ? -15.157 -13.549 49.839 1.00 112.47 ? 2072 LYS B N 1 ATOM 7784 C CA . LYS B 2 425 ? -16.224 -13.918 50.777 1.00 113.64 ? 2072 LYS B CA 1 ATOM 7785 C C . LYS B 2 425 ? -17.601 -13.326 50.365 1.00 123.14 ? 2072 LYS B C 1 ATOM 7786 O O . LYS B 2 425 ? -17.715 -12.153 49.997 1.00 138.88 ? 2072 LYS B O 1 ATOM 7787 C CB . LYS B 2 425 ? -15.784 -13.585 52.233 1.00 108.18 ? 2072 LYS B CB 1 ATOM 7788 C CG . LYS B 2 425 ? -16.846 -13.134 53.235 1.00 101.90 ? 2072 LYS B CG 1 ATOM 7789 C CD . LYS B 2 425 ? -16.211 -12.530 54.480 1.00 110.62 ? 2072 LYS B CD 1 ATOM 7790 C CE . LYS B 2 425 ? -15.743 -11.092 54.243 1.00 129.84 ? 2072 LYS B CE 1 ATOM 7791 N NZ . LYS B 2 425 ? -15.015 -10.423 55.376 1.00 145.95 ? 2072 LYS B NZ 1 ATOM 7792 N N . VAL B 2 426 ? -18.626 -14.173 50.388 1.00 118.24 ? 2073 VAL B N 1 ATOM 7793 C CA . VAL B 2 426 ? -20.011 -13.781 50.139 1.00 114.44 ? 2073 VAL B CA 1 ATOM 7794 C C . VAL B 2 426 ? -20.798 -13.885 51.451 1.00 128.15 ? 2073 VAL B C 1 ATOM 7795 O O . VAL B 2 426 ? -20.803 -14.936 52.098 1.00 144.58 ? 2073 VAL B O 1 ATOM 7796 C CB . VAL B 2 426 ? -20.635 -14.698 49.054 1.00 103.18 ? 2073 VAL B CB 1 ATOM 7797 C CG1 . VAL B 2 426 ? -22.152 -14.703 49.076 1.00 102.42 ? 2073 VAL B CG1 1 ATOM 7798 C CG2 . VAL B 2 426 ? -20.185 -14.258 47.693 1.00 109.81 ? 2073 VAL B CG2 1 ATOM 7799 N N . ASP B 2 427 ? -21.440 -12.798 51.866 1.00 134.46 ? 2074 ASP B N 1 ATOM 7800 C CA . ASP B 2 427 ? -22.470 -12.891 52.900 1.00 146.70 ? 2074 ASP B CA 1 ATOM 7801 C C . ASP B 2 427 ? -23.777 -13.221 52.175 1.00 153.26 ? 2074 ASP B C 1 ATOM 7802 O O . ASP B 2 427 ? -24.339 -12.343 51.518 1.00 173.29 ? 2074 ASP B O 1 ATOM 7803 C CB . ASP B 2 427 ? -22.603 -11.560 53.660 1.00 153.49 ? 2074 ASP B CB 1 ATOM 7804 C CG . ASP B 2 427 ? -23.395 -11.684 54.971 1.00 155.65 ? 2074 ASP B CG 1 ATOM 7805 O OD1 . ASP B 2 427 ? -24.337 -12.502 55.092 1.00 145.25 ? 2074 ASP B OD1 1 ATOM 7806 O OD2 . ASP B 2 427 ? -23.074 -10.923 55.898 1.00 167.64 ? 2074 ASP B OD2 1 ATOM 7807 N N . LEU B 2 428 ? -24.260 -14.465 52.268 1.00 143.51 ? 2075 LEU B N 1 ATOM 7808 C CA . LEU B 2 428 ? -25.537 -14.826 51.623 1.00 137.79 ? 2075 LEU B CA 1 ATOM 7809 C C . LEU B 2 428 ? -26.727 -14.096 52.266 1.00 151.02 ? 2075 LEU B C 1 ATOM 7810 O O . LEU B 2 428 ? -27.885 -14.231 51.825 1.00 146.54 ? 2075 LEU B O 1 ATOM 7811 C CB . LEU B 2 428 ? -25.728 -16.340 51.585 1.00 127.28 ? 2075 LEU B CB 1 ATOM 7812 C CG . LEU B 2 428 ? -25.003 -16.956 50.383 1.00 122.82 ? 2075 LEU B CG 1 ATOM 7813 C CD1 . LEU B 2 428 ? -24.482 -18.368 50.656 1.00 120.43 ? 2075 LEU B CD1 1 ATOM 7814 C CD2 . LEU B 2 428 ? -25.905 -16.902 49.155 1.00 118.67 ? 2075 LEU B CD2 1 ATOM 7815 N N . LEU B 2 429 ? -26.384 -13.292 53.283 1.00 158.85 ? 2076 LEU B N 1 ATOM 7816 C CA . LEU B 2 429 ? -27.284 -12.433 54.052 1.00 153.30 ? 2076 LEU B CA 1 ATOM 7817 C C . LEU B 2 429 ? -28.431 -13.255 54.570 1.00 154.46 ? 2076 LEU B C 1 ATOM 7818 O O . LEU B 2 429 ? -29.583 -13.023 54.211 1.00 158.19 ? 2076 LEU B O 1 ATOM 7819 C CB . LEU B 2 429 ? -27.764 -11.233 53.228 1.00 158.22 ? 2076 LEU B CB 1 ATOM 7820 C CG . LEU B 2 429 ? -26.715 -10.164 52.887 1.00 175.55 ? 2076 LEU B CG 1 ATOM 7821 C CD1 . LEU B 2 429 ? -27.288 -9.124 51.937 1.00 179.21 ? 2076 LEU B CD1 1 ATOM 7822 C CD2 . LEU B 2 429 ? -26.139 -9.490 54.127 1.00 185.35 ? 2076 LEU B CD2 1 ATOM 7823 N N . ALA B 2 430 ? -28.083 -14.239 55.399 1.00 151.77 ? 2077 ALA B N 1 ATOM 7824 C CA . ALA B 2 430 ? -29.017 -15.244 55.909 1.00 151.45 ? 2077 ALA B CA 1 ATOM 7825 C C . ALA B 2 430 ? -28.417 -16.648 55.901 1.00 146.27 ? 2077 ALA B C 1 ATOM 7826 O O . ALA B 2 430 ? -27.832 -17.067 54.893 1.00 149.41 ? 2077 ALA B O 1 ATOM 7827 C CB . ALA B 2 430 ? -30.314 -15.243 55.116 1.00 157.65 ? 2077 ALA B CB 1 ATOM 7828 N N . PRO B 2 431 ? -28.545 -17.366 57.037 1.00 139.93 ? 2078 PRO B N 1 ATOM 7829 C CA . PRO B 2 431 ? -28.311 -18.799 57.167 1.00 129.34 ? 2078 PRO B CA 1 ATOM 7830 C C . PRO B 2 431 ? -28.938 -19.626 56.008 1.00 132.86 ? 2078 PRO B C 1 ATOM 7831 O O . PRO B 2 431 ? -30.145 -19.474 55.758 1.00 139.17 ? 2078 PRO B O 1 ATOM 7832 C CB . PRO B 2 431 ? -29.014 -19.106 58.485 1.00 128.25 ? 2078 PRO B CB 1 ATOM 7833 C CG . PRO B 2 431 ? -28.864 -17.869 59.322 1.00 129.43 ? 2078 PRO B CG 1 ATOM 7834 C CD . PRO B 2 431 ? -28.707 -16.721 58.363 1.00 141.71 ? 2078 PRO B CD 1 ATOM 7835 N N . MET B 2 432 ? -28.130 -20.464 55.322 1.00 127.49 ? 2079 MET B N 1 ATOM 7836 C CA . MET B 2 432 ? -28.547 -21.262 54.126 1.00 121.35 ? 2079 MET B CA 1 ATOM 7837 C C . MET B 2 432 ? -27.715 -22.509 53.886 1.00 128.09 ? 2079 MET B C 1 ATOM 7838 O O . MET B 2 432 ? -26.505 -22.486 54.140 1.00 132.92 ? 2079 MET B O 1 ATOM 7839 C CB . MET B 2 432 ? -28.413 -20.450 52.848 1.00 111.85 ? 2079 MET B CB 1 ATOM 7840 C CG . MET B 2 432 ? -29.557 -19.515 52.557 1.00 122.21 ? 2079 MET B CG 1 ATOM 7841 S SD . MET B 2 432 ? -29.133 -18.709 51.015 1.00 144.11 ? 2079 MET B SD 1 ATOM 7842 C CE . MET B 2 432 ? -29.684 -17.021 51.286 1.00 150.48 ? 2079 MET B CE 1 ATOM 7843 N N . ILE B 2 433 ? -28.349 -23.572 53.358 1.00 137.49 ? 2080 ILE B N 1 ATOM 7844 C CA . ILE B 2 433 ? -27.620 -24.800 52.909 1.00 136.14 ? 2080 ILE B CA 1 ATOM 7845 C C . ILE B 2 433 ? -27.036 -24.581 51.505 1.00 128.02 ? 2080 ILE B C 1 ATOM 7846 O O . ILE B 2 433 ? -27.748 -24.160 50.595 1.00 121.98 ? 2080 ILE B O 1 ATOM 7847 C CB . ILE B 2 433 ? -28.439 -26.146 52.983 1.00 126.22 ? 2080 ILE B CB 1 ATOM 7848 C CG1 . ILE B 2 433 ? -29.737 -26.088 52.171 1.00 128.27 ? 2080 ILE B CG1 1 ATOM 7849 C CG2 . ILE B 2 433 ? -28.746 -26.567 54.419 1.00 114.69 ? 2080 ILE B CG2 1 ATOM 7850 C CD1 . ILE B 2 433 ? -30.313 -27.445 51.795 1.00 125.13 ? 2080 ILE B CD1 1 ATOM 7851 N N . ILE B 2 434 ? -25.737 -24.828 51.348 1.00 123.59 ? 2081 ILE B N 1 ATOM 7852 C CA . ILE B 2 434 ? -25.068 -24.617 50.058 1.00 122.70 ? 2081 ILE B CA 1 ATOM 7853 C C . ILE B 2 434 ? -24.447 -25.915 49.557 1.00 130.27 ? 2081 ILE B C 1 ATOM 7854 O O . ILE B 2 434 ? -23.480 -26.400 50.126 1.00 142.57 ? 2081 ILE B O 1 ATOM 7855 C CB . ILE B 2 434 ? -24.059 -23.430 50.065 1.00 116.80 ? 2081 ILE B CB 1 ATOM 7856 C CG1 . ILE B 2 434 ? -23.127 -23.435 51.278 1.00 110.26 ? 2081 ILE B CG1 1 ATOM 7857 C CG2 . ILE B 2 434 ? -24.805 -22.113 50.092 1.00 126.62 ? 2081 ILE B CG2 1 ATOM 7858 C CD1 . ILE B 2 434 ? -22.654 -22.050 51.691 1.00 100.27 ? 2081 ILE B CD1 1 ATOM 7859 N N . HIS B 2 435 ? -25.029 -26.475 48.498 1.00 134.92 ? 2082 HIS B N 1 ATOM 7860 C CA . HIS B 2 435 ? -24.679 -27.815 48.007 1.00 131.13 ? 2082 HIS B CA 1 ATOM 7861 C C . HIS B 2 435 ? -23.466 -27.895 47.098 1.00 130.66 ? 2082 HIS B C 1 ATOM 7862 O O . HIS B 2 435 ? -22.904 -28.971 46.940 1.00 134.03 ? 2082 HIS B O 1 ATOM 7863 C CB . HIS B 2 435 ? -25.846 -28.426 47.249 1.00 129.86 ? 2082 HIS B CB 1 ATOM 7864 C CG . HIS B 2 435 ? -27.016 -28.755 48.109 1.00 131.03 ? 2082 HIS B CG 1 ATOM 7865 N ND1 . HIS B 2 435 ? -28.038 -27.862 48.341 1.00 134.31 ? 2082 HIS B ND1 1 ATOM 7866 C CD2 . HIS B 2 435 ? -27.335 -29.879 48.787 1.00 135.84 ? 2082 HIS B CD2 1 ATOM 7867 C CE1 . HIS B 2 435 ? -28.938 -28.420 49.129 1.00 130.85 ? 2082 HIS B CE1 1 ATOM 7868 N NE2 . HIS B 2 435 ? -28.533 -29.643 49.416 1.00 139.59 ? 2082 HIS B NE2 1 ATOM 7869 N N . GLY B 2 436 ? -23.089 -26.781 46.472 1.00 131.79 ? 2083 GLY B N 1 ATOM 7870 C CA . GLY B 2 436 ? -21.933 -26.757 45.571 1.00 126.62 ? 2083 GLY B CA 1 ATOM 7871 C C . GLY B 2 436 ? -21.528 -25.388 45.053 1.00 124.86 ? 2083 GLY B C 1 ATOM 7872 O O . GLY B 2 436 ? -22.346 -24.466 44.989 1.00 128.39 ? 2083 GLY B O 1 ATOM 7873 N N . ILE B 2 437 ? -20.261 -25.248 44.677 1.00 120.26 ? 2084 ILE B N 1 ATOM 7874 C CA . ILE B 2 437 ? -19.821 -24.022 44.007 1.00 123.78 ? 2084 ILE B CA 1 ATOM 7875 C C . ILE B 2 437 ? -19.339 -24.247 42.559 1.00 127.34 ? 2084 ILE B C 1 ATOM 7876 O O . ILE B 2 437 ? -18.595 -25.199 42.268 1.00 127.25 ? 2084 ILE B O 1 ATOM 7877 C CB . ILE B 2 437 ? -18.773 -23.240 44.829 1.00 115.61 ? 2084 ILE B CB 1 ATOM 7878 C CG1 . ILE B 2 437 ? -18.653 -21.814 44.292 1.00 111.31 ? 2084 ILE B CG1 1 ATOM 7879 C CG2 . ILE B 2 437 ? -17.425 -23.946 44.810 1.00 121.25 ? 2084 ILE B CG2 1 ATOM 7880 C CD1 . ILE B 2 437 ? -17.569 -21.000 44.949 1.00 105.25 ? 2084 ILE B CD1 1 ATOM 7881 N N . LYS B 2 438 ? -19.789 -23.369 41.663 1.00 118.84 ? 2085 LYS B N 1 ATOM 7882 C CA . LYS B 2 438 ? -19.347 -23.383 40.278 1.00 117.53 ? 2085 LYS B CA 1 ATOM 7883 C C . LYS B 2 438 ? -18.234 -22.352 40.122 1.00 126.94 ? 2085 LYS B C 1 ATOM 7884 O O . LYS B 2 438 ? -18.414 -21.199 40.511 1.00 127.74 ? 2085 LYS B O 1 ATOM 7885 C CB . LYS B 2 438 ? -20.502 -23.062 39.329 1.00 108.40 ? 2085 LYS B CB 1 ATOM 7886 C CG . LYS B 2 438 ? -21.649 -24.066 39.293 1.00 102.54 ? 2085 LYS B CG 1 ATOM 7887 C CD . LYS B 2 438 ? -22.505 -23.808 38.057 1.00 109.63 ? 2085 LYS B CD 1 ATOM 7888 C CE . LYS B 2 438 ? -24.009 -23.947 38.285 1.00 118.72 ? 2085 LYS B CE 1 ATOM 7889 N NZ . LYS B 2 438 ? -24.571 -25.300 37.972 1.00 134.70 ? 2085 LYS B NZ 1 ATOM 7890 N N . THR B 2 439 ? -17.096 -22.785 39.563 1.00 138.54 ? 2086 THR B N 1 ATOM 7891 C CA . THR B 2 439 ? -15.872 -21.961 39.405 1.00 137.51 ? 2086 THR B CA 1 ATOM 7892 C C . THR B 2 439 ? -15.512 -21.645 37.931 1.00 132.94 ? 2086 THR B C 1 ATOM 7893 O O . THR B 2 439 ? -15.935 -22.361 37.008 1.00 121.49 ? 2086 THR B O 1 ATOM 7894 C CB . THR B 2 439 ? -14.653 -22.588 40.141 1.00 138.28 ? 2086 THR B CB 1 ATOM 7895 O OG1 . THR B 2 439 ? -14.830 -24.006 40.265 1.00 140.35 ? 2086 THR B OG1 1 ATOM 7896 C CG2 . THR B 2 439 ? -14.511 -22.018 41.536 1.00 137.31 ? 2086 THR B CG2 1 ATOM 7897 N N . GLN B 2 440 ? -14.735 -20.572 37.728 1.00 133.15 ? 2087 GLN B N 1 ATOM 7898 C CA . GLN B 2 440 ? -14.390 -20.074 36.380 1.00 129.45 ? 2087 GLN B CA 1 ATOM 7899 C C . GLN B 2 440 ? -13.076 -19.303 36.290 1.00 130.68 ? 2087 GLN B C 1 ATOM 7900 O O . GLN B 2 440 ? -12.482 -18.941 37.313 1.00 133.60 ? 2087 GLN B O 1 ATOM 7901 C CB . GLN B 2 440 ? -15.490 -19.178 35.870 1.00 127.84 ? 2087 GLN B CB 1 ATOM 7902 C CG . GLN B 2 440 ? -15.434 -18.937 34.390 1.00 135.06 ? 2087 GLN B CG 1 ATOM 7903 C CD . GLN B 2 440 ? -16.793 -19.139 33.794 1.00 151.37 ? 2087 GLN B CD 1 ATOM 7904 O OE1 . GLN B 2 440 ? -17.489 -18.183 33.456 1.00 160.41 ? 2087 GLN B OE1 1 ATOM 7905 N NE2 . GLN B 2 440 ? -17.208 -20.397 33.708 1.00 160.83 ? 2087 GLN B NE2 1 ATOM 7906 N N . GLY B 2 441 ? -12.637 -19.055 35.055 1.00 127.46 ? 2088 GLY B N 1 ATOM 7907 C CA . GLY B 2 441 ? -11.445 -18.246 34.790 1.00 134.73 ? 2088 GLY B CA 1 ATOM 7908 C C . GLY B 2 441 ? -11.756 -16.974 34.013 1.00 139.94 ? 2088 GLY B C 1 ATOM 7909 O O . GLY B 2 441 ? -12.879 -16.471 34.079 1.00 139.83 ? 2088 GLY B O 1 ATOM 7910 N N . ALA B 2 442 ? -10.760 -16.454 33.288 1.00 142.02 ? 2089 ALA B N 1 ATOM 7911 C CA . ALA B 2 442 ? -10.940 -15.316 32.369 1.00 158.32 ? 2089 ALA B CA 1 ATOM 7912 C C . ALA B 2 442 ? -9.767 -15.149 31.388 1.00 179.34 ? 2089 ALA B C 1 ATOM 7913 O O . ALA B 2 442 ? -8.607 -15.285 31.780 1.00 191.04 ? 2089 ALA B O 1 ATOM 7914 C CB . ALA B 2 442 ? -11.154 -14.024 33.145 1.00 161.07 ? 2089 ALA B CB 1 ATOM 7915 N N . ARG B 2 443 ? -10.074 -14.850 30.120 1.00 188.68 ? 2090 ARG B N 1 ATOM 7916 C CA . ARG B 2 443 ? -9.050 -14.539 29.096 1.00 174.48 ? 2090 ARG B CA 1 ATOM 7917 C C . ARG B 2 443 ? -8.456 -13.180 29.508 1.00 170.56 ? 2090 ARG B C 1 ATOM 7918 O O . ARG B 2 443 ? -9.153 -12.346 30.117 1.00 159.51 ? 2090 ARG B O 1 ATOM 7919 C CB . ARG B 2 443 ? -9.668 -14.535 27.650 1.00 163.85 ? 2090 ARG B CB 1 ATOM 7920 C CG . ARG B 2 443 ? -8.786 -14.997 26.471 1.00 150.64 ? 2090 ARG B CG 1 ATOM 7921 C CD . ARG B 2 443 ? -9.565 -15.481 25.221 1.00 160.65 ? 2090 ARG B CD 1 ATOM 7922 N NE . ARG B 2 443 ? -8.937 -15.114 23.909 1.00 195.61 ? 2090 ARG B NE 1 ATOM 7923 C CZ . ARG B 2 443 ? -8.627 -15.921 22.860 1.00 188.46 ? 2090 ARG B CZ 1 ATOM 7924 N NH1 . ARG B 2 443 ? -8.853 -17.233 22.862 1.00 185.45 ? 2090 ARG B NH1 1 ATOM 7925 N NH2 . ARG B 2 443 ? -8.069 -15.402 21.765 1.00 166.29 ? 2090 ARG B NH2 1 ATOM 7926 N N . GLN B 2 444 ? -7.163 -12.993 29.244 1.00 176.07 ? 2091 GLN B N 1 ATOM 7927 C CA . GLN B 2 444 ? -6.527 -11.671 29.366 1.00 186.03 ? 2091 GLN B CA 1 ATOM 7928 C C . GLN B 2 444 ? -6.167 -11.080 28.001 1.00 184.57 ? 2091 GLN B C 1 ATOM 7929 O O . GLN B 2 444 ? -7.037 -10.551 27.303 1.00 197.64 ? 2091 GLN B O 1 ATOM 7930 C CB . GLN B 2 444 ? -5.322 -11.713 30.292 1.00 190.35 ? 2091 GLN B CB 1 ATOM 7931 C CG . GLN B 2 444 ? -5.567 -11.016 31.617 1.00 190.10 ? 2091 GLN B CG 1 ATOM 7932 C CD . GLN B 2 444 ? -5.300 -9.525 31.546 1.00 189.72 ? 2091 GLN B CD 1 ATOM 7933 O OE1 . GLN B 2 444 ? -4.206 -9.060 31.882 1.00 197.16 ? 2091 GLN B OE1 1 ATOM 7934 N NE2 . GLN B 2 444 ? -6.294 -8.769 31.100 1.00 182.27 ? 2091 GLN B NE2 1 ATOM 7935 N N . LYS B 2 445 ? -4.911 -11.141 27.595 1.00 169.23 ? 2092 LYS B N 1 ATOM 7936 C CA . LYS B 2 445 ? -4.719 -10.988 26.174 1.00 181.93 ? 2092 LYS B CA 1 ATOM 7937 C C . LYS B 2 445 ? -4.654 -12.387 25.581 1.00 183.86 ? 2092 LYS B C 1 ATOM 7938 O O . LYS B 2 445 ? -5.663 -12.894 25.107 1.00 194.23 ? 2092 LYS B O 1 ATOM 7939 C CB . LYS B 2 445 ? -3.568 -10.056 25.785 1.00 194.91 ? 2092 LYS B CB 1 ATOM 7940 C CG . LYS B 2 445 ? -2.563 -9.729 26.871 1.00 199.28 ? 2092 LYS B CG 1 ATOM 7941 C CD . LYS B 2 445 ? -1.611 -8.658 26.353 1.00 203.98 ? 2092 LYS B CD 1 ATOM 7942 C CE . LYS B 2 445 ? -0.317 -8.613 27.146 1.00 201.43 ? 2092 LYS B CE 1 ATOM 7943 N NZ . LYS B 2 445 ? -0.566 -8.191 28.552 1.00 193.35 ? 2092 LYS B NZ 1 ATOM 7944 N N . PHE B 2 446 ? -3.494 -13.026 25.628 1.00 183.97 ? 2093 PHE B N 1 ATOM 7945 C CA . PHE B 2 446 ? -3.411 -14.443 25.308 1.00 177.29 ? 2093 PHE B CA 1 ATOM 7946 C C . PHE B 2 446 ? -2.746 -15.060 26.508 1.00 177.23 ? 2093 PHE B C 1 ATOM 7947 O O . PHE B 2 446 ? -1.543 -15.341 26.521 1.00 180.48 ? 2093 PHE B O 1 ATOM 7948 C CB . PHE B 2 446 ? -2.606 -14.717 24.040 1.00 184.32 ? 2093 PHE B CB 1 ATOM 7949 C CG . PHE B 2 446 ? -2.667 -13.619 23.033 1.00 184.68 ? 2093 PHE B CG 1 ATOM 7950 C CD1 . PHE B 2 446 ? -3.880 -13.256 22.454 1.00 177.77 ? 2093 PHE B CD1 1 ATOM 7951 C CD2 . PHE B 2 446 ? -1.500 -12.956 22.657 1.00 191.44 ? 2093 PHE B CD2 1 ATOM 7952 C CE1 . PHE B 2 446 ? -3.931 -12.233 21.536 1.00 188.45 ? 2093 PHE B CE1 1 ATOM 7953 C CE2 . PHE B 2 446 ? -1.540 -11.938 21.729 1.00 203.33 ? 2093 PHE B CE2 1 ATOM 7954 C CZ . PHE B 2 446 ? -2.760 -11.575 21.171 1.00 208.23 ? 2093 PHE B CZ 1 ATOM 7955 N N . SER B 2 447 ? -3.549 -15.226 27.543 1.00 169.31 ? 2094 SER B N 1 ATOM 7956 C CA . SER B 2 447 ? -3.031 -15.566 28.840 1.00 163.76 ? 2094 SER B CA 1 ATOM 7957 C C . SER B 2 447 ? -4.148 -16.245 29.614 1.00 154.82 ? 2094 SER B C 1 ATOM 7958 O O . SER B 2 447 ? -5.118 -15.605 30.036 1.00 145.91 ? 2094 SER B O 1 ATOM 7959 C CB . SER B 2 447 ? -2.479 -14.301 29.535 1.00 168.53 ? 2094 SER B CB 1 ATOM 7960 O OG . SER B 2 447 ? -2.864 -13.090 28.867 1.00 158.84 ? 2094 SER B OG 1 ATOM 7961 N N . SER B 2 448 ? -4.028 -17.564 29.737 1.00 161.69 ? 2095 SER B N 1 ATOM 7962 C CA . SER B 2 448 ? -4.982 -18.368 30.502 1.00 163.96 ? 2095 SER B CA 1 ATOM 7963 C C . SER B 2 448 ? -5.004 -17.856 31.954 1.00 157.52 ? 2095 SER B C 1 ATOM 7964 O O . SER B 2 448 ? -3.966 -17.792 32.627 1.00 155.43 ? 2095 SER B O 1 ATOM 7965 C CB . SER B 2 448 ? -4.644 -19.880 30.420 1.00 171.35 ? 2095 SER B CB 1 ATOM 7966 O OG . SER B 2 448 ? -5.270 -20.544 29.319 1.00 155.37 ? 2095 SER B OG 1 ATOM 7967 N N . LEU B 2 449 ? -6.192 -17.473 32.418 1.00 151.43 ? 2096 LEU B N 1 ATOM 7968 C CA . LEU B 2 449 ? -6.337 -16.848 33.730 1.00 145.20 ? 2096 LEU B CA 1 ATOM 7969 C C . LEU B 2 449 ? -7.486 -17.434 34.603 1.00 141.34 ? 2096 LEU B C 1 ATOM 7970 O O . LEU B 2 449 ? -8.655 -17.038 34.474 1.00 128.35 ? 2096 LEU B O 1 ATOM 7971 C CB . LEU B 2 449 ? -6.455 -15.336 33.542 1.00 142.11 ? 2096 LEU B CB 1 ATOM 7972 C CG . LEU B 2 449 ? -5.823 -14.458 34.610 1.00 144.45 ? 2096 LEU B CG 1 ATOM 7973 C CD1 . LEU B 2 449 ? -4.321 -14.703 34.688 1.00 140.60 ? 2096 LEU B CD1 1 ATOM 7974 C CD2 . LEU B 2 449 ? -6.158 -12.997 34.339 1.00 144.67 ? 2096 LEU B CD2 1 ATOM 7975 N N . TYR B 2 450 ? -7.111 -18.365 35.496 1.00 142.36 ? 2097 TYR B N 1 ATOM 7976 C CA . TYR B 2 450 ? -8.033 -19.239 36.255 1.00 132.66 ? 2097 TYR B CA 1 ATOM 7977 C C . TYR B 2 450 ? -7.503 -19.595 37.668 1.00 133.28 ? 2097 TYR B C 1 ATOM 7978 O O . TYR B 2 450 ? -6.276 -19.543 37.915 1.00 130.21 ? 2097 TYR B O 1 ATOM 7979 C CB . TYR B 2 450 ? -8.311 -20.524 35.450 1.00 132.71 ? 2097 TYR B CB 1 ATOM 7980 C CG . TYR B 2 450 ? -7.067 -21.282 34.974 1.00 139.09 ? 2097 TYR B CG 1 ATOM 7981 C CD1 . TYR B 2 450 ? -6.302 -22.020 35.860 1.00 150.35 ? 2097 TYR B CD1 1 ATOM 7982 C CD2 . TYR B 2 450 ? -6.668 -21.272 33.640 1.00 148.19 ? 2097 TYR B CD2 1 ATOM 7983 C CE1 . TYR B 2 450 ? -5.170 -22.716 35.445 1.00 161.38 ? 2097 TYR B CE1 1 ATOM 7984 C CE2 . TYR B 2 450 ? -5.530 -21.968 33.217 1.00 160.54 ? 2097 TYR B CE2 1 ATOM 7985 C CZ . TYR B 2 450 ? -4.781 -22.692 34.131 1.00 159.67 ? 2097 TYR B CZ 1 ATOM 7986 O OH . TYR B 2 450 ? -3.650 -23.406 33.776 1.00 161.57 ? 2097 TYR B OH 1 ATOM 7987 N N . ILE B 2 451 ? -8.406 -19.941 38.600 1.00 126.47 ? 2098 ILE B N 1 ATOM 7988 C CA . ILE B 2 451 ? -7.932 -20.442 39.897 1.00 126.81 ? 2098 ILE B CA 1 ATOM 7989 C C . ILE B 2 451 ? -7.823 -21.921 39.812 1.00 125.44 ? 2098 ILE B C 1 ATOM 7990 O O . ILE B 2 451 ? -8.750 -22.598 39.340 1.00 126.35 ? 2098 ILE B O 1 ATOM 7991 C CB . ILE B 2 451 ? -8.816 -20.125 41.109 1.00 129.47 ? 2098 ILE B CB 1 ATOM 7992 C CG1 . ILE B 2 451 ? -8.734 -18.624 41.452 1.00 132.31 ? 2098 ILE B CG1 1 ATOM 7993 C CG2 . ILE B 2 451 ? -8.357 -20.991 42.292 1.00 125.50 ? 2098 ILE B CG2 1 ATOM 7994 C CD1 . ILE B 2 451 ? -9.289 -18.197 42.806 1.00 119.04 ? 2098 ILE B CD1 1 ATOM 7995 N N . SER B 2 452 ? -6.700 -22.414 40.309 1.00 123.58 ? 2099 SER B N 1 ATOM 7996 C CA . SER B 2 452 ? -6.307 -23.775 40.038 1.00 144.48 ? 2099 SER B CA 1 ATOM 7997 C C . SER B 2 452 ? -6.782 -24.801 41.078 1.00 156.51 ? 2099 SER B C 1 ATOM 7998 O O . SER B 2 452 ? -7.478 -25.770 40.743 1.00 155.01 ? 2099 SER B O 1 ATOM 7999 C CB . SER B 2 452 ? -4.794 -23.805 39.895 1.00 158.07 ? 2099 SER B CB 1 ATOM 8000 O OG . SER B 2 452 ? -4.310 -25.126 39.859 1.00 196.38 ? 2099 SER B OG 1 ATOM 8001 N N . GLN B 2 453 ? -6.367 -24.581 42.327 1.00 166.65 ? 2100 GLN B N 1 ATOM 8002 C CA . GLN B 2 453 ? -6.683 -25.419 43.483 1.00 148.60 ? 2100 GLN B CA 1 ATOM 8003 C C . GLN B 2 453 ? -7.203 -24.419 44.512 1.00 139.44 ? 2100 GLN B C 1 ATOM 8004 O O . GLN B 2 453 ? -6.811 -23.250 44.513 1.00 134.63 ? 2100 GLN B O 1 ATOM 8005 C CB . GLN B 2 453 ? -5.409 -26.118 43.984 1.00 148.45 ? 2100 GLN B CB 1 ATOM 8006 C CG . GLN B 2 453 ? -5.600 -27.234 45.004 1.00 162.53 ? 2100 GLN B CG 1 ATOM 8007 C CD . GLN B 2 453 ? -4.340 -28.082 45.201 1.00 184.52 ? 2100 GLN B CD 1 ATOM 8008 O OE1 . GLN B 2 453 ? -3.873 -28.743 44.271 1.00 191.55 ? 2100 GLN B OE1 1 ATOM 8009 N NE2 . GLN B 2 453 ? -3.790 -28.072 46.418 1.00 191.20 ? 2100 GLN B NE2 1 ATOM 8010 N N . PHE B 2 454 ? -8.113 -24.863 45.363 1.00 133.03 ? 2101 PHE B N 1 ATOM 8011 C CA . PHE B 2 454 ? -8.630 -23.998 46.410 1.00 129.03 ? 2101 PHE B CA 1 ATOM 8012 C C . PHE B 2 454 ? -9.290 -24.807 47.502 1.00 126.90 ? 2101 PHE B C 1 ATOM 8013 O O . PHE B 2 454 ? -9.621 -25.969 47.276 1.00 127.58 ? 2101 PHE B O 1 ATOM 8014 C CB . PHE B 2 454 ? -9.571 -22.925 45.837 1.00 125.34 ? 2101 PHE B CB 1 ATOM 8015 C CG . PHE B 2 454 ? -10.930 -23.424 45.427 1.00 120.70 ? 2101 PHE B CG 1 ATOM 8016 C CD1 . PHE B 2 454 ? -11.099 -24.183 44.279 1.00 122.44 ? 2101 PHE B CD1 1 ATOM 8017 C CD2 . PHE B 2 454 ? -12.052 -23.084 46.165 1.00 118.10 ? 2101 PHE B CD2 1 ATOM 8018 C CE1 . PHE B 2 454 ? -12.359 -24.614 43.885 1.00 119.99 ? 2101 PHE B CE1 1 ATOM 8019 C CE2 . PHE B 2 454 ? -13.309 -23.505 45.774 1.00 117.42 ? 2101 PHE B CE2 1 ATOM 8020 C CZ . PHE B 2 454 ? -13.466 -24.271 44.630 1.00 117.23 ? 2101 PHE B CZ 1 ATOM 8021 N N . ILE B 2 455 ? -9.435 -24.206 48.686 1.00 126.88 ? 2102 ILE B N 1 ATOM 8022 C CA . ILE B 2 455 ? -10.147 -24.831 49.825 1.00 130.01 ? 2102 ILE B CA 1 ATOM 8023 C C . ILE B 2 455 ? -11.359 -23.976 50.190 1.00 126.81 ? 2102 ILE B C 1 ATOM 8024 O O . ILE B 2 455 ? -11.487 -22.862 49.670 1.00 127.58 ? 2102 ILE B O 1 ATOM 8025 C CB . ILE B 2 455 ? -9.244 -25.007 51.073 1.00 120.11 ? 2102 ILE B CB 1 ATOM 8026 C CG1 . ILE B 2 455 ? -8.682 -23.658 51.531 1.00 116.66 ? 2102 ILE B CG1 1 ATOM 8027 C CG2 . ILE B 2 455 ? -8.116 -25.998 50.796 1.00 109.82 ? 2102 ILE B CG2 1 ATOM 8028 C CD1 . ILE B 2 455 ? -9.681 -22.687 52.128 1.00 111.24 ? 2102 ILE B CD1 1 ATOM 8029 N N . ILE B 2 456 ? -12.236 -24.463 51.072 1.00 116.45 ? 2103 ILE B N 1 ATOM 8030 C CA . ILE B 2 456 ? -13.327 -23.587 51.491 1.00 114.54 ? 2103 ILE B CA 1 ATOM 8031 C C . ILE B 2 456 ? -13.495 -23.382 52.983 1.00 124.23 ? 2103 ILE B C 1 ATOM 8032 O O . ILE B 2 456 ? -13.416 -24.332 53.755 1.00 140.51 ? 2103 ILE B O 1 ATOM 8033 C CB . ILE B 2 456 ? -14.650 -23.903 50.781 1.00 103.48 ? 2103 ILE B CB 1 ATOM 8034 C CG1 . ILE B 2 456 ? -14.616 -23.215 49.430 1.00 103.27 ? 2103 ILE B CG1 1 ATOM 8035 C CG2 . ILE B 2 456 ? -15.849 -23.378 51.558 1.00 91.89 ? 2103 ILE B CG2 1 ATOM 8036 C CD1 . ILE B 2 456 ? -15.778 -23.554 48.546 1.00 118.17 ? 2103 ILE B CD1 1 ATOM 8037 N N . MET B 2 457 ? -13.683 -22.114 53.357 1.00 123.89 ? 2104 MET B N 1 ATOM 8038 C CA . MET B 2 457 ? -14.085 -21.705 54.704 1.00 124.54 ? 2104 MET B CA 1 ATOM 8039 C C . MET B 2 457 ? -15.472 -21.019 54.666 1.00 128.98 ? 2104 MET B C 1 ATOM 8040 O O . MET B 2 457 ? -15.905 -20.541 53.608 1.00 126.07 ? 2104 MET B O 1 ATOM 8041 C CB . MET B 2 457 ? -13.027 -20.796 55.341 1.00 122.87 ? 2104 MET B CB 1 ATOM 8042 C CG . MET B 2 457 ? -11.772 -21.516 55.819 1.00 130.47 ? 2104 MET B CG 1 ATOM 8043 S SD . MET B 2 457 ? -10.528 -20.335 56.413 1.00 165.15 ? 2104 MET B SD 1 ATOM 8044 C CE . MET B 2 457 ? -8.912 -21.090 56.084 1.00 158.20 ? 2104 MET B CE 1 ATOM 8045 N N . TYR B 2 458 ? -16.166 -21.000 55.813 1.00 132.06 ? 2105 TYR B N 1 ATOM 8046 C CA . TYR B 2 458 ? -17.550 -20.495 55.938 1.00 125.78 ? 2105 TYR B CA 1 ATOM 8047 C C . TYR B 2 458 ? -17.941 -20.248 57.375 1.00 124.72 ? 2105 TYR B C 1 ATOM 8048 O O . TYR B 2 458 ? -17.475 -20.944 58.275 1.00 122.79 ? 2105 TYR B O 1 ATOM 8049 C CB . TYR B 2 458 ? -18.559 -21.481 55.345 1.00 125.62 ? 2105 TYR B CB 1 ATOM 8050 C CG . TYR B 2 458 ? -18.719 -22.802 56.083 1.00 128.65 ? 2105 TYR B CG 1 ATOM 8051 C CD1 . TYR B 2 458 ? -17.735 -23.807 56.016 1.00 124.65 ? 2105 TYR B CD1 1 ATOM 8052 C CD2 . TYR B 2 458 ? -19.871 -23.060 56.813 1.00 135.51 ? 2105 TYR B CD2 1 ATOM 8053 C CE1 . TYR B 2 458 ? -17.897 -25.014 56.672 1.00 125.02 ? 2105 TYR B CE1 1 ATOM 8054 C CE2 . TYR B 2 458 ? -20.046 -24.264 57.469 1.00 144.45 ? 2105 TYR B CE2 1 ATOM 8055 C CZ . TYR B 2 458 ? -19.058 -25.229 57.396 1.00 142.65 ? 2105 TYR B CZ 1 ATOM 8056 O OH . TYR B 2 458 ? -19.265 -26.402 58.070 1.00 167.24 ? 2105 TYR B OH 1 ATOM 8057 N N . SER B 2 459 ? -18.809 -19.267 57.591 1.00 127.28 ? 2106 SER B N 1 ATOM 8058 C CA . SER B 2 459 ? -19.326 -19.027 58.928 1.00 135.18 ? 2106 SER B CA 1 ATOM 8059 C C . SER B 2 459 ? -20.836 -18.824 58.931 1.00 141.88 ? 2106 SER B C 1 ATOM 8060 O O . SER B 2 459 ? -21.425 -18.351 57.959 1.00 144.12 ? 2106 SER B O 1 ATOM 8061 C CB . SER B 2 459 ? -18.590 -17.884 59.646 1.00 136.63 ? 2106 SER B CB 1 ATOM 8062 O OG . SER B 2 459 ? -18.620 -18.069 61.060 1.00 130.65 ? 2106 SER B OG 1 ATOM 8063 N N . LEU B 2 460 ? -21.432 -19.210 60.054 1.00 155.56 ? 2107 LEU B N 1 ATOM 8064 C CA . LEU B 2 460 ? -22.874 -19.282 60.256 1.00 156.64 ? 2107 LEU B CA 1 ATOM 8065 C C . LEU B 2 460 ? -23.311 -18.111 61.112 1.00 162.97 ? 2107 LEU B C 1 ATOM 8066 O O . LEU B 2 460 ? -24.499 -17.843 61.257 1.00 170.61 ? 2107 LEU B O 1 ATOM 8067 C CB . LEU B 2 460 ? -23.229 -20.616 60.932 1.00 158.11 ? 2107 LEU B CB 1 ATOM 8068 C CG . LEU B 2 460 ? -22.122 -21.269 61.795 1.00 173.16 ? 2107 LEU B CG 1 ATOM 8069 C CD1 . LEU B 2 460 ? -22.262 -20.902 63.278 1.00 176.59 ? 2107 LEU B CD1 1 ATOM 8070 C CD2 . LEU B 2 460 ? -22.011 -22.788 61.581 1.00 158.10 ? 2107 LEU B CD2 1 ATOM 8071 N N . ASP B 2 461 ? -22.330 -17.421 61.681 1.00 174.56 ? 2108 ASP B N 1 ATOM 8072 C CA . ASP B 2 461 ? -22.569 -16.189 62.418 1.00 181.51 ? 2108 ASP B CA 1 ATOM 8073 C C . ASP B 2 461 ? -21.989 -15.004 61.638 1.00 171.49 ? 2108 ASP B C 1 ATOM 8074 O O . ASP B 2 461 ? -22.730 -14.267 60.989 1.00 165.24 ? 2108 ASP B O 1 ATOM 8075 C CB . ASP B 2 461 ? -22.023 -16.287 63.861 1.00 194.91 ? 2108 ASP B CB 1 ATOM 8076 C CG . ASP B 2 461 ? -20.504 -16.097 63.954 1.00 194.34 ? 2108 ASP B CG 1 ATOM 8077 O OD1 . ASP B 2 461 ? -19.736 -16.880 63.340 1.00 187.82 ? 2108 ASP B OD1 1 ATOM 8078 O OD2 . ASP B 2 461 ? -20.087 -15.155 64.663 1.00 194.45 ? 2108 ASP B OD2 1 ATOM 8079 N N . GLY B 2 462 ? -20.665 -14.862 61.688 1.00 163.75 ? 2109 GLY B N 1 ATOM 8080 C CA . GLY B 2 462 ? -19.937 -13.823 60.980 1.00 154.13 ? 2109 GLY B CA 1 ATOM 8081 C C . GLY B 2 462 ? -18.499 -13.758 61.441 1.00 153.86 ? 2109 GLY B C 1 ATOM 8082 O O . GLY B 2 462 ? -17.581 -13.642 60.631 1.00 148.25 ? 2109 GLY B O 1 ATOM 8083 N N . LYS B 2 463 ? -18.309 -13.853 62.752 1.00 169.23 ? 2110 LYS B N 1 ATOM 8084 C CA . LYS B 2 463 ? -17.004 -13.589 63.355 1.00 190.39 ? 2110 LYS B CA 1 ATOM 8085 C C . LYS B 2 463 ? -16.104 -14.833 63.322 1.00 180.79 ? 2110 LYS B C 1 ATOM 8086 O O . LYS B 2 463 ? -15.177 -14.879 62.510 1.00 178.01 ? 2110 LYS B O 1 ATOM 8087 C CB . LYS B 2 463 ? -17.117 -12.967 64.781 1.00 218.32 ? 2110 LYS B CB 1 ATOM 8088 C CG . LYS B 2 463 ? -18.103 -11.794 64.991 1.00 227.41 ? 2110 LYS B CG 1 ATOM 8089 C CD . LYS B 2 463 ? -18.123 -10.734 63.879 1.00 227.05 ? 2110 LYS B CD 1 ATOM 8090 C CE . LYS B 2 463 ? -17.071 -9.646 64.045 1.00 222.22 ? 2110 LYS B CE 1 ATOM 8091 N NZ . LYS B 2 463 ? -17.356 -8.791 65.226 1.00 221.97 ? 2110 LYS B NZ 1 ATOM 8092 N N . LYS B 2 464 ? -16.376 -15.824 64.185 1.00 182.47 ? 2111 LYS B N 1 ATOM 8093 C CA . LYS B 2 464 ? -15.597 -17.083 64.198 1.00 178.82 ? 2111 LYS B CA 1 ATOM 8094 C C . LYS B 2 464 ? -15.984 -18.051 63.068 1.00 168.94 ? 2111 LYS B C 1 ATOM 8095 O O . LYS B 2 464 ? -17.114 -18.561 62.990 1.00 153.60 ? 2111 LYS B O 1 ATOM 8096 C CB . LYS B 2 464 ? -15.469 -17.777 65.591 1.00 186.46 ? 2111 LYS B CB 1 ATOM 8097 C CG . LYS B 2 464 ? -16.481 -17.450 66.703 1.00 195.54 ? 2111 LYS B CG 1 ATOM 8098 C CD . LYS B 2 464 ? -17.785 -18.246 66.617 1.00 194.37 ? 2111 LYS B CD 1 ATOM 8099 C CE . LYS B 2 464 ? -17.570 -19.752 66.512 1.00 189.83 ? 2111 LYS B CE 1 ATOM 8100 N NZ . LYS B 2 464 ? -18.543 -20.391 65.577 1.00 174.70 ? 2111 LYS B NZ 1 ATOM 8101 N N . TRP B 2 465 ? -14.987 -18.269 62.209 1.00 166.64 ? 2112 TRP B N 1 ATOM 8102 C CA . TRP B 2 465 ? -15.081 -18.963 60.931 1.00 155.76 ? 2112 TRP B CA 1 ATOM 8103 C C . TRP B 2 465 ? -14.808 -20.459 61.058 1.00 161.89 ? 2112 TRP B C 1 ATOM 8104 O O . TRP B 2 465 ? -14.535 -20.948 62.153 1.00 196.73 ? 2112 TRP B O 1 ATOM 8105 C CB . TRP B 2 465 ? -14.026 -18.381 60.011 1.00 153.12 ? 2112 TRP B CB 1 ATOM 8106 C CG . TRP B 2 465 ? -14.349 -17.054 59.486 1.00 163.57 ? 2112 TRP B CG 1 ATOM 8107 C CD1 . TRP B 2 465 ? -13.904 -15.845 59.955 1.00 177.28 ? 2112 TRP B CD1 1 ATOM 8108 C CD2 . TRP B 2 465 ? -15.174 -16.776 58.355 1.00 163.44 ? 2112 TRP B CD2 1 ATOM 8109 N NE1 . TRP B 2 465 ? -14.419 -14.828 59.186 1.00 189.25 ? 2112 TRP B NE1 1 ATOM 8110 C CE2 . TRP B 2 465 ? -15.200 -15.374 58.195 1.00 179.71 ? 2112 TRP B CE2 1 ATOM 8111 C CE3 . TRP B 2 465 ? -15.891 -17.577 57.454 1.00 147.08 ? 2112 TRP B CE3 1 ATOM 8112 C CZ2 . TRP B 2 465 ? -15.924 -14.756 57.167 1.00 174.41 ? 2112 TRP B CZ2 1 ATOM 8113 C CZ3 . TRP B 2 465 ? -16.606 -16.968 56.441 1.00 142.09 ? 2112 TRP B CZ3 1 ATOM 8114 C CH2 . TRP B 2 465 ? -16.617 -15.572 56.302 1.00 157.67 ? 2112 TRP B CH2 1 ATOM 8115 N N . GLN B 2 466 ? -14.850 -21.172 59.930 1.00 152.10 ? 2113 GLN B N 1 ATOM 8116 C CA . GLN B 2 466 ? -14.644 -22.626 59.900 1.00 150.62 ? 2113 GLN B CA 1 ATOM 8117 C C . GLN B 2 466 ? -14.111 -23.145 58.566 1.00 160.79 ? 2113 GLN B C 1 ATOM 8118 O O . GLN B 2 466 ? -14.424 -22.586 57.524 1.00 174.68 ? 2113 GLN B O 1 ATOM 8119 C CB . GLN B 2 466 ? -15.966 -23.303 60.153 1.00 143.35 ? 2113 GLN B CB 1 ATOM 8120 C CG . GLN B 2 466 ? -15.827 -24.751 60.524 1.00 151.63 ? 2113 GLN B CG 1 ATOM 8121 C CD . GLN B 2 466 ? -16.795 -25.103 61.610 1.00 164.88 ? 2113 GLN B CD 1 ATOM 8122 O OE1 . GLN B 2 466 ? -17.979 -24.747 61.542 1.00 171.31 ? 2113 GLN B OE1 1 ATOM 8123 N NE2 . GLN B 2 466 ? -16.300 -25.781 62.640 1.00 177.32 ? 2113 GLN B NE2 1 ATOM 8124 N N . THR B 2 467 ? -13.343 -24.233 58.589 1.00 164.42 ? 2114 THR B N 1 ATOM 8125 C CA . THR B 2 467 ? -12.861 -24.853 57.345 1.00 161.07 ? 2114 THR B CA 1 ATOM 8126 C C . THR B 2 467 ? -13.636 -26.122 56.982 1.00 160.77 ? 2114 THR B C 1 ATOM 8127 O O . THR B 2 467 ? -13.975 -26.922 57.855 1.00 161.35 ? 2114 THR B O 1 ATOM 8128 C CB . THR B 2 467 ? -11.370 -25.213 57.418 1.00 167.94 ? 2114 THR B CB 1 ATOM 8129 O OG1 . THR B 2 467 ? -10.652 -24.183 58.106 1.00 180.68 ? 2114 THR B OG1 1 ATOM 8130 C CG2 . THR B 2 467 ? -10.802 -25.394 56.026 1.00 171.32 ? 2114 THR B CG2 1 ATOM 8131 N N . TYR B 2 468 ? -13.884 -26.305 55.685 1.00 162.88 ? 2115 TYR B N 1 ATOM 8132 C CA . TYR B 2 468 ? -14.671 -27.429 55.184 1.00 147.45 ? 2115 TYR B CA 1 ATOM 8133 C C . TYR B 2 468 ? -13.833 -28.644 54.777 1.00 141.00 ? 2115 TYR B C 1 ATOM 8134 O O . TYR B 2 468 ? -12.992 -28.589 53.856 1.00 136.33 ? 2115 TYR B O 1 ATOM 8135 C CB . TYR B 2 468 ? -15.599 -26.982 54.049 1.00 139.98 ? 2115 TYR B CB 1 ATOM 8136 C CG . TYR B 2 468 ? -16.358 -28.101 53.377 1.00 133.04 ? 2115 TYR B CG 1 ATOM 8137 C CD1 . TYR B 2 468 ? -17.343 -28.797 54.045 1.00 135.56 ? 2115 TYR B CD1 1 ATOM 8138 C CD2 . TYR B 2 468 ? -16.103 -28.443 52.059 1.00 142.38 ? 2115 TYR B CD2 1 ATOM 8139 C CE1 . TYR B 2 468 ? -18.049 -29.812 53.424 1.00 140.59 ? 2115 TYR B CE1 1 ATOM 8140 C CE2 . TYR B 2 468 ? -16.800 -29.460 51.425 1.00 139.25 ? 2115 TYR B CE2 1 ATOM 8141 C CZ . TYR B 2 468 ? -17.774 -30.136 52.112 1.00 139.18 ? 2115 TYR B CZ 1 ATOM 8142 O OH . TYR B 2 468 ? -18.468 -31.147 51.494 1.00 141.98 ? 2115 TYR B OH 1 ATOM 8143 N N . ARG B 2 469 ? -14.080 -29.715 55.529 1.00 139.99 ? 2116 ARG B N 1 ATOM 8144 C CA . ARG B 2 469 ? -13.605 -31.073 55.275 1.00 151.63 ? 2116 ARG B CA 1 ATOM 8145 C C . ARG B 2 469 ? -14.808 -31.921 54.917 1.00 149.18 ? 2116 ARG B C 1 ATOM 8146 O O . ARG B 2 469 ? -15.411 -32.583 55.778 1.00 148.49 ? 2116 ARG B O 1 ATOM 8147 C CB . ARG B 2 469 ? -12.886 -31.674 56.509 1.00 160.66 ? 2116 ARG B CB 1 ATOM 8148 C CG . ARG B 2 469 ? -12.748 -33.211 56.564 1.00 151.27 ? 2116 ARG B CG 1 ATOM 8149 C CD . ARG B 2 469 ? -11.579 -33.572 57.465 1.00 148.41 ? 2116 ARG B CD 1 ATOM 8150 N NE . ARG B 2 469 ? -11.392 -34.984 57.796 1.00 148.55 ? 2116 ARG B NE 1 ATOM 8151 C CZ . ARG B 2 469 ? -12.169 -35.690 58.616 1.00 157.23 ? 2116 ARG B CZ 1 ATOM 8152 N NH1 . ARG B 2 469 ? -13.264 -35.164 59.148 1.00 157.85 ? 2116 ARG B NH1 1 ATOM 8153 N NH2 . ARG B 2 469 ? -11.865 -36.949 58.886 1.00 164.03 ? 2116 ARG B NH2 1 ATOM 8154 N N . GLY B 2 470 ? -15.160 -31.889 53.638 1.00 152.27 ? 2117 GLY B N 1 ATOM 8155 C CA . GLY B 2 470 ? -16.121 -32.833 53.104 1.00 153.28 ? 2117 GLY B CA 1 ATOM 8156 C C . GLY B 2 470 ? -15.810 -34.233 53.585 1.00 149.45 ? 2117 GLY B C 1 ATOM 8157 O O . GLY B 2 470 ? -14.781 -34.484 54.242 1.00 137.16 ? 2117 GLY B O 1 ATOM 8158 N N . ASN B 2 471 ? -16.697 -35.156 53.246 1.00 154.20 ? 2118 ASN B N 1 ATOM 8159 C CA . ASN B 2 471 ? -16.567 -36.512 53.741 1.00 164.74 ? 2118 ASN B CA 1 ATOM 8160 C C . ASN B 2 471 ? -15.104 -36.967 53.906 1.00 161.90 ? 2118 ASN B C 1 ATOM 8161 O O . ASN B 2 471 ? -14.160 -36.363 53.353 1.00 124.11 ? 2118 ASN B O 1 ATOM 8162 C CB . ASN B 2 471 ? -17.458 -37.515 52.962 1.00 164.91 ? 2118 ASN B CB 1 ATOM 8163 C CG . ASN B 2 471 ? -17.371 -37.337 51.460 1.00 160.21 ? 2118 ASN B CG 1 ATOM 8164 O OD1 . ASN B 2 471 ? -16.316 -36.990 50.958 1.00 164.16 ? 2118 ASN B OD1 1 ATOM 8165 N ND2 . ASN B 2 471 ? -18.463 -37.573 50.727 1.00 164.43 ? 2118 ASN B ND2 1 ATOM 8166 N N . SER B 2 472 ? -14.948 -37.994 54.739 1.00 191.89 ? 2119 SER B N 1 ATOM 8167 C CA . SER B 2 472 ? -13.669 -38.647 55.006 1.00 222.76 ? 2119 SER B CA 1 ATOM 8168 C C . SER B 2 472 ? -12.598 -38.316 53.954 1.00 232.65 ? 2119 SER B C 1 ATOM 8169 O O . SER B 2 472 ? -12.639 -38.799 52.816 1.00 271.81 ? 2119 SER B O 1 ATOM 8170 C CB . SER B 2 472 ? -13.863 -40.173 55.132 1.00 220.54 ? 2119 SER B CB 1 ATOM 8171 O OG . SER B 2 472 ? -14.504 -40.532 56.346 1.00 197.46 ? 2119 SER B OG 1 ATOM 8172 N N . THR B 2 473 ? -11.642 -37.486 54.343 1.00 200.58 ? 2120 THR B N 1 ATOM 8173 C CA . THR B 2 473 ? -10.612 -37.057 53.428 1.00 171.66 ? 2120 THR B CA 1 ATOM 8174 C C . THR B 2 473 ? -9.244 -37.183 54.137 1.00 167.63 ? 2120 THR B C 1 ATOM 8175 O O . THR B 2 473 ? -8.419 -38.063 53.814 1.00 148.03 ? 2120 THR B O 1 ATOM 8176 C CB . THR B 2 473 ? -11.002 -35.658 52.873 1.00 159.54 ? 2120 THR B CB 1 ATOM 8177 O OG1 . THR B 2 473 ? -9.844 -34.893 52.534 1.00 186.77 ? 2120 THR B OG1 1 ATOM 8178 C CG2 . THR B 2 473 ? -11.818 -34.897 53.882 1.00 140.59 ? 2120 THR B CG2 1 ATOM 8179 N N . GLY B 2 474 ? -9.061 -36.344 55.152 1.00 169.34 ? 2121 GLY B N 1 ATOM 8180 C CA . GLY B 2 474 ? -7.829 -36.264 55.923 1.00 187.21 ? 2121 GLY B CA 1 ATOM 8181 C C . GLY B 2 474 ? -7.916 -35.080 56.877 1.00 194.66 ? 2121 GLY B C 1 ATOM 8182 O O . GLY B 2 474 ? -8.515 -35.193 57.948 1.00 203.52 ? 2121 GLY B O 1 ATOM 8183 N N . THR B 2 475 ? -7.349 -33.943 56.460 1.00 188.68 ? 2122 THR B N 1 ATOM 8184 C CA . THR B 2 475 ? -7.217 -32.707 57.264 1.00 174.80 ? 2122 THR B CA 1 ATOM 8185 C C . THR B 2 475 ? -8.271 -31.625 56.956 1.00 162.61 ? 2122 THR B C 1 ATOM 8186 O O . THR B 2 475 ? -8.795 -30.940 57.855 1.00 141.76 ? 2122 THR B O 1 ATOM 8187 C CB . THR B 2 475 ? -5.841 -32.064 57.015 1.00 185.93 ? 2122 THR B CB 1 ATOM 8188 O OG1 . THR B 2 475 ? -5.957 -30.650 57.192 1.00 195.30 ? 2122 THR B OG1 1 ATOM 8189 C CG2 . THR B 2 475 ? -5.323 -32.351 55.570 1.00 182.24 ? 2122 THR B CG2 1 ATOM 8190 N N . LEU B 2 476 ? -8.507 -31.451 55.657 1.00 162.66 ? 2123 LEU B N 1 ATOM 8191 C CA . LEU B 2 476 ? -9.570 -30.618 55.109 1.00 157.34 ? 2123 LEU B CA 1 ATOM 8192 C C . LEU B 2 476 ? -9.707 -30.914 53.594 1.00 156.64 ? 2123 LEU B C 1 ATOM 8193 O O . LEU B 2 476 ? -8.752 -31.392 52.958 1.00 154.80 ? 2123 LEU B O 1 ATOM 8194 C CB . LEU B 2 476 ? -9.298 -29.139 55.395 1.00 151.26 ? 2123 LEU B CB 1 ATOM 8195 C CG . LEU B 2 476 ? -8.525 -28.266 54.401 1.00 152.74 ? 2123 LEU B CG 1 ATOM 8196 C CD1 . LEU B 2 476 ? -7.219 -28.900 53.921 1.00 145.97 ? 2123 LEU B CD1 1 ATOM 8197 C CD2 . LEU B 2 476 ? -9.433 -27.835 53.243 1.00 148.58 ? 2123 LEU B CD2 1 ATOM 8198 N N . MET B 2 477 ? -10.882 -30.642 53.020 1.00 153.75 ? 2124 MET B N 1 ATOM 8199 C CA . MET B 2 477 ? -11.116 -31.018 51.630 1.00 143.57 ? 2124 MET B CA 1 ATOM 8200 C C . MET B 2 477 ? -10.658 -29.976 50.644 1.00 139.62 ? 2124 MET B C 1 ATOM 8201 O O . MET B 2 477 ? -11.082 -28.802 50.701 1.00 122.59 ? 2124 MET B O 1 ATOM 8202 C CB . MET B 2 477 ? -12.554 -31.415 51.337 1.00 139.75 ? 2124 MET B CB 1 ATOM 8203 C CG . MET B 2 477 ? -12.584 -32.577 50.370 1.00 148.09 ? 2124 MET B CG 1 ATOM 8204 S SD . MET B 2 477 ? -13.769 -32.398 49.030 1.00 169.41 ? 2124 MET B SD 1 ATOM 8205 C CE . MET B 2 477 ? -13.160 -33.680 47.892 1.00 162.22 ? 2124 MET B CE 1 ATOM 8206 N N . VAL B 2 478 ? -9.785 -30.472 49.759 1.00 140.33 ? 2125 VAL B N 1 ATOM 8207 C CA . VAL B 2 478 ? -9.102 -29.763 48.680 1.00 132.28 ? 2125 VAL B CA 1 ATOM 8208 C C . VAL B 2 478 ? -9.961 -29.838 47.447 1.00 134.12 ? 2125 VAL B C 1 ATOM 8209 O O . VAL B 2 478 ? -10.408 -30.919 47.069 1.00 149.93 ? 2125 VAL B O 1 ATOM 8210 C CB . VAL B 2 478 ? -7.849 -30.541 48.253 1.00 133.06 ? 2125 VAL B CB 1 ATOM 8211 C CG1 . VAL B 2 478 ? -6.840 -29.620 47.570 1.00 124.22 ? 2125 VAL B CG1 1 ATOM 8212 C CG2 . VAL B 2 478 ? -7.266 -31.335 49.423 1.00 138.08 ? 2125 VAL B CG2 1 ATOM 8213 N N . PHE B 2 479 ? -10.155 -28.705 46.789 1.00 137.39 ? 2126 PHE B N 1 ATOM 8214 C CA . PHE B 2 479 ? -11.012 -28.654 45.610 1.00 143.02 ? 2126 PHE B CA 1 ATOM 8215 C C . PHE B 2 479 ? -10.200 -28.469 44.343 1.00 155.46 ? 2126 PHE B C 1 ATOM 8216 O O . PHE B 2 479 ? -9.059 -27.992 44.373 1.00 169.45 ? 2126 PHE B O 1 ATOM 8217 C CB . PHE B 2 479 ? -12.062 -27.544 45.753 1.00 137.39 ? 2126 PHE B CB 1 ATOM 8218 C CG . PHE B 2 479 ? -13.017 -27.765 46.891 1.00 135.33 ? 2126 PHE B CG 1 ATOM 8219 C CD1 . PHE B 2 479 ? -14.180 -28.499 46.705 1.00 135.62 ? 2126 PHE B CD1 1 ATOM 8220 C CD2 . PHE B 2 479 ? -12.744 -27.258 48.154 1.00 140.97 ? 2126 PHE B CD2 1 ATOM 8221 C CE1 . PHE B 2 479 ? -15.054 -28.722 47.750 1.00 131.80 ? 2126 PHE B CE1 1 ATOM 8222 C CE2 . PHE B 2 479 ? -13.609 -27.478 49.206 1.00 141.74 ? 2126 PHE B CE2 1 ATOM 8223 C CZ . PHE B 2 479 ? -14.766 -28.211 48.998 1.00 142.85 ? 2126 PHE B CZ 1 ATOM 8224 N N . PHE B 2 480 ? -10.784 -28.853 43.221 1.00 155.67 ? 2127 PHE B N 1 ATOM 8225 C CA . PHE B 2 480 ? -10.110 -28.624 41.968 1.00 161.30 ? 2127 PHE B CA 1 ATOM 8226 C C . PHE B 2 480 ? -10.841 -27.623 41.095 1.00 161.29 ? 2127 PHE B C 1 ATOM 8227 O O . PHE B 2 480 ? -11.997 -27.819 40.707 1.00 152.76 ? 2127 PHE B O 1 ATOM 8228 C CB . PHE B 2 480 ? -9.841 -29.934 41.255 1.00 172.99 ? 2127 PHE B CB 1 ATOM 8229 C CG . PHE B 2 480 ? -8.877 -30.809 41.985 1.00 169.57 ? 2127 PHE B CG 1 ATOM 8230 C CD1 . PHE B 2 480 ? -7.566 -30.396 42.185 1.00 175.14 ? 2127 PHE B CD1 1 ATOM 8231 C CD2 . PHE B 2 480 ? -9.277 -32.037 42.485 1.00 170.93 ? 2127 PHE B CD2 1 ATOM 8232 C CE1 . PHE B 2 480 ? -6.667 -31.202 42.862 1.00 189.15 ? 2127 PHE B CE1 1 ATOM 8233 C CE2 . PHE B 2 480 ? -8.382 -32.851 43.163 1.00 177.70 ? 2127 PHE B CE2 1 ATOM 8234 C CZ . PHE B 2 480 ? -7.077 -32.433 43.354 1.00 187.47 ? 2127 PHE B CZ 1 ATOM 8235 N N . GLY B 2 481 ? -10.138 -26.535 40.814 1.00 165.14 ? 2128 GLY B N 1 ATOM 8236 C CA . GLY B 2 481 ? -10.662 -25.464 39.987 1.00 161.95 ? 2128 GLY B CA 1 ATOM 8237 C C . GLY B 2 481 ? -10.419 -25.743 38.527 1.00 155.57 ? 2128 GLY B C 1 ATOM 8238 O O . GLY B 2 481 ? -10.288 -26.910 38.109 1.00 178.10 ? 2128 GLY B O 1 ATOM 8239 N N . ASN B 2 482 ? -10.340 -24.668 37.752 1.00 131.27 ? 2129 ASN B N 1 ATOM 8240 C CA . ASN B 2 482 ? -10.376 -24.788 36.299 1.00 131.32 ? 2129 ASN B CA 1 ATOM 8241 C C . ASN B 2 482 ? -9.022 -25.117 35.746 1.00 131.24 ? 2129 ASN B C 1 ATOM 8242 O O . ASN B 2 482 ? -8.046 -25.059 36.492 1.00 125.93 ? 2129 ASN B O 1 ATOM 8243 C CB . ASN B 2 482 ? -10.910 -23.506 35.697 1.00 126.97 ? 2129 ASN B CB 1 ATOM 8244 C CG . ASN B 2 482 ? -12.024 -22.924 36.526 1.00 125.10 ? 2129 ASN B CG 1 ATOM 8245 O OD1 . ASN B 2 482 ? -11.906 -22.802 37.768 1.00 117.58 ? 2129 ASN B OD1 1 ATOM 8246 N ND2 . ASN B 2 482 ? -13.127 -22.579 35.857 1.00 119.51 ? 2129 ASN B ND2 1 ATOM 8247 N N . VAL B 2 483 ? -8.966 -25.497 34.468 1.00 129.34 ? 2130 VAL B N 1 ATOM 8248 C CA . VAL B 2 483 ? -7.680 -25.698 33.789 1.00 140.04 ? 2130 VAL B CA 1 ATOM 8249 C C . VAL B 2 483 ? -7.644 -24.877 32.497 1.00 140.83 ? 2130 VAL B C 1 ATOM 8250 O O . VAL B 2 483 ? -6.799 -25.090 31.610 1.00 147.81 ? 2130 VAL B O 1 ATOM 8251 C CB . VAL B 2 483 ? -7.358 -27.199 33.538 1.00 152.40 ? 2130 VAL B CB 1 ATOM 8252 C CG1 . VAL B 2 483 ? -5.842 -27.431 33.396 1.00 159.09 ? 2130 VAL B CG1 1 ATOM 8253 C CG2 . VAL B 2 483 ? -7.952 -28.080 34.644 1.00 149.47 ? 2130 VAL B CG2 1 ATOM 8254 N N . ASP B 2 484 ? -8.577 -23.935 32.405 1.00 142.17 ? 2131 ASP B N 1 ATOM 8255 C CA . ASP B 2 484 ? -8.615 -22.984 31.306 1.00 152.19 ? 2131 ASP B CA 1 ATOM 8256 C C . ASP B 2 484 ? -9.482 -21.774 31.630 1.00 145.48 ? 2131 ASP B C 1 ATOM 8257 O O . ASP B 2 484 ? -10.250 -21.750 32.606 1.00 133.67 ? 2131 ASP B O 1 ATOM 8258 C CB . ASP B 2 484 ? -9.093 -23.642 30.001 1.00 174.66 ? 2131 ASP B CB 1 ATOM 8259 C CG . ASP B 2 484 ? -10.604 -23.823 29.953 1.00 196.26 ? 2131 ASP B CG 1 ATOM 8260 O OD1 . ASP B 2 484 ? -11.185 -24.234 30.984 1.00 212.03 ? 2131 ASP B OD1 1 ATOM 8261 O OD2 . ASP B 2 484 ? -11.211 -23.556 28.889 1.00 201.92 ? 2131 ASP B OD2 1 ATOM 8262 N N . SER B 2 485 ? -9.363 -20.796 30.743 1.00 146.67 ? 2132 SER B N 1 ATOM 8263 C CA . SER B 2 485 ? -9.965 -19.479 30.849 1.00 145.68 ? 2132 SER B CA 1 ATOM 8264 C C . SER B 2 485 ? -11.511 -19.395 30.763 1.00 154.10 ? 2132 SER B C 1 ATOM 8265 O O . SER B 2 485 ? -12.045 -18.307 30.546 1.00 157.11 ? 2132 SER B O 1 ATOM 8266 C CB . SER B 2 485 ? -9.347 -18.631 29.736 1.00 139.44 ? 2132 SER B CB 1 ATOM 8267 O OG . SER B 2 485 ? -9.255 -19.386 28.528 1.00 136.63 ? 2132 SER B OG 1 ATOM 8268 N N . SER B 2 486 ? -12.231 -20.506 30.945 1.00 158.89 ? 2133 SER B N 1 ATOM 8269 C CA . SER B 2 486 ? -13.666 -20.544 30.609 1.00 162.13 ? 2133 SER B CA 1 ATOM 8270 C C . SER B 2 486 ? -14.339 -21.873 30.909 1.00 173.67 ? 2133 SER B C 1 ATOM 8271 O O . SER B 2 486 ? -15.572 -21.961 30.931 1.00 171.07 ? 2133 SER B O 1 ATOM 8272 C CB . SER B 2 486 ? -13.849 -20.279 29.122 1.00 167.52 ? 2133 SER B CB 1 ATOM 8273 O OG . SER B 2 486 ? -13.170 -21.276 28.375 1.00 180.74 ? 2133 SER B OG 1 ATOM 8274 N N . GLY B 2 487 ? -13.526 -22.915 31.073 1.00 188.69 ? 2134 GLY B N 1 ATOM 8275 C CA . GLY B 2 487 ? -14.000 -24.202 31.574 1.00 187.80 ? 2134 GLY B CA 1 ATOM 8276 C C . GLY B 2 487 ? -14.625 -23.923 32.921 1.00 183.21 ? 2134 GLY B C 1 ATOM 8277 O O . GLY B 2 487 ? -14.308 -22.907 33.566 1.00 183.59 ? 2134 GLY B O 1 ATOM 8278 N N . ILE B 2 488 ? -15.505 -24.817 33.357 1.00 163.34 ? 2135 ILE B N 1 ATOM 8279 C CA . ILE B 2 488 ? -16.462 -24.441 34.395 1.00 144.13 ? 2135 ILE B CA 1 ATOM 8280 C C . ILE B 2 488 ? -16.763 -25.516 35.490 1.00 147.49 ? 2135 ILE B C 1 ATOM 8281 O O . ILE B 2 488 ? -17.835 -26.121 35.497 1.00 156.35 ? 2135 ILE B O 1 ATOM 8282 C CB . ILE B 2 488 ? -17.703 -23.844 33.679 1.00 126.00 ? 2135 ILE B CB 1 ATOM 8283 C CG1 . ILE B 2 488 ? -18.910 -23.742 34.632 1.00 122.16 ? 2135 ILE B CG1 1 ATOM 8284 C CG2 . ILE B 2 488 ? -17.926 -24.564 32.336 1.00 110.39 ? 2135 ILE B CG2 1 ATOM 8285 C CD1 . ILE B 2 488 ? -19.938 -22.689 34.264 1.00 119.43 ? 2135 ILE B CD1 1 ATOM 8286 N N . LYS B 2 489 ? -15.810 -25.734 36.414 1.00 143.94 ? 2136 LYS B N 1 ATOM 8287 C CA . LYS B 2 489 ? -15.839 -26.854 37.397 1.00 135.85 ? 2136 LYS B CA 1 ATOM 8288 C C . LYS B 2 489 ? -16.925 -26.572 38.383 1.00 143.45 ? 2136 LYS B C 1 ATOM 8289 O O . LYS B 2 489 ? -17.039 -25.443 38.864 1.00 158.63 ? 2136 LYS B O 1 ATOM 8290 C CB . LYS B 2 489 ? -14.509 -26.991 38.182 1.00 131.03 ? 2136 LYS B CB 1 ATOM 8291 C CG . LYS B 2 489 ? -14.111 -28.407 38.639 1.00 135.14 ? 2136 LYS B CG 1 ATOM 8292 C CD . LYS B 2 489 ? -12.935 -28.983 37.820 1.00 150.12 ? 2136 LYS B CD 1 ATOM 8293 C CE . LYS B 2 489 ? -12.550 -30.409 38.203 1.00 148.22 ? 2136 LYS B CE 1 ATOM 8294 N NZ . LYS B 2 489 ? -13.751 -31.264 38.468 1.00 145.89 ? 2136 LYS B NZ 1 ATOM 8295 N N . HIS B 2 490 ? -17.720 -27.592 38.688 1.00 146.14 ? 2137 HIS B N 1 ATOM 8296 C CA . HIS B 2 490 ? -18.774 -27.461 39.687 1.00 147.97 ? 2137 HIS B CA 1 ATOM 8297 C C . HIS B 2 490 ? -18.517 -28.506 40.758 1.00 155.83 ? 2137 HIS B C 1 ATOM 8298 O O . HIS B 2 490 ? -18.875 -29.658 40.567 1.00 189.42 ? 2137 HIS B O 1 ATOM 8299 C CB . HIS B 2 490 ? -20.140 -27.618 39.003 1.00 140.63 ? 2137 HIS B CB 1 ATOM 8300 C CG . HIS B 2 490 ? -21.263 -27.992 39.919 1.00 146.20 ? 2137 HIS B CG 1 ATOM 8301 N ND1 . HIS B 2 490 ? -22.376 -28.677 39.475 1.00 167.01 ? 2137 HIS B ND1 1 ATOM 8302 C CD2 . HIS B 2 490 ? -21.451 -27.788 41.245 1.00 149.26 ? 2137 HIS B CD2 1 ATOM 8303 C CE1 . HIS B 2 490 ? -23.204 -28.876 40.486 1.00 177.32 ? 2137 HIS B CE1 1 ATOM 8304 N NE2 . HIS B 2 490 ? -22.664 -28.351 41.573 1.00 174.87 ? 2137 HIS B NE2 1 ATOM 8305 N N . ASN B 2 491 ? -17.848 -28.123 41.853 1.00 153.10 ? 2138 ASN B N 1 ATOM 8306 C CA . ASN B 2 491 ? -17.560 -29.064 42.950 1.00 144.97 ? 2138 ASN B CA 1 ATOM 8307 C C . ASN B 2 491 ? -18.775 -29.095 43.840 1.00 149.50 ? 2138 ASN B C 1 ATOM 8308 O O . ASN B 2 491 ? -19.303 -28.025 44.171 1.00 153.02 ? 2138 ASN B O 1 ATOM 8309 C CB . ASN B 2 491 ? -16.358 -28.626 43.784 1.00 146.04 ? 2138 ASN B CB 1 ATOM 8310 C CG . ASN B 2 491 ? -15.109 -28.408 42.954 1.00 167.42 ? 2138 ASN B CG 1 ATOM 8311 O OD1 . ASN B 2 491 ? -14.440 -29.365 42.546 1.00 181.85 ? 2138 ASN B OD1 1 ATOM 8312 N ND2 . ASN B 2 491 ? -14.771 -27.138 42.720 1.00 166.89 ? 2138 ASN B ND2 1 ATOM 8313 N N . ILE B 2 492 ? -19.243 -30.298 44.198 1.00 147.83 ? 2139 ILE B N 1 ATOM 8314 C CA . ILE B 2 492 ? -20.403 -30.424 45.114 1.00 135.49 ? 2139 ILE B CA 1 ATOM 8315 C C . ILE B 2 492 ? -19.915 -30.575 46.550 1.00 125.60 ? 2139 ILE B C 1 ATOM 8316 O O . ILE B 2 492 ? -18.877 -31.204 46.790 1.00 117.43 ? 2139 ILE B O 1 ATOM 8317 C CB . ILE B 2 492 ? -21.481 -31.512 44.735 1.00 134.49 ? 2139 ILE B CB 1 ATOM 8318 C CG1 . ILE B 2 492 ? -20.898 -32.670 43.898 1.00 140.90 ? 2139 ILE B CG1 1 ATOM 8319 C CG2 . ILE B 2 492 ? -22.708 -30.876 44.058 1.00 126.41 ? 2139 ILE B CG2 1 ATOM 8320 C CD1 . ILE B 2 492 ? -21.817 -33.874 43.753 1.00 146.77 ? 2139 ILE B CD1 1 ATOM 8321 N N . PHE B 2 493 ? -20.640 -29.929 47.472 1.00 127.24 ? 2140 PHE B N 1 ATOM 8322 C CA . PHE B 2 493 ? -20.421 -30.050 48.913 1.00 135.74 ? 2140 PHE B CA 1 ATOM 8323 C C . PHE B 2 493 ? -21.166 -31.303 49.414 1.00 156.54 ? 2140 PHE B C 1 ATOM 8324 O O . PHE B 2 493 ? -22.392 -31.274 49.701 1.00 133.44 ? 2140 PHE B O 1 ATOM 8325 C CB . PHE B 2 493 ? -20.832 -28.767 49.655 1.00 130.90 ? 2140 PHE B CB 1 ATOM 8326 C CG . PHE B 2 493 ? -20.067 -27.520 49.224 1.00 126.19 ? 2140 PHE B CG 1 ATOM 8327 C CD1 . PHE B 2 493 ? -18.671 -27.517 49.146 1.00 115.06 ? 2140 PHE B CD1 1 ATOM 8328 C CD2 . PHE B 2 493 ? -20.751 -26.329 48.928 1.00 122.31 ? 2140 PHE B CD2 1 ATOM 8329 C CE1 . PHE B 2 493 ? -17.990 -26.370 48.761 1.00 105.80 ? 2140 PHE B CE1 1 ATOM 8330 C CE2 . PHE B 2 493 ? -20.069 -25.181 48.546 1.00 111.50 ? 2140 PHE B CE2 1 ATOM 8331 C CZ . PHE B 2 493 ? -18.689 -25.206 48.462 1.00 105.88 ? 2140 PHE B CZ 1 ATOM 8332 N N . ASN B 2 494 ? -20.364 -32.385 49.502 1.00 189.12 ? 2141 ASN B N 1 ATOM 8333 C CA . ASN B 2 494 ? -20.787 -33.813 49.545 1.00 172.46 ? 2141 ASN B CA 1 ATOM 8334 C C . ASN B 2 494 ? -21.758 -34.025 50.660 1.00 133.21 ? 2141 ASN B C 1 ATOM 8335 O O . ASN B 2 494 ? -22.912 -34.399 50.376 1.00 105.85 ? 2141 ASN B O 1 ATOM 8336 C CB . ASN B 2 494 ? -19.607 -34.808 49.711 1.00 194.37 ? 2141 ASN B CB 1 ATOM 8337 C CG . ASN B 2 494 ? -18.252 -34.252 49.271 1.00 218.56 ? 2141 ASN B CG 1 ATOM 8338 O OD1 . ASN B 2 494 ? -17.655 -34.740 48.304 1.00 229.31 ? 2141 ASN B OD1 1 ATOM 8339 N ND2 . ASN B 2 494 ? -17.739 -33.263 50.007 1.00 221.34 ? 2141 ASN B ND2 1 ATOM 8340 N N . PRO B 2 495 ? -21.255 -33.831 51.917 1.00 121.76 ? 2142 PRO B N 1 ATOM 8341 C CA . PRO B 2 495 ? -22.001 -33.236 53.027 1.00 125.02 ? 2142 PRO B CA 1 ATOM 8342 C C . PRO B 2 495 ? -22.066 -31.713 52.772 1.00 123.54 ? 2142 PRO B C 1 ATOM 8343 O O . PRO B 2 495 ? -21.062 -31.103 52.391 1.00 112.31 ? 2142 PRO B O 1 ATOM 8344 C CB . PRO B 2 495 ? -21.142 -33.566 54.253 1.00 120.97 ? 2142 PRO B CB 1 ATOM 8345 C CG . PRO B 2 495 ? -19.751 -33.694 53.721 1.00 108.52 ? 2142 PRO B CG 1 ATOM 8346 C CD . PRO B 2 495 ? -19.908 -34.272 52.350 1.00 111.16 ? 2142 PRO B CD 1 ATOM 8347 N N . PRO B 2 496 ? -23.246 -31.106 52.964 1.00 126.75 ? 2143 PRO B N 1 ATOM 8348 C CA . PRO B 2 496 ? -23.531 -29.776 52.417 1.00 122.96 ? 2143 PRO B CA 1 ATOM 8349 C C . PRO B 2 496 ? -23.294 -28.656 53.416 1.00 128.17 ? 2143 PRO B C 1 ATOM 8350 O O . PRO B 2 496 ? -23.815 -28.699 54.538 1.00 141.78 ? 2143 PRO B O 1 ATOM 8351 C CB . PRO B 2 496 ? -25.017 -29.858 52.105 1.00 122.86 ? 2143 PRO B CB 1 ATOM 8352 C CG . PRO B 2 496 ? -25.544 -30.860 53.119 1.00 134.29 ? 2143 PRO B CG 1 ATOM 8353 C CD . PRO B 2 496 ? -24.395 -31.640 53.719 1.00 126.81 ? 2143 PRO B CD 1 ATOM 8354 N N . ILE B 2 497 ? -22.523 -27.653 53.006 1.00 127.55 ? 2144 ILE B N 1 ATOM 8355 C CA . ILE B 2 497 ? -22.197 -26.535 53.890 1.00 116.90 ? 2144 ILE B CA 1 ATOM 8356 C C . ILE B 2 497 ? -23.436 -25.778 54.327 1.00 115.23 ? 2144 ILE B C 1 ATOM 8357 O O . ILE B 2 497 ? -24.414 -25.613 53.585 1.00 108.71 ? 2144 ILE B O 1 ATOM 8358 C CB . ILE B 2 497 ? -21.148 -25.576 53.312 1.00 113.76 ? 2144 ILE B CB 1 ATOM 8359 C CG1 . ILE B 2 497 ? -19.762 -26.214 53.409 1.00 121.87 ? 2144 ILE B CG1 1 ATOM 8360 C CG2 . ILE B 2 497 ? -21.166 -24.266 54.081 1.00 108.01 ? 2144 ILE B CG2 1 ATOM 8361 C CD1 . ILE B 2 497 ? -18.809 -25.837 52.287 1.00 130.71 ? 2144 ILE B CD1 1 ATOM 8362 N N . ILE B 2 498 ? -23.354 -25.338 55.568 1.00 114.64 ? 2145 ILE B N 1 ATOM 8363 C CA . ILE B 2 498 ? -24.488 -24.886 56.300 1.00 113.25 ? 2145 ILE B CA 1 ATOM 8364 C C . ILE B 2 498 ? -24.030 -23.615 56.976 1.00 117.07 ? 2145 ILE B C 1 ATOM 8365 O O . ILE B 2 498 ? -23.483 -23.647 58.089 1.00 122.81 ? 2145 ILE B O 1 ATOM 8366 C CB . ILE B 2 498 ? -25.014 -26.009 57.256 1.00 117.81 ? 2145 ILE B CB 1 ATOM 8367 C CG1 . ILE B 2 498 ? -26.346 -25.594 57.852 1.00 106.14 ? 2145 ILE B CG1 1 ATOM 8368 C CG2 . ILE B 2 498 ? -23.984 -26.472 58.319 1.00 123.97 ? 2145 ILE B CG2 1 ATOM 8369 C CD1 . ILE B 2 498 ? -27.243 -24.889 56.869 1.00 101.82 ? 2145 ILE B CD1 1 ATOM 8370 N N . ALA B 2 499 ? -24.214 -22.506 56.252 1.00 120.43 ? 2146 ALA B N 1 ATOM 8371 C CA . ALA B 2 499 ? -23.654 -21.197 56.633 1.00 123.70 ? 2146 ALA B CA 1 ATOM 8372 C C . ALA B 2 499 ? -24.468 -19.998 56.154 1.00 121.98 ? 2146 ALA B C 1 ATOM 8373 O O . ALA B 2 499 ? -25.367 -20.120 55.315 1.00 119.24 ? 2146 ALA B O 1 ATOM 8374 C CB . ALA B 2 499 ? -22.207 -21.066 56.145 1.00 112.13 ? 2146 ALA B CB 1 ATOM 8375 N N . ARG B 2 500 ? -24.130 -18.841 56.719 1.00 128.44 ? 2147 ARG B N 1 ATOM 8376 C CA . ARG B 2 500 ? -24.548 -17.542 56.206 1.00 132.22 ? 2147 ARG B CA 1 ATOM 8377 C C . ARG B 2 500 ? -23.517 -17.018 55.206 1.00 130.20 ? 2147 ARG B C 1 ATOM 8378 O O . ARG B 2 500 ? -23.859 -16.578 54.103 1.00 118.14 ? 2147 ARG B O 1 ATOM 8379 C CB . ARG B 2 500 ? -24.677 -16.538 57.351 1.00 136.64 ? 2147 ARG B CB 1 ATOM 8380 C CG . ARG B 2 500 ? -25.239 -15.221 56.871 1.00 145.18 ? 2147 ARG B CG 1 ATOM 8381 C CD . ARG B 2 500 ? -25.190 -14.137 57.914 1.00 156.40 ? 2147 ARG B CD 1 ATOM 8382 N NE . ARG B 2 500 ? -25.686 -12.891 57.338 1.00 165.37 ? 2147 ARG B NE 1 ATOM 8383 C CZ . ARG B 2 500 ? -26.770 -12.251 57.760 1.00 174.99 ? 2147 ARG B CZ 1 ATOM 8384 N NH1 . ARG B 2 500 ? -27.471 -12.730 58.789 1.00 182.12 ? 2147 ARG B NH1 1 ATOM 8385 N NH2 . ARG B 2 500 ? -27.137 -11.120 57.164 1.00 171.72 ? 2147 ARG B NH2 1 ATOM 8386 N N . TYR B 2 501 ? -22.256 -17.070 55.637 1.00 136.60 ? 2148 TYR B N 1 ATOM 8387 C CA . TYR B 2 501 ? -21.082 -16.635 54.888 1.00 131.19 ? 2148 TYR B CA 1 ATOM 8388 C C . TYR B 2 501 ? -20.378 -17.822 54.264 1.00 129.38 ? 2148 TYR B C 1 ATOM 8389 O O . TYR B 2 501 ? -20.472 -18.945 54.776 1.00 144.18 ? 2148 TYR B O 1 ATOM 8390 C CB . TYR B 2 501 ? -20.082 -16.014 55.846 1.00 137.40 ? 2148 TYR B CB 1 ATOM 8391 C CG . TYR B 2 501 ? -20.552 -14.771 56.539 1.00 152.82 ? 2148 TYR B CG 1 ATOM 8392 C CD1 . TYR B 2 501 ? -21.590 -14.807 57.475 1.00 150.88 ? 2148 TYR B CD1 1 ATOM 8393 C CD2 . TYR B 2 501 ? -19.931 -13.549 56.282 1.00 166.48 ? 2148 TYR B CD2 1 ATOM 8394 C CE1 . TYR B 2 501 ? -22.005 -13.653 58.109 1.00 159.25 ? 2148 TYR B CE1 1 ATOM 8395 C CE2 . TYR B 2 501 ? -20.333 -12.390 56.919 1.00 166.77 ? 2148 TYR B CE2 1 ATOM 8396 C CZ . TYR B 2 501 ? -21.366 -12.450 57.826 1.00 164.60 ? 2148 TYR B CZ 1 ATOM 8397 O OH . TYR B 2 501 ? -21.749 -11.290 58.438 1.00 174.35 ? 2148 TYR B OH 1 ATOM 8398 N N . ILE B 2 502 ? -19.645 -17.564 53.184 1.00 114.84 ? 2149 ILE B N 1 ATOM 8399 C CA . ILE B 2 502 ? -18.792 -18.575 52.550 1.00 105.80 ? 2149 ILE B CA 1 ATOM 8400 C C . ILE B 2 502 ? -17.546 -17.921 51.973 1.00 106.24 ? 2149 ILE B C 1 ATOM 8401 O O . ILE B 2 502 ? -17.636 -16.933 51.254 1.00 109.78 ? 2149 ILE B O 1 ATOM 8402 C CB . ILE B 2 502 ? -19.551 -19.429 51.490 1.00 100.87 ? 2149 ILE B CB 1 ATOM 8403 C CG1 . ILE B 2 502 ? -18.619 -20.494 50.878 1.00 97.26 ? 2149 ILE B CG1 1 ATOM 8404 C CG2 . ILE B 2 502 ? -20.233 -18.562 50.434 1.00 95.82 ? 2149 ILE B CG2 1 ATOM 8405 C CD1 . ILE B 2 502 ? -19.330 -21.694 50.271 1.00 95.09 ? 2149 ILE B CD1 1 ATOM 8406 N N . ARG B 2 503 ? -16.383 -18.467 52.299 1.00 112.43 ? 2150 ARG B N 1 ATOM 8407 C CA . ARG B 2 503 ? -15.110 -17.865 51.883 1.00 120.96 ? 2150 ARG B CA 1 ATOM 8408 C C . ARG B 2 503 ? -14.290 -18.840 51.040 1.00 116.58 ? 2150 ARG B C 1 ATOM 8409 O O . ARG B 2 503 ? -14.134 -20.009 51.414 1.00 121.83 ? 2150 ARG B O 1 ATOM 8410 C CB . ARG B 2 503 ? -14.320 -17.426 53.119 1.00 126.44 ? 2150 ARG B CB 1 ATOM 8411 C CG . ARG B 2 503 ? -13.209 -16.443 52.844 1.00 122.05 ? 2150 ARG B CG 1 ATOM 8412 C CD . ARG B 2 503 ? -12.940 -15.629 54.086 1.00 126.11 ? 2150 ARG B CD 1 ATOM 8413 N NE . ARG B 2 503 ? -12.516 -16.447 55.214 1.00 131.11 ? 2150 ARG B NE 1 ATOM 8414 C CZ . ARG B 2 503 ? -12.206 -15.950 56.412 1.00 154.85 ? 2150 ARG B CZ 1 ATOM 8415 N NH1 . ARG B 2 503 ? -12.275 -14.642 56.641 1.00 170.17 ? 2150 ARG B NH1 1 ATOM 8416 N NH2 . ARG B 2 503 ? -11.828 -16.754 57.395 1.00 165.05 ? 2150 ARG B NH2 1 ATOM 8417 N N . LEU B 2 504 ? -13.780 -18.380 49.900 1.00 105.46 ? 2151 LEU B N 1 ATOM 8418 C CA . LEU B 2 504 ? -12.966 -19.268 49.089 1.00 105.46 ? 2151 LEU B CA 1 ATOM 8419 C C . LEU B 2 504 ? -11.538 -18.756 48.909 1.00 116.12 ? 2151 LEU B C 1 ATOM 8420 O O . LEU B 2 504 ? -11.313 -17.701 48.319 1.00 119.81 ? 2151 LEU B O 1 ATOM 8421 C CB . LEU B 2 504 ? -13.667 -19.659 47.776 1.00 96.27 ? 2151 LEU B CB 1 ATOM 8422 C CG . LEU B 2 504 ? -13.216 -19.370 46.339 1.00 100.96 ? 2151 LEU B CG 1 ATOM 8423 C CD1 . LEU B 2 504 ? -11.751 -19.691 46.069 1.00 106.46 ? 2151 LEU B CD1 1 ATOM 8424 C CD2 . LEU B 2 504 ? -14.075 -20.179 45.382 1.00 98.44 ? 2151 LEU B CD2 1 ATOM 8425 N N . HIS B 2 505 ? -10.588 -19.514 49.457 1.00 127.12 ? 2152 HIS B N 1 ATOM 8426 C CA . HIS B 2 505 ? -9.165 -19.197 49.385 1.00 134.13 ? 2152 HIS B CA 1 ATOM 8427 C C . HIS B 2 505 ? -8.553 -20.115 48.332 1.00 135.19 ? 2152 HIS B C 1 ATOM 8428 O O . HIS B 2 505 ? -8.746 -21.337 48.419 1.00 128.98 ? 2152 HIS B O 1 ATOM 8429 C CB . HIS B 2 505 ? -8.475 -19.449 50.739 1.00 141.88 ? 2152 HIS B CB 1 ATOM 8430 C CG . HIS B 2 505 ? -9.201 -18.879 51.922 1.00 150.76 ? 2152 HIS B CG 1 ATOM 8431 N ND1 . HIS B 2 505 ? -8.545 -18.255 52.963 1.00 162.50 ? 2152 HIS B ND1 1 ATOM 8432 C CD2 . HIS B 2 505 ? -10.522 -18.842 52.235 1.00 145.10 ? 2152 HIS B CD2 1 ATOM 8433 C CE1 . HIS B 2 505 ? -9.429 -17.850 53.860 1.00 161.20 ? 2152 HIS B CE1 1 ATOM 8434 N NE2 . HIS B 2 505 ? -10.636 -18.193 53.441 1.00 149.12 ? 2152 HIS B NE2 1 ATOM 8435 N N . PRO B 2 506 ? -7.857 -19.536 47.317 1.00 136.87 ? 2153 PRO B N 1 ATOM 8436 C CA . PRO B 2 506 ? -6.996 -20.250 46.331 1.00 136.57 ? 2153 PRO B CA 1 ATOM 8437 C C . PRO B 2 506 ? -5.674 -20.845 46.906 1.00 131.93 ? 2153 PRO B C 1 ATOM 8438 O O . PRO B 2 506 ? -5.094 -20.224 47.785 1.00 132.73 ? 2153 PRO B O 1 ATOM 8439 C CB . PRO B 2 506 ? -6.680 -19.150 45.294 1.00 133.46 ? 2153 PRO B CB 1 ATOM 8440 C CG . PRO B 2 506 ? -6.986 -17.853 45.965 1.00 123.79 ? 2153 PRO B CG 1 ATOM 8441 C CD . PRO B 2 506 ? -8.133 -18.153 46.876 1.00 125.74 ? 2153 PRO B CD 1 ATOM 8442 N N . THR B 2 507 ? -5.213 -22.014 46.426 1.00 128.41 ? 2154 THR B N 1 ATOM 8443 C CA . THR B 2 507 ? -3.905 -22.598 46.858 1.00 147.31 ? 2154 THR B CA 1 ATOM 8444 C C . THR B 2 507 ? -2.876 -22.695 45.742 1.00 157.82 ? 2154 THR B C 1 ATOM 8445 O O . THR B 2 507 ? -1.673 -22.784 46.014 1.00 164.09 ? 2154 THR B O 1 ATOM 8446 C CB . THR B 2 507 ? -4.011 -24.036 47.410 1.00 156.76 ? 2154 THR B CB 1 ATOM 8447 O OG1 . THR B 2 507 ? -5.358 -24.311 47.806 1.00 160.91 ? 2154 THR B OG1 1 ATOM 8448 C CG2 . THR B 2 507 ? -2.966 -24.304 48.580 1.00 153.56 ? 2154 THR B CG2 1 ATOM 8449 N N . HIS B 2 508 ? -3.362 -22.767 44.503 1.00 165.45 ? 2155 HIS B N 1 ATOM 8450 C CA . HIS B 2 508 ? -2.539 -22.628 43.295 1.00 180.65 ? 2155 HIS B CA 1 ATOM 8451 C C . HIS B 2 508 ? -3.371 -21.899 42.218 1.00 171.79 ? 2155 HIS B C 1 ATOM 8452 O O . HIS B 2 508 ? -4.609 -21.821 42.294 1.00 160.59 ? 2155 HIS B O 1 ATOM 8453 C CB . HIS B 2 508 ? -2.062 -23.993 42.758 1.00 199.29 ? 2155 HIS B CB 1 ATOM 8454 C CG . HIS B 2 508 ? -1.255 -24.818 43.726 1.00 203.96 ? 2155 HIS B CG 1 ATOM 8455 N ND1 . HIS B 2 508 ? -1.826 -25.541 44.755 1.00 192.20 ? 2155 HIS B ND1 1 ATOM 8456 C CD2 . HIS B 2 508 ? 0.072 -25.094 43.770 1.00 209.72 ? 2155 HIS B CD2 1 ATOM 8457 C CE1 . HIS B 2 508 ? -0.885 -26.195 45.412 1.00 191.66 ? 2155 HIS B CE1 1 ATOM 8458 N NE2 . HIS B 2 508 ? 0.275 -25.944 44.831 1.00 202.81 ? 2155 HIS B NE2 1 ATOM 8459 N N . TYR B 2 509 ? -2.701 -21.357 41.212 1.00 169.01 ? 2156 TYR B N 1 ATOM 8460 C CA . TYR B 2 509 ? -3.410 -20.594 40.192 1.00 161.00 ? 2156 TYR B CA 1 ATOM 8461 C C . TYR B 2 509 ? -2.617 -20.566 38.916 1.00 163.05 ? 2156 TYR B C 1 ATOM 8462 O O . TYR B 2 509 ? -1.518 -21.155 38.840 1.00 158.14 ? 2156 TYR B O 1 ATOM 8463 C CB . TYR B 2 509 ? -3.706 -19.169 40.665 1.00 157.80 ? 2156 TYR B CB 1 ATOM 8464 C CG . TYR B 2 509 ? -2.540 -18.461 41.332 1.00 164.20 ? 2156 TYR B CG 1 ATOM 8465 C CD1 . TYR B 2 509 ? -1.470 -19.174 41.895 1.00 168.18 ? 2156 TYR B CD1 1 ATOM 8466 C CD2 . TYR B 2 509 ? -2.502 -17.075 41.394 1.00 160.52 ? 2156 TYR B CD2 1 ATOM 8467 C CE1 . TYR B 2 509 ? -0.419 -18.519 42.507 1.00 168.98 ? 2156 TYR B CE1 1 ATOM 8468 C CE2 . TYR B 2 509 ? -1.465 -16.411 42.011 1.00 164.17 ? 2156 TYR B CE2 1 ATOM 8469 C CZ . TYR B 2 509 ? -0.432 -17.137 42.560 1.00 169.45 ? 2156 TYR B CZ 1 ATOM 8470 O OH . TYR B 2 509 ? 0.594 -16.467 43.156 1.00 183.04 ? 2156 TYR B OH 1 ATOM 8471 N N . SER B 2 510 ? -3.193 -19.875 37.927 1.00 156.64 ? 2157 SER B N 1 ATOM 8472 C CA . SER B 2 510 ? -2.656 -19.817 36.572 1.00 163.91 ? 2157 SER B CA 1 ATOM 8473 C C . SER B 2 510 ? -1.509 -18.837 36.521 1.00 170.43 ? 2157 SER B C 1 ATOM 8474 O O . SER B 2 510 ? -0.369 -19.229 36.287 1.00 195.58 ? 2157 SER B O 1 ATOM 8475 C CB . SER B 2 510 ? -3.730 -19.397 35.571 1.00 158.04 ? 2157 SER B CB 1 ATOM 8476 O OG . SER B 2 510 ? -3.993 -18.011 35.675 1.00 161.08 ? 2157 SER B OG 1 ATOM 8477 N N . ILE B 2 511 ? -1.826 -17.559 36.721 1.00 158.33 ? 2158 ILE B N 1 ATOM 8478 C CA . ILE B 2 511 ? -0.826 -16.498 36.830 1.00 152.97 ? 2158 ILE B CA 1 ATOM 8479 C C . ILE B 2 511 ? -1.354 -15.369 37.700 1.00 159.12 ? 2158 ILE B C 1 ATOM 8480 O O . ILE B 2 511 ? -0.603 -14.520 38.201 1.00 173.22 ? 2158 ILE B O 1 ATOM 8481 C CB . ILE B 2 511 ? -0.337 -16.017 35.463 1.00 144.66 ? 2158 ILE B CB 1 ATOM 8482 C CG1 . ILE B 2 511 ? -1.264 -16.555 34.358 1.00 139.99 ? 2158 ILE B CG1 1 ATOM 8483 C CG2 . ILE B 2 511 ? 1.117 -16.452 35.288 1.00 154.68 ? 2158 ILE B CG2 1 ATOM 8484 C CD1 . ILE B 2 511 ? -0.591 -16.930 33.041 1.00 153.79 ? 2158 ILE B CD1 1 ATOM 8485 N N . ARG B 2 512 ? -2.666 -15.395 37.883 1.00 155.65 ? 2159 ARG B N 1 ATOM 8486 C CA . ARG B 2 512 ? -3.328 -14.656 38.930 1.00 145.32 ? 2159 ARG B CA 1 ATOM 8487 C C . ARG B 2 512 ? -4.512 -15.490 39.362 1.00 137.58 ? 2159 ARG B C 1 ATOM 8488 O O . ARG B 2 512 ? -5.207 -16.099 38.547 1.00 125.16 ? 2159 ARG B O 1 ATOM 8489 C CB . ARG B 2 512 ? -3.782 -13.292 38.437 1.00 146.27 ? 2159 ARG B CB 1 ATOM 8490 C CG . ARG B 2 512 ? -2.643 -12.428 37.925 1.00 161.35 ? 2159 ARG B CG 1 ATOM 8491 C CD . ARG B 2 512 ? -2.970 -10.953 38.003 1.00 174.39 ? 2159 ARG B CD 1 ATOM 8492 N NE . ARG B 2 512 ? -4.217 -10.608 37.323 1.00 173.61 ? 2159 ARG B NE 1 ATOM 8493 C CZ . ARG B 2 512 ? -4.286 -9.892 36.207 1.00 179.85 ? 2159 ARG B CZ 1 ATOM 8494 N NH1 . ARG B 2 512 ? -3.171 -9.439 35.627 1.00 191.04 ? 2159 ARG B NH1 1 ATOM 8495 N NH2 . ARG B 2 512 ? -5.473 -9.627 35.672 1.00 175.43 ? 2159 ARG B NH2 1 ATOM 8496 N N . SER B 2 513 ? -4.712 -15.544 40.666 1.00 143.56 ? 2160 SER B N 1 ATOM 8497 C CA . SER B 2 513 ? -5.891 -16.168 41.222 1.00 146.84 ? 2160 SER B CA 1 ATOM 8498 C C . SER B 2 513 ? -7.109 -15.368 40.722 1.00 143.58 ? 2160 SER B C 1 ATOM 8499 O O . SER B 2 513 ? -7.425 -14.295 41.253 1.00 155.59 ? 2160 SER B O 1 ATOM 8500 C CB . SER B 2 513 ? -5.808 -16.193 42.760 1.00 157.40 ? 2160 SER B CB 1 ATOM 8501 O OG . SER B 2 513 ? -4.567 -16.709 43.237 1.00 160.31 ? 2160 SER B OG 1 ATOM 8502 N N . THR B 2 514 ? -7.763 -15.891 39.685 1.00 128.21 ? 2161 THR B N 1 ATOM 8503 C CA . THR B 2 514 ? -8.875 -15.218 39.004 1.00 120.78 ? 2161 THR B CA 1 ATOM 8504 C C . THR B 2 514 ? -10.165 -16.038 39.071 1.00 127.10 ? 2161 THR B C 1 ATOM 8505 O O . THR B 2 514 ? -10.130 -17.270 38.964 1.00 140.64 ? 2161 THR B O 1 ATOM 8506 C CB . THR B 2 514 ? -8.503 -14.978 37.544 1.00 114.92 ? 2161 THR B CB 1 ATOM 8507 O OG1 . THR B 2 514 ? -7.169 -14.450 37.500 1.00 115.65 ? 2161 THR B OG1 1 ATOM 8508 C CG2 . THR B 2 514 ? -9.499 -14.028 36.867 1.00 111.53 ? 2161 THR B CG2 1 ATOM 8509 N N . LEU B 2 515 ? -11.308 -15.370 39.233 1.00 130.58 ? 2162 LEU B N 1 ATOM 8510 C CA . LEU B 2 515 ? -12.541 -16.094 39.577 1.00 131.25 ? 2162 LEU B CA 1 ATOM 8511 C C . LEU B 2 515 ? -13.858 -15.448 39.158 1.00 132.06 ? 2162 LEU B C 1 ATOM 8512 O O . LEU B 2 515 ? -14.171 -14.314 39.548 1.00 134.56 ? 2162 LEU B O 1 ATOM 8513 C CB . LEU B 2 515 ? -12.570 -16.413 41.090 1.00 127.68 ? 2162 LEU B CB 1 ATOM 8514 C CG . LEU B 2 515 ? -13.707 -17.202 41.761 1.00 117.51 ? 2162 LEU B CG 1 ATOM 8515 C CD1 . LEU B 2 515 ? -13.774 -18.664 41.332 1.00 110.57 ? 2162 LEU B CD1 1 ATOM 8516 C CD2 . LEU B 2 515 ? -13.561 -17.086 43.270 1.00 112.82 ? 2162 LEU B CD2 1 ATOM 8517 N N . ARG B 2 516 ? -14.605 -16.202 38.353 1.00 136.74 ? 2163 ARG B N 1 ATOM 8518 C CA . ARG B 2 516 ? -16.054 -16.050 38.205 1.00 139.88 ? 2163 ARG B CA 1 ATOM 8519 C C . ARG B 2 516 ? -16.688 -17.266 38.873 1.00 134.07 ? 2163 ARG B C 1 ATOM 8520 O O . ARG B 2 516 ? -16.061 -18.331 38.940 1.00 137.40 ? 2163 ARG B O 1 ATOM 8521 C CB . ARG B 2 516 ? -16.462 -15.980 36.734 1.00 145.34 ? 2163 ARG B CB 1 ATOM 8522 C CG . ARG B 2 516 ? -16.260 -14.620 36.088 1.00 149.75 ? 2163 ARG B CG 1 ATOM 8523 C CD . ARG B 2 516 ? -16.553 -14.671 34.603 1.00 145.50 ? 2163 ARG B CD 1 ATOM 8524 N NE . ARG B 2 516 ? -15.585 -15.501 33.899 1.00 148.01 ? 2163 ARG B NE 1 ATOM 8525 C CZ . ARG B 2 516 ? -15.669 -15.827 32.614 1.00 164.52 ? 2163 ARG B CZ 1 ATOM 8526 N NH1 . ARG B 2 516 ? -16.686 -15.397 31.872 1.00 174.94 ? 2163 ARG B NH1 1 ATOM 8527 N NH2 . ARG B 2 516 ? -14.733 -16.592 32.071 1.00 176.99 ? 2163 ARG B NH2 1 ATOM 8528 N N . MET B 2 517 ? -17.912 -17.113 39.380 1.00 126.62 ? 2164 MET B N 1 ATOM 8529 C CA . MET B 2 517 ? -18.526 -18.165 40.204 1.00 124.38 ? 2164 MET B CA 1 ATOM 8530 C C . MET B 2 517 ? -19.989 -17.933 40.593 1.00 124.17 ? 2164 MET B C 1 ATOM 8531 O O . MET B 2 517 ? -20.450 -16.805 40.769 1.00 131.71 ? 2164 MET B O 1 ATOM 8532 C CB . MET B 2 517 ? -17.702 -18.403 41.480 1.00 120.39 ? 2164 MET B CB 1 ATOM 8533 C CG . MET B 2 517 ? -17.358 -17.111 42.198 1.00 127.24 ? 2164 MET B CG 1 ATOM 8534 S SD . MET B 2 517 ? -17.594 -17.125 43.976 1.00 120.17 ? 2164 MET B SD 1 ATOM 8535 C CE . MET B 2 517 ? -19.229 -17.854 44.107 1.00 127.56 ? 2164 MET B CE 1 ATOM 8536 N N . GLU B 2 518 ? -20.702 -19.030 40.756 1.00 119.48 ? 2165 GLU B N 1 ATOM 8537 C CA . GLU B 2 518 ? -22.061 -18.996 41.215 1.00 120.59 ? 2165 GLU B CA 1 ATOM 8538 C C . GLU B 2 518 ? -22.143 -19.991 42.365 1.00 123.33 ? 2165 GLU B C 1 ATOM 8539 O O . GLU B 2 518 ? -21.436 -21.010 42.375 1.00 119.53 ? 2165 GLU B O 1 ATOM 8540 C CB . GLU B 2 518 ? -22.958 -19.412 40.058 1.00 135.30 ? 2165 GLU B CB 1 ATOM 8541 C CG . GLU B 2 518 ? -24.361 -19.860 40.420 1.00 152.90 ? 2165 GLU B CG 1 ATOM 8542 C CD . GLU B 2 518 ? -25.328 -18.710 40.459 1.00 163.23 ? 2165 GLU B CD 1 ATOM 8543 O OE1 . GLU B 2 518 ? -25.092 -17.770 41.260 1.00 153.50 ? 2165 GLU B OE1 1 ATOM 8544 O OE2 . GLU B 2 518 ? -26.303 -18.757 39.671 1.00 176.79 ? 2165 GLU B OE2 1 ATOM 8545 N N . LEU B 2 519 ? -22.992 -19.690 43.341 1.00 124.30 ? 2166 LEU B N 1 ATOM 8546 C CA . LEU B 2 519 ? -23.237 -20.611 44.448 1.00 116.87 ? 2166 LEU B CA 1 ATOM 8547 C C . LEU B 2 519 ? -24.482 -21.454 44.247 1.00 122.39 ? 2166 LEU B C 1 ATOM 8548 O O . LEU B 2 519 ? -25.542 -20.948 43.865 1.00 129.37 ? 2166 LEU B O 1 ATOM 8549 C CB . LEU B 2 519 ? -23.339 -19.842 45.751 1.00 106.13 ? 2166 LEU B CB 1 ATOM 8550 C CG . LEU B 2 519 ? -21.943 -19.651 46.307 1.00 108.00 ? 2166 LEU B CG 1 ATOM 8551 C CD1 . LEU B 2 519 ? -21.804 -18.290 46.958 1.00 116.37 ? 2166 LEU B CD1 1 ATOM 8552 C CD2 . LEU B 2 519 ? -21.621 -20.772 47.278 1.00 113.45 ? 2166 LEU B CD2 1 ATOM 8553 N N . MET B 2 520 ? -24.352 -22.748 44.500 1.00 117.99 ? 2167 MET B N 1 ATOM 8554 C CA . MET B 2 520 ? -25.520 -23.616 44.497 1.00 125.23 ? 2167 MET B CA 1 ATOM 8555 C C . MET B 2 520 ? -25.989 -23.933 45.917 1.00 129.04 ? 2167 MET B C 1 ATOM 8556 O O . MET B 2 520 ? -25.221 -24.400 46.759 1.00 135.59 ? 2167 MET B O 1 ATOM 8557 C CB . MET B 2 520 ? -25.264 -24.874 43.677 1.00 118.25 ? 2167 MET B CB 1 ATOM 8558 C CG . MET B 2 520 ? -24.897 -24.541 42.247 1.00 123.65 ? 2167 MET B CG 1 ATOM 8559 S SD . MET B 2 520 ? -26.243 -23.836 41.271 1.00 142.16 ? 2167 MET B SD 1 ATOM 8560 C CE . MET B 2 520 ? -26.872 -25.305 40.420 1.00 144.10 ? 2167 MET B CE 1 ATOM 8561 N N . GLY B 2 521 ? -27.258 -23.647 46.175 1.00 126.71 ? 2168 GLY B N 1 ATOM 8562 C CA . GLY B 2 521 ? -27.822 -23.786 47.499 1.00 124.19 ? 2168 GLY B CA 1 ATOM 8563 C C . GLY B 2 521 ? -29.328 -23.716 47.448 1.00 136.07 ? 2168 GLY B C 1 ATOM 8564 O O . GLY B 2 521 ? -29.925 -23.923 46.398 1.00 141.27 ? 2168 GLY B O 1 ATOM 8565 N N . CYS B 2 522 ? -29.927 -23.392 48.590 1.00 142.84 ? 2169 CYS B N 1 ATOM 8566 C CA . CYS B 2 522 ? -31.347 -23.579 48.866 1.00 149.42 ? 2169 CYS B CA 1 ATOM 8567 C C . CYS B 2 522 ? -31.471 -23.062 50.286 1.00 146.81 ? 2169 CYS B C 1 ATOM 8568 O O . CYS B 2 522 ? -30.502 -23.149 51.055 1.00 137.14 ? 2169 CYS B O 1 ATOM 8569 C CB . CYS B 2 522 ? -31.680 -25.078 48.805 1.00 173.93 ? 2169 CYS B CB 1 ATOM 8570 S SG . CYS B 2 522 ? -33.396 -25.613 49.061 1.00 215.83 ? 2169 CYS B SG 1 ATOM 8571 N N . ASP B 2 523 ? -32.627 -22.511 50.649 1.00 149.77 ? 2170 ASP B N 1 ATOM 8572 C CA . ASP B 2 523 ? -32.777 -21.933 51.986 1.00 162.00 ? 2170 ASP B CA 1 ATOM 8573 C C . ASP B 2 523 ? -32.685 -23.042 53.040 1.00 173.52 ? 2170 ASP B C 1 ATOM 8574 O O . ASP B 2 523 ? -32.391 -24.193 52.713 1.00 193.55 ? 2170 ASP B O 1 ATOM 8575 C CB . ASP B 2 523 ? -34.105 -21.208 52.125 1.00 164.60 ? 2170 ASP B CB 1 ATOM 8576 C CG . ASP B 2 523 ? -35.214 -22.140 52.545 1.00 179.29 ? 2170 ASP B CG 1 ATOM 8577 O OD1 . ASP B 2 523 ? -35.515 -23.077 51.771 1.00 174.34 ? 2170 ASP B OD1 1 ATOM 8578 O OD2 . ASP B 2 523 ? -35.754 -21.956 53.663 1.00 195.73 ? 2170 ASP B OD2 1 ATOM 8579 N N . LEU B 2 524 ? -32.952 -22.700 54.300 1.00 169.79 ? 2171 LEU B N 1 ATOM 8580 C CA . LEU B 2 524 ? -32.884 -23.672 55.390 1.00 144.21 ? 2171 LEU B CA 1 ATOM 8581 C C . LEU B 2 524 ? -33.917 -24.766 55.278 1.00 144.96 ? 2171 LEU B C 1 ATOM 8582 O O . LEU B 2 524 ? -33.585 -25.965 55.217 1.00 133.38 ? 2171 LEU B O 1 ATOM 8583 C CB . LEU B 2 524 ? -33.037 -22.968 56.726 1.00 127.93 ? 2171 LEU B CB 1 ATOM 8584 C CG . LEU B 2 524 ? -31.659 -22.846 57.338 1.00 120.32 ? 2171 LEU B CG 1 ATOM 8585 C CD1 . LEU B 2 524 ? -31.772 -23.072 58.837 1.00 124.26 ? 2171 LEU B CD1 1 ATOM 8586 C CD2 . LEU B 2 524 ? -30.726 -23.871 56.698 1.00 109.66 ? 2171 LEU B CD2 1 ATOM 8587 N N . ASN B 2 525 ? -35.166 -24.315 55.237 1.00 148.36 ? 2172 ASN B N 1 ATOM 8588 C CA . ASN B 2 525 ? -36.332 -25.165 55.180 1.00 155.74 ? 2172 ASN B CA 1 ATOM 8589 C C . ASN B 2 525 ? -36.570 -25.889 53.859 1.00 154.79 ? 2172 ASN B C 1 ATOM 8590 O O . ASN B 2 525 ? -37.668 -26.379 53.616 1.00 165.91 ? 2172 ASN B O 1 ATOM 8591 C CB . ASN B 2 525 ? -37.556 -24.347 55.562 1.00 165.18 ? 2172 ASN B CB 1 ATOM 8592 C CG . ASN B 2 525 ? -37.806 -24.371 57.044 1.00 179.85 ? 2172 ASN B CG 1 ATOM 8593 O OD1 . ASN B 2 525 ? -36.876 -24.235 57.840 1.00 175.75 ? 2172 ASN B OD1 1 ATOM 8594 N ND2 . ASN B 2 525 ? -39.061 -24.577 57.429 1.00 201.92 ? 2172 ASN B ND2 1 ATOM 8595 N N . SER B 2 526 ? -35.549 -25.951 53.012 1.00 162.51 ? 2173 SER B N 1 ATOM 8596 C CA . SER B 2 526 ? -35.615 -26.678 51.740 1.00 157.06 ? 2173 SER B CA 1 ATOM 8597 C C . SER B 2 526 ? -36.788 -26.267 50.793 1.00 163.24 ? 2173 SER B C 1 ATOM 8598 O O . SER B 2 526 ? -37.141 -27.021 49.867 1.00 160.76 ? 2173 SER B O 1 ATOM 8599 C CB . SER B 2 526 ? -35.564 -28.197 52.000 1.00 148.23 ? 2173 SER B CB 1 ATOM 8600 O OG . SER B 2 526 ? -34.454 -28.542 52.819 1.00 139.86 ? 2173 SER B OG 1 ATOM 8601 N N . CYS B 2 527 ? -37.360 -25.072 51.004 1.00 169.69 ? 2174 CYS B N 1 ATOM 8602 C CA . CYS B 2 527 ? -38.532 -24.617 50.223 1.00 171.82 ? 2174 CYS B CA 1 ATOM 8603 C C . CYS B 2 527 ? -38.358 -23.318 49.400 1.00 168.46 ? 2174 CYS B C 1 ATOM 8604 O O . CYS B 2 527 ? -39.101 -22.343 49.578 1.00 164.56 ? 2174 CYS B O 1 ATOM 8605 C CB . CYS B 2 527 ? -39.797 -24.547 51.100 1.00 170.18 ? 2174 CYS B CB 1 ATOM 8606 S SG . CYS B 2 527 ? -41.333 -24.295 50.161 1.00 182.31 ? 2174 CYS B SG 1 ATOM 8607 N N . SER B 2 528 ? -37.387 -23.321 48.491 1.00 163.73 ? 2175 SER B N 1 ATOM 8608 C CA . SER B 2 528 ? -37.252 -22.247 47.506 1.00 165.78 ? 2175 SER B CA 1 ATOM 8609 C C . SER B 2 528 ? -37.016 -22.831 46.106 1.00 159.31 ? 2175 SER B C 1 ATOM 8610 O O . SER B 2 528 ? -35.903 -22.786 45.577 1.00 155.34 ? 2175 SER B O 1 ATOM 8611 C CB . SER B 2 528 ? -36.161 -21.226 47.911 1.00 182.71 ? 2175 SER B CB 1 ATOM 8612 O OG . SER B 2 528 ? -34.930 -21.857 48.242 1.00 186.85 ? 2175 SER B OG 1 ATOM 8613 N N . MET B 2 529 ? -38.076 -23.380 45.513 1.00 156.89 ? 2176 MET B N 1 ATOM 8614 C CA . MET B 2 529 ? -37.968 -24.067 44.223 1.00 154.48 ? 2176 MET B CA 1 ATOM 8615 C C . MET B 2 529 ? -38.982 -23.545 43.206 1.00 146.04 ? 2176 MET B C 1 ATOM 8616 O O . MET B 2 529 ? -40.070 -23.112 43.578 1.00 143.34 ? 2176 MET B O 1 ATOM 8617 C CB . MET B 2 529 ? -38.137 -25.585 44.413 1.00 166.24 ? 2176 MET B CB 1 ATOM 8618 C CG . MET B 2 529 ? -37.268 -26.451 43.498 1.00 172.20 ? 2176 MET B CG 1 ATOM 8619 S SD . MET B 2 529 ? -35.461 -26.360 43.717 1.00 172.32 ? 2176 MET B SD 1 ATOM 8620 C CE . MET B 2 529 ? -34.873 -25.765 42.133 1.00 177.23 ? 2176 MET B CE 1 ATOM 8621 N N . PRO B 2 530 ? -38.611 -23.560 41.916 1.00 145.89 ? 2177 PRO B N 1 ATOM 8622 C CA . PRO B 2 530 ? -39.503 -23.365 40.778 1.00 148.48 ? 2177 PRO B CA 1 ATOM 8623 C C . PRO B 2 530 ? -40.810 -24.139 40.915 1.00 150.30 ? 2177 PRO B C 1 ATOM 8624 O O . PRO B 2 530 ? -40.779 -25.347 41.118 1.00 160.89 ? 2177 PRO B O 1 ATOM 8625 C CB . PRO B 2 530 ? -38.696 -23.960 39.609 1.00 161.30 ? 2177 PRO B CB 1 ATOM 8626 C CG . PRO B 2 530 ? -37.279 -24.130 40.100 1.00 166.30 ? 2177 PRO B CG 1 ATOM 8627 C CD . PRO B 2 530 ? -37.207 -23.539 41.482 1.00 158.93 ? 2177 PRO B CD 1 ATOM 8628 N N . LEU B 2 531 ? -41.947 -23.458 40.790 1.00 154.16 ? 2178 LEU B N 1 ATOM 8629 C CA . LEU B 2 531 ? -43.253 -24.104 41.002 1.00 147.04 ? 2178 LEU B CA 1 ATOM 8630 C C . LEU B 2 531 ? -43.947 -24.644 39.761 1.00 149.34 ? 2178 LEU B C 1 ATOM 8631 O O . LEU B 2 531 ? -45.036 -25.211 39.861 1.00 152.32 ? 2178 LEU B O 1 ATOM 8632 C CB . LEU B 2 531 ? -44.201 -23.187 41.767 1.00 137.57 ? 2178 LEU B CB 1 ATOM 8633 C CG . LEU B 2 531 ? -44.026 -23.368 43.265 1.00 133.74 ? 2178 LEU B CG 1 ATOM 8634 C CD1 . LEU B 2 531 ? -44.660 -22.197 43.978 1.00 146.64 ? 2178 LEU B CD1 1 ATOM 8635 C CD2 . LEU B 2 531 ? -44.635 -24.682 43.719 1.00 126.85 ? 2178 LEU B CD2 1 ATOM 8636 N N . GLY B 2 532 ? -43.327 -24.465 38.599 1.00 152.61 ? 2179 GLY B N 1 ATOM 8637 C CA . GLY B 2 532 ? -43.823 -25.096 37.389 1.00 152.47 ? 2179 GLY B CA 1 ATOM 8638 C C . GLY B 2 532 ? -44.077 -24.218 36.183 1.00 147.61 ? 2179 GLY B C 1 ATOM 8639 O O . GLY B 2 532 ? -44.050 -24.714 35.061 1.00 157.04 ? 2179 GLY B O 1 ATOM 8640 N N . MET B 2 533 ? -44.324 -22.926 36.396 1.00 137.79 ? 2180 MET B N 1 ATOM 8641 C CA . MET B 2 533 ? -44.675 -22.030 35.290 1.00 136.63 ? 2180 MET B CA 1 ATOM 8642 C C . MET B 2 533 ? -43.807 -22.287 34.048 1.00 143.25 ? 2180 MET B C 1 ATOM 8643 O O . MET B 2 533 ? -44.337 -22.555 32.959 1.00 138.44 ? 2180 MET B O 1 ATOM 8644 C CB . MET B 2 533 ? -44.608 -20.565 35.728 1.00 131.66 ? 2180 MET B CB 1 ATOM 8645 C CG . MET B 2 533 ? -45.648 -20.176 36.769 1.00 146.14 ? 2180 MET B CG 1 ATOM 8646 S SD . MET B 2 533 ? -47.351 -20.043 36.159 1.00 146.57 ? 2180 MET B SD 1 ATOM 8647 C CE . MET B 2 533 ? -47.365 -18.349 35.577 1.00 146.11 ? 2180 MET B CE 1 ATOM 8648 N N . GLU B 2 534 ? -42.480 -22.237 34.237 1.00 151.74 ? 2181 GLU B N 1 ATOM 8649 C CA . GLU B 2 534 ? -41.488 -22.428 33.164 1.00 147.05 ? 2181 GLU B CA 1 ATOM 8650 C C . GLU B 2 534 ? -41.357 -23.898 32.848 1.00 155.25 ? 2181 GLU B C 1 ATOM 8651 O O . GLU B 2 534 ? -41.244 -24.263 31.678 1.00 163.53 ? 2181 GLU B O 1 ATOM 8652 C CB . GLU B 2 534 ? -40.120 -21.867 33.560 1.00 141.46 ? 2181 GLU B CB 1 ATOM 8653 C CG . GLU B 2 534 ? -39.078 -21.879 32.448 1.00 159.28 ? 2181 GLU B CG 1 ATOM 8654 C CD . GLU B 2 534 ? -37.656 -22.032 32.982 1.00 173.82 ? 2181 GLU B CD 1 ATOM 8655 O OE1 . GLU B 2 534 ? -37.413 -21.632 34.151 1.00 171.82 ? 2181 GLU B OE1 1 ATOM 8656 O OE2 . GLU B 2 534 ? -36.783 -22.553 32.236 1.00 166.55 ? 2181 GLU B OE2 1 ATOM 8657 N N . SER B 2 535 ? -41.382 -24.727 33.897 1.00 157.49 ? 2182 SER B N 1 ATOM 8658 C CA . SER B 2 535 ? -41.384 -26.196 33.778 1.00 165.26 ? 2182 SER B CA 1 ATOM 8659 C C . SER B 2 535 ? -42.488 -26.756 32.858 1.00 164.84 ? 2182 SER B C 1 ATOM 8660 O O . SER B 2 535 ? -42.467 -27.942 32.529 1.00 167.23 ? 2182 SER B O 1 ATOM 8661 C CB . SER B 2 535 ? -41.517 -26.858 35.169 1.00 163.51 ? 2182 SER B CB 1 ATOM 8662 O OG . SER B 2 535 ? -40.377 -26.667 35.992 1.00 163.29 ? 2182 SER B OG 1 ATOM 8663 N N . LYS B 2 536 ? -43.432 -25.905 32.442 1.00 167.92 ? 2183 LYS B N 1 ATOM 8664 C CA . LYS B 2 536 ? -44.732 -26.340 31.900 1.00 163.72 ? 2183 LYS B CA 1 ATOM 8665 C C . LYS B 2 536 ? -45.373 -27.337 32.855 1.00 157.80 ? 2183 LYS B C 1 ATOM 8666 O O . LYS B 2 536 ? -46.410 -27.931 32.544 1.00 159.35 ? 2183 LYS B O 1 ATOM 8667 C CB . LYS B 2 536 ? -44.619 -26.951 30.500 1.00 184.24 ? 2183 LYS B CB 1 ATOM 8668 C CG . LYS B 2 536 ? -45.029 -26.039 29.355 1.00 191.56 ? 2183 LYS B CG 1 ATOM 8669 C CD . LYS B 2 536 ? -45.300 -26.859 28.096 1.00 198.22 ? 2183 LYS B CD 1 ATOM 8670 C CE . LYS B 2 536 ? -44.620 -26.260 26.876 1.00 195.11 ? 2183 LYS B CE 1 ATOM 8671 N NZ . LYS B 2 536 ? -44.706 -24.771 26.883 1.00 190.51 ? 2183 LYS B NZ 1 ATOM 8672 N N . ALA B 2 537 ? -44.728 -27.511 34.011 1.00 148.70 ? 2184 ALA B N 1 ATOM 8673 C CA . ALA B 2 537 ? -45.232 -28.322 35.112 1.00 147.43 ? 2184 ALA B CA 1 ATOM 8674 C C . ALA B 2 537 ? -46.631 -27.839 35.573 1.00 146.00 ? 2184 ALA B C 1 ATOM 8675 O O . ALA B 2 537 ? -47.522 -28.640 35.835 1.00 151.90 ? 2184 ALA B O 1 ATOM 8676 C CB . ALA B 2 537 ? -44.219 -28.350 36.260 1.00 135.07 ? 2184 ALA B CB 1 ATOM 8677 N N . ILE B 2 538 ? -46.823 -26.527 35.643 1.00 145.60 ? 2185 ILE B N 1 ATOM 8678 C CA . ILE B 2 538 ? -48.148 -25.927 35.793 1.00 142.48 ? 2185 ILE B CA 1 ATOM 8679 C C . ILE B 2 538 ? -48.910 -25.988 34.451 1.00 160.07 ? 2185 ILE B C 1 ATOM 8680 O O . ILE B 2 538 ? -48.405 -25.514 33.432 1.00 172.74 ? 2185 ILE B O 1 ATOM 8681 C CB . ILE B 2 538 ? -47.986 -24.475 36.276 1.00 126.25 ? 2185 ILE B CB 1 ATOM 8682 C CG1 . ILE B 2 538 ? -47.808 -24.456 37.798 1.00 116.13 ? 2185 ILE B CG1 1 ATOM 8683 C CG2 . ILE B 2 538 ? -49.133 -23.599 35.786 1.00 129.02 ? 2185 ILE B CG2 1 ATOM 8684 C CD1 . ILE B 2 538 ? -47.151 -23.201 38.331 1.00 106.58 ? 2185 ILE B CD1 1 ATOM 8685 N N . SER B 2 539 ? -50.112 -26.571 34.453 1.00 175.12 ? 2186 SER B N 1 ATOM 8686 C CA . SER B 2 539 ? -50.899 -26.797 33.219 1.00 182.29 ? 2186 SER B CA 1 ATOM 8687 C C . SER B 2 539 ? -51.175 -25.521 32.419 1.00 179.50 ? 2186 SER B C 1 ATOM 8688 O O . SER B 2 539 ? -51.133 -24.414 32.972 1.00 160.75 ? 2186 SER B O 1 ATOM 8689 C CB . SER B 2 539 ? -52.210 -27.532 33.539 1.00 194.58 ? 2186 SER B CB 1 ATOM 8690 O OG . SER B 2 539 ? -53.238 -27.195 32.621 1.00 204.92 ? 2186 SER B OG 1 ATOM 8691 N N . ASP B 2 540 ? -51.445 -25.683 31.119 1.00 191.04 ? 2187 ASP B N 1 ATOM 8692 C CA . ASP B 2 540 ? -51.664 -24.528 30.230 1.00 193.13 ? 2187 ASP B CA 1 ATOM 8693 C C . ASP B 2 540 ? -52.831 -23.670 30.688 1.00 182.42 ? 2187 ASP B C 1 ATOM 8694 O O . ASP B 2 540 ? -52.607 -22.616 31.281 1.00 187.92 ? 2187 ASP B O 1 ATOM 8695 C CB . ASP B 2 540 ? -51.771 -24.910 28.740 1.00 201.04 ? 2187 ASP B CB 1 ATOM 8696 C CG . ASP B 2 540 ? -50.603 -24.357 27.904 1.00 194.68 ? 2187 ASP B CG 1 ATOM 8697 O OD1 . ASP B 2 540 ? -50.179 -23.193 28.134 1.00 173.51 ? 2187 ASP B OD1 1 ATOM 8698 O OD2 . ASP B 2 540 ? -50.113 -25.088 27.012 1.00 197.02 ? 2187 ASP B OD2 1 ATOM 8699 N N . ALA B 2 541 ? -54.062 -24.114 30.445 1.00 168.85 ? 2188 ALA B N 1 ATOM 8700 C CA . ALA B 2 541 ? -55.207 -23.394 30.984 1.00 157.69 ? 2188 ALA B CA 1 ATOM 8701 C C . ALA B 2 541 ? -55.388 -23.683 32.498 1.00 152.58 ? 2188 ALA B C 1 ATOM 8702 O O . ALA B 2 541 ? -56.473 -23.987 32.969 1.00 161.19 ? 2188 ALA B O 1 ATOM 8703 C CB . ALA B 2 541 ? -56.467 -23.674 30.164 1.00 160.14 ? 2188 ALA B CB 1 ATOM 8704 N N . GLN B 2 542 ? -54.293 -23.600 33.249 1.00 147.86 ? 2189 GLN B N 1 ATOM 8705 C CA . GLN B 2 542 ? -54.311 -23.556 34.716 1.00 150.01 ? 2189 GLN B CA 1 ATOM 8706 C C . GLN B 2 542 ? -54.104 -22.075 35.139 1.00 150.13 ? 2189 GLN B C 1 ATOM 8707 O O . GLN B 2 542 ? -54.120 -21.728 36.331 1.00 135.80 ? 2189 GLN B O 1 ATOM 8708 C CB . GLN B 2 542 ? -53.188 -24.443 35.246 1.00 150.46 ? 2189 GLN B CB 1 ATOM 8709 C CG . GLN B 2 542 ? -53.302 -24.896 36.688 1.00 159.98 ? 2189 GLN B CG 1 ATOM 8710 C CD . GLN B 2 542 ? -52.299 -25.995 37.038 1.00 171.57 ? 2189 GLN B CD 1 ATOM 8711 O OE1 . GLN B 2 542 ? -52.276 -27.056 36.407 1.00 183.39 ? 2189 GLN B OE1 1 ATOM 8712 N NE2 . GLN B 2 542 ? -51.476 -25.753 38.061 1.00 168.29 ? 2189 GLN B NE2 1 ATOM 8713 N N . ILE B 2 543 ? -53.911 -21.233 34.113 1.00 158.40 ? 2190 ILE B N 1 ATOM 8714 C CA . ILE B 2 543 ? -53.689 -19.782 34.184 1.00 152.44 ? 2190 ILE B CA 1 ATOM 8715 C C . ILE B 2 543 ? -54.576 -19.109 33.152 1.00 163.33 ? 2190 ILE B C 1 ATOM 8716 O O . ILE B 2 543 ? -54.423 -19.358 31.947 1.00 171.54 ? 2190 ILE B O 1 ATOM 8717 C CB . ILE B 2 543 ? -52.266 -19.392 33.694 1.00 141.08 ? 2190 ILE B CB 1 ATOM 8718 C CG1 . ILE B 2 543 ? -51.163 -20.021 34.542 1.00 134.86 ? 2190 ILE B CG1 1 ATOM 8719 C CG2 . ILE B 2 543 ? -52.105 -17.878 33.612 1.00 134.48 ? 2190 ILE B CG2 1 ATOM 8720 C CD1 . ILE B 2 543 ? -49.914 -20.312 33.745 1.00 126.62 ? 2190 ILE B CD1 1 ATOM 8721 N N . THR B 2 544 ? -55.499 -18.263 33.591 1.00 171.74 ? 2191 THR B N 1 ATOM 8722 C CA . THR B 2 544 ? -55.947 -17.179 32.701 1.00 189.66 ? 2191 THR B CA 1 ATOM 8723 C C . THR B 2 544 ? -55.913 -15.841 33.444 1.00 180.34 ? 2191 THR B C 1 ATOM 8724 O O . THR B 2 544 ? -55.687 -15.801 34.659 1.00 175.29 ? 2191 THR B O 1 ATOM 8725 C CB . THR B 2 544 ? -57.260 -17.429 31.861 1.00 199.63 ? 2191 THR B CB 1 ATOM 8726 O OG1 . THR B 2 544 ? -58.379 -17.724 32.710 1.00 204.35 ? 2191 THR B OG1 1 ATOM 8727 C CG2 . THR B 2 544 ? -57.075 -18.527 30.740 1.00 185.56 ? 2191 THR B CG2 1 ATOM 8728 N N . ALA B 2 545 ? -56.090 -14.758 32.692 1.00 167.54 ? 2192 ALA B N 1 ATOM 8729 C CA . ALA B 2 545 ? -55.892 -13.423 33.204 1.00 152.73 ? 2192 ALA B CA 1 ATOM 8730 C C . ALA B 2 545 ? -57.131 -12.575 33.013 1.00 152.72 ? 2192 ALA B C 1 ATOM 8731 O O . ALA B 2 545 ? -58.125 -13.027 32.455 1.00 150.71 ? 2192 ALA B O 1 ATOM 8732 C CB . ALA B 2 545 ? -54.703 -12.780 32.526 1.00 150.56 ? 2192 ALA B CB 1 ATOM 8733 N N . SER B 2 546 ? -57.038 -11.336 33.484 1.00 153.54 ? 2193 SER B N 1 ATOM 8734 C CA . SER B 2 546 ? -58.142 -10.385 33.551 1.00 158.89 ? 2193 SER B CA 1 ATOM 8735 C C . SER B 2 546 ? -58.640 -9.945 32.189 1.00 168.88 ? 2193 SER B C 1 ATOM 8736 O O . SER B 2 546 ? -59.408 -8.985 32.077 1.00 190.16 ? 2193 SER B O 1 ATOM 8737 C CB . SER B 2 546 ? -57.699 -9.157 34.346 1.00 153.03 ? 2193 SER B CB 1 ATOM 8738 O OG . SER B 2 546 ? -56.370 -8.790 34.020 1.00 145.76 ? 2193 SER B OG 1 ATOM 8739 N N . SER B 2 547 ? -58.224 -10.681 31.170 1.00 166.76 ? 2194 SER B N 1 ATOM 8740 C CA . SER B 2 547 ? -58.353 -10.298 29.777 1.00 173.30 ? 2194 SER B CA 1 ATOM 8741 C C . SER B 2 547 ? -56.939 -10.264 29.268 1.00 171.17 ? 2194 SER B C 1 ATOM 8742 O O . SER B 2 547 ? -55.973 -10.373 30.033 1.00 163.77 ? 2194 SER B O 1 ATOM 8743 C CB . SER B 2 547 ? -58.962 -8.904 29.587 1.00 173.13 ? 2194 SER B CB 1 ATOM 8744 O OG . SER B 2 547 ? -57.943 -7.912 29.606 1.00 160.01 ? 2194 SER B OG 1 ATOM 8745 N N . TYR B 2 548 ? -56.828 -10.089 27.964 1.00 176.53 ? 2195 TYR B N 1 ATOM 8746 C CA . TYR B 2 548 ? -55.559 -10.139 27.307 1.00 175.82 ? 2195 TYR B CA 1 ATOM 8747 C C . TYR B 2 548 ? -55.694 -9.577 25.917 1.00 189.81 ? 2195 TYR B C 1 ATOM 8748 O O . TYR B 2 548 ? -56.778 -9.567 25.323 1.00 211.91 ? 2195 TYR B O 1 ATOM 8749 C CB . TYR B 2 548 ? -55.030 -11.573 27.261 1.00 168.67 ? 2195 TYR B CB 1 ATOM 8750 C CG . TYR B 2 548 ? -55.900 -12.553 26.510 1.00 177.20 ? 2195 TYR B CG 1 ATOM 8751 C CD1 . TYR B 2 548 ? -57.132 -12.969 27.020 1.00 181.60 ? 2195 TYR B CD1 1 ATOM 8752 C CD2 . TYR B 2 548 ? -55.482 -13.081 25.296 1.00 183.14 ? 2195 TYR B CD2 1 ATOM 8753 C CE1 . TYR B 2 548 ? -57.922 -13.875 26.335 1.00 186.69 ? 2195 TYR B CE1 1 ATOM 8754 C CE2 . TYR B 2 548 ? -56.262 -13.997 24.611 1.00 191.96 ? 2195 TYR B CE2 1 ATOM 8755 C CZ . TYR B 2 548 ? -57.478 -14.386 25.134 1.00 191.11 ? 2195 TYR B CZ 1 ATOM 8756 O OH . TYR B 2 548 ? -58.240 -15.290 24.443 1.00 203.33 ? 2195 TYR B OH 1 ATOM 8757 N N . PHE B 2 549 ? -54.573 -9.087 25.414 1.00 190.35 ? 2196 PHE B N 1 ATOM 8758 C CA . PHE B 2 549 ? -54.495 -8.640 24.053 1.00 179.74 ? 2196 PHE B CA 1 ATOM 8759 C C . PHE B 2 549 ? -54.444 -9.862 23.153 1.00 166.09 ? 2196 PHE B C 1 ATOM 8760 O O . PHE B 2 549 ? -53.791 -10.873 23.458 1.00 149.25 ? 2196 PHE B O 1 ATOM 8761 C CB . PHE B 2 549 ? -53.270 -7.740 23.851 1.00 181.97 ? 2196 PHE B CB 1 ATOM 8762 C CG . PHE B 2 549 ? -53.118 -7.239 22.449 1.00 187.67 ? 2196 PHE B CG 1 ATOM 8763 C CD1 . PHE B 2 549 ? -54.066 -6.380 21.899 1.00 199.65 ? 2196 PHE B CD1 1 ATOM 8764 C CD2 . PHE B 2 549 ? -52.038 -7.637 21.673 1.00 185.55 ? 2196 PHE B CD2 1 ATOM 8765 C CE1 . PHE B 2 549 ? -53.936 -5.922 20.599 1.00 204.67 ? 2196 PHE B CE1 1 ATOM 8766 C CE2 . PHE B 2 549 ? -51.899 -7.187 20.374 1.00 193.30 ? 2196 PHE B CE2 1 ATOM 8767 C CZ . PHE B 2 549 ? -52.849 -6.325 19.838 1.00 208.02 ? 2196 PHE B CZ 1 ATOM 8768 N N . THR B 2 550 ? -55.190 -9.770 22.066 1.00 160.29 ? 2197 THR B N 1 ATOM 8769 C CA . THR B 2 550 ? -55.075 -10.713 20.980 1.00 166.26 ? 2197 THR B CA 1 ATOM 8770 C C . THR B 2 550 ? -55.787 -10.144 19.774 1.00 173.69 ? 2197 THR B C 1 ATOM 8771 O O . THR B 2 550 ? -56.803 -9.474 19.916 1.00 180.71 ? 2197 THR B O 1 ATOM 8772 C CB . THR B 2 550 ? -55.633 -12.103 21.331 1.00 168.82 ? 2197 THR B CB 1 ATOM 8773 O OG1 . THR B 2 550 ? -55.629 -12.913 20.149 1.00 171.44 ? 2197 THR B OG1 1 ATOM 8774 C CG2 . THR B 2 550 ? -57.056 -12.010 21.904 1.00 176.95 ? 2197 THR B CG2 1 ATOM 8775 N N . ASN B 2 551 ? -55.225 -10.390 18.595 1.00 182.96 ? 2198 ASN B N 1 ATOM 8776 C CA . ASN B 2 551 ? -55.820 -9.946 17.336 1.00 197.03 ? 2198 ASN B CA 1 ATOM 8777 C C . ASN B 2 551 ? -55.578 -10.952 16.215 1.00 199.73 ? 2198 ASN B C 1 ATOM 8778 O O . ASN B 2 551 ? -54.981 -12.019 16.442 1.00 178.25 ? 2198 ASN B O 1 ATOM 8779 C CB . ASN B 2 551 ? -55.362 -8.519 16.941 1.00 200.75 ? 2198 ASN B CB 1 ATOM 8780 C CG . ASN B 2 551 ? -53.883 -8.435 16.574 1.00 204.10 ? 2198 ASN B CG 1 ATOM 8781 O OD1 . ASN B 2 551 ? -53.295 -9.368 16.017 1.00 212.92 ? 2198 ASN B OD1 1 ATOM 8782 N ND2 . ASN B 2 551 ? -53.279 -7.292 16.867 1.00 205.14 ? 2198 ASN B ND2 1 ATOM 8783 N N . MET B 2 552 ? -56.034 -10.592 15.011 1.00 213.65 ? 2199 MET B N 1 ATOM 8784 C CA . MET B 2 552 ? -55.963 -11.466 13.841 1.00 214.46 ? 2199 MET B CA 1 ATOM 8785 C C . MET B 2 552 ? -54.575 -12.089 13.680 1.00 204.87 ? 2199 MET B C 1 ATOM 8786 O O . MET B 2 552 ? -54.436 -13.173 13.115 1.00 217.70 ? 2199 MET B O 1 ATOM 8787 C CB . MET B 2 552 ? -56.391 -10.729 12.565 1.00 217.43 ? 2199 MET B CB 1 ATOM 8788 C CG . MET B 2 552 ? -56.905 -11.671 11.483 1.00 225.23 ? 2199 MET B CG 1 ATOM 8789 S SD . MET B 2 552 ? -56.767 -11.078 9.782 1.00 240.65 ? 2199 MET B SD 1 ATOM 8790 C CE . MET B 2 552 ? -54.994 -11.041 9.524 1.00 225.62 ? 2199 MET B CE 1 ATOM 8791 N N . PHE B 2 553 ? -53.556 -11.413 14.198 1.00 186.53 ? 2200 PHE B N 1 ATOM 8792 C CA . PHE B 2 553 ? -52.221 -11.963 14.166 1.00 187.96 ? 2200 PHE B CA 1 ATOM 8793 C C . PHE B 2 553 ? -51.782 -12.576 15.505 1.00 195.64 ? 2200 PHE B C 1 ATOM 8794 O O . PHE B 2 553 ? -51.712 -13.802 15.621 1.00 217.84 ? 2200 PHE B O 1 ATOM 8795 C CB . PHE B 2 553 ? -51.231 -10.954 13.580 1.00 179.96 ? 2200 PHE B CB 1 ATOM 8796 C CG . PHE B 2 553 ? -51.364 -10.788 12.084 1.00 193.24 ? 2200 PHE B CG 1 ATOM 8797 C CD1 . PHE B 2 553 ? -51.196 -11.879 11.225 1.00 206.03 ? 2200 PHE B CD1 1 ATOM 8798 C CD2 . PHE B 2 553 ? -51.661 -9.549 11.525 1.00 197.21 ? 2200 PHE B CD2 1 ATOM 8799 C CE1 . PHE B 2 553 ? -51.321 -11.733 9.847 1.00 215.20 ? 2200 PHE B CE1 1 ATOM 8800 C CE2 . PHE B 2 553 ? -51.789 -9.400 10.148 1.00 203.19 ? 2200 PHE B CE2 1 ATOM 8801 C CZ . PHE B 2 553 ? -51.612 -10.488 9.308 1.00 211.78 ? 2200 PHE B CZ 1 ATOM 8802 N N . ALA B 2 554 ? -51.530 -11.749 16.517 1.00 193.72 ? 2201 ALA B N 1 ATOM 8803 C CA . ALA B 2 554 ? -51.010 -12.229 17.814 1.00 184.40 ? 2201 ALA B CA 1 ATOM 8804 C C . ALA B 2 554 ? -52.011 -13.012 18.706 1.00 179.73 ? 2201 ALA B C 1 ATOM 8805 O O . ALA B 2 554 ? -53.202 -13.115 18.383 1.00 176.33 ? 2201 ALA B O 1 ATOM 8806 C CB . ALA B 2 554 ? -50.396 -11.062 18.585 1.00 180.64 ? 2201 ALA B CB 1 ATOM 8807 N N . THR B 2 555 ? -51.493 -13.584 19.801 1.00 173.15 ? 2202 THR B N 1 ATOM 8808 C CA . THR B 2 555 ? -52.287 -14.171 20.902 1.00 176.45 ? 2202 THR B CA 1 ATOM 8809 C C . THR B 2 555 ? -51.457 -14.204 22.186 1.00 167.03 ? 2202 THR B C 1 ATOM 8810 O O . THR B 2 555 ? -50.837 -15.231 22.515 1.00 159.80 ? 2202 THR B O 1 ATOM 8811 C CB . THR B 2 555 ? -52.806 -15.593 20.582 1.00 188.29 ? 2202 THR B CB 1 ATOM 8812 O OG1 . THR B 2 555 ? -53.659 -15.537 19.434 1.00 203.60 ? 2202 THR B OG1 1 ATOM 8813 C CG2 . THR B 2 555 ? -53.596 -16.198 21.770 1.00 180.21 ? 2202 THR B CG2 1 ATOM 8814 N N . TRP B 2 556 ? -51.450 -13.078 22.902 1.00 162.69 ? 2203 TRP B N 1 ATOM 8815 C CA . TRP B 2 556 ? -50.680 -12.945 24.142 1.00 158.59 ? 2203 TRP B CA 1 ATOM 8816 C C . TRP B 2 556 ? -51.419 -13.597 25.292 1.00 162.24 ? 2203 TRP B C 1 ATOM 8817 O O . TRP B 2 556 ? -51.661 -12.973 26.327 1.00 169.88 ? 2203 TRP B O 1 ATOM 8818 C CB . TRP B 2 556 ? -50.362 -11.480 24.444 1.00 154.55 ? 2203 TRP B CB 1 ATOM 8819 C CG . TRP B 2 556 ? -49.579 -10.850 23.348 1.00 167.25 ? 2203 TRP B CG 1 ATOM 8820 C CD1 . TRP B 2 556 ? -50.079 -10.182 22.270 1.00 175.45 ? 2203 TRP B CD1 1 ATOM 8821 C CD2 . TRP B 2 556 ? -48.153 -10.860 23.189 1.00 170.31 ? 2203 TRP B CD2 1 ATOM 8822 N NE1 . TRP B 2 556 ? -49.057 -9.757 21.458 1.00 180.42 ? 2203 TRP B NE1 1 ATOM 8823 C CE2 . TRP B 2 556 ? -47.863 -10.161 21.996 1.00 174.21 ? 2203 TRP B CE2 1 ATOM 8824 C CE3 . TRP B 2 556 ? -47.093 -11.382 23.941 1.00 173.00 ? 2203 TRP B CE3 1 ATOM 8825 C CZ2 . TRP B 2 556 ? -46.555 -9.977 21.532 1.00 171.10 ? 2203 TRP B CZ2 1 ATOM 8826 C CZ3 . TRP B 2 556 ? -45.795 -11.195 23.481 1.00 171.25 ? 2203 TRP B CZ3 1 ATOM 8827 C CH2 . TRP B 2 556 ? -45.540 -10.499 22.284 1.00 171.68 ? 2203 TRP B CH2 1 ATOM 8828 N N . SER B 2 557 ? -51.768 -14.866 25.088 1.00 165.22 ? 2204 SER B N 1 ATOM 8829 C CA . SER B 2 557 ? -52.520 -15.664 26.052 1.00 160.23 ? 2204 SER B CA 1 ATOM 8830 C C . SER B 2 557 ? -51.853 -15.675 27.424 1.00 145.77 ? 2204 SER B C 1 ATOM 8831 O O . SER B 2 557 ? -50.644 -15.810 27.519 1.00 145.62 ? 2204 SER B O 1 ATOM 8832 C CB . SER B 2 557 ? -52.726 -17.096 25.527 1.00 169.26 ? 2204 SER B CB 1 ATOM 8833 O OG . SER B 2 557 ? -51.687 -17.496 24.638 1.00 174.57 ? 2204 SER B OG 1 ATOM 8834 N N . PRO B 2 558 ? -52.640 -15.496 28.490 1.00 142.14 ? 2205 PRO B N 1 ATOM 8835 C CA . PRO B 2 558 ? -52.191 -15.633 29.871 1.00 146.80 ? 2205 PRO B CA 1 ATOM 8836 C C . PRO B 2 558 ? -51.313 -16.873 30.106 1.00 148.61 ? 2205 PRO B C 1 ATOM 8837 O O . PRO B 2 558 ? -50.379 -16.861 30.916 1.00 140.79 ? 2205 PRO B O 1 ATOM 8838 C CB . PRO B 2 558 ? -53.512 -15.778 30.639 1.00 151.00 ? 2205 PRO B CB 1 ATOM 8839 C CG . PRO B 2 558 ? -54.583 -15.931 29.597 1.00 154.15 ? 2205 PRO B CG 1 ATOM 8840 C CD . PRO B 2 558 ? -54.065 -15.159 28.440 1.00 148.55 ? 2205 PRO B CD 1 ATOM 8841 N N . SER B 2 559 ? -51.624 -17.926 29.368 1.00 156.06 ? 2206 SER B N 1 ATOM 8842 C CA . SER B 2 559 ? -50.914 -19.191 29.411 1.00 159.69 ? 2206 SER B CA 1 ATOM 8843 C C . SER B 2 559 ? -49.498 -19.150 28.810 1.00 151.91 ? 2206 SER B C 1 ATOM 8844 O O . SER B 2 559 ? -48.895 -20.208 28.570 1.00 145.35 ? 2206 SER B O 1 ATOM 8845 C CB . SER B 2 559 ? -51.778 -20.215 28.682 1.00 179.67 ? 2206 SER B CB 1 ATOM 8846 O OG . SER B 2 559 ? -52.892 -19.562 28.067 1.00 193.72 ? 2206 SER B OG 1 ATOM 8847 N N . LYS B 2 560 ? -48.992 -17.929 28.578 1.00 145.10 ? 2207 LYS B N 1 ATOM 8848 C CA . LYS B 2 560 ? -47.648 -17.663 28.015 1.00 137.63 ? 2207 LYS B CA 1 ATOM 8849 C C . LYS B 2 560 ? -46.757 -16.938 29.029 1.00 125.63 ? 2207 LYS B C 1 ATOM 8850 O O . LYS B 2 560 ? -45.617 -16.598 28.726 1.00 113.94 ? 2207 LYS B O 1 ATOM 8851 C CB . LYS B 2 560 ? -47.710 -16.827 26.700 1.00 138.36 ? 2207 LYS B CB 1 ATOM 8852 C CG . LYS B 2 560 ? -48.291 -17.510 25.454 1.00 142.03 ? 2207 LYS B CG 1 ATOM 8853 C CD . LYS B 2 560 ? -47.279 -17.738 24.338 1.00 135.97 ? 2207 LYS B CD 1 ATOM 8854 C CE . LYS B 2 560 ? -47.980 -18.156 23.048 1.00 147.45 ? 2207 LYS B CE 1 ATOM 8855 N NZ . LYS B 2 560 ? -47.079 -18.155 21.853 1.00 150.37 ? 2207 LYS B NZ 1 ATOM 8856 N N . ALA B 2 561 ? -47.277 -16.696 30.229 1.00 131.66 ? 2208 ALA B N 1 ATOM 8857 C CA . ALA B 2 561 ? -46.531 -15.942 31.258 1.00 140.50 ? 2208 ALA B CA 1 ATOM 8858 C C . ALA B 2 561 ? -45.396 -16.770 31.898 1.00 128.80 ? 2208 ALA B C 1 ATOM 8859 O O . ALA B 2 561 ? -45.309 -16.944 33.121 1.00 119.07 ? 2208 ALA B O 1 ATOM 8860 C CB . ALA B 2 561 ? -47.485 -15.372 32.311 1.00 145.31 ? 2208 ALA B CB 1 ATOM 8861 N N . ARG B 2 562 ? -44.507 -17.258 31.052 1.00 119.01 ? 2209 ARG B N 1 ATOM 8862 C CA . ARG B 2 562 ? -43.657 -18.334 31.469 1.00 123.13 ? 2209 ARG B CA 1 ATOM 8863 C C . ARG B 2 562 ? -42.179 -17.995 31.446 1.00 121.62 ? 2209 ARG B C 1 ATOM 8864 O O . ARG B 2 562 ? -41.537 -18.016 30.390 1.00 116.41 ? 2209 ARG B O 1 ATOM 8865 C CB . ARG B 2 562 ? -43.967 -19.574 30.637 1.00 142.50 ? 2209 ARG B CB 1 ATOM 8866 C CG . ARG B 2 562 ? -45.371 -20.109 30.871 1.00 145.08 ? 2209 ARG B CG 1 ATOM 8867 C CD . ARG B 2 562 ? -45.675 -21.344 30.036 1.00 148.34 ? 2209 ARG B CD 1 ATOM 8868 N NE . ARG B 2 562 ? -47.044 -21.757 30.285 1.00 147.86 ? 2209 ARG B NE 1 ATOM 8869 C CZ . ARG B 2 562 ? -47.388 -22.636 31.214 1.00 153.41 ? 2209 ARG B CZ 1 ATOM 8870 N NH1 . ARG B 2 562 ? -46.450 -23.223 31.956 1.00 141.70 ? 2209 ARG B NH1 1 ATOM 8871 N NH2 . ARG B 2 562 ? -48.672 -22.933 31.390 1.00 161.89 ? 2209 ARG B NH2 1 ATOM 8872 N N . LEU B 2 563 ? -41.665 -17.730 32.652 1.00 122.93 ? 2210 LEU B N 1 ATOM 8873 C CA . LEU B 2 563 ? -40.291 -17.268 32.927 1.00 120.22 ? 2210 LEU B CA 1 ATOM 8874 C C . LEU B 2 563 ? -39.307 -17.379 31.785 1.00 118.59 ? 2210 LEU B C 1 ATOM 8875 O O . LEU B 2 563 ? -38.573 -16.432 31.503 1.00 121.14 ? 2210 LEU B O 1 ATOM 8876 C CB . LEU B 2 563 ? -39.694 -17.932 34.174 1.00 120.65 ? 2210 LEU B CB 1 ATOM 8877 C CG . LEU B 2 563 ? -38.542 -17.142 34.809 1.00 124.69 ? 2210 LEU B CG 1 ATOM 8878 C CD1 . LEU B 2 563 ? -39.086 -15.905 35.515 1.00 116.80 ? 2210 LEU B CD1 1 ATOM 8879 C CD2 . LEU B 2 563 ? -37.686 -17.999 35.744 1.00 137.33 ? 2210 LEU B CD2 1 ATOM 8880 N N . HIS B 2 564 ? -39.244 -18.508 31.112 1.00 113.85 ? 2211 HIS B N 1 ATOM 8881 C CA . HIS B 2 564 ? -38.332 -18.439 30.018 1.00 122.97 ? 2211 HIS B CA 1 ATOM 8882 C C . HIS B 2 564 ? -38.908 -18.394 28.621 1.00 130.24 ? 2211 HIS B C 1 ATOM 8883 O O . HIS B 2 564 ? -38.371 -17.700 27.762 1.00 131.84 ? 2211 HIS B O 1 ATOM 8884 C CB . HIS B 2 564 ? -37.063 -19.240 30.256 1.00 135.53 ? 2211 HIS B CB 1 ATOM 8885 C CG . HIS B 2 564 ? -36.106 -18.531 31.171 1.00 141.23 ? 2211 HIS B CG 1 ATOM 8886 N ND1 . HIS B 2 564 ? -34.907 -18.004 30.739 1.00 147.73 ? 2211 HIS B ND1 1 ATOM 8887 C CD2 . HIS B 2 564 ? -36.204 -18.210 32.484 1.00 140.97 ? 2211 HIS B CD2 1 ATOM 8888 C CE1 . HIS B 2 564 ? -34.295 -17.418 31.753 1.00 145.23 ? 2211 HIS B CE1 1 ATOM 8889 N NE2 . HIS B 2 564 ? -35.062 -17.528 32.824 1.00 136.41 ? 2211 HIS B NE2 1 ATOM 8890 N N . LEU B 2 565 ? -40.027 -19.089 28.427 1.00 135.94 ? 2212 LEU B N 1 ATOM 8891 C CA . LEU B 2 565 ? -40.724 -19.136 27.134 1.00 141.08 ? 2212 LEU B CA 1 ATOM 8892 C C . LEU B 2 565 ? -40.202 -18.208 26.026 1.00 142.36 ? 2212 LEU B C 1 ATOM 8893 O O . LEU B 2 565 ? -40.404 -16.987 26.049 1.00 134.24 ? 2212 LEU B O 1 ATOM 8894 C CB . LEU B 2 565 ? -42.232 -18.920 27.319 1.00 136.99 ? 2212 LEU B CB 1 ATOM 8895 C CG . LEU B 2 565 ? -43.046 -18.373 26.127 1.00 144.36 ? 2212 LEU B CG 1 ATOM 8896 C CD1 . LEU B 2 565 ? -43.241 -19.327 24.951 1.00 151.69 ? 2212 LEU B CD1 1 ATOM 8897 C CD2 . LEU B 2 565 ? -44.395 -17.885 26.606 1.00 149.86 ? 2212 LEU B CD2 1 ATOM 8898 N N . GLN B 2 566 ? -39.529 -18.806 25.057 1.00 150.20 ? 2213 GLN B N 1 ATOM 8899 C CA . GLN B 2 566 ? -39.337 -18.161 23.781 1.00 160.83 ? 2213 GLN B CA 1 ATOM 8900 C C . GLN B 2 566 ? -40.465 -18.693 22.922 1.00 171.36 ? 2213 GLN B C 1 ATOM 8901 O O . GLN B 2 566 ? -40.681 -19.902 22.878 1.00 207.04 ? 2213 GLN B O 1 ATOM 8902 C CB . GLN B 2 566 ? -38.006 -18.573 23.182 1.00 169.32 ? 2213 GLN B CB 1 ATOM 8903 C CG . GLN B 2 566 ? -37.362 -17.476 22.365 1.00 176.06 ? 2213 GLN B CG 1 ATOM 8904 C CD . GLN B 2 566 ? -36.434 -16.607 23.200 1.00 185.01 ? 2213 GLN B CD 1 ATOM 8905 O OE1 . GLN B 2 566 ? -36.837 -15.967 24.193 1.00 182.23 ? 2213 GLN B OE1 1 ATOM 8906 N NE2 . GLN B 2 566 ? -35.171 -16.575 22.793 1.00 182.79 ? 2213 GLN B NE2 1 ATOM 8907 N N . GLY B 2 567 ? -41.197 -17.810 22.255 1.00 163.10 ? 2214 GLY B N 1 ATOM 8908 C CA . GLY B 2 567 ? -42.386 -18.225 21.506 1.00 167.66 ? 2214 GLY B CA 1 ATOM 8909 C C . GLY B 2 567 ? -42.722 -17.246 20.406 1.00 173.91 ? 2214 GLY B C 1 ATOM 8910 O O . GLY B 2 567 ? -41.908 -16.349 20.098 1.00 156.03 ? 2214 GLY B O 1 ATOM 8911 N N . ARG B 2 568 ? -43.913 -17.413 19.815 1.00 183.98 ? 2215 ARG B N 1 ATOM 8912 C CA . ARG B 2 568 ? -44.358 -16.534 18.718 1.00 194.57 ? 2215 ARG B CA 1 ATOM 8913 C C . ARG B 2 568 ? -44.662 -15.160 19.333 1.00 184.82 ? 2215 ARG B C 1 ATOM 8914 O O . ARG B 2 568 ? -43.899 -14.208 19.145 1.00 194.19 ? 2215 ARG B O 1 ATOM 8915 C CB . ARG B 2 568 ? -45.547 -17.137 17.917 1.00 205.50 ? 2215 ARG B CB 1 ATOM 8916 C CG . ARG B 2 568 ? -45.467 -17.041 16.374 1.00 195.66 ? 2215 ARG B CG 1 ATOM 8917 C CD . ARG B 2 568 ? -44.376 -17.925 15.760 1.00 206.63 ? 2215 ARG B CD 1 ATOM 8918 N NE . ARG B 2 568 ? -44.622 -19.378 15.876 1.00 237.83 ? 2215 ARG B NE 1 ATOM 8919 C CZ . ARG B 2 568 ? -44.130 -20.208 16.819 1.00 233.77 ? 2215 ARG B CZ 1 ATOM 8920 N NH1 . ARG B 2 568 ? -43.342 -19.780 17.801 1.00 219.54 ? 2215 ARG B NH1 1 ATOM 8921 N NH2 . ARG B 2 568 ? -44.436 -21.501 16.788 1.00 232.07 ? 2215 ARG B NH2 1 ATOM 8922 N N . SER B 2 569 ? -45.748 -15.071 20.094 1.00 164.52 ? 2216 SER B N 1 ATOM 8923 C CA . SER B 2 569 ? -45.975 -13.935 20.969 1.00 147.41 ? 2216 SER B CA 1 ATOM 8924 C C . SER B 2 569 ? -45.833 -14.523 22.366 1.00 141.55 ? 2216 SER B C 1 ATOM 8925 O O . SER B 2 569 ? -46.642 -15.348 22.796 1.00 145.65 ? 2216 SER B O 1 ATOM 8926 C CB . SER B 2 569 ? -47.356 -13.354 20.725 1.00 155.51 ? 2216 SER B CB 1 ATOM 8927 O OG . SER B 2 569 ? -48.308 -14.395 20.556 1.00 179.58 ? 2216 SER B OG 1 ATOM 8928 N N . ASN B 2 570 ? -44.775 -14.135 23.065 1.00 135.81 ? 2217 ASN B N 1 ATOM 8929 C CA . ASN B 2 570 ? -44.312 -14.954 24.184 1.00 137.80 ? 2217 ASN B CA 1 ATOM 8930 C C . ASN B 2 570 ? -44.359 -14.348 25.556 1.00 125.99 ? 2217 ASN B C 1 ATOM 8931 O O . ASN B 2 570 ? -43.324 -14.081 26.162 1.00 121.37 ? 2217 ASN B O 1 ATOM 8932 C CB . ASN B 2 570 ? -42.925 -15.591 23.915 1.00 156.37 ? 2217 ASN B CB 1 ATOM 8933 C CG . ASN B 2 570 ? -41.842 -14.579 23.568 1.00 153.91 ? 2217 ASN B CG 1 ATOM 8934 O OD1 . ASN B 2 570 ? -42.011 -13.377 23.749 1.00 157.33 ? 2217 ASN B OD1 1 ATOM 8935 N ND2 . ASN B 2 570 ? -40.715 -15.075 23.054 1.00 151.55 ? 2217 ASN B ND2 1 ATOM 8936 N N . ALA B 2 571 ? -45.573 -14.169 26.047 1.00 123.73 ? 2218 ALA B N 1 ATOM 8937 C CA . ALA B 2 571 ? -45.821 -13.609 27.357 1.00 126.57 ? 2218 ALA B CA 1 ATOM 8938 C C . ALA B 2 571 ? -47.281 -13.299 27.408 1.00 140.07 ? 2218 ALA B C 1 ATOM 8939 O O . ALA B 2 571 ? -47.987 -13.341 26.391 1.00 144.47 ? 2218 ALA B O 1 ATOM 8940 C CB . ALA B 2 571 ? -45.040 -12.323 27.577 1.00 124.76 ? 2218 ALA B CB 1 ATOM 8941 N N . TRP B 2 572 ? -47.732 -12.972 28.607 1.00 148.65 ? 2219 TRP B N 1 ATOM 8942 C CA . TRP B 2 572 ? -49.051 -12.428 28.768 1.00 142.19 ? 2219 TRP B CA 1 ATOM 8943 C C . TRP B 2 572 ? -48.972 -10.918 28.562 1.00 135.64 ? 2219 TRP B C 1 ATOM 8944 O O . TRP B 2 572 ? -47.957 -10.283 28.862 1.00 124.89 ? 2219 TRP B O 1 ATOM 8945 C CB . TRP B 2 572 ? -49.648 -12.806 30.130 1.00 132.73 ? 2219 TRP B CB 1 ATOM 8946 C CG . TRP B 2 572 ? -50.855 -12.030 30.417 1.00 131.81 ? 2219 TRP B CG 1 ATOM 8947 C CD1 . TRP B 2 572 ? -52.036 -12.047 29.722 1.00 137.20 ? 2219 TRP B CD1 1 ATOM 8948 C CD2 . TRP B 2 572 ? -51.008 -11.073 31.450 1.00 132.60 ? 2219 TRP B CD2 1 ATOM 8949 N NE1 . TRP B 2 572 ? -52.920 -11.154 30.271 1.00 137.42 ? 2219 TRP B NE1 1 ATOM 8950 C CE2 . TRP B 2 572 ? -52.317 -10.543 31.338 1.00 136.35 ? 2219 TRP B CE2 1 ATOM 8951 C CE3 . TRP B 2 572 ? -50.169 -10.612 32.474 1.00 132.90 ? 2219 TRP B CE3 1 ATOM 8952 C CZ2 . TRP B 2 572 ? -52.812 -9.578 32.215 1.00 138.68 ? 2219 TRP B CZ2 1 ATOM 8953 C CZ3 . TRP B 2 572 ? -50.656 -9.648 33.344 1.00 140.48 ? 2219 TRP B CZ3 1 ATOM 8954 C CH2 . TRP B 2 572 ? -51.971 -9.141 33.209 1.00 142.99 ? 2219 TRP B CH2 1 ATOM 8955 N N . ARG B 2 573 ? -50.034 -10.383 27.975 1.00 142.87 ? 2220 ARG B N 1 ATOM 8956 C CA . ARG B 2 573 ? -50.281 -8.957 27.885 1.00 151.29 ? 2220 ARG B CA 1 ATOM 8957 C C . ARG B 2 573 ? -51.788 -8.802 28.003 1.00 158.09 ? 2220 ARG B C 1 ATOM 8958 O O . ARG B 2 573 ? -52.521 -9.575 27.395 1.00 170.37 ? 2220 ARG B O 1 ATOM 8959 C CB . ARG B 2 573 ? -49.824 -8.410 26.532 1.00 157.37 ? 2220 ARG B CB 1 ATOM 8960 C CG . ARG B 2 573 ? -48.331 -8.514 26.243 1.00 157.85 ? 2220 ARG B CG 1 ATOM 8961 C CD . ARG B 2 573 ? -47.996 -7.841 24.924 1.00 152.41 ? 2220 ARG B CD 1 ATOM 8962 N NE . ARG B 2 573 ? -48.849 -6.678 24.722 1.00 156.06 ? 2220 ARG B NE 1 ATOM 8963 C CZ . ARG B 2 573 ? -48.925 -5.981 23.596 1.00 166.08 ? 2220 ARG B CZ 1 ATOM 8964 N NH1 . ARG B 2 573 ? -48.190 -6.303 22.538 1.00 161.13 ? 2220 ARG B NH1 1 ATOM 8965 N NH2 . ARG B 2 573 ? -49.745 -4.946 23.537 1.00 183.25 ? 2220 ARG B NH2 1 ATOM 8966 N N . PRO B 2 574 ? -52.264 -7.829 28.800 1.00 161.55 ? 2221 PRO B N 1 ATOM 8967 C CA . PRO B 2 574 ? -53.697 -7.507 28.792 1.00 181.57 ? 2221 PRO B CA 1 ATOM 8968 C C . PRO B 2 574 ? -54.070 -6.708 27.535 1.00 197.36 ? 2221 PRO B C 1 ATOM 8969 O O . PRO B 2 574 ? -53.164 -6.205 26.849 1.00 207.62 ? 2221 PRO B O 1 ATOM 8970 C CB . PRO B 2 574 ? -53.875 -6.657 30.051 1.00 174.55 ? 2221 PRO B CB 1 ATOM 8971 C CG . PRO B 2 574 ? -52.535 -6.068 30.305 1.00 159.18 ? 2221 PRO B CG 1 ATOM 8972 C CD . PRO B 2 574 ? -51.533 -7.076 29.831 1.00 154.72 ? 2221 PRO B CD 1 ATOM 8973 N N . GLN B 2 575 ? -55.367 -6.597 27.223 1.00 191.32 ? 2222 GLN B N 1 ATOM 8974 C CA . GLN B 2 575 ? -55.775 -5.873 26.010 1.00 190.40 ? 2222 GLN B CA 1 ATOM 8975 C C . GLN B 2 575 ? -55.653 -4.355 26.142 1.00 193.97 ? 2222 GLN B C 1 ATOM 8976 O O . GLN B 2 575 ? -54.875 -3.747 25.412 1.00 211.14 ? 2222 GLN B O 1 ATOM 8977 C CB . GLN B 2 575 ? -57.133 -6.315 25.469 1.00 189.12 ? 2222 GLN B CB 1 ATOM 8978 C CG . GLN B 2 575 ? -58.132 -6.685 26.535 1.00 202.53 ? 2222 GLN B CG 1 ATOM 8979 C CD . GLN B 2 575 ? -59.558 -6.519 26.066 1.00 216.29 ? 2222 GLN B CD 1 ATOM 8980 O OE1 . GLN B 2 575 ? -60.430 -7.317 26.421 1.00 215.46 ? 2222 GLN B OE1 1 ATOM 8981 N NE2 . GLN B 2 575 ? -59.811 -5.472 25.272 1.00 213.36 ? 2222 GLN B NE2 1 ATOM 8982 N N . VAL B 2 576 ? -56.387 -3.731 27.056 1.00 188.89 ? 2223 VAL B N 1 ATOM 8983 C CA . VAL B 2 576 ? -56.094 -2.325 27.383 1.00 201.64 ? 2223 VAL B CA 1 ATOM 8984 C C . VAL B 2 576 ? -55.069 -2.372 28.530 1.00 179.67 ? 2223 VAL B C 1 ATOM 8985 O O . VAL B 2 576 ? -54.898 -3.430 29.145 1.00 167.10 ? 2223 VAL B O 1 ATOM 8986 C CB . VAL B 2 576 ? -57.377 -1.501 27.748 1.00 237.02 ? 2223 VAL B CB 1 ATOM 8987 C CG1 . VAL B 2 576 ? -57.119 0.008 27.733 1.00 237.07 ? 2223 VAL B CG1 1 ATOM 8988 C CG2 . VAL B 2 576 ? -58.534 -1.825 26.805 1.00 252.50 ? 2223 VAL B CG2 1 ATOM 8989 N N . ASN B 2 577 ? -54.379 -1.258 28.800 1.00 166.94 ? 2224 ASN B N 1 ATOM 8990 C CA . ASN B 2 577 ? -53.449 -1.179 29.942 1.00 155.94 ? 2224 ASN B CA 1 ATOM 8991 C C . ASN B 2 577 ? -54.043 -0.544 31.205 1.00 151.97 ? 2224 ASN B C 1 ATOM 8992 O O . ASN B 2 577 ? -54.248 0.666 31.262 1.00 154.99 ? 2224 ASN B O 1 ATOM 8993 C CB . ASN B 2 577 ? -52.151 -0.474 29.547 1.00 155.22 ? 2224 ASN B CB 1 ATOM 8994 C CG . ASN B 2 577 ? -51.576 -1.011 28.261 1.00 157.59 ? 2224 ASN B CG 1 ATOM 8995 O OD1 . ASN B 2 577 ? -52.176 -0.832 27.205 1.00 171.15 ? 2224 ASN B OD1 1 ATOM 8996 N ND2 . ASN B 2 577 ? -50.416 -1.676 28.335 1.00 143.59 ? 2224 ASN B ND2 1 ATOM 8997 N N . ASN B 2 578 ? -54.296 -1.374 32.214 1.00 147.54 ? 2225 ASN B N 1 ATOM 8998 C CA . ASN B 2 578 ? -54.988 -0.961 33.429 1.00 149.18 ? 2225 ASN B CA 1 ATOM 8999 C C . ASN B 2 578 ? -54.172 -1.094 34.665 1.00 145.89 ? 2225 ASN B C 1 ATOM 9000 O O . ASN B 2 578 ? -53.520 -2.109 34.858 1.00 145.66 ? 2225 ASN B O 1 ATOM 9001 C CB . ASN B 2 578 ? -56.191 -1.839 33.665 1.00 169.46 ? 2225 ASN B CB 1 ATOM 9002 C CG . ASN B 2 578 ? -57.412 -1.327 32.978 1.00 193.62 ? 2225 ASN B CG 1 ATOM 9003 O OD1 . ASN B 2 578 ? -57.344 -0.392 32.169 1.00 200.66 ? 2225 ASN B OD1 1 ATOM 9004 N ND2 . ASN B 2 578 ? -58.555 -1.935 33.291 1.00 215.23 ? 2225 ASN B ND2 1 ATOM 9005 N N . PRO B 2 579 ? -54.236 -0.088 35.535 1.00 153.02 ? 2226 PRO B N 1 ATOM 9006 C CA . PRO B 2 579 ? -53.603 -0.217 36.842 1.00 166.38 ? 2226 PRO B CA 1 ATOM 9007 C C . PRO B 2 579 ? -54.152 -1.392 37.672 1.00 179.13 ? 2226 PRO B C 1 ATOM 9008 O O . PRO B 2 579 ? -53.377 -2.091 38.339 1.00 177.92 ? 2226 PRO B O 1 ATOM 9009 C CB . PRO B 2 579 ? -53.899 1.137 37.503 1.00 182.80 ? 2226 PRO B CB 1 ATOM 9010 C CG . PRO B 2 579 ? -53.999 2.099 36.354 1.00 175.55 ? 2226 PRO B CG 1 ATOM 9011 C CD . PRO B 2 579 ? -54.623 1.306 35.233 1.00 165.00 ? 2226 PRO B CD 1 ATOM 9012 N N . LYS B 2 580 ? -55.465 -1.614 37.626 1.00 194.97 ? 2227 LYS B N 1 ATOM 9013 C CA . LYS B 2 580 ? -56.067 -2.726 38.368 1.00 204.15 ? 2227 LYS B CA 1 ATOM 9014 C C . LYS B 2 580 ? -56.362 -3.886 37.427 1.00 184.21 ? 2227 LYS B C 1 ATOM 9015 O O . LYS B 2 580 ? -57.515 -4.290 37.216 1.00 183.88 ? 2227 LYS B O 1 ATOM 9016 C CB . LYS B 2 580 ? -57.303 -2.286 39.182 1.00 231.03 ? 2227 LYS B CB 1 ATOM 9017 C CG . LYS B 2 580 ? -57.021 -1.457 40.447 1.00 233.61 ? 2227 LYS B CG 1 ATOM 9018 C CD . LYS B 2 580 ? -55.857 -1.995 41.287 1.00 231.03 ? 2227 LYS B CD 1 ATOM 9019 C CE . LYS B 2 580 ? -56.169 -3.303 41.999 1.00 215.48 ? 2227 LYS B CE 1 ATOM 9020 N NZ . LYS B 2 580 ? -57.172 -3.075 43.069 1.00 219.71 ? 2227 LYS B NZ 1 ATOM 9021 N N . GLU B 2 581 ? -55.275 -4.389 36.854 1.00 160.50 ? 2228 GLU B N 1 ATOM 9022 C CA . GLU B 2 581 ? -55.295 -5.544 35.986 1.00 152.59 ? 2228 GLU B CA 1 ATOM 9023 C C . GLU B 2 581 ? -54.577 -6.647 36.738 1.00 152.73 ? 2228 GLU B C 1 ATOM 9024 O O . GLU B 2 581 ? -54.004 -6.367 37.791 1.00 155.73 ? 2228 GLU B O 1 ATOM 9025 C CB . GLU B 2 581 ? -54.589 -5.217 34.677 1.00 141.66 ? 2228 GLU B CB 1 ATOM 9026 C CG . GLU B 2 581 ? -55.098 -6.002 33.482 1.00 144.49 ? 2228 GLU B CG 1 ATOM 9027 C CD . GLU B 2 581 ? -56.497 -5.602 33.018 1.00 151.63 ? 2228 GLU B CD 1 ATOM 9028 O OE1 . GLU B 2 581 ? -57.292 -5.053 33.820 1.00 160.24 ? 2228 GLU B OE1 1 ATOM 9029 O OE2 . GLU B 2 581 ? -56.810 -5.853 31.831 1.00 149.70 ? 2228 GLU B OE2 1 ATOM 9030 N N . TRP B 2 582 ? -54.621 -7.883 36.221 1.00 155.13 ? 2229 TRP B N 1 ATOM 9031 C CA . TRP B 2 582 ? -54.046 -9.066 36.911 1.00 159.04 ? 2229 TRP B CA 1 ATOM 9032 C C . TRP B 2 582 ? -53.799 -10.303 36.034 1.00 153.01 ? 2229 TRP B C 1 ATOM 9033 O O . TRP B 2 582 ? -54.298 -10.393 34.911 1.00 162.44 ? 2229 TRP B O 1 ATOM 9034 C CB . TRP B 2 582 ? -54.910 -9.477 38.119 1.00 168.88 ? 2229 TRP B CB 1 ATOM 9035 C CG . TRP B 2 582 ? -56.386 -9.676 37.819 1.00 174.13 ? 2229 TRP B CG 1 ATOM 9036 C CD1 . TRP B 2 582 ? -57.397 -8.807 38.105 1.00 183.28 ? 2229 TRP B CD1 1 ATOM 9037 C CD2 . TRP B 2 582 ? -57.005 -10.820 37.196 1.00 174.14 ? 2229 TRP B CD2 1 ATOM 9038 N NE1 . TRP B 2 582 ? -58.602 -9.327 37.692 1.00 195.77 ? 2229 TRP B NE1 1 ATOM 9039 C CE2 . TRP B 2 582 ? -58.389 -10.562 37.134 1.00 180.55 ? 2229 TRP B CE2 1 ATOM 9040 C CE3 . TRP B 2 582 ? -56.524 -12.031 36.679 1.00 171.31 ? 2229 TRP B CE3 1 ATOM 9041 C CZ2 . TRP B 2 582 ? -59.299 -11.473 36.575 1.00 181.78 ? 2229 TRP B CZ2 1 ATOM 9042 C CZ3 . TRP B 2 582 ? -57.436 -12.939 36.133 1.00 167.72 ? 2229 TRP B CZ3 1 ATOM 9043 C CH2 . TRP B 2 582 ? -58.801 -12.650 36.082 1.00 168.63 ? 2229 TRP B CH2 1 ATOM 9044 N N . LEU B 2 583 ? -53.036 -11.256 36.566 1.00 137.29 ? 2230 LEU B N 1 ATOM 9045 C CA . LEU B 2 583 ? -52.857 -12.552 35.927 1.00 129.51 ? 2230 LEU B CA 1 ATOM 9046 C C . LEU B 2 583 ? -52.956 -13.562 37.018 1.00 130.57 ? 2230 LEU B C 1 ATOM 9047 O O . LEU B 2 583 ? -52.512 -13.304 38.145 1.00 120.14 ? 2230 LEU B O 1 ATOM 9048 C CB . LEU B 2 583 ? -51.486 -12.669 35.283 1.00 129.46 ? 2230 LEU B CB 1 ATOM 9049 C CG . LEU B 2 583 ? -51.066 -14.048 34.777 1.00 125.96 ? 2230 LEU B CG 1 ATOM 9050 C CD1 . LEU B 2 583 ? -51.297 -14.134 33.286 1.00 132.06 ? 2230 LEU B CD1 1 ATOM 9051 C CD2 . LEU B 2 583 ? -49.601 -14.299 35.076 1.00 125.12 ? 2230 LEU B CD2 1 ATOM 9052 N N . GLN B 2 584 ? -53.509 -14.720 36.674 1.00 144.41 ? 2231 GLN B N 1 ATOM 9053 C CA . GLN B 2 584 ? -53.936 -15.682 37.686 1.00 160.51 ? 2231 GLN B CA 1 ATOM 9054 C C . GLN B 2 584 ? -53.584 -17.125 37.425 1.00 157.70 ? 2231 GLN B C 1 ATOM 9055 O O . GLN B 2 584 ? -53.999 -17.750 36.431 1.00 143.77 ? 2231 GLN B O 1 ATOM 9056 C CB . GLN B 2 584 ? -55.439 -15.573 37.950 1.00 176.59 ? 2231 GLN B CB 1 ATOM 9057 C CG . GLN B 2 584 ? -55.943 -16.347 39.163 1.00 169.98 ? 2231 GLN B CG 1 ATOM 9058 C CD . GLN B 2 584 ? -57.377 -16.802 38.979 1.00 179.73 ? 2231 GLN B CD 1 ATOM 9059 O OE1 . GLN B 2 584 ? -57.835 -16.995 37.852 1.00 178.09 ? 2231 GLN B OE1 1 ATOM 9060 N NE2 . GLN B 2 584 ? -58.094 -16.982 40.083 1.00 193.31 ? 2231 GLN B NE2 1 ATOM 9061 N N . VAL B 2 585 ? -52.863 -17.633 38.413 1.00 164.22 ? 2232 VAL B N 1 ATOM 9062 C CA . VAL B 2 585 ? -52.372 -18.989 38.485 1.00 177.04 ? 2232 VAL B CA 1 ATOM 9063 C C . VAL B 2 585 ? -53.151 -19.772 39.562 1.00 185.25 ? 2232 VAL B C 1 ATOM 9064 O O . VAL B 2 585 ? -53.171 -19.400 40.742 1.00 189.00 ? 2232 VAL B O 1 ATOM 9065 C CB . VAL B 2 585 ? -50.846 -18.961 38.771 1.00 171.93 ? 2232 VAL B CB 1 ATOM 9066 C CG1 . VAL B 2 585 ? -50.507 -17.878 39.787 1.00 169.50 ? 2232 VAL B CG1 1 ATOM 9067 C CG2 . VAL B 2 585 ? -50.319 -20.313 39.223 1.00 176.33 ? 2232 VAL B CG2 1 ATOM 9068 N N . ASP B 2 586 ? -53.819 -20.840 39.137 1.00 186.33 ? 2233 ASP B N 1 ATOM 9069 C CA . ASP B 2 586 ? -54.444 -21.767 40.068 1.00 195.40 ? 2233 ASP B CA 1 ATOM 9070 C C . ASP B 2 586 ? -53.440 -22.864 40.402 1.00 198.11 ? 2233 ASP B C 1 ATOM 9071 O O . ASP B 2 586 ? -53.232 -23.775 39.597 1.00 210.03 ? 2233 ASP B O 1 ATOM 9072 C CB . ASP B 2 586 ? -55.716 -22.377 39.449 1.00 207.40 ? 2233 ASP B CB 1 ATOM 9073 C CG . ASP B 2 586 ? -56.183 -23.647 40.170 1.00 214.95 ? 2233 ASP B CG 1 ATOM 9074 O OD1 . ASP B 2 586 ? -56.413 -23.590 41.398 1.00 214.22 ? 2233 ASP B OD1 1 ATOM 9075 O OD2 . ASP B 2 586 ? -56.306 -24.703 39.506 1.00 210.07 ? 2233 ASP B OD2 1 ATOM 9076 N N . PHE B 2 587 ? -52.795 -22.781 41.565 1.00 187.53 ? 2234 PHE B N 1 ATOM 9077 C CA . PHE B 2 587 ? -52.057 -23.942 42.049 1.00 180.70 ? 2234 PHE B CA 1 ATOM 9078 C C . PHE B 2 587 ? -53.104 -25.024 42.222 1.00 195.10 ? 2234 PHE B C 1 ATOM 9079 O O . PHE B 2 587 ? -54.185 -24.773 42.766 1.00 201.81 ? 2234 PHE B O 1 ATOM 9080 C CB . PHE B 2 587 ? -51.361 -23.687 43.386 1.00 169.29 ? 2234 PHE B CB 1 ATOM 9081 C CG . PHE B 2 587 ? -50.292 -22.642 43.330 1.00 162.41 ? 2234 PHE B CG 1 ATOM 9082 C CD1 . PHE B 2 587 ? -49.482 -22.508 42.211 1.00 153.88 ? 2234 PHE B CD1 1 ATOM 9083 C CD2 . PHE B 2 587 ? -50.078 -21.797 44.418 1.00 171.70 ? 2234 PHE B CD2 1 ATOM 9084 C CE1 . PHE B 2 587 ? -48.494 -21.537 42.169 1.00 151.40 ? 2234 PHE B CE1 1 ATOM 9085 C CE2 . PHE B 2 587 ? -49.086 -20.822 44.387 1.00 163.29 ? 2234 PHE B CE2 1 ATOM 9086 C CZ . PHE B 2 587 ? -48.296 -20.693 43.258 1.00 156.15 ? 2234 PHE B CZ 1 ATOM 9087 N N . GLN B 2 588 ? -52.809 -26.217 41.730 1.00 201.92 ? 2235 GLN B N 1 ATOM 9088 C CA . GLN B 2 588 ? -53.733 -27.324 41.908 1.00 208.08 ? 2235 GLN B CA 1 ATOM 9089 C C . GLN B 2 588 ? -54.102 -27.466 43.401 1.00 197.06 ? 2235 GLN B C 1 ATOM 9090 O O . GLN B 2 588 ? -55.267 -27.330 43.781 1.00 183.48 ? 2235 GLN B O 1 ATOM 9091 C CB . GLN B 2 588 ? -53.149 -28.618 41.309 1.00 225.56 ? 2235 GLN B CB 1 ATOM 9092 C CG . GLN B 2 588 ? -53.069 -28.637 39.778 1.00 228.52 ? 2235 GLN B CG 1 ATOM 9093 C CD . GLN B 2 588 ? -54.438 -28.678 39.087 1.00 228.45 ? 2235 GLN B CD 1 ATOM 9094 O OE1 . GLN B 2 588 ? -54.848 -29.719 38.571 1.00 232.98 ? 2235 GLN B OE1 1 ATOM 9095 N NE2 . GLN B 2 588 ? -55.146 -27.544 39.072 1.00 207.19 ? 2235 GLN B NE2 1 ATOM 9096 N N . LYS B 2 589 ? -53.088 -27.671 44.240 1.00 194.18 ? 2236 LYS B N 1 ATOM 9097 C CA . LYS B 2 589 ? -53.270 -27.921 45.672 1.00 184.18 ? 2236 LYS B CA 1 ATOM 9098 C C . LYS B 2 589 ? -53.075 -26.619 46.501 1.00 164.78 ? 2236 LYS B C 1 ATOM 9099 O O . LYS B 2 589 ? -53.306 -25.516 46.001 1.00 147.78 ? 2236 LYS B O 1 ATOM 9100 C CB . LYS B 2 589 ? -52.317 -29.058 46.147 1.00 198.89 ? 2236 LYS B CB 1 ATOM 9101 C CG . LYS B 2 589 ? -51.764 -30.053 45.095 1.00 195.96 ? 2236 LYS B CG 1 ATOM 9102 C CD . LYS B 2 589 ? -52.791 -30.975 44.424 1.00 201.20 ? 2236 LYS B CD 1 ATOM 9103 C CE . LYS B 2 589 ? -53.604 -31.821 45.401 1.00 209.08 ? 2236 LYS B CE 1 ATOM 9104 N NZ . LYS B 2 589 ? -52.952 -33.103 45.786 1.00 211.02 ? 2236 LYS B NZ 1 ATOM 9105 N N . THR B 2 590 ? -52.669 -26.755 47.764 1.00 160.77 ? 2237 THR B N 1 ATOM 9106 C CA . THR B 2 590 ? -52.218 -25.615 48.563 1.00 158.53 ? 2237 THR B CA 1 ATOM 9107 C C . THR B 2 590 ? -50.697 -25.591 48.573 1.00 166.42 ? 2237 THR B C 1 ATOM 9108 O O . THR B 2 590 ? -50.040 -26.600 48.891 1.00 166.97 ? 2237 THR B O 1 ATOM 9109 C CB . THR B 2 590 ? -52.708 -25.671 50.020 1.00 156.03 ? 2237 THR B CB 1 ATOM 9110 O OG1 . THR B 2 590 ? -54.098 -26.006 50.048 1.00 162.50 ? 2237 THR B OG1 1 ATOM 9111 C CG2 . THR B 2 590 ? -52.482 -24.325 50.723 1.00 149.69 ? 2237 THR B CG2 1 ATOM 9112 N N . MET B 2 591 ? -50.142 -24.433 48.226 1.00 166.83 ? 2238 MET B N 1 ATOM 9113 C CA . MET B 2 591 ? -48.694 -24.283 48.129 1.00 160.68 ? 2238 MET B CA 1 ATOM 9114 C C . MET B 2 591 ? -48.154 -23.183 49.059 1.00 149.89 ? 2238 MET B C 1 ATOM 9115 O O . MET B 2 591 ? -48.815 -22.178 49.301 1.00 138.15 ? 2238 MET B O 1 ATOM 9116 C CB . MET B 2 591 ? -48.266 -24.031 46.670 1.00 160.40 ? 2238 MET B CB 1 ATOM 9117 C CG . MET B 2 591 ? -48.817 -24.993 45.611 1.00 161.84 ? 2238 MET B CG 1 ATOM 9118 S SD . MET B 2 591 ? -48.208 -26.696 45.659 1.00 178.20 ? 2238 MET B SD 1 ATOM 9119 C CE . MET B 2 591 ? -48.483 -27.252 43.964 1.00 171.83 ? 2238 MET B CE 1 ATOM 9120 N N . LYS B 2 592 ? -46.959 -23.414 49.598 1.00 151.16 ? 2239 LYS B N 1 ATOM 9121 C CA . LYS B 2 592 ? -46.198 -22.411 50.340 1.00 149.63 ? 2239 LYS B CA 1 ATOM 9122 C C . LYS B 2 592 ? -45.321 -21.656 49.324 1.00 154.45 ? 2239 LYS B C 1 ATOM 9123 O O . LYS B 2 592 ? -44.525 -22.274 48.609 1.00 158.36 ? 2239 LYS B O 1 ATOM 9124 C CB . LYS B 2 592 ? -45.334 -23.094 51.418 1.00 143.96 ? 2239 LYS B CB 1 ATOM 9125 C CG . LYS B 2 592 ? -44.642 -22.168 52.415 1.00 141.12 ? 2239 LYS B CG 1 ATOM 9126 C CD . LYS B 2 592 ? -43.526 -22.895 53.164 1.00 146.43 ? 2239 LYS B CD 1 ATOM 9127 C CE . LYS B 2 592 ? -42.652 -21.934 53.973 1.00 154.82 ? 2239 LYS B CE 1 ATOM 9128 N NZ . LYS B 2 592 ? -41.304 -22.460 54.363 1.00 154.97 ? 2239 LYS B NZ 1 ATOM 9129 N N . VAL B 2 593 ? -45.476 -20.334 49.257 1.00 153.20 ? 2240 VAL B N 1 ATOM 9130 C CA . VAL B 2 593 ? -44.756 -19.492 48.289 1.00 140.64 ? 2240 VAL B CA 1 ATOM 9131 C C . VAL B 2 593 ? -43.536 -18.803 48.984 1.00 140.64 ? 2240 VAL B C 1 ATOM 9132 O O . VAL B 2 593 ? -43.680 -18.293 50.099 1.00 133.54 ? 2240 VAL B O 1 ATOM 9133 C CB . VAL B 2 593 ? -45.755 -18.509 47.573 1.00 133.01 ? 2240 VAL B CB 1 ATOM 9134 C CG1 . VAL B 2 593 ? -45.082 -17.715 46.459 1.00 125.73 ? 2240 VAL B CG1 1 ATOM 9135 C CG2 . VAL B 2 593 ? -46.977 -19.256 47.009 1.00 118.38 ? 2240 VAL B CG2 1 ATOM 9136 N N . THR B 2 594 ? -42.343 -18.872 48.362 1.00 148.70 ? 2241 THR B N 1 ATOM 9137 C CA . THR B 2 594 ? -41.130 -18.062 48.733 1.00 164.45 ? 2241 THR B CA 1 ATOM 9138 C C . THR B 2 594 ? -41.214 -16.681 48.101 1.00 159.11 ? 2241 THR B C 1 ATOM 9139 O O . THR B 2 594 ? -41.010 -15.666 48.766 1.00 159.24 ? 2241 THR B O 1 ATOM 9140 C CB . THR B 2 594 ? -39.769 -18.724 48.302 1.00 175.26 ? 2241 THR B CB 1 ATOM 9141 O OG1 . THR B 2 594 ? -39.387 -19.710 49.269 1.00 184.94 ? 2241 THR B OG1 1 ATOM 9142 C CG2 . THR B 2 594 ? -38.554 -17.680 48.087 1.00 147.10 ? 2241 THR B CG2 1 ATOM 9143 N N . GLY B 2 595 ? -41.505 -16.667 46.805 1.00 147.78 ? 2242 GLY B N 1 ATOM 9144 C CA . GLY B 2 595 ? -41.648 -15.437 46.064 1.00 142.42 ? 2242 GLY B CA 1 ATOM 9145 C C . GLY B 2 595 ? -41.854 -15.696 44.591 1.00 132.66 ? 2242 GLY B C 1 ATOM 9146 O O . GLY B 2 595 ? -42.101 -16.835 44.170 1.00 124.91 ? 2242 GLY B O 1 ATOM 9147 N N . VAL B 2 596 ? -41.732 -14.623 43.816 1.00 120.81 ? 2243 VAL B N 1 ATOM 9148 C CA . VAL B 2 596 ? -42.007 -14.645 42.389 1.00 115.14 ? 2243 VAL B CA 1 ATOM 9149 C C . VAL B 2 596 ? -40.859 -14.015 41.605 1.00 121.99 ? 2243 VAL B C 1 ATOM 9150 O O . VAL B 2 596 ? -40.281 -13.007 42.038 1.00 125.62 ? 2243 VAL B O 1 ATOM 9151 C CB . VAL B 2 596 ? -43.298 -13.871 42.093 1.00 112.42 ? 2243 VAL B CB 1 ATOM 9152 C CG1 . VAL B 2 596 ? -44.468 -14.818 41.906 1.00 115.52 ? 2243 VAL B CG1 1 ATOM 9153 C CG2 . VAL B 2 596 ? -43.576 -12.896 43.224 1.00 111.51 ? 2243 VAL B CG2 1 ATOM 9154 N N . THR B 2 597 ? -40.525 -14.631 40.468 1.00 123.14 ? 2244 THR B N 1 ATOM 9155 C CA . THR B 2 597 ? -39.541 -14.099 39.521 1.00 120.93 ? 2244 THR B CA 1 ATOM 9156 C C . THR B 2 597 ? -40.395 -13.530 38.402 1.00 122.53 ? 2244 THR B C 1 ATOM 9157 O O . THR B 2 597 ? -41.274 -14.242 37.888 1.00 118.63 ? 2244 THR B O 1 ATOM 9158 C CB . THR B 2 597 ? -38.648 -15.225 38.931 1.00 119.35 ? 2244 THR B CB 1 ATOM 9159 O OG1 . THR B 2 597 ? -38.907 -16.467 39.600 1.00 124.52 ? 2244 THR B OG1 1 ATOM 9160 C CG2 . THR B 2 597 ? -37.149 -14.896 39.010 1.00 112.34 ? 2244 THR B CG2 1 ATOM 9161 N N . THR B 2 598 ? -40.186 -12.250 38.060 1.00 120.77 ? 2245 THR B N 1 ATOM 9162 C CA . THR B 2 598 ? -40.930 -11.612 36.941 1.00 119.38 ? 2245 THR B CA 1 ATOM 9163 C C . THR B 2 598 ? -40.048 -11.289 35.712 1.00 117.26 ? 2245 THR B C 1 ATOM 9164 O O . THR B 2 598 ? -38.828 -11.438 35.769 1.00 108.31 ? 2245 THR B O 1 ATOM 9165 C CB . THR B 2 598 ? -41.842 -10.424 37.372 1.00 112.27 ? 2245 THR B CB 1 ATOM 9166 O OG1 . THR B 2 598 ? -41.051 -9.341 37.870 1.00 112.04 ? 2245 THR B OG1 1 ATOM 9167 C CG2 . THR B 2 598 ? -42.886 -10.869 38.430 1.00 106.24 ? 2245 THR B CG2 1 ATOM 9168 N N . GLN B 2 599 ? -40.680 -10.862 34.612 1.00 123.52 ? 2246 GLN B N 1 ATOM 9169 C CA . GLN B 2 599 ? -40.014 -10.715 33.304 1.00 120.23 ? 2246 GLN B CA 1 ATOM 9170 C C . GLN B 2 599 ? -40.717 -9.714 32.365 1.00 126.07 ? 2246 GLN B C 1 ATOM 9171 O O . GLN B 2 599 ? -41.843 -9.241 32.630 1.00 130.78 ? 2246 GLN B O 1 ATOM 9172 C CB . GLN B 2 599 ? -39.901 -12.083 32.634 1.00 113.01 ? 2246 GLN B CB 1 ATOM 9173 C CG . GLN B 2 599 ? -38.902 -12.173 31.496 1.00 122.32 ? 2246 GLN B CG 1 ATOM 9174 C CD . GLN B 2 599 ? -38.087 -13.456 31.542 1.00 129.64 ? 2246 GLN B CD 1 ATOM 9175 O OE1 . GLN B 2 599 ? -37.968 -14.079 32.593 1.00 137.85 ? 2246 GLN B OE1 1 ATOM 9176 N NE2 . GLN B 2 599 ? -37.511 -13.849 30.409 1.00 131.32 ? 2246 GLN B NE2 1 ATOM 9177 N N . GLY B 2 600 ? -40.024 -9.372 31.283 1.00 116.61 ? 2247 GLY B N 1 ATOM 9178 C CA . GLY B 2 600 ? -40.600 -8.566 30.219 1.00 117.47 ? 2247 GLY B CA 1 ATOM 9179 C C . GLY B 2 600 ? -40.605 -9.340 28.917 1.00 123.45 ? 2247 GLY B C 1 ATOM 9180 O O . GLY B 2 600 ? -40.613 -10.573 28.937 1.00 129.29 ? 2247 GLY B O 1 ATOM 9181 N N . VAL B 2 601 ? -40.613 -8.615 27.794 1.00 123.05 ? 2248 VAL B N 1 ATOM 9182 C CA . VAL B 2 601 ? -40.520 -9.182 26.428 1.00 119.95 ? 2248 VAL B CA 1 ATOM 9183 C C . VAL B 2 601 ? -39.982 -8.158 25.455 1.00 126.51 ? 2248 VAL B C 1 ATOM 9184 O O . VAL B 2 601 ? -40.086 -6.961 25.711 1.00 135.96 ? 2248 VAL B O 1 ATOM 9185 C CB . VAL B 2 601 ? -41.880 -9.627 25.838 1.00 113.97 ? 2248 VAL B CB 1 ATOM 9186 C CG1 . VAL B 2 601 ? -42.045 -11.116 25.981 1.00 123.73 ? 2248 VAL B CG1 1 ATOM 9187 C CG2 . VAL B 2 601 ? -43.062 -8.881 26.443 1.00 107.26 ? 2248 VAL B CG2 1 ATOM 9188 N N . LYS B 2 602 ? -39.413 -8.612 24.343 1.00 127.39 ? 2249 LYS B N 1 ATOM 9189 C CA . LYS B 2 602 ? -39.173 -7.701 23.237 1.00 147.48 ? 2249 LYS B CA 1 ATOM 9190 C C . LYS B 2 602 ? -40.106 -8.096 22.099 1.00 159.87 ? 2249 LYS B C 1 ATOM 9191 O O . LYS B 2 602 ? -40.317 -9.291 21.863 1.00 171.79 ? 2249 LYS B O 1 ATOM 9192 C CB . LYS B 2 602 ? -37.694 -7.685 22.821 1.00 169.94 ? 2249 LYS B CB 1 ATOM 9193 C CG . LYS B 2 602 ? -37.425 -6.954 21.503 1.00 203.01 ? 2249 LYS B CG 1 ATOM 9194 C CD . LYS B 2 602 ? -36.390 -5.840 21.599 1.00 201.87 ? 2249 LYS B CD 1 ATOM 9195 C CE . LYS B 2 602 ? -36.443 -4.970 20.348 1.00 198.64 ? 2249 LYS B CE 1 ATOM 9196 N NZ . LYS B 2 602 ? -36.473 -3.505 20.634 1.00 184.67 ? 2249 LYS B NZ 1 ATOM 9197 N N . SER B 2 603 ? -40.676 -7.105 21.410 1.00 166.12 ? 2250 SER B N 1 ATOM 9198 C CA . SER B 2 603 ? -41.657 -7.392 20.354 1.00 176.77 ? 2250 SER B CA 1 ATOM 9199 C C . SER B 2 603 ? -41.280 -6.879 18.963 1.00 172.01 ? 2250 SER B C 1 ATOM 9200 O O . SER B 2 603 ? -42.153 -6.632 18.102 1.00 146.42 ? 2250 SER B O 1 ATOM 9201 C CB . SER B 2 603 ? -43.027 -6.873 20.754 1.00 188.37 ? 2250 SER B CB 1 ATOM 9202 O OG . SER B 2 603 ? -44.021 -7.715 20.207 1.00 205.53 ? 2250 SER B OG 1 ATOM 9203 N N . LEU B 2 604 ? -39.967 -6.747 18.759 1.00 181.59 ? 2251 LEU B N 1 ATOM 9204 C CA . LEU B 2 604 ? -39.389 -6.100 17.575 1.00 192.24 ? 2251 LEU B CA 1 ATOM 9205 C C . LEU B 2 604 ? -39.855 -4.603 17.574 1.00 182.00 ? 2251 LEU B C 1 ATOM 9206 O O . LEU B 2 604 ? -39.123 -3.647 17.178 1.00 144.17 ? 2251 LEU B O 1 ATOM 9207 C CB . LEU B 2 604 ? -39.739 -6.907 16.287 1.00 194.72 ? 2251 LEU B CB 1 ATOM 9208 C CG . LEU B 2 604 ? -39.125 -8.259 15.798 1.00 174.86 ? 2251 LEU B CG 1 ATOM 9209 C CD1 . LEU B 2 604 ? -37.881 -8.055 14.912 1.00 158.65 ? 2251 LEU B CD1 1 ATOM 9210 C CD2 . LEU B 2 604 ? -38.906 -9.316 16.895 1.00 162.46 ? 2251 LEU B CD2 1 ATOM 9211 N N . LEU B 2 605 ? -41.086 -4.426 18.052 1.00 176.40 ? 2252 LEU B N 1 ATOM 9212 C CA . LEU B 2 605 ? -41.532 -3.168 18.573 1.00 183.41 ? 2252 LEU B CA 1 ATOM 9213 C C . LEU B 2 605 ? -40.453 -2.667 19.523 1.00 182.96 ? 2252 LEU B C 1 ATOM 9214 O O . LEU B 2 605 ? -39.323 -2.313 19.106 1.00 161.70 ? 2252 LEU B O 1 ATOM 9215 C CB . LEU B 2 605 ? -42.838 -3.369 19.353 1.00 186.24 ? 2252 LEU B CB 1 ATOM 9216 C CG . LEU B 2 605 ? -44.190 -3.112 18.682 1.00 199.32 ? 2252 LEU B CG 1 ATOM 9217 C CD1 . LEU B 2 605 ? -45.315 -3.133 19.720 1.00 191.74 ? 2252 LEU B CD1 1 ATOM 9218 C CD2 . LEU B 2 605 ? -44.193 -1.794 17.905 1.00 204.99 ? 2252 LEU B CD2 1 ATOM 9219 N N . THR B 2 606 ? -40.823 -2.654 20.803 1.00 179.92 ? 2253 THR B N 1 ATOM 9220 C CA . THR B 2 606 ? -39.948 -2.224 21.874 1.00 183.14 ? 2253 THR B CA 1 ATOM 9221 C C . THR B 2 606 ? -40.028 -3.267 22.968 1.00 160.95 ? 2253 THR B C 1 ATOM 9222 O O . THR B 2 606 ? -40.859 -4.187 22.900 1.00 143.85 ? 2253 THR B O 1 ATOM 9223 C CB . THR B 2 606 ? -40.376 -0.862 22.485 1.00 199.05 ? 2253 THR B CB 1 ATOM 9224 O OG1 . THR B 2 606 ? -41.311 -0.192 21.623 1.00 206.32 ? 2253 THR B OG1 1 ATOM 9225 C CG2 . THR B 2 606 ? -39.139 0.041 22.792 1.00 189.71 ? 2253 THR B CG2 1 ATOM 9226 N N . SER B 2 607 ? -39.134 -3.100 23.949 1.00 146.75 ? 2254 SER B N 1 ATOM 9227 C CA . SER B 2 607 ? -39.159 -3.770 25.245 1.00 131.98 ? 2254 SER B CA 1 ATOM 9228 C C . SER B 2 607 ? -40.413 -3.398 26.004 1.00 132.37 ? 2254 SER B C 1 ATOM 9229 O O . SER B 2 607 ? -40.725 -2.217 26.127 1.00 142.73 ? 2254 SER B O 1 ATOM 9230 C CB . SER B 2 607 ? -37.992 -3.288 26.100 1.00 123.94 ? 2254 SER B CB 1 ATOM 9231 O OG . SER B 2 607 ? -36.760 -3.620 25.527 1.00 126.46 ? 2254 SER B OG 1 ATOM 9232 N N . MET B 2 608 ? -41.113 -4.397 26.535 1.00 120.55 ? 2255 MET B N 1 ATOM 9233 C CA . MET B 2 608 ? -42.258 -4.165 27.401 1.00 112.18 ? 2255 MET B CA 1 ATOM 9234 C C . MET B 2 608 ? -41.908 -4.879 28.672 1.00 112.61 ? 2255 MET B C 1 ATOM 9235 O O . MET B 2 608 ? -41.422 -6.008 28.604 1.00 119.99 ? 2255 MET B O 1 ATOM 9236 C CB . MET B 2 608 ? -43.511 -4.783 26.793 1.00 115.60 ? 2255 MET B CB 1 ATOM 9237 C CG . MET B 2 608 ? -43.582 -4.622 25.284 1.00 135.22 ? 2255 MET B CG 1 ATOM 9238 S SD . MET B 2 608 ? -45.007 -5.354 24.466 1.00 163.64 ? 2255 MET B SD 1 ATOM 9239 C CE . MET B 2 608 ? -44.940 -4.495 22.890 1.00 174.51 ? 2255 MET B CE 1 ATOM 9240 N N . TYR B 2 609 ? -42.096 -4.228 29.820 1.00 110.83 ? 2256 TYR B N 1 ATOM 9241 C CA . TYR B 2 609 ? -41.974 -4.926 31.112 1.00 115.10 ? 2256 TYR B CA 1 ATOM 9242 C C . TYR B 2 609 ? -42.785 -4.303 32.198 1.00 117.71 ? 2256 TYR B C 1 ATOM 9243 O O . TYR B 2 609 ? -43.216 -3.155 32.062 1.00 120.25 ? 2256 TYR B O 1 ATOM 9244 C CB . TYR B 2 609 ? -40.537 -5.049 31.586 1.00 113.16 ? 2256 TYR B CB 1 ATOM 9245 C CG . TYR B 2 609 ? -39.727 -3.788 31.576 1.00 117.76 ? 2256 TYR B CG 1 ATOM 9246 C CD1 . TYR B 2 609 ? -39.001 -3.418 30.443 1.00 129.93 ? 2256 TYR B CD1 1 ATOM 9247 C CD2 . TYR B 2 609 ? -39.623 -2.997 32.713 1.00 128.20 ? 2256 TYR B CD2 1 ATOM 9248 C CE1 . TYR B 2 609 ? -38.217 -2.273 30.425 1.00 137.41 ? 2256 TYR B CE1 1 ATOM 9249 C CE2 . TYR B 2 609 ? -38.844 -1.843 32.710 1.00 143.31 ? 2256 TYR B CE2 1 ATOM 9250 C CZ . TYR B 2 609 ? -38.145 -1.488 31.558 1.00 142.52 ? 2256 TYR B CZ 1 ATOM 9251 O OH . TYR B 2 609 ? -37.376 -0.354 31.537 1.00 148.33 ? 2256 TYR B OH 1 ATOM 9252 N N . VAL B 2 610 ? -43.004 -5.052 33.275 1.00 116.13 ? 2257 VAL B N 1 ATOM 9253 C CA . VAL B 2 610 ? -43.704 -4.456 34.393 1.00 122.36 ? 2257 VAL B CA 1 ATOM 9254 C C . VAL B 2 610 ? -42.699 -3.947 35.390 1.00 129.07 ? 2257 VAL B C 1 ATOM 9255 O O . VAL B 2 610 ? -41.783 -4.673 35.792 1.00 134.09 ? 2257 VAL B O 1 ATOM 9256 C CB . VAL B 2 610 ? -44.698 -5.398 35.063 1.00 120.59 ? 2257 VAL B CB 1 ATOM 9257 C CG1 . VAL B 2 610 ? -45.385 -4.679 36.212 1.00 110.37 ? 2257 VAL B CG1 1 ATOM 9258 C CG2 . VAL B 2 610 ? -45.723 -5.877 34.048 1.00 126.06 ? 2257 VAL B CG2 1 ATOM 9259 N N . LYS B 2 611 ? -42.885 -2.685 35.760 1.00 133.87 ? 2258 LYS B N 1 ATOM 9260 C CA . LYS B 2 611 ? -41.965 -1.971 36.621 1.00 156.69 ? 2258 LYS B CA 1 ATOM 9261 C C . LYS B 2 611 ? -42.268 -2.327 38.069 1.00 158.95 ? 2258 LYS B C 1 ATOM 9262 O O . LYS B 2 611 ? -41.363 -2.609 38.853 1.00 165.34 ? 2258 LYS B O 1 ATOM 9263 C CB . LYS B 2 611 ? -42.106 -0.446 36.408 1.00 181.07 ? 2258 LYS B CB 1 ATOM 9264 C CG . LYS B 2 611 ? -40.818 0.392 36.393 1.00 204.50 ? 2258 LYS B CG 1 ATOM 9265 C CD . LYS B 2 611 ? -40.036 0.361 37.708 1.00 223.69 ? 2258 LYS B CD 1 ATOM 9266 C CE . LYS B 2 611 ? -38.936 -0.704 37.715 1.00 210.27 ? 2258 LYS B CE 1 ATOM 9267 N NZ . LYS B 2 611 ? -38.510 -1.106 39.089 1.00 182.45 ? 2258 LYS B NZ 1 ATOM 9268 N N . GLU B 2 612 ? -43.549 -2.305 38.418 1.00 155.58 ? 2259 GLU B N 1 ATOM 9269 C CA . GLU B 2 612 ? -43.975 -2.405 39.808 1.00 155.69 ? 2259 GLU B CA 1 ATOM 9270 C C . GLU B 2 612 ? -45.259 -3.188 39.887 1.00 150.02 ? 2259 GLU B C 1 ATOM 9271 O O . GLU B 2 612 ? -46.121 -3.035 39.036 1.00 155.84 ? 2259 GLU B O 1 ATOM 9272 C CB . GLU B 2 612 ? -44.232 -1.013 40.381 1.00 162.52 ? 2259 GLU B CB 1 ATOM 9273 C CG . GLU B 2 612 ? -42.989 -0.196 40.683 1.00 171.77 ? 2259 GLU B CG 1 ATOM 9274 C CD . GLU B 2 612 ? -43.320 1.137 41.326 1.00 183.84 ? 2259 GLU B CD 1 ATOM 9275 O OE1 . GLU B 2 612 ? -44.455 1.638 41.135 1.00 179.36 ? 2259 GLU B OE1 1 ATOM 9276 O OE2 . GLU B 2 612 ? -42.439 1.683 42.027 1.00 199.67 ? 2259 GLU B OE2 1 ATOM 9277 N N . PHE B 2 613 ? -45.422 -4.000 40.919 1.00 148.84 ? 2260 PHE B N 1 ATOM 9278 C CA . PHE B 2 613 ? -46.637 -4.787 40.988 1.00 152.70 ? 2260 PHE B CA 1 ATOM 9279 C C . PHE B 2 613 ? -47.082 -5.211 42.373 1.00 160.43 ? 2260 PHE B C 1 ATOM 9280 O O . PHE B 2 613 ? -46.330 -5.123 43.337 1.00 160.00 ? 2260 PHE B O 1 ATOM 9281 C CB . PHE B 2 613 ? -46.519 -6.011 40.089 1.00 148.13 ? 2260 PHE B CB 1 ATOM 9282 C CG . PHE B 2 613 ? -45.509 -7.005 40.550 1.00 139.15 ? 2260 PHE B CG 1 ATOM 9283 C CD1 . PHE B 2 613 ? -44.171 -6.865 40.198 1.00 137.68 ? 2260 PHE B CD1 1 ATOM 9284 C CD2 . PHE B 2 613 ? -45.898 -8.096 41.309 1.00 136.14 ? 2260 PHE B CD2 1 ATOM 9285 C CE1 . PHE B 2 613 ? -43.231 -7.798 40.599 1.00 136.56 ? 2260 PHE B CE1 1 ATOM 9286 C CE2 . PHE B 2 613 ? -44.965 -9.028 41.715 1.00 142.97 ? 2260 PHE B CE2 1 ATOM 9287 C CZ . PHE B 2 613 ? -43.629 -8.882 41.359 1.00 138.75 ? 2260 PHE B CZ 1 ATOM 9288 N N . LEU B 2 614 ? -48.323 -5.690 42.432 1.00 163.43 ? 2261 LEU B N 1 ATOM 9289 C CA . LEU B 2 614 ? -48.945 -6.117 43.670 1.00 155.63 ? 2261 LEU B CA 1 ATOM 9290 C C . LEU B 2 614 ? -49.464 -7.502 43.639 1.00 161.23 ? 2261 LEU B C 1 ATOM 9291 O O . LEU B 2 614 ? -49.993 -7.947 42.628 1.00 167.03 ? 2261 LEU B O 1 ATOM 9292 C CB . LEU B 2 614 ? -50.094 -5.214 44.015 1.00 143.18 ? 2261 LEU B CB 1 ATOM 9293 C CG . LEU B 2 614 ? -49.306 -4.424 45.014 1.00 146.40 ? 2261 LEU B CG 1 ATOM 9294 C CD1 . LEU B 2 614 ? -49.052 -3.037 44.435 1.00 139.76 ? 2261 LEU B CD1 1 ATOM 9295 C CD2 . LEU B 2 614 ? -50.039 -4.434 46.347 1.00 160.93 ? 2261 LEU B CD2 1 ATOM 9296 N N . ILE B 2 615 ? -49.335 -8.195 44.758 1.00 159.16 ? 2262 ILE B N 1 ATOM 9297 C CA . ILE B 2 615 ? -49.918 -9.510 44.798 1.00 153.61 ? 2262 ILE B CA 1 ATOM 9298 C C . ILE B 2 615 ? -51.162 -9.513 45.629 1.00 163.43 ? 2262 ILE B C 1 ATOM 9299 O O . ILE B 2 615 ? -51.150 -9.098 46.785 1.00 167.61 ? 2262 ILE B O 1 ATOM 9300 C CB . ILE B 2 615 ? -48.976 -10.589 45.320 1.00 138.30 ? 2262 ILE B CB 1 ATOM 9301 C CG1 . ILE B 2 615 ? -47.627 -10.460 44.644 1.00 129.42 ? 2262 ILE B CG1 1 ATOM 9302 C CG2 . ILE B 2 615 ? -49.585 -11.962 45.056 1.00 131.03 ? 2262 ILE B CG2 1 ATOM 9303 C CD1 . ILE B 2 615 ? -46.539 -11.195 45.382 1.00 136.24 ? 2262 ILE B CD1 1 ATOM 9304 N N . SER B 2 616 ? -52.240 -9.954 44.996 1.00 169.58 ? 2263 SER B N 1 ATOM 9305 C CA . SER B 2 616 ? -53.387 -10.444 45.711 1.00 179.97 ? 2263 SER B CA 1 ATOM 9306 C C . SER B 2 616 ? -53.279 -11.959 45.700 1.00 177.42 ? 2263 SER B C 1 ATOM 9307 O O . SER B 2 616 ? -52.754 -12.560 44.749 1.00 162.04 ? 2263 SER B O 1 ATOM 9308 C CB . SER B 2 616 ? -54.689 -9.983 45.057 1.00 192.02 ? 2263 SER B CB 1 ATOM 9309 O OG . SER B 2 616 ? -54.707 -10.302 43.682 1.00 200.39 ? 2263 SER B OG 1 ATOM 9310 N N . SER B 2 617 ? -53.733 -12.558 46.793 1.00 182.58 ? 2264 SER B N 1 ATOM 9311 C CA . SER B 2 617 ? -53.918 -13.993 46.877 1.00 178.05 ? 2264 SER B CA 1 ATOM 9312 C C . SER B 2 617 ? -55.350 -14.252 47.313 1.00 184.73 ? 2264 SER B C 1 ATOM 9313 O O . SER B 2 617 ? -56.000 -13.368 47.882 1.00 192.46 ? 2264 SER B O 1 ATOM 9314 C CB . SER B 2 617 ? -52.919 -14.632 47.849 1.00 170.93 ? 2264 SER B CB 1 ATOM 9315 O OG . SER B 2 617 ? -53.036 -14.106 49.158 1.00 169.92 ? 2264 SER B OG 1 ATOM 9316 N N . SER B 2 618 ? -55.847 -15.446 47.004 1.00 186.53 ? 2265 SER B N 1 ATOM 9317 C CA . SER B 2 618 ? -57.158 -15.896 47.470 1.00 195.16 ? 2265 SER B CA 1 ATOM 9318 C C . SER B 2 618 ? -57.016 -17.257 48.124 1.00 185.56 ? 2265 SER B C 1 ATOM 9319 O O . SER B 2 618 ? -55.944 -17.633 48.596 1.00 182.90 ? 2265 SER B O 1 ATOM 9320 C CB . SER B 2 618 ? -58.183 -15.957 46.321 1.00 199.83 ? 2265 SER B CB 1 ATOM 9321 O OG . SER B 2 618 ? -59.424 -16.515 46.740 1.00 201.82 ? 2265 SER B OG 1 ATOM 9322 N N . GLN B 2 619 ? -58.109 -17.995 48.134 1.00 178.20 ? 2266 GLN B N 1 ATOM 9323 C CA . GLN B 2 619 ? -58.123 -19.269 48.759 1.00 182.74 ? 2266 GLN B CA 1 ATOM 9324 C C . GLN B 2 619 ? -59.312 -20.036 48.219 1.00 199.43 ? 2266 GLN B C 1 ATOM 9325 O O . GLN B 2 619 ? -59.272 -21.259 48.098 1.00 217.11 ? 2266 GLN B O 1 ATOM 9326 C CB . GLN B 2 619 ? -58.204 -19.069 50.274 1.00 184.25 ? 2266 GLN B CB 1 ATOM 9327 C CG . GLN B 2 619 ? -57.640 -20.218 51.096 1.00 193.46 ? 2266 GLN B CG 1 ATOM 9328 C CD . GLN B 2 619 ? -56.246 -20.666 50.670 1.00 186.69 ? 2266 GLN B CD 1 ATOM 9329 O OE1 . GLN B 2 619 ? -55.534 -21.312 51.444 1.00 183.28 ? 2266 GLN B OE1 1 ATOM 9330 N NE2 . GLN B 2 619 ? -55.851 -20.336 49.438 1.00 182.16 ? 2266 GLN B NE2 1 ATOM 9331 N N . ASP B 2 620 ? -60.352 -19.294 47.853 1.00 210.72 ? 2267 ASP B N 1 ATOM 9332 C CA . ASP B 2 620 ? -61.649 -19.859 47.487 1.00 218.38 ? 2267 ASP B CA 1 ATOM 9333 C C . ASP B 2 620 ? -61.953 -19.728 45.996 1.00 207.48 ? 2267 ASP B C 1 ATOM 9334 O O . ASP B 2 620 ? -62.633 -20.575 45.414 1.00 201.27 ? 2267 ASP B O 1 ATOM 9335 C CB . ASP B 2 620 ? -62.758 -19.188 48.308 1.00 241.40 ? 2267 ASP B CB 1 ATOM 9336 C CG . ASP B 2 620 ? -62.549 -17.675 48.472 1.00 246.88 ? 2267 ASP B CG 1 ATOM 9337 O OD1 . ASP B 2 620 ? -61.832 -17.048 47.653 1.00 230.62 ? 2267 ASP B OD1 1 ATOM 9338 O OD2 . ASP B 2 620 ? -63.109 -17.114 49.438 1.00 257.68 ? 2267 ASP B OD2 1 ATOM 9339 N N . GLY B 2 621 ? -61.452 -18.658 45.390 1.00 200.48 ? 2268 GLY B N 1 ATOM 9340 C CA . GLY B 2 621 ? -61.645 -18.427 43.971 1.00 201.30 ? 2268 GLY B CA 1 ATOM 9341 C C . GLY B 2 621 ? -62.074 -17.008 43.711 1.00 207.90 ? 2268 GLY B C 1 ATOM 9342 O O . GLY B 2 621 ? -61.605 -16.387 42.757 1.00 201.94 ? 2268 GLY B O 1 ATOM 9343 N N . HIS B 2 622 ? -62.952 -16.496 44.575 1.00 224.41 ? 2269 HIS B N 1 ATOM 9344 C CA . HIS B 2 622 ? -63.522 -15.149 44.412 1.00 239.00 ? 2269 HIS B CA 1 ATOM 9345 C C . HIS B 2 622 ? -63.161 -14.140 45.534 1.00 240.79 ? 2269 HIS B C 1 ATOM 9346 O O . HIS B 2 622 ? -63.301 -12.929 45.307 1.00 232.19 ? 2269 HIS B O 1 ATOM 9347 C CB . HIS B 2 622 ? -65.052 -15.207 44.198 1.00 244.15 ? 2269 HIS B CB 1 ATOM 9348 C CG . HIS B 2 622 ? -65.603 -16.599 44.129 1.00 251.45 ? 2269 HIS B CG 1 ATOM 9349 N ND1 . HIS B 2 622 ? -66.336 -17.160 45.154 1.00 268.95 ? 2269 HIS B ND1 1 ATOM 9350 C CD2 . HIS B 2 622 ? -65.510 -17.550 43.170 1.00 246.99 ? 2269 HIS B CD2 1 ATOM 9351 C CE1 . HIS B 2 622 ? -66.679 -18.394 44.829 1.00 269.18 ? 2269 HIS B CE1 1 ATOM 9352 N NE2 . HIS B 2 622 ? -66.187 -18.656 43.630 1.00 264.66 ? 2269 HIS B NE2 1 ATOM 9353 N N . GLN B 2 623 ? -62.709 -14.618 46.715 1.00 237.96 ? 2270 GLN B N 1 ATOM 9354 C CA . GLN B 2 623 ? -62.316 -13.714 47.847 1.00 227.66 ? 2270 GLN B CA 1 ATOM 9355 C C . GLN B 2 623 ? -60.813 -13.548 48.112 1.00 209.40 ? 2270 GLN B C 1 ATOM 9356 O O . GLN B 2 623 ? -60.183 -14.349 48.819 1.00 184.84 ? 2270 GLN B O 1 ATOM 9357 C CB . GLN B 2 623 ? -63.056 -13.991 49.173 1.00 241.74 ? 2270 GLN B CB 1 ATOM 9358 C CG . GLN B 2 623 ? -63.554 -12.698 49.837 1.00 259.29 ? 2270 GLN B CG 1 ATOM 9359 C CD . GLN B 2 623 ? -63.073 -12.487 51.267 1.00 258.70 ? 2270 GLN B CD 1 ATOM 9360 O OE1 . GLN B 2 623 ? -63.095 -13.407 52.082 1.00 256.86 ? 2270 GLN B OE1 1 ATOM 9361 N NE2 . GLN B 2 623 ? -62.649 -11.255 51.580 1.00 254.63 ? 2270 GLN B NE2 1 ATOM 9362 N N . TRP B 2 624 ? -60.303 -12.441 47.567 1.00 214.42 ? 2271 TRP B N 1 ATOM 9363 C CA . TRP B 2 624 ? -58.894 -12.054 47.519 1.00 208.52 ? 2271 TRP B CA 1 ATOM 9364 C C . TRP B 2 624 ? -58.555 -11.082 48.630 1.00 220.91 ? 2271 TRP B C 1 ATOM 9365 O O . TRP B 2 624 ? -59.184 -10.025 48.769 1.00 238.54 ? 2271 TRP B O 1 ATOM 9366 C CB . TRP B 2 624 ? -58.596 -11.368 46.176 1.00 196.62 ? 2271 TRP B CB 1 ATOM 9367 C CG . TRP B 2 624 ? -58.984 -12.206 45.021 1.00 189.89 ? 2271 TRP B CG 1 ATOM 9368 C CD1 . TRP B 2 624 ? -60.227 -12.316 44.453 1.00 194.80 ? 2271 TRP B CD1 1 ATOM 9369 C CD2 . TRP B 2 624 ? -58.135 -13.092 44.306 1.00 178.83 ? 2271 TRP B CD2 1 ATOM 9370 N NE1 . TRP B 2 624 ? -60.196 -13.221 43.422 1.00 188.20 ? 2271 TRP B NE1 1 ATOM 9371 C CE2 . TRP B 2 624 ? -58.920 -13.712 43.310 1.00 180.96 ? 2271 TRP B CE2 1 ATOM 9372 C CE3 . TRP B 2 624 ? -56.779 -13.420 44.403 1.00 171.82 ? 2271 TRP B CE3 1 ATOM 9373 C CZ2 . TRP B 2 624 ? -58.394 -14.644 42.421 1.00 179.52 ? 2271 TRP B CZ2 1 ATOM 9374 C CZ3 . TRP B 2 624 ? -56.257 -14.346 43.519 1.00 174.01 ? 2271 TRP B CZ3 1 ATOM 9375 C CH2 . TRP B 2 624 ? -57.061 -14.945 42.536 1.00 176.06 ? 2271 TRP B CH2 1 ATOM 9376 N N . THR B 2 625 ? -57.552 -11.432 49.420 1.00 217.99 ? 2272 THR B N 1 ATOM 9377 C CA . THR B 2 625 ? -57.021 -10.482 50.381 1.00 220.49 ? 2272 THR B CA 1 ATOM 9378 C C . THR B 2 625 ? -55.544 -10.173 50.041 1.00 207.10 ? 2272 THR B C 1 ATOM 9379 O O . THR B 2 625 ? -54.639 -10.984 50.272 1.00 189.42 ? 2272 THR B O 1 ATOM 9380 C CB . THR B 2 625 ? -57.320 -10.899 51.848 1.00 226.57 ? 2272 THR B CB 1 ATOM 9381 O OG1 . THR B 2 625 ? -57.436 -12.329 51.926 1.00 206.32 ? 2272 THR B OG1 1 ATOM 9382 C CG2 . THR B 2 625 ? -58.649 -10.232 52.361 1.00 222.08 ? 2272 THR B CG2 1 ATOM 9383 N N . LEU B 2 626 ? -55.354 -8.988 49.452 1.00 204.30 ? 2273 LEU B N 1 ATOM 9384 C CA . LEU B 2 626 ? -54.084 -8.495 48.889 1.00 195.08 ? 2273 LEU B CA 1 ATOM 9385 C C . LEU B 2 626 ? -52.881 -8.570 49.863 1.00 196.71 ? 2273 LEU B C 1 ATOM 9386 O O . LEU B 2 626 ? -53.054 -8.453 51.078 1.00 203.74 ? 2273 LEU B O 1 ATOM 9387 C CB . LEU B 2 626 ? -54.284 -7.053 48.337 1.00 188.26 ? 2273 LEU B CB 1 ATOM 9388 C CG . LEU B 2 626 ? -54.894 -6.741 46.935 1.00 175.56 ? 2273 LEU B CG 1 ATOM 9389 C CD1 . LEU B 2 626 ? -56.360 -7.132 46.765 1.00 178.87 ? 2273 LEU B CD1 1 ATOM 9390 C CD2 . LEU B 2 626 ? -54.712 -5.282 46.531 1.00 154.58 ? 2273 LEU B CD2 1 ATOM 9391 N N . PHE B 2 627 ? -51.674 -8.770 49.327 1.00 192.38 ? 2274 PHE B N 1 ATOM 9392 C CA . PHE B 2 627 ? -50.467 -8.901 50.155 1.00 185.98 ? 2274 PHE B CA 1 ATOM 9393 C C . PHE B 2 627 ? -49.996 -7.584 50.709 1.00 187.82 ? 2274 PHE B C 1 ATOM 9394 O O . PHE B 2 627 ? -49.392 -6.781 49.994 1.00 185.19 ? 2274 PHE B O 1 ATOM 9395 C CB . PHE B 2 627 ? -49.305 -9.530 49.388 1.00 177.62 ? 2274 PHE B CB 1 ATOM 9396 C CG . PHE B 2 627 ? -48.277 -10.199 50.273 1.00 182.03 ? 2274 PHE B CG 1 ATOM 9397 C CD1 . PHE B 2 627 ? -48.661 -10.909 51.418 1.00 191.46 ? 2274 PHE B CD1 1 ATOM 9398 C CD2 . PHE B 2 627 ? -46.924 -10.166 49.940 1.00 174.56 ? 2274 PHE B CD2 1 ATOM 9399 C CE1 . PHE B 2 627 ? -47.711 -11.546 52.218 1.00 190.19 ? 2274 PHE B CE1 1 ATOM 9400 C CE2 . PHE B 2 627 ? -45.974 -10.812 50.732 1.00 168.84 ? 2274 PHE B CE2 1 ATOM 9401 C CZ . PHE B 2 627 ? -46.365 -11.502 51.869 1.00 169.77 ? 2274 PHE B CZ 1 ATOM 9402 N N . PHE B 2 628 ? -50.279 -7.380 51.990 1.00 198.58 ? 2275 PHE B N 1 ATOM 9403 C CA . PHE B 2 628 ? -49.682 -6.303 52.754 1.00 212.87 ? 2275 PHE B CA 1 ATOM 9404 C C . PHE B 2 628 ? -48.256 -6.728 53.161 1.00 216.20 ? 2275 PHE B C 1 ATOM 9405 O O . PHE B 2 628 ? -47.842 -7.854 52.872 1.00 219.81 ? 2275 PHE B O 1 ATOM 9406 C CB . PHE B 2 628 ? -50.566 -5.953 53.965 1.00 224.58 ? 2275 PHE B CB 1 ATOM 9407 C CG . PHE B 2 628 ? -51.885 -5.288 53.601 1.00 238.19 ? 2275 PHE B CG 1 ATOM 9408 C CD1 . PHE B 2 628 ? -51.944 -3.923 53.287 1.00 242.27 ? 2275 PHE B CD1 1 ATOM 9409 C CD2 . PHE B 2 628 ? -53.076 -6.017 53.592 1.00 240.21 ? 2275 PHE B CD2 1 ATOM 9410 C CE1 . PHE B 2 628 ? -53.151 -3.309 52.961 1.00 234.03 ? 2275 PHE B CE1 1 ATOM 9411 C CE2 . PHE B 2 628 ? -54.285 -5.406 53.268 1.00 237.90 ? 2275 PHE B CE2 1 ATOM 9412 C CZ . PHE B 2 628 ? -54.321 -4.053 52.949 1.00 235.41 ? 2275 PHE B CZ 1 ATOM 9413 N N . GLN B 2 629 ? -47.496 -5.831 53.790 1.00 222.44 ? 2276 GLN B N 1 ATOM 9414 C CA . GLN B 2 629 ? -46.133 -6.145 54.248 1.00 222.31 ? 2276 GLN B CA 1 ATOM 9415 C C . GLN B 2 629 ? -45.960 -5.856 55.741 1.00 237.44 ? 2276 GLN B C 1 ATOM 9416 O O . GLN B 2 629 ? -45.443 -6.697 56.483 1.00 238.03 ? 2276 GLN B O 1 ATOM 9417 C CB . GLN B 2 629 ? -45.083 -5.381 53.435 1.00 219.62 ? 2276 GLN B CB 1 ATOM 9418 C CG . GLN B 2 629 ? -43.689 -5.417 54.043 1.00 229.11 ? 2276 GLN B CG 1 ATOM 9419 C CD . GLN B 2 629 ? -42.716 -4.455 53.391 1.00 242.57 ? 2276 GLN B CD 1 ATOM 9420 O OE1 . GLN B 2 629 ? -41.692 -4.870 52.845 1.00 262.55 ? 2276 GLN B OE1 1 ATOM 9421 N NE2 . GLN B 2 629 ? -43.030 -3.164 53.441 1.00 233.44 ? 2276 GLN B NE2 1 ATOM 9422 N N . ASN B 2 630 ? -46.373 -4.654 56.156 1.00 243.73 ? 2277 ASN B N 1 ATOM 9423 C CA . ASN B 2 630 ? -46.405 -4.233 57.567 1.00 239.95 ? 2277 ASN B CA 1 ATOM 9424 C C . ASN B 2 630 ? -47.237 -2.960 57.748 1.00 231.76 ? 2277 ASN B C 1 ATOM 9425 O O . ASN B 2 630 ? -46.816 -2.012 58.410 1.00 227.43 ? 2277 ASN B O 1 ATOM 9426 C CB . ASN B 2 630 ? -44.986 -4.082 58.169 1.00 249.09 ? 2277 ASN B CB 1 ATOM 9427 C CG . ASN B 2 630 ? -44.041 -3.257 57.298 1.00 243.09 ? 2277 ASN B CG 1 ATOM 9428 O OD1 . ASN B 2 630 ? -44.390 -2.179 56.816 1.00 231.92 ? 2277 ASN B OD1 1 ATOM 9429 N ND2 . ASN B 2 630 ? -42.819 -3.759 57.116 1.00 240.68 ? 2277 ASN B ND2 1 ATOM 9430 N N . GLY B 2 631 ? -48.433 -2.968 57.164 1.00 228.37 ? 2278 GLY B N 1 ATOM 9431 C CA . GLY B 2 631 ? -49.262 -1.766 57.028 1.00 239.57 ? 2278 GLY B CA 1 ATOM 9432 C C . GLY B 2 631 ? -49.239 -1.335 55.571 1.00 234.51 ? 2278 GLY B C 1 ATOM 9433 O O . GLY B 2 631 ? -50.261 -0.931 54.997 1.00 228.86 ? 2278 GLY B O 1 ATOM 9434 N N . LYS B 2 632 ? -48.043 -1.422 54.992 1.00 231.21 ? 2279 LYS B N 1 ATOM 9435 C CA . LYS B 2 632 ? -47.811 -1.321 53.558 1.00 225.96 ? 2279 LYS B CA 1 ATOM 9436 C C . LYS B 2 632 ? -48.667 -2.361 52.858 1.00 218.14 ? 2279 LYS B C 1 ATOM 9437 O O . LYS B 2 632 ? -48.832 -3.462 53.378 1.00 217.79 ? 2279 LYS B O 1 ATOM 9438 C CB . LYS B 2 632 ? -46.341 -1.657 53.277 1.00 223.90 ? 2279 LYS B CB 1 ATOM 9439 C CG . LYS B 2 632 ? -45.525 -0.593 52.554 1.00 226.33 ? 2279 LYS B CG 1 ATOM 9440 C CD . LYS B 2 632 ? -45.118 -1.061 51.160 1.00 210.02 ? 2279 LYS B CD 1 ATOM 9441 C CE . LYS B 2 632 ? -43.726 -0.576 50.780 1.00 202.22 ? 2279 LYS B CE 1 ATOM 9442 N NZ . LYS B 2 632 ? -43.619 0.909 50.740 1.00 210.27 ? 2279 LYS B NZ 1 ATOM 9443 N N . VAL B 2 633 ? -49.219 -1.999 51.699 1.00 208.09 ? 2280 VAL B N 1 ATOM 9444 C CA . VAL B 2 633 ? -49.745 -2.980 50.745 1.00 191.78 ? 2280 VAL B CA 1 ATOM 9445 C C . VAL B 2 633 ? -48.579 -3.309 49.809 1.00 188.68 ? 2280 VAL B C 1 ATOM 9446 O O . VAL B 2 633 ? -48.409 -2.621 48.821 1.00 193.63 ? 2280 VAL B O 1 ATOM 9447 C CB . VAL B 2 633 ? -50.906 -2.401 49.902 1.00 178.54 ? 2280 VAL B CB 1 ATOM 9448 C CG1 . VAL B 2 633 ? -51.832 -3.522 49.451 1.00 165.81 ? 2280 VAL B CG1 1 ATOM 9449 C CG2 . VAL B 2 633 ? -51.662 -1.303 50.655 1.00 182.21 ? 2280 VAL B CG2 1 ATOM 9450 N N . LYS B 2 634 ? -47.777 -4.340 50.113 1.00 196.37 ? 2281 LYS B N 1 ATOM 9451 C CA . LYS B 2 634 ? -46.431 -4.514 49.487 1.00 187.90 ? 2281 LYS B CA 1 ATOM 9452 C C . LYS B 2 634 ? -46.382 -4.288 47.965 1.00 180.00 ? 2281 LYS B C 1 ATOM 9453 O O . LYS B 2 634 ? -46.968 -5.071 47.194 1.00 170.37 ? 2281 LYS B O 1 ATOM 9454 C CB . LYS B 2 634 ? -45.739 -5.843 49.900 1.00 187.36 ? 2281 LYS B CB 1 ATOM 9455 C CG . LYS B 2 634 ? -44.349 -6.093 49.283 1.00 177.86 ? 2281 LYS B CG 1 ATOM 9456 C CD . LYS B 2 634 ? -43.147 -5.451 49.987 1.00 184.41 ? 2281 LYS B CD 1 ATOM 9457 C CE . LYS B 2 634 ? -43.192 -3.914 50.092 1.00 192.20 ? 2281 LYS B CE 1 ATOM 9458 N NZ . LYS B 2 634 ? -42.824 -3.039 48.932 1.00 162.05 ? 2281 LYS B NZ 1 ATOM 9459 N N . VAL B 2 635 ? -45.684 -3.206 47.575 1.00 175.31 ? 2282 VAL B N 1 ATOM 9460 C CA . VAL B 2 635 ? -45.506 -2.758 46.169 1.00 165.85 ? 2282 VAL B CA 1 ATOM 9461 C C . VAL B 2 635 ? -44.226 -3.296 45.582 1.00 159.10 ? 2282 VAL B C 1 ATOM 9462 O O . VAL B 2 635 ? -43.143 -2.764 45.846 1.00 157.99 ? 2282 VAL B O 1 ATOM 9463 C CB . VAL B 2 635 ? -45.392 -1.225 46.034 1.00 165.43 ? 2282 VAL B CB 1 ATOM 9464 C CG1 . VAL B 2 635 ? -46.611 -0.635 45.329 1.00 158.93 ? 2282 VAL B CG1 1 ATOM 9465 C CG2 . VAL B 2 635 ? -45.088 -0.576 47.384 1.00 173.73 ? 2282 VAL B CG2 1 ATOM 9466 N N . PHE B 2 636 ? -44.360 -4.328 44.760 1.00 149.58 ? 2283 PHE B N 1 ATOM 9467 C CA . PHE B 2 636 ? -43.226 -5.147 44.403 1.00 140.63 ? 2283 PHE B CA 1 ATOM 9468 C C . PHE B 2 636 ? -42.330 -4.490 43.386 1.00 143.96 ? 2283 PHE B C 1 ATOM 9469 O O . PHE B 2 636 ? -42.783 -3.665 42.586 1.00 144.22 ? 2283 PHE B O 1 ATOM 9470 C CB . PHE B 2 636 ? -43.680 -6.541 43.998 1.00 134.92 ? 2283 PHE B CB 1 ATOM 9471 C CG . PHE B 2 636 ? -44.150 -7.344 45.159 1.00 147.35 ? 2283 PHE B CG 1 ATOM 9472 C CD1 . PHE B 2 636 ? -43.236 -7.993 45.977 1.00 146.17 ? 2283 PHE B CD1 1 ATOM 9473 C CD2 . PHE B 2 636 ? -45.506 -7.391 45.487 1.00 166.90 ? 2283 PHE B CD2 1 ATOM 9474 C CE1 . PHE B 2 636 ? -43.667 -8.710 47.082 1.00 163.54 ? 2283 PHE B CE1 1 ATOM 9475 C CE2 . PHE B 2 636 ? -45.948 -8.102 46.596 1.00 176.62 ? 2283 PHE B CE2 1 ATOM 9476 C CZ . PHE B 2 636 ? -45.023 -8.768 47.391 1.00 176.51 ? 2283 PHE B CZ 1 ATOM 9477 N N . GLN B 2 637 ? -41.048 -4.846 43.464 1.00 146.72 ? 2284 GLN B N 1 ATOM 9478 C CA . GLN B 2 637 ? -40.015 -4.226 42.658 1.00 145.45 ? 2284 GLN B CA 1 ATOM 9479 C C . GLN B 2 637 ? -39.625 -4.995 41.390 1.00 147.86 ? 2284 GLN B C 1 ATOM 9480 O O . GLN B 2 637 ? -38.691 -5.793 41.421 1.00 162.75 ? 2284 GLN B O 1 ATOM 9481 C CB . GLN B 2 637 ? -38.814 -3.869 43.536 1.00 137.26 ? 2284 GLN B CB 1 ATOM 9482 C CG . GLN B 2 637 ? -38.979 -2.465 44.115 1.00 159.77 ? 2284 GLN B CG 1 ATOM 9483 C CD . GLN B 2 637 ? -39.752 -1.462 43.204 1.00 161.90 ? 2284 GLN B CD 1 ATOM 9484 O OE1 . GLN B 2 637 ? -39.518 -1.357 41.983 1.00 150.08 ? 2284 GLN B OE1 1 ATOM 9485 N NE2 . GLN B 2 637 ? -40.664 -0.703 43.818 1.00 161.71 ? 2284 GLN B NE2 1 ATOM 9486 N N . GLY B 2 638 ? -40.338 -4.721 40.286 1.00 147.41 ? 2285 GLY B N 1 ATOM 9487 C CA . GLY B 2 638 ? -40.214 -5.459 39.008 1.00 144.30 ? 2285 GLY B CA 1 ATOM 9488 C C . GLY B 2 638 ? -39.010 -5.155 38.118 1.00 147.23 ? 2285 GLY B C 1 ATOM 9489 O O . GLY B 2 638 ? -38.040 -4.532 38.547 1.00 157.76 ? 2285 GLY B O 1 ATOM 9490 N N . ASN B 2 639 ? -39.084 -5.589 36.866 1.00 140.30 ? 2286 ASN B N 1 ATOM 9491 C CA . ASN B 2 639 ? -37.922 -5.619 35.974 1.00 144.87 ? 2286 ASN B CA 1 ATOM 9492 C C . ASN B 2 639 ? -37.385 -4.262 35.509 1.00 147.24 ? 2286 ASN B C 1 ATOM 9493 O O . ASN B 2 639 ? -37.903 -3.200 35.883 1.00 135.99 ? 2286 ASN B O 1 ATOM 9494 C CB . ASN B 2 639 ? -38.258 -6.463 34.750 1.00 150.82 ? 2286 ASN B CB 1 ATOM 9495 C CG . ASN B 2 639 ? -39.174 -7.621 35.073 1.00 155.24 ? 2286 ASN B CG 1 ATOM 9496 O OD1 . ASN B 2 639 ? -38.740 -8.764 34.994 1.00 162.49 ? 2286 ASN B OD1 1 ATOM 9497 N ND2 . ASN B 2 639 ? -40.447 -7.338 35.437 1.00 134.79 ? 2286 ASN B ND2 1 ATOM 9498 N N . GLN B 2 640 ? -36.346 -4.313 34.674 1.00 148.23 ? 2287 GLN B N 1 ATOM 9499 C CA . GLN B 2 640 ? -35.846 -3.115 34.010 1.00 149.12 ? 2287 GLN B CA 1 ATOM 9500 C C . GLN B 2 640 ? -35.567 -3.241 32.495 1.00 157.65 ? 2287 GLN B C 1 ATOM 9501 O O . GLN B 2 640 ? -34.965 -2.340 31.895 1.00 173.28 ? 2287 GLN B O 1 ATOM 9502 C CB . GLN B 2 640 ? -34.635 -2.592 34.760 1.00 153.96 ? 2287 GLN B CB 1 ATOM 9503 C CG . GLN B 2 640 ? -35.033 -1.645 35.875 1.00 185.78 ? 2287 GLN B CG 1 ATOM 9504 C CD . GLN B 2 640 ? -34.344 -1.963 37.182 1.00 216.85 ? 2287 GLN B CD 1 ATOM 9505 O OE1 . GLN B 2 640 ? -33.941 -3.107 37.425 1.00 245.91 ? 2287 GLN B OE1 1 ATOM 9506 N NE2 . GLN B 2 640 ? -34.216 -0.954 38.045 1.00 218.17 ? 2287 GLN B NE2 1 ATOM 9507 N N . ASP B 2 641 ? -36.063 -4.320 31.875 1.00 156.84 ? 2288 ASP B N 1 ATOM 9508 C CA . ASP B 2 641 ? -35.692 -4.725 30.500 1.00 142.03 ? 2288 ASP B CA 1 ATOM 9509 C C . ASP B 2 641 ? -36.585 -5.805 29.935 1.00 131.28 ? 2288 ASP B C 1 ATOM 9510 O O . ASP B 2 641 ? -37.363 -6.413 30.658 1.00 139.36 ? 2288 ASP B O 1 ATOM 9511 C CB . ASP B 2 641 ? -34.312 -5.343 30.540 1.00 146.33 ? 2288 ASP B CB 1 ATOM 9512 C CG . ASP B 2 641 ? -34.036 -6.040 31.850 1.00 150.50 ? 2288 ASP B CG 1 ATOM 9513 O OD1 . ASP B 2 641 ? -34.986 -6.521 32.528 1.00 149.25 ? 2288 ASP B OD1 1 ATOM 9514 O OD2 . ASP B 2 641 ? -32.852 -6.068 32.216 1.00 161.54 ? 2288 ASP B OD2 1 ATOM 9515 N N . SER B 2 642 ? -36.437 -6.090 28.653 1.00 129.13 ? 2289 SER B N 1 ATOM 9516 C CA . SER B 2 642 ? -37.077 -7.276 28.110 1.00 156.68 ? 2289 SER B CA 1 ATOM 9517 C C . SER B 2 642 ? -36.646 -8.543 28.872 1.00 168.68 ? 2289 SER B C 1 ATOM 9518 O O . SER B 2 642 ? -37.495 -9.190 29.484 1.00 184.73 ? 2289 SER B O 1 ATOM 9519 C CB . SER B 2 642 ? -36.819 -7.416 26.610 1.00 191.30 ? 2289 SER B CB 1 ATOM 9520 O OG . SER B 2 642 ? -35.448 -7.628 26.329 1.00 223.54 ? 2289 SER B OG 1 ATOM 9521 N N . PHE B 2 643 ? -35.345 -8.876 28.859 1.00 169.89 ? 2290 PHE B N 1 ATOM 9522 C CA . PHE B 2 643 ? -34.810 -10.063 29.576 1.00 157.04 ? 2290 PHE B CA 1 ATOM 9523 C C . PHE B 2 643 ? -34.783 -9.894 31.088 1.00 162.99 ? 2290 PHE B C 1 ATOM 9524 O O . PHE B 2 643 ? -35.661 -9.239 31.664 1.00 193.74 ? 2290 PHE B O 1 ATOM 9525 C CB . PHE B 2 643 ? -33.410 -10.479 29.093 1.00 159.25 ? 2290 PHE B CB 1 ATOM 9526 C CG . PHE B 2 643 ? -32.439 -9.333 28.859 1.00 172.08 ? 2290 PHE B CG 1 ATOM 9527 C CD1 . PHE B 2 643 ? -32.441 -8.186 29.650 1.00 159.99 ? 2290 PHE B CD1 1 ATOM 9528 C CD2 . PHE B 2 643 ? -31.472 -9.434 27.838 1.00 199.45 ? 2290 PHE B CD2 1 ATOM 9529 C CE1 . PHE B 2 643 ? -31.532 -7.158 29.404 1.00 175.87 ? 2290 PHE B CE1 1 ATOM 9530 C CE2 . PHE B 2 643 ? -30.557 -8.410 27.591 1.00 198.25 ? 2290 PHE B CE2 1 ATOM 9531 C CZ . PHE B 2 643 ? -30.588 -7.270 28.379 1.00 192.18 ? 2290 PHE B CZ 1 ATOM 9532 N N . THR B 2 644 ? -33.774 -10.487 31.722 1.00 142.30 ? 2291 THR B N 1 ATOM 9533 C CA . THR B 2 644 ? -33.535 -10.312 33.165 1.00 145.15 ? 2291 THR B CA 1 ATOM 9534 C C . THR B 2 644 ? -34.704 -10.691 34.070 1.00 140.86 ? 2291 THR B C 1 ATOM 9535 O O . THR B 2 644 ? -35.653 -9.901 34.259 1.00 153.30 ? 2291 THR B O 1 ATOM 9536 C CB . THR B 2 644 ? -33.025 -8.890 33.503 1.00 156.55 ? 2291 THR B CB 1 ATOM 9537 O OG1 . THR B 2 644 ? -31.595 -8.898 33.507 1.00 169.47 ? 2291 THR B OG1 1 ATOM 9538 C CG2 . THR B 2 644 ? -33.545 -8.360 34.877 1.00 150.73 ? 2291 THR B CG2 1 ATOM 9539 N N . PRO B 2 645 ? -34.651 -11.920 34.604 1.00 127.88 ? 2292 PRO B N 1 ATOM 9540 C CA . PRO B 2 645 ? -35.549 -12.361 35.655 1.00 134.43 ? 2292 PRO B CA 1 ATOM 9541 C C . PRO B 2 645 ? -35.157 -11.724 36.968 1.00 136.31 ? 2292 PRO B C 1 ATOM 9542 O O . PRO B 2 645 ? -34.037 -11.912 37.442 1.00 135.32 ? 2292 PRO B O 1 ATOM 9543 C CB . PRO B 2 645 ? -35.329 -13.878 35.702 1.00 141.54 ? 2292 PRO B CB 1 ATOM 9544 C CG . PRO B 2 645 ? -34.876 -14.216 34.328 1.00 146.69 ? 2292 PRO B CG 1 ATOM 9545 C CD . PRO B 2 645 ? -34.002 -13.056 33.938 1.00 134.90 ? 2292 PRO B CD 1 ATOM 9546 N N . VAL B 2 646 ? -36.079 -10.955 37.537 1.00 141.52 ? 2293 VAL B N 1 ATOM 9547 C CA . VAL B 2 646 ? -35.842 -10.282 38.802 1.00 140.15 ? 2293 VAL B CA 1 ATOM 9548 C C . VAL B 2 646 ? -36.953 -10.726 39.764 1.00 126.29 ? 2293 VAL B C 1 ATOM 9549 O O . VAL B 2 646 ? -38.140 -10.807 39.400 1.00 108.00 ? 2293 VAL B O 1 ATOM 9550 C CB . VAL B 2 646 ? -35.625 -8.745 38.598 1.00 164.41 ? 2293 VAL B CB 1 ATOM 9551 C CG1 . VAL B 2 646 ? -36.902 -8.029 38.182 1.00 175.60 ? 2293 VAL B CG1 1 ATOM 9552 C CG2 . VAL B 2 646 ? -34.957 -8.086 39.806 1.00 184.06 ? 2293 VAL B CG2 1 ATOM 9553 N N . VAL B 2 647 ? -36.527 -11.075 40.977 1.00 129.90 ? 2294 VAL B N 1 ATOM 9554 C CA . VAL B 2 647 ? -37.302 -11.935 41.880 1.00 122.38 ? 2294 VAL B CA 1 ATOM 9555 C C . VAL B 2 647 ? -37.504 -11.343 43.288 1.00 136.58 ? 2294 VAL B C 1 ATOM 9556 O O . VAL B 2 647 ? -36.542 -10.868 43.903 1.00 144.17 ? 2294 VAL B O 1 ATOM 9557 C CB . VAL B 2 647 ? -36.650 -13.338 41.965 1.00 103.57 ? 2294 VAL B CB 1 ATOM 9558 C CG1 . VAL B 2 647 ? -35.143 -13.256 42.169 1.00 97.11 ? 2294 VAL B CG1 1 ATOM 9559 C CG2 . VAL B 2 647 ? -37.292 -14.138 43.056 1.00 95.72 ? 2294 VAL B CG2 1 ATOM 9560 N N . ASN B 2 648 ? -38.747 -11.358 43.790 1.00 143.57 ? 2295 ASN B N 1 ATOM 9561 C CA . ASN B 2 648 ? -39.039 -10.848 45.144 1.00 147.01 ? 2295 ASN B CA 1 ATOM 9562 C C . ASN B 2 648 ? -39.385 -11.954 46.104 1.00 145.52 ? 2295 ASN B C 1 ATOM 9563 O O . ASN B 2 648 ? -40.266 -12.774 45.819 1.00 136.73 ? 2295 ASN B O 1 ATOM 9564 C CB . ASN B 2 648 ? -40.190 -9.846 45.156 1.00 148.56 ? 2295 ASN B CB 1 ATOM 9565 C CG . ASN B 2 648 ? -40.051 -8.794 44.093 1.00 154.23 ? 2295 ASN B CG 1 ATOM 9566 O OD1 . ASN B 2 648 ? -40.457 -9.011 42.948 1.00 152.46 ? 2295 ASN B OD1 1 ATOM 9567 N ND2 . ASN B 2 648 ? -39.476 -7.641 44.458 1.00 159.83 ? 2295 ASN B ND2 1 ATOM 9568 N N . SER B 2 649 ? -38.698 -11.951 47.247 1.00 149.51 ? 2296 SER B N 1 ATOM 9569 C CA . SER B 2 649 ? -38.970 -12.888 48.331 1.00 161.60 ? 2296 SER B CA 1 ATOM 9570 C C . SER B 2 649 ? -40.301 -12.500 48.939 1.00 170.64 ? 2296 SER B C 1 ATOM 9571 O O . SER B 2 649 ? -40.826 -11.439 48.615 1.00 185.08 ? 2296 SER B O 1 ATOM 9572 C CB . SER B 2 649 ? -37.867 -12.822 49.391 1.00 160.41 ? 2296 SER B CB 1 ATOM 9573 O OG . SER B 2 649 ? -36.980 -13.925 49.280 1.00 161.61 ? 2296 SER B OG 1 ATOM 9574 N N . LEU B 2 650 ? -40.862 -13.348 49.800 1.00 170.75 ? 2297 LEU B N 1 ATOM 9575 C CA . LEU B 2 650 ? -42.075 -12.956 50.515 1.00 168.78 ? 2297 LEU B CA 1 ATOM 9576 C C . LEU B 2 650 ? -41.913 -12.839 52.052 1.00 186.15 ? 2297 LEU B C 1 ATOM 9577 O O . LEU B 2 650 ? -41.360 -13.737 52.727 1.00 173.91 ? 2297 LEU B O 1 ATOM 9578 C CB . LEU B 2 650 ? -43.312 -13.755 50.058 1.00 150.62 ? 2297 LEU B CB 1 ATOM 9579 C CG . LEU B 2 650 ? -43.673 -13.711 48.559 1.00 130.37 ? 2297 LEU B CG 1 ATOM 9580 C CD1 . LEU B 2 650 ? -45.025 -14.349 48.273 1.00 132.85 ? 2297 LEU B CD1 1 ATOM 9581 C CD2 . LEU B 2 650 ? -43.667 -12.304 48.009 1.00 123.01 ? 2297 LEU B CD2 1 ATOM 9582 N N . ASP B 2 651 ? -42.378 -11.675 52.538 1.00 202.73 ? 2298 ASP B N 1 ATOM 9583 C CA . ASP B 2 651 ? -42.325 -11.203 53.931 1.00 201.04 ? 2298 ASP B CA 1 ATOM 9584 C C . ASP B 2 651 ? -42.711 -12.377 54.836 1.00 195.87 ? 2298 ASP B C 1 ATOM 9585 O O . ASP B 2 651 ? -41.828 -13.145 55.224 1.00 188.96 ? 2298 ASP B O 1 ATOM 9586 C CB . ASP B 2 651 ? -43.254 -9.968 54.135 1.00 221.16 ? 2298 ASP B CB 1 ATOM 9587 C CG . ASP B 2 651 ? -42.596 -8.601 53.760 1.00 226.52 ? 2298 ASP B CG 1 ATOM 9588 O OD1 . ASP B 2 651 ? -42.417 -8.277 52.555 1.00 223.62 ? 2298 ASP B OD1 1 ATOM 9589 O OD2 . ASP B 2 651 ? -42.319 -7.808 54.691 1.00 221.01 ? 2298 ASP B OD2 1 ATOM 9590 N N . PRO B 2 652 ? -44.017 -12.535 55.167 1.00 204.40 ? 2299 PRO B N 1 ATOM 9591 C CA . PRO B 2 652 ? -44.352 -13.891 55.583 1.00 216.67 ? 2299 PRO B CA 1 ATOM 9592 C C . PRO B 2 652 ? -44.508 -14.744 54.315 1.00 211.55 ? 2299 PRO B C 1 ATOM 9593 O O . PRO B 2 652 ? -45.166 -14.300 53.365 1.00 228.80 ? 2299 PRO B O 1 ATOM 9594 C CB . PRO B 2 652 ? -45.703 -13.734 56.319 1.00 224.23 ? 2299 PRO B CB 1 ATOM 9595 C CG . PRO B 2 652 ? -46.085 -12.285 56.242 1.00 216.92 ? 2299 PRO B CG 1 ATOM 9596 C CD . PRO B 2 652 ? -45.186 -11.632 55.233 1.00 208.36 ? 2299 PRO B CD 1 ATOM 9597 N N . PRO B 2 653 ? -43.864 -15.926 54.265 1.00 189.35 ? 2300 PRO B N 1 ATOM 9598 C CA . PRO B 2 653 ? -44.128 -16.845 53.155 1.00 171.52 ? 2300 PRO B CA 1 ATOM 9599 C C . PRO B 2 653 ? -45.620 -17.148 53.030 1.00 162.87 ? 2300 PRO B C 1 ATOM 9600 O O . PRO B 2 653 ? -46.281 -17.393 54.032 1.00 164.98 ? 2300 PRO B O 1 ATOM 9601 C CB . PRO B 2 653 ? -43.337 -18.079 53.552 1.00 175.71 ? 2300 PRO B CB 1 ATOM 9602 C CG . PRO B 2 653 ? -42.147 -17.495 54.247 1.00 185.27 ? 2300 PRO B CG 1 ATOM 9603 C CD . PRO B 2 653 ? -42.690 -16.347 55.050 1.00 186.24 ? 2300 PRO B CD 1 ATOM 9604 N N . LEU B 2 654 ? -46.138 -17.112 51.807 1.00 157.82 ? 2301 LEU B N 1 ATOM 9605 C CA . LEU B 2 654 ? -47.581 -17.059 51.572 1.00 176.23 ? 2301 LEU B CA 1 ATOM 9606 C C . LEU B 2 654 ? -48.226 -18.420 51.293 1.00 197.42 ? 2301 LEU B C 1 ATOM 9607 O O . LEU B 2 654 ? -48.100 -18.929 50.172 1.00 227.40 ? 2301 LEU B O 1 ATOM 9608 C CB . LEU B 2 654 ? -47.841 -16.154 50.371 1.00 170.50 ? 2301 LEU B CB 1 ATOM 9609 C CG . LEU B 2 654 ? -49.207 -15.498 50.147 1.00 180.96 ? 2301 LEU B CG 1 ATOM 9610 C CD1 . LEU B 2 654 ? -49.296 -15.119 48.677 1.00 172.19 ? 2301 LEU B CD1 1 ATOM 9611 C CD2 . LEU B 2 654 ? -50.412 -16.340 50.568 1.00 180.46 ? 2301 LEU B CD2 1 ATOM 9612 N N . LEU B 2 655 ? -48.938 -18.991 52.275 1.00 194.83 ? 2302 LEU B N 1 ATOM 9613 C CA . LEU B 2 655 ? -49.662 -20.270 52.065 1.00 181.11 ? 2302 LEU B CA 1 ATOM 9614 C C . LEU B 2 655 ? -50.934 -19.991 51.256 1.00 177.64 ? 2302 LEU B C 1 ATOM 9615 O O . LEU B 2 655 ? -51.639 -19.023 51.552 1.00 176.29 ? 2302 LEU B O 1 ATOM 9616 C CB . LEU B 2 655 ? -49.987 -20.990 53.392 1.00 176.47 ? 2302 LEU B CB 1 ATOM 9617 C CG . LEU B 2 655 ? -48.902 -21.321 54.439 1.00 168.03 ? 2302 LEU B CG 1 ATOM 9618 C CD1 . LEU B 2 655 ? -49.508 -21.895 55.711 1.00 172.78 ? 2302 LEU B CD1 1 ATOM 9619 C CD2 . LEU B 2 655 ? -47.868 -22.287 53.901 1.00 160.01 ? 2302 LEU B CD2 1 ATOM 9620 N N . THR B 2 656 ? -51.202 -20.809 50.227 1.00 173.21 ? 2303 THR B N 1 ATOM 9621 C CA . THR B 2 656 ? -52.281 -20.522 49.244 1.00 164.25 ? 2303 THR B CA 1 ATOM 9622 C C . THR B 2 656 ? -52.565 -21.554 48.112 1.00 164.01 ? 2303 THR B C 1 ATOM 9623 O O . THR B 2 656 ? -51.890 -22.580 47.951 1.00 151.33 ? 2303 THR B O 1 ATOM 9624 C CB . THR B 2 656 ? -52.135 -19.104 48.608 1.00 152.91 ? 2303 THR B CB 1 ATOM 9625 O OG1 . THR B 2 656 ? -53.274 -18.824 47.782 1.00 145.11 ? 2303 THR B OG1 1 ATOM 9626 C CG2 . THR B 2 656 ? -50.837 -18.977 47.780 1.00 144.85 ? 2303 THR B CG2 1 ATOM 9627 N N . ARG B 2 657 ? -53.587 -21.216 47.332 1.00 169.33 ? 2304 ARG B N 1 ATOM 9628 C CA . ARG B 2 657 ? -54.120 -22.020 46.246 1.00 180.16 ? 2304 ARG B CA 1 ATOM 9629 C C . ARG B 2 657 ? -54.291 -21.051 45.091 1.00 172.44 ? 2304 ARG B C 1 ATOM 9630 O O . ARG B 2 657 ? -54.287 -21.425 43.915 1.00 169.24 ? 2304 ARG B O 1 ATOM 9631 C CB . ARG B 2 657 ? -55.496 -22.553 46.665 1.00 201.27 ? 2304 ARG B CB 1 ATOM 9632 C CG . ARG B 2 657 ? -56.044 -23.735 45.874 1.00 207.35 ? 2304 ARG B CG 1 ATOM 9633 C CD . ARG B 2 657 ? -56.958 -23.293 44.744 1.00 200.32 ? 2304 ARG B CD 1 ATOM 9634 N NE . ARG B 2 657 ? -58.147 -24.137 44.642 1.00 206.19 ? 2304 ARG B NE 1 ATOM 9635 C CZ . ARG B 2 657 ? -58.320 -25.103 43.745 1.00 204.75 ? 2304 ARG B CZ 1 ATOM 9636 N NH1 . ARG B 2 657 ? -57.373 -25.364 42.849 1.00 198.40 ? 2304 ARG B NH1 1 ATOM 9637 N NH2 . ARG B 2 657 ? -59.447 -25.812 43.745 1.00 204.10 ? 2304 ARG B NH2 1 ATOM 9638 N N . TYR B 2 658 ? -54.442 -19.787 45.449 1.00 168.47 ? 2305 TYR B N 1 ATOM 9639 C CA . TYR B 2 658 ? -54.693 -18.762 44.473 1.00 172.96 ? 2305 TYR B CA 1 ATOM 9640 C C . TYR B 2 658 ? -53.700 -17.619 44.588 1.00 175.66 ? 2305 TYR B C 1 ATOM 9641 O O . TYR B 2 658 ? -53.592 -16.985 45.640 1.00 183.41 ? 2305 TYR B O 1 ATOM 9642 C CB . TYR B 2 658 ? -56.121 -18.270 44.627 1.00 182.03 ? 2305 TYR B CB 1 ATOM 9643 C CG . TYR B 2 658 ? -57.106 -19.156 43.929 1.00 185.11 ? 2305 TYR B CG 1 ATOM 9644 C CD1 . TYR B 2 658 ? -57.243 -19.095 42.549 1.00 189.58 ? 2305 TYR B CD1 1 ATOM 9645 C CD2 . TYR B 2 658 ? -57.887 -20.059 44.633 1.00 185.57 ? 2305 TYR B CD2 1 ATOM 9646 C CE1 . TYR B 2 658 ? -58.139 -19.898 41.878 1.00 194.20 ? 2305 TYR B CE1 1 ATOM 9647 C CE2 . TYR B 2 658 ? -58.791 -20.870 43.970 1.00 194.78 ? 2305 TYR B CE2 1 ATOM 9648 C CZ . TYR B 2 658 ? -58.907 -20.785 42.587 1.00 197.18 ? 2305 TYR B CZ 1 ATOM 9649 O OH . TYR B 2 658 ? -59.788 -21.573 41.886 1.00 207.71 ? 2305 TYR B OH 1 ATOM 9650 N N . LEU B 2 659 ? -52.968 -17.381 43.499 1.00 171.95 ? 2306 LEU B N 1 ATOM 9651 C CA . LEU B 2 659 ? -51.993 -16.298 43.413 1.00 158.85 ? 2306 LEU B CA 1 ATOM 9652 C C . LEU B 2 659 ? -52.355 -15.388 42.253 1.00 159.78 ? 2306 LEU B C 1 ATOM 9653 O O . LEU B 2 659 ? -53.001 -15.813 41.285 1.00 158.75 ? 2306 LEU B O 1 ATOM 9654 C CB . LEU B 2 659 ? -50.576 -16.851 43.236 1.00 149.84 ? 2306 LEU B CB 1 ATOM 9655 C CG . LEU B 2 659 ? -49.428 -15.920 43.632 1.00 155.27 ? 2306 LEU B CG 1 ATOM 9656 C CD1 . LEU B 2 659 ? -49.388 -15.738 45.138 1.00 173.22 ? 2306 LEU B CD1 1 ATOM 9657 C CD2 . LEU B 2 659 ? -48.087 -16.438 43.145 1.00 154.88 ? 2306 LEU B CD2 1 ATOM 9658 N N . ARG B 2 660 ? -51.937 -14.132 42.351 1.00 159.50 ? 2307 ARG B N 1 ATOM 9659 C CA . ARG B 2 660 ? -52.329 -13.150 41.368 1.00 158.82 ? 2307 ARG B CA 1 ATOM 9660 C C . ARG B 2 660 ? -51.474 -11.916 41.466 1.00 161.63 ? 2307 ARG B C 1 ATOM 9661 O O . ARG B 2 660 ? -51.603 -11.159 42.431 1.00 169.12 ? 2307 ARG B O 1 ATOM 9662 C CB . ARG B 2 660 ? -53.753 -12.749 41.647 1.00 161.62 ? 2307 ARG B CB 1 ATOM 9663 C CG . ARG B 2 660 ? -54.627 -12.789 40.435 1.00 170.83 ? 2307 ARG B CG 1 ATOM 9664 C CD . ARG B 2 660 ? -55.997 -12.292 40.820 1.00 178.01 ? 2307 ARG B CD 1 ATOM 9665 N NE . ARG B 2 660 ? -57.031 -13.017 40.104 1.00 170.20 ? 2307 ARG B NE 1 ATOM 9666 C CZ . ARG B 2 660 ? -58.298 -12.646 40.061 1.00 173.11 ? 2307 ARG B CZ 1 ATOM 9667 N NH1 . ARG B 2 660 ? -58.696 -11.554 40.705 1.00 184.92 ? 2307 ARG B NH1 1 ATOM 9668 N NH2 . ARG B 2 660 ? -59.164 -13.376 39.378 1.00 179.10 ? 2307 ARG B NH2 1 ATOM 9669 N N . ILE B 2 661 ? -50.596 -11.711 40.487 1.00 159.22 ? 2308 ILE B N 1 ATOM 9670 C CA . ILE B 2 661 ? -49.809 -10.479 40.458 1.00 151.13 ? 2308 ILE B CA 1 ATOM 9671 C C . ILE B 2 661 ? -50.663 -9.407 39.795 1.00 144.35 ? 2308 ILE B C 1 ATOM 9672 O O . ILE B 2 661 ? -51.531 -9.724 38.968 1.00 128.10 ? 2308 ILE B O 1 ATOM 9673 C CB . ILE B 2 661 ? -48.397 -10.628 39.818 1.00 148.39 ? 2308 ILE B CB 1 ATOM 9674 C CG1 . ILE B 2 661 ? -48.472 -11.123 38.375 1.00 149.82 ? 2308 ILE B CG1 1 ATOM 9675 C CG2 . ILE B 2 661 ? -47.505 -11.544 40.647 1.00 142.38 ? 2308 ILE B CG2 1 ATOM 9676 C CD1 . ILE B 2 661 ? -48.559 -10.005 37.362 1.00 155.89 ? 2308 ILE B CD1 1 ATOM 9677 N N . HIS B 2 662 ? -50.416 -8.158 40.200 1.00 149.02 ? 2309 HIS B N 1 ATOM 9678 C CA . HIS B 2 662 ? -51.225 -6.986 39.839 1.00 160.05 ? 2309 HIS B CA 1 ATOM 9679 C C . HIS B 2 662 ? -50.363 -5.849 39.264 1.00 149.36 ? 2309 HIS B C 1 ATOM 9680 O O . HIS B 2 662 ? -49.931 -4.971 40.027 1.00 155.45 ? 2309 HIS B O 1 ATOM 9681 C CB . HIS B 2 662 ? -51.982 -6.460 41.076 1.00 171.50 ? 2309 HIS B CB 1 ATOM 9682 C CG . HIS B 2 662 ? -53.384 -6.970 41.197 1.00 191.92 ? 2309 HIS B CG 1 ATOM 9683 N ND1 . HIS B 2 662 ? -53.715 -8.079 41.948 1.00 190.84 ? 2309 HIS B ND1 1 ATOM 9684 C CD2 . HIS B 2 662 ? -54.546 -6.512 40.669 1.00 204.55 ? 2309 HIS B CD2 1 ATOM 9685 C CE1 . HIS B 2 662 ? -55.019 -8.285 41.871 1.00 202.18 ? 2309 HIS B CE1 1 ATOM 9686 N NE2 . HIS B 2 662 ? -55.546 -7.352 41.098 1.00 211.93 ? 2309 HIS B NE2 1 ATOM 9687 N N . PRO B 2 663 ? -50.119 -5.845 37.926 1.00 133.43 ? 2310 PRO B N 1 ATOM 9688 C CA . PRO B 2 663 ? -49.248 -4.800 37.388 1.00 129.88 ? 2310 PRO B CA 1 ATOM 9689 C C . PRO B 2 663 ? -49.762 -3.398 37.727 1.00 135.60 ? 2310 PRO B C 1 ATOM 9690 O O . PRO B 2 663 ? -50.870 -3.041 37.340 1.00 145.72 ? 2310 PRO B O 1 ATOM 9691 C CB . PRO B 2 663 ? -49.259 -5.056 35.863 1.00 118.98 ? 2310 PRO B CB 1 ATOM 9692 C CG . PRO B 2 663 ? -50.426 -5.932 35.613 1.00 118.33 ? 2310 PRO B CG 1 ATOM 9693 C CD . PRO B 2 663 ? -50.597 -6.747 36.861 1.00 126.62 ? 2310 PRO B CD 1 ATOM 9694 N N . GLN B 2 664 ? -48.978 -2.629 38.475 1.00 135.56 ? 2311 GLN B N 1 ATOM 9695 C CA . GLN B 2 664 ? -49.322 -1.238 38.710 1.00 146.83 ? 2311 GLN B CA 1 ATOM 9696 C C . GLN B 2 664 ? -48.752 -0.298 37.631 1.00 159.09 ? 2311 GLN B C 1 ATOM 9697 O O . GLN B 2 664 ? -49.511 0.188 36.808 1.00 176.42 ? 2311 GLN B O 1 ATOM 9698 C CB . GLN B 2 664 ? -48.985 -0.814 40.136 1.00 153.53 ? 2311 GLN B CB 1 ATOM 9699 C CG . GLN B 2 664 ? -49.777 -1.583 41.191 1.00 166.85 ? 2311 GLN B CG 1 ATOM 9700 C CD . GLN B 2 664 ? -51.289 -1.425 41.060 1.00 172.11 ? 2311 GLN B CD 1 ATOM 9701 O OE1 . GLN B 2 664 ? -51.785 -0.345 40.723 1.00 167.18 ? 2311 GLN B OE1 1 ATOM 9702 N NE2 . GLN B 2 664 ? -52.032 -2.506 41.341 1.00 172.06 ? 2311 GLN B NE2 1 ATOM 9703 N N . SER B 2 665 ? -47.445 -0.046 37.603 1.00 163.75 ? 2312 SER B N 1 ATOM 9704 C CA . SER B 2 665 ? -46.867 0.776 36.530 1.00 158.81 ? 2312 SER B CA 1 ATOM 9705 C C . SER B 2 665 ? -45.820 -0.013 35.777 1.00 149.20 ? 2312 SER B C 1 ATOM 9706 O O . SER B 2 665 ? -45.024 -0.736 36.371 1.00 145.45 ? 2312 SER B O 1 ATOM 9707 C CB . SER B 2 665 ? -46.231 2.032 37.093 1.00 175.65 ? 2312 SER B CB 1 ATOM 9708 O OG . SER B 2 665 ? -45.112 1.664 37.878 1.00 187.90 ? 2312 SER B OG 1 ATOM 9709 N N . TRP B 2 666 ? -45.808 0.151 34.465 1.00 146.32 ? 2313 TRP B N 1 ATOM 9710 C CA . TRP B 2 666 ? -44.994 -0.691 33.594 1.00 141.60 ? 2313 TRP B CA 1 ATOM 9711 C C . TRP B 2 666 ? -43.961 0.134 32.860 1.00 137.65 ? 2313 TRP B C 1 ATOM 9712 O O . TRP B 2 666 ? -43.257 0.931 33.491 1.00 161.75 ? 2313 TRP B O 1 ATOM 9713 C CB . TRP B 2 666 ? -45.886 -1.373 32.585 1.00 140.97 ? 2313 TRP B CB 1 ATOM 9714 C CG . TRP B 2 666 ? -46.947 -0.459 32.114 1.00 140.88 ? 2313 TRP B CG 1 ATOM 9715 C CD1 . TRP B 2 666 ? -46.884 0.383 31.062 1.00 139.52 ? 2313 TRP B CD1 1 ATOM 9716 C CD2 . TRP B 2 666 ? -48.229 -0.271 32.705 1.00 141.04 ? 2313 TRP B CD2 1 ATOM 9717 N NE1 . TRP B 2 666 ? -48.056 1.079 30.938 1.00 139.82 ? 2313 TRP B NE1 1 ATOM 9718 C CE2 . TRP B 2 666 ? -48.901 0.695 31.938 1.00 137.79 ? 2313 TRP B CE2 1 ATOM 9719 C CE3 . TRP B 2 666 ? -48.879 -0.839 33.801 1.00 143.59 ? 2313 TRP B CE3 1 ATOM 9720 C CZ2 . TRP B 2 666 ? -50.185 1.109 32.220 1.00 143.29 ? 2313 TRP B CZ2 1 ATOM 9721 C CZ3 . TRP B 2 666 ? -50.153 -0.439 34.075 1.00 152.42 ? 2313 TRP B CZ3 1 ATOM 9722 C CH2 . TRP B 2 666 ? -50.798 0.532 33.288 1.00 156.21 ? 2313 TRP B CH2 1 ATOM 9723 N N . VAL B 2 667 ? -43.876 -0.039 31.537 1.00 117.66 ? 2314 VAL B N 1 ATOM 9724 C CA . VAL B 2 667 ? -42.861 0.659 30.749 1.00 114.71 ? 2314 VAL B CA 1 ATOM 9725 C C . VAL B 2 667 ? -43.362 1.221 29.406 1.00 126.52 ? 2314 VAL B C 1 ATOM 9726 O O . VAL B 2 667 ? -43.399 2.460 29.192 1.00 138.18 ? 2314 VAL B O 1 ATOM 9727 C CB . VAL B 2 667 ? -41.649 -0.258 30.530 1.00 107.38 ? 2314 VAL B CB 1 ATOM 9728 C CG1 . VAL B 2 667 ? -42.012 -1.414 29.603 1.00 104.64 ? 2314 VAL B CG1 1 ATOM 9729 C CG2 . VAL B 2 667 ? -40.457 0.542 30.034 1.00 97.96 ? 2314 VAL B CG2 1 ATOM 9730 N N . HIS B 2 668 ? -43.735 0.291 28.524 1.00 126.08 ? 2315 HIS B N 1 ATOM 9731 C CA . HIS B 2 668 ? -44.268 0.572 27.195 1.00 132.46 ? 2315 HIS B CA 1 ATOM 9732 C C . HIS B 2 668 ? -45.630 -0.145 27.046 1.00 131.53 ? 2315 HIS B C 1 ATOM 9733 O O . HIS B 2 668 ? -46.563 0.355 26.402 1.00 129.86 ? 2315 HIS B O 1 ATOM 9734 C CB . HIS B 2 668 ? -43.318 0.017 26.126 1.00 145.33 ? 2315 HIS B CB 1 ATOM 9735 C CG . HIS B 2 668 ? -42.055 0.806 25.910 1.00 151.18 ? 2315 HIS B CG 1 ATOM 9736 N ND1 . HIS B 2 668 ? -42.006 1.937 25.122 1.00 159.83 ? 2315 HIS B ND1 1 ATOM 9737 C CD2 . HIS B 2 668 ? -40.778 0.567 26.297 1.00 151.54 ? 2315 HIS B CD2 1 ATOM 9738 C CE1 . HIS B 2 668 ? -40.764 2.386 25.072 1.00 161.48 ? 2315 HIS B CE1 1 ATOM 9739 N NE2 . HIS B 2 668 ? -39.997 1.568 25.770 1.00 160.55 ? 2315 HIS B NE2 1 ATOM 9740 N N . GLN B 2 669 ? -45.716 -1.333 27.636 1.00 137.58 ? 2316 GLN B N 1 ATOM 9741 C CA . GLN B 2 669 ? -46.929 -2.152 27.650 1.00 148.29 ? 2316 GLN B CA 1 ATOM 9742 C C . GLN B 2 669 ? -46.892 -2.944 28.931 1.00 151.73 ? 2316 GLN B C 1 ATOM 9743 O O . GLN B 2 669 ? -45.809 -3.076 29.532 1.00 157.08 ? 2316 GLN B O 1 ATOM 9744 C CB . GLN B 2 669 ? -46.900 -3.158 26.508 1.00 145.84 ? 2316 GLN B CB 1 ATOM 9745 C CG . GLN B 2 669 ? -47.020 -2.548 25.136 1.00 147.14 ? 2316 GLN B CG 1 ATOM 9746 C CD . GLN B 2 669 ? -48.439 -2.210 24.819 1.00 156.83 ? 2316 GLN B CD 1 ATOM 9747 O OE1 . GLN B 2 669 ? -49.329 -2.401 25.653 1.00 158.80 ? 2316 GLN B OE1 1 ATOM 9748 N NE2 . GLN B 2 669 ? -48.672 -1.721 23.607 1.00 170.13 ? 2316 GLN B NE2 1 ATOM 9749 N N . ILE B 2 670 ? -48.037 -3.484 29.361 1.00 138.24 ? 2317 ILE B N 1 ATOM 9750 C CA . ILE B 2 670 ? -47.949 -4.534 30.369 1.00 124.60 ? 2317 ILE B CA 1 ATOM 9751 C C . ILE B 2 670 ? -47.528 -5.750 29.576 1.00 116.94 ? 2317 ILE B C 1 ATOM 9752 O O . ILE B 2 670 ? -48.066 -6.006 28.492 1.00 114.83 ? 2317 ILE B O 1 ATOM 9753 C CB . ILE B 2 670 ? -49.225 -4.791 31.213 1.00 124.58 ? 2317 ILE B CB 1 ATOM 9754 C CG1 . ILE B 2 670 ? -49.642 -3.555 32.000 1.00 125.96 ? 2317 ILE B CG1 1 ATOM 9755 C CG2 . ILE B 2 670 ? -48.962 -5.850 32.276 1.00 117.94 ? 2317 ILE B CG2 1 ATOM 9756 C CD1 . ILE B 2 670 ? -50.530 -2.603 31.243 1.00 127.90 ? 2317 ILE B CD1 1 ATOM 9757 N N . ALA B 2 671 ? -46.501 -6.421 30.095 1.00 112.38 ? 2318 ALA B N 1 ATOM 9758 C CA . ALA B 2 671 ? -45.989 -7.670 29.560 1.00 114.46 ? 2318 ALA B CA 1 ATOM 9759 C C . ALA B 2 671 ? -45.320 -8.454 30.663 1.00 116.79 ? 2318 ALA B C 1 ATOM 9760 O O . ALA B 2 671 ? -44.466 -7.945 31.426 1.00 106.78 ? 2318 ALA B O 1 ATOM 9761 C CB . ALA B 2 671 ? -45.026 -7.439 28.417 1.00 116.08 ? 2318 ALA B CB 1 ATOM 9762 N N . LEU B 2 672 ? -45.737 -9.710 30.727 1.00 127.34 ? 2319 LEU B N 1 ATOM 9763 C CA . LEU B 2 672 ? -45.303 -10.622 31.757 1.00 128.58 ? 2319 LEU B CA 1 ATOM 9764 C C . LEU B 2 672 ? -44.949 -11.994 31.228 1.00 123.68 ? 2319 LEU B C 1 ATOM 9765 O O . LEU B 2 672 ? -45.768 -12.690 30.639 1.00 127.60 ? 2319 LEU B O 1 ATOM 9766 C CB . LEU B 2 672 ? -46.359 -10.751 32.866 1.00 121.88 ? 2319 LEU B CB 1 ATOM 9767 C CG . LEU B 2 672 ? -46.011 -10.109 34.207 1.00 118.03 ? 2319 LEU B CG 1 ATOM 9768 C CD1 . LEU B 2 672 ? -46.200 -11.155 35.289 1.00 116.58 ? 2319 LEU B CD1 1 ATOM 9769 C CD2 . LEU B 2 672 ? -44.590 -9.546 34.251 1.00 118.56 ? 2319 LEU B CD2 1 ATOM 9770 N N . ARG B 2 673 ? -43.695 -12.352 31.414 1.00 118.13 ? 2320 ARG B N 1 ATOM 9771 C CA . ARG B 2 673 ? -43.361 -13.728 31.628 1.00 124.96 ? 2320 ARG B CA 1 ATOM 9772 C C . ARG B 2 673 ? -43.165 -13.767 33.125 1.00 127.03 ? 2320 ARG B C 1 ATOM 9773 O O . ARG B 2 673 ? -43.187 -12.705 33.752 1.00 131.60 ? 2320 ARG B O 1 ATOM 9774 C CB . ARG B 2 673 ? -42.085 -14.076 30.900 1.00 129.25 ? 2320 ARG B CB 1 ATOM 9775 C CG . ARG B 2 673 ? -42.325 -14.753 29.570 1.00 130.89 ? 2320 ARG B CG 1 ATOM 9776 C CD . ARG B 2 673 ? -41.012 -14.921 28.851 1.00 119.07 ? 2320 ARG B CD 1 ATOM 9777 N NE . ARG B 2 673 ? -40.409 -13.625 28.645 1.00 113.43 ? 2320 ARG B NE 1 ATOM 9778 C CZ . ARG B 2 673 ? -39.506 -13.383 27.715 1.00 136.12 ? 2320 ARG B CZ 1 ATOM 9779 N NH1 . ARG B 2 673 ? -39.102 -14.362 26.913 1.00 158.87 ? 2320 ARG B NH1 1 ATOM 9780 N NH2 . ARG B 2 673 ? -39.005 -12.165 27.587 1.00 154.59 ? 2320 ARG B NH2 1 ATOM 9781 N N . MET B 2 674 ? -42.985 -14.956 33.705 1.00 125.39 ? 2321 MET B N 1 ATOM 9782 C CA . MET B 2 674 ? -42.806 -15.072 35.155 1.00 124.29 ? 2321 MET B CA 1 ATOM 9783 C C . MET B 2 674 ? -42.858 -16.513 35.620 1.00 123.28 ? 2321 MET B C 1 ATOM 9784 O O . MET B 2 674 ? -43.539 -17.331 34.999 1.00 129.04 ? 2321 MET B O 1 ATOM 9785 C CB . MET B 2 674 ? -43.893 -14.250 35.859 1.00 130.81 ? 2321 MET B CB 1 ATOM 9786 C CG . MET B 2 674 ? -44.438 -14.804 37.154 1.00 139.29 ? 2321 MET B CG 1 ATOM 9787 S SD . MET B 2 674 ? -46.205 -15.025 36.918 1.00 148.77 ? 2321 MET B SD 1 ATOM 9788 C CE . MET B 2 674 ? -46.781 -14.488 38.525 1.00 167.02 ? 2321 MET B CE 1 ATOM 9789 N N . GLU B 2 675 ? -42.139 -16.822 36.704 1.00 117.59 ? 2322 GLU B N 1 ATOM 9790 C CA . GLU B 2 675 ? -42.405 -18.053 37.456 1.00 115.13 ? 2322 GLU B CA 1 ATOM 9791 C C . GLU B 2 675 ? -42.664 -17.804 38.911 1.00 122.33 ? 2322 GLU B C 1 ATOM 9792 O O . GLU B 2 675 ? -42.454 -16.693 39.416 1.00 128.52 ? 2322 GLU B O 1 ATOM 9793 C CB . GLU B 2 675 ? -41.279 -19.054 37.373 1.00 109.86 ? 2322 GLU B CB 1 ATOM 9794 C CG . GLU B 2 675 ? -41.663 -20.372 38.011 1.00 112.48 ? 2322 GLU B CG 1 ATOM 9795 C CD . GLU B 2 675 ? -41.057 -21.550 37.292 1.00 134.60 ? 2322 GLU B CD 1 ATOM 9796 O OE1 . GLU B 2 675 ? -39.892 -21.439 36.829 1.00 145.23 ? 2322 GLU B OE1 1 ATOM 9797 O OE2 . GLU B 2 675 ? -41.750 -22.585 37.179 1.00 136.92 ? 2322 GLU B OE2 1 ATOM 9798 N N . VAL B 2 676 ? -43.099 -18.870 39.578 1.00 121.61 ? 2323 VAL B N 1 ATOM 9799 C CA . VAL B 2 676 ? -43.386 -18.842 41.006 1.00 123.16 ? 2323 VAL B CA 1 ATOM 9800 C C . VAL B 2 676 ? -42.418 -19.711 41.810 1.00 132.41 ? 2323 VAL B C 1 ATOM 9801 O O . VAL B 2 676 ? -41.954 -20.742 41.330 1.00 145.83 ? 2323 VAL B O 1 ATOM 9802 C CB . VAL B 2 676 ? -44.831 -19.256 41.271 1.00 109.13 ? 2323 VAL B CB 1 ATOM 9803 C CG1 . VAL B 2 676 ? -45.178 -19.017 42.733 1.00 107.47 ? 2323 VAL B CG1 1 ATOM 9804 C CG2 . VAL B 2 676 ? -45.747 -18.460 40.350 1.00 101.72 ? 2323 VAL B CG2 1 ATOM 9805 N N . LEU B 2 677 ? -42.106 -19.278 43.027 1.00 130.38 ? 2324 LEU B N 1 ATOM 9806 C CA . LEU B 2 677 ? -41.169 -20.000 43.871 1.00 140.53 ? 2324 LEU B CA 1 ATOM 9807 C C . LEU B 2 677 ? -41.865 -20.589 45.109 1.00 154.45 ? 2324 LEU B C 1 ATOM 9808 O O . LEU B 2 677 ? -42.756 -19.948 45.668 1.00 170.78 ? 2324 LEU B O 1 ATOM 9809 C CB . LEU B 2 677 ? -40.000 -19.080 44.263 1.00 136.74 ? 2324 LEU B CB 1 ATOM 9810 C CG . LEU B 2 677 ? -38.674 -19.234 43.492 1.00 137.40 ? 2324 LEU B CG 1 ATOM 9811 C CD1 . LEU B 2 677 ? -38.781 -18.714 42.060 1.00 129.32 ? 2324 LEU B CD1 1 ATOM 9812 C CD2 . LEU B 2 677 ? -37.490 -18.606 44.243 1.00 136.71 ? 2324 LEU B CD2 1 ATOM 9813 N N . GLY B 2 678 ? -41.475 -21.808 45.512 1.00 151.49 ? 2325 GLY B N 1 ATOM 9814 C CA . GLY B 2 678 ? -42.001 -22.454 46.729 1.00 146.66 ? 2325 GLY B CA 1 ATOM 9815 C C . GLY B 2 678 ? -42.167 -23.972 46.692 1.00 157.03 ? 2325 GLY B C 1 ATOM 9816 O O . GLY B 2 678 ? -41.388 -24.680 46.030 1.00 163.02 ? 2325 GLY B O 1 ATOM 9817 N N . CYS B 2 679 ? -43.182 -24.473 47.415 1.00 159.27 ? 2326 CYS B N 1 ATOM 9818 C CA . CYS B 2 679 ? -43.413 -25.927 47.564 1.00 159.03 ? 2326 CYS B CA 1 ATOM 9819 C C . CYS B 2 679 ? -44.748 -26.380 48.237 1.00 148.63 ? 2326 CYS B C 1 ATOM 9820 O O . CYS B 2 679 ? -45.756 -25.687 48.192 1.00 136.52 ? 2326 CYS B O 1 ATOM 9821 C CB . CYS B 2 679 ? -42.218 -26.556 48.280 1.00 172.31 ? 2326 CYS B CB 1 ATOM 9822 S SG . CYS B 2 679 ? -42.187 -26.134 50.033 1.00 193.57 ? 2326 CYS B SG 1 ATOM 9823 N N . GLU B 2 680 ? -44.731 -27.554 48.857 1.00 152.78 ? 2327 GLU B N 1 ATOM 9824 C CA . GLU B 2 680 ? -45.944 -28.231 49.308 1.00 168.41 ? 2327 GLU B CA 1 ATOM 9825 C C . GLU B 2 680 ? -46.210 -28.034 50.801 1.00 168.70 ? 2327 GLU B C 1 ATOM 9826 O O . GLU B 2 680 ? -45.364 -28.418 51.606 1.00 178.47 ? 2327 GLU B O 1 ATOM 9827 C CB . GLU B 2 680 ? -45.756 -29.725 49.052 1.00 188.95 ? 2327 GLU B CB 1 ATOM 9828 C CG . GLU B 2 680 ? -45.474 -30.091 47.605 1.00 194.70 ? 2327 GLU B CG 1 ATOM 9829 C CD . GLU B 2 680 ? -46.732 -30.521 46.876 1.00 207.01 ? 2327 GLU B CD 1 ATOM 9830 O OE1 . GLU B 2 680 ? -47.247 -31.616 47.192 1.00 211.62 ? 2327 GLU B OE1 1 ATOM 9831 O OE2 . GLU B 2 680 ? -47.206 -29.773 45.993 1.00 208.70 ? 2327 GLU B OE2 1 ATOM 9832 N N . ALA B 2 681 ? -47.365 -27.483 51.189 1.00 158.00 ? 2328 ALA B N 1 ATOM 9833 C CA . ALA B 2 681 ? -47.665 -27.309 52.635 1.00 163.11 ? 2328 ALA B CA 1 ATOM 9834 C C . ALA B 2 681 ? -48.733 -28.261 53.187 1.00 170.92 ? 2328 ALA B C 1 ATOM 9835 O O . ALA B 2 681 ? -48.774 -29.420 52.769 1.00 164.68 ? 2328 ALA B O 1 ATOM 9836 C CB . ALA B 2 681 ? -47.995 -25.862 52.968 1.00 162.13 ? 2328 ALA B CB 1 ATOM 9837 N N . GLN B 2 682 ? -49.557 -27.795 54.139 1.00 181.62 ? 2329 GLN B N 1 ATOM 9838 C CA . GLN B 2 682 ? -50.688 -28.594 54.665 1.00 200.40 ? 2329 GLN B CA 1 ATOM 9839 C C . GLN B 2 682 ? -51.842 -28.652 53.655 1.00 214.26 ? 2329 GLN B C 1 ATOM 9840 O O . GLN B 2 682 ? -52.746 -27.800 53.681 1.00 213.27 ? 2329 GLN B O 1 ATOM 9841 C CB . GLN B 2 682 ? -51.174 -28.087 56.037 1.00 205.07 ? 2329 GLN B CB 1 ATOM 9842 C CG . GLN B 2 682 ? -50.324 -28.563 57.223 1.00 213.65 ? 2329 GLN B CG 1 ATOM 9843 C CD . GLN B 2 682 ? -50.986 -29.598 58.150 1.00 208.19 ? 2329 GLN B CD 1 ATOM 9844 O OE1 . GLN B 2 682 ? -50.584 -30.775 58.197 1.00 202.69 ? 2329 GLN B OE1 1 ATOM 9845 N NE2 . GLN B 2 682 ? -51.969 -29.149 58.927 1.00 196.54 ? 2329 GLN B NE2 1 ATOM 9846 N N . ASP B 2 683 ? -51.796 -29.683 52.796 1.00 228.56 ? 2330 ASP B N 1 ATOM 9847 C CA . ASP B 2 683 ? -52.588 -29.787 51.547 1.00 226.80 ? 2330 ASP B CA 1 ATOM 9848 C C . ASP B 2 683 ? -54.034 -30.265 51.742 1.00 220.09 ? 2330 ASP B C 1 ATOM 9849 O O . ASP B 2 683 ? -54.273 -31.461 51.950 1.00 210.78 ? 2330 ASP B O 1 ATOM 9850 C CB . ASP B 2 683 ? -51.851 -30.654 50.499 1.00 229.76 ? 2330 ASP B CB 1 ATOM 9851 C CG . ASP B 2 683 ? -50.527 -30.016 49.997 1.00 229.90 ? 2330 ASP B CG 1 ATOM 9852 O OD1 . ASP B 2 683 ? -50.162 -28.889 50.402 1.00 221.63 ? 2330 ASP B OD1 1 ATOM 9853 O OD2 . ASP B 2 683 ? -49.836 -30.655 49.178 1.00 229.55 ? 2330 ASP B OD2 1 ATOM 9854 N N . LEU B 2 684 ? -54.961 -29.304 51.588 1.00 220.88 ? 2331 LEU B N 1 ATOM 9855 C CA . LEU B 2 684 ? -56.378 -29.288 52.069 1.00 229.24 ? 2331 LEU B CA 1 ATOM 9856 C C . LEU B 2 684 ? -56.522 -28.258 53.254 1.00 232.33 ? 2331 LEU B C 1 ATOM 9857 O O . LEU B 2 684 ? -55.700 -27.333 53.360 1.00 220.59 ? 2331 LEU B O 1 ATOM 9858 C CB . LEU B 2 684 ? -56.966 -30.706 52.371 1.00 232.59 ? 2331 LEU B CB 1 ATOM 9859 C CG . LEU B 2 684 ? -57.697 -31.578 51.309 1.00 221.32 ? 2331 LEU B CG 1 ATOM 9860 C CD1 . LEU B 2 684 ? -57.519 -33.080 51.530 1.00 204.89 ? 2331 LEU B CD1 1 ATOM 9861 C CD2 . LEU B 2 684 ? -59.182 -31.242 51.208 1.00 222.36 ? 2331 LEU B CD2 1 ATOM 9862 N N . TYR B 2 685 ? -57.565 -28.400 54.090 1.00 235.29 ? 2332 TYR B N 1 ATOM 9863 C CA . TYR B 2 685 ? -57.809 -27.626 55.355 1.00 228.26 ? 2332 TYR B CA 1 ATOM 9864 C C . TYR B 2 685 ? -56.557 -27.327 56.189 1.00 229.88 ? 2332 TYR B C 1 ATOM 9865 O O . TYR B 2 685 ? -55.761 -26.437 55.861 1.00 228.75 ? 2332 TYR B O 1 ATOM 9866 C CB . TYR B 2 685 ? -58.812 -28.399 56.229 1.00 215.29 ? 2332 TYR B CB 1 ATOM 9867 C CG . TYR B 2 685 ? -58.776 -29.856 55.846 1.00 219.02 ? 2332 TYR B CG 1 ATOM 9868 C CD1 . TYR B 2 685 ? -57.653 -30.635 56.135 1.00 212.77 ? 2332 TYR B CD1 1 ATOM 9869 C CD2 . TYR B 2 685 ? -59.808 -30.440 55.104 1.00 227.60 ? 2332 TYR B CD2 1 ATOM 9870 C CE1 . TYR B 2 685 ? -57.572 -31.965 55.745 1.00 210.33 ? 2332 TYR B CE1 1 ATOM 9871 C CE2 . TYR B 2 685 ? -59.739 -31.777 54.713 1.00 228.22 ? 2332 TYR B CE2 1 ATOM 9872 C CZ . TYR B 2 685 ? -58.609 -32.533 55.038 1.00 217.57 ? 2332 TYR B CZ 1 ATOM 9873 O OH . TYR B 2 685 ? -58.495 -33.852 54.669 1.00 213.16 ? 2332 TYR B OH 1 HETATM 9874 ZN ZN . ZN C 3 . ? -46.020 -46.934 91.765 1.00 144.14 ? 800 ZN A ZN 1 HETATM 9875 CA CA . CA D 4 . ? -45.562 -26.004 64.360 1.00 130.36 ? 801 CA A CA 1 HETATM 9876 C C1 . NAG E 5 . ? -56.123 -43.904 100.096 1.00 199.21 ? 1755 NAG A C1 1 HETATM 9877 C C2 . NAG E 5 . ? -55.119 -44.857 100.808 1.00 237.33 ? 1755 NAG A C2 1 HETATM 9878 C C3 . NAG E 5 . ? -54.443 -44.326 102.115 1.00 231.21 ? 1755 NAG A C3 1 HETATM 9879 C C4 . NAG E 5 . ? -54.344 -42.796 102.304 1.00 227.31 ? 1755 NAG A C4 1 HETATM 9880 C C5 . NAG E 5 . ? -55.338 -42.003 101.404 1.00 223.55 ? 1755 NAG A C5 1 HETATM 9881 C C6 . NAG E 5 . ? -54.582 -41.241 100.308 1.00 213.13 ? 1755 NAG A C6 1 HETATM 9882 C C7 . NAG E 5 . ? -55.335 -47.378 100.424 1.00 241.93 ? 1755 NAG A C7 1 HETATM 9883 C C8 . NAG E 5 . ? -56.223 -48.584 100.625 1.00 201.13 ? 1755 NAG A C8 1 HETATM 9884 N N2 . NAG E 5 . ? -55.775 -46.185 100.899 1.00 258.83 ? 1755 NAG A N2 1 HETATM 9885 O O3 . NAG E 5 . ? -53.107 -44.800 102.198 1.00 207.65 ? 1755 NAG A O3 1 HETATM 9886 O O4 . NAG E 5 . ? -54.457 -42.360 103.680 1.00 237.66 ? 1755 NAG A O4 1 HETATM 9887 O O5 . NAG E 5 . ? -56.443 -42.736 100.837 1.00 197.88 ? 1755 NAG A O5 1 HETATM 9888 O O6 . NAG E 5 . ? -55.210 -40.007 100.053 1.00 212.87 ? 1755 NAG A O6 1 HETATM 9889 O O7 . NAG E 5 . ? -54.253 -47.544 99.853 1.00 245.73 ? 1755 NAG A O7 1 HETATM 9890 C C1 . NAG F 5 . ? -53.404 -42.587 104.689 1.00 242.59 ? 1756 NAG A C1 1 HETATM 9891 C C2 . NAG F 5 . ? -52.170 -41.675 104.570 1.00 262.20 ? 1756 NAG A C2 1 HETATM 9892 C C3 . NAG F 5 . ? -52.624 -40.217 104.664 1.00 300.30 ? 1756 NAG A C3 1 HETATM 9893 C C4 . NAG F 5 . ? -53.583 -39.997 105.849 1.00 320.88 ? 1756 NAG A C4 1 HETATM 9894 C C5 . NAG F 5 . ? -53.675 -41.237 106.758 1.00 298.23 ? 1756 NAG A C5 1 HETATM 9895 C C6 . NAG F 5 . ? -54.663 -41.014 107.922 1.00 280.15 ? 1756 NAG A C6 1 HETATM 9896 C C7 . NAG F 5 . ? -50.333 -42.826 105.903 1.00 245.54 ? 1756 NAG A C7 1 HETATM 9897 C C8 . NAG F 5 . ? -49.450 -42.679 107.125 1.00 217.77 ? 1756 NAG A C8 1 HETATM 9898 N N2 . NAG F 5 . ? -51.193 -41.836 105.657 1.00 256.50 ? 1756 NAG A N2 1 HETATM 9899 O O3 . NAG F 5 . ? -53.226 -39.810 103.451 1.00 294.81 ? 1756 NAG A O3 1 HETATM 9900 O O4 . NAG F 5 . ? -53.165 -38.885 106.622 1.00 356.90 ? 1756 NAG A O4 1 HETATM 9901 O O5 . NAG F 5 . ? -53.940 -42.445 106.012 1.00 251.70 ? 1756 NAG A O5 1 HETATM 9902 O O6 . NAG F 5 . ? -54.203 -40.066 108.878 1.00 241.27 ? 1756 NAG A O6 1 HETATM 9903 O O7 . NAG F 5 . ? -50.251 -43.815 105.180 1.00 252.47 ? 1756 NAG A O7 1 HETATM 9904 C C1 . EDO G 6 . ? -40.556 -49.931 76.097 1.00 186.38 ? 3333 EDO A C1 1 HETATM 9905 O O1 . EDO G 6 . ? -39.153 -50.118 75.865 1.00 170.35 ? 3333 EDO A O1 1 HETATM 9906 C C2 . EDO G 6 . ? -41.032 -48.692 75.343 1.00 187.42 ? 3333 EDO A C2 1 HETATM 9907 O O2 . EDO G 6 . ? -42.461 -48.669 75.246 1.00 174.37 ? 3333 EDO A O2 1 HETATM 9908 CU CU . CU1 H 7 . ? -34.427 -37.540 80.425 1.00 133.45 ? 1 CU1 B CU 1 HETATM 9909 C C1 . NAG I 5 . ? -19.802 -37.979 51.053 1.00 151.53 ? 2334 NAG B C1 1 HETATM 9910 C C2 . NAG I 5 . ? -19.695 -38.684 49.692 1.00 172.27 ? 2334 NAG B C2 1 HETATM 9911 C C3 . NAG I 5 . ? -20.730 -39.821 49.570 1.00 179.17 ? 2334 NAG B C3 1 HETATM 9912 C C4 . NAG I 5 . ? -21.825 -39.826 50.648 1.00 205.08 ? 2334 NAG B C4 1 HETATM 9913 C C5 . NAG I 5 . ? -21.243 -39.532 52.064 1.00 206.53 ? 2334 NAG B C5 1 HETATM 9914 C C6 . NAG I 5 . ? -21.283 -40.748 53.005 1.00 209.05 ? 2334 NAG B C6 1 HETATM 9915 C C7 . NAG I 5 . ? -18.815 -37.557 47.597 1.00 173.93 ? 2334 NAG B C7 1 HETATM 9916 C C8 . NAG I 5 . ? -17.429 -38.171 47.647 1.00 159.19 ? 2334 NAG B C8 1 HETATM 9917 N N2 . NAG I 5 . ? -19.781 -37.799 48.523 1.00 171.35 ? 2334 NAG B N2 1 HETATM 9918 O O3 . NAG I 5 . ? -20.120 -41.100 49.568 1.00 173.03 ? 2334 NAG B O3 1 HETATM 9919 O O4 . NAG I 5 . ? -22.892 -38.935 50.279 1.00 221.19 ? 2334 NAG B O4 1 HETATM 9920 O O5 . NAG I 5 . ? -19.915 -39.005 52.017 1.00 171.52 ? 2334 NAG B O5 1 HETATM 9921 O O6 . NAG I 5 . ? -20.940 -40.420 54.341 1.00 173.43 ? 2334 NAG B O6 1 HETATM 9922 O O7 . NAG I 5 . ? -19.045 -36.802 46.662 1.00 157.37 ? 2334 NAG B O7 1 HETATM 9923 C C1 . NAG J 5 . ? -23.896 -39.414 49.321 1.00 216.86 ? 2335 NAG B C1 1 HETATM 9924 C C2 . NAG J 5 . ? -23.315 -39.425 47.877 1.00 234.10 ? 2335 NAG B C2 1 HETATM 9925 C C3 . NAG J 5 . ? -23.506 -40.789 47.137 1.00 224.43 ? 2335 NAG B C3 1 HETATM 9926 C C4 . NAG J 5 . ? -24.701 -41.709 47.487 1.00 205.60 ? 2335 NAG B C4 1 HETATM 9927 C C5 . NAG J 5 . ? -25.389 -41.299 48.802 1.00 186.53 ? 2335 NAG B C5 1 HETATM 9928 C C6 . NAG J 5 . ? -25.889 -42.555 49.503 1.00 180.36 ? 2335 NAG B C6 1 HETATM 9929 C C7 . NAG J 5 . ? -23.298 -36.921 47.090 1.00 212.59 ? 2335 NAG B C7 1 HETATM 9930 C C8 . NAG J 5 . ? -23.884 -35.983 46.046 1.00 164.55 ? 2335 NAG B C8 1 HETATM 9931 N N2 . NAG J 5 . ? -23.679 -38.234 47.039 1.00 248.03 ? 2335 NAG B N2 1 HETATM 9932 O O3 . NAG J 5 . ? -22.352 -41.587 47.304 1.00 223.63 ? 2335 NAG B O3 1 HETATM 9933 O O4 . NAG J 5 . ? -25.572 -41.747 46.346 1.00 217.14 ? 2335 NAG B O4 1 HETATM 9934 O O5 . NAG J 5 . ? -24.549 -40.621 49.732 1.00 180.40 ? 2335 NAG B O5 1 HETATM 9935 O O6 . NAG J 5 . ? -24.953 -43.599 49.367 1.00 167.48 ? 2335 NAG B O6 1 HETATM 9936 O O7 . NAG J 5 . ? -22.526 -36.445 47.932 1.00 186.69 ? 2335 NAG B O7 1 HETATM 9937 C C1 . BMA K 8 . ? -26.508 -42.830 45.975 1.00 236.08 ? 2336 BMA B C1 1 HETATM 9938 C C2 . BMA K 8 . ? -26.030 -44.287 45.891 1.00 250.55 ? 2336 BMA B C2 1 HETATM 9939 C C3 . BMA K 8 . ? -26.985 -45.016 44.915 1.00 263.90 ? 2336 BMA B C3 1 HETATM 9940 C C4 . BMA K 8 . ? -28.490 -44.702 45.141 1.00 239.60 ? 2336 BMA B C4 1 HETATM 9941 C C5 . BMA K 8 . ? -28.848 -43.334 45.756 1.00 236.58 ? 2336 BMA B C5 1 HETATM 9942 C C6 . BMA K 8 . ? -30.113 -43.410 46.629 1.00 237.87 ? 2336 BMA B C6 1 HETATM 9943 O O2 . BMA K 8 . ? -26.030 -44.914 47.157 1.00 240.31 ? 2336 BMA B O2 1 HETATM 9944 O O3 . BMA K 8 . ? -26.739 -46.425 44.854 1.00 297.90 ? 2336 BMA B O3 1 HETATM 9945 O O4 . BMA K 8 . ? -29.175 -44.799 43.907 1.00 202.80 ? 2336 BMA B O4 1 HETATM 9946 O O5 . BMA K 8 . ? -27.800 -42.808 46.572 1.00 258.90 ? 2336 BMA B O5 1 HETATM 9947 O O6 . BMA K 8 . ? -31.336 -43.665 45.952 1.00 229.08 ? 2336 BMA B O6 1 HETATM 9948 C C1 . BMA L 8 . ? -26.464 -46.831 43.480 1.00 291.47 ? 2337 BMA B C1 1 HETATM 9949 C C2 . BMA L 8 . ? -25.312 -47.857 43.373 1.00 275.61 ? 2337 BMA B C2 1 HETATM 9950 C C3 . BMA L 8 . ? -25.228 -48.590 42.003 1.00 279.90 ? 2337 BMA B C3 1 HETATM 9951 C C4 . BMA L 8 . ? -26.485 -48.546 41.104 1.00 279.32 ? 2337 BMA B C4 1 HETATM 9952 C C5 . BMA L 8 . ? -27.343 -47.307 41.360 1.00 263.14 ? 2337 BMA B C5 1 HETATM 9953 C C6 . BMA L 8 . ? -28.639 -47.321 40.562 1.00 227.86 ? 2337 BMA B C6 1 HETATM 9954 O O2 . BMA L 8 . ? -25.316 -48.754 44.475 1.00 231.89 ? 2337 BMA B O2 1 HETATM 9955 O O3 . BMA L 8 . ? -24.834 -49.934 42.191 1.00 291.35 ? 2337 BMA B O3 1 HETATM 9956 O O4 . BMA L 8 . ? -26.130 -48.623 39.731 1.00 270.31 ? 2337 BMA B O4 1 HETATM 9957 O O5 . BMA L 8 . ? -27.614 -47.238 42.746 1.00 284.28 ? 2337 BMA B O5 1 HETATM 9958 O O6 . BMA L 8 . ? -28.389 -46.681 39.331 1.00 221.83 ? 2337 BMA B O6 1 HETATM 9959 C C1 . BMA M 8 . ? -31.837 -45.014 46.185 1.00 247.49 ? 2338 BMA B C1 1 HETATM 9960 C C2 . BMA M 8 . ? -31.766 -45.476 47.654 1.00 253.31 ? 2338 BMA B C2 1 HETATM 9961 C C3 . BMA M 8 . ? -32.176 -46.958 47.767 1.00 251.90 ? 2338 BMA B C3 1 HETATM 9962 C C4 . BMA M 8 . ? -33.537 -47.192 47.109 1.00 265.59 ? 2338 BMA B C4 1 HETATM 9963 C C5 . BMA M 8 . ? -33.612 -46.572 45.692 1.00 269.84 ? 2338 BMA B C5 1 HETATM 9964 C C6 . BMA M 8 . ? -35.034 -46.614 45.115 1.00 270.35 ? 2338 BMA B C6 1 HETATM 9965 O O2 . BMA M 8 . ? -32.582 -44.636 48.443 1.00 248.40 ? 2338 BMA B O2 1 HETATM 9966 O O3 . BMA M 8 . ? -32.194 -47.455 49.097 1.00 211.92 ? 2338 BMA B O3 1 HETATM 9967 O O4 . BMA M 8 . ? -33.773 -48.586 47.104 1.00 269.03 ? 2338 BMA B O4 1 HETATM 9968 O O5 . BMA M 8 . ? -33.152 -45.219 45.681 1.00 253.93 ? 2338 BMA B O5 1 HETATM 9969 O O6 . BMA M 8 . ? -35.041 -46.865 43.722 1.00 244.83 ? 2338 BMA B O6 1 HETATM 9970 C C1 . EDO N 6 . ? -17.242 -41.636 56.880 1.00 134.20 ? 3333 EDO B C1 1 HETATM 9971 O O1 . EDO N 6 . ? -16.925 -40.886 55.693 1.00 129.02 ? 3333 EDO B O1 1 HETATM 9972 C C2 . EDO N 6 . ? -18.553 -42.409 56.718 1.00 143.66 ? 3333 EDO B C2 1 HETATM 9973 O O2 . EDO N 6 . ? -19.491 -41.745 55.847 1.00 141.61 ? 3333 EDO B O2 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ALA A 1 ? 2.1599 1.9484 1.8258 0.0261 -0.0371 0.4923 1 ALA A N 2 C CA . ALA A 1 ? 2.2716 2.0295 1.8924 0.0475 0.0078 0.4791 1 ALA A CA 3 C C . ALA A 1 ? 2.2730 2.0690 1.9762 0.0739 0.0350 0.5112 1 ALA A C 4 O O . ALA A 1 ? 2.6010 2.3825 2.2706 0.0819 0.0407 0.5286 1 ALA A O 5 C CB . ALA A 1 ? 2.3027 2.0101 1.8055 0.0338 -0.0148 0.4784 1 ALA A CB 6 N N . THR A 2 ? 2.0237 1.8626 1.8284 0.0882 0.0541 0.5192 2 THR A N 7 C CA . THR A 2 ? 2.0077 1.8754 1.8904 0.1156 0.0835 0.5483 2 THR A CA 8 C C . THR A 2 ? 2.0270 1.9436 2.0211 0.1298 0.0969 0.5648 2 THR A C 9 O O . THR A 2 ? 2.1707 2.1274 2.2155 0.1188 0.0616 0.5929 2 THR A O 10 C CB . THR A 2 ? 2.0666 1.9409 1.9399 0.1165 0.0572 0.5933 2 THR A CB 11 O OG1 . THR A 2 ? 2.0366 1.9031 1.9329 0.1428 0.0991 0.6027 2 THR A OG1 12 C CG2 . THR A 2 ? 1.9422 1.8709 1.8878 0.1081 0.0091 0.6439 2 THR A CG2 13 N N . ARG A 3 ? 2.0469 1.9595 2.0791 0.1542 0.1476 0.5506 3 ARG A N 14 C CA . ARG A 3 ? 2.0075 1.9510 2.1188 0.1659 0.1686 0.5501 3 ARG A CA 15 C C . ARG A 3 ? 2.0083 1.9576 2.1838 0.1982 0.2154 0.5615 3 ARG A C 16 O O . ARG A 3 ? 2.0735 1.9969 2.2384 0.2081 0.2543 0.5278 3 ARG A O 17 C CB . ARG A 3 ? 1.9384 1.8561 2.0079 0.1563 0.1843 0.5007 3 ARG A CB 18 C CG . ARG A 3 ? 1.8763 1.8237 1.9929 0.1491 0.1769 0.4985 3 ARG A CG 19 C CD . ARG A 3 ? 1.8989 1.8178 1.9496 0.1268 0.1637 0.4593 3 ARG A CD 20 N NE . ARG A 3 ? 2.0626 1.9758 2.0676 0.1000 0.1128 0.4676 3 ARG A NE 21 C CZ . ARG A 3 ? 2.1370 2.0408 2.1142 0.0766 0.0863 0.4504 3 ARG A CZ 22 N NH1 . ARG A 3 ? 2.2464 2.1502 2.2413 0.0780 0.1067 0.4262 3 ARG A NH1 23 N NH2 . ARG A 3 ? 2.1863 2.0762 2.1136 0.0509 0.0381 0.4576 3 ARG A NH2 24 N N . ARG A 4 ? 1.9503 1.9304 2.1917 0.2145 0.2120 0.6082 4 ARG A N 25 C CA . ARG A 4 ? 1.9655 1.9355 2.2536 0.2473 0.2603 0.6166 4 ARG A CA 26 C C . ARG A 4 ? 1.9852 1.9689 2.3349 0.2667 0.2977 0.6105 4 ARG A C 27 O O . ARG A 4 ? 1.9532 1.9840 2.3671 0.2673 0.2853 0.6363 4 ARG A O 28 C CB . ARG A 4 ? 1.9936 1.9809 2.3253 0.2635 0.2521 0.6681 4 ARG A CB 29 C CG . ARG A 4 ? 2.0810 2.0361 2.4348 0.2951 0.3032 0.6690 4 ARG A CG 30 C CD . ARG A 4 ? 2.2052 2.1710 2.5979 0.3123 0.2965 0.7204 4 ARG A CD 31 N NE . ARG A 4 ? 2.3287 2.2661 2.6500 0.2978 0.2760 0.7209 4 ARG A NE 32 C CZ . ARG A 4 ? 2.3821 2.3403 2.6736 0.2763 0.2248 0.7449 4 ARG A CZ 33 N NH1 . ARG A 4 ? 2.4814 2.4910 2.8132 0.2637 0.1835 0.7712 4 ARG A NH1 34 N NH2 . ARG A 4 ? 2.1691 2.0945 2.3874 0.2660 0.2140 0.7437 4 ARG A NH2 35 N N . TYR A 5 ? 2.0268 1.9669 2.3550 0.2820 0.3435 0.5784 5 TYR A N 36 C CA . TYR A 5 ? 1.9219 1.8581 2.2831 0.2998 0.3838 0.5635 5 TYR A CA 37 C C . TYR A 5 ? 1.9979 1.9064 2.3911 0.3336 0.4308 0.5740 5 TYR A C 38 O O . TYR A 5 ? 1.9495 1.8064 2.2989 0.3376 0.4513 0.5525 5 TYR A O 39 C CB . TYR A 5 ? 1.7247 1.6270 2.0216 0.2840 0.3937 0.5101 5 TYR A CB 40 C CG . TYR A 5 ? 1.6951 1.6233 1.9746 0.2572 0.3582 0.4994 5 TYR A CG 41 C CD1 . TYR A 5 ? 1.8235 1.8032 2.1518 0.2484 0.3238 0.5349 5 TYR A CD1 42 C CD2 . TYR A 5 ? 1.7606 1.6612 1.9794 0.2402 0.3585 0.4556 5 TYR A CD2 43 C CE1 . TYR A 5 ? 2.0429 2.0390 2.3529 0.2216 0.2901 0.5240 5 TYR A CE1 44 C CE2 . TYR A 5 ? 1.9357 1.8533 2.1374 0.2170 0.3282 0.4451 5 TYR A CE2 45 C CZ . TYR A 5 ? 2.1140 2.0759 2.3583 0.2071 0.2942 0.4777 5 TYR A CZ 46 O OH . TYR A 5 ? 2.2762 2.2475 2.5009 0.1822 0.2635 0.4659 5 TYR A OH 47 N N . TYR A 6 ? 1.9061 1.8464 2.3767 0.3579 0.4496 0.6075 6 TYR A N 48 C CA . TYR A 6 ? 1.8930 1.8089 2.4020 0.3937 0.4922 0.6273 6 TYR A CA 49 C C . TYR A 6 ? 1.9332 1.7892 2.4124 0.4121 0.5466 0.5894 6 TYR A C 50 O O . TYR A 6 ? 1.9384 1.7736 2.4549 0.4456 0.5884 0.6058 6 TYR A O 51 C CB . TYR A 6 ? 1.8543 1.8300 2.4650 0.4159 0.4902 0.6877 6 TYR A CB 52 C CG . TYR A 6 ? 1.9455 1.9433 2.5801 0.4148 0.4562 0.7313 6 TYR A CG 53 C CD1 . TYR A 6 ? 1.9672 1.9424 2.5290 0.3880 0.4219 0.7148 6 TYR A CD1 54 C CD2 . TYR A 6 ? 1.9741 2.0142 2.7030 0.4418 0.4603 0.7910 6 TYR A CD2 55 C CE1 . TYR A 6 ? 2.0292 2.0200 2.6026 0.3864 0.3910 0.7547 6 TYR A CE1 56 C CE2 . TYR A 6 ? 2.0302 2.0901 2.7781 0.4398 0.4259 0.8334 6 TYR A CE2 57 C CZ . TYR A 6 ? 2.0954 2.1283 2.7600 0.4111 0.3907 0.8138 6 TYR A CZ 58 O OH . TYR A 6 ? 2.2472 2.2945 2.9178 0.4075 0.3562 0.8547 6 TYR A OH 59 N N . LEU A 7 ? 1.8058 1.6296 2.2133 0.3896 0.5443 0.5395 7 LEU A N 60 C CA . LEU A 7 ? 1.7566 1.5260 2.1212 0.3966 0.5840 0.4976 7 LEU A CA 61 C C . LEU A 7 ? 1.9007 1.6056 2.2595 0.4262 0.6334 0.4923 7 LEU A C 62 O O . LEU A 7 ? 1.9976 1.6794 2.3622 0.4351 0.6361 0.5079 7 LEU A O 63 C CB . LEU A 7 ? 1.6739 1.4167 1.9624 0.3647 0.5632 0.4529 7 LEU A CB 64 C CG . LEU A 7 ? 1.8441 1.5592 2.0880 0.3569 0.5798 0.4109 7 LEU A CG 65 C CD1 . LEU A 7 ? 1.9450 1.6813 2.1523 0.3244 0.5433 0.3880 7 LEU A CD1 66 C CD2 . LEU A 7 ? 1.9177 1.5577 2.1113 0.3619 0.6099 0.3792 7 LEU A CD2 67 N N . GLY A 8 ? 1.9210 1.5916 2.2626 0.4409 0.6726 0.4698 8 GLY A N 68 C CA . GLY A 8 ? 1.9869 1.5829 2.3092 0.4686 0.7227 0.4583 8 GLY A CA 69 C C . GLY A 8 ? 2.0942 1.6276 2.3418 0.4626 0.7476 0.4082 8 GLY A C 70 O O . GLY A 8 ? 2.0294 1.5881 2.2621 0.4498 0.7397 0.3930 8 GLY A O 71 N N . ALA A 9 ? 2.1671 1.6159 2.3654 0.4703 0.7754 0.3833 9 ALA A N 72 C CA . ALA A 9 ? 2.2521 1.6342 2.3644 0.4537 0.7850 0.3317 9 ALA A CA 73 C C . ALA A 9 ? 2.3401 1.6549 2.4220 0.4831 0.8389 0.3180 9 ALA A C 74 O O . ALA A 9 ? 2.4048 1.6322 2.4340 0.4868 0.8607 0.2937 9 ALA A O 75 C CB . ALA A 9 ? 2.2871 1.6175 2.3492 0.4276 0.7654 0.3054 9 ALA A CB 76 N N . VAL A 10 ? 2.4179 1.7703 2.5276 0.5015 0.8598 0.3323 10 VAL A N 77 C CA . VAL A 10 ? 2.5845 1.8862 2.6817 0.5394 0.9202 0.3320 10 VAL A CA 78 C C . VAL A 10 ? 2.6959 1.9305 2.6957 0.5304 0.9391 0.2850 10 VAL A C 79 O O . VAL A 10 ? 2.8349 2.0943 2.8014 0.4990 0.9065 0.2637 10 VAL A O 80 C CB . VAL A 10 ? 2.4974 1.8805 2.6897 0.5689 0.9390 0.3820 10 VAL A CB 81 C CG1 . VAL A 10 ? 2.4849 1.8226 2.6657 0.6102 1.0072 0.3836 10 VAL A CG1 82 C CG2 . VAL A 10 ? 2.3829 1.8178 2.6660 0.5817 0.9241 0.4305 10 VAL A CG2 83 N N . GLU A 11 ? 2.7216 1.8667 2.6723 0.5586 0.9919 0.2695 11 GLU A N 84 C CA . GLU A 11 ? 2.7537 1.8294 2.6066 0.5547 1.0149 0.2288 11 GLU A CA 85 C C . GLU A 11 ? 2.8157 1.9145 2.6961 0.5923 1.0658 0.2521 11 GLU A C 86 O O . GLU A 11 ? 2.9168 1.9912 2.8308 0.6363 1.1192 0.2756 11 GLU A O 87 C CB . GLU A 11 ? 2.8800 1.8263 2.6390 0.5561 1.0380 0.1894 11 GLU A CB 88 C CG . GLU A 11 ? 2.9604 1.8613 2.7555 0.5926 1.0765 0.2105 11 GLU A CG 89 C CD . GLU A 11 ? 3.0771 1.8626 2.7909 0.5773 1.0749 0.1724 11 GLU A CD 90 O OE1 . GLU A 11 ? 2.9577 1.7302 2.6223 0.5314 1.0264 0.1417 11 GLU A OE1 91 O OE2 . GLU A 11 ? 3.3458 2.0527 3.0487 0.6114 1.1226 0.1749 11 GLU A OE2 92 N N . LEU A 12 ? 2.6688 1.8186 2.5422 0.5759 1.0503 0.2494 12 LEU A N 93 C CA . LEU A 12 ? 2.6685 1.8260 2.5462 0.6073 1.1018 0.2644 12 LEU A CA 94 C C . LEU A 12 ? 2.5545 1.6435 2.3107 0.5923 1.1117 0.2195 12 LEU A C 95 O O . LEU A 12 ? 2.5392 1.5412 2.1973 0.5705 1.0976 0.1748 12 LEU A O 96 C CB . LEU A 12 ? 2.6562 1.9390 2.6574 0.6159 1.0927 0.3187 12 LEU A CB 97 C CG . LEU A 12 ? 2.8086 2.1348 2.9231 0.6565 1.1227 0.3726 12 LEU A CG 98 C CD1 . LEU A 12 ? 2.4491 1.8936 2.6765 0.6384 1.0691 0.4160 12 LEU A CD1 99 C CD2 . LEU A 12 ? 2.7792 2.0938 2.9227 0.7091 1.2010 0.4002 12 LEU A CD2 100 N N . SER A 13 ? 2.4536 1.5790 2.2156 0.6033 1.1352 0.2333 13 SER A N 101 C CA . SER A 13 ? 2.5151 1.5637 2.1577 0.6020 1.1625 0.1976 13 SER A CA 102 C C . SER A 13 ? 2.4841 1.5953 2.1214 0.5769 1.1355 0.2001 13 SER A C 103 O O . SER A 13 ? 2.5014 1.6967 2.2256 0.5920 1.1492 0.2416 13 SER A O 104 C CB . SER A 13 ? 2.5570 1.5412 2.1773 0.6562 1.2486 0.2073 13 SER A CB 105 O OG . SER A 13 ? 2.3742 1.4136 2.1164 0.6944 1.2791 0.2569 13 SER A OG 106 N N . TRP A 14 ? 2.5044 1.5753 2.0450 0.5394 1.0980 0.1596 14 TRP A N 107 C CA . TRP A 14 ? 2.6678 1.8113 2.2228 0.5080 1.0545 0.1648 14 TRP A CA 108 C C . TRP A 14 ? 2.9325 2.0690 2.4303 0.5122 1.0806 0.1641 14 TRP A C 109 O O . TRP A 14 ? 3.3303 2.3944 2.7579 0.5413 1.1393 0.1556 14 TRP A O 110 C CB . TRP A 14 ? 2.7131 1.8498 2.2310 0.4605 0.9853 0.1329 14 TRP A CB 111 C CG . TRP A 14 ? 2.7814 2.0088 2.3507 0.4323 0.9369 0.1473 14 TRP A CG 112 C CD1 . TRP A 14 ? 2.8662 2.0916 2.3829 0.3957 0.8914 0.1233 14 TRP A CD1 113 C CD2 . TRP A 14 ? 2.5770 1.9071 2.2604 0.4389 0.9301 0.1905 14 TRP A CD2 114 N NE1 . TRP A 14 ? 2.7672 2.0837 2.3567 0.3815 0.8599 0.1475 14 TRP A NE1 115 C CE2 . TRP A 14 ? 2.5638 1.9430 2.2526 0.4056 0.8813 0.1875 14 TRP A CE2 116 C CE3 . TRP A 14 ? 2.3116 1.6959 2.0948 0.4690 0.9589 0.2333 14 TRP A CE3 117 C CZ2 . TRP A 14 ? 2.3272 1.7995 2.1097 0.4000 0.8606 0.2220 14 TRP A CZ2 118 C CZ3 . TRP A 14 ? 2.1397 1.6212 2.0186 0.4611 0.9347 0.2693 14 TRP A CZ3 119 C CH2 . TRP A 14 ? 2.2010 1.7221 2.0756 0.4261 0.8859 0.2618 14 TRP A CH2 120 N N . ASP A 15 ? 2.8523 2.0622 2.3814 0.4857 1.0406 0.1755 15 ASP A N 121 C CA . ASP A 15 ? 2.7163 1.9003 2.1572 0.4711 1.0395 0.1591 15 ASP A CA 122 C C . ASP A 15 ? 2.6491 1.9078 2.1215 0.4507 1.0119 0.1784 15 ASP A C 123 O O . ASP A 15 ? 2.2463 1.5147 1.6908 0.4131 0.9552 0.1592 15 ASP A O 124 C CB . ASP A 15 ? 2.8090 1.9129 2.1657 0.5057 1.1107 0.1525 15 ASP A CB 125 C CG . ASP A 15 ? 3.0864 2.1009 2.2974 0.4842 1.0990 0.1095 15 ASP A CG 126 O OD1 . ASP A 15 ? 2.9734 1.9864 2.1593 0.4434 1.0345 0.0846 15 ASP A OD1 127 O OD2 . ASP A 15 ? 3.4227 2.3705 2.5461 0.5074 1.1530 0.1026 15 ASP A OD2 128 N N . TYR A 16 ? 2.7285 2.0338 2.2575 0.4775 1.0564 0.2172 16 TYR A N 129 C CA . TYR A 16 ? 2.6102 1.9531 2.1373 0.4733 1.0644 0.2375 16 TYR A CA 130 C C . TYR A 16 ? 2.4614 1.7818 1.9036 0.4368 1.0191 0.2100 16 TYR A C 131 O O . TYR A 16 ? 2.4014 1.6829 1.7627 0.4418 1.0461 0.2061 16 TYR A O 132 C CB . TYR A 16 ? 2.5073 1.9630 2.1764 0.4779 1.0622 0.2905 16 TYR A CB 133 C CG . TYR A 16 ? 2.6680 2.1732 2.4513 0.4989 1.0734 0.3209 16 TYR A CG 134 C CD1 . TYR A 16 ? 2.9087 2.3847 2.6889 0.4958 1.0520 0.2992 16 TYR A CD1 135 C CD2 . TYR A 16 ? 2.5926 2.1764 2.4909 0.5197 1.1020 0.3742 16 TYR A CD2 136 C CE1 . TYR A 16 ? 2.8487 2.3675 2.7286 0.5140 1.0584 0.3280 16 TYR A CE1 137 C CE2 . TYR A 16 ? 2.8253 2.4567 2.8302 0.5370 1.1061 0.4048 16 TYR A CE2 138 C CZ . TYR A 16 ? 2.8841 2.4809 2.8761 0.5345 1.0836 0.3807 16 TYR A CZ 139 O OH . TYR A 16 ? 2.7095 2.3474 2.7984 0.5506 1.0836 0.4099 16 TYR A OH 140 N N . VAL A 44 ? 3.2319 1.9546 2.0150 0.5705 1.3191 0.0766 44 VAL A N 141 C CA . VAL A 44 ? 3.5432 2.1872 2.3032 0.6103 1.3800 0.0662 44 VAL A CA 142 C C . VAL A 44 ? 3.5751 2.1680 2.3192 0.5860 1.3315 0.0291 44 VAL A C 143 O O . VAL A 44 ? 3.7957 2.2848 2.4686 0.6077 1.3706 0.0039 44 VAL A O 144 C CB . VAL A 44 ? 3.7579 2.2808 2.3675 0.6473 1.4641 0.0500 44 VAL A CB 145 C CG1 . VAL A 44 ? 3.5843 2.1308 2.2699 0.7101 1.5599 0.0927 44 VAL A CG1 146 C CG2 . VAL A 44 ? 3.7367 2.2364 2.2334 0.6260 1.4535 0.0409 44 VAL A CG2 147 N N . VAL A 45 ? 3.4963 2.1612 2.3120 0.5438 1.2513 0.0283 45 VAL A N 148 C CA . VAL A 45 ? 3.6058 2.2169 2.3873 0.5119 1.1982 -0.0097 45 VAL A CA 149 C C . VAL A 45 ? 3.6631 2.3378 2.5792 0.5120 1.1733 0.0072 45 VAL A C 150 O O . VAL A 45 ? 3.6084 2.3702 2.6504 0.5394 1.1978 0.0501 45 VAL A O 151 C CB . VAL A 45 ? 3.5128 2.1033 2.2067 0.4569 1.1243 -0.0414 45 VAL A CB 152 C CG1 . VAL A 45 ? 3.5296 2.0314 2.0685 0.4574 1.1495 -0.0631 45 VAL A CG1 153 C CG2 . VAL A 45 ? 3.1832 1.9008 1.9818 0.4290 1.0669 -0.0144 45 VAL A CG2 154 N N . TYR A 46 ? 3.7693 2.3919 2.6505 0.4828 1.1291 -0.0253 46 TYR A N 155 C CA . TYR A 46 ? 3.4907 2.1637 2.4715 0.4644 1.0820 -0.0192 46 TYR A CA 156 C C . TYR A 46 ? 3.1324 1.8878 2.2621 0.4890 1.0928 0.0205 46 TYR A C 157 O O . TYR A 46 ? 2.9726 1.8186 2.1983 0.5102 1.1113 0.0612 46 TYR A O 158 C CB . TYR A 46 ? 3.5460 2.2638 2.5304 0.4109 1.0003 -0.0321 46 TYR A CB 159 C CG . TYR A 46 ? 3.8529 2.4736 2.6955 0.3777 0.9725 -0.0762 46 TYR A CG 160 C CD1 . TYR A 46 ? 3.9805 2.4922 2.7425 0.3673 0.9700 -0.1115 46 TYR A CD1 161 C CD2 . TYR A 46 ? 4.0480 2.6830 2.8358 0.3554 0.9469 -0.0810 46 TYR A CD2 162 C CE1 . TYR A 46 ? 4.2956 2.7170 2.9268 0.3326 0.9386 -0.1507 46 TYR A CE1 163 C CE2 . TYR A 46 ? 4.2388 2.7868 2.8966 0.3229 0.9163 -0.1183 46 TYR A CE2 164 C CZ . TYR A 46 ? 4.3882 2.8301 2.9681 0.3104 0.9107 -0.1533 46 TYR A CZ 165 O OH . TYR A 46 ? 4.7766 3.1310 3.2269 0.2743 0.8750 -0.1891 46 TYR A OH 166 N N . LYS A 47 ? 3.0019 1.7308 2.1526 0.4807 1.0733 0.0105 47 LYS A N 167 C CA . LYS A 47 ? 2.9351 1.7216 2.2090 0.5077 1.0892 0.0471 47 LYS A CA 168 C C . LYS A 47 ? 2.9145 1.6925 2.2240 0.4887 1.0516 0.0405 47 LYS A C 169 O O . LYS A 47 ? 2.8209 1.4972 2.0663 0.4934 1.0691 0.0150 47 LYS A O 170 C CB . LYS A 47 ? 3.1002 1.8369 2.3717 0.5635 1.1716 0.0622 47 LYS A CB 171 C CG . LYS A 47 ? 3.0449 1.8037 2.3085 0.5922 1.2217 0.0816 47 LYS A CG 172 C CD . LYS A 47 ? 3.0271 1.6635 2.1333 0.5986 1.2605 0.0423 47 LYS A CD 173 C CE . LYS A 47 ? 2.8491 1.5255 1.9437 0.6106 1.2886 0.0604 47 LYS A CE 174 N NZ . LYS A 47 ? 2.9025 1.4706 1.8300 0.5983 1.2992 0.0175 47 LYS A NZ 175 N N . LYS A 48 ? 2.8908 1.7722 2.3027 0.4705 1.0053 0.0661 48 LYS A N 176 C CA . LYS A 48 ? 2.8607 1.7492 2.3092 0.4470 0.9628 0.0632 48 LYS A CA 177 C C . LYS A 48 ? 2.8199 1.8026 2.3980 0.4582 0.9502 0.1072 48 LYS A C 178 O O . LYS A 48 ? 2.8273 1.8827 2.4825 0.4830 0.9693 0.1444 48 LYS A O 179 C CB . LYS A 48 ? 2.6548 1.5419 2.0548 0.3953 0.9006 0.0333 48 LYS A CB 180 C CG . LYS A 48 ? 2.5324 1.4537 1.8986 0.3763 0.8799 0.0256 48 LYS A CG 181 C CD . LYS A 48 ? 2.4601 1.5004 1.9233 0.3799 0.8659 0.0621 48 LYS A CD 182 C CE . LYS A 48 ? 2.5415 1.6209 1.9809 0.3477 0.8244 0.0522 48 LYS A CE 183 N NZ . LYS A 48 ? 2.4870 1.5319 1.8472 0.3500 0.8433 0.0390 48 LYS A NZ 184 N N . THR A 49 ? 2.7906 1.7695 2.3888 0.4382 0.9170 0.1038 49 THR A N 185 C CA . THR A 49 ? 2.5737 1.6320 2.2772 0.4417 0.8963 0.1416 49 THR A CA 186 C C . THR A 49 ? 2.3834 1.5407 2.1375 0.4114 0.8421 0.1542 49 THR A C 187 O O . THR A 49 ? 2.3132 1.4639 2.0238 0.3762 0.8050 0.1279 49 THR A O 188 C CB . THR A 49 ? 2.6843 1.6879 2.3851 0.4371 0.8909 0.1362 49 THR A CB 189 O OG1 . THR A 49 ? 2.4742 1.5476 2.2352 0.4142 0.8448 0.1541 49 THR A OG1 190 C CG2 . THR A 49 ? 2.8159 1.7155 2.4140 0.4121 0.8844 0.0896 49 THR A CG2 191 N N . LEU A 50 ? 2.3477 1.5925 2.1929 0.4250 0.8371 0.1950 50 LEU A N 192 C CA . LEU A 50 ? 2.2596 1.5955 2.1518 0.3993 0.7886 0.2089 50 LEU A CA 193 C C . LEU A 50 ? 2.2312 1.6439 2.2176 0.4077 0.7721 0.2526 50 LEU A C 194 O O . LEU A 50 ? 2.2935 1.7037 2.3250 0.4370 0.7994 0.2801 50 LEU A O 195 C CB . LEU A 50 ? 2.0413 1.4098 1.9194 0.3928 0.7865 0.2041 50 LEU A CB 196 C CG . LEU A 50 ? 2.0884 1.4018 1.9148 0.4161 0.8358 0.1925 50 LEU A CG 197 C CD1 . LEU A 50 ? 1.9665 1.3224 1.8617 0.4533 0.8760 0.2325 50 LEU A CD1 198 C CD2 . LEU A 50 ? 1.9967 1.2927 1.7517 0.3934 0.8225 0.1631 50 LEU A CD2 199 N N . PHE A 51 ? 2.1231 1.5998 2.1359 0.3822 0.7272 0.2596 51 PHE A N 200 C CA . PHE A 51 ? 1.9967 1.5369 2.0826 0.3845 0.7048 0.2976 51 PHE A CA 201 C C . PHE A 51 ? 1.8379 1.4384 1.9981 0.4073 0.7185 0.3385 51 PHE A C 202 O O . PHE A 51 ? 1.7702 1.3684 1.9265 0.4203 0.7462 0.3372 51 PHE A O 203 C CB . PHE A 51 ? 2.0612 1.6408 2.1409 0.3504 0.6547 0.2898 51 PHE A CB 204 C CG . PHE A 51 ? 2.1030 1.6422 2.1414 0.3317 0.6392 0.2674 51 PHE A CG 205 C CD1 . PHE A 51 ? 2.0684 1.5948 2.1274 0.3400 0.6412 0.2851 51 PHE A CD1 206 C CD2 . PHE A 51 ? 2.0559 1.5729 2.0403 0.3055 0.6224 0.2326 51 PHE A CD2 207 C CE1 . PHE A 51 ? 2.0180 1.5097 2.0442 0.3220 0.6286 0.2682 51 PHE A CE1 208 C CE2 . PHE A 51 ? 2.0173 1.5034 1.9740 0.2875 0.6087 0.2167 51 PHE A CE2 209 C CZ . PHE A 51 ? 2.0653 1.5380 2.0425 0.2954 0.6129 0.2342 51 PHE A CZ 210 N N . VAL A 52 ? 1.8025 1.4570 2.0305 0.4114 0.6989 0.3772 52 VAL A N 211 C CA . VAL A 52 ? 1.8150 1.5380 2.1271 0.4284 0.7033 0.4226 52 VAL A CA 212 C C . VAL A 52 ? 1.8895 1.6710 2.2701 0.4260 0.6696 0.4655 52 VAL A C 213 O O . VAL A 52 ? 1.9743 1.7390 2.3381 0.4174 0.6499 0.4634 52 VAL A O 214 C CB . VAL A 52 ? 1.7921 1.4940 2.1331 0.4694 0.7619 0.4402 52 VAL A CB 215 C CG1 . VAL A 52 ? 1.8512 1.4776 2.1603 0.4900 0.7934 0.4283 52 VAL A CG1 216 C CG2 . VAL A 52 ? 1.6782 1.4574 2.1258 0.4881 0.7622 0.4981 52 VAL A CG2 217 N N . GLU A 53 ? 1.8502 1.6993 2.3096 0.4343 0.6645 0.5074 53 GLU A N 218 C CA . GLU A 53 ? 1.9415 1.8545 2.4565 0.4196 0.6169 0.5449 53 GLU A CA 219 C C . GLU A 53 ? 1.8607 1.7895 2.4360 0.4416 0.6186 0.5890 53 GLU A C 220 O O . GLU A 53 ? 1.8091 1.7313 2.3633 0.4274 0.5870 0.5900 53 GLU A O 221 C CB . GLU A 53 ? 2.2033 2.1850 2.7751 0.4091 0.5985 0.5702 53 GLU A CB 222 C CG . GLU A 53 ? 2.5953 2.5708 3.1105 0.3791 0.5793 0.5322 53 GLU A CG 223 C CD . GLU A 53 ? 2.7277 2.7254 3.2202 0.3414 0.5182 0.5259 53 GLU A CD 224 O OE1 . GLU A 53 ? 2.4293 2.4395 2.9345 0.3362 0.4895 0.5458 53 GLU A OE1 225 O OE2 . GLU A 53 ? 2.8256 2.8247 3.2837 0.3178 0.5003 0.5013 53 GLU A OE2 226 N N . PHE A 54 ? 1.9743 1.9246 2.6246 0.4770 0.6566 0.6271 54 PHE A N 227 C CA . PHE A 54 ? 2.0538 2.0414 2.7929 0.5026 0.6585 0.6851 54 PHE A CA 228 C C . PHE A 54 ? 2.0125 2.0634 2.7968 0.4801 0.5959 0.7246 54 PHE A C 229 O O . PHE A 54 ? 2.0986 2.1432 2.8238 0.4451 0.5496 0.7015 54 PHE A O 230 C CB . PHE A 54 ? 2.2376 2.1583 2.9569 0.5329 0.6985 0.6802 54 PHE A CB 231 C CG . PHE A 54 ? 2.3425 2.1829 2.9933 0.5485 0.7521 0.6338 54 PHE A CG 232 C CD1 . PHE A 54 ? 2.2667 2.1099 2.9367 0.5704 0.7965 0.6349 54 PHE A CD1 233 C CD2 . PHE A 54 ? 2.5360 2.2966 3.0994 0.5390 0.7565 0.5894 54 PHE A CD2 234 C CE1 . PHE A 54 ? 2.4567 2.2185 3.0494 0.5826 0.8433 0.5898 54 PHE A CE1 235 C CE2 . PHE A 54 ? 2.5684 2.2497 3.0616 0.5490 0.8002 0.5454 54 PHE A CE2 236 C CZ . PHE A 54 ? 2.5546 2.2342 3.0575 0.5707 0.8428 0.5444 54 PHE A CZ 237 N N . THR A 55 ? 1.9577 2.0665 2.8458 0.5021 0.5964 0.7861 55 THR A N 238 C CA . THR A 55 ? 1.9758 2.1460 2.9107 0.4812 0.5341 0.8302 55 THR A CA 239 C C . THR A 55 ? 2.1300 2.3043 3.1158 0.5074 0.5370 0.8761 55 THR A C 240 O O . THR A 55 ? 2.1062 2.3151 3.1068 0.4882 0.4828 0.9071 55 THR A O 241 C CB . THR A 55 ? 1.8190 2.0747 2.8344 0.4648 0.5023 0.8679 55 THR A CB 242 O OG1 . THR A 55 ? 1.6018 1.8784 2.5778 0.4182 0.4306 0.8615 55 THR A OG1 243 C CG2 . THR A 55 ? 1.7989 2.1264 2.9537 0.4963 0.5132 0.9450 55 THR A CG2 244 N N . ASP A 56 ? 2.2621 2.3943 3.2666 0.5508 0.6003 0.8788 56 ASP A N 245 C CA . ASP A 56 ? 2.3506 2.4717 3.3974 0.5808 0.6133 0.9177 56 ASP A CA 246 C C . ASP A 56 ? 2.4278 2.5378 3.4264 0.5545 0.5606 0.9195 56 ASP A C 247 O O . ASP A 56 ? 2.1334 2.2303 3.0502 0.5144 0.5202 0.8819 56 ASP A O 248 C CB . ASP A 56 ? 2.4096 2.4432 3.4220 0.6199 0.6872 0.8890 56 ASP A CB 249 C CG . ASP A 56 ? 2.3739 2.3182 3.2606 0.5984 0.6873 0.8235 56 ASP A CG 250 O OD1 . ASP A 56 ? 2.2907 2.2270 3.1408 0.5759 0.6467 0.8233 56 ASP A OD1 251 O OD2 . ASP A 56 ? 2.2707 2.1519 3.0948 0.6040 0.7289 0.7739 56 ASP A OD2 252 N N . HIS A 57 ? 2.6793 2.7925 3.7299 0.5804 0.5657 0.9656 57 HIS A N 253 C CA . HIS A 57 ? 2.6850 2.7667 3.6818 0.5660 0.5350 0.9651 57 HIS A CA 254 C C . HIS A 57 ? 2.9313 2.9212 3.8839 0.5941 0.5930 0.9359 57 HIS A C 255 O O . HIS A 57 ? 2.8093 2.7406 3.6691 0.5728 0.5859 0.8932 57 HIS A O 256 C CB . HIS A 57 ? 2.7274 2.8740 3.8082 0.5719 0.4944 1.0397 57 HIS A CB 257 C CG . HIS A 57 ? 2.7658 2.9133 3.7820 0.5345 0.4312 1.0410 57 HIS A CG 258 N ND1 . HIS A 57 ? 2.6729 2.8070 3.5939 0.4905 0.3950 0.9927 57 HIS A ND1 259 C CD2 . HIS A 57 ? 2.9396 3.0980 3.9699 0.5359 0.3996 1.0866 57 HIS A CD2 260 C CE1 . HIS A 57 ? 2.8399 2.9731 3.7143 0.4671 0.3468 1.0063 57 HIS A CE1 261 N NE2 . HIS A 57 ? 2.9887 3.1369 3.9258 0.4927 0.3471 1.0632 57 HIS A NE2 262 N N . LEU A 58 ? 3.3827 3.3571 4.4002 0.6413 0.6517 0.9579 58 LEU A N 263 C CA . LEU A 58 ? 3.7570 3.6322 4.7297 0.6696 0.7109 0.9281 58 LEU A CA 264 C C . LEU A 58 ? 4.1778 3.9802 5.0693 0.6680 0.7560 0.8580 58 LEU A C 265 O O . LEU A 58 ? 4.8867 4.6230 5.6836 0.6446 0.7517 0.8079 58 LEU A O 266 C CB . LEU A 58 ? 3.3100 3.1785 4.3727 0.7227 0.7530 0.9840 58 LEU A CB 267 C CG . LEU A 58 ? 2.8564 2.7072 3.9330 0.7314 0.7365 1.0220 58 LEU A CG 268 C CD1 . LEU A 58 ? 2.5624 2.4089 3.7377 0.7887 0.7843 1.0785 58 LEU A CD1 269 C CD2 . LEU A 58 ? 2.6675 2.4248 3.6323 0.7104 0.7394 0.9690 58 LEU A CD2 270 N N . PHE A 59 ? 3.8152 3.6291 4.7397 0.6903 0.7968 0.8552 59 PHE A N 271 C CA . PHE A 59 ? 3.3564 3.0954 4.1933 0.6878 0.8378 0.7889 59 PHE A CA 272 C C . PHE A 59 ? 2.8087 2.5843 3.6548 0.6860 0.8529 0.7755 59 PHE A C 273 O O . PHE A 59 ? 2.4206 2.1485 3.1793 0.6665 0.8612 0.7183 59 PHE A O 274 C CB . PHE A 59 ? 3.6298 3.2620 4.4331 0.7253 0.9032 0.7700 59 PHE A CB 275 C CG . PHE A 59 ? 3.6840 3.2468 4.4257 0.7104 0.8888 0.7504 59 PHE A CG 276 C CD1 . PHE A 59 ? 3.5323 3.0400 4.1685 0.6711 0.8698 0.6898 59 PHE A CD1 277 C CD2 . PHE A 59 ? 3.5828 3.1358 4.3773 0.7366 0.8960 0.7958 59 PHE A CD2 278 C CE1 . PHE A 59 ? 3.2949 2.7436 3.8834 0.6568 0.8583 0.6764 59 PHE A CE1 279 C CE2 . PHE A 59 ? 3.3081 2.7981 4.0491 0.7223 0.8843 0.7810 59 PHE A CE2 280 C CZ . PHE A 59 ? 3.1449 2.5833 3.7839 0.6819 0.8662 0.7213 59 PHE A CZ 281 N N . ASN A 60 ? 2.5588 2.4230 3.5101 0.7012 0.8501 0.8295 60 ASN A N 282 C CA . ASN A 60 ? 2.4317 2.3217 3.4184 0.7204 0.8914 0.8330 60 ASN A CA 283 C C . ASN A 60 ? 2.4445 2.3806 3.4116 0.6864 0.8651 0.8115 60 ASN A C 284 O O . ASN A 60 ? 2.4372 2.3799 3.3441 0.6407 0.8110 0.7804 60 ASN A O 285 C CB . ASN A 60 ? 2.2692 2.2313 3.3959 0.7620 0.9153 0.9091 60 ASN A CB 286 C CG . ASN A 60 ? 2.0834 2.1637 3.3005 0.7349 0.8502 0.9607 60 ASN A CG 287 O OD1 . ASN A 60 ? 2.1171 2.2308 3.3515 0.7131 0.7925 0.9853 60 ASN A OD1 288 N ND2 . ASN A 60 ? 1.9128 2.0540 3.1855 0.7350 0.8588 0.9783 60 ASN A ND2 289 N N . ILE A 61 ? 2.3910 2.3576 3.4138 0.7125 0.9088 0.8320 61 ILE A N 290 C CA . ILE A 61 ? 2.3531 2.3729 3.3833 0.6887 0.8938 0.8262 61 ILE A CA 291 C C . ILE A 61 ? 2.2008 2.3096 3.2770 0.6447 0.8119 0.8535 61 ILE A C 292 O O . ILE A 61 ? 1.9870 2.1551 3.1495 0.6484 0.7814 0.9082 61 ILE A O 293 C CB . ILE A 61 ? 2.3511 2.4018 3.4614 0.7317 0.9602 0.8624 61 ILE A CB 294 C CG1 . ILE A 61 ? 2.2060 2.2628 3.2760 0.7145 0.9715 0.8335 61 ILE A CG1 295 C CG2 . ILE A 61 ? 2.3383 2.4934 3.6040 0.7499 0.9484 0.9457 61 ILE A CG2 296 C CD1 . ILE A 61 ? 1.8235 1.8862 2.9389 0.7576 1.0481 0.8558 61 ILE A CD1 297 N N . ALA A 62 ? 2.1671 2.2775 3.1780 0.6026 0.7753 0.8137 62 ALA A N 298 C CA . ALA A 62 ? 2.3580 2.5518 3.4152 0.5634 0.7090 0.8388 62 ALA A CA 299 C C . ALA A 62 ? 2.5209 2.6919 3.4789 0.5149 0.6639 0.7838 62 ALA A C 300 O O . ALA A 62 ? 2.7546 2.9016 3.6544 0.4901 0.6224 0.7622 62 ALA A O 301 C CB . ALA A 62 ? 2.1103 2.3587 3.2399 0.5585 0.6609 0.8919 62 ALA A CB 302 N N . LYS A 63 ? 2.4279 2.6083 3.3707 0.5026 0.6728 0.7650 63 LYS A N 303 C CA . LYS A 63 ? 2.2071 2.3511 3.0480 0.4641 0.6434 0.7075 63 LYS A CA 304 C C . LYS A 63 ? 2.1952 2.3523 3.0249 0.4510 0.6522 0.6920 63 LYS A C 305 O O . LYS A 63 ? 2.1480 2.2462 2.8859 0.4436 0.6675 0.6401 63 LYS A O 306 C CB . LYS A 63 ? 2.1859 2.2364 2.9229 0.4732 0.6744 0.6526 63 LYS A CB 307 C CG . LYS A 63 ? 2.1876 2.1883 2.8919 0.5019 0.7412 0.6299 63 LYS A CG 308 C CD . LYS A 63 ? 2.0227 2.0478 2.8156 0.5479 0.7964 0.6775 63 LYS A CD 309 C CE . LYS A 63 ? 1.8065 1.7997 2.6188 0.5793 0.8196 0.6943 63 LYS A CE 310 N NZ . LYS A 63 ? 1.7085 1.6885 2.5683 0.6300 0.8923 0.7199 63 LYS A NZ 311 N N . PRO A 64 ? 2.1769 2.4102 3.0983 0.4454 0.6393 0.7373 64 PRO A N 312 C CA . PRO A 64 ? 2.0851 2.3294 3.0110 0.4458 0.6677 0.7326 64 PRO A CA 313 C C . PRO A 64 ? 2.0376 2.2406 2.8626 0.4122 0.6453 0.6766 64 PRO A C 314 O O . PRO A 64 ? 1.9667 2.1996 2.7936 0.3747 0.5888 0.6766 64 PRO A O 315 C CB . PRO A 64 ? 1.9437 2.2839 2.9902 0.4333 0.6373 0.7941 64 PRO A CB 316 C CG . PRO A 64 ? 2.0705 2.4478 3.1830 0.4379 0.6068 0.8359 64 PRO A CG 317 C CD . PRO A 64 ? 2.0854 2.3963 3.0974 0.4277 0.5854 0.7901 64 PRO A CD 318 N N . ARG A 65 ? 2.1768 2.3106 2.9154 0.4252 0.6879 0.6314 65 ARG A N 319 C CA . ARG A 65 ? 2.2276 2.3151 2.8645 0.3957 0.6671 0.5762 65 ARG A CA 320 C C . ARG A 65 ? 2.2326 2.3342 2.8624 0.3835 0.6746 0.5715 65 ARG A C 321 O O . ARG A 65 ? 2.5085 2.6105 3.1576 0.4096 0.7266 0.5859 65 ARG A O 322 C CB . ARG A 65 ? 2.2196 2.2205 2.7567 0.4069 0.6932 0.5265 65 ARG A CB 323 C CG . ARG A 65 ? 2.1329 2.0796 2.6211 0.4343 0.7557 0.5065 65 ARG A CG 324 C CD . ARG A 65 ? 2.0876 1.9532 2.4611 0.4234 0.7560 0.4485 65 ARG A CD 325 N NE . ARG A 65 ? 2.1406 1.9757 2.4931 0.4208 0.7384 0.4354 65 ARG A NE 326 C CZ . ARG A 65 ? 2.2290 2.0627 2.5507 0.3903 0.6897 0.4149 65 ARG A CZ 327 N NH1 . ARG A 65 ? 2.0572 1.9142 2.3617 0.3595 0.6515 0.4018 65 ARG A NH1 328 N NH2 . ARG A 65 ? 2.3295 2.1355 2.6373 0.3922 0.6818 0.4087 65 ARG A NH2 329 N N . PRO A 66 ? 2.1108 2.2192 2.7089 0.3454 0.6258 0.5515 66 PRO A N 330 C CA . PRO A 66 ? 1.9705 2.1009 2.5789 0.3331 0.6289 0.5571 66 PRO A CA 331 C C . PRO A 66 ? 1.9282 1.9985 2.4476 0.3412 0.6657 0.5169 66 PRO A C 332 O O . PRO A 66 ? 1.7866 1.7975 2.2221 0.3391 0.6641 0.4737 66 PRO A O 333 C CB . PRO A 66 ? 1.8825 2.0324 2.4846 0.2908 0.5627 0.5489 66 PRO A CB 334 C CG . PRO A 66 ? 1.9425 2.0470 2.4753 0.2826 0.5392 0.5120 66 PRO A CG 335 C CD . PRO A 66 ? 2.1859 2.2730 2.7286 0.3150 0.5734 0.5201 66 PRO A CD 336 N N . PRO A 67 ? 1.9334 2.0205 2.4727 0.3494 0.6975 0.5339 67 PRO A N 337 C CA . PRO A 67 ? 1.9083 1.9479 2.3719 0.3568 0.7333 0.5067 67 PRO A CA 338 C C . PRO A 67 ? 1.8425 1.8082 2.1904 0.3462 0.7228 0.4493 67 PRO A C 339 O O . PRO A 67 ? 1.7223 1.6302 2.0072 0.3673 0.7612 0.4262 67 PRO A O 340 C CB . PRO A 67 ? 2.0084 2.0928 2.5082 0.3327 0.7120 0.5263 67 PRO A CB 341 C CG . PRO A 67 ? 1.9265 2.0883 2.5450 0.3270 0.6905 0.5786 67 PRO A CG 342 C CD . PRO A 67 ? 1.9048 2.0683 2.5516 0.3456 0.6926 0.5878 67 PRO A CD 343 N N . TRP A 68 ? 1.8429 1.8100 2.1658 0.3133 0.6708 0.4281 68 TRP A N 344 C CA . TRP A 68 ? 1.9357 1.8499 2.1648 0.2985 0.6591 0.3832 68 TRP A CA 345 C C . TRP A 68 ? 2.0876 1.9599 2.2644 0.2920 0.6387 0.3484 68 TRP A C 346 O O . TRP A 68 ? 2.1716 1.9934 2.2709 0.2866 0.6400 0.3130 68 TRP A O 347 C CB . TRP A 68 ? 1.8461 1.7884 2.0860 0.2686 0.6190 0.3848 68 TRP A CB 348 C CG . TRP A 68 ? 1.8529 1.8417 2.1588 0.2522 0.5779 0.4060 68 TRP A CG 349 C CD1 . TRP A 68 ? 1.8377 1.8848 2.2333 0.2521 0.5736 0.4504 68 TRP A CD1 350 C CD2 . TRP A 68 ? 1.8233 1.8023 2.1088 0.2336 0.5352 0.3858 68 TRP A CD2 351 N NE1 . TRP A 68 ? 1.8516 1.9220 2.2768 0.2319 0.5261 0.4569 68 TRP A NE1 352 C CE2 . TRP A 68 ? 1.8368 1.8640 2.1915 0.2216 0.5043 0.4168 68 TRP A CE2 353 C CE3 . TRP A 68 ? 1.7694 1.7039 1.9849 0.2252 0.5201 0.3462 68 TRP A CE3 354 C CZ2 . TRP A 68 ? 1.8509 1.8764 2.1953 0.2024 0.4606 0.4066 68 TRP A CZ2 355 C CZ3 . TRP A 68 ? 1.7368 1.6749 1.9512 0.2084 0.4812 0.3385 68 TRP A CZ3 356 C CH2 . TRP A 68 ? 1.7229 1.7027 1.9953 0.1977 0.4527 0.3671 68 TRP A CH2 357 N N . MET A 69 ? 2.1015 1.9962 2.3217 0.2907 0.6177 0.3611 69 MET A N 358 C CA . MET A 69 ? 2.0633 1.9207 2.2447 0.2901 0.6076 0.3363 69 MET A CA 359 C C . MET A 69 ? 2.2381 2.0410 2.3769 0.3162 0.6545 0.3225 69 MET A C 360 O O . MET A 69 ? 2.7603 2.5490 2.9117 0.3314 0.6663 0.3275 69 MET A O 361 C CB . MET A 69 ? 2.0438 1.9371 2.2870 0.2920 0.5883 0.3633 69 MET A CB 362 C CG . MET A 69 ? 2.0292 1.9417 2.2747 0.2645 0.5359 0.3589 69 MET A CG 363 S SD . MET A 69 ? 2.2679 2.2080 2.5692 0.2724 0.5214 0.3905 69 MET A SD 364 C CE . MET A 69 ? 1.9197 1.9029 2.2449 0.2389 0.4615 0.4033 69 MET A CE 365 N N . GLY A 70 ? 1.9984 1.7664 2.0829 0.3210 0.6806 0.3056 70 GLY A N 366 C CA . GLY A 70 ? 1.8828 1.5953 1.9229 0.3480 0.7318 0.2960 70 GLY A CA 367 C C . GLY A 70 ? 1.9574 1.6331 1.9946 0.3670 0.7508 0.2921 70 GLY A C 368 O O . GLY A 70 ? 1.8906 1.5961 1.9968 0.3882 0.7677 0.3248 70 GLY A O 369 N N . LEU A 71 ? 2.0104 1.6202 1.9698 0.3587 0.7474 0.2542 71 LEU A N 370 C CA . LEU A 71 ? 2.1118 1.6790 2.0613 0.3704 0.7586 0.2461 71 LEU A CA 371 C C . LEU A 71 ? 2.1252 1.7242 2.1093 0.3503 0.7133 0.2492 71 LEU A C 372 O O . LEU A 71 ? 2.2682 1.8495 2.2655 0.3591 0.7171 0.2532 71 LEU A O 373 C CB . LEU A 71 ? 2.1366 1.6143 1.9857 0.3668 0.7726 0.2047 71 LEU A CB 374 C CG . LEU A 71 ? 2.0279 1.4758 1.8001 0.3370 0.7451 0.1698 71 LEU A CG 375 C CD1 . LEU A 71 ? 1.8381 1.3438 1.6398 0.3072 0.6938 0.1713 71 LEU A CD1 376 C CD2 . LEU A 71 ? 1.9936 1.3605 1.6916 0.3281 0.7441 0.1351 71 LEU A CD2 377 N N . LEU A 72 ? 2.1542 1.7959 2.1488 0.3241 0.6727 0.2476 72 LEU A N 378 C CA . LEU A 72 ? 2.1260 1.7941 2.1396 0.3030 0.6300 0.2471 72 LEU A CA 379 C C . LEU A 72 ? 2.1452 1.8404 2.2193 0.3161 0.6289 0.2771 72 LEU A C 380 O O . LEU A 72 ? 2.0779 1.8221 2.2173 0.3279 0.6330 0.3124 72 LEU A O 381 C CB . LEU A 72 ? 2.0630 1.7795 2.0940 0.2813 0.5963 0.2516 72 LEU A CB 382 C CG . LEU A 72 ? 1.9839 1.6975 1.9839 0.2541 0.5581 0.2284 72 LEU A CG 383 C CD1 . LEU A 72 ? 1.9757 1.6983 1.9548 0.2399 0.5468 0.2181 72 LEU A CD1 384 C CD2 . LEU A 72 ? 1.9745 1.7266 2.0151 0.2449 0.5277 0.2454 72 LEU A CD2 385 N N . GLY A 73 ? 2.1242 1.7877 2.1786 0.3131 0.6225 0.2657 73 GLY A N 386 C CA . GLY A 73 ? 2.0398 1.7278 2.1426 0.3199 0.6123 0.2927 73 GLY A CA 387 C C . GLY A 73 ? 1.9520 1.7048 2.0977 0.3038 0.5741 0.3143 73 GLY A C 388 O O . GLY A 73 ? 1.9556 1.7192 2.0769 0.2813 0.5488 0.2972 73 GLY A O 389 N N . PRO A 74 ? 1.7847 1.5779 1.9930 0.3146 0.5680 0.3525 74 PRO A N 390 C CA . PRO A 74 ? 1.5946 1.4485 1.8483 0.2998 0.5311 0.3787 74 PRO A CA 391 C C . PRO A 74 ? 1.5625 1.4143 1.7726 0.2698 0.4912 0.3558 74 PRO A C 392 O O . PRO A 74 ? 1.5192 1.3366 1.6859 0.2637 0.4878 0.3347 74 PRO A O 393 C CB . PRO A 74 ? 1.5025 1.3798 1.8090 0.3133 0.5263 0.4164 74 PRO A CB 394 C CG . PRO A 74 ? 1.5400 1.3629 1.8123 0.3268 0.5499 0.4011 74 PRO A CG 395 C CD . PRO A 74 ? 1.6534 1.4286 1.8836 0.3365 0.5874 0.3705 74 PRO A CD 396 N N . THR A 75 ? 1.6316 1.5174 1.8535 0.2515 0.4633 0.3607 75 THR A N 397 C CA . THR A 75 ? 1.6890 1.5669 1.8661 0.2259 0.4301 0.3379 75 THR A CA 398 C C . THR A 75 ? 1.6885 1.5808 1.8727 0.2178 0.3997 0.3566 75 THR A C 399 O O . THR A 75 ? 1.6958 1.6272 1.9235 0.2126 0.3765 0.3873 75 THR A O 400 C CB . THR A 75 ? 1.7808 1.6792 1.9602 0.2089 0.4124 0.3332 75 THR A CB 401 O OG1 . THR A 75 ? 1.7957 1.6783 1.9617 0.2165 0.4407 0.3173 75 THR A OG1 402 C CG2 . THR A 75 ? 1.9400 1.8233 2.0713 0.1863 0.3830 0.3092 75 THR A CG2 403 N N . ILE A 76 ? 1.7116 1.5726 1.8544 0.2162 0.3997 0.3411 76 ILE A N 404 C CA . ILE A 76 ? 1.6534 1.5204 1.7875 0.2080 0.3723 0.3567 76 ILE A CA 405 C C . ILE A 76 ? 1.6898 1.5517 1.7777 0.1838 0.3415 0.3381 76 ILE A C 406 O O . ILE A 76 ? 1.6264 1.4670 1.6785 0.1767 0.3484 0.3069 76 ILE A O 407 C CB . ILE A 76 ? 1.6323 1.4697 1.7490 0.2193 0.3888 0.3568 76 ILE A CB 408 C CG1 . ILE A 76 ? 1.6629 1.4637 1.7211 0.2086 0.3933 0.3227 76 ILE A CG1 409 C CG2 . ILE A 76 ? 1.5488 1.3753 1.7003 0.2447 0.4250 0.3680 76 ILE A CG2 410 C CD1 . ILE A 76 ? 1.6603 1.4570 1.6837 0.1964 0.3700 0.3268 76 ILE A CD1 411 N N . GLN A 77 ? 1.7047 1.5831 1.7914 0.1715 0.3073 0.3579 77 GLN A N 412 C CA . GLN A 77 ? 1.7627 1.6324 1.8054 0.1487 0.2775 0.3418 77 GLN A CA 413 C C . GLN A 77 ? 1.7662 1.6294 1.7726 0.1358 0.2448 0.3540 77 GLN A C 414 O O . GLN A 77 ? 1.7907 1.6817 1.8288 0.1302 0.2175 0.3861 77 GLN A O 415 C CB . GLN A 77 ? 1.7631 1.6605 1.8420 0.1383 0.2609 0.3508 77 GLN A CB 416 C CG . GLN A 77 ? 1.8783 1.7555 1.9198 0.1247 0.2568 0.3196 77 GLN A CG 417 C CD . GLN A 77 ? 2.0889 1.9912 2.1642 0.1099 0.2336 0.3330 77 GLN A CD 418 O OE1 . GLN A 77 ? 2.1529 2.0597 2.2446 0.1108 0.2474 0.3236 77 GLN A OE1 419 N NE2 . GLN A 77 ? 2.2205 2.1400 2.3079 0.0946 0.1961 0.3578 77 GLN A NE2 420 N N . ALA A 78 ? 1.6762 1.5034 1.6163 0.1303 0.2469 0.3302 78 ALA A N 421 C CA . ALA A 78 ? 1.6751 1.4855 1.5618 0.1184 0.2196 0.3379 78 ALA A CA 422 C C . ALA A 78 ? 1.7119 1.4876 1.5276 0.1024 0.2066 0.3097 78 ALA A C 423 O O . ALA A 78 ? 1.6528 1.4146 1.4581 0.1030 0.2236 0.2817 78 ALA A O 424 C CB . ALA A 78 ? 1.7227 1.5187 1.5919 0.1312 0.2382 0.3459 78 ALA A CB 425 N N . GLU A 79 ? 1.8240 1.5826 1.5877 0.0890 0.1763 0.3185 79 GLU A N 426 C CA . GLU A 79 ? 2.0016 1.7168 1.6856 0.0753 0.1652 0.2926 79 GLU A CA 427 C C . GLU A 79 ? 2.0126 1.6925 1.6347 0.0853 0.1920 0.2785 79 GLU A C 428 O O . GLU A 79 ? 1.9270 1.6170 1.5729 0.1009 0.2193 0.2867 79 GLU A O 429 C CB . GLU A 79 ? 2.2214 1.9274 1.8686 0.0522 0.1153 0.3075 79 GLU A CB 430 C CG . GLU A 79 ? 2.2138 1.9460 1.9097 0.0353 0.0836 0.3175 79 GLU A CG 431 C CD . GLU A 79 ? 2.4559 2.1681 2.1015 0.0071 0.0297 0.3281 79 GLU A CD 432 O OE1 . GLU A 79 ? 2.5271 2.2309 2.1341 0.0032 0.0103 0.3466 79 GLU A OE1 433 O OE2 . GLU A 79 ? 2.5181 2.2192 2.1588 -0.0127 0.0052 0.3179 79 GLU A OE2 434 N N . VAL A 80 ? 2.0048 1.6401 1.5464 0.0760 0.1851 0.2581 80 VAL A N 435 C CA . VAL A 80 ? 1.9992 1.5991 1.4784 0.0858 0.2137 0.2451 80 VAL A CA 436 C C . VAL A 80 ? 2.0617 1.6405 1.4773 0.0794 0.1935 0.2642 80 VAL A C 437 O O . VAL A 80 ? 2.1367 1.6677 1.4633 0.0740 0.1914 0.2505 80 VAL A O 438 C CB . VAL A 80 ? 2.1329 1.6901 1.5558 0.0850 0.2279 0.2111 80 VAL A CB 439 C CG1 . VAL A 80 ? 2.1316 1.7016 1.5984 0.1015 0.2698 0.1949 80 VAL A CG1 440 C CG2 . VAL A 80 ? 2.0960 1.6394 1.5058 0.0662 0.1929 0.2006 80 VAL A CG2 441 N N . TYR A 81 ? 2.1237 1.7357 1.5825 0.0807 0.1790 0.2971 81 TYR A N 442 C CA . TYR A 81 ? 2.2865 1.8841 1.6971 0.0818 0.1730 0.3197 81 TYR A CA 443 C C . TYR A 81 ? 2.3151 1.9595 1.8033 0.0874 0.1614 0.3573 81 TYR A C 444 O O . TYR A 81 ? 2.4260 2.0692 1.8993 0.0927 0.1610 0.3829 81 TYR A O 445 C CB . TYR A 81 ? 2.4484 2.0030 1.7593 0.0618 0.1348 0.3186 81 TYR A CB 446 C CG . TYR A 81 ? 2.6608 2.1554 1.8712 0.0660 0.1627 0.2893 81 TYR A CG 447 C CD1 . TYR A 81 ? 2.8483 2.3308 2.0339 0.0834 0.2038 0.2933 81 TYR A CD1 448 C CD2 . TYR A 81 ? 2.7462 2.1946 1.8895 0.0538 0.1512 0.2590 81 TYR A CD2 449 C CE1 . TYR A 81 ? 3.0690 2.5000 2.1690 0.0902 0.2348 0.2701 81 TYR A CE1 450 C CE2 . TYR A 81 ? 2.8422 2.2331 1.8950 0.0618 0.1827 0.2331 81 TYR A CE2 451 C CZ . TYR A 81 ? 3.0373 2.4225 2.0710 0.0810 0.2258 0.2398 81 TYR A CZ 452 O OH . TYR A 81 ? 3.1815 2.5137 2.1321 0.0918 0.2624 0.2181 81 TYR A OH 453 N N . ASP A 82 ? 2.2304 1.9143 1.8024 0.0884 0.1561 0.3612 82 ASP A N 454 C CA . ASP A 82 ? 2.1860 1.9156 1.8428 0.0975 0.1505 0.3962 82 ASP A CA 455 C C . ASP A 82 ? 2.1888 1.9196 1.8725 0.1192 0.1914 0.4025 82 ASP A C 456 O O . ASP A 82 ? 2.2554 1.9582 1.9023 0.1251 0.2234 0.3790 82 ASP A O 457 C CB . ASP A 82 ? 2.1395 1.9044 1.8736 0.0975 0.1486 0.3936 82 ASP A CB 458 C CG . ASP A 82 ? 2.3934 2.1595 2.1114 0.0734 0.1054 0.3917 82 ASP A CG 459 O OD1 . ASP A 82 ? 2.4825 2.2119 2.1172 0.0559 0.0787 0.3835 82 ASP A OD1 460 O OD2 . ASP A 82 ? 2.5155 2.3158 2.3016 0.0713 0.0988 0.3985 82 ASP A OD2 461 N N . THR A 83 ? 2.1979 1.9597 1.9470 0.1307 0.1901 0.4365 83 THR A N 462 C CA . THR A 83 ? 2.0348 1.7944 1.8184 0.1513 0.2288 0.4433 83 THR A CA 463 C C . THR A 83 ? 1.8766 1.6702 1.7517 0.1655 0.2389 0.4579 83 THR A C 464 O O . THR A 83 ? 1.9281 1.7536 1.8492 0.1673 0.2149 0.4929 83 THR A O 465 C CB . THR A 83 ? 2.0385 1.7869 1.7954 0.1560 0.2246 0.4748 83 THR A CB 466 O OG1 . THR A 83 ? 2.1073 1.8270 1.7721 0.1404 0.2042 0.4695 83 THR A OG1 467 C CG2 . THR A 83 ? 1.9745 1.7035 1.7417 0.1716 0.2688 0.4691 83 THR A CG2 468 N N . VAL A 84 ? 1.6842 1.4707 1.5847 0.1754 0.2742 0.4322 84 VAL A N 469 C CA . VAL A 84 ? 1.7754 1.5840 1.7510 0.1915 0.2915 0.4427 84 VAL A CA 470 C C . VAL A 84 ? 1.9345 1.7332 1.9393 0.2113 0.3155 0.4649 84 VAL A C 471 O O . VAL A 84 ? 2.1080 1.8754 2.0785 0.2125 0.3339 0.4555 84 VAL A O 472 C CB . VAL A 84 ? 1.7247 1.5252 1.7076 0.1925 0.3160 0.4063 84 VAL A CB 473 C CG1 . VAL A 84 ? 1.7600 1.5515 1.7868 0.2128 0.3529 0.4060 84 VAL A CG1 474 C CG2 . VAL A 84 ? 1.7002 1.5289 1.7043 0.1826 0.2941 0.4048 84 VAL A CG2 475 N N . VAL A 85 ? 1.8848 1.7097 1.9564 0.2272 0.3166 0.4968 85 VAL A N 476 C CA . VAL A 85 ? 1.8060 1.6171 1.9099 0.2490 0.3418 0.5193 85 VAL A CA 477 C C . VAL A 85 ? 1.8710 1.6880 2.0404 0.2720 0.3725 0.5240 85 VAL A C 478 O O . VAL A 85 ? 1.7664 1.6153 1.9987 0.2875 0.3685 0.5614 85 VAL A O 479 C CB . VAL A 85 ? 1.7288 1.5567 1.8426 0.2517 0.3158 0.5657 85 VAL A CB 480 C CG1 . VAL A 85 ? 1.7387 1.5443 1.8831 0.2752 0.3465 0.5860 85 VAL A CG1 481 C CG2 . VAL A 85 ? 1.7218 1.5339 1.7569 0.2305 0.2902 0.5600 85 VAL A CG2 482 N N . ILE A 86 ? 1.9832 1.7670 2.1355 0.2745 0.4042 0.4867 86 ILE A N 483 C CA . ILE A 86 ? 2.1173 1.8898 2.3109 0.2961 0.4394 0.4832 86 ILE A CA 484 C C . ILE A 86 ? 2.1223 1.8641 2.3379 0.3185 0.4658 0.5038 86 ILE A C 485 O O . ILE A 86 ? 2.2091 1.9152 2.3896 0.3131 0.4716 0.4961 86 ILE A O 486 C CB . ILE A 86 ? 2.1958 1.9375 2.3535 0.2881 0.4598 0.4358 86 ILE A CB 487 C CG1 . ILE A 86 ? 2.1105 1.8726 2.2326 0.2629 0.4318 0.4137 86 ILE A CG1 488 C CG2 . ILE A 86 ? 2.4451 2.1797 2.6382 0.3090 0.4918 0.4329 86 ILE A CG2 489 C CD1 . ILE A 86 ? 2.0673 1.8385 2.1953 0.2606 0.4389 0.3913 86 ILE A CD1 490 N N . THR A 87 ? 1.9953 1.7509 2.2724 0.3445 0.4833 0.5323 87 THR A N 491 C CA . THR A 87 ? 1.9504 1.6755 2.2549 0.3697 0.5100 0.5559 87 THR A CA 492 C C . THR A 87 ? 1.9062 1.5902 2.2191 0.3905 0.5564 0.5335 87 THR A C 493 O O . THR A 87 ? 1.9364 1.6438 2.3012 0.4122 0.5730 0.5521 87 THR A O 494 C CB . THR A 87 ? 1.9597 1.7346 2.3332 0.3864 0.4929 0.6142 87 THR A CB 495 O OG1 . THR A 87 ? 1.9426 1.7657 2.3042 0.3614 0.4424 0.6285 87 THR A OG1 496 C CG2 . THR A 87 ? 1.8774 1.6233 2.2681 0.4059 0.5071 0.6449 87 THR A CG2 497 N N . LEU A 88 ? 1.8901 1.5126 2.1503 0.3828 0.5770 0.4942 88 LEU A N 498 C CA . LEU A 88 ? 1.9618 1.5368 2.2084 0.3960 0.6162 0.4640 88 LEU A CA 499 C C . LEU A 88 ? 2.2518 1.7856 2.5314 0.4313 0.6569 0.4836 88 LEU A C 500 O O . LEU A 88 ? 2.5887 2.0981 2.8763 0.4382 0.6597 0.5034 88 LEU A O 501 C CB . LEU A 88 ? 1.8583 1.3784 2.0372 0.3728 0.6196 0.4171 88 LEU A CB 502 C CG . LEU A 88 ? 1.7976 1.2613 1.9502 0.3833 0.6556 0.3849 88 LEU A CG 503 C CD1 . LEU A 88 ? 1.7130 1.2120 1.8626 0.3789 0.6516 0.3701 88 LEU A CD1 504 C CD2 . LEU A 88 ? 1.8954 1.2923 1.9889 0.3627 0.6600 0.3468 88 LEU A CD2 505 N N . LYS A 89 ? 2.3128 1.8325 2.6065 0.4542 0.6918 0.4770 89 LYS A N 506 C CA . LYS A 89 ? 2.3366 1.8173 2.6667 0.4946 0.7375 0.4989 89 LYS A CA 507 C C . LYS A 89 ? 2.2987 1.6810 2.5725 0.5053 0.7819 0.4593 89 LYS A C 508 O O . LYS A 89 ? 2.2107 1.5456 2.5042 0.5373 0.8196 0.4747 89 LYS A O 509 C CB . LYS A 89 ? 2.3167 1.8578 2.7224 0.5229 0.7514 0.5368 89 LYS A CB 510 C CG . LYS A 89 ? 2.1403 1.6993 2.6270 0.5596 0.7686 0.5930 89 LYS A CG 511 C CD . LYS A 89 ? 2.0216 1.6741 2.5953 0.5717 0.7564 0.6394 89 LYS A CD 512 C CE . LYS A 89 ? 1.8318 1.5396 2.3846 0.5349 0.7143 0.6208 89 LYS A CE 513 N NZ . LYS A 89 ? 1.6302 1.4321 2.2532 0.5254 0.6708 0.6671 89 LYS A NZ 514 N N . ASN A 90 ? 2.2617 1.6117 2.4654 0.4787 0.7758 0.4104 90 ASN A N 515 C CA . ASN A 90 ? 2.3483 1.6019 2.4840 0.4813 0.8100 0.3675 90 ASN A CA 516 C C . ASN A 90 ? 2.4012 1.5993 2.5483 0.5246 0.8661 0.3764 90 ASN A C 517 O O . ASN A 90 ? 2.3711 1.5075 2.5178 0.5411 0.8886 0.3833 90 ASN A O 518 C CB . ASN A 90 ? 2.5016 1.6919 2.5853 0.4542 0.7963 0.3414 90 ASN A CB 519 C CG . ASN A 90 ? 2.6518 1.7401 2.6587 0.4499 0.8230 0.2952 90 ASN A CG 520 O OD1 . ASN A 90 ? 2.6871 1.7417 2.6736 0.4725 0.8583 0.2830 90 ASN A OD1 521 N ND2 . ASN A 90 ? 2.7038 1.7413 2.6660 0.4195 0.8056 0.2703 90 ASN A ND2 522 N N . MET A 91 ? 2.5093 1.7240 2.6627 0.5434 0.8915 0.3752 91 MET A N 523 C CA . MET A 91 ? 2.5230 1.6913 2.6914 0.5895 0.9512 0.3873 91 MET A CA 524 C C . MET A 91 ? 2.5124 1.5689 2.5804 0.5894 0.9855 0.3351 91 MET A C 525 O O . MET A 91 ? 2.6939 1.6834 2.7507 0.6267 1.0399 0.3355 91 MET A O 526 C CB . MET A 91 ? 2.6185 1.8710 2.8609 0.6144 0.9650 0.4244 91 MET A CB 527 C CG . MET A 91 ? 2.6971 2.0617 3.0261 0.6030 0.9177 0.4708 91 MET A CG 528 S SD . MET A 91 ? 2.9590 2.4137 3.4167 0.6449 0.9377 0.5416 91 MET A SD 529 C CE . MET A 91 ? 2.9948 2.3741 3.4789 0.6971 0.9984 0.5644 91 MET A CE 530 N N . ALA A 92 ? 2.4514 1.4850 2.4453 0.5471 0.9527 0.2913 92 ALA A N 531 C CA . ALA A 92 ? 2.6097 1.5415 2.4991 0.5372 0.9724 0.2394 92 ALA A CA 532 C C . ALA A 92 ? 2.8168 1.6325 2.6575 0.5424 0.9949 0.2203 92 ALA A C 533 O O . ALA A 92 ? 2.8468 1.6646 2.7378 0.5520 0.9933 0.2480 92 ALA A O 534 C CB . ALA A 92 ? 2.5358 1.4880 2.3737 0.4879 0.9231 0.2054 92 ALA A CB 535 N N . SER A 93 ? 2.9753 1.6867 2.7155 0.5354 1.0150 0.1739 93 SER A N 536 C CA . SER A 93 ? 3.1131 1.7044 2.7864 0.5239 1.0219 0.1442 93 SER A CA 537 C C . SER A 93 ? 3.2072 1.7912 2.8328 0.4650 0.9640 0.1120 93 SER A C 538 O O . SER A 93 ? 3.2188 1.7070 2.7832 0.4430 0.9582 0.0830 93 SER A O 539 C CB . SER A 93 ? 3.1849 1.6564 2.7690 0.5494 1.0767 0.1120 93 SER A CB 540 O OG . SER A 93 ? 3.0989 1.5832 2.6298 0.5427 1.0784 0.0893 93 SER A OG 541 N N . HIS A 94 ? 3.2254 1.9135 2.8853 0.4409 0.9223 0.1205 94 HIS A N 542 C CA . HIS A 94 ? 3.0446 1.7578 2.6829 0.3895 0.8673 0.1003 94 HIS A CA 543 C C . HIS A 94 ? 2.9537 1.7188 2.6600 0.3761 0.8383 0.1296 94 HIS A C 544 O O . HIS A 94 ? 2.8104 1.6428 2.5925 0.4008 0.8446 0.1704 94 HIS A O 545 C CB . HIS A 94 ? 2.8311 1.6346 2.4811 0.3786 0.8441 0.1009 94 HIS A CB 546 C CG . HIS A 94 ? 2.7982 1.5784 2.3774 0.3375 0.8112 0.0622 94 HIS A CG 547 N ND1 . HIS A 94 ? 2.7011 1.4885 2.2366 0.3368 0.8145 0.0448 94 HIS A ND1 548 C CD2 . HIS A 94 ? 2.7598 1.5114 2.3082 0.2955 0.7739 0.0408 94 HIS A CD2 549 C CE1 . HIS A 94 ? 2.7321 1.4953 2.2107 0.2965 0.7787 0.0142 94 HIS A CE1 550 N NE2 . HIS A 94 ? 2.7517 1.4955 2.2407 0.2705 0.7531 0.0119 94 HIS A NE2 551 N N . PRO A 95 ? 3.0043 1.7397 2.6850 0.3362 0.8058 0.1118 95 PRO A N 552 C CA . PRO A 95 ? 2.9888 1.7926 2.7351 0.3230 0.7776 0.1427 95 PRO A CA 553 C C . PRO A 95 ? 2.9334 1.8390 2.7035 0.3017 0.7402 0.1466 95 PRO A C 554 O O . PRO A 95 ? 3.2292 2.1290 2.9584 0.2694 0.7151 0.1180 95 PRO A O 555 C CB . PRO A 95 ? 2.9923 1.7232 2.7059 0.2892 0.7616 0.1245 95 PRO A CB 556 C CG . PRO A 95 ? 3.1208 1.7378 2.7508 0.2872 0.7819 0.0846 95 PRO A CG 557 C CD . PRO A 95 ? 3.0612 1.6978 2.6614 0.3046 0.7963 0.0706 95 PRO A CD 558 N N . VAL A 96 ? 2.6652 1.6594 2.4985 0.3191 0.7355 0.1815 96 VAL A N 559 C CA . VAL A 96 ? 2.5320 1.6152 2.3828 0.3016 0.7031 0.1836 96 VAL A CA 560 C C . VAL A 96 ? 2.4476 1.6091 2.3539 0.2974 0.6791 0.2171 96 VAL A C 561 O O . VAL A 96 ? 2.3711 1.5380 2.3158 0.3166 0.6894 0.2485 96 VAL A O 562 C CB . VAL A 96 ? 2.5438 1.6628 2.3961 0.3208 0.7153 0.1828 96 VAL A CB 563 C CG1 . VAL A 96 ? 2.7689 1.8145 2.5515 0.3202 0.7349 0.1461 96 VAL A CG1 564 C CG2 . VAL A 96 ? 2.6049 1.7576 2.5157 0.3598 0.7400 0.2210 96 VAL A CG2 565 N N . SER A 97 ? 2.4435 1.6623 2.3496 0.2734 0.6479 0.2106 97 SER A N 566 C CA . SER A 97 ? 2.3277 1.6126 2.2688 0.2648 0.6235 0.2357 97 SER A CA 567 C C . SER A 97 ? 2.2475 1.6087 2.2104 0.2692 0.6074 0.2467 97 SER A C 568 O O . SER A 97 ? 2.1492 1.5228 2.1221 0.2883 0.6202 0.2496 97 SER A O 569 C CB . SER A 97 ? 2.2004 1.4799 2.1245 0.2312 0.6023 0.2222 97 SER A CB 570 O OG . SER A 97 ? 2.0124 1.3050 1.9109 0.2100 0.5856 0.1946 97 SER A OG 571 N N . LEU A 98 ? 2.1101 1.5186 2.0796 0.2517 0.5811 0.2539 98 LEU A N 572 C CA . LEU A 98 ? 1.9625 1.4359 1.9454 0.2505 0.5610 0.2622 98 LEU A CA 573 C C . LEU A 98 ? 1.9206 1.4205 1.8889 0.2261 0.5372 0.2550 98 LEU A C 574 O O . LEU A 98 ? 1.9380 1.4632 1.9150 0.2246 0.5260 0.2760 98 LEU A O 575 C CB . LEU A 98 ? 1.8862 1.3954 1.9088 0.2709 0.5593 0.3001 98 LEU A CB 576 C CG . LEU A 98 ? 1.8356 1.3953 1.8871 0.2826 0.5517 0.3153 98 LEU A CG 577 C CD1 . LEU A 98 ? 1.7944 1.3977 1.8735 0.2856 0.5304 0.3515 98 LEU A CD1 578 C CD2 . LEU A 98 ? 1.8206 1.4059 1.8531 0.2665 0.5362 0.2920 98 LEU A CD2 579 N N . HIS A 99 ? 1.9899 1.4833 1.9347 0.2082 0.5307 0.2267 99 HIS A N 580 C CA . HIS A 99 ? 2.0853 1.6013 2.0209 0.1876 0.5134 0.2201 99 HIS A CA 581 C C . HIS A 99 ? 2.0913 1.6527 2.0242 0.1839 0.4963 0.2153 99 HIS A C 582 O O . HIS A 99 ? 2.1178 1.6812 2.0411 0.1792 0.4929 0.1962 99 HIS A O 583 C CB . HIS A 99 ? 2.1032 1.5867 2.0227 0.1675 0.5137 0.1968 99 HIS A CB 584 C CG . HIS A 99 ? 1.9983 1.5086 1.9187 0.1489 0.5001 0.1938 99 HIS A CG 585 N ND1 . HIS A 99 ? 2.0363 1.5371 1.9509 0.1289 0.4926 0.1752 99 HIS A ND1 586 C CD2 . HIS A 99 ? 1.9810 1.5261 1.9068 0.1485 0.4941 0.2084 99 HIS A CD2 587 C CE1 . HIS A 99 ? 2.0541 1.5868 1.9790 0.1190 0.4853 0.1805 99 HIS A CE1 588 N NE2 . HIS A 99 ? 2.1260 1.6825 2.0530 0.1314 0.4880 0.1989 99 HIS A NE2 589 N N . ALA A 100 ? 2.0539 1.6465 1.9900 0.1848 0.4849 0.2327 100 ALA A N 590 C CA . ALA A 100 ? 1.9926 1.6202 1.9207 0.1798 0.4677 0.2277 100 ALA A CA 591 C C . ALA A 100 ? 1.9861 1.6185 1.8986 0.1641 0.4628 0.2129 100 ALA A C 592 O O . ALA A 100 ? 2.1009 1.7217 2.0116 0.1576 0.4699 0.2167 100 ALA A O 593 C CB . ALA A 100 ? 1.9032 1.5559 1.8343 0.1868 0.4550 0.2517 100 ALA A CB 594 N N . VAL A 101 ? 1.8100 1.4606 1.7158 0.1592 0.4522 0.1987 101 VAL A N 595 C CA . VAL A 101 ? 1.6215 1.2795 1.5194 0.1477 0.4490 0.1854 101 VAL A CA 596 C C . VAL A 101 ? 1.5411 1.2199 1.4231 0.1489 0.4374 0.1872 101 VAL A C 597 O O . VAL A 101 ? 1.4272 1.1174 1.3085 0.1521 0.4263 0.1864 101 VAL A O 598 C CB . VAL A 101 ? 1.4821 1.1359 1.3836 0.1405 0.4463 0.1655 101 VAL A CB 599 C CG1 . VAL A 101 ? 1.4226 1.0867 1.3266 0.1293 0.4428 0.1564 101 VAL A CG1 600 C CG2 . VAL A 101 ? 1.5259 1.1483 1.4305 0.1385 0.4556 0.1606 101 VAL A CG2 601 N N . GLY A 102 ? 1.5865 1.2672 1.4543 0.1462 0.4412 0.1899 102 GLY A N 602 C CA . GLY A 102 ? 1.7621 1.4516 1.6046 0.1469 0.4318 0.1867 102 GLY A CA 603 C C . GLY A 102 ? 1.8633 1.5498 1.6787 0.1509 0.4234 0.2026 102 GLY A C 604 O O . GLY A 102 ? 1.8182 1.5036 1.6026 0.1497 0.4119 0.1995 102 GLY A O 605 N N . VAL A 103 ? 1.8096 1.4910 1.6341 0.1549 0.4277 0.2201 103 VAL A N 606 C CA . VAL A 103 ? 1.8147 1.4926 1.6133 0.1579 0.4197 0.2402 103 VAL A CA 607 C C . VAL A 103 ? 1.8457 1.5110 1.6467 0.1603 0.4380 0.2549 103 VAL A C 608 O O . VAL A 103 ? 1.9027 1.5620 1.7348 0.1597 0.4517 0.2518 103 VAL A O 609 C CB . VAL A 103 ? 1.7594 1.4492 1.5767 0.1621 0.4021 0.2552 103 VAL A CB 610 C CG1 . VAL A 103 ? 1.6844 1.3858 1.4886 0.1563 0.3790 0.2483 103 VAL A CG1 611 C CG2 . VAL A 103 ? 1.7555 1.4464 1.6165 0.1677 0.4137 0.2525 103 VAL A CG2 612 N N . SER A 104 ? 1.8041 1.4614 1.5687 0.1616 0.4377 0.2707 104 SER A N 613 C CA . SER A 104 ? 1.9255 1.5706 1.6923 0.1636 0.4566 0.2881 104 SER A CA 614 C C . SER A 104 ? 2.0140 1.6555 1.7881 0.1700 0.4488 0.3161 104 SER A C 615 O O . SER A 104 ? 1.8884 1.5412 1.6676 0.1732 0.4273 0.3242 104 SER A O 616 C CB . SER A 104 ? 2.0006 1.6364 1.7261 0.1624 0.4723 0.2896 104 SER A CB 617 O OG . SER A 104 ? 2.1049 1.7298 1.7803 0.1651 0.4642 0.3088 104 SER A OG 618 N N . TYR A 105 ? 2.0947 1.7223 1.8754 0.1716 0.4667 0.3332 105 TYR A N 619 C CA . TYR A 105 ? 2.0214 1.6409 1.8199 0.1793 0.4660 0.3612 105 TYR A CA 620 C C . TYR A 105 ? 2.0191 1.6209 1.8119 0.1772 0.4885 0.3763 105 TYR A C 621 O O . TYR A 105 ? 2.1053 1.7062 1.8859 0.1702 0.5040 0.3651 105 TYR A O 622 C CB . TYR A 105 ? 2.0959 1.7105 1.9453 0.1841 0.4710 0.3547 105 TYR A CB 623 C CG . TYR A 105 ? 2.1125 1.7234 1.9799 0.1758 0.4812 0.3236 105 TYR A CG 624 C CD1 . TYR A 105 ? 2.0767 1.6756 1.9489 0.1658 0.4985 0.3169 105 TYR A CD1 625 C CD2 . TYR A 105 ? 2.1002 1.7215 1.9822 0.1771 0.4721 0.3041 105 TYR A CD2 626 C CE1 . TYR A 105 ? 2.1711 1.7691 2.0612 0.1560 0.5020 0.2916 105 TYR A CE1 627 C CE2 . TYR A 105 ? 2.0949 1.7117 1.9880 0.1688 0.4780 0.2778 105 TYR A CE2 628 C CZ . TYR A 105 ? 2.1448 1.7502 2.0417 0.1577 0.4908 0.2715 105 TYR A CZ 629 O OH . TYR A 105 ? 2.0359 1.6392 1.9451 0.1473 0.4913 0.2481 105 TYR A OH 630 N N . TRP A 106 ? 1.9708 1.5597 1.7782 0.1838 0.4922 0.4040 106 TRP A N 631 C CA . TRP A 106 ? 2.0511 1.6191 1.8690 0.1804 0.5163 0.4188 106 TRP A CA 632 C C . TRP A 106 ? 2.0147 1.5645 1.8828 0.1773 0.5278 0.4063 106 TRP A C 633 O O . TRP A 106 ? 2.0524 1.6068 1.9384 0.1779 0.5200 0.3827 106 TRP A O 634 C CB . TRP A 106 ? 2.0791 1.6363 1.8833 0.1884 0.5152 0.4574 106 TRP A CB 635 C CG . TRP A 106 ? 2.1983 1.7653 1.9443 0.1898 0.5005 0.4714 106 TRP A CG 636 C CD1 . TRP A 106 ? 2.2289 1.8103 1.9559 0.1945 0.4706 0.4797 106 TRP A CD1 637 C CD2 . TRP A 106 ? 2.3943 1.9541 2.0883 0.1855 0.5143 0.4802 106 TRP A CD2 638 N NE1 . TRP A 106 ? 2.4173 1.9958 2.0761 0.1912 0.4611 0.4908 106 TRP A NE1 639 C CE2 . TRP A 106 ? 2.5318 2.0950 2.1654 0.1875 0.4904 0.4905 106 TRP A CE2 640 C CE3 . TRP A 106 ? 2.5892 2.1395 2.2822 0.1799 0.5456 0.4818 106 TRP A CE3 641 C CZ2 . TRP A 106 ? 2.8050 2.3551 2.3655 0.1855 0.4990 0.4994 106 TRP A CZ2 642 C CZ3 . TRP A 106 ? 2.8367 2.3806 2.4668 0.1802 0.5580 0.4937 106 TRP A CZ3 643 C CH2 . TRP A 106 ? 2.9743 2.5145 2.5332 0.1838 0.5358 0.5008 106 TRP A CH2 644 N N . LYS A 107 ? 1.8092 1.3340 1.6959 0.1732 0.5458 0.4219 107 LYS A N 645 C CA . LYS A 107 ? 1.7941 1.2909 1.7195 0.1672 0.5545 0.4076 107 LYS A CA 646 C C . LYS A 107 ? 1.9520 1.4213 1.8994 0.1815 0.5547 0.4168 107 LYS A C 647 O O . LYS A 107 ? 2.1376 1.5691 2.1070 0.1768 0.5659 0.4092 107 LYS A O 648 C CB . LYS A 107 ? 1.6859 1.1660 1.6279 0.1502 0.5719 0.4119 107 LYS A CB 649 C CG . LYS A 107 ? 1.7149 1.2178 1.6601 0.1351 0.5722 0.3884 107 LYS A CG 650 C CD . LYS A 107 ? 1.8160 1.2996 1.7974 0.1142 0.5807 0.3820 107 LYS A CD 651 C CE . LYS A 107 ? 1.8172 1.3006 1.8112 0.1035 0.5675 0.3474 107 LYS A CE 652 N NZ . LYS A 107 ? 1.7996 1.2773 1.8269 0.0783 0.5697 0.3428 107 LYS A NZ 653 N N . ALA A 108 ? 2.0068 1.4929 1.9484 0.1987 0.5424 0.4338 108 ALA A N 654 C CA . ALA A 108 ? 1.8883 1.3577 1.8575 0.2173 0.5439 0.4442 108 ALA A CA 655 C C . ALA A 108 ? 1.8836 1.3853 1.8551 0.2262 0.5277 0.4325 108 ALA A C 656 O O . ALA A 108 ? 1.9117 1.4211 1.9053 0.2443 0.5233 0.4516 108 ALA A O 657 C CB . ALA A 108 ? 1.8851 1.3477 1.8610 0.2313 0.5448 0.4875 108 ALA A CB 658 N N . SER A 109 ? 1.9474 1.4713 1.8993 0.2131 0.5187 0.4049 109 SER A N 659 C CA . SER A 109 ? 2.1183 1.6569 2.0780 0.2155 0.5117 0.3801 109 SER A CA 660 C C . SER A 109 ? 2.1731 1.6990 2.1237 0.1975 0.5186 0.3467 109 SER A C 661 O O . SER A 109 ? 2.1635 1.6642 2.1155 0.1870 0.5306 0.3473 109 SER A O 662 C CB . SER A 109 ? 2.1360 1.7174 2.0820 0.2171 0.4877 0.3855 109 SER A CB 663 O OG . SER A 109 ? 2.0771 1.6720 2.0408 0.2322 0.4776 0.4191 109 SER A OG 664 N N . GLU A 110 ? 2.2198 1.7637 2.1650 0.1927 0.5099 0.3210 110 GLU A N 665 C CA . GLU A 110 ? 2.3045 1.8364 2.2464 0.1764 0.5136 0.2914 110 GLU A CA 666 C C . GLU A 110 ? 2.3766 1.8693 2.3284 0.1796 0.5246 0.2770 110 GLU A C 667 O O . GLU A 110 ? 2.6129 2.1045 2.5586 0.1757 0.5213 0.2530 110 GLU A O 668 C CB . GLU A 110 ? 2.2079 1.7320 2.1479 0.1605 0.5208 0.2953 110 GLU A CB 669 C CG . GLU A 110 ? 1.9708 1.4799 1.9187 0.1414 0.5225 0.2716 110 GLU A CG 670 C CD . GLU A 110 ? 1.8634 1.3623 1.8239 0.1261 0.5319 0.2834 110 GLU A CD 671 O OE1 . GLU A 110 ? 1.8076 1.2856 1.7734 0.1303 0.5423 0.3059 110 GLU A OE1 672 O OE2 . GLU A 110 ? 1.7979 1.3113 1.7677 0.1098 0.5291 0.2730 110 GLU A OE2 673 N N . GLY A 111 ? 2.2174 1.6731 2.1797 0.1866 0.5386 0.2918 111 GLY A N 674 C CA . GLY A 111 ? 2.1609 1.5692 2.1257 0.1950 0.5531 0.2803 111 GLY A CA 675 C C . GLY A 111 ? 2.2038 1.5755 2.1525 0.1742 0.5534 0.2497 111 GLY A C 676 O O . GLY A 111 ? 2.2441 1.5926 2.1776 0.1771 0.5572 0.2275 111 GLY A O 677 N N . ALA A 112 ? 2.1511 1.5179 2.1028 0.1523 0.5490 0.2506 112 ALA A N 678 C CA . ALA A 112 ? 2.1560 1.4883 2.0982 0.1277 0.5441 0.2264 112 ALA A CA 679 C C . ALA A 112 ? 2.0696 1.3699 2.0259 0.1103 0.5488 0.2390 112 ALA A C 680 O O . ALA A 112 ? 1.8200 1.1465 1.7941 0.1110 0.5524 0.2650 112 ALA A O 681 C CB . ALA A 112 ? 2.2733 1.6493 2.2137 0.1120 0.5265 0.2112 112 ALA A CB 682 N N . GLU A 113 ? 2.1596 1.4003 2.1045 0.0935 0.5484 0.2210 113 GLU A N 683 C CA . GLU A 113 ? 2.4293 1.6284 2.3887 0.0759 0.5530 0.2333 113 GLU A CA 684 C C . GLU A 113 ? 2.5231 1.7265 2.4969 0.0386 0.5351 0.2255 113 GLU A C 685 O O . GLU A 113 ? 2.9176 2.0914 2.8711 0.0200 0.5203 0.1985 113 GLU A O 686 C CB . GLU A 113 ? 2.5980 1.7130 2.5361 0.0836 0.5672 0.2241 113 GLU A CB 687 C CG . GLU A 113 ? 2.7722 1.8330 2.7230 0.0622 0.5703 0.2347 113 GLU A CG 688 C CD . GLU A 113 ? 2.9732 1.9569 2.9103 0.0812 0.5924 0.2383 113 GLU A CD 689 O OE1 . GLU A 113 ? 3.1249 2.0465 3.0234 0.0855 0.5977 0.2098 113 GLU A OE1 690 O OE2 . GLU A 113 ? 2.9259 1.9083 2.8882 0.0928 0.6059 0.2704 113 GLU A OE2 691 N N . TYR A 114 ? 2.3742 1.6144 2.3828 0.0280 0.5368 0.2517 114 TYR A N 692 C CA . TYR A 114 ? 2.2151 1.4638 2.2545 -0.0073 0.5238 0.2554 114 TYR A CA 693 C C . TYR A 114 ? 2.1820 1.4276 2.2546 -0.0142 0.5382 0.2897 114 TYR A C 694 O O . TYR A 114 ? 2.2997 1.4835 2.3718 -0.0228 0.5433 0.2940 114 TYR A O 695 C CB . TYR A 114 ? 2.1246 1.4426 2.1808 -0.0151 0.5101 0.2509 114 TYR A CB 696 C CG . TYR A 114 ? 2.1901 1.5691 2.2423 0.0125 0.5205 0.2616 114 TYR A CG 697 C CD1 . TYR A 114 ? 2.1610 1.5387 2.1809 0.0412 0.5257 0.2540 114 TYR A CD1 698 C CD2 . TYR A 114 ? 2.2261 1.6620 2.3064 0.0093 0.5253 0.2798 114 TYR A CD2 699 C CE1 . TYR A 114 ? 2.0110 1.4390 2.0240 0.0616 0.5301 0.2631 114 TYR A CE1 700 C CE2 . TYR A 114 ? 2.0439 1.5238 2.1095 0.0329 0.5340 0.2864 114 TYR A CE2 701 C CZ . TYR A 114 ? 1.9001 1.3747 1.9307 0.0569 0.5335 0.2771 114 TYR A CZ 702 O OH . TYR A 114 ? 1.6917 1.2046 1.7049 0.0756 0.5372 0.2830 114 TYR A OH 703 N N . ASP A 115 ? 2.0999 1.4073 2.1977 -0.0099 0.5468 0.3144 115 ASP A N 704 C CA . ASP A 115 ? 2.0662 1.3765 2.1899 -0.0119 0.5651 0.3510 115 ASP A CA 705 C C . ASP A 115 ? 2.0560 1.4134 2.1660 0.0163 0.5808 0.3713 115 ASP A C 706 O O . ASP A 115 ? 1.9969 1.4017 2.1241 0.0139 0.5901 0.3896 115 ASP A O 707 C CB . ASP A 115 ? 2.0328 1.3665 2.2061 -0.0440 0.5616 0.3660 115 ASP A CB 708 C CG . ASP A 115 ? 2.1040 1.3861 2.2908 -0.0779 0.5413 0.3500 115 ASP A CG 709 O OD1 . ASP A 115 ? 2.1311 1.4044 2.2993 -0.0869 0.5190 0.3180 115 ASP A OD1 710 O OD2 . ASP A 115 ? 2.0952 1.3421 2.3074 -0.0968 0.5465 0.3700 115 ASP A OD2 711 N N . ASP A 116 ? 2.1820 1.5248 2.2592 0.0432 0.5835 0.3682 116 ASP A N 712 C CA . ASP A 116 ? 2.2731 1.6444 2.3327 0.0675 0.5952 0.3933 116 ASP A CA 713 C C . ASP A 116 ? 2.2465 1.6108 2.3265 0.0587 0.6128 0.4297 116 ASP A C 714 O O . ASP A 116 ? 2.2675 1.6677 2.3391 0.0663 0.6246 0.4525 116 ASP A O 715 C CB . ASP A 116 ? 2.3929 1.7384 2.4294 0.0935 0.5949 0.3944 116 ASP A CB 716 C CG . ASP A 116 ? 2.4581 1.8020 2.4787 0.1022 0.5817 0.3608 116 ASP A CG 717 O OD1 . ASP A 116 ? 2.5220 1.8524 2.5467 0.0843 0.5725 0.3332 116 ASP A OD1 718 O OD2 . ASP A 116 ? 2.5187 1.8746 2.5235 0.1262 0.5799 0.3644 116 ASP A OD2 719 N N . GLN A 117 ? 2.1691 1.4830 2.2727 0.0416 0.6151 0.4345 117 GLN A N 720 C CA . GLN A 117 ? 2.2101 1.5058 2.3338 0.0347 0.6323 0.4717 117 GLN A CA 721 C C . GLN A 117 ? 2.4106 1.6835 2.5120 0.0612 0.6421 0.4960 117 GLN A C 722 O O . GLN A 117 ? 2.8629 2.1117 2.9779 0.0581 0.6562 0.5287 117 GLN A O 723 C CB . GLN A 117 ? 2.0695 1.4184 2.2078 0.0283 0.6465 0.4966 117 GLN A CB 724 C CG . GLN A 117 ? 2.1533 1.4976 2.3434 -0.0044 0.6513 0.5098 117 GLN A CG 725 C CD . GLN A 117 ? 2.2335 1.5866 2.4480 -0.0281 0.6299 0.4779 117 GLN A CD 726 O OE1 . GLN A 117 ? 2.0766 1.4328 2.2649 -0.0193 0.6128 0.4440 117 GLN A OE1 727 N NE2 . GLN A 117 ? 2.4293 1.7883 2.6968 -0.0598 0.6293 0.4914 117 GLN A NE2 728 N N . THR A 118 ? 2.3363 1.6189 2.4081 0.0866 0.6338 0.4835 118 THR A N 729 C CA . THR A 118 ? 2.3165 1.5994 2.3690 0.1134 0.6391 0.5127 118 THR A CA 730 C C . THR A 118 ? 2.3192 1.5423 2.3822 0.1251 0.6441 0.5213 118 THR A C 731 O O . THR A 118 ? 2.2559 1.4332 2.3293 0.1161 0.6426 0.4955 118 THR A O 732 C CB . THR A 118 ? 2.3066 1.6324 2.3288 0.1342 0.6255 0.5011 118 THR A CB 733 O OG1 . THR A 118 ? 2.3042 1.6223 2.3284 0.1345 0.6140 0.4628 118 THR A OG1 734 C CG2 . THR A 118 ? 2.2727 1.6514 2.2736 0.1293 0.6254 0.5033 118 THR A CG2 735 N N . SER A 119 ? 2.4624 1.6834 2.5192 0.1458 0.6503 0.5583 119 SER A N 736 C CA . SER A 119 ? 2.6912 1.8618 2.7602 0.1655 0.6567 0.5726 119 SER A CA 737 C C . SER A 119 ? 2.5927 1.7627 2.6574 0.1863 0.6486 0.5465 119 SER A C 738 O O . SER A 119 ? 2.4755 1.6886 2.5254 0.1860 0.6354 0.5218 119 SER A O 739 C CB . SER A 119 ? 2.8881 2.0692 2.9522 0.1842 0.6610 0.6227 119 SER A CB 740 O OG . SER A 119 ? 3.0025 2.2287 3.0480 0.2069 0.6457 0.6291 119 SER A OG 741 N N . GLN A 120 ? 2.6088 1.7289 2.6880 0.2059 0.6590 0.5541 120 GLN A N 742 C CA . GLN A 120 ? 2.7092 1.8198 2.7881 0.2248 0.6586 0.5279 120 GLN A CA 743 C C . GLN A 120 ? 2.7086 1.8842 2.7851 0.2472 0.6447 0.5396 120 GLN A C 744 O O . GLN A 120 ? 2.7682 1.9642 2.8381 0.2512 0.6378 0.5106 120 GLN A O 745 C CB . GLN A 120 ? 2.8924 1.9254 2.9867 0.2426 0.6793 0.5316 120 GLN A CB 746 C CG . GLN A 120 ? 3.0648 2.0211 3.1519 0.2169 0.6887 0.5038 120 GLN A CG 747 C CD . GLN A 120 ? 3.2449 2.2000 3.3391 0.1853 0.6856 0.5203 120 GLN A CD 748 O OE1 . GLN A 120 ? 3.1938 2.1885 3.2816 0.1587 0.6725 0.5052 120 GLN A OE1 749 N NE2 . GLN A 120 ? 3.4049 2.3149 3.5163 0.1892 0.6996 0.5542 120 GLN A NE2 750 N N . ARG A 121 ? 2.7163 1.9244 2.7958 0.2594 0.6380 0.5823 121 ARG A N 751 C CA . ARG A 121 ? 2.6701 1.9400 2.7458 0.2756 0.6183 0.5941 121 ARG A CA 752 C C . ARG A 121 ? 2.6495 1.9658 2.6939 0.2548 0.6020 0.5650 121 ARG A C 753 O O . ARG A 121 ? 2.6675 2.0332 2.7009 0.2608 0.5827 0.5654 121 ARG A O 754 C CB . ARG A 121 ? 2.5127 1.8047 2.5917 0.2902 0.6091 0.6473 121 ARG A CB 755 C CG . ARG A 121 ? 2.3604 1.6861 2.4645 0.3174 0.5955 0.6692 121 ARG A CG 756 C CD . ARG A 121 ? 2.3627 1.7233 2.4592 0.3248 0.5749 0.7196 121 ARG A CD 757 N NE . ARG A 121 ? 2.6948 2.0170 2.8130 0.3379 0.5892 0.7615 121 ARG A NE 758 C CZ . ARG A 121 ? 3.0005 2.2996 3.0955 0.3243 0.5969 0.7802 121 ARG A CZ 759 N NH1 . ARG A 121 ? 3.2188 2.5313 3.2696 0.2983 0.5942 0.7608 121 ARG A NH1 760 N NH2 . ARG A 121 ? 3.0289 2.2912 3.1477 0.3379 0.6100 0.8210 121 ARG A NH2 761 N N . GLU A 122 ? 2.5406 1.8379 2.5749 0.2298 0.6100 0.5409 122 GLU A N 762 C CA . GLU A 122 ? 2.3829 1.7150 2.3958 0.2102 0.6000 0.5100 122 GLU A CA 763 C C . GLU A 122 ? 2.1527 1.4590 2.1722 0.1974 0.6035 0.4665 122 GLU A C 764 O O . GLU A 122 ? 1.9864 1.3208 1.9935 0.1829 0.5943 0.4400 122 GLU A O 765 C CB . GLU A 122 ? 2.5413 1.8846 2.5396 0.1911 0.6051 0.5239 122 GLU A CB 766 C CG . GLU A 122 ? 2.6839 2.0556 2.6561 0.1997 0.5999 0.5618 122 GLU A CG 767 C CD . GLU A 122 ? 2.7274 2.1071 2.6823 0.1822 0.6122 0.5729 122 GLU A CD 768 O OE1 . GLU A 122 ? 2.7968 2.1451 2.7697 0.1747 0.6290 0.5942 122 GLU A OE1 769 O OE2 . GLU A 122 ? 2.6404 2.0557 2.5649 0.1764 0.6073 0.5613 122 GLU A OE2 770 N N . LYS A 123 ? 2.0985 1.3472 2.1332 0.2026 0.6167 0.4597 123 LYS A N 771 C CA . LYS A 123 ? 2.1485 1.3648 2.1776 0.1927 0.6181 0.4178 123 LYS A CA 772 C C . LYS A 123 ? 2.2152 1.4064 2.2468 0.2186 0.6269 0.4073 123 LYS A C 773 O O . LYS A 123 ? 2.1070 1.2547 2.1255 0.2132 0.6329 0.3745 123 LYS A O 774 C CB . LYS A 123 ? 2.1261 1.2846 2.1587 0.1670 0.6255 0.4067 123 LYS A CB 775 C CG . LYS A 123 ? 2.0243 1.2129 2.0563 0.1356 0.6141 0.3944 123 LYS A CG 776 C CD . LYS A 123 ? 2.0011 1.1357 2.0344 0.1074 0.6120 0.3687 123 LYS A CD 777 C CE . LYS A 123 ? 2.0290 1.1904 2.0827 0.0774 0.6067 0.3794 123 LYS A CE 778 N NZ . LYS A 123 ? 2.0985 1.2476 2.1545 0.0460 0.5914 0.3488 123 LYS A NZ 779 N N . GLU A 124 ? 2.3404 1.5589 2.3880 0.2464 0.6277 0.4370 124 GLU A N 780 C CA . GLU A 124 ? 2.4114 1.6197 2.4721 0.2751 0.6387 0.4352 124 GLU A CA 781 C C . GLU A 124 ? 2.3880 1.6343 2.4368 0.2739 0.6283 0.4062 124 GLU A C 782 O O . GLU A 124 ? 2.6113 1.8299 2.6581 0.2874 0.6426 0.3872 124 GLU A O 783 C CB . GLU A 124 ? 2.4294 1.6667 2.5212 0.3032 0.6383 0.4815 124 GLU A CB 784 C CG . GLU A 124 ? 2.6603 1.8377 2.7766 0.3288 0.6650 0.4999 124 GLU A CG 785 C CD . GLU A 124 ? 2.8930 2.0837 3.0352 0.3426 0.6621 0.5519 124 GLU A CD 786 O OE1 . GLU A 124 ? 2.9535 2.2111 3.1025 0.3455 0.6389 0.5779 124 GLU A OE1 787 O OE2 . GLU A 124 ? 2.9825 2.1130 3.1345 0.3490 0.6813 0.5666 124 GLU A OE2 788 N N . ASP A 125 ? 2.2048 1.5104 2.2428 0.2590 0.6056 0.4037 125 ASP A N 789 C CA . ASP A 125 ? 2.0181 1.3587 2.0443 0.2545 0.5941 0.3768 125 ASP A CA 790 C C . ASP A 125 ? 2.0857 1.3832 2.0890 0.2385 0.6011 0.3354 125 ASP A C 791 O O . ASP A 125 ? 2.0689 1.3657 2.0645 0.2461 0.6046 0.3149 125 ASP A O 792 C CB . ASP A 125 ? 2.0241 1.4240 2.0372 0.2392 0.5703 0.3800 125 ASP A CB 793 C CG . ASP A 125 ? 2.0291 1.4207 2.0274 0.2148 0.5689 0.3772 125 ASP A CG 794 O OD1 . ASP A 125 ? 2.0128 1.3844 2.0178 0.2154 0.5770 0.4027 125 ASP A OD1 795 O OD2 . ASP A 125 ? 2.0597 1.4675 2.0435 0.1959 0.5606 0.3527 125 ASP A OD2 796 N N . ASP A 126 ? 2.1935 1.4532 2.1867 0.2161 0.6028 0.3265 126 ASP A N 797 C CA . ASP A 126 ? 2.2665 1.4955 2.2366 0.1897 0.5979 0.2897 126 ASP A CA 798 C C . ASP A 126 ? 2.2163 1.3884 2.1614 0.1947 0.6095 0.2589 126 ASP A C 799 O O . ASP A 126 ? 2.0587 1.2155 1.9786 0.1726 0.5990 0.2281 126 ASP A O 800 C CB . ASP A 126 ? 2.3188 1.5165 2.2935 0.1643 0.5973 0.2949 126 ASP A CB 801 C CG . ASP A 126 ? 2.2434 1.4967 2.2328 0.1539 0.5877 0.3184 126 ASP A CG 802 O OD1 . ASP A 126 ? 2.2851 1.5747 2.2817 0.1722 0.5880 0.3454 126 ASP A OD1 803 O OD2 . ASP A 126 ? 2.1721 1.4311 2.1651 0.1272 0.5801 0.3112 126 ASP A OD2 804 N N . LYS A 127 ? 2.2398 1.3811 2.1910 0.2246 0.6317 0.2697 127 LYS A N 805 C CA . LYS A 127 ? 2.2565 1.3250 2.1797 0.2360 0.6534 0.2460 127 LYS A CA 806 C C . LYS A 127 ? 2.1716 1.2322 2.1223 0.2762 0.6797 0.2738 127 LYS A C 807 O O . LYS A 127 ? 2.2881 1.3041 2.2511 0.2848 0.6942 0.2917 127 LYS A O 808 C CB . LYS A 127 ? 2.4214 1.4043 2.3203 0.2141 0.6578 0.2303 127 LYS A CB 809 C CG . LYS A 127 ? 2.5568 1.4970 2.4090 0.1827 0.6441 0.1890 127 LYS A CG 810 C CD . LYS A 127 ? 2.7806 1.6107 2.5969 0.1752 0.6586 0.1706 127 LYS A CD 811 C CE . LYS A 127 ? 2.8924 1.6634 2.6448 0.1705 0.6620 0.1292 127 LYS A CE 812 N NZ . LYS A 127 ? 2.8981 1.5628 2.6109 0.1915 0.6955 0.1162 127 LYS A NZ 813 N N . VAL A 128 ? 2.1505 1.2543 2.1171 0.3010 0.6865 0.2816 128 VAL A N 814 C CA . VAL A 128 ? 2.4152 1.5084 2.4164 0.3412 0.7147 0.3113 128 VAL A CA 815 C C . VAL A 128 ? 2.7202 1.7256 2.6890 0.3596 0.7512 0.2875 128 VAL A C 816 O O . VAL A 128 ? 2.9049 1.8985 2.8381 0.3578 0.7572 0.2575 128 VAL A O 817 C CB . VAL A 128 ? 2.3181 1.4952 2.3644 0.3635 0.7092 0.3400 128 VAL A CB 818 C CG1 . VAL A 128 ? 2.1754 1.3667 2.2755 0.3925 0.7197 0.3881 128 VAL A CG1 819 C CG2 . VAL A 128 ? 2.3725 1.6264 2.4201 0.3383 0.6713 0.3404 128 VAL A CG2 820 N N . PHE A 129 ? 2.7887 1.7282 2.7652 0.3776 0.7767 0.3011 129 PHE A N 821 C CA . PHE A 129 ? 2.8718 1.7087 2.8069 0.3946 0.8145 0.2762 129 PHE A CA 822 C C . PHE A 129 ? 2.9469 1.7964 2.9036 0.4388 0.8496 0.2885 129 PHE A C 823 O O . PHE A 129 ? 2.8142 1.7455 2.8359 0.4598 0.8459 0.3286 129 PHE A O 824 C CB . PHE A 129 ? 2.8975 1.6547 2.8353 0.4001 0.8314 0.2882 129 PHE A CB 825 C CG . PHE A 129 ? 2.8749 1.5747 2.7689 0.3559 0.8100 0.2606 129 PHE A CG 826 C CD1 . PHE A 129 ? 2.8313 1.5487 2.6865 0.3164 0.7793 0.2268 129 PHE A CD1 827 C CD2 . PHE A 129 ? 3.0118 1.6377 2.9077 0.3539 0.8212 0.2709 129 PHE A CD2 828 C CE1 . PHE A 129 ? 2.8977 1.5685 2.7236 0.2749 0.7580 0.2066 129 PHE A CE1 829 C CE2 . PHE A 129 ? 3.0660 1.6405 2.9291 0.3111 0.8006 0.2491 129 PHE A CE2 830 C CZ . PHE A 129 ? 3.0676 1.6677 2.8983 0.2711 0.7681 0.2178 129 PHE A CZ 831 N N . PRO A 130 ? 3.0633 1.8319 2.9647 0.4521 0.8835 0.2556 130 PRO A N 832 C CA . PRO A 130 ? 2.9943 1.7702 2.9154 0.4967 0.9248 0.2680 130 PRO A CA 833 C C . PRO A 130 ? 2.8763 1.6842 2.8819 0.5388 0.9476 0.3226 130 PRO A C 834 O O . PRO A 130 ? 3.0066 1.7552 3.0195 0.5485 0.9614 0.3348 130 PRO A O 835 C CB . PRO A 130 ? 3.1465 1.7946 2.9832 0.5048 0.9634 0.2257 130 PRO A CB 836 C CG . PRO A 130 ? 3.1886 1.7957 2.9541 0.4527 0.9262 0.1824 130 PRO A CG 837 C CD . PRO A 130 ? 3.1642 1.8305 2.9780 0.4241 0.8836 0.2055 130 PRO A CD 838 N N . GLY A 131 ? 2.7002 1.6019 2.7716 0.5615 0.9485 0.3571 131 GLY A N 839 C CA . GLY A 131 ? 2.6082 1.5621 2.7726 0.5981 0.9601 0.4164 131 GLY A CA 840 C C . GLY A 131 ? 2.5290 1.5679 2.7433 0.5761 0.9096 0.4515 131 GLY A C 841 O O . GLY A 131 ? 2.3321 1.4190 2.6220 0.6010 0.9095 0.5042 131 GLY A O 842 N N . GLY A 132 ? 2.5818 1.6399 2.7527 0.5304 0.8672 0.4238 132 GLY A N 843 C CA . GLY A 132 ? 2.7465 1.8590 2.9378 0.5041 0.8228 0.4462 132 GLY A CA 844 C C . GLY A 132 ? 2.7117 1.9324 2.9339 0.4878 0.7805 0.4653 132 GLY A C 845 O O . GLY A 132 ? 2.4659 1.7116 2.6504 0.4569 0.7552 0.4346 132 GLY A O 846 N N . SER A 133 ? 2.7297 2.0107 3.0197 0.5080 0.7714 0.5174 133 SER A N 847 C CA . SER A 133 ? 2.5344 1.9103 2.8524 0.4919 0.7274 0.5415 133 SER A CA 848 C C . SER A 133 ? 2.7001 2.0845 2.9904 0.4610 0.6916 0.5451 133 SER A C 849 O O . SER A 133 ? 2.8786 2.2363 3.1800 0.4681 0.6953 0.5707 133 SER A O 850 C CB . SER A 133 ? 2.3275 1.7641 2.7299 0.5241 0.7288 0.5984 133 SER A CB 851 O OG . SER A 133 ? 2.1780 1.6152 2.6107 0.5530 0.7646 0.5978 133 SER A OG 852 N N . HIS A 134 ? 2.6888 2.1057 2.9408 0.4280 0.6609 0.5191 134 HIS A N 853 C CA . HIS A 134 ? 2.6164 2.0576 2.8453 0.4012 0.6268 0.5272 134 HIS A CA 854 C C . HIS A 134 ? 2.4314 1.9355 2.6428 0.3776 0.5915 0.5152 134 HIS A C 855 O O . HIS A 134 ? 2.1391 1.6458 2.3302 0.3679 0.5937 0.4803 134 HIS A O 856 C CB . HIS A 134 ? 2.6408 2.0177 2.8242 0.3819 0.6363 0.5014 134 HIS A CB 857 C CG . HIS A 134 ? 2.6540 2.0564 2.7995 0.3487 0.6073 0.4894 134 HIS A CG 858 N ND1 . HIS A 134 ? 2.5496 1.9719 2.6635 0.3265 0.5938 0.4533 134 HIS A ND1 859 C CD2 . HIS A 134 ? 2.6458 2.0557 2.7795 0.3362 0.5923 0.5105 134 HIS A CD2 860 C CE1 . HIS A 134 ? 2.3519 1.7924 2.4389 0.3033 0.5738 0.4522 134 HIS A CE1 861 N NE2 . HIS A 134 ? 2.5132 1.9462 2.6089 0.3084 0.5734 0.4861 134 HIS A NE2 862 N N . THR A 135 ? 2.3845 1.9340 2.5999 0.3686 0.5591 0.5453 135 THR A N 863 C CA . THR A 135 ? 2.2314 1.8383 2.4331 0.3496 0.5232 0.5427 135 THR A CA 864 C C . THR A 135 ? 2.1856 1.7819 2.3266 0.3199 0.5111 0.5095 135 THR A C 865 O O . THR A 135 ? 2.1661 1.7278 2.2816 0.3120 0.5191 0.5071 135 THR A O 866 C CB . THR A 135 ? 2.2773 1.9290 2.4977 0.3506 0.4906 0.5900 135 THR A CB 867 O OG1 . THR A 135 ? 2.5593 2.2164 2.8425 0.3803 0.5031 0.6323 135 THR A OG1 868 C CG2 . THR A 135 ? 2.2470 1.9547 2.4655 0.3357 0.4552 0.5900 135 THR A CG2 869 N N . TYR A 136 ? 2.1133 1.7412 2.2357 0.3043 0.4922 0.4876 136 TYR A N 870 C CA . TYR A 136 ? 2.0740 1.6996 2.1434 0.2785 0.4799 0.4588 136 TYR A CA 871 C C . TYR A 136 ? 2.0128 1.6805 2.0620 0.2660 0.4440 0.4727 136 TYR A C 872 O O . TYR A 136 ? 1.8300 1.5343 1.9094 0.2727 0.4241 0.4977 136 TYR A O 873 C CB . TYR A 136 ? 2.0730 1.6907 2.1293 0.2695 0.4892 0.4165 136 TYR A CB 874 C CG . TYR A 136 ? 2.0933 1.6602 2.1482 0.2735 0.5196 0.3935 136 TYR A CG 875 C CD1 . TYR A 136 ? 2.1302 1.6729 2.2164 0.2966 0.5439 0.4018 136 TYR A CD1 876 C CD2 . TYR A 136 ? 2.1000 1.6409 2.1219 0.2539 0.5239 0.3639 136 TYR A CD2 877 C CE1 . TYR A 136 ? 2.0951 1.5801 2.1679 0.2984 0.5705 0.3775 136 TYR A CE1 878 C CE2 . TYR A 136 ? 2.2134 1.7039 2.2297 0.2529 0.5458 0.3424 136 TYR A CE2 879 C CZ . TYR A 136 ? 2.1471 1.6057 2.1831 0.2743 0.5683 0.3474 136 TYR A CZ 880 O OH . TYR A 136 ? 2.1599 1.5581 2.1783 0.2713 0.5885 0.3229 136 TYR A OH 881 N N . VAL A 137 ? 1.9627 1.6226 1.9604 0.2474 0.4363 0.4572 137 VAL A N 882 C CA . VAL A 137 ? 1.8638 1.5497 1.8238 0.2327 0.4054 0.4581 137 VAL A CA 883 C C . VAL A 137 ? 1.9324 1.6088 1.8478 0.2159 0.4086 0.4212 137 VAL A C 884 O O . VAL A 137 ? 1.9961 1.6483 1.8881 0.2105 0.4265 0.4113 137 VAL A O 885 C CB . VAL A 137 ? 1.8179 1.5041 1.7476 0.2302 0.3882 0.4905 137 VAL A CB 886 C CG1 . VAL A 137 ? 1.7105 1.3686 1.5876 0.2196 0.4030 0.4770 137 VAL A CG1 887 C CG2 . VAL A 137 ? 1.7653 1.4818 1.6739 0.2199 0.3484 0.5019 137 VAL A CG2 888 N N . TRP A 138 ? 1.9687 1.6662 1.8768 0.2078 0.3906 0.4050 138 TRP A N 889 C CA . TRP A 138 ? 1.9611 1.6533 1.8263 0.1934 0.3887 0.3745 138 TRP A CA 890 C C . TRP A 138 ? 2.0063 1.7075 1.8239 0.1824 0.3582 0.3816 138 TRP A C 891 O O . TRP A 138 ? 1.9150 1.6383 1.7470 0.1813 0.3305 0.4006 138 TRP A O 892 C CB . TRP A 138 ? 1.8934 1.5947 1.7820 0.1918 0.3929 0.3475 138 TRP A CB 893 C CG . TRP A 138 ? 1.8475 1.5351 1.7732 0.2012 0.4185 0.3381 138 TRP A CG 894 C CD1 . TRP A 138 ? 2.0056 1.6645 1.9337 0.2035 0.4417 0.3346 138 TRP A CD1 895 C CD2 . TRP A 138 ? 1.8097 1.5060 1.7679 0.2078 0.4237 0.3291 138 TRP A CD2 896 N NE1 . TRP A 138 ? 1.9772 1.6211 1.9316 0.2103 0.4588 0.3219 138 TRP A NE1 897 C CE2 . TRP A 138 ? 1.9126 1.5791 1.8837 0.2145 0.4502 0.3184 138 TRP A CE2 898 C CE3 . TRP A 138 ? 1.8105 1.5345 1.7866 0.2078 0.4090 0.3301 138 TRP A CE3 899 C CZ2 . TRP A 138 ? 2.0017 1.6616 1.9940 0.2230 0.4642 0.3071 138 TRP A CZ2 900 C CZ3 . TRP A 138 ? 2.0425 1.7664 2.0478 0.2171 0.4248 0.3221 138 TRP A CZ3 901 C CH2 . TRP A 138 ? 2.1208 1.8111 2.1299 0.2255 0.4533 0.3098 138 TRP A CH2 902 N N . GLN A 139 ? 1.9496 1.6314 1.7104 0.1741 0.3634 0.3678 139 GLN A N 903 C CA . GLN A 139 ? 1.9665 1.6444 1.6690 0.1622 0.3384 0.3611 139 GLN A CA 904 C C . GLN A 139 ? 1.8841 1.5542 1.5667 0.1557 0.3465 0.3250 139 GLN A C 905 O O . GLN A 139 ? 1.6996 1.3712 1.4142 0.1593 0.3700 0.3066 139 GLN A O 906 C CB . GLN A 139 ? 1.9974 1.6542 1.6348 0.1593 0.3329 0.3787 139 GLN A CB 907 C CG . GLN A 139 ? 2.2019 1.8395 1.8275 0.1655 0.3684 0.3796 139 GLN A CG 908 C CD . GLN A 139 ? 2.4879 2.1258 2.1343 0.1735 0.3711 0.4149 139 GLN A CD 909 O OE1 . GLN A 139 ? 2.7176 2.3538 2.4112 0.1812 0.3955 0.4188 139 GLN A OE1 910 N NE2 . GLN A 139 ? 2.5971 2.2341 2.2067 0.1708 0.3437 0.4419 139 GLN A NE2 911 N N . VAL A 140 ? 1.8916 1.5506 1.5204 0.1454 0.3248 0.3161 140 VAL A N 912 C CA . VAL A 140 ? 2.0351 1.6870 1.6498 0.1398 0.3266 0.2852 140 VAL A CA 913 C C . VAL A 140 ? 2.2247 1.8413 1.7559 0.1344 0.3259 0.2718 140 VAL A C 914 O O . VAL A 140 ? 2.4523 2.0559 1.9468 0.1236 0.3000 0.2622 140 VAL A O 915 C CB . VAL A 140 ? 1.9914 1.6648 1.6399 0.1322 0.2985 0.2831 140 VAL A CB 916 C CG1 . VAL A 140 ? 1.8052 1.5058 1.5298 0.1408 0.3125 0.2843 140 VAL A CG1 917 C CG2 . VAL A 140 ? 2.0551 1.7361 1.6907 0.1229 0.2597 0.3091 140 VAL A CG2 918 N N . LEU A 141 ? 2.2852 1.8833 1.7866 0.1419 0.3564 0.2711 141 LEU A N 919 C CA . LEU A 141 ? 2.4482 2.0069 1.8616 0.1412 0.3642 0.2626 141 LEU A CA 920 C C . LEU A 141 ? 2.4928 2.0295 1.8729 0.1384 0.3648 0.2324 141 LEU A C 921 O O . LEU A 141 ? 2.3390 1.8950 1.7721 0.1387 0.3671 0.2169 141 LEU A O 922 C CB . LEU A 141 ? 2.3612 1.9111 1.7653 0.1522 0.4050 0.2699 141 LEU A CB 923 C CG . LEU A 141 ? 2.3193 1.8847 1.7548 0.1549 0.4057 0.3008 141 LEU A CG 924 C CD1 . LEU A 141 ? 2.0630 1.6575 1.5879 0.1593 0.4223 0.3011 141 LEU A CD1 925 C CD2 . LEU A 141 ? 2.6064 2.1466 1.9841 0.1604 0.4299 0.3162 141 LEU A CD2 926 N N . LYS A 142 ? 2.4846 1.9764 1.7726 0.1362 0.3636 0.2243 142 LYS A N 927 C CA . LYS A 142 ? 2.4250 1.8850 1.6727 0.1353 0.3667 0.1952 142 LYS A CA 928 C C . LYS A 142 ? 2.3418 1.8252 1.6555 0.1481 0.4026 0.1827 142 LYS A C 929 O O . LYS A 142 ? 2.3271 1.8110 1.6612 0.1470 0.3993 0.1635 142 LYS A O 930 C CB . LYS A 142 ? 2.5820 1.9812 1.7158 0.1379 0.3781 0.1863 142 LYS A CB 931 C CG . LYS A 142 ? 2.7684 2.1210 1.8397 0.1291 0.3594 0.1593 142 LYS A CG 932 C CD . LYS A 142 ? 2.9469 2.2444 1.9424 0.1445 0.4005 0.1378 142 LYS A CD 933 C CE . LYS A 142 ? 3.0535 2.3073 2.0101 0.1386 0.3873 0.1081 142 LYS A CE 934 N NZ . LYS A 142 ? 2.6182 1.9121 1.6695 0.1371 0.3803 0.0993 142 LYS A NZ 935 N N . GLU A 143 ? 2.4259 1.9303 1.7767 0.1581 0.4333 0.1968 143 GLU A N 936 C CA . GLU A 143 ? 2.4049 1.9378 1.8275 0.1668 0.4628 0.1916 143 GLU A CA 937 C C . GLU A 143 ? 1.9870 1.5565 1.4878 0.1601 0.4430 0.1868 143 GLU A C 938 O O . GLU A 143 ? 1.7176 1.2927 1.2431 0.1614 0.4461 0.1699 143 GLU A O 939 C CB . GLU A 143 ? 2.6961 2.2393 2.1366 0.1747 0.4960 0.2116 143 GLU A CB 940 C CG . GLU A 143 ? 3.1031 2.6804 2.6269 0.1781 0.5198 0.2134 143 GLU A CG 941 C CD . GLU A 143 ? 3.3378 2.9147 2.8726 0.1881 0.5495 0.2009 143 GLU A CD 942 O OE1 . GLU A 143 ? 3.5358 3.0812 3.0115 0.1956 0.5574 0.1875 143 GLU A OE1 943 O OE2 . GLU A 143 ? 3.1779 2.7851 2.7828 0.1882 0.5646 0.2054 143 GLU A OE2 944 N N . ASN A 144 ? 1.8887 1.4798 1.4244 0.1544 0.4241 0.2024 144 ASN A N 945 C CA . ASN A 144 ? 1.8751 1.4969 1.4813 0.1513 0.4147 0.1994 144 ASN A CA 946 C C . ASN A 144 ? 1.8944 1.5178 1.5045 0.1454 0.3936 0.1828 144 ASN A C 947 O O . ASN A 144 ? 1.6962 1.3416 1.3582 0.1443 0.3911 0.1772 144 ASN A O 948 C CB . ASN A 144 ? 1.9580 1.5962 1.5945 0.1497 0.4012 0.2207 144 ASN A CB 949 C CG . ASN A 144 ? 2.0023 1.6450 1.6664 0.1549 0.4252 0.2345 144 ASN A CG 950 O OD1 . ASN A 144 ? 1.9881 1.6423 1.6988 0.1554 0.4392 0.2281 144 ASN A OD1 951 N ND2 . ASN A 144 ? 1.9941 1.6254 1.6279 0.1570 0.4272 0.2551 144 ASN A ND2 952 N N . GLY A 145 ? 1.9563 1.5514 1.5061 0.1410 0.3793 0.1749 145 GLY A N 953 C CA . GLY A 145 ? 2.0106 1.5996 1.5535 0.1315 0.3527 0.1630 145 GLY A CA 954 C C . GLY A 145 ? 2.0590 1.6367 1.6037 0.1349 0.3642 0.1408 145 GLY A C 955 O O . GLY A 145 ? 2.1743 1.7461 1.7179 0.1460 0.3942 0.1340 145 GLY A O 956 N N . PRO A 146 ? 2.1173 1.6930 1.6680 0.1254 0.3403 0.1325 146 PRO A N 957 C CA . PRO A 146 ? 1.9890 1.5623 1.5595 0.1279 0.3471 0.1159 146 PRO A CA 958 C C . PRO A 146 ? 1.9923 1.5192 1.5041 0.1336 0.3598 0.0981 146 PRO A C 959 O O . PRO A 146 ? 1.9289 1.4151 1.3732 0.1266 0.3452 0.0928 146 PRO A O 960 C CB . PRO A 146 ? 1.9736 1.5584 1.5665 0.1137 0.3146 0.1189 146 PRO A CB 961 C CG . PRO A 146 ? 2.1763 1.7618 1.7493 0.1025 0.2879 0.1353 146 PRO A CG 962 C CD . PRO A 146 ? 2.3007 1.8698 1.8300 0.1097 0.3026 0.1405 146 PRO A CD 963 N N . MET A 147 ? 2.0670 1.5979 1.6037 0.1464 0.3865 0.0897 147 MET A N 964 C CA . MET A 147 ? 2.2591 1.7478 1.7468 0.1588 0.4104 0.0761 147 MET A CA 965 C C . MET A 147 ? 2.2757 1.7177 1.7149 0.1516 0.3918 0.0595 147 MET A C 966 O O . MET A 147 ? 2.1193 1.5718 1.5833 0.1376 0.3627 0.0594 147 MET A O 967 C CB . MET A 147 ? 2.3677 1.8784 1.9063 0.1752 0.4430 0.0764 147 MET A CB 968 C CG . MET A 147 ? 2.5434 2.0222 2.0409 0.1938 0.4808 0.0722 147 MET A CG 969 S SD . MET A 147 ? 2.6665 2.1328 2.1103 0.1940 0.4919 0.0838 147 MET A SD 970 C CE . MET A 147 ? 2.4876 2.0195 2.0221 0.1936 0.5018 0.1050 147 MET A CE 971 N N . ALA A 148 ? 2.4389 1.8256 1.8065 0.1615 0.4110 0.0462 148 ALA A N 972 C CA . ALA A 148 ? 2.3810 1.7076 1.6905 0.1573 0.4003 0.0266 148 ALA A CA 973 C C . ALA A 148 ? 2.1425 1.4906 1.5107 0.1477 0.3782 0.0252 148 ALA A C 974 O O . ALA A 148 ? 2.0923 1.4379 1.4567 0.1263 0.3401 0.0266 148 ALA A O 975 C CB . ALA A 148 ? 2.3844 1.6620 1.6464 0.1815 0.4440 0.0128 148 ALA A CB 976 N N . SER A 149 ? 1.9705 1.3456 1.3991 0.1624 0.4002 0.0267 149 SER A N 977 C CA . SER A 149 ? 1.9574 1.3399 1.4255 0.1549 0.3820 0.0246 149 SER A CA 978 C C . SER A 149 ? 1.9545 1.4051 1.5080 0.1502 0.3729 0.0406 149 SER A C 979 O O . SER A 149 ? 2.0224 1.4869 1.6185 0.1527 0.3723 0.0417 149 SER A O 980 C CB . SER A 149 ? 2.0902 1.4292 1.5428 0.1719 0.4053 0.0108 149 SER A CB 981 O OG . SER A 149 ? 2.2372 1.5732 1.6877 0.1973 0.4483 0.0112 149 SER A OG 982 N N . ASP A 150 ? 1.9782 1.4672 1.5527 0.1436 0.3655 0.0534 150 ASP A N 983 C CA . ASP A 150 ? 2.1391 1.6790 1.7791 0.1366 0.3533 0.0657 150 ASP A CA 984 C C . ASP A 150 ? 2.2029 1.7499 1.8426 0.1173 0.3203 0.0734 150 ASP A C 985 O O . ASP A 150 ? 2.1033 1.6169 1.6931 0.1071 0.3029 0.0695 150 ASP A O 986 C CB . ASP A 150 ? 2.2784 1.8612 1.9629 0.1452 0.3723 0.0761 150 ASP A CB 987 C CG . ASP A 150 ? 2.3067 1.8910 1.9687 0.1463 0.3797 0.0826 150 ASP A CG 988 O OD1 . ASP A 150 ? 2.4670 2.0280 2.0832 0.1385 0.3650 0.0825 150 ASP A OD1 989 O OD2 . ASP A 150 ? 2.0152 1.6244 1.7072 0.1533 0.3983 0.0897 150 ASP A OD2 990 N N . PRO A 151 ? 2.2932 1.8816 1.9872 0.1120 0.3116 0.0852 151 PRO A N 991 C CA . PRO A 151 ? 2.1178 1.7302 1.8345 0.0983 0.2883 0.0999 151 PRO A CA 992 C C . PRO A 151 ? 1.9688 1.5681 1.6514 0.0869 0.2671 0.1064 151 PRO A C 993 O O . PRO A 151 ? 1.9518 1.5244 1.5863 0.0909 0.2735 0.0997 151 PRO A O 994 C CB . PRO A 151 ? 2.1764 1.8297 1.9368 0.1065 0.3037 0.1099 151 PRO A CB 995 C CG . PRO A 151 ? 2.3744 2.0284 2.1456 0.1187 0.3262 0.1004 151 PRO A CG 996 C CD . PRO A 151 ? 2.3530 1.9708 2.0933 0.1215 0.3281 0.0873 151 PRO A CD 997 N N . LEU A 152 ? 1.9133 1.5329 1.6218 0.0726 0.2418 0.1222 152 LEU A N 998 C CA . LEU A 152 ? 1.9574 1.5734 1.6437 0.0601 0.2164 0.1344 152 LEU A CA 999 C C . LEU A 152 ? 1.9481 1.5993 1.6617 0.0688 0.2253 0.1520 152 LEU A C 1000 O O . LEU A 152 ? 1.8488 1.4913 1.5316 0.0651 0.2137 0.1600 152 LEU A O 1001 C CB . LEU A 152 ? 2.0075 1.6315 1.7156 0.0389 0.1819 0.1480 152 LEU A CB 1002 C CG . LEU A 152 ? 2.1041 1.6887 1.7507 0.0207 0.1498 0.1460 152 LEU A CG 1003 C CD1 . LEU A 152 ? 2.2451 1.8122 1.8935 -0.0032 0.1169 0.1471 152 LEU A CD1 1004 C CD2 . LEU A 152 ? 2.1209 1.7297 1.7718 0.0166 0.1334 0.1688 152 LEU A CD2 1005 N N . CYS A 153 ? 2.0590 1.7452 1.8263 0.0797 0.2450 0.1584 153 CYS A N 1006 C CA . CYS A 153 ? 1.9785 1.6880 1.7694 0.0927 0.2640 0.1688 153 CYS A CA 1007 C C . CYS A 153 ? 1.7967 1.5108 1.6033 0.1058 0.2935 0.1568 153 CYS A C 1008 O O . CYS A 153 ? 1.7667 1.4915 1.5993 0.1068 0.2991 0.1532 153 CYS A O 1009 C CB . CYS A 153 ? 2.0833 1.8295 1.9259 0.0917 0.2556 0.1938 153 CYS A CB 1010 S SG . CYS A 153 ? 2.6846 2.4323 2.5154 0.0749 0.2165 0.2149 153 CYS A SG 1011 N N . LEU A 154 ? 1.7498 1.4557 1.5401 0.1144 0.3110 0.1526 154 LEU A N 1012 C CA . LEU A 154 ? 1.7763 1.4870 1.5833 0.1230 0.3340 0.1435 154 LEU A CA 1013 C C . LEU A 154 ? 1.7430 1.4756 1.5883 0.1269 0.3405 0.1543 154 LEU A C 1014 O O . LEU A 154 ? 1.5835 1.3257 1.4402 0.1286 0.3365 0.1705 154 LEU A O 1015 C CB . LEU A 154 ? 1.9608 1.6578 1.7447 0.1291 0.3506 0.1395 154 LEU A CB 1016 C CG . LEU A 154 ? 1.9908 1.6591 1.7265 0.1284 0.3490 0.1301 154 LEU A CG 1017 C CD1 . LEU A 154 ? 1.9458 1.6021 1.6541 0.1345 0.3649 0.1340 154 LEU A CD1 1018 C CD2 . LEU A 154 ? 2.0354 1.6949 1.7729 0.1316 0.3572 0.1151 154 LEU A CD2 1019 N N . THR A 155 ? 1.7199 1.4578 1.5830 0.1290 0.3505 0.1464 155 THR A N 1020 C CA . THR A 155 ? 1.7186 1.4666 1.6063 0.1340 0.3612 0.1524 155 THR A CA 1021 C C . THR A 155 ? 1.8331 1.5711 1.7179 0.1380 0.3772 0.1476 155 THR A C 1022 O O . THR A 155 ? 1.9901 1.7215 1.8684 0.1356 0.3821 0.1363 155 THR A O 1023 C CB . THR A 155 ? 1.6541 1.4080 1.5535 0.1326 0.3621 0.1478 155 THR A CB 1024 O OG1 . THR A 155 ? 1.6075 1.3763 1.5245 0.1307 0.3524 0.1616 155 THR A OG1 1025 C CG2 . THR A 155 ? 1.6479 1.3972 1.5529 0.1378 0.3786 0.1447 155 THR A CG2 1026 N N . TYR A 156 ? 1.8186 1.5562 1.7125 0.1438 0.3842 0.1593 156 TYR A N 1027 C CA . TYR A 156 ? 1.7057 1.4293 1.6007 0.1469 0.3996 0.1575 156 TYR A CA 1028 C C . TYR A 156 ? 1.6299 1.3501 1.5409 0.1555 0.4104 0.1655 156 TYR A C 1029 O O . TYR A 156 ? 1.7212 1.4511 1.6426 0.1584 0.4099 0.1683 156 TYR A O 1030 C CB . TYR A 156 ? 1.7997 1.5184 1.6857 0.1482 0.4010 0.1671 156 TYR A CB 1031 C CG . TYR A 156 ? 1.8657 1.5822 1.7289 0.1437 0.3969 0.1621 156 TYR A CG 1032 C CD1 . TYR A 156 ? 1.9028 1.6170 1.7643 0.1398 0.4027 0.1488 156 TYR A CD1 1033 C CD2 . TYR A 156 ? 1.8919 1.6065 1.7338 0.1442 0.3886 0.1726 156 TYR A CD2 1034 C CE1 . TYR A 156 ? 1.8176 1.5276 1.6597 0.1400 0.4056 0.1461 156 TYR A CE1 1035 C CE2 . TYR A 156 ? 1.8899 1.5942 1.7011 0.1425 0.3898 0.1671 156 TYR A CE2 1036 C CZ . TYR A 156 ? 1.8706 1.5725 1.6832 0.1420 0.4011 0.1539 156 TYR A CZ 1037 O OH . TYR A 156 ? 2.0143 1.7037 1.7963 0.1442 0.4080 0.1502 156 TYR A OH 1038 N N . SER A 157 ? 1.5968 1.3013 1.5105 0.1608 0.4229 0.1708 157 SER A N 1039 C CA . SER A 157 ? 1.6972 1.3908 1.6242 0.1728 0.4385 0.1788 157 SER A CA 1040 C C . SER A 157 ? 1.8728 1.5389 1.7972 0.1762 0.4523 0.1809 157 SER A C 1041 O O . SER A 157 ? 1.8771 1.5354 1.7915 0.1670 0.4494 0.1759 157 SER A O 1042 C CB . SER A 157 ? 1.6106 1.2943 1.5305 0.1740 0.4474 0.1660 157 SER A CB 1043 O OG . SER A 157 ? 1.6308 1.2804 1.5287 0.1689 0.4567 0.1489 157 SER A OG 1044 N N . TYR A 158 ? 1.9946 1.6455 1.9309 0.1904 0.4692 0.1906 158 TYR A N 1045 C CA . TYR A 158 ? 1.8044 1.4245 1.7412 0.1960 0.4836 0.1960 158 TYR A CA 1046 C C . TYR A 158 ? 1.7308 1.3090 1.6536 0.2025 0.5047 0.1826 158 TYR A C 1047 O O . TYR A 158 ? 1.7520 1.3300 1.6677 0.2071 0.5110 0.1747 158 TYR A O 1048 C CB . TYR A 158 ? 1.7621 1.3980 1.7264 0.2105 0.4849 0.2258 158 TYR A CB 1049 C CG . TYR A 158 ? 1.7177 1.3747 1.7126 0.2276 0.4915 0.2440 158 TYR A CG 1050 C CD1 . TYR A 158 ? 1.7835 1.4142 1.7849 0.2446 0.5189 0.2434 158 TYR A CD1 1051 C CD2 . TYR A 158 ? 1.6322 1.3336 1.6500 0.2266 0.4711 0.2636 158 TYR A CD2 1052 C CE1 . TYR A 158 ? 1.8303 1.4845 1.8676 0.2627 0.5297 0.2645 158 TYR A CE1 1053 C CE2 . TYR A 158 ? 1.6740 1.4010 1.7308 0.2405 0.4761 0.2853 158 TYR A CE2 1054 C CZ . TYR A 158 ? 1.8068 1.5132 1.8771 0.2600 0.5074 0.2873 158 TYR A CZ 1055 O OH . TYR A 158 ? 1.9118 1.6471 2.0281 0.2766 0.5176 0.3126 158 TYR A OH 1056 N N . LEU A 159 ? 1.7014 1.2396 1.6161 0.2026 0.5166 0.1802 159 LEU A N 1057 C CA . LEU A 159 ? 1.8557 1.3402 1.7447 0.2062 0.5359 0.1634 159 LEU A CA 1058 C C . LEU A 159 ? 1.9840 1.4226 1.8708 0.2087 0.5492 0.1669 159 LEU A C 1059 O O . LEU A 159 ? 2.0355 1.4868 1.9408 0.2048 0.5422 0.1822 159 LEU A O 1060 C CB . LEU A 159 ? 1.8448 1.3139 1.6995 0.1848 0.5234 0.1359 159 LEU A CB 1061 C CG . LEU A 159 ? 1.7545 1.2340 1.6115 0.1616 0.5031 0.1311 159 LEU A CG 1062 C CD1 . LEU A 159 ? 1.7147 1.1397 1.5503 0.1467 0.5054 0.1171 159 LEU A CD1 1063 C CD2 . LEU A 159 ? 1.7765 1.2895 1.6286 0.1492 0.4839 0.1209 159 LEU A CD2 1064 N N . SER A 160 ? 2.0555 1.4352 1.9140 0.2148 0.5695 0.1520 160 SER A N 1065 C CA . SER A 160 ? 2.0351 1.3567 1.8833 0.2138 0.5820 0.1499 160 SER A CA 1066 C C . SER A 160 ? 2.0556 1.3514 1.8790 0.1819 0.5629 0.1294 160 SER A C 1067 O O . SER A 160 ? 1.9434 1.2193 1.7313 0.1657 0.5533 0.1050 160 SER A O 1068 C CB . SER A 160 ? 2.1410 1.4013 1.9639 0.2348 0.6138 0.1417 160 SER A CB 1069 O OG . SER A 160 ? 2.3795 1.5838 2.1997 0.2380 0.6277 0.1451 160 SER A OG 1070 N N . HIS A 161 ? 2.1522 1.4511 1.9978 0.1726 0.5568 0.1431 161 HIS A N 1071 C CA . HIS A 161 ? 2.3026 1.5895 2.1421 0.1421 0.5388 0.1327 161 HIS A CA 1072 C C . HIS A 161 ? 2.5675 1.7863 2.3984 0.1357 0.5498 0.1319 161 HIS A C 1073 O O . HIS A 161 ? 2.5942 1.8181 2.4507 0.1261 0.5467 0.1487 161 HIS A O 1074 C CB . HIS A 161 ? 2.2352 1.5855 2.1090 0.1346 0.5241 0.1512 161 HIS A CB 1075 C CG . HIS A 161 ? 2.2958 1.6540 2.1734 0.1051 0.5053 0.1430 161 HIS A CG 1076 N ND1 . HIS A 161 ? 2.4966 1.8182 2.3794 0.0858 0.5039 0.1443 161 HIS A ND1 1077 C CD2 . HIS A 161 ? 2.3008 1.7014 2.1844 0.0917 0.4873 0.1366 161 HIS A CD2 1078 C CE1 . HIS A 161 ? 2.5672 1.9132 2.4633 0.0611 0.4853 0.1406 161 HIS A CE1 1079 N NE2 . HIS A 161 ? 2.4294 1.8233 2.3263 0.0658 0.4759 0.1361 161 HIS A NE2 1080 N N . VAL A 162 ? 2.6144 1.7649 2.4052 0.1417 0.5647 0.1123 162 VAL A N 1081 C CA . VAL A 162 ? 2.4209 1.4889 2.1901 0.1333 0.5747 0.1043 162 VAL A CA 1082 C C . VAL A 162 ? 2.4220 1.4163 2.1310 0.1101 0.5662 0.0697 162 VAL A C 1083 O O . VAL A 162 ? 2.6557 1.5868 2.3500 0.0913 0.5634 0.0626 162 VAL A O 1084 C CB . VAL A 162 ? 2.3359 1.3656 2.1124 0.1670 0.6084 0.1198 162 VAL A CB 1085 C CG1 . VAL A 162 ? 2.3975 1.4216 2.2093 0.1623 0.6093 0.1443 162 VAL A CG1 1086 C CG2 . VAL A 162 ? 2.1440 1.2296 1.9462 0.2009 0.6229 0.1380 162 VAL A CG2 1087 N N . ASP A 163 ? 2.3300 1.3277 2.0016 0.1103 0.5612 0.0495 163 ASP A N 1088 C CA . ASP A 163 ? 2.5084 1.4440 2.1157 0.0830 0.5444 0.0170 163 ASP A CA 1089 C C . ASP A 163 ? 2.4673 1.4579 2.0652 0.0774 0.5257 0.0094 163 ASP A C 1090 O O . ASP A 163 ? 2.5117 1.4621 2.0521 0.0596 0.5115 -0.0152 163 ASP A O 1091 C CB . ASP A 163 ? 2.9397 1.7717 2.4788 0.0991 0.5741 -0.0048 163 ASP A CB 1092 C CG . ASP A 163 ? 3.2612 2.0051 2.7197 0.0641 0.5529 -0.0405 163 ASP A CG 1093 O OD1 . ASP A 163 ? 3.2351 2.0058 2.6856 0.0310 0.5147 -0.0494 163 ASP A OD1 1094 O OD2 . ASP A 163 ? 3.3666 2.0086 2.7657 0.0706 0.5748 -0.0596 163 ASP A OD2 1095 N N . LEU A 164 ? 2.4186 1.4975 2.0701 0.0914 0.5241 0.0313 164 LEU A N 1096 C CA . LEU A 164 ? 2.3459 1.4825 1.9979 0.0906 0.5096 0.0289 164 LEU A CA 1097 C C . LEU A 164 ? 2.6000 1.6909 2.1849 0.0932 0.5153 0.0051 164 LEU A C 1098 O O . LEU A 164 ? 2.9290 2.0281 2.5058 0.1214 0.5399 0.0084 164 LEU A O 1099 C CB . LEU A 164 ? 2.0266 1.2094 1.7053 0.0596 0.4740 0.0313 164 LEU A CB 1100 C CG . LEU A 164 ? 1.8382 1.1029 1.5792 0.0685 0.4713 0.0561 164 LEU A CG 1101 C CD1 . LEU A 164 ? 1.9015 1.1900 1.6715 0.0383 0.4452 0.0607 164 LEU A CD1 1102 C CD2 . LEU A 164 ? 1.7551 1.0722 1.4999 0.0827 0.4697 0.0581 164 LEU A CD2 1103 N N . VAL A 165 ? 2.5698 1.6134 2.1066 0.0625 0.4914 -0.0168 165 VAL A N 1104 C CA . VAL A 165 ? 2.6799 1.6645 2.1359 0.0602 0.4941 -0.0420 165 VAL A CA 1105 C C . VAL A 165 ? 2.8649 1.7851 2.2779 0.0942 0.5402 -0.0495 165 VAL A C 1106 O O . VAL A 165 ? 3.1070 2.0218 2.4833 0.1133 0.5594 -0.0552 165 VAL A O 1107 C CB . VAL A 165 ? 2.6300 1.5542 2.0367 0.0189 0.4602 -0.0635 165 VAL A CB 1108 C CG1 . VAL A 165 ? 2.7299 1.6190 2.0568 0.0085 0.4476 -0.0855 165 VAL A CG1 1109 C CG2 . VAL A 165 ? 2.4434 1.4332 1.9172 -0.0102 0.4229 -0.0473 165 VAL A CG2 1110 N N . LYS A 166 ? 2.7657 1.6381 2.1864 0.1034 0.5604 -0.0468 166 LYS A N 1111 C CA . LYS A 166 ? 2.8304 1.6487 2.2264 0.1411 0.6086 -0.0477 166 LYS A CA 1112 C C . LYS A 166 ? 2.8252 1.7257 2.2824 0.1770 0.6318 -0.0194 166 LYS A C 1113 O O . LYS A 166 ? 3.0629 1.9506 2.4928 0.2034 0.6623 -0.0215 166 LYS A O 1114 C CB . LYS A 166 ? 2.8944 1.6566 2.3030 0.1436 0.6223 -0.0439 166 LYS A CB 1115 C CG . LYS A 166 ? 2.7631 1.4446 2.1373 0.1795 0.6725 -0.0485 166 LYS A CG 1116 C CD . LYS A 166 ? 2.5533 1.2002 1.9622 0.1820 0.6814 -0.0358 166 LYS A CD 1117 C CE . LYS A 166 ? 2.6330 1.1670 1.9825 0.2073 0.7253 -0.0516 166 LYS A CE 1118 N NZ . LYS A 166 ? 2.7128 1.1734 1.9583 0.1983 0.7284 -0.0889 166 LYS A NZ 1119 N N . ASP A 167 ? 2.6988 1.6827 2.2355 0.1755 0.6156 0.0071 167 ASP A N 1120 C CA . ASP A 167 ? 2.6167 1.6736 2.2187 0.2066 0.6332 0.0379 167 ASP A CA 1121 C C . ASP A 167 ? 2.5382 1.6646 2.1544 0.2102 0.6243 0.0443 167 ASP A C 1122 O O . ASP A 167 ? 2.4207 1.5718 2.0575 0.2391 0.6501 0.0600 167 ASP A O 1123 C CB . ASP A 167 ? 2.5630 1.6700 2.2327 0.2029 0.6192 0.0634 167 ASP A CB 1124 C CG . ASP A 167 ? 2.7657 1.8088 2.4315 0.2023 0.6308 0.0638 167 ASP A CG 1125 O OD1 . ASP A 167 ? 2.8104 1.7961 2.4593 0.2282 0.6657 0.0638 167 ASP A OD1 1126 O OD2 . ASP A 167 ? 2.8022 1.8523 2.4850 0.1767 0.6068 0.0660 167 ASP A OD2 1127 N N . LEU A 168 ? 2.5951 1.7549 2.2072 0.1812 0.5882 0.0354 168 LEU A N 1128 C CA . LEU A 168 ? 2.4778 1.6959 2.0987 0.1812 0.5769 0.0396 168 LEU A CA 1129 C C . LEU A 168 ? 2.4205 1.5950 1.9846 0.1960 0.6026 0.0266 168 LEU A C 1130 O O . LEU A 168 ? 2.2805 1.4855 1.8670 0.2217 0.6263 0.0428 168 LEU A O 1131 C CB . LEU A 168 ? 2.4627 1.7080 2.0798 0.1480 0.5363 0.0299 168 LEU A CB 1132 C CG . LEU A 168 ? 2.5942 1.8890 2.2652 0.1317 0.5110 0.0428 168 LEU A CG 1133 C CD1 . LEU A 168 ? 2.6788 2.0003 2.3473 0.1039 0.4767 0.0349 168 LEU A CD1 1134 C CD2 . LEU A 168 ? 2.4261 1.7846 2.1559 0.1507 0.5175 0.0688 168 LEU A CD2 1135 N N . ASN A 169 ? 2.4286 1.5281 1.9179 0.1791 0.5983 -0.0013 169 ASN A N 1136 C CA . ASN A 169 ? 2.4766 1.5216 1.8892 0.1870 0.6185 -0.0192 169 ASN A CA 1137 C C . ASN A 169 ? 2.4818 1.5004 1.8914 0.2275 0.6714 -0.0099 169 ASN A C 1138 O O . ASN A 169 ? 2.5428 1.5543 1.9191 0.2435 0.6948 -0.0108 169 ASN A O 1139 C CB . ASN A 169 ? 2.5627 1.5183 1.8884 0.1594 0.6023 -0.0517 169 ASN A CB 1140 C CG . ASN A 169 ? 2.6328 1.6170 1.9509 0.1206 0.5510 -0.0594 169 ASN A CG 1141 O OD1 . ASN A 169 ? 2.5828 1.5229 1.8259 0.1034 0.5370 -0.0792 169 ASN A OD1 1142 N ND2 . ASN A 169 ? 2.6891 1.7463 2.0838 0.1074 0.5234 -0.0422 169 ASN A ND2 1143 N N . SER A 170 ? 2.4913 1.4974 1.9396 0.2450 0.6914 0.0023 170 SER A N 1144 C CA . SER A 170 ? 2.5743 1.5626 2.0372 0.2871 0.7434 0.0179 170 SER A CA 1145 C C . SER A 170 ? 2.5500 1.6360 2.0976 0.3088 0.7512 0.0542 170 SER A C 1146 O O . SER A 170 ? 2.5352 1.6217 2.0917 0.3414 0.7925 0.0687 170 SER A O 1147 C CB . SER A 170 ? 2.5850 1.5229 2.0616 0.2989 0.7612 0.0209 170 SER A CB 1148 O OG . SER A 170 ? 2.5900 1.4179 1.9775 0.2866 0.7674 -0.0131 170 SER A OG 1149 N N . GLY A 171 ? 2.4663 1.6318 2.0751 0.2907 0.7127 0.0697 171 GLY A N 1150 C CA . GLY A 171 ? 2.4031 1.6582 2.0827 0.3025 0.7099 0.1006 171 GLY A CA 1151 C C . GLY A 171 ? 2.2421 1.5643 2.0021 0.3019 0.6891 0.1285 171 GLY A C 1152 O O . GLY A 171 ? 2.0525 1.4310 1.8750 0.3209 0.6981 0.1598 171 GLY A O 1153 N N . LEU A 172 ? 2.1265 1.4440 1.8847 0.2786 0.6599 0.1194 172 LEU A N 1154 C CA . LEU A 172 ? 2.0834 1.4508 1.9036 0.2791 0.6439 0.1447 172 LEU A CA 1155 C C . LEU A 172 ? 2.0083 1.4318 1.8439 0.2533 0.6038 0.1441 172 LEU A C 1156 O O . LEU A 172 ? 2.0293 1.4431 1.8511 0.2310 0.5821 0.1316 172 LEU A O 1157 C CB . LEU A 172 ? 2.0912 1.4099 1.9081 0.2809 0.6518 0.1441 172 LEU A CB 1158 C CG . LEU A 172 ? 2.0546 1.3132 1.8619 0.3112 0.6953 0.1480 172 LEU A CG 1159 C CD1 . LEU A 172 ? 2.0768 1.2525 1.8352 0.2985 0.6983 0.1241 172 LEU A CD1 1160 C CD2 . LEU A 172 ? 1.8955 1.1917 1.7729 0.3410 0.7126 0.1878 172 LEU A CD2 1161 N N . ILE A 173 ? 1.9765 1.4563 1.8416 0.2570 0.5964 0.1586 173 ILE A N 1162 C CA . ILE A 173 ? 1.8974 1.4304 1.7814 0.2377 0.5620 0.1618 173 ILE A CA 1163 C C . ILE A 173 ? 1.8714 1.4637 1.8042 0.2474 0.5569 0.1888 173 ILE A C 1164 O O . ILE A 173 ? 1.8289 1.4337 1.7672 0.2564 0.5692 0.1940 173 ILE A O 1165 C CB . ILE A 173 ? 1.8337 1.3586 1.6774 0.2153 0.5438 0.1363 173 ILE A CB 1166 C CG1 . ILE A 173 ? 1.8531 1.4267 1.7181 0.1988 0.5126 0.1404 173 ILE A CG1 1167 C CG2 . ILE A 173 ? 1.7105 1.2263 1.5296 0.2224 0.5586 0.1300 173 ILE A CG2 1168 C CD1 . ILE A 173 ? 1.9909 1.5540 1.8291 0.1759 0.4926 0.1197 173 ILE A CD1 1169 N N . GLY A 174 ? 1.8373 1.4637 1.8038 0.2443 0.5381 0.2074 174 GLY A N 1170 C CA . GLY A 174 ? 1.7583 1.4395 1.7683 0.2465 0.5234 0.2328 174 GLY A CA 1171 C C . GLY A 174 ? 1.6976 1.4031 1.6962 0.2240 0.4908 0.2234 174 GLY A C 1172 O O . GLY A 174 ? 1.6162 1.3035 1.5856 0.2105 0.4811 0.2049 174 GLY A O 1173 N N . ALA A 175 ? 1.7410 1.4860 1.7646 0.2201 0.4752 0.2373 175 ALA A N 1174 C CA . ALA A 175 ? 1.7751 1.5363 1.7847 0.2005 0.4466 0.2277 175 ALA A CA 1175 C C . ALA A 175 ? 1.8507 1.6269 1.8673 0.1944 0.4245 0.2417 175 ALA A C 1176 O O . ALA A 175 ? 1.9746 1.7758 2.0254 0.2001 0.4171 0.2687 175 ALA A O 1177 C CB . ALA A 175 ? 1.6877 1.4758 1.7151 0.1965 0.4393 0.2346 175 ALA A CB 1178 N N . LEU A 176 ? 1.7245 1.4857 1.7087 0.1832 0.4144 0.2257 176 LEU A N 1179 C CA . LEU A 176 ? 1.6108 1.3790 1.5881 0.1777 0.3961 0.2371 176 LEU A CA 1180 C C . LEU A 176 ? 1.5655 1.3394 1.5189 0.1625 0.3733 0.2270 176 LEU A C 1181 O O . LEU A 176 ? 1.5606 1.3202 1.4887 0.1561 0.3759 0.2053 176 LEU A O 1182 C CB . LEU A 176 ? 1.6303 1.3736 1.5890 0.1798 0.4075 0.2324 176 LEU A CB 1183 C CG . LEU A 176 ? 1.6706 1.4096 1.6013 0.1715 0.3947 0.2336 176 LEU A CG 1184 C CD1 . LEU A 176 ? 1.5925 1.3479 1.5267 0.1713 0.3745 0.2589 176 LEU A CD1 1185 C CD2 . LEU A 176 ? 1.8340 1.5485 1.7556 0.1741 0.4127 0.2299 176 LEU A CD2 1186 N N . LEU A 177 ? 1.4733 1.2663 1.4354 0.1566 0.3501 0.2442 177 LEU A N 1187 C CA . LEU A 177 ? 1.4879 1.2776 1.4218 0.1418 0.3278 0.2339 177 LEU A CA 1188 C C . LEU A 177 ? 1.5896 1.3680 1.4874 0.1346 0.3095 0.2392 177 LEU A C 1189 O O . LEU A 177 ? 1.5045 1.2959 1.4148 0.1344 0.2946 0.2636 177 LEU A O 1190 C CB . LEU A 177 ? 1.3978 1.2105 1.3610 0.1349 0.3116 0.2449 177 LEU A CB 1191 C CG . LEU A 177 ? 1.3525 1.1712 1.3381 0.1408 0.3307 0.2371 177 LEU A CG 1192 C CD1 . LEU A 177 ? 1.3546 1.1943 1.3653 0.1306 0.3130 0.2483 177 LEU A CD1 1193 C CD2 . LEU A 177 ? 1.3978 1.1924 1.3505 0.1394 0.3427 0.2084 177 LEU A CD2 1194 N N . VAL A 178 ? 1.6780 1.4317 1.5306 0.1296 0.3116 0.2183 178 VAL A N 1195 C CA . VAL A 178 ? 1.7492 1.4826 1.5513 0.1230 0.2978 0.2190 178 VAL A CA 1196 C C . VAL A 178 ? 1.6971 1.4132 1.4627 0.1096 0.2766 0.2060 178 VAL A C 1197 O O . VAL A 178 ? 1.6898 1.4002 1.4577 0.1086 0.2834 0.1881 178 VAL A O 1198 C CB . VAL A 178 ? 1.8231 1.5357 1.5959 0.1301 0.3218 0.2084 178 VAL A CB 1199 C CG1 . VAL A 178 ? 1.8313 1.5292 1.5873 0.1297 0.3349 0.1834 178 VAL A CG1 1200 C CG2 . VAL A 178 ? 1.8706 1.5655 1.5951 0.1272 0.3119 0.2190 178 VAL A CG2 1201 N N . CYS A 179 ? 1.6565 1.3594 1.3841 0.0987 0.2502 0.2151 179 CYS A N 1202 C CA . CYS A 179 ? 1.8093 1.4999 1.5164 0.0817 0.2202 0.2104 179 CYS A CA 1203 C C . CYS A 179 ? 1.9217 1.5722 1.5523 0.0694 0.1981 0.2053 179 CYS A C 1204 O O . CYS A 179 ? 2.1483 1.7969 1.7559 0.0685 0.1882 0.2216 179 CYS A O 1205 C CB . CYS A 179 ? 1.9803 1.7093 1.7450 0.0739 0.1962 0.2372 179 CYS A CB 1206 S SG . CYS A 179 ? 2.4056 2.1699 2.2453 0.0882 0.2251 0.2382 179 CYS A SG 1207 N N . ARG A 180 ? 1.8959 1.5108 1.4836 0.0596 0.1890 0.1839 180 ARG A N 1208 C CA . ARG A 180 ? 2.1099 1.6743 1.6109 0.0468 0.1677 0.1753 180 ARG A CA 1209 C C . ARG A 180 ? 2.2729 1.8476 1.7705 0.0257 0.1201 0.2011 180 ARG A C 1210 O O . ARG A 180 ? 2.3961 2.0222 1.9686 0.0243 0.1082 0.2276 180 ARG A O 1211 C CB . ARG A 180 ? 2.2857 1.8048 1.7449 0.0408 0.1676 0.1472 180 ARG A CB 1212 C CG . ARG A 180 ? 2.6758 2.1301 2.0358 0.0451 0.1808 0.1255 180 ARG A CG 1213 C CD . ARG A 180 ? 2.8280 2.2302 2.1456 0.0411 0.1820 0.0979 180 ARG A CD 1214 N NE . ARG A 180 ? 2.8673 2.2804 2.2258 0.0612 0.2209 0.0844 180 ARG A NE 1215 C CZ . ARG A 180 ? 2.7874 2.2328 2.2154 0.0602 0.2197 0.0861 180 ARG A CZ 1216 N NH1 . ARG A 180 ? 2.8128 2.2856 2.2832 0.0417 0.1862 0.1012 180 ARG A NH1 1217 N NH2 . ARG A 180 ? 2.7912 2.2435 2.2484 0.0779 0.2525 0.0755 180 ARG A NH2 1218 N N . GLU A 181 ? 2.3869 1.9112 1.7970 0.0100 0.0937 0.1944 181 GLU A N 1219 C CA . GLU A 181 ? 2.4346 1.9605 1.8266 -0.0147 0.0407 0.2186 181 GLU A CA 1220 C C . GLU A 181 ? 2.5482 2.1135 2.0110 -0.0367 -0.0008 0.2406 181 GLU A C 1221 O O . GLU A 181 ? 2.5525 2.1401 2.0294 -0.0533 -0.0416 0.2709 181 GLU A O 1222 C CB . GLU A 181 ? 2.4708 1.9197 1.7400 -0.0306 0.0198 0.1986 181 GLU A CB 1223 C CG . GLU A 181 ? 2.7529 2.1796 1.9530 -0.0218 0.0290 0.2057 181 GLU A CG 1224 C CD . GLU A 181 ? 2.8692 2.3019 2.0783 0.0102 0.0898 0.1953 181 GLU A CD 1225 O OE1 . GLU A 181 ? 2.7635 2.2260 2.0425 0.0250 0.1208 0.1861 181 GLU A OE1 1226 O OE2 . GLU A 181 ? 3.0527 2.4594 2.1974 0.0190 0.1052 0.1980 181 GLU A OE2 1227 N N . GLY A 182 ? 2.6639 2.2379 2.1714 -0.0377 0.0083 0.2282 182 GLY A N 1228 C CA . GLY A 182 ? 2.4034 2.0186 1.9870 -0.0569 -0.0241 0.2510 182 GLY A CA 1229 C C . GLY A 182 ? 2.2551 1.9400 1.9452 -0.0359 0.0056 0.2721 182 GLY A C 1230 O O . GLY A 182 ? 1.8625 1.5495 1.5672 -0.0135 0.0497 0.2538 182 GLY A O 1231 N N . SER A 183 ? 2.4515 2.1909 2.2139 -0.0433 -0.0191 0.3116 183 SER A N 1232 C CA . SER A 183 ? 2.5325 2.3346 2.3904 -0.0203 0.0106 0.3365 183 SER A CA 1233 C C . SER A 183 ? 2.7258 2.5889 2.6738 -0.0316 -0.0199 0.3833 183 SER A C 1234 O O . SER A 183 ? 2.5689 2.4329 2.5053 -0.0563 -0.0692 0.4041 183 SER A O 1235 C CB . SER A 183 ? 2.3472 2.1481 2.1878 0.0050 0.0420 0.3363 183 SER A CB 1236 O OG . SER A 183 ? 2.0327 1.8846 1.9572 0.0264 0.0681 0.3608 183 SER A OG 1237 N N . LEU A 184 ? 3.1980 3.1108 3.2343 -0.0125 0.0111 0.4008 184 LEU A N 1238 C CA . LEU A 184 ? 3.4673 3.4463 3.6079 -0.0162 -0.0041 0.4482 184 LEU A CA 1239 C C . LEU A 184 ? 3.8229 3.8353 3.9952 -0.0135 -0.0262 0.4887 184 LEU A C 1240 O O . LEU A 184 ? 4.3690 4.4380 4.6289 -0.0193 -0.0466 0.5335 184 LEU A O 1241 C CB . LEU A 184 ? 2.9091 2.9225 3.1217 0.0098 0.0464 0.4523 184 LEU A CB 1242 C CG . LEU A 184 ? 2.4540 2.5268 2.7717 0.0124 0.0546 0.4882 184 LEU A CG 1243 C CD1 . LEU A 184 ? 2.3866 2.4693 2.7271 -0.0227 0.0115 0.5004 184 LEU A CD1 1244 C CD2 . LEU A 184 ? 2.0500 2.1239 2.3854 0.0405 0.1129 0.4719 184 LEU A CD2 1245 N N . ALA A 185 ? 3.6904 3.6695 3.7953 -0.0046 -0.0219 0.4761 185 ALA A N 1246 C CA . ALA A 185 ? 3.5311 3.5321 3.6492 -0.0038 -0.0469 0.5129 185 ALA A CA 1247 C C . ALA A 185 ? 3.6087 3.5619 3.6265 -0.0305 -0.0937 0.5029 185 ALA A C 1248 O O . ALA A 185 ? 3.5061 3.4667 3.5133 -0.0315 -0.1166 0.5297 185 ALA A O 1249 C CB . ALA A 185 ? 3.2126 3.2190 3.3457 0.0324 0.0010 0.5159 185 ALA A CB 1250 N N . LYS A 186 ? 3.7154 3.6155 3.6562 -0.0505 -0.1052 0.4642 186 LYS A N 1251 C CA . LYS A 186 ? 3.8662 3.7086 3.7006 -0.0798 -0.1506 0.4489 186 LYS A CA 1252 C C . LYS A 186 ? 3.8661 3.6597 3.6505 -0.0968 -0.1526 0.4085 186 LYS A C 1253 O O . LYS A 186 ? 3.9455 3.6976 3.6779 -0.0800 -0.1110 0.3685 186 LYS A O 1254 C CB . LYS A 186 ? 3.7342 3.5309 3.4760 -0.0650 -0.1315 0.4313 186 LYS A CB 1255 C CG . LYS A 186 ? 3.3930 3.1963 3.1110 -0.0754 -0.1723 0.4666 186 LYS A CG 1256 C CD . LYS A 186 ? 3.1851 2.9293 2.7903 -0.0659 -0.1549 0.4441 186 LYS A CD 1257 C CE . LYS A 186 ? 3.1010 2.8603 2.7386 -0.0276 -0.0921 0.4397 186 LYS A CE 1258 N NZ . LYS A 186 ? 3.1344 2.8331 2.6692 -0.0165 -0.0599 0.4066 186 LYS A NZ 1259 N N . GLU A 187 ? 3.6974 3.4973 3.5033 -0.1302 -0.2013 0.4218 187 GLU A N 1260 C CA . GLU A 187 ? 3.4451 3.2072 3.2276 -0.1479 -0.2058 0.3918 187 GLU A CA 1261 C C . GLU A 187 ? 3.2863 3.1137 3.1904 -0.1398 -0.1859 0.4131 187 GLU A C 1262 O O . GLU A 187 ? 3.1669 2.9936 3.0869 -0.1163 -0.1362 0.3908 187 GLU A O 1263 C CB . GLU A 187 ? 3.3572 3.0491 3.0447 -0.1308 -0.1637 0.3386 187 GLU A CB 1264 C CG . GLU A 187 ? 3.4030 3.0361 3.0391 -0.1507 -0.1746 0.3053 187 GLU A CG 1265 C CD . GLU A 187 ? 3.3416 3.0046 3.0544 -0.1393 -0.1423 0.3007 187 GLU A CD 1266 O OE1 . GLU A 187 ? 3.2583 2.9553 3.0165 -0.1067 -0.0919 0.2992 187 GLU A OE1 1267 O OE2 . GLU A 187 ? 3.2470 2.8958 2.9710 -0.1645 -0.1687 0.2989 187 GLU A OE2 1268 N N . LYS A 188 ? 3.2616 3.1461 3.2512 -0.1600 -0.2257 0.4592 188 LYS A N 1269 C CA . LYS A 188 ? 3.1669 3.1266 3.2855 -0.1486 -0.2045 0.4925 188 LYS A CA 1270 C C . LYS A 188 ? 3.2616 3.2116 3.4013 -0.1561 -0.1896 0.4743 188 LYS A C 1271 O O . LYS A 188 ? 3.0198 3.0167 3.2406 -0.1340 -0.1485 0.4876 188 LYS A O 1272 C CB . LYS A 188 ? 3.0313 3.0588 3.2427 -0.1689 -0.2528 0.5525 188 LYS A CB 1273 C CG . LYS A 188 ? 2.8282 2.8772 3.0383 -0.1606 -0.2700 0.5813 188 LYS A CG 1274 C CD . LYS A 188 ? 2.6576 2.7693 2.9594 -0.1180 -0.2192 0.6105 188 LYS A CD 1275 C CE . LYS A 188 ? 2.5805 2.7709 3.0212 -0.1137 -0.2097 0.6549 188 LYS A CE 1276 N NZ . LYS A 188 ? 2.4067 2.5897 2.8626 -0.1006 -0.1618 0.6279 188 LYS A NZ 1277 N N . THR A 189 ? 3.4461 3.3309 3.5082 -0.1858 -0.2208 0.4443 189 THR A N 1278 C CA . THR A 189 ? 3.2285 3.0962 3.3056 -0.1989 -0.2159 0.4296 189 THR A CA 1279 C C . THR A 189 ? 3.4819 3.3192 3.5264 -0.1681 -0.1561 0.3894 189 THR A C 1280 O O . THR A 189 ? 3.3580 3.1752 3.4066 -0.1769 -0.1505 0.3758 189 THR A O 1281 C CB . THR A 189 ? 2.8806 2.6842 2.8911 -0.2447 -0.2744 0.4146 189 THR A CB 1282 O OG1 . THR A 189 ? 2.3954 2.1873 2.4325 -0.2543 -0.2654 0.4051 189 THR A OG1 1283 C CG2 . THR A 189 ? 2.8021 2.5133 2.6700 -0.2446 -0.2770 0.3668 189 THR A CG2 1284 N N . GLN A 190 ? 3.6169 3.4498 3.6300 -0.1342 -0.1145 0.3725 190 GLN A N 1285 C CA . GLN A 190 ? 3.3499 3.1770 3.3615 -0.1031 -0.0573 0.3470 190 GLN A CA 1286 C C . GLN A 190 ? 3.2620 3.1518 3.3793 -0.0986 -0.0414 0.3782 190 GLN A C 1287 O O . GLN A 190 ? 2.9936 2.9449 3.1881 -0.0878 -0.0345 0.4151 190 GLN A O 1288 C CB . GLN A 190 ? 3.0287 2.8554 3.0125 -0.0702 -0.0185 0.3346 190 GLN A CB 1289 C CG . GLN A 190 ? 3.0915 2.9835 3.1570 -0.0471 0.0059 0.3677 190 GLN A CG 1290 C CD . GLN A 190 ? 3.0896 3.0047 3.2008 -0.0215 0.0563 0.3630 190 GLN A CD 1291 O OE1 . GLN A 190 ? 3.0065 2.8870 3.0720 -0.0088 0.0850 0.3292 190 GLN A OE1 1292 N NE2 . GLN A 190 ? 2.9665 2.9397 3.1673 -0.0135 0.0674 0.3989 190 GLN A NE2 1293 N N . THR A 191 ? 3.1279 2.9994 3.2476 -0.1079 -0.0373 0.3659 191 THR A N 1294 C CA . THR A 191 ? 2.8248 2.7482 3.0363 -0.1086 -0.0254 0.3960 191 THR A CA 1295 C C . THR A 191 ? 2.9675 2.8785 3.1709 -0.0853 0.0232 0.3729 191 THR A C 1296 O O . THR A 191 ? 3.0836 3.0182 3.3399 -0.0890 0.0333 0.3893 191 THR A O 1297 C CB . THR A 191 ? 2.5055 2.4319 2.7494 -0.1503 -0.0777 0.4188 191 THR A CB 1298 O OG1 . THR A 191 ? 2.2966 2.2830 2.6411 -0.1496 -0.0630 0.4556 191 THR A OG1 1299 C CG2 . THR A 191 ? 2.3682 2.2155 2.5302 -0.1725 -0.0989 0.3812 191 THR A CG2 1300 N N . LEU A 192 ? 2.8578 2.7342 2.9968 -0.0620 0.0522 0.3383 192 LEU A N 1301 C CA . LEU A 192 ? 2.6203 2.4828 2.7434 -0.0395 0.0949 0.3153 192 LEU A CA 1302 C C . LEU A 192 ? 2.5801 2.4934 2.7654 -0.0155 0.1347 0.3363 192 LEU A C 1303 O O . LEU A 192 ? 2.4996 2.4507 2.7239 -0.0041 0.1425 0.3588 192 LEU A O 1304 C CB . LEU A 192 ? 2.5329 2.3470 2.5759 -0.0239 0.1114 0.2760 192 LEU A CB 1305 C CG . LEU A 192 ? 2.7472 2.5543 2.7534 -0.0109 0.1166 0.2673 192 LEU A CG 1306 C CD1 . LEU A 192 ? 2.6630 2.4435 2.6232 0.0123 0.1517 0.2367 192 LEU A CD1 1307 C CD2 . LEU A 192 ? 2.9422 2.7162 2.8992 -0.0333 0.0755 0.2636 192 LEU A CD2 1308 N N . HIS A 193 ? 2.5492 2.4591 2.7393 -0.0071 0.1605 0.3293 193 HIS A N 1309 C CA . HIS A 193 ? 2.2358 2.1848 2.4738 0.0138 0.1990 0.3482 193 HIS A CA 1310 C C . HIS A 193 ? 2.0482 1.9810 2.2463 0.0414 0.2366 0.3235 193 HIS A C 1311 O O . HIS A 193 ? 2.0242 1.9281 2.1835 0.0456 0.2486 0.3000 193 HIS A O 1312 C CB . HIS A 193 ? 2.1342 2.0908 2.4017 0.0047 0.2038 0.3610 193 HIS A CB 1313 C CG . HIS A 193 ? 2.0684 2.0806 2.4167 0.0073 0.2168 0.4036 193 HIS A CG 1314 N ND1 . HIS A 193 ? 2.1231 2.1562 2.5230 -0.0136 0.2018 0.4313 193 HIS A ND1 1315 C CD2 . HIS A 193 ? 2.0479 2.0994 2.4388 0.0287 0.2444 0.4259 193 HIS A CD2 1316 C CE1 . HIS A 193 ? 2.3227 2.4106 2.7973 -0.0040 0.2220 0.4707 193 HIS A CE1 1317 N NE2 . HIS A 193 ? 2.2990 2.3974 2.7683 0.0230 0.2492 0.4676 193 HIS A NE2 1318 N N . LYS A 194 ? 1.7694 1.7201 1.9795 0.0590 0.2535 0.3308 194 LYS A N 1319 C CA . LYS A 194 ? 1.6841 1.6107 1.8486 0.0798 0.2808 0.3044 194 LYS A CA 1320 C C . LYS A 194 ? 1.6638 1.6060 1.8468 0.1052 0.3193 0.3132 194 LYS A C 1321 O O . LYS A 194 ? 1.7169 1.6852 1.9389 0.1138 0.3238 0.3363 194 LYS A O 1322 C CB . LYS A 194 ? 1.6512 1.5489 1.7675 0.0752 0.2620 0.2829 194 LYS A CB 1323 C CG . LYS A 194 ? 1.7139 1.6286 1.8472 0.0771 0.2509 0.3001 194 LYS A CG 1324 C CD . LYS A 194 ? 1.7208 1.6017 1.7963 0.0731 0.2362 0.2781 194 LYS A CD 1325 C CE . LYS A 194 ? 1.6646 1.5625 1.7553 0.0750 0.2244 0.2987 194 LYS A CE 1326 N NZ . LYS A 194 ? 1.6646 1.5349 1.7069 0.0562 0.1896 0.2894 194 LYS A NZ 1327 N N . PHE A 195 ? 1.6049 1.5260 1.7551 0.1170 0.3458 0.2938 195 PHE A N 1328 C CA . PHE A 195 ? 1.5846 1.5032 1.7321 0.1398 0.3832 0.2940 195 PHE A CA 1329 C C . PHE A 195 ? 1.5302 1.4135 1.6249 0.1465 0.3899 0.2637 195 PHE A C 1330 O O . PHE A 195 ? 1.5307 1.3938 1.5912 0.1357 0.3716 0.2424 195 PHE A O 1331 C CB . PHE A 195 ? 1.7134 1.6324 1.8603 0.1461 0.4083 0.2984 195 PHE A CB 1332 C CG . PHE A 195 ? 1.7938 1.7513 2.0009 0.1412 0.4083 0.3332 195 PHE A CG 1333 C CD1 . PHE A 195 ? 1.8562 1.8441 2.1143 0.1581 0.4347 0.3634 195 PHE A CD1 1334 C CD2 . PHE A 195 ? 1.7615 1.7249 1.9790 0.1202 0.3830 0.3382 195 PHE A CD2 1335 C CE1 . PHE A 195 ? 1.8931 1.9230 2.2174 0.1531 0.4356 0.4004 195 PHE A CE1 1336 C CE2 . PHE A 195 ? 1.8430 1.8435 2.1220 0.1126 0.3813 0.3731 195 PHE A CE2 1337 C CZ . PHE A 195 ? 1.9061 1.9432 2.2416 0.1286 0.4075 0.4056 195 PHE A CZ 1338 N N . ILE A 196 ? 1.5466 1.4210 1.6368 0.1648 0.4182 0.2633 196 ILE A N 1339 C CA . ILE A 196 ? 1.5671 1.4081 1.6138 0.1698 0.4252 0.2382 196 ILE A CA 1340 C C . ILE A 196 ? 1.5993 1.4123 1.6086 0.1779 0.4507 0.2224 196 ILE A C 1341 O O . ILE A 196 ? 1.5858 1.3902 1.5959 0.1944 0.4803 0.2289 196 ILE A O 1342 C CB . ILE A 196 ? 1.5736 1.4170 1.6382 0.1814 0.4322 0.2490 196 ILE A CB 1343 C CG1 . ILE A 196 ? 1.5368 1.4041 1.6271 0.1701 0.4009 0.2644 196 ILE A CG1 1344 C CG2 . ILE A 196 ? 1.4353 1.2411 1.4582 0.1865 0.4438 0.2253 196 ILE A CG2 1345 C CD1 . ILE A 196 ? 1.4165 1.3254 1.5672 0.1697 0.3925 0.2999 196 ILE A CD1 1346 N N . LEU A 197 ? 1.7418 1.5384 1.7162 0.1667 0.4390 0.2026 197 LEU A N 1347 C CA . LEU A 197 ? 1.8735 1.6416 1.8057 0.1706 0.4561 0.1881 197 LEU A CA 1348 C C . LEU A 197 ? 1.8548 1.5883 1.7500 0.1718 0.4609 0.1667 197 LEU A C 1349 O O . LEU A 197 ? 1.9571 1.6859 1.8435 0.1613 0.4420 0.1536 197 LEU A O 1350 C CB . LEU A 197 ? 1.8292 1.5980 1.7452 0.1585 0.4414 0.1827 197 LEU A CB 1351 C CG . LEU A 197 ? 1.8225 1.6059 1.7529 0.1632 0.4566 0.2023 197 LEU A CG 1352 C CD1 . LEU A 197 ? 1.7852 1.6043 1.7677 0.1557 0.4407 0.2239 197 LEU A CD1 1353 C CD2 . LEU A 197 ? 1.7335 1.4995 1.6242 0.1577 0.4559 0.1941 197 LEU A CD2 1354 N N . LEU A 198 ? 1.7572 1.4644 1.6316 0.1850 0.4882 0.1644 198 LEU A N 1355 C CA . LEU A 198 ? 1.7322 1.3982 1.5668 0.1839 0.4931 0.1438 198 LEU A CA 1356 C C . LEU A 198 ? 1.7915 1.4210 1.5690 0.1805 0.5008 0.1283 198 LEU A C 1357 O O . LEU A 198 ? 1.9571 1.5678 1.7138 0.1941 0.5288 0.1324 198 LEU A O 1358 C CB . LEU A 198 ? 1.6746 1.3256 1.5203 0.2015 0.5183 0.1509 198 LEU A CB 1359 C CG . LEU A 198 ? 1.6386 1.2470 1.4555 0.2002 0.5223 0.1336 198 LEU A CG 1360 C CD1 . LEU A 198 ? 1.7011 1.2801 1.5126 0.2227 0.5588 0.1396 198 LEU A CD1 1361 C CD2 . LEU A 198 ? 1.5954 1.1669 1.3585 0.1831 0.5096 0.1083 198 LEU A CD2 1362 N N . PHE A 199 ? 1.7347 1.3530 1.4858 0.1630 0.4770 0.1121 199 PHE A N 1363 C CA . PHE A 199 ? 1.9248 1.5075 1.6171 0.1557 0.4765 0.0983 199 PHE A CA 1364 C C . PHE A 199 ? 2.1220 1.6510 1.7672 0.1517 0.4819 0.0785 199 PHE A C 1365 O O . PHE A 199 ? 2.1124 1.6306 1.7453 0.1335 0.4575 0.0660 199 PHE A O 1366 C CB . PHE A 199 ? 1.8720 1.4742 1.5652 0.1383 0.4453 0.0963 199 PHE A CB 1367 C CG . PHE A 199 ? 1.8515 1.4912 1.5758 0.1412 0.4421 0.1137 199 PHE A CG 1368 C CD1 . PHE A 199 ? 1.8712 1.5482 1.6490 0.1418 0.4325 0.1246 199 PHE A CD1 1369 C CD2 . PHE A 199 ? 1.8955 1.5288 1.5909 0.1416 0.4476 0.1192 199 PHE A CD2 1370 C CE1 . PHE A 199 ? 1.8398 1.5447 1.6442 0.1413 0.4269 0.1397 199 PHE A CE1 1371 C CE2 . PHE A 199 ? 1.8797 1.5454 1.6067 0.1425 0.4442 0.1369 199 PHE A CE2 1372 C CZ . PHE A 199 ? 1.8116 1.5120 1.5943 0.1414 0.4329 0.1465 199 PHE A CZ 1373 N N . ALA A 200 ? 2.3061 1.7998 1.9265 0.1687 0.5148 0.0770 200 ALA A N 1374 C CA . ALA A 200 ? 2.3957 1.8308 1.9744 0.1678 0.5246 0.0588 200 ALA A CA 1375 C C . ALA A 200 ? 2.5594 1.9276 2.0494 0.1593 0.5278 0.0372 200 ALA A C 1376 O O . ALA A 200 ? 2.6231 1.9667 2.0706 0.1729 0.5541 0.0379 200 ALA A O 1377 C CB . ALA A 200 ? 2.2903 1.7178 1.8944 0.1930 0.5595 0.0694 200 ALA A CB 1378 N N . VAL A 201 ? 2.6123 1.9495 2.0731 0.1359 0.5007 0.0193 201 VAL A N 1379 C CA . VAL A 201 ? 2.5039 1.7659 1.8742 0.1239 0.4993 -0.0036 201 VAL A CA 1380 C C . VAL A 201 ? 2.4940 1.6932 1.8386 0.1334 0.5249 -0.0169 201 VAL A C 1381 O O . VAL A 201 ? 2.3959 1.5779 1.7497 0.1167 0.5060 -0.0257 201 VAL A O 1382 C CB . VAL A 201 ? 2.4684 1.7286 1.8200 0.0890 0.4506 -0.0136 201 VAL A CB 1383 C CG1 . VAL A 201 ? 2.3774 1.5850 1.6351 0.0779 0.4436 -0.0273 201 VAL A CG1 1384 C CG2 . VAL A 201 ? 2.1235 1.4640 1.5503 0.0808 0.4221 0.0047 201 VAL A CG2 1385 N N . PHE A 202 ? 2.5406 1.7068 1.8587 0.1619 0.5702 -0.0156 202 PHE A N 1386 C CA . PHE A 202 ? 2.7165 1.8149 2.0059 0.1757 0.6004 -0.0275 202 PHE A CA 1387 C C . PHE A 202 ? 3.0559 2.0526 2.2334 0.1629 0.6023 -0.0585 202 PHE A C 1388 O O . PHE A 202 ? 3.1879 2.1414 2.2934 0.1753 0.6282 -0.0661 202 PHE A O 1389 C CB . PHE A 202 ? 2.6589 1.7659 1.9761 0.2155 0.6525 -0.0094 202 PHE A CB 1390 C CG . PHE A 202 ? 2.5165 1.7036 1.9387 0.2274 0.6512 0.0190 202 PHE A CG 1391 C CD1 . PHE A 202 ? 2.4584 1.6583 1.9245 0.2165 0.6306 0.0205 202 PHE A CD1 1392 C CD2 . PHE A 202 ? 2.5481 1.7970 2.0233 0.2469 0.6679 0.0456 202 PHE A CD2 1393 C CE1 . PHE A 202 ? 2.4034 1.6730 1.9567 0.2262 0.6271 0.0466 202 PHE A CE1 1394 C CE2 . PHE A 202 ? 2.3672 1.6865 1.9338 0.2542 0.6610 0.0717 202 PHE A CE2 1395 C CZ . PHE A 202 ? 2.2834 1.6111 1.8845 0.2441 0.6404 0.0713 202 PHE A CZ 1396 N N . ASP A 203 ? 3.0961 2.0514 2.2561 0.1375 0.5755 -0.0756 203 ASP A N 1397 C CA . ASP A 203 ? 3.1120 1.9596 2.1630 0.1217 0.5737 -0.1071 203 ASP A CA 1398 C C . ASP A 203 ? 3.1275 1.9098 2.1560 0.1542 0.6274 -0.1128 203 ASP A C 1399 O O . ASP A 203 ? 3.3276 2.1330 2.4272 0.1666 0.6386 -0.0996 203 ASP A O 1400 C CB . ASP A 203 ? 3.1316 1.9623 2.1844 0.0804 0.5237 -0.1193 203 ASP A CB 1401 C CG . ASP A 203 ? 3.2334 1.9569 2.1673 0.0534 0.5064 -0.1518 203 ASP A CG 1402 O OD1 . ASP A 203 ? 3.2553 1.8928 2.0995 0.0723 0.5448 -0.1702 203 ASP A OD1 1403 O OD2 . ASP A 203 ? 3.2705 1.9948 2.2006 0.0125 0.4538 -0.1579 203 ASP A OD2 1404 N N . GLU A 204 ? 3.0547 1.7553 1.9848 0.1700 0.6628 -0.1305 204 GLU A N 1405 C CA . GLU A 204 ? 3.0230 1.6586 1.9320 0.2071 0.7218 -0.1341 204 GLU A CA 1406 C C . GLU A 204 ? 3.1931 1.7057 2.0113 0.1915 0.7207 -0.1682 204 GLU A C 1407 O O . GLU A 204 ? 3.1976 1.6523 2.0097 0.2187 0.7639 -0.1716 204 GLU A O 1408 C CB . GLU A 204 ? 2.9569 1.5804 1.8273 0.2445 0.7762 -0.1270 204 GLU A CB 1409 C CG . GLU A 204 ? 2.9839 1.6267 1.9237 0.2924 0.8349 -0.1026 204 GLU A CG 1410 C CD . GLU A 204 ? 2.8469 1.6036 1.9281 0.2961 0.8171 -0.0679 204 GLU A CD 1411 O OE1 . GLU A 204 ? 2.7493 1.5996 1.8907 0.2928 0.7995 -0.0453 204 GLU A OE1 1412 O OE2 . GLU A 204 ? 2.7628 1.5101 1.8895 0.3020 0.8207 -0.0633 204 GLU A OE2 1413 N N . GLY A 205 ? 3.2997 1.7738 2.0522 0.1464 0.6688 -0.1914 205 GLY A N 1414 C CA . GLY A 205 ? 3.4028 1.7696 2.0828 0.1194 0.6513 -0.2220 205 GLY A CA 1415 C C . GLY A 205 ? 3.2195 1.6311 1.9859 0.0887 0.6062 -0.2126 205 GLY A C 1416 O O . GLY A 205 ? 3.3484 1.7092 2.0709 0.0458 0.5613 -0.2320 205 GLY A O 1417 N N . LYS A 206 ? 2.9896 1.4962 1.8778 0.1096 0.6175 -0.1810 206 LYS A N 1418 C CA . LYS A 206 ? 2.8667 1.4232 1.8438 0.0873 0.5840 -0.1668 206 LYS A CA 1419 C C . LYS A 206 ? 2.7711 1.3895 1.8457 0.1269 0.6218 -0.1368 206 LYS A C 1420 O O . LYS A 206 ? 2.5536 1.2746 1.7237 0.1267 0.6050 -0.1100 206 LYS A O 1421 C CB . LYS A 206 ? 2.7884 1.4350 1.8153 0.0533 0.5280 -0.1546 206 LYS A CB 1422 C CG . LYS A 206 ? 2.8969 1.4905 1.8496 0.0055 0.4774 -0.1780 206 LYS A CG 1423 C CD . LYS A 206 ? 2.9017 1.5908 1.9212 -0.0249 0.4246 -0.1601 206 LYS A CD 1424 C CE . LYS A 206 ? 2.9895 1.6279 1.9460 -0.0750 0.3700 -0.1786 206 LYS A CE 1425 N NZ . LYS A 206 ? 3.0416 1.6243 2.0021 -0.1038 0.3512 -0.1876 206 LYS A NZ 1426 N N . SER A 207 ? 2.8881 1.4379 1.9339 0.1609 0.6731 -0.1414 207 SER A N 1427 C CA . SER A 207 ? 2.8845 1.4876 2.0051 0.2070 0.7179 -0.1116 207 SER A CA 1428 C C . SER A 207 ? 2.9277 1.4688 2.0605 0.2247 0.7471 -0.1099 207 SER A C 1429 O O . SER A 207 ? 2.6633 1.2298 1.8582 0.2115 0.7267 -0.0968 207 SER A O 1430 C CB . SER A 207 ? 2.9456 1.5268 2.0126 0.2399 0.7627 -0.1149 207 SER A CB 1431 O OG . SER A 207 ? 2.9074 1.5410 2.0474 0.2856 0.8084 -0.0833 207 SER A OG 1432 N N . TRP A 208 ? 3.1764 1.6368 2.2497 0.2586 0.8000 -0.1207 208 TRP A N 1433 C CA . TRP A 208 ? 3.3920 1.7432 2.4231 0.2713 0.8308 -0.1353 208 TRP A CA 1434 C C . TRP A 208 ? 3.5553 1.8017 2.4614 0.2850 0.8665 -0.1670 208 TRP A C 1435 O O . TRP A 208 ? 3.8271 1.9733 2.6819 0.3139 0.9156 -0.1791 208 TRP A O 1436 C CB . TRP A 208 ? 3.3733 1.7598 2.4963 0.3164 0.8734 -0.0998 208 TRP A CB 1437 C CG . TRP A 208 ? 3.2940 1.7819 2.4896 0.3519 0.8986 -0.0656 208 TRP A CG 1438 C CD1 . TRP A 208 ? 3.1119 1.7273 2.4095 0.3476 0.8708 -0.0325 208 TRP A CD1 1439 C CD2 . TRP A 208 ? 3.3563 1.8244 2.5287 0.3961 0.9570 -0.0598 208 TRP A CD2 1440 N NE1 . TRP A 208 ? 3.0250 1.7017 2.3667 0.3831 0.9037 -0.0063 208 TRP A NE1 1441 C CE2 . TRP A 208 ? 3.1516 1.7446 2.4234 0.4140 0.9579 -0.0203 208 TRP A CE2 1442 C CE3 . TRP A 208 ? 3.6669 2.0206 2.7425 0.4227 1.0105 -0.0836 208 TRP A CE3 1443 C CZ2 . TRP A 208 ? 3.2526 1.8680 2.5406 0.4558 1.0088 -0.0005 208 TRP A CZ2 1444 C CZ3 . TRP A 208 ? 3.8096 2.1838 2.8971 0.4684 1.0667 -0.0644 208 TRP A CZ3 1445 C CH2 . TRP A 208 ? 3.6440 2.1525 2.8425 0.4837 1.0645 -0.0214 208 TRP A CH2 1446 N N . HIS A 209 ? 3.4872 1.7570 2.3438 0.2657 0.8431 -0.1787 209 HIS A N 1447 C CA . HIS A 209 ? 3.8386 2.0029 2.5540 0.2645 0.8613 -0.2139 209 HIS A CA 1448 C C . HIS A 209 ? 4.1124 2.1452 2.7314 0.2300 0.8388 -0.2530 209 HIS A C 1449 O O . HIS A 209 ? 4.2070 2.2580 2.8428 0.1812 0.7766 -0.2588 209 HIS A O 1450 C CB . HIS A 209 ? 3.7848 2.0106 2.4755 0.2405 0.8252 -0.2150 209 HIS A CB 1451 C CG . HIS A 209 ? 3.8292 1.9598 2.3754 0.2427 0.8460 -0.2451 209 HIS A CG 1452 N ND1 . HIS A 209 ? 3.5887 1.7568 2.0957 0.2207 0.8146 -0.2475 209 HIS A ND1 1453 C CD2 . HIS A 209 ? 3.8865 1.8822 2.3127 0.2640 0.8950 -0.2737 209 HIS A CD2 1454 C CE1 . HIS A 209 ? 3.6450 1.7083 2.0132 0.2273 0.8417 -0.2752 209 HIS A CE1 1455 N NE2 . HIS A 209 ? 3.8429 1.7980 2.1565 0.2538 0.8918 -0.2929 209 HIS A NE2 1456 N N . SER A 210 ? 4.1789 2.0813 2.7046 0.2568 0.8915 -0.2768 210 SER A N 1457 C CA . SER A 210 ? 4.1921 1.9472 2.6125 0.2287 0.8789 -0.3167 210 SER A CA 1458 C C . SER A 210 ? 4.3751 1.9815 2.6485 0.2580 0.9383 -0.3505 210 SER A C 1459 O O . SER A 210 ? 4.3263 1.9211 2.5216 0.2664 0.9535 -0.3608 210 SER A O 1460 C CB . SER A 210 ? 4.0560 1.8034 2.5579 0.2313 0.8807 -0.3030 210 SER A CB 1461 O OG . SER A 210 ? 4.0436 1.7449 2.5590 0.2897 0.9554 -0.2923 210 SER A OG 1462 N N . PRO A 229 ? 4.0420 2.2046 2.2236 0.1528 0.7330 -0.2732 229 PRO A N 1463 C CA . PRO A 229 ? 3.6759 1.9528 2.0258 0.1751 0.7450 -0.2394 229 PRO A CA 1464 C C . PRO A 229 ? 3.2618 1.6819 1.7364 0.1542 0.6924 -0.2081 229 PRO A C 1465 O O . PRO A 229 ? 3.1142 1.5467 1.5940 0.1106 0.6286 -0.2155 229 PRO A O 1466 C CB . PRO A 229 ? 3.7063 1.9228 2.0657 0.1641 0.7369 -0.2578 229 PRO A CB 1467 C CG . PRO A 229 ? 3.8582 1.9115 2.0476 0.1572 0.7536 -0.3009 229 PRO A CG 1468 C CD . PRO A 229 ? 3.9689 1.9863 2.0410 0.1549 0.7579 -0.3104 229 PRO A CD 1469 N N . LYS A 230 ? 3.1278 1.6495 1.6982 0.1836 0.7184 -0.1735 230 LYS A N 1470 C CA . LYS A 230 ? 3.2496 1.9056 1.9553 0.1694 0.6755 -0.1430 230 LYS A CA 1471 C C . LYS A 230 ? 3.1519 1.9197 1.9464 0.1895 0.6875 -0.1061 230 LYS A C 1472 O O . LYS A 230 ? 3.2320 2.0231 1.9981 0.1748 0.6643 -0.1010 230 LYS A O 1473 C CB . LYS A 230 ? 3.1467 1.8099 1.8372 0.1184 0.6011 -0.1545 230 LYS A CB 1474 C CG . LYS A 230 ? 2.7947 1.5505 1.6119 0.1020 0.5619 -0.1362 230 LYS A CG 1475 C CD . LYS A 230 ? 2.7007 1.4849 1.5158 0.0585 0.4951 -0.1374 230 LYS A CD 1476 C CE . LYS A 230 ? 2.6771 1.5514 1.5440 0.0640 0.4852 -0.1115 230 LYS A CE 1477 N NZ . LYS A 230 ? 2.6574 1.5303 1.5028 0.1016 0.5400 -0.1016 230 LYS A NZ 1478 N N . MET A 231 ? 3.0179 1.8550 1.9218 0.2184 0.7164 -0.0792 231 MET A N 1479 C CA . MET A 231 ? 2.7823 1.7285 1.7842 0.2293 0.7159 -0.0441 231 MET A CA 1480 C C . MET A 231 ? 2.7611 1.7751 1.8180 0.1936 0.6508 -0.0394 231 MET A C 1481 O O . MET A 231 ? 2.5794 1.5585 1.6033 0.1640 0.6122 -0.0601 231 MET A O 1482 C CB . MET A 231 ? 2.7548 1.7545 1.8597 0.2652 0.7568 -0.0158 231 MET A CB 1483 C CG . MET A 231 ? 2.7735 1.7660 1.8738 0.3070 0.8237 0.0030 231 MET A CG 1484 S SD . MET A 231 ? 2.5628 1.6435 1.8044 0.3456 0.8631 0.0484 231 MET A SD 1485 C CE . MET A 231 ? 2.2633 1.3581 1.5708 0.3338 0.8307 0.0440 231 MET A CE 1486 N N . HIS A 232 ? 2.9453 2.0516 2.0859 0.1968 0.6404 -0.0116 232 HIS A N 1487 C CA . HIS A 232 ? 2.6527 1.8235 1.8374 0.1685 0.5864 -0.0035 232 HIS A CA 1488 C C . HIS A 232 ? 2.3124 1.5726 1.5854 0.1801 0.5892 0.0279 232 HIS A C 1489 O O . HIS A 232 ? 2.1312 1.4141 1.3928 0.1724 0.5757 0.0370 232 HIS A O 1490 C CB . HIS A 232 ? 2.8019 1.9299 1.8927 0.1460 0.5615 -0.0178 232 HIS A CB 1491 C CG . HIS A 232 ? 2.6743 1.8389 1.7893 0.1130 0.5027 -0.0176 232 HIS A CG 1492 N ND1 . HIS A 232 ? 2.6290 1.7458 1.6877 0.0829 0.4653 -0.0384 232 HIS A ND1 1493 C CD2 . HIS A 232 ? 2.5078 1.7489 1.6946 0.1058 0.4759 0.0024 232 HIS A CD2 1494 C CE1 . HIS A 232 ? 2.5331 1.7026 1.6370 0.0602 0.4192 -0.0283 232 HIS A CE1 1495 N NE2 . HIS A 232 ? 2.5769 1.8190 1.7557 0.0750 0.4267 -0.0048 232 HIS A NE2 1496 N N . THR A 233 ? 2.2609 1.5687 1.6200 0.1960 0.6026 0.0450 233 THR A N 1497 C CA . THR A 233 ? 2.2802 1.6517 1.7095 0.2151 0.6229 0.0757 233 THR A CA 1498 C C . THR A 233 ? 2.2709 1.7214 1.7869 0.2037 0.5897 0.0941 233 THR A C 1499 O O . THR A 233 ? 2.3003 1.7634 1.8218 0.1813 0.5501 0.0848 233 THR A O 1500 C CB . THR A 233 ? 2.2540 1.6248 1.7220 0.2457 0.6678 0.0893 233 THR A CB 1501 O OG1 . THR A 233 ? 2.0682 1.5064 1.6337 0.2474 0.6540 0.1103 233 THR A OG1 1502 C CG2 . THR A 233 ? 2.2968 1.5932 1.7118 0.2519 0.6853 0.0659 233 THR A CG2 1503 N N . VAL A 234 ? 2.1745 1.6748 1.7562 0.2197 0.6079 0.1212 234 VAL A N 1504 C CA . VAL A 234 ? 1.9182 1.4858 1.5831 0.2126 0.5828 0.1398 234 VAL A CA 1505 C C . VAL A 234 ? 1.7927 1.3891 1.5219 0.2333 0.6076 0.1625 234 VAL A C 1506 O O . VAL A 234 ? 1.6666 1.2913 1.4299 0.2466 0.6300 0.1873 234 VAL A O 1507 C CB . VAL A 234 ? 1.8819 1.4859 1.5628 0.2038 0.5692 0.1553 234 VAL A CB 1508 C CG1 . VAL A 234 ? 1.6532 1.3177 1.4169 0.2004 0.5522 0.1771 234 VAL A CG1 1509 C CG2 . VAL A 234 ? 1.8438 1.4309 1.4782 0.1823 0.5367 0.1381 234 VAL A CG2 1510 N N . ASN A 235 ? 1.8320 1.4228 1.5809 0.2357 0.6034 0.1570 235 ASN A N 1511 C CA . ASN A 235 ? 1.9629 1.5820 1.7751 0.2546 0.6221 0.1809 235 ASN A CA 1512 C C . ASN A 235 ? 2.1359 1.7145 1.9280 0.2820 0.6699 0.1833 235 ASN A C 1513 O O . ASN A 235 ? 2.1272 1.7313 1.9774 0.3020 0.6908 0.2085 235 ASN A O 1514 C CB . ASN A 235 ? 1.9368 1.6184 1.8162 0.2557 0.6180 0.2125 235 ASN A CB 1515 C CG . ASN A 235 ? 1.9515 1.6773 1.8851 0.2408 0.5804 0.2216 235 ASN A CG 1516 O OD1 . ASN A 235 ? 2.0425 1.8056 2.0378 0.2486 0.5817 0.2475 235 ASN A OD1 1517 N ND2 . ASN A 235 ? 1.9445 1.6647 1.8538 0.2197 0.5468 0.2015 235 ASN A ND2 1518 N N . GLY A 236 ? 2.2440 1.7571 1.9527 0.2830 0.6862 0.1578 236 GLY A N 1519 C CA . GLY A 236 ? 2.4092 1.8676 2.0803 0.3102 0.7362 0.1550 236 GLY A CA 1520 C C . GLY A 236 ? 2.6040 2.0521 2.2424 0.3251 0.7723 0.1641 236 GLY A C 1521 O O . GLY A 236 ? 2.7129 2.1040 2.3001 0.3485 0.8189 0.1581 236 GLY A O 1522 N N . TYR A 237 ? 2.5085 2.0076 2.1736 0.3120 0.7529 0.1791 237 TYR A N 1523 C CA . TYR A 237 ? 2.4102 1.9052 2.0457 0.3223 0.7832 0.1908 237 TYR A CA 1524 C C . TYR A 237 ? 2.4231 1.8800 1.9697 0.3004 0.7614 0.1665 237 TYR A C 1525 O O . TYR A 237 ? 2.1399 1.6207 1.6934 0.2732 0.7134 0.1588 237 TYR A O 1526 C CB . TYR A 237 ? 2.2050 1.7799 1.9321 0.3243 0.7819 0.2299 237 TYR A CB 1527 C CG . TYR A 237 ? 2.0734 1.6929 1.8933 0.3457 0.8031 0.2617 237 TYR A CG 1528 C CD1 . TYR A 237 ? 2.0907 1.7004 1.9229 0.3799 0.8621 0.2827 237 TYR A CD1 1529 C CD2 . TYR A 237 ? 2.0388 1.7112 1.9351 0.3323 0.7642 0.2735 237 TYR A CD2 1530 C CE1 . TYR A 237 ? 2.0343 1.6927 1.9633 0.3998 0.8790 0.3176 237 TYR A CE1 1531 C CE2 . TYR A 237 ? 1.9812 1.6987 1.9651 0.3491 0.7771 0.3065 237 TYR A CE2 1532 C CZ . TYR A 237 ? 1.9693 1.6829 1.9742 0.3826 0.8330 0.3299 237 TYR A CZ 1533 O OH . TYR A 237 ? 1.9656 1.7301 2.0669 0.3987 0.8419 0.3668 237 TYR A OH 1534 N N . VAL A 238 ? 2.5178 1.9138 1.9799 0.3145 0.7998 0.1567 238 VAL A N 1535 C CA . VAL A 238 ? 2.4639 1.8038 1.8212 0.2954 0.7817 0.1296 238 VAL A CA 1536 C C . VAL A 238 ? 2.4818 1.8401 1.8231 0.2985 0.7972 0.1499 238 VAL A C 1537 O O . VAL A 238 ? 2.3925 1.7966 1.7986 0.3185 0.8303 0.1827 238 VAL A O 1538 C CB . VAL A 238 ? 2.5484 1.7902 1.8016 0.3071 0.8126 0.1002 238 VAL A CB 1539 C CG1 . VAL A 238 ? 2.5478 1.7447 1.7390 0.2747 0.7628 0.0652 238 VAL A CG1 1540 C CG2 . VAL A 238 ? 2.3813 1.6121 1.6768 0.3380 0.8559 0.1074 238 VAL A CG2 1541 N N . ASN A 239 ? 2.5792 1.9043 1.8388 0.2777 0.7720 0.1338 239 ASN A N 1542 C CA . ASN A 239 ? 2.8040 2.1356 2.0313 0.2797 0.7871 0.1523 239 ASN A CA 1543 C C . ASN A 239 ? 2.8886 2.3083 2.2206 0.2771 0.7773 0.1894 239 ASN A C 1544 O O . ASN A 239 ? 3.3335 2.7733 2.6607 0.2560 0.7421 0.1939 239 ASN A O 1545 C CB . ASN A 239 ? 2.9806 2.2461 2.1207 0.3076 0.8507 0.1506 239 ASN A CB 1546 C CG . ASN A 239 ? 3.2682 2.4404 2.2655 0.2935 0.8388 0.1144 239 ASN A CG 1547 O OD1 . ASN A 239 ? 3.2404 2.4121 2.2182 0.2617 0.7808 0.0979 239 ASN A OD1 1548 N ND2 . ASN A 239 ? 3.5650 2.6565 2.4608 0.3157 0.8916 0.1024 239 ASN A ND2 1549 N N . ARG A 240 ? 2.5798 2.0491 2.0049 0.2970 0.8064 0.2170 240 ARG A N 1550 C CA . ARG A 240 ? 2.2023 1.7561 1.7433 0.2874 0.7814 0.2465 240 ARG A CA 1551 C C . ARG A 240 ? 2.0829 1.6822 1.7123 0.3120 0.8222 0.2815 240 ARG A C 1552 O O . ARG A 240 ? 2.0858 1.7344 1.7732 0.3130 0.8317 0.3155 240 ARG A O 1553 C CB . ARG A 240 ? 2.1781 1.7596 1.7216 0.2676 0.7546 0.2608 240 ARG A CB 1554 C CG . ARG A 240 ? 2.4738 2.0275 1.9499 0.2776 0.7912 0.2739 240 ARG A CG 1555 C CD . ARG A 240 ? 2.5918 2.1890 2.1035 0.2617 0.7707 0.3005 240 ARG A CD 1556 N NE . ARG A 240 ? 2.4757 2.0591 1.9447 0.2351 0.7184 0.2824 240 ARG A NE 1557 C CZ . ARG A 240 ? 2.5889 2.1223 1.9558 0.2289 0.7148 0.2702 240 ARG A CZ 1558 N NH1 . ARG A 240 ? 2.8237 2.3077 2.1072 0.2472 0.7621 0.2699 240 ARG A NH1 1559 N NH2 . ARG A 240 ? 2.4614 1.9924 1.8074 0.2050 0.6641 0.2592 240 ARG A NH2 1560 N N . SER A 241 ? 2.0651 1.6485 1.7085 0.3316 0.8458 0.2756 241 SER A N 1561 C CA . SER A 241 ? 2.0069 1.6481 1.7594 0.3500 0.8678 0.3107 241 SER A CA 1562 C C . SER A 241 ? 1.9505 1.6446 1.7816 0.3266 0.8110 0.3126 241 SER A C 1563 O O . SER A 241 ? 2.0238 1.7211 1.8362 0.2986 0.7634 0.2961 241 SER A O 1564 C CB . SER A 241 ? 2.1169 1.7168 1.8526 0.3830 0.9178 0.3064 241 SER A CB 1565 O OG . SER A 241 ? 2.2861 1.8148 1.9363 0.3767 0.9037 0.2627 241 SER A OG 1566 N N . LEU A 242 ? 1.8223 1.5556 1.7375 0.3383 0.8158 0.3333 242 LEU A N 1567 C CA . LEU A 242 ? 1.8828 1.6637 1.8671 0.3168 0.7638 0.3375 242 LEU A CA 1568 C C . LEU A 242 ? 1.9976 1.8472 2.0671 0.3064 0.7517 0.3764 242 LEU A C 1569 O O . LEU A 242 ? 2.3919 2.2466 2.4437 0.2872 0.7316 0.3747 242 LEU A O 1570 C CB . LEU A 242 ? 1.8284 1.5848 1.7575 0.2873 0.7131 0.3014 242 LEU A CB 1571 C CG . LEU A 242 ? 1.7459 1.5020 1.6828 0.2711 0.6700 0.2804 242 LEU A CG 1572 C CD1 . LEU A 242 ? 1.6640 1.4061 1.5564 0.2443 0.6284 0.2549 242 LEU A CD1 1573 C CD2 . LEU A 242 ? 1.6026 1.4145 1.6302 0.2679 0.6497 0.3056 242 LEU A CD2 1574 N N . PRO A 243 ? 1.9843 1.8872 2.1493 0.3172 0.7608 0.4135 243 PRO A N 1575 C CA . PRO A 243 ? 2.0568 2.0238 2.3049 0.3050 0.7502 0.4539 243 PRO A CA 1576 C C . PRO A 243 ? 2.0078 2.0031 2.2868 0.2696 0.6847 0.4493 243 PRO A C 1577 O O . PRO A 243 ? 1.9750 1.9624 2.2243 0.2484 0.6610 0.4384 243 PRO A O 1578 C CB . PRO A 243 ? 2.0020 2.0149 2.3425 0.3296 0.7827 0.4968 243 PRO A CB 1579 C CG . PRO A 243 ? 2.0932 2.0770 2.4146 0.3428 0.7819 0.4759 243 PRO A CG 1580 C CD . PRO A 243 ? 1.9448 1.8571 2.1538 0.3338 0.7681 0.4218 243 PRO A CD 1581 N N . GLY A 244 ? 1.9428 1.9655 2.2750 0.2645 0.6572 0.4575 244 GLY A N 1582 C CA . GLY A 244 ? 1.7792 1.8246 2.1382 0.2326 0.5972 0.4549 244 GLY A CA 1583 C C . GLY A 244 ? 1.6350 1.6763 1.9727 0.2061 0.5689 0.4464 244 GLY A C 1584 O O . GLY A 244 ? 1.6382 1.7103 2.0204 0.1996 0.5747 0.4760 244 GLY A O 1585 N N . LEU A 245 ? 1.5983 1.6016 1.8718 0.1915 0.5393 0.4081 245 LEU A N 1586 C CA . LEU A 245 ? 1.5780 1.5665 1.8201 0.1703 0.5153 0.3951 245 LEU A CA 1587 C C . LEU A 245 ? 1.5736 1.5992 1.8754 0.1538 0.5052 0.4294 245 LEU A C 1588 O O . LEU A 245 ? 1.5137 1.5484 1.8244 0.1615 0.5358 0.4502 245 LEU A O 1589 C CB . LEU A 245 ? 1.4329 1.3729 1.5893 0.1793 0.5350 0.3651 245 LEU A CB 1590 C CG . LEU A 245 ? 1.3501 1.2502 1.4475 0.1863 0.5325 0.3286 245 LEU A CG 1591 C CD1 . LEU A 245 ? 1.2544 1.1465 1.3417 0.1679 0.4893 0.3060 245 LEU A CD1 1592 C CD2 . LEU A 245 ? 1.4022 1.3055 1.5187 0.2076 0.5591 0.3356 245 LEU A CD2 1593 N N . ILE A 246 ? 1.5502 1.5933 1.8895 0.1299 0.4610 0.4349 246 ILE A N 1594 C CA . ILE A 246 ? 1.5301 1.6023 1.9264 0.1063 0.4375 0.4635 246 ILE A CA 1595 C C . ILE A 246 ? 1.5445 1.5978 1.9253 0.0795 0.3849 0.4433 246 ILE A C 1596 O O . ILE A 246 ? 1.6497 1.6961 2.0183 0.0794 0.3666 0.4281 246 ILE A O 1597 C CB . ILE A 246 ? 1.5815 1.7114 2.0724 0.1075 0.4432 0.5098 246 ILE A CB 1598 C CG1 . ILE A 246 ? 1.6240 1.7642 2.1275 0.1240 0.4469 0.5084 246 ILE A CG1 1599 C CG2 . ILE A 246 ? 1.6017 1.7560 2.1255 0.1235 0.4909 0.5424 246 ILE A CG2 1600 C CD1 . ILE A 246 ? 1.4797 1.6369 2.0164 0.1019 0.3962 0.5141 246 ILE A CD1 1601 N N . GLY A 247 ? 1.5148 1.5554 1.8924 0.0580 0.3627 0.4433 247 GLY A N 1602 C CA . GLY A 247 ? 1.5018 1.5154 1.8597 0.0327 0.3151 0.4239 247 GLY A CA 1603 C C . GLY A 247 ? 1.4994 1.5274 1.9077 0.0057 0.2915 0.4516 247 GLY A C 1604 O O . GLY A 247 ? 1.5471 1.5994 1.9925 0.0086 0.3154 0.4800 247 GLY A O 1605 N N . CYS A 248 ? 1.5550 1.5657 1.9636 -0.0214 0.2458 0.4452 248 CYS A N 1606 C CA . CYS A 248 ? 1.7796 1.8025 2.2411 -0.0511 0.2203 0.4744 248 CYS A CA 1607 C C . CYS A 248 ? 1.7066 1.6817 2.1277 -0.0624 0.2121 0.4570 248 CYS A C 1608 O O . CYS A 248 ? 1.9053 1.8313 2.2576 -0.0574 0.2050 0.4186 248 CYS A O 1609 C CB . CYS A 248 ? 2.1589 2.1907 2.6511 -0.0791 0.1722 0.4851 248 CYS A CB 1610 S SG . CYS A 248 ? 2.6498 2.7405 3.1962 -0.0650 0.1784 0.5109 248 CYS A SG 1611 N N . HIS A 249 ? 1.5047 1.4949 1.9717 -0.0760 0.2152 0.4876 249 HIS A N 1612 C CA . HIS A 249 ? 1.5500 1.4992 1.9805 -0.0785 0.2192 0.4759 249 HIS A CA 1613 C C . HIS A 249 ? 1.6222 1.5057 1.9910 -0.0913 0.1854 0.4372 249 HIS A C 1614 O O . HIS A 249 ? 1.6395 1.4870 1.9496 -0.0742 0.1983 0.4081 249 HIS A O 1615 C CB . HIS A 249 ? 1.6992 1.6721 2.1933 -0.0964 0.2223 0.5186 249 HIS A CB 1616 C CG . HIS A 249 ? 1.7897 1.7164 2.2513 -0.1036 0.2193 0.5104 249 HIS A CG 1617 N ND1 . HIS A 249 ? 1.7604 1.6727 2.2583 -0.1353 0.1923 0.5310 249 HIS A ND1 1618 C CD2 . HIS A 249 ? 1.8050 1.6967 2.2043 -0.0837 0.2383 0.4862 249 HIS A CD2 1619 C CE1 . HIS A 249 ? 1.8598 1.7279 2.3178 -0.1322 0.1972 0.5193 249 HIS A CE1 1620 N NE2 . HIS A 249 ? 1.7840 1.6416 2.1838 -0.1008 0.2243 0.4934 249 HIS A NE2 1621 N N . ARG A 250 ? 1.7518 1.6176 2.1318 -0.1209 0.1427 0.4371 250 ARG A N 1622 C CA . ARG A 250 ? 1.9708 1.7646 2.2898 -0.1337 0.1148 0.4029 250 ARG A CA 1623 C C . ARG A 250 ? 1.9044 1.6695 2.1554 -0.1147 0.1170 0.3623 250 ARG A C 1624 O O . ARG A 250 ? 1.9816 1.6942 2.1753 -0.1060 0.1190 0.3316 250 ARG A O 1625 C CB . ARG A 250 ? 2.3763 2.1467 2.7167 -0.1750 0.0660 0.4134 250 ARG A CB 1626 C CG . ARG A 250 ? 2.5070 2.2999 2.9193 -0.2006 0.0577 0.4554 250 ARG A CG 1627 C CD . ARG A 250 ? 2.4235 2.1478 2.8085 -0.2207 0.0383 0.4446 250 ARG A CD 1628 N NE . ARG A 250 ? 2.3677 2.0858 2.7444 -0.1988 0.0745 0.4473 250 ARG A NE 1629 C CZ . ARG A 250 ? 2.4363 2.1193 2.7495 -0.1702 0.0965 0.4148 250 ARG A CZ 1630 N NH1 . ARG A 250 ? 2.2563 1.9063 2.5077 -0.1572 0.0912 0.3754 250 ARG A NH1 1631 N NH2 . ARG A 250 ? 2.4761 2.1593 2.7902 -0.1548 0.1239 0.4254 250 ARG A NH2 1632 N N . LYS A 251 ? 1.8106 1.6126 2.0736 -0.1070 0.1189 0.3658 251 LYS A N 1633 C CA . LYS A 251 ? 1.7461 1.5251 1.9516 -0.0933 0.1172 0.3329 251 LYS A CA 1634 C C . LYS A 251 ? 1.6597 1.4486 1.8376 -0.0584 0.1573 0.3161 251 LYS A C 1635 O O . LYS A 251 ? 1.6048 1.4064 1.7930 -0.0449 0.1843 0.3241 251 LYS A O 1636 C CB . LYS A 251 ? 1.9382 1.7454 2.1672 -0.1060 0.0927 0.3461 251 LYS A CB 1637 C CG . LYS A 251 ? 2.1923 2.0649 2.4695 -0.0860 0.1186 0.3696 251 LYS A CG 1638 C CD . LYS A 251 ? 2.3884 2.2892 2.6987 -0.1028 0.0869 0.3899 251 LYS A CD 1639 C CE . LYS A 251 ? 2.5427 2.4549 2.9075 -0.1401 0.0481 0.4208 251 LYS A CE 1640 N NZ . LYS A 251 ? 2.5808 2.4909 2.9502 -0.1698 -0.0033 0.4301 251 LYS A NZ 1641 N N . SER A 252 ? 1.7092 1.4906 1.8503 -0.0461 0.1589 0.2944 252 SER A N 1642 C CA . SER A 252 ? 1.7292 1.5068 1.8340 -0.0177 0.1893 0.2724 252 SER A CA 1643 C C . SER A 252 ? 1.6880 1.5024 1.8054 -0.0020 0.2059 0.2779 252 SER A C 1644 O O . SER A 252 ? 1.6845 1.5244 1.8324 -0.0111 0.1912 0.2955 252 SER A O 1645 C CB . SER A 252 ? 1.7811 1.5050 1.8236 -0.0148 0.1810 0.2380 252 SER A CB 1646 O OG . SER A 252 ? 1.9458 1.6382 1.9712 -0.0378 0.1468 0.2333 252 SER A OG 1647 N N . VAL A 253 ? 1.6196 1.4347 1.7139 0.0209 0.2348 0.2638 253 VAL A N 1648 C CA . VAL A 253 ? 1.7159 1.5615 1.8231 0.0377 0.2563 0.2703 253 VAL A CA 1649 C C . VAL A 253 ? 1.8741 1.6992 1.9355 0.0535 0.2685 0.2426 253 VAL A C 1650 O O . VAL A 253 ? 2.2371 2.0405 2.2691 0.0598 0.2768 0.2257 253 VAL A O 1651 C CB . VAL A 253 ? 1.6196 1.4939 1.7565 0.0490 0.2856 0.2908 253 VAL A CB 1652 C CG1 . VAL A 253 ? 1.4333 1.3168 1.5575 0.0716 0.3151 0.2847 253 VAL A CG1 1653 C CG2 . VAL A 253 ? 1.7525 1.6636 1.9528 0.0367 0.2784 0.3268 253 VAL A CG2 1654 N N . TYR A 254 ? 1.7242 1.5582 1.7842 0.0591 0.2688 0.2414 254 TYR A N 1655 C CA . TYR A 254 ? 1.5919 1.4065 1.6118 0.0711 0.2776 0.2176 254 TYR A CA 1656 C C . TYR A 254 ? 1.4784 1.3080 1.5031 0.0887 0.3048 0.2192 254 TYR A C 1657 O O . TYR A 254 ? 1.5695 1.4252 1.6278 0.0934 0.3129 0.2395 254 TYR A O 1658 C CB . TYR A 254 ? 1.6641 1.4695 1.6696 0.0639 0.2574 0.2143 254 TYR A CB 1659 C CG . TYR A 254 ? 1.7993 1.5723 1.7777 0.0475 0.2315 0.2036 254 TYR A CG 1660 C CD1 . TYR A 254 ? 1.9274 1.6635 1.8600 0.0524 0.2353 0.1781 254 TYR A CD1 1661 C CD2 . TYR A 254 ? 1.8367 1.6134 1.8362 0.0268 0.2040 0.2200 254 TYR A CD2 1662 C CE1 . TYR A 254 ? 2.2263 1.9232 2.1270 0.0402 0.2161 0.1662 254 TYR A CE1 1663 C CE2 . TYR A 254 ? 2.0250 1.7606 1.9905 0.0102 0.1794 0.2073 254 TYR A CE2 1664 C CZ . TYR A 254 ? 2.2446 1.9368 2.1568 0.0185 0.1875 0.1789 254 TYR A CZ 1665 O OH . TYR A 254 ? 2.5871 2.2287 2.4578 0.0052 0.1680 0.1637 254 TYR A OH 1666 N N . TRP A 255 ? 1.4651 1.2769 1.4581 0.0983 0.3185 0.1992 255 TRP A N 1667 C CA . TRP A 255 ? 1.6392 1.4550 1.6282 0.1128 0.3427 0.1974 255 TRP A CA 1668 C C . TRP A 255 ? 1.5942 1.3961 1.5608 0.1176 0.3441 0.1822 255 TRP A C 1669 O O . TRP A 255 ? 1.7456 1.5300 1.6881 0.1150 0.3379 0.1654 255 TRP A O 1670 C CB . TRP A 255 ? 1.7797 1.5860 1.7500 0.1181 0.3584 0.1901 255 TRP A CB 1671 C CG . TRP A 255 ? 1.6766 1.4896 1.6574 0.1133 0.3583 0.2021 255 TRP A CG 1672 C CD1 . TRP A 255 ? 1.6191 1.4193 1.5839 0.1079 0.3500 0.1951 255 TRP A CD1 1673 C CD2 . TRP A 255 ? 1.6446 1.4794 1.6568 0.1148 0.3694 0.2263 255 TRP A CD2 1674 N NE1 . TRP A 255 ? 1.6446 1.4546 1.6248 0.1047 0.3540 0.2127 255 TRP A NE1 1675 C CE2 . TRP A 255 ? 1.6485 1.4808 1.6587 0.1085 0.3668 0.2323 255 TRP A CE2 1676 C CE3 . TRP A 255 ? 1.6131 1.4717 1.6606 0.1216 0.3823 0.2469 255 TRP A CE3 1677 C CZ2 . TRP A 255 ? 1.6413 1.4935 1.6813 0.1076 0.3777 0.2577 255 TRP A CZ2 1678 C CZ3 . TRP A 255 ? 1.6214 1.5029 1.7034 0.1221 0.3940 0.2728 255 TRP A CZ3 1679 C CH2 . TRP A 255 ? 1.6541 1.5320 1.7311 0.1145 0.3922 0.2779 255 TRP A CH2 1680 N N . HIS A 256 ? 1.4155 1.2252 1.3931 0.1260 0.3547 0.1902 256 HIS A N 1681 C CA . HIS A 256 ? 1.4617 1.2567 1.4190 0.1307 0.3594 0.1778 256 HIS A CA 1682 C C . HIS A 256 ? 1.4895 1.2708 1.4315 0.1388 0.3803 0.1675 256 HIS A C 1683 O O . HIS A 256 ? 1.6649 1.4468 1.6154 0.1488 0.3981 0.1754 256 HIS A O 1684 C CB . HIS A 256 ? 1.5090 1.3149 1.4832 0.1340 0.3562 0.1928 256 HIS A CB 1685 C CG . HIS A 256 ? 1.7148 1.5269 1.6916 0.1219 0.3297 0.2005 256 HIS A CG 1686 N ND1 . HIS A 256 ? 1.9035 1.6949 1.8464 0.1143 0.3163 0.1850 256 HIS A ND1 1687 C CD2 . HIS A 256 ? 1.8717 1.7052 1.8783 0.1148 0.3130 0.2222 256 HIS A CD2 1688 C CE1 . HIS A 256 ? 2.0550 1.8475 1.9967 0.1025 0.2921 0.1936 256 HIS A CE1 1689 N NE2 . HIS A 256 ? 2.0169 1.8369 1.9996 0.1006 0.2865 0.2170 256 HIS A NE2 1690 N N . VAL A 257 ? 1.4625 1.2293 1.3816 0.1343 0.3775 0.1509 257 VAL A N 1691 C CA . VAL A 257 ? 1.4405 1.1910 1.3389 0.1367 0.3903 0.1409 257 VAL A CA 1692 C C . VAL A 257 ? 1.4733 1.2059 1.3585 0.1383 0.3977 0.1309 257 VAL A C 1693 O O . VAL A 257 ? 1.5813 1.3132 1.4669 0.1339 0.3900 0.1252 257 VAL A O 1694 C CB . VAL A 257 ? 1.3431 1.0895 1.2275 0.1292 0.3802 0.1325 257 VAL A CB 1695 C CG1 . VAL A 257 ? 1.2430 0.9744 1.1027 0.1302 0.3904 0.1288 257 VAL A CG1 1696 C CG2 . VAL A 257 ? 1.3470 1.1068 1.2459 0.1252 0.3685 0.1410 257 VAL A CG2 1697 N N . ILE A 258 ? 1.4539 1.1688 1.3264 0.1447 0.4148 0.1294 258 ILE A N 1698 C CA . ILE A 258 ? 1.5440 1.2340 1.4007 0.1437 0.4212 0.1190 258 ILE A CA 1699 C C . ILE A 258 ? 1.7745 1.4362 1.5950 0.1378 0.4237 0.1053 258 ILE A C 1700 O O . ILE A 258 ? 1.8417 1.4881 1.6419 0.1448 0.4385 0.1058 258 ILE A O 1701 C CB . ILE A 258 ? 1.4732 1.1547 1.3405 0.1564 0.4390 0.1281 258 ILE A CB 1702 C CG1 . ILE A 258 ? 1.4208 1.1311 1.3203 0.1602 0.4317 0.1448 258 ILE A CG1 1703 C CG2 . ILE A 258 ? 1.4417 1.0943 1.2950 0.1533 0.4439 0.1183 258 ILE A CG2 1704 C CD1 . ILE A 258 ? 1.4778 1.1858 1.3953 0.1740 0.4471 0.1597 258 ILE A CD1 1705 N N . GLY A 259 ? 1.8952 1.5500 1.7070 0.1245 0.4089 0.0949 259 GLY A N 1706 C CA . GLY A 259 ? 2.0501 1.6721 1.8248 0.1145 0.4057 0.0819 259 GLY A CA 1707 C C . GLY A 259 ? 2.3068 1.8934 2.0668 0.1150 0.4180 0.0747 259 GLY A C 1708 O O . GLY A 259 ? 2.5546 2.1477 2.3388 0.1137 0.4171 0.0779 259 GLY A O 1709 N N . MET A 260 ? 2.3803 1.9250 2.0971 0.1179 0.4316 0.0653 260 MET A N 1710 C CA . MET A 260 ? 2.3794 1.8778 2.0739 0.1173 0.4433 0.0557 260 MET A CA 1711 C C . MET A 260 ? 2.3222 1.7639 1.9523 0.1050 0.4402 0.0367 260 MET A C 1712 O O . MET A 260 ? 2.2322 1.6621 1.8237 0.1056 0.4414 0.0324 260 MET A O 1713 C CB . MET A 260 ? 2.6206 2.1131 2.3293 0.1408 0.4732 0.0657 260 MET A CB 1714 C CG . MET A 260 ? 2.9404 2.4038 2.6543 0.1416 0.4816 0.0639 260 MET A CG 1715 S SD . MET A 260 ? 3.4624 2.8709 3.1492 0.1657 0.5210 0.0625 260 MET A SD 1716 C CE . MET A 260 ? 3.3323 2.6715 2.9348 0.1529 0.5214 0.0349 260 MET A CE 1717 N N . GLY A 261 ? 2.3270 1.7305 1.9427 0.0922 0.4351 0.0262 261 GLY A N 1718 C CA . GLY A 261 ? 2.4306 1.7722 1.9815 0.0746 0.4256 0.0064 261 GLY A CA 1719 C C . GLY A 261 ? 2.5483 1.8578 2.1034 0.0579 0.4165 -0.0004 261 GLY A C 1720 O O . GLY A 261 ? 2.5911 1.9289 2.2000 0.0614 0.4196 0.0118 261 GLY A O 1721 N N . THR A 262 ? 2.5674 1.8142 2.0615 0.0377 0.4037 -0.0194 262 THR A N 1722 C CA . THR A 262 ? 2.4753 1.6776 1.9639 0.0189 0.3950 -0.0277 262 THR A CA 1723 C C . THR A 262 ? 2.3635 1.5803 1.8618 -0.0183 0.3493 -0.0279 262 THR A C 1724 O O . THR A 262 ? 2.1864 1.4033 1.7178 -0.0385 0.3332 -0.0237 262 THR A O 1725 C CB . THR A 262 ? 2.6179 1.7258 2.0271 0.0267 0.4200 -0.0492 262 THR A CB 1726 O OG1 . THR A 262 ? 2.5413 1.6136 1.9661 0.0269 0.4323 -0.0498 262 THR A OG1 1727 C CG2 . THR A 262 ? 2.6700 1.7120 1.9886 0.0016 0.3974 -0.0727 262 THR A CG2 1728 N N . THR A 263 ? 2.3639 1.6018 1.8429 -0.0258 0.3290 -0.0280 263 THR A N 1729 C CA . THR A 263 ? 2.4191 1.6645 1.8966 -0.0603 0.2840 -0.0273 263 THR A CA 1730 C C . THR A 263 ? 2.4470 1.7706 1.9729 -0.0556 0.2694 -0.0085 263 THR A C 1731 O O . THR A 263 ? 2.7108 2.0614 2.2427 -0.0288 0.2929 -0.0031 263 THR A O 1732 C CB . THR A 263 ? 2.5660 1.7292 1.9405 -0.0777 0.2708 -0.0509 263 THR A CB 1733 O OG1 . THR A 263 ? 2.7098 1.8836 2.0805 -0.1131 0.2211 -0.0474 263 THR A OG1 1734 C CG2 . THR A 263 ? 2.5581 1.7023 1.8726 -0.0504 0.3000 -0.0583 263 THR A CG2 1735 N N . PRO A 264 ? 2.3389 1.6993 1.9042 -0.0813 0.2311 0.0036 264 PRO A N 1736 C CA . PRO A 264 ? 2.3061 1.7370 1.9214 -0.0765 0.2171 0.0231 264 PRO A CA 1737 C C . PRO A 264 ? 2.4782 1.9112 2.0497 -0.0667 0.2148 0.0221 264 PRO A C 1738 O O . PRO A 264 ? 2.5095 1.9979 2.1257 -0.0639 0.2016 0.0396 264 PRO A O 1739 C CB . PRO A 264 ? 2.1879 1.6415 1.8432 -0.1101 0.1740 0.0357 264 PRO A CB 1740 C CG . PRO A 264 ? 2.2021 1.5876 1.8095 -0.1372 0.1595 0.0192 264 PRO A CG 1741 C CD . PRO A 264 ? 2.3246 1.6707 1.9097 -0.1142 0.2023 0.0051 264 PRO A CD 1742 N N . GLU A 265 ? 2.6703 2.0445 2.1581 -0.0600 0.2300 0.0043 265 GLU A N 1743 C CA . GLU A 265 ? 2.7420 2.1185 2.1875 -0.0525 0.2279 0.0067 265 GLU A CA 1744 C C . GLU A 265 ? 2.5254 1.9559 2.0188 -0.0224 0.2545 0.0212 265 GLU A C 1745 O O . GLU A 265 ? 2.3652 1.7926 1.8659 0.0013 0.2907 0.0186 265 GLU A O 1746 C CB . GLU A 265 ? 3.0943 2.3898 2.4291 -0.0551 0.2366 -0.0147 265 GLU A CB 1747 C CG . GLU A 265 ? 3.2743 2.5410 2.5762 -0.0227 0.2878 -0.0232 265 GLU A CG 1748 C CD . GLU A 265 ? 3.5185 2.7023 2.7055 -0.0241 0.2990 -0.0432 265 GLU A CD 1749 O OE1 . GLU A 265 ? 3.6302 2.7467 2.7560 -0.0464 0.2830 -0.0627 265 GLU A OE1 1750 O OE2 . GLU A 265 ? 3.4958 2.6786 2.6511 -0.0035 0.3245 -0.0391 265 GLU A OE2 1751 N N . VAL A 266 ? 2.4208 1.8986 1.9469 -0.0256 0.2329 0.0380 266 VAL A N 1752 C CA . VAL A 266 ? 2.1051 1.6407 1.6925 -0.0047 0.2460 0.0547 266 VAL A CA 1753 C C . VAL A 266 ? 2.1703 1.7036 1.7239 0.0115 0.2619 0.0587 266 VAL A C 1754 O O . VAL A 266 ? 2.4827 1.9700 1.9621 0.0090 0.2666 0.0490 266 VAL A O 1755 C CB . VAL A 266 ? 1.8383 1.4245 1.4877 -0.0162 0.2152 0.0729 266 VAL A CB 1756 C CG1 . VAL A 266 ? 1.6472 1.2395 1.2718 -0.0232 0.1912 0.0835 266 VAL A CG1 1757 C CG2 . VAL A 266 ? 1.6941 1.3291 1.4170 0.0029 0.2331 0.0842 266 VAL A CG2 1758 N N . HIS A 267 ? 1.9653 1.5440 1.5704 0.0276 0.2713 0.0730 267 HIS A N 1759 C CA . HIS A 267 ? 2.0317 1.6136 1.6187 0.0428 0.2884 0.0804 267 HIS A CA 1760 C C . HIS A 267 ? 2.1303 1.7594 1.7706 0.0481 0.2777 0.0989 267 HIS A C 1761 O O . HIS A 267 ? 2.3542 2.0147 2.0504 0.0466 0.2665 0.1048 267 HIS A O 1762 C CB . HIS A 267 ? 1.9451 1.5201 1.5354 0.0630 0.3260 0.0766 267 HIS A CB 1763 C CG . HIS A 267 ? 2.0478 1.5711 1.5832 0.0645 0.3451 0.0604 267 HIS A CG 1764 N ND1 . HIS A 267 ? 2.2454 1.7291 1.7145 0.0711 0.3643 0.0559 267 HIS A ND1 1765 C CD2 . HIS A 267 ? 2.1696 1.6702 1.7055 0.0621 0.3513 0.0482 267 HIS A CD2 1766 C CE1 . HIS A 267 ? 2.3717 1.8072 1.8007 0.0736 0.3821 0.0398 267 HIS A CE1 1767 N NE2 . HIS A 267 ? 2.2133 1.6581 1.6834 0.0675 0.3733 0.0352 267 HIS A NE2 1768 N N . SER A 268 ? 2.1670 1.7974 1.7887 0.0554 0.2843 0.1088 268 SER A N 1769 C CA . SER A 268 ? 2.0243 1.6904 1.6924 0.0629 0.2798 0.1258 268 SER A CA 1770 C C . SER A 268 ? 2.0034 1.6655 1.6590 0.0767 0.3071 0.1317 268 SER A C 1771 O O . SER A 268 ? 2.2150 1.8595 1.8251 0.0762 0.3113 0.1377 268 SER A O 1772 C CB . SER A 268 ? 2.0077 1.6814 1.6690 0.0514 0.2491 0.1391 268 SER A CB 1773 O OG . SER A 268 ? 1.8330 1.5421 1.5554 0.0567 0.2387 0.1539 268 SER A OG 1774 N N . ILE A 269 ? 1.7318 1.4096 1.4265 0.0879 0.3254 0.1318 269 ILE A N 1775 C CA . ILE A 269 ? 1.6664 1.3472 1.3631 0.0991 0.3493 0.1415 269 ILE A CA 1776 C C . ILE A 269 ? 1.7911 1.4947 1.5210 0.1001 0.3414 0.1585 269 ILE A C 1777 O O . ILE A 269 ? 1.9082 1.6288 1.6781 0.0989 0.3272 0.1592 269 ILE A O 1778 C CB . ILE A 269 ? 1.5331 1.2211 1.2586 0.1086 0.3687 0.1372 269 ILE A CB 1779 C CG1 . ILE A 269 ? 1.5714 1.2307 1.2626 0.1096 0.3805 0.1221 269 ILE A CG1 1780 C CG2 . ILE A 269 ? 1.4217 1.1221 1.1650 0.1185 0.3898 0.1526 269 ILE A CG2 1781 C CD1 . ILE A 269 ? 1.6419 1.2933 1.3295 0.0975 0.3593 0.1090 269 ILE A CD1 1782 N N . PHE A 270 ? 1.8319 1.5321 1.5438 0.1029 0.3526 0.1727 270 PHE A N 1783 C CA . PHE A 270 ? 1.8304 1.5483 1.5755 0.1033 0.3484 0.1911 270 PHE A CA 1784 C C . PHE A 270 ? 1.7748 1.5016 1.5369 0.1101 0.3730 0.2039 270 PHE A C 1785 O O . PHE A 270 ? 1.8575 1.5739 1.5933 0.1170 0.3969 0.2031 270 PHE A O 1786 C CB . PHE A 270 ? 1.9583 1.6682 1.6736 0.0983 0.3365 0.2043 270 PHE A CB 1787 C CG . PHE A 270 ? 2.0428 1.7520 1.7544 0.0907 0.3074 0.1999 270 PHE A CG 1788 C CD1 . PHE A 270 ? 2.0478 1.7423 1.7247 0.0840 0.2978 0.1852 270 PHE A CD1 1789 C CD2 . PHE A 270 ? 1.9448 1.6671 1.6902 0.0899 0.2892 0.2132 270 PHE A CD2 1790 C CE1 . PHE A 270 ? 1.9773 1.6777 1.6609 0.0751 0.2686 0.1862 270 PHE A CE1 1791 C CE2 . PHE A 270 ? 1.9497 1.6771 1.7018 0.0849 0.2640 0.2144 270 PHE A CE2 1792 C CZ . PHE A 270 ? 1.9667 1.6869 1.6913 0.0767 0.2526 0.2022 270 PHE A CZ 1793 N N . LEU A 271 ? 1.5548 1.2992 1.3622 0.1081 0.3680 0.2168 271 LEU A N 1794 C CA . LEU A 271 ? 1.5393 1.2972 1.3700 0.1111 0.3875 0.2357 271 LEU A CA 1795 C C . LEU A 271 ? 1.6631 1.4233 1.5007 0.1058 0.3826 0.2566 271 LEU A C 1796 O O . LEU A 271 ? 1.8614 1.6234 1.7261 0.0991 0.3623 0.2586 271 LEU A O 1797 C CB . LEU A 271 ? 1.4413 1.2174 1.3231 0.1092 0.3835 0.2366 271 LEU A CB 1798 C CG . LEU A 271 ? 1.3918 1.1886 1.3108 0.1087 0.3984 0.2622 271 LEU A CG 1799 C CD1 . LEU A 271 ? 1.2983 1.1050 1.2221 0.1203 0.4253 0.2658 271 LEU A CD1 1800 C CD2 . LEU A 271 ? 1.3705 1.1793 1.3381 0.0968 0.3773 0.2695 271 LEU A CD2 1801 N N . GLU A 272 ? 1.7957 1.5524 1.6073 0.1098 0.4038 0.2728 272 GLU A N 1802 C CA . GLU A 272 ? 1.8901 1.6486 1.7050 0.1054 0.4044 0.2979 272 GLU A CA 1803 C C . GLU A 272 ? 1.8121 1.5819 1.6826 0.0952 0.3846 0.3092 272 GLU A C 1804 O O . GLU A 272 ? 1.7654 1.5511 1.6828 0.0913 0.3848 0.3133 272 GLU A O 1805 C CB . GLU A 272 ? 2.1109 1.8759 1.9180 0.1130 0.4402 0.3196 272 GLU A CB 1806 C CG . GLU A 272 ? 2.4595 2.2135 2.2309 0.1122 0.4488 0.3415 272 GLU A CG 1807 C CD . GLU A 272 ? 2.6920 2.4417 2.4302 0.1246 0.4912 0.3562 272 GLU A CD 1808 O OE1 . GLU A 272 ? 2.6350 2.3787 2.3569 0.1358 0.5123 0.3420 272 GLU A OE1 1809 O OE2 . GLU A 272 ? 3.0541 2.8039 2.7817 0.1245 0.5061 0.3832 272 GLU A OE2 1810 N N . GLY A 273 ? 1.8052 1.5631 1.6680 0.0905 0.3661 0.3147 273 GLY A N 1811 C CA . GLY A 273 ? 1.9270 1.6835 1.8329 0.0816 0.3485 0.3251 273 GLY A CA 1812 C C . GLY A 273 ? 1.9717 1.7230 1.9003 0.0797 0.3299 0.3023 273 GLY A C 1813 O O . GLY A 273 ? 2.3473 2.0832 2.2840 0.0784 0.3120 0.2981 273 GLY A O 1814 N N . HIS A 274 ? 1.8700 1.6321 1.8053 0.0819 0.3369 0.2884 274 HIS A N 1815 C CA . HIS A 274 ? 1.8306 1.5887 1.7861 0.0791 0.3230 0.2700 274 HIS A CA 1816 C C . HIS A 274 ? 1.7441 1.4929 1.6788 0.0864 0.3153 0.2450 274 HIS A C 1817 O O . HIS A 274 ? 1.8301 1.5829 1.7382 0.0926 0.3235 0.2369 274 HIS A O 1818 C CB . HIS A 274 ? 1.7709 1.5481 1.7514 0.0761 0.3320 0.2741 274 HIS A CB 1819 C CG . HIS A 274 ? 1.8442 1.6339 1.8616 0.0655 0.3341 0.3013 274 HIS A CG 1820 N ND1 . HIS A 274 ? 1.7969 1.6139 1.8397 0.0663 0.3521 0.3195 274 HIS A ND1 1821 C CD2 . HIS A 274 ? 1.9163 1.6951 1.9538 0.0536 0.3212 0.3160 274 HIS A CD2 1822 C CE1 . HIS A 274 ? 1.9703 1.7974 2.0518 0.0538 0.3489 0.3456 274 HIS A CE1 1823 N NE2 . HIS A 274 ? 2.0124 1.8142 2.0890 0.0448 0.3293 0.3431 274 HIS A NE2 1824 N N . THR A 275 ? 1.6716 1.4051 1.6182 0.0852 0.3007 0.2339 275 THR A N 1825 C CA . THR A 275 ? 1.4933 1.2195 1.4307 0.0927 0.2955 0.2138 275 THR A CA 1826 C C . THR A 275 ? 1.4289 1.1573 1.3684 0.0927 0.2978 0.1976 275 THR A C 1827 O O . THR A 275 ? 1.4167 1.1514 1.3678 0.0860 0.2989 0.2025 275 THR A O 1828 C CB . THR A 275 ? 1.5838 1.2877 1.5316 0.0952 0.2845 0.2129 275 THR A CB 1829 O OG1 . THR A 275 ? 1.5951 1.2809 1.5559 0.0864 0.2785 0.2150 275 THR A OG1 1830 C CG2 . THR A 275 ? 1.7817 1.4844 1.7287 0.0978 0.2800 0.2309 275 THR A CG2 1831 N N . PHE A 276 ? 1.5043 1.2302 1.4356 0.0996 0.2980 0.1815 276 PHE A N 1832 C CA . PHE A 276 ? 1.6381 1.3640 1.5676 0.0999 0.3006 0.1682 276 PHE A CA 1833 C C . PHE A 276 ? 1.7865 1.4911 1.7130 0.1035 0.2962 0.1547 276 PHE A C 1834 O O . PHE A 276 ? 1.7779 1.4672 1.7070 0.1092 0.2940 0.1536 276 PHE A O 1835 C CB . PHE A 276 ? 1.4889 1.2289 1.4075 0.1046 0.3104 0.1606 276 PHE A CB 1836 C CG . PHE A 276 ? 1.4166 1.1690 1.3285 0.1036 0.3202 0.1698 276 PHE A CG 1837 C CD1 . PHE A 276 ? 1.4429 1.2046 1.3679 0.1004 0.3256 0.1808 276 PHE A CD1 1838 C CD2 . PHE A 276 ? 1.4310 1.1839 1.3224 0.1057 0.3241 0.1690 276 PHE A CD2 1839 C CE1 . PHE A 276 ? 1.5411 1.3125 1.4602 0.1034 0.3413 0.1909 276 PHE A CE1 1840 C CE2 . PHE A 276 ? 1.4011 1.1560 1.2748 0.1067 0.3371 0.1755 276 PHE A CE2 1841 C CZ . PHE A 276 ? 1.5015 1.2657 1.3897 0.1075 0.3490 0.1866 276 PHE A CZ 1842 N N . LEU A 277 ? 1.7343 1.4365 1.6533 0.1018 0.2970 0.1458 277 LEU A N 1843 C CA . LEU A 277 ? 1.7059 1.3873 1.6111 0.1074 0.2985 0.1315 277 LEU A CA 1844 C C . LEU A 277 ? 1.8615 1.5552 1.7593 0.1119 0.3074 0.1238 277 LEU A C 1845 O O . LEU A 277 ? 1.9597 1.6628 1.8552 0.1069 0.3061 0.1258 277 LEU A O 1846 C CB . LEU A 277 ? 1.5814 1.2329 1.4735 0.0988 0.2870 0.1277 277 LEU A CB 1847 C CG . LEU A 277 ? 1.5781 1.2085 1.4763 0.0998 0.2832 0.1318 277 LEU A CG 1848 C CD1 . LEU A 277 ? 1.6740 1.3042 1.5859 0.0845 0.2699 0.1463 277 LEU A CD1 1849 C CD2 . LEU A 277 ? 1.7161 1.3033 1.5913 0.1075 0.2865 0.1170 277 LEU A CD2 1850 N N . VAL A 278 ? 1.8969 1.5929 1.7970 0.1216 0.3165 0.1183 278 VAL A N 1851 C CA . VAL A 278 ? 1.7932 1.4949 1.6875 0.1263 0.3263 0.1114 278 VAL A CA 1852 C C . VAL A 278 ? 1.7896 1.4662 1.6706 0.1351 0.3339 0.1026 278 VAL A C 1853 O O . VAL A 278 ? 1.4959 1.1526 1.3766 0.1395 0.3331 0.1017 278 VAL A O 1854 C CB . VAL A 278 ? 1.8364 1.5604 1.7468 0.1288 0.3313 0.1145 278 VAL A CB 1855 C CG1 . VAL A 278 ? 1.9284 1.6649 1.8411 0.1219 0.3249 0.1222 278 VAL A CG1 1856 C CG2 . VAL A 278 ? 1.7702 1.4951 1.6982 0.1376 0.3352 0.1163 278 VAL A CG2 1857 N N . ARG A 279 ? 2.0158 1.6896 1.8828 0.1386 0.3436 0.0967 279 ARG A N 1858 C CA . ARG A 279 ? 2.1015 1.7496 1.9492 0.1494 0.3572 0.0886 279 ARG A CA 1859 C C . ARG A 279 ? 1.9495 1.5605 1.7753 0.1479 0.3491 0.0828 279 ARG A C 1860 O O . ARG A 279 ? 2.2571 1.8466 2.0532 0.1375 0.3365 0.0780 279 ARG A O 1861 C CB . ARG A 279 ? 2.3666 2.0320 2.2450 0.1620 0.3731 0.0936 279 ARG A CB 1862 C CG . ARG A 279 ? 2.5422 2.2201 2.4228 0.1665 0.3891 0.0944 279 ARG A CG 1863 C CD . ARG A 279 ? 2.4003 2.1157 2.3220 0.1639 0.3900 0.1046 279 ARG A CD 1864 N NE . ARG A 279 ? 2.2400 1.9669 2.1555 0.1521 0.3823 0.1045 279 ARG A NE 1865 C CZ . ARG A 279 ? 2.1333 1.8515 2.0261 0.1512 0.3885 0.1016 279 ARG A CZ 1866 N NH1 . ARG A 279 ? 1.9093 1.6059 1.7762 0.1596 0.4014 0.0973 279 ARG A NH1 1867 N NH2 . ARG A 279 ? 2.2579 1.9853 2.1501 0.1427 0.3828 0.1035 279 ARG A NH2 1868 N N . ASN A 280 ? 1.6615 1.2649 1.5042 0.1564 0.3533 0.0851 280 ASN A N 1869 C CA . ASN A 280 ? 1.7342 1.3044 1.5635 0.1516 0.3420 0.0825 280 ASN A CA 1870 C C . ASN A 280 ? 1.8865 1.4665 1.7505 0.1568 0.3402 0.0936 280 ASN A C 1871 O O . ASN A 280 ? 1.9429 1.4888 1.8000 0.1589 0.3375 0.0923 280 ASN A O 1872 C CB . ASN A 280 ? 1.8525 1.3677 1.6369 0.1589 0.3515 0.0674 280 ASN A CB 1873 C CG . ASN A 280 ? 2.0618 1.5350 1.8250 0.1478 0.3343 0.0628 280 ASN A CG 1874 O OD1 . ASN A 280 ? 2.1475 1.6266 1.9078 0.1278 0.3115 0.0666 280 ASN A OD1 1875 N ND2 . ASN A 280 ? 2.1978 1.6304 1.9531 0.1604 0.3453 0.0576 280 ASN A ND2 1876 N N . HIS A 281 ? 1.9497 1.5725 1.8480 0.1577 0.3399 0.1054 281 HIS A N 1877 C CA . HIS A 281 ? 1.8700 1.5047 1.7992 0.1625 0.3360 0.1189 281 HIS A CA 1878 C C . HIS A 281 ? 1.8715 1.5223 1.8052 0.1478 0.3189 0.1288 281 HIS A C 1879 O O . HIS A 281 ? 1.8429 1.5146 1.7712 0.1376 0.3145 0.1290 281 HIS A O 1880 C CB . HIS A 281 ? 1.9421 1.6109 1.9052 0.1722 0.3438 0.1282 281 HIS A CB 1881 C CG . HIS A 281 ? 1.9081 1.5698 1.8728 0.1872 0.3656 0.1222 281 HIS A CG 1882 N ND1 . HIS A 281 ? 1.8440 1.4882 1.8238 0.2066 0.3822 0.1256 281 HIS A ND1 1883 C CD2 . HIS A 281 ? 1.8388 1.5071 1.7919 0.1871 0.3766 0.1148 281 HIS A CD2 1884 C CE1 . HIS A 281 ? 1.8499 1.4907 1.8259 0.2184 0.4047 0.1204 281 HIS A CE1 1885 N NE2 . HIS A 281 ? 1.8229 1.4783 1.7818 0.2058 0.4006 0.1141 281 HIS A NE2 1886 N N . ARG A 282 ? 1.8589 1.4970 1.8022 0.1482 0.3122 0.1384 282 ARG A N 1887 C CA . ARG A 282 ? 1.8021 1.4590 1.7542 0.1382 0.3002 0.1532 282 ARG A CA 1888 C C . ARG A 282 ? 1.7811 1.4745 1.7455 0.1394 0.2993 0.1601 282 ARG A C 1889 O O . ARG A 282 ? 1.9077 1.6114 1.8934 0.1490 0.3005 0.1666 282 ARG A O 1890 C CB . ARG A 282 ? 1.8391 1.4758 1.8035 0.1423 0.2954 0.1652 282 ARG A CB 1891 C CG . ARG A 282 ? 1.9128 1.5604 1.8804 0.1309 0.2845 0.1824 282 ARG A CG 1892 C CD . ARG A 282 ? 1.9538 1.5909 1.9090 0.1158 0.2801 0.1800 282 ARG A CD 1893 N NE . ARG A 282 ? 1.9387 1.5329 1.8891 0.1134 0.2762 0.1749 282 ARG A NE 1894 C CZ . ARG A 282 ? 2.0947 1.6717 2.0362 0.0980 0.2677 0.1719 282 ARG A CZ 1895 N NH1 . ARG A 282 ? 1.9029 1.5078 1.8468 0.0859 0.2644 0.1764 282 ARG A NH1 1896 N NH2 . ARG A 282 ? 2.4503 1.9796 2.3813 0.0945 0.2618 0.1655 282 ARG A NH2 1897 N N . GLN A 283 ? 1.6782 1.3891 1.6299 0.1294 0.2973 0.1590 283 GLN A N 1898 C CA . GLN A 283 ? 1.6834 1.4183 1.6353 0.1265 0.2934 0.1642 283 GLN A CA 1899 C C . GLN A 283 ? 1.7046 1.4409 1.6404 0.1178 0.2891 0.1739 283 GLN A C 1900 O O . GLN A 283 ? 1.8844 1.6147 1.8130 0.1132 0.2938 0.1723 283 GLN A O 1901 C CB . GLN A 283 ? 1.7012 1.4446 1.6444 0.1244 0.3007 0.1516 283 GLN A CB 1902 C CG . GLN A 283 ? 1.9703 1.7309 1.9252 0.1247 0.2978 0.1524 283 GLN A CG 1903 C CD . GLN A 283 ? 2.2371 1.9999 2.1923 0.1261 0.3087 0.1407 283 GLN A CD 1904 O OE1 . GLN A 283 ? 2.3419 2.1010 2.3110 0.1352 0.3180 0.1375 283 GLN A OE1 1905 N NE2 . GLN A 283 ? 2.1723 1.9373 2.1093 0.1183 0.3100 0.1350 283 GLN A NE2 1906 N N . ALA A 284 ? 1.6547 1.3988 1.5852 0.1152 0.2804 0.1866 284 ALA A N 1907 C CA . ALA A 284 ? 1.6861 1.4280 1.5961 0.1086 0.2818 0.1971 284 ALA A CA 1908 C C . ALA A 284 ? 1.6839 1.4309 1.5628 0.1037 0.2874 0.1920 284 ALA A C 1909 O O . ALA A 284 ? 1.7225 1.4669 1.5822 0.1011 0.2970 0.1982 284 ALA A O 1910 C CB . ALA A 284 ? 1.8671 1.6061 1.7795 0.1086 0.2715 0.2168 284 ALA A CB 1911 N N . SER A 285 ? 1.6527 1.4047 1.5275 0.1028 0.2830 0.1817 285 SER A N 1912 C CA . SER A 285 ? 1.6143 1.3620 1.4588 0.0984 0.2898 0.1712 285 SER A CA 1913 C C . SER A 285 ? 1.6567 1.4071 1.5177 0.1019 0.2994 0.1572 285 SER A C 1914 O O . SER A 285 ? 2.0340 1.7898 1.9232 0.1062 0.2968 0.1548 285 SER A O 1915 C CB . SER A 285 ? 1.6114 1.3578 1.4350 0.0903 0.2735 0.1710 285 SER A CB 1916 O OG . SER A 285 ? 1.5608 1.3211 1.4143 0.0901 0.2547 0.1814 285 SER A OG 1917 N N . LEU A 286 ? 1.5939 1.3380 1.4366 0.1018 0.3128 0.1493 286 LEU A N 1918 C CA . LEU A 286 ? 1.5402 1.2851 1.3921 0.1032 0.3181 0.1371 286 LEU A CA 1919 C C . LEU A 286 ? 1.6504 1.3884 1.4819 0.0954 0.3093 0.1320 286 LEU A C 1920 O O . LEU A 286 ? 1.6691 1.3950 1.4666 0.0903 0.3055 0.1345 286 LEU A O 1921 C CB . LEU A 286 ? 1.4607 1.2012 1.3058 0.1073 0.3354 0.1337 286 LEU A CB 1922 C CG . LEU A 286 ? 1.3921 1.1403 1.2550 0.1115 0.3434 0.1416 286 LEU A CG 1923 C CD1 . LEU A 286 ? 1.2838 1.0303 1.1427 0.1166 0.3601 0.1411 286 LEU A CD1 1924 C CD2 . LEU A 286 ? 1.4332 1.1860 1.3199 0.1118 0.3349 0.1400 286 LEU A CD2 1925 N N . GLU A 287 ? 1.7495 1.4932 1.5989 0.0929 0.3046 0.1260 287 GLU A N 1926 C CA . GLU A 287 ? 1.9203 1.6567 1.7535 0.0811 0.2918 0.1224 287 GLU A CA 1927 C C . GLU A 287 ? 1.8921 1.6164 1.7193 0.0789 0.3021 0.1106 287 GLU A C 1928 O O . GLU A 287 ? 2.2443 1.9805 2.1021 0.0798 0.3038 0.1099 287 GLU A O 1929 C CB . GLU A 287 ? 2.1334 1.8904 1.9994 0.0764 0.2717 0.1328 287 GLU A CB 1930 C CG . GLU A 287 ? 2.5574 2.3325 2.4636 0.0889 0.2755 0.1418 287 GLU A CG 1931 C CD . GLU A 287 ? 2.9815 2.7692 2.9045 0.0883 0.2576 0.1580 287 GLU A CD 1932 O OE1 . GLU A 287 ? 3.2925 3.0723 3.1849 0.0803 0.2445 0.1636 287 GLU A OE1 1933 O OE2 . GLU A 287 ? 2.9654 2.7689 2.9304 0.0974 0.2582 0.1665 287 GLU A OE2 1934 N N . ILE A 288 ? 1.7348 1.4328 1.5213 0.0779 0.3124 0.1027 288 ILE A N 1935 C CA . ILE A 288 ? 1.7473 1.4295 1.5285 0.0792 0.3263 0.0930 288 ILE A CA 1936 C C . ILE A 288 ? 1.9453 1.6092 1.7124 0.0631 0.3127 0.0852 288 ILE A C 1937 O O . ILE A 288 ? 2.1446 1.7837 1.8699 0.0517 0.3009 0.0802 288 ILE A O 1938 C CB . ILE A 288 ? 1.7824 1.4421 1.5317 0.0891 0.3487 0.0896 288 ILE A CB 1939 C CG1 . ILE A 288 ? 1.7873 1.4696 1.5623 0.1022 0.3606 0.1005 288 ILE A CG1 1940 C CG2 . ILE A 288 ? 1.9628 1.6003 1.7047 0.0909 0.3625 0.0806 288 ILE A CG2 1941 C CD1 . ILE A 288 ? 1.8448 1.5441 1.6563 0.1086 0.3660 0.1029 288 ILE A CD1 1942 N N . SER A 289 ? 2.1124 1.7859 1.9117 0.0609 0.3137 0.0849 289 SER A N 1943 C CA . SER A 289 ? 2.2355 1.8937 2.0313 0.0432 0.3002 0.0800 289 SER A CA 1944 C C . SER A 289 ? 2.1143 1.7351 1.8835 0.0438 0.3169 0.0684 289 SER A C 1945 O O . SER A 289 ? 1.9124 1.5251 1.6723 0.0603 0.3399 0.0666 289 SER A O 1946 C CB . SER A 289 ? 2.4392 2.1332 2.2932 0.0390 0.2914 0.0914 289 SER A CB 1947 O OG . SER A 289 ? 2.6117 2.3314 2.4969 0.0568 0.3076 0.0979 289 SER A OG 1948 N N . PRO A 290 ? 2.1187 1.7156 1.8781 0.0251 0.3041 0.0623 290 PRO A N 1949 C CA . PRO A 290 ? 2.0597 1.6210 1.8054 0.0220 0.3161 0.0536 290 PRO A CA 1950 C C . PRO A 290 ? 1.9577 1.5226 1.7166 0.0444 0.3457 0.0561 290 PRO A C 1951 O O . PRO A 290 ? 2.0882 1.6221 1.8114 0.0560 0.3640 0.0489 290 PRO A O 1952 C CB . PRO A 290 ? 2.1679 1.7493 1.9591 0.0041 0.2988 0.0620 290 PRO A CB 1953 C CG . PRO A 290 ? 2.3253 1.9292 2.1251 -0.0109 0.2688 0.0689 290 PRO A CG 1954 C CD . PRO A 290 ? 2.2423 1.8478 2.0105 0.0021 0.2719 0.0669 290 PRO A CD 1955 N N . ILE A 291 ? 1.7933 1.3940 1.6005 0.0513 0.3513 0.0677 291 ILE A N 1956 C CA . ILE A 291 ? 1.8921 1.4975 1.7082 0.0715 0.3747 0.0726 291 ILE A CA 1957 C C . ILE A 291 ? 1.8637 1.5123 1.7148 0.0825 0.3766 0.0843 291 ILE A C 1958 O O . ILE A 291 ? 1.9884 1.6536 1.8670 0.0819 0.3783 0.0916 291 ILE A O 1959 C CB . ILE A 291 ? 1.8262 1.4014 1.6396 0.0717 0.3882 0.0713 291 ILE A CB 1960 C CG1 . ILE A 291 ? 1.7925 1.3662 1.6067 0.0936 0.4108 0.0776 291 ILE A CG1 1961 C CG2 . ILE A 291 ? 1.7453 1.3366 1.5947 0.0605 0.3821 0.0796 291 ILE A CG2 1962 C CD1 . ILE A 291 ? 1.8083 1.3332 1.5952 0.0990 0.4279 0.0712 291 ILE A CD1 1963 N N . THR A 292 ? 1.8157 1.4771 1.6609 0.0925 0.3778 0.0861 292 THR A N 1964 C CA . THR A 292 ? 1.8413 1.5347 1.7097 0.0978 0.3729 0.0933 292 THR A CA 1965 C C . THR A 292 ? 1.6804 1.3824 1.5507 0.1112 0.3820 0.0993 292 THR A C 1966 O O . THR A 292 ? 1.4980 1.1967 1.3567 0.1161 0.3852 0.1003 292 THR A O 1967 C CB . THR A 292 ? 2.0579 1.7603 1.9225 0.0923 0.3581 0.0925 292 THR A CB 1968 O OG1 . THR A 292 ? 2.2745 1.9590 2.1215 0.0780 0.3467 0.0865 292 THR A OG1 1969 C CG2 . THR A 292 ? 2.0603 1.7895 1.9550 0.0937 0.3510 0.0992 292 THR A CG2 1970 N N . PHE A 293 ? 1.7462 1.4590 1.6304 0.1161 0.3855 0.1051 293 PHE A N 1971 C CA . PHE A 293 ? 1.7998 1.5219 1.6856 0.1245 0.3865 0.1122 293 PHE A CA 1972 C C . PHE A 293 ? 1.8516 1.5855 1.7413 0.1240 0.3775 0.1117 293 PHE A C 1973 O O . PHE A 293 ? 2.1167 1.8529 2.0104 0.1241 0.3787 0.1107 293 PHE A O 1974 C CB . PHE A 293 ? 1.8500 1.5704 1.7381 0.1298 0.3934 0.1201 293 PHE A CB 1975 C CG . PHE A 293 ? 1.8126 1.5165 1.7001 0.1299 0.4042 0.1205 293 PHE A CG 1976 C CD1 . PHE A 293 ? 1.9089 1.5948 1.7880 0.1303 0.4108 0.1158 293 PHE A CD1 1977 C CD2 . PHE A 293 ? 1.6987 1.3997 1.5898 0.1298 0.4095 0.1258 293 PHE A CD2 1978 C CE1 . PHE A 293 ? 1.9155 1.5769 1.7897 0.1298 0.4210 0.1144 293 PHE A CE1 1979 C CE2 . PHE A 293 ? 1.7951 1.4772 1.6872 0.1287 0.4191 0.1273 293 PHE A CE2 1980 C CZ . PHE A 293 ? 1.9790 1.6394 1.8629 0.1284 0.4241 0.1207 293 PHE A CZ 1981 N N . LEU A 294 ? 1.8478 1.5864 1.7364 0.1244 0.3710 0.1134 294 LEU A N 1982 C CA . LEU A 294 ? 1.8280 1.5706 1.7178 0.1241 0.3622 0.1130 294 LEU A CA 1983 C C . LEU A 294 ? 1.7799 1.5259 1.6704 0.1241 0.3563 0.1206 294 LEU A C 1984 O O . LEU A 294 ? 1.6603 1.4112 1.5565 0.1258 0.3611 0.1278 294 LEU A O 1985 C CB . LEU A 294 ? 1.7655 1.5107 1.6593 0.1210 0.3565 0.1103 294 LEU A CB 1986 C CG . LEU A 294 ? 1.7555 1.5024 1.6458 0.1192 0.3527 0.1148 294 LEU A CG 1987 C CD1 . LEU A 294 ? 1.8296 1.5777 1.7250 0.1188 0.3436 0.1181 294 LEU A CD1 1988 C CD2 . LEU A 294 ? 1.7155 1.4589 1.5966 0.1150 0.3516 0.1124 294 LEU A CD2 1989 N N . THR A 295 ? 1.7781 1.5201 1.6646 0.1219 0.3466 0.1203 295 THR A N 1990 C CA . THR A 295 ? 1.7523 1.4982 1.6435 0.1177 0.3363 0.1295 295 THR A CA 1991 C C . THR A 295 ? 1.7548 1.4938 1.6461 0.1126 0.3256 0.1284 295 THR A C 1992 O O . THR A 295 ? 1.7773 1.4995 1.6551 0.1135 0.3231 0.1194 295 THR A O 1993 C CB . THR A 295 ? 1.7921 1.5342 1.6735 0.1167 0.3309 0.1336 295 THR A CB 1994 O OG1 . THR A 295 ? 1.6923 1.4335 1.5745 0.1079 0.3127 0.1415 295 THR A OG1 1995 C CG2 . THR A 295 ? 1.8949 1.6199 1.7520 0.1203 0.3368 0.1227 295 THR A CG2 1996 N N . ALA A 296 ? 1.6864 1.4368 1.5938 0.1090 0.3229 0.1389 296 ALA A N 1997 C CA . ALA A 296 ? 1.6135 1.3580 1.5242 0.1049 0.3160 0.1401 296 ALA A CA 1998 C C . ALA A 296 ? 1.5231 1.2743 1.4513 0.0957 0.3054 0.1548 296 ALA A C 1999 O O . ALA A 296 ? 1.2711 1.0421 1.2191 0.0947 0.3087 0.1691 296 ALA A O 2000 C CB . ALA A 296 ? 1.6799 1.4292 1.5905 0.1095 0.3249 0.1387 296 ALA A CB 2001 N N . GLN A 297 ? 1.6228 1.3567 1.5473 0.0898 0.2946 0.1528 297 GLN A N 2002 C CA . GLN A 297 ? 1.7490 1.4821 1.6898 0.0772 0.2805 0.1659 297 GLN A CA 2003 C C . GLN A 297 ? 1.8646 1.6025 1.8198 0.0760 0.2841 0.1771 297 GLN A C 2004 O O . GLN A 297 ? 1.9298 1.6584 1.8739 0.0832 0.2899 0.1704 297 GLN A O 2005 C CB . GLN A 297 ? 1.6959 1.3943 1.6146 0.0692 0.2638 0.1547 297 GLN A CB 2006 C CG . GLN A 297 ? 1.9376 1.6278 1.8707 0.0516 0.2440 0.1669 297 GLN A CG 2007 C CD . GLN A 297 ? 2.2132 1.8597 2.1125 0.0418 0.2256 0.1528 297 GLN A CD 2008 O OE1 . GLN A 297 ? 2.1315 1.7609 1.9975 0.0482 0.2285 0.1373 297 GLN A OE1 2009 N NE2 . GLN A 297 ? 2.3738 1.9968 2.2766 0.0257 0.2075 0.1578 297 GLN A NE2 2010 N N . THR A 298 ? 1.8364 1.5904 1.8191 0.0664 0.2799 0.1974 298 THR A N 2011 C CA . THR A 298 ? 1.6970 1.4565 1.6919 0.0654 0.2860 0.2117 298 THR A CA 2012 C C . THR A 298 ? 1.7231 1.4676 1.7333 0.0498 0.2685 0.2221 298 THR A C 2013 O O . THR A 298 ? 1.7794 1.5055 1.7817 0.0509 0.2677 0.2213 298 THR A O 2014 C CB . THR A 298 ? 1.6241 1.4148 1.6373 0.0711 0.3059 0.2303 298 THR A CB 2015 O OG1 . THR A 298 ? 1.6719 1.4690 1.6693 0.0836 0.3203 0.2192 298 THR A OG1 2016 C CG2 . THR A 298 ? 1.4822 1.2715 1.4871 0.0749 0.3173 0.2391 298 THR A CG2 2017 N N . LEU A 299 ? 1.6548 1.4054 1.6882 0.0343 0.2525 0.2336 299 LEU A N 2018 C CA . LEU A 299 ? 1.8484 1.5862 1.9027 0.0155 0.2350 0.2485 299 LEU A CA 2019 C C . LEU A 299 ? 1.8875 1.6439 1.9675 0.0161 0.2493 0.2726 299 LEU A C 2020 O O . LEU A 299 ? 1.8976 1.6358 1.9597 0.0232 0.2559 0.2684 299 LEU A O 2021 C CB . LEU A 299 ? 1.9216 1.6071 1.9434 0.0108 0.2198 0.2284 299 LEU A CB 2022 C CG . LEU A 299 ? 1.7841 1.4513 1.8220 -0.0005 0.2127 0.2429 299 LEU A CG 2023 C CD1 . LEU A 299 ? 1.6338 1.2924 1.6959 -0.0282 0.1859 0.2570 299 LEU A CD1 2024 C CD2 . LEU A 299 ? 1.8516 1.4738 1.8586 0.0092 0.2144 0.2254 299 LEU A CD2 2025 N N . LEU A 300 ? 1.8543 1.6466 1.9783 0.0085 0.2537 0.3007 300 LEU A N 2026 C CA . LEU A 300 ? 1.7195 1.5333 1.8656 0.0119 0.2744 0.3265 300 LEU A CA 2027 C C . LEU A 300 ? 1.6724 1.4823 1.8553 -0.0104 0.2575 0.3498 300 LEU A C 2028 O O . LEU A 300 ? 1.6686 1.5047 1.8987 -0.0255 0.2476 0.3721 300 LEU A O 2029 C CB . LEU A 300 ? 1.5423 1.4004 1.7157 0.0232 0.3006 0.3462 300 LEU A CB 2030 C CG . LEU A 300 ? 1.4760 1.3426 1.6404 0.0325 0.3009 0.3303 300 LEU A CG 2031 C CD1 . LEU A 300 ? 1.4436 1.3356 1.6583 0.0167 0.2816 0.3498 300 LEU A CD1 2032 C CD2 . LEU A 300 ? 1.4581 1.3400 1.6066 0.0557 0.3359 0.3295 300 LEU A CD2 2033 N N . MET A 301 ? 1.6782 1.4561 1.8439 -0.0134 0.2528 0.3471 301 MET A N 2034 C CA . MET A 301 ? 1.7213 1.5009 1.9256 -0.0318 0.2460 0.3765 301 MET A CA 2035 C C . MET A 301 ? 1.7876 1.6036 2.0076 -0.0194 0.2791 0.4036 301 MET A C 2036 O O . MET A 301 ? 1.8129 1.6392 2.0010 0.0027 0.3031 0.3932 301 MET A O 2037 C CB . MET A 301 ? 1.7289 1.4592 1.9114 -0.0380 0.2320 0.3679 301 MET A CB 2038 C CG . MET A 301 ? 1.8197 1.5150 2.0143 -0.0648 0.1979 0.3644 301 MET A CG 2039 S SD . MET A 301 ? 2.0109 1.6614 2.1499 -0.0590 0.1808 0.3190 301 MET A SD 2040 C CE . MET A 301 ? 1.8333 1.4793 1.9299 -0.0247 0.2088 0.2993 301 MET A CE 2041 N N . ASP A 302 ? 1.8225 1.6544 2.0891 -0.0348 0.2803 0.4386 302 ASP A N 2042 C CA . ASP A 302 ? 1.8504 1.7124 2.1310 -0.0242 0.3148 0.4696 302 ASP A CA 2043 C C . ASP A 302 ? 1.7615 1.6715 2.0671 -0.0105 0.3435 0.4843 302 ASP A C 2044 O O . ASP A 302 ? 1.6740 1.5857 1.9465 0.0080 0.3543 0.4604 302 ASP A O 2045 C CB . ASP A 302 ? 1.9746 1.8124 2.1942 -0.0049 0.3313 0.4564 302 ASP A CB 2046 C CG . ASP A 302 ? 1.9859 1.7756 2.1782 -0.0111 0.3054 0.4375 302 ASP A CG 2047 O OD1 . ASP A 302 ? 1.9958 1.7620 2.2099 -0.0308 0.2772 0.4338 302 ASP A OD1 2048 O OD2 . ASP A 302 ? 1.9673 1.7408 2.1145 0.0044 0.3139 0.4273 302 ASP A OD2 2049 N N . LEU A 303 ? 1.6171 1.5650 1.9840 -0.0185 0.3583 0.5259 303 LEU A N 2050 C CA . LEU A 303 ? 1.5609 1.5557 1.9612 -0.0027 0.3919 0.5472 303 LEU A CA 2051 C C . LEU A 303 ? 1.6050 1.5948 1.9509 0.0260 0.4371 0.5449 303 LEU A C 2052 O O . LEU A 303 ? 1.6832 1.6510 1.9939 0.0272 0.4454 0.5492 303 LEU A O 2053 C CB . LEU A 303 ? 1.5583 1.5980 2.0474 -0.0192 0.3974 0.5977 303 LEU A CB 2054 C CG . LEU A 303 ? 1.5544 1.6123 2.1151 -0.0513 0.3545 0.6131 303 LEU A CG 2055 C CD1 . LEU A 303 ? 1.5274 1.5360 2.0692 -0.0794 0.3101 0.5969 303 LEU A CD1 2056 C CD2 . LEU A 303 ? 1.6348 1.7525 2.2908 -0.0593 0.3742 0.6706 303 LEU A CD2 2057 N N . GLY A 304 ? 1.6768 1.6834 2.0128 0.0485 0.4658 0.5394 304 GLY A N 2058 C CA . GLY A 304 ? 1.7901 1.7882 2.0724 0.0748 0.5122 0.5403 304 GLY A CA 2059 C C . GLY A 304 ? 1.8144 1.8029 2.0542 0.0977 0.5301 0.5125 304 GLY A C 2060 O O . GLY A 304 ? 1.8024 1.8064 2.0745 0.0968 0.5160 0.5039 304 GLY A O 2061 N N . GLN A 305 ? 1.8970 1.8569 2.0614 0.1172 0.5607 0.4999 305 GLN A N 2062 C CA . GLN A 305 ? 1.8770 1.8141 1.9850 0.1377 0.5775 0.4695 305 GLN A CA 2063 C C . GLN A 305 ? 1.7692 1.6610 1.7961 0.1345 0.5555 0.4339 305 GLN A C 2064 O O . GLN A 305 ? 1.9044 1.7796 1.8989 0.1281 0.5505 0.4395 305 GLN A O 2065 C CB . GLN A 305 ? 2.1368 2.0718 2.2182 0.1638 0.6352 0.4850 305 GLN A CB 2066 C CG . GLN A 305 ? 2.2693 2.2309 2.3990 0.1815 0.6613 0.4943 305 GLN A CG 2067 C CD . GLN A 305 ? 2.2838 2.2349 2.3814 0.2115 0.7245 0.5080 305 GLN A CD 2068 O OE1 . GLN A 305 ? 2.3927 2.3623 2.5120 0.2175 0.7582 0.5437 305 GLN A OE1 2069 N NE2 . GLN A 305 ? 2.2478 2.1660 2.2930 0.2311 0.7433 0.4804 305 GLN A NE2 2070 N N . PHE A 306 ? 1.7116 1.5859 1.7103 0.1386 0.5418 0.4004 306 PHE A N 2071 C CA . PHE A 306 ? 1.8252 1.6638 1.7618 0.1334 0.5158 0.3683 306 PHE A CA 2072 C C . PHE A 306 ? 1.8365 1.6497 1.7208 0.1470 0.5276 0.3396 306 PHE A C 2073 O O . PHE A 306 ? 1.8001 1.6243 1.7123 0.1533 0.5317 0.3326 306 PHE A O 2074 C CB . PHE A 306 ? 1.8923 1.7348 1.8621 0.1156 0.4711 0.3556 306 PHE A CB 2075 C CG . PHE A 306 ? 1.8541 1.7139 1.8770 0.0991 0.4549 0.3808 306 PHE A CG 2076 C CD1 . PHE A 306 ? 1.8023 1.6455 1.8055 0.0911 0.4430 0.3872 306 PHE A CD1 2077 C CD2 . PHE A 306 ? 1.9196 1.8102 2.0132 0.0898 0.4481 0.3989 306 PHE A CD2 2078 C CE1 . PHE A 306 ? 1.8423 1.6950 1.8938 0.0750 0.4279 0.4097 306 PHE A CE1 2079 C CE2 . PHE A 306 ? 1.7377 1.6388 1.8788 0.0708 0.4296 0.4212 306 PHE A CE2 2080 C CZ . PHE A 306 ? 1.7777 1.6576 1.8969 0.0636 0.4207 0.4257 306 PHE A CZ 2081 N N . LEU A 307 ? 1.8455 1.6224 1.6528 0.1498 0.5301 0.3240 307 LEU A N 2082 C CA . LEU A 307 ? 1.8927 1.6373 1.6434 0.1575 0.5345 0.2946 307 LEU A CA 2083 C C . LEU A 307 ? 1.9930 1.7350 1.7516 0.1457 0.4951 0.2695 307 LEU A C 2084 O O . LEU A 307 ? 2.1362 1.8798 1.8984 0.1332 0.4655 0.2683 307 LEU A O 2085 C CB . LEU A 307 ? 1.9102 1.6142 1.5717 0.1598 0.5443 0.2881 307 LEU A CB 2086 C CG . LEU A 307 ? 1.9510 1.6138 1.5445 0.1584 0.5331 0.2550 307 LEU A CG 2087 C CD1 . LEU A 307 ? 2.0239 1.6724 1.6113 0.1745 0.5641 0.2435 307 LEU A CD1 2088 C CD2 . LEU A 307 ? 2.0720 1.6948 1.5751 0.1546 0.5324 0.2519 307 LEU A CD2 2089 N N . LEU A 308 ? 1.9739 1.7112 1.7367 0.1510 0.4969 0.2513 308 LEU A N 2090 C CA . LEU A 308 ? 1.9074 1.6298 1.6515 0.1421 0.4674 0.2251 308 LEU A CA 2091 C C . LEU A 308 ? 1.9809 1.6638 1.6590 0.1483 0.4814 0.2049 308 LEU A C 2092 O O . LEU A 308 ? 1.9777 1.6463 1.6360 0.1628 0.5163 0.2085 308 LEU A O 2093 C CB . LEU A 308 ? 1.7700 1.5150 1.5696 0.1384 0.4501 0.2196 308 LEU A CB 2094 C CG . LEU A 308 ? 1.9113 1.6575 1.7251 0.1490 0.4673 0.2140 308 LEU A CG 2095 C CD1 . LEU A 308 ? 1.9956 1.7579 1.8485 0.1415 0.4420 0.2061 308 LEU A CD1 2096 C CD2 . LEU A 308 ? 1.8574 1.6235 1.7046 0.1617 0.4984 0.2387 308 LEU A CD2 2097 N N . PHE A 309 ? 1.9979 1.6615 1.6436 0.1371 0.4547 0.1851 309 PHE A N 2098 C CA . PHE A 309 ? 2.1297 1.7476 1.6993 0.1356 0.4584 0.1663 309 PHE A CA 2099 C C . PHE A 309 ? 2.1913 1.8023 1.7497 0.1189 0.4203 0.1503 309 PHE A C 2100 O O . PHE A 309 ? 2.3202 1.9612 1.9312 0.1127 0.3972 0.1528 309 PHE A O 2101 C CB . PHE A 309 ? 2.1148 1.7103 1.6246 0.1366 0.4701 0.1764 309 PHE A CB 2102 C CG . PHE A 309 ? 2.1641 1.7785 1.6850 0.1245 0.4415 0.1901 309 PHE A CG 2103 C CD1 . PHE A 309 ? 2.1141 1.7677 1.7008 0.1256 0.4397 0.2113 309 PHE A CD1 2104 C CD2 . PHE A 309 ? 2.2738 1.8659 1.7427 0.1109 0.4134 0.1829 309 PHE A CD2 2105 C CE1 . PHE A 309 ? 2.1709 1.8368 1.7691 0.1161 0.4151 0.2243 309 PHE A CE1 2106 C CE2 . PHE A 309 ? 2.3148 1.9255 1.7995 0.1021 0.3875 0.1989 309 PHE A CE2 2107 C CZ . PHE A 309 ? 2.2645 1.9103 1.8135 0.1060 0.3903 0.2191 309 PHE A CZ 2108 N N . CYS A 310 ? 2.0985 1.6680 1.5865 0.1112 0.4137 0.1357 310 CYS A N 2109 C CA . CYS A 310 ? 2.1004 1.6649 1.5827 0.0936 0.3771 0.1232 310 CYS A CA 2110 C C . CYS A 310 ? 2.1314 1.6787 1.5591 0.0800 0.3529 0.1283 310 CYS A C 2111 O O . CYS A 310 ? 2.1340 1.6375 1.4823 0.0791 0.3637 0.1227 310 CYS A O 2112 C CB . CYS A 310 ? 2.2223 1.7526 1.6781 0.0919 0.3839 0.1011 310 CYS A CB 2113 S SG . CYS A 310 ? 2.4159 1.9257 1.8494 0.0670 0.3433 0.0842 310 CYS A SG 2114 N N . HIS A 311 ? 2.1648 1.7445 1.6334 0.0709 0.3215 0.1403 311 HIS A N 2115 C CA . HIS A 311 ? 2.3993 1.9732 1.8307 0.0595 0.2957 0.1533 311 HIS A CA 2116 C C . HIS A 311 ? 2.5434 2.0800 1.9075 0.0401 0.2682 0.1407 311 HIS A C 2117 O O . HIS A 311 ? 2.7743 2.2856 2.0719 0.0316 0.2557 0.1474 311 HIS A O 2118 C CB . HIS A 311 ? 2.3579 1.9763 1.8597 0.0572 0.2700 0.1714 311 HIS A CB 2119 C CG . HIS A 311 ? 2.4261 2.0478 1.9093 0.0558 0.2595 0.1945 311 HIS A CG 2120 N ND1 . HIS A 311 ? 2.4296 2.0197 1.8337 0.0453 0.2462 0.1984 311 HIS A ND1 2121 C CD2 . HIS A 311 ? 2.4176 2.0666 1.9485 0.0627 0.2592 0.2155 311 HIS A CD2 2122 C CE1 . HIS A 311 ? 2.4237 2.0255 1.8301 0.0469 0.2392 0.2231 311 HIS A CE1 2123 N NE2 . HIS A 311 ? 2.3888 2.0258 1.8740 0.0575 0.2473 0.2338 311 HIS A NE2 2124 N N . ILE A 312 ? 2.4625 1.9947 1.8428 0.0313 0.2566 0.1239 312 ILE A N 2125 C CA . ILE A 312 ? 2.4271 1.9290 1.7587 0.0076 0.2223 0.1136 312 ILE A CA 2126 C C . ILE A 312 ? 2.5101 1.9457 1.7252 0.0018 0.2302 0.1017 312 ILE A C 2127 O O . ILE A 312 ? 2.4613 1.8683 1.6387 0.0194 0.2725 0.0936 312 ILE A O 2128 C CB . ILE A 312 ? 2.3525 1.8553 1.7206 0.0010 0.2184 0.0970 312 ILE A CB 2129 C CG1 . ILE A 312 ? 2.1526 1.6195 1.4912 0.0161 0.2608 0.0780 312 ILE A CG1 2130 C CG2 . ILE A 312 ? 2.0857 1.6504 1.5593 0.0062 0.2099 0.1101 312 ILE A CG2 2131 C CD1 . ILE A 312 ? 2.0890 1.5525 1.4606 0.0114 0.2609 0.0635 312 ILE A CD1 2132 N N . SER A 313 ? 2.5952 2.0061 1.7540 -0.0225 0.1894 0.1023 313 SER A N 2133 C CA . SER A 313 ? 2.8073 2.1527 1.8419 -0.0310 0.1887 0.0952 313 SER A CA 2134 C C . SER A 313 ? 2.8897 2.1576 1.8289 -0.0261 0.2229 0.0660 313 SER A C 2135 O O . SER A 313 ? 2.7841 2.0186 1.6601 -0.0080 0.2628 0.0653 313 SER A O 2136 C CB . SER A 313 ? 2.8508 2.1878 1.8498 -0.0630 0.1283 0.1029 313 SER A CB 2137 O OG . SER A 313 ? 2.8000 2.1930 1.8556 -0.0619 0.1054 0.1345 313 SER A OG 2138 N N . SER A 314 ? 2.9466 2.1831 1.8745 -0.0417 0.2087 0.0436 314 SER A N 2139 C CA . SER A 314 ? 3.1500 2.2998 1.9759 -0.0405 0.2351 0.0141 314 SER A CA 2140 C C . SER A 314 ? 3.1335 2.2807 1.9893 -0.0077 0.2963 0.0058 314 SER A C 2141 O O . SER A 314 ? 3.3070 2.3826 2.0853 0.0006 0.3281 -0.0166 314 SER A O 2142 C CB . SER A 314 ? 3.2453 2.3539 2.0415 -0.0735 0.1931 -0.0062 314 SER A CB 2143 O OG . SER A 314 ? 3.0931 2.2718 1.9937 -0.0909 0.1494 0.0107 314 SER A OG 2144 N N . HIS A 315 ? 2.9547 2.1772 1.9213 0.0110 0.3117 0.0248 315 HIS A N 2145 C CA . HIS A 315 ? 2.9240 2.1580 1.9342 0.0412 0.3640 0.0242 315 HIS A CA 2146 C C . HIS A 315 ? 3.0230 2.2624 2.0142 0.0658 0.4054 0.0407 315 HIS A C 2147 O O . HIS A 315 ? 3.0473 2.2896 2.0621 0.0919 0.4528 0.0433 315 HIS A O 2148 C CB . HIS A 315 ? 2.7841 2.0939 1.9193 0.0457 0.3556 0.0370 315 HIS A CB 2149 C CG . HIS A 315 ? 2.6990 2.0111 1.8667 0.0256 0.3236 0.0253 315 HIS A CG 2150 N ND1 . HIS A 315 ? 2.7776 2.1157 2.0173 0.0348 0.3368 0.0231 315 HIS A ND1 2151 C CD2 . HIS A 315 ? 2.7138 2.0081 1.8554 -0.0043 0.2783 0.0182 315 HIS A CD2 2152 C CE1 . HIS A 315 ? 2.7171 2.0520 1.9730 0.0126 0.3046 0.0150 315 HIS A CE1 2153 N NE2 . HIS A 315 ? 2.7455 2.0559 1.9468 -0.0120 0.2680 0.0124 315 HIS A NE2 2154 N N . GLN A 316 ? 3.0098 2.2541 1.9643 0.0569 0.3865 0.0554 316 GLN A N 2155 C CA . GLN A 316 ? 3.0621 2.3181 2.0043 0.0765 0.4207 0.0767 316 GLN A CA 2156 C C . GLN A 316 ? 3.1343 2.3452 2.0269 0.1035 0.4831 0.0697 316 GLN A C 2157 O O . GLN A 316 ? 3.1705 2.4197 2.1234 0.1271 0.5218 0.0883 316 GLN A O 2158 C CB . GLN A 316 ? 3.1628 2.3981 2.0283 0.0597 0.3918 0.0864 316 GLN A CB 2159 C CG . GLN A 316 ? 3.3031 2.5549 2.1594 0.0762 0.4213 0.1134 316 GLN A CG 2160 C CD . GLN A 316 ? 3.5335 2.7543 2.2978 0.0591 0.3927 0.1223 316 GLN A CD 2161 O OE1 . GLN A 316 ? 3.7335 2.9772 2.5167 0.0363 0.3384 0.1295 316 GLN A OE1 2162 N NE2 . GLN A 316 ? 3.5977 2.7664 2.2619 0.0709 0.4300 0.1244 316 GLN A NE2 2163 N N . HIS A 317 ? 3.2031 2.3310 1.9874 0.0998 0.4928 0.0437 317 HIS A N 2164 C CA . HIS A 317 ? 3.2261 2.3033 1.9583 0.1283 0.5559 0.0362 317 HIS A CA 2165 C C . HIS A 317 ? 3.2331 2.3131 2.0247 0.1421 0.5776 0.0242 317 HIS A C 2166 O O . HIS A 317 ? 3.4868 2.5696 2.3025 0.1726 0.6319 0.0330 317 HIS A O 2167 C CB . HIS A 317 ? 3.4924 2.4673 2.0692 0.1206 0.5616 0.0123 317 HIS A CB 2168 C CG . HIS A 317 ? 3.7502 2.7139 2.2543 0.1185 0.5627 0.0291 317 HIS A CG 2169 N ND1 . HIS A 317 ? 3.7290 2.7520 2.2765 0.0998 0.5169 0.0523 317 HIS A ND1 2170 C CD2 . HIS A 317 ? 4.0673 2.9673 2.4588 0.1345 0.6068 0.0286 317 HIS A CD2 2171 C CE1 . HIS A 317 ? 4.0455 3.0425 2.5105 0.1027 0.5296 0.0661 317 HIS A CE1 2172 N NE2 . HIS A 317 ? 4.2739 3.1963 2.6408 0.1233 0.5846 0.0520 317 HIS A NE2 2173 N N . ASP A 318 ? 3.2297 2.3114 2.0493 0.1202 0.5360 0.0075 318 ASP A N 2174 C CA . ASP A 318 ? 3.3049 2.3904 2.1841 0.1312 0.5522 -0.0022 318 ASP A CA 2175 C C . ASP A 318 ? 3.1818 2.3422 2.1763 0.1586 0.5852 0.0241 318 ASP A C 2176 O O . ASP A 318 ? 3.1912 2.3570 2.2360 0.1726 0.6049 0.0212 318 ASP A O 2177 C CB . ASP A 318 ? 3.3041 2.3981 2.2144 0.1009 0.4980 -0.0161 318 ASP A CB 2178 C CG . ASP A 318 ? 3.2521 2.2571 2.0493 0.0752 0.4726 -0.0457 318 ASP A CG 2179 O OD1 . ASP A 318 ? 3.1913 2.1324 1.8757 0.0737 0.4822 -0.0546 318 ASP A OD1 2180 O OD2 . ASP A 318 ? 3.0835 2.0813 1.9044 0.0549 0.4419 -0.0590 318 ASP A OD2 2181 N N . GLY A 319 ? 2.9047 2.1202 1.9388 0.1642 0.5882 0.0510 319 GLY A N 2182 C CA . GLY A 319 ? 2.5989 1.8695 1.7158 0.1906 0.6268 0.0783 319 GLY A CA 2183 C C . GLY A 319 ? 2.4999 1.8306 1.7294 0.1937 0.6170 0.0869 319 GLY A C 2184 O O . GLY A 319 ? 2.3195 1.6641 1.5960 0.2172 0.6540 0.0978 319 GLY A O 2185 N N . MET A 320 ? 2.5171 1.8818 1.7882 0.1705 0.5677 0.0831 320 MET A N 2186 C CA . MET A 320 ? 2.4815 1.9102 1.8572 0.1722 0.5560 0.0961 320 MET A CA 2187 C C . MET A 320 ? 2.3589 1.8458 1.7881 0.1700 0.5454 0.1217 320 MET A C 2188 O O . MET A 320 ? 2.3097 1.8093 1.7333 0.1521 0.5109 0.1229 320 MET A O 2189 C CB . MET A 320 ? 2.5119 1.9427 1.9103 0.1543 0.5198 0.0791 320 MET A CB 2190 C CG . MET A 320 ? 2.4892 1.9438 1.8995 0.1295 0.4715 0.0774 320 MET A CG 2191 S SD . MET A 320 ? 2.2473 1.7658 1.7600 0.1244 0.4466 0.0858 320 MET A SD 2192 C CE . MET A 320 ? 2.1703 1.6642 1.6910 0.1274 0.4558 0.0700 320 MET A CE 2193 N N . GLU A 321 ? 2.2034 1.7217 1.6833 0.1889 0.5773 0.1444 321 GLU A N 2194 C CA . GLU A 321 ? 2.0473 1.6149 1.5784 0.1892 0.5765 0.1723 321 GLU A CA 2195 C C . GLU A 321 ? 2.0236 1.6189 1.6089 0.2111 0.6168 0.1971 321 GLU A C 2196 O O . GLU A 321 ? 2.0993 1.6646 1.6573 0.2309 0.6567 0.1953 321 GLU A O 2197 C CB . GLU A 321 ? 2.0721 1.6188 1.5399 0.1839 0.5774 0.1777 321 GLU A CB 2198 C CG . GLU A 321 ? 2.3724 1.8484 1.7317 0.1867 0.5940 0.1570 321 GLU A CG 2199 C CD . GLU A 321 ? 2.6305 2.0851 1.9242 0.1879 0.6083 0.1691 321 GLU A CD 2200 O OE1 . GLU A 321 ? 2.6168 2.1062 1.9508 0.1985 0.6316 0.1979 321 GLU A OE1 2201 O OE2 . GLU A 321 ? 3.0520 2.4535 2.2514 0.1770 0.5954 0.1512 321 GLU A OE2 2202 N N . ALA A 322 ? 1.9466 1.5980 1.6113 0.2071 0.6055 0.2213 322 ALA A N 2203 C CA . ALA A 322 ? 1.8866 1.5730 1.6083 0.2231 0.6392 0.2538 322 ALA A CA 2204 C C . ALA A 322 ? 1.8694 1.6050 1.6533 0.2081 0.6151 0.2778 322 ALA A C 2205 O O . ALA A 322 ? 1.5719 1.3114 1.3543 0.1884 0.5746 0.2674 322 ALA A O 2206 C CB . ALA A 322 ? 1.6411 1.3440 1.4169 0.2387 0.6567 0.2601 322 ALA A CB 2207 N N . TYR A 323 ? 1.9319 1.7026 1.7709 0.2182 0.6421 0.3116 323 TYR A N 2208 C CA . TYR A 323 ? 1.9565 1.7696 1.8548 0.2038 0.6246 0.3389 323 TYR A CA 2209 C C . TYR A 323 ? 1.8120 1.6691 1.7965 0.1917 0.5935 0.3486 323 TYR A C 2210 O O . TYR A 323 ? 1.7381 1.6106 1.7604 0.2025 0.6037 0.3536 323 TYR A O 2211 C CB . TYR A 323 ? 2.0397 1.8695 1.9558 0.2178 0.6693 0.3747 323 TYR A CB 2212 C CG . TYR A 323 ? 2.2290 2.0226 2.0644 0.2217 0.6914 0.3750 323 TYR A CG 2213 C CD1 . TYR A 323 ? 2.3347 2.1078 2.1224 0.2030 0.6572 0.3612 323 TYR A CD1 2214 C CD2 . TYR A 323 ? 2.3732 2.1548 2.1830 0.2453 0.7482 0.3935 323 TYR A CD2 2215 C CE1 . TYR A 323 ? 2.4171 2.1584 2.1304 0.2055 0.6742 0.3651 323 TYR A CE1 2216 C CE2 . TYR A 323 ? 2.5008 2.2464 2.2296 0.2486 0.7690 0.3954 323 TYR A CE2 2217 C CZ . TYR A 323 ? 2.5864 2.3123 2.2660 0.2275 0.7294 0.3813 323 TYR A CZ 2218 O OH . TYR A 323 ? 2.9350 2.6253 2.5313 0.2296 0.7464 0.3856 323 TYR A OH 2219 N N . VAL A 324 ? 1.6826 1.5540 1.6914 0.1697 0.5551 0.3507 324 VAL A N 2220 C CA . VAL A 324 ? 1.5255 1.4335 1.6087 0.1547 0.5250 0.3641 324 VAL A CA 2221 C C . VAL A 324 ? 1.5799 1.5178 1.7147 0.1433 0.5243 0.3987 324 VAL A C 2222 O O . VAL A 324 ? 1.6469 1.5699 1.7545 0.1346 0.5178 0.3989 324 VAL A O 2223 C CB . VAL A 324 ? 1.4477 1.3398 1.5149 0.1357 0.4802 0.3391 324 VAL A CB 2224 C CG1 . VAL A 324 ? 1.3215 1.2415 1.4520 0.1190 0.4497 0.3518 324 VAL A CG1 2225 C CG2 . VAL A 324 ? 1.6287 1.4907 1.6450 0.1423 0.4756 0.3050 324 VAL A CG2 2226 N N . LYS A 325 ? 1.6262 1.6072 1.8390 0.1416 0.5281 0.4304 325 LYS A N 2227 C CA . LYS A 325 ? 1.6405 1.6510 1.9092 0.1261 0.5227 0.4653 325 LYS A CA 2228 C C . LYS A 325 ? 1.5413 1.5668 1.8593 0.0979 0.4724 0.4686 325 LYS A C 2229 O O . LYS A 325 ? 1.5125 1.5294 1.8227 0.0933 0.4461 0.4464 325 LYS A O 2230 C CB . LYS A 325 ? 1.7743 1.8214 2.0933 0.1432 0.5696 0.5067 325 LYS A CB 2231 C CG . LYS A 325 ? 1.9185 2.0223 2.3403 0.1387 0.5658 0.5446 325 LYS A CG 2232 C CD . LYS A 325 ? 2.0362 2.1762 2.5086 0.1557 0.6170 0.5902 325 LYS A CD 2233 C CE . LYS A 325 ? 2.0031 2.1534 2.4955 0.1385 0.6169 0.6171 325 LYS A CE 2234 N NZ . LYS A 325 ? 1.9661 2.1687 2.5650 0.1113 0.5862 0.6570 325 LYS A NZ 2235 N N . VAL A 326 ? 1.4702 1.5110 1.8302 0.0779 0.4585 0.4944 326 VAL A N 2236 C CA . VAL A 326 ? 1.4664 1.5067 1.8578 0.0481 0.4085 0.4934 326 VAL A CA 2237 C C . VAL A 326 ? 1.4327 1.5056 1.8991 0.0268 0.4007 0.5366 326 VAL A C 2238 O O . VAL A 326 ? 1.4858 1.5377 1.9406 0.0121 0.3892 0.5385 326 VAL A O 2239 C CB . VAL A 326 ? 1.5271 1.5141 1.8487 0.0395 0.3799 0.4526 326 VAL A CB 2240 C CG1 . VAL A 326 ? 1.5220 1.4834 1.7947 0.0476 0.3991 0.4477 326 VAL A CG1 2241 C CG2 . VAL A 326 ? 1.6371 1.6109 1.9804 0.0094 0.3332 0.4511 326 VAL A CG2 2242 N N . ASP A 327 ? 1.4208 1.5458 1.9687 0.0245 0.4066 0.5742 327 ASP A N 2243 C CA . ASP A 327 ? 1.6108 1.7690 2.2395 -0.0023 0.3903 0.6172 327 ASP A CA 2244 C C . ASP A 327 ? 1.4555 1.6189 2.1230 -0.0349 0.3317 0.6176 327 ASP A C 2245 O O . ASP A 327 ? 1.3881 1.5380 2.0258 -0.0312 0.3132 0.5908 327 ASP A O 2246 C CB . ASP A 327 ? 2.0137 2.2296 2.7169 0.0132 0.4379 0.6690 327 ASP A CB 2247 C CG . ASP A 327 ? 2.5184 2.7373 3.2386 0.0044 0.4570 0.6991 327 ASP A CG 2248 O OD1 . ASP A 327 ? 2.4488 2.6331 3.0968 0.0218 0.4871 0.6827 327 ASP A OD1 2249 O OD2 . ASP A 327 ? 2.6847 2.9407 3.4913 -0.0215 0.4404 0.7414 327 ASP A OD2 2250 N N . SER A 328 ? 1.5511 1.7279 2.2773 -0.0681 0.3016 0.6468 328 SER A N 2251 C CA . SER A 328 ? 1.6611 1.8265 2.4069 -0.1055 0.2393 0.6431 328 SER A CA 2252 C C . SER A 328 ? 1.7614 1.9786 2.5748 -0.1108 0.2216 0.6687 328 SER A C 2253 O O . SER A 328 ? 1.8698 2.1512 2.7782 -0.1117 0.2367 0.7196 328 SER A O 2254 C CB . SER A 328 ? 1.7421 1.9058 2.5364 -0.1423 0.2123 0.6716 328 SER A CB 2255 O OG . SER A 328 ? 1.8383 1.9454 2.5694 -0.1435 0.2158 0.6470 328 SER A OG 2256 N N . CYS A 329 ? 1.8732 2.0644 2.6414 -0.1146 0.1894 0.6369 329 CYS A N 2257 C CA . CYS A 329 ? 1.9807 2.2160 2.8087 -0.1253 0.1614 0.6618 329 CYS A CA 2258 C C . CYS A 329 ? 2.1118 2.3505 2.9894 -0.1743 0.1027 0.6857 329 CYS A C 2259 O O . CYS A 329 ? 2.0813 2.2647 2.9136 -0.1983 0.0768 0.6637 329 CYS A O 2260 C CB . CYS A 329 ? 2.1380 2.3387 2.8929 -0.1150 0.1451 0.6203 329 CYS A CB 2261 S SG . CYS A 329 ? 2.6028 2.7822 3.2839 -0.0638 0.2067 0.5837 329 CYS A SG 2262 N N . PRO A 330 ? 2.2787 2.5820 3.2538 -0.1899 0.0813 0.7337 330 PRO A N 2263 C CA . PRO A 330 ? 2.4141 2.7068 3.4147 -0.2414 0.0115 0.7463 330 PRO A CA 2264 C C . PRO A 330 ? 2.5491 2.7940 3.4692 -0.2511 -0.0333 0.7062 330 PRO A C 2265 O O . PRO A 330 ? 2.3637 2.6169 3.2549 -0.2193 -0.0108 0.6911 330 PRO A O 2266 C CB . PRO A 330 ? 2.4733 2.8601 3.6152 -0.2534 0.0056 0.8172 330 PRO A CB 2267 C CG . PRO A 330 ? 2.3877 2.8273 3.5748 -0.2053 0.0830 0.8412 330 PRO A CG 2268 C CD . PRO A 330 ? 2.3581 2.7451 3.4325 -0.1657 0.1186 0.7842 330 PRO A CD 2269 N N . GLU A 331 ? 2.7220 2.9125 3.6022 -0.2945 -0.0939 0.6893 331 GLU A N 2270 C CA . GLU A 331 ? 2.8222 2.9484 3.6052 -0.3079 -0.1379 0.6460 331 GLU A CA 2271 C C . GLU A 331 ? 3.0026 3.1538 3.8261 -0.3463 -0.2043 0.6750 331 GLU A C 2272 O O . GLU A 331 ? 2.7091 2.8504 3.4864 -0.3400 -0.2221 0.6593 331 GLU A O 2273 C CB . GLU A 331 ? 2.8067 2.8354 3.4922 -0.3267 -0.1567 0.5987 331 GLU A CB 2274 C CG . GLU A 331 ? 2.8430 2.8636 3.5695 -0.3472 -0.1543 0.6165 331 GLU A CG 2275 C CD . GLU A 331 ? 2.7706 2.8648 3.6265 -0.3792 -0.1782 0.6816 331 GLU A CD 2276 O OE1 . GLU A 331 ? 2.6753 2.7623 3.5518 -0.4256 -0.2432 0.6972 331 GLU A OE1 2277 O OE2 . GLU A 331 ? 2.6471 2.8060 3.5840 -0.3583 -0.1313 0.7189 331 GLU A OE2 2278 N N . GLU A 332 ? 3.5140 3.6953 4.4218 -0.3881 -0.2432 0.7181 332 GLU A N 2279 C CA . GLU A 332 ? 3.8130 4.0350 4.7868 -0.4293 -0.3093 0.7597 332 GLU A CA 2280 C C . GLU A 332 ? 3.8501 4.1603 4.9766 -0.4466 -0.3067 0.8297 332 GLU A C 2281 O O . GLU A 332 ? 3.9552 4.2478 5.1102 -0.4935 -0.3498 0.8454 332 GLU A O 2282 C CB . GLU A 332 ? 3.6968 3.8284 4.5808 -0.4808 -0.3839 0.7274 332 GLU A CB 2283 C CG . GLU A 332 ? 3.4267 3.5822 4.3427 -0.5240 -0.4607 0.7586 332 GLU A CG 2284 C CD . GLU A 332 ? 3.3028 3.4159 4.1137 -0.5127 -0.4792 0.7222 332 GLU A CD 2285 O OE1 . GLU A 332 ? 3.0955 3.1988 3.8508 -0.4624 -0.4228 0.6900 332 GLU A OE1 2286 O OE2 . GLU A 332 ? 3.2469 3.3348 4.0291 -0.5564 -0.5526 0.7272 332 GLU A OE2 2287 N N . PRO A 333 ? 3.5904 3.9929 4.8153 -0.4082 -0.2539 0.8729 333 PRO A N 2288 C CA . PRO A 333 ? 3.2019 3.6846 4.5644 -0.4125 -0.2297 0.9359 333 PRO A CA 2289 C C . PRO A 333 ? 3.1292 3.6829 4.6156 -0.4580 -0.2920 1.0012 333 PRO A C 2290 O O . PRO A 333 ? 3.3399 3.9235 4.9132 -0.4915 -0.3084 1.0425 333 PRO A O 2291 C CB . PRO A 333 ? 2.9625 3.5043 4.3642 -0.3498 -0.1471 0.9506 333 PRO A CB 2292 C CG . PRO A 333 ? 3.0746 3.6057 4.4193 -0.3287 -0.1563 0.9257 333 PRO A CG 2293 C CD . PRO A 333 ? 3.4453 3.8826 4.6650 -0.3619 -0.2179 0.8705 333 PRO A CD 2294 N N . LYS A 377 ? 2.5370 1.7914 2.4356 -0.1413 0.2149 -0.2784 377 LYS A N 2295 C CA . LYS A 377 ? 2.6002 1.8968 2.4494 -0.1686 0.1864 -0.2814 377 LYS A CA 2296 C C . LYS A 377 ? 2.5464 1.9002 2.4285 -0.1845 0.1484 -0.2460 377 LYS A C 2297 O O . LYS A 377 ? 2.4002 1.8183 2.2797 -0.1820 0.1307 -0.2244 377 LYS A O 2298 C CB . LYS A 377 ? 2.6521 1.8930 2.4255 -0.2034 0.1867 -0.3264 377 LYS A CB 2299 C CG . LYS A 377 ? 2.5882 1.7578 2.3607 -0.2291 0.1860 -0.3476 377 LYS A CG 2300 C CD . LYS A 377 ? 2.7496 1.8439 2.4417 -0.2545 0.2007 -0.4007 377 LYS A CD 2301 C CE . LYS A 377 ? 2.7698 1.8938 2.3861 -0.2866 0.1764 -0.4161 377 LYS A CE 2302 N NZ . LYS A 377 ? 2.6432 1.8221 2.2440 -0.2608 0.1859 -0.4050 377 LYS A NZ 2303 N N . HIS A 378 ? 2.5021 1.8299 2.4163 -0.1996 0.1390 -0.2396 378 HIS A N 2304 C CA . HIS A 378 ? 2.2628 1.6380 2.2189 -0.2121 0.1091 -0.2038 378 HIS A CA 2305 C C . HIS A 378 ? 2.0974 1.5214 2.1081 -0.1763 0.1139 -0.1653 378 HIS A C 2306 O O . HIS A 378 ? 2.3491 1.7481 2.3931 -0.1498 0.1369 -0.1608 378 HIS A O 2307 C CB . HIS A 378 ? 2.3325 1.6582 2.3144 -0.2324 0.1060 -0.2066 378 HIS A CB 2308 C CG . HIS A 378 ? 2.6775 1.9503 2.6063 -0.2744 0.0971 -0.2444 378 HIS A CG 2309 N ND1 . HIS A 378 ? 2.7526 2.0578 2.6577 -0.3143 0.0619 -0.2420 378 HIS A ND1 2310 C CD2 . HIS A 378 ? 2.9695 2.1579 2.8621 -0.2840 0.1188 -0.2859 378 HIS A CD2 2311 C CE1 . HIS A 378 ? 2.9652 2.2092 2.8188 -0.3499 0.0592 -0.2811 378 HIS A CE1 2312 N NE2 . HIS A 378 ? 3.2388 2.4074 3.0811 -0.3320 0.0948 -0.3101 378 HIS A NE2 2313 N N . PRO A 379 ? 1.8623 1.3546 1.8837 -0.1760 0.0922 -0.1362 379 PRO A N 2314 C CA . PRO A 379 ? 1.7402 1.2822 1.7966 -0.1442 0.0955 -0.1036 379 PRO A CA 2315 C C . PRO A 379 ? 1.6928 1.2265 1.8049 -0.1248 0.1048 -0.0801 379 PRO A C 2316 O O . PRO A 379 ? 1.7576 1.2616 1.8911 -0.1392 0.1017 -0.0781 379 PRO A O 2317 C CB . PRO A 379 ? 1.7112 1.3137 1.7683 -0.1574 0.0685 -0.0792 379 PRO A CB 2318 C CG . PRO A 379 ? 1.7285 1.3151 1.7801 -0.1946 0.0496 -0.0865 379 PRO A CG 2319 C CD . PRO A 379 ? 1.7838 1.3072 1.7913 -0.2098 0.0613 -0.1292 379 PRO A CD 2320 N N . LYS A 380 ? 1.6936 1.2538 1.8284 -0.0944 0.1148 -0.0609 380 LYS A N 2321 C CA . LYS A 380 ? 1.9503 1.5048 2.1346 -0.0758 0.1228 -0.0369 380 LYS A CA 2322 C C . LYS A 380 ? 1.8934 1.4997 2.1028 -0.0714 0.1067 0.0001 380 LYS A C 2323 O O . LYS A 380 ? 1.7564 1.4059 1.9477 -0.0739 0.0944 0.0080 380 LYS A O 2324 C CB . LYS A 380 ? 2.3727 1.9199 2.5694 -0.0455 0.1450 -0.0384 380 LYS A CB 2325 C CG . LYS A 380 ? 2.7852 2.3071 3.0305 -0.0280 0.1585 -0.0221 380 LYS A CG 2326 C CD . LYS A 380 ? 2.9534 2.5092 3.2255 0.0013 0.1650 0.0013 380 LYS A CD 2327 C CE . LYS A 380 ? 2.7749 2.3251 3.0345 0.0174 0.1847 -0.0176 380 LYS A CE 2328 N NZ . LYS A 380 ? 2.8871 2.3838 3.1650 0.0285 0.2108 -0.0330 380 LYS A NZ 2329 N N . THR A 381 ? 1.8646 1.4647 2.1150 -0.0635 0.1091 0.0235 381 THR A N 2330 C CA . THR A 381 ? 1.7564 1.4022 2.0287 -0.0526 0.1002 0.0593 381 THR A CA 2331 C C . THR A 381 ? 1.6960 1.3537 1.9853 -0.0236 0.1106 0.0747 381 THR A C 2332 O O . THR A 381 ? 1.6449 1.2831 1.9666 -0.0117 0.1195 0.0871 381 THR A O 2333 C CB . THR A 381 ? 1.7324 1.3762 2.0345 -0.0671 0.0916 0.0814 381 THR A CB 2334 O OG1 . THR A 381 ? 1.8435 1.4692 2.1321 -0.0972 0.0820 0.0633 381 THR A OG1 2335 C CG2 . THR A 381 ? 1.5440 1.2410 1.8544 -0.0613 0.0818 0.1141 381 THR A CG2 2336 N N . TRP A 382 ? 1.6927 1.3835 1.9602 -0.0135 0.1084 0.0748 382 TRP A N 2337 C CA . TRP A 382 ? 1.7552 1.4620 2.0333 0.0087 0.1143 0.0874 382 TRP A CA 2338 C C . TRP A 382 ? 1.7873 1.5216 2.0835 0.0156 0.1061 0.1214 382 TRP A C 2339 O O . TRP A 382 ? 1.8637 1.6272 2.1429 0.0115 0.0968 0.1320 382 TRP A O 2340 C CB . TRP A 382 ? 1.8226 1.5514 2.0677 0.0126 0.1139 0.0746 382 TRP A CB 2341 C CG . TRP A 382 ? 1.8778 1.5827 2.1133 0.0162 0.1281 0.0484 382 TRP A CG 2342 C CD1 . TRP A 382 ? 1.7647 1.4394 1.9796 0.0029 0.1339 0.0206 382 TRP A CD1 2343 C CD2 . TRP A 382 ? 2.1106 1.8206 2.3561 0.0338 0.1396 0.0483 382 TRP A CD2 2344 N NE1 . TRP A 382 ? 1.7833 1.4419 1.9920 0.0133 0.1513 0.0023 382 TRP A NE1 2345 C CE2 . TRP A 382 ? 2.1135 1.7956 2.3451 0.0328 0.1553 0.0204 382 TRP A CE2 2346 C CE3 . TRP A 382 ? 2.4539 2.1912 2.7185 0.0487 0.1374 0.0701 382 TRP A CE3 2347 C CZ2 . TRP A 382 ? 2.6503 2.3336 2.8918 0.0488 0.1716 0.0155 382 TRP A CZ2 2348 C CZ3 . TRP A 382 ? 2.5841 2.3247 2.8606 0.0620 0.1499 0.0659 382 TRP A CZ3 2349 C CH2 . TRP A 382 ? 2.6934 2.4086 2.9611 0.0631 0.1680 0.0399 382 TRP A CH2 2350 N N . VAL A 383 ? 1.7181 1.4434 2.0477 0.0272 0.1108 0.1398 383 VAL A N 2351 C CA . VAL A 383 ? 1.5556 1.3051 1.8990 0.0322 0.1030 0.1737 383 VAL A CA 2352 C C . VAL A 383 ? 1.5170 1.2890 1.8666 0.0489 0.1013 0.1918 383 VAL A C 2353 O O . VAL A 383 ? 1.6604 1.4207 2.0374 0.0604 0.1084 0.1943 383 VAL A O 2354 C CB . VAL A 383 ? 1.4714 1.1969 1.8500 0.0277 0.1055 0.1898 383 VAL A CB 2355 C CG1 . VAL A 383 ? 1.3975 1.1472 1.7917 0.0358 0.0997 0.2276 383 VAL A CG1 2356 C CG2 . VAL A 383 ? 1.4948 1.2086 1.8661 0.0060 0.1015 0.1794 383 VAL A CG2 2357 N N . HIS A 384 ? 1.4094 1.2131 1.7339 0.0499 0.0922 0.2045 384 HIS A N 2358 C CA . HIS A 384 ? 1.5177 1.3436 1.8442 0.0606 0.0864 0.2248 384 HIS A CA 2359 C C . HIS A 384 ? 1.5949 1.4413 1.9093 0.0594 0.0785 0.2520 384 HIS A C 2360 O O . HIS A 384 ? 1.5378 1.3912 1.8284 0.0525 0.0783 0.2508 384 HIS A O 2361 C CB . HIS A 384 ? 1.5404 1.3823 1.8395 0.0633 0.0836 0.2109 384 HIS A CB 2362 C CG . HIS A 384 ? 1.6225 1.4515 1.9068 0.0593 0.0909 0.1798 384 HIS A CG 2363 N ND1 . HIS A 384 ? 1.7226 1.5242 2.0226 0.0564 0.1008 0.1621 384 HIS A ND1 2364 C CD2 . HIS A 384 ? 1.6884 1.5267 1.9410 0.0571 0.0902 0.1638 384 HIS A CD2 2365 C CE1 . HIS A 384 ? 1.7168 1.5145 1.9925 0.0522 0.1050 0.1370 384 HIS A CE1 2366 N NE2 . HIS A 384 ? 1.6774 1.4981 1.9269 0.0532 0.0988 0.1391 384 HIS A NE2 2367 N N . TYR A 385 ? 1.6733 1.5316 2.0044 0.0668 0.0728 0.2781 385 TYR A N 2368 C CA . TYR A 385 ? 1.6484 1.5297 1.9573 0.0664 0.0643 0.3040 385 TYR A CA 2369 C C . TYR A 385 ? 1.6733 1.5749 1.9502 0.0675 0.0546 0.3019 385 TYR A C 2370 O O . TYR A 385 ? 1.5846 1.4951 1.8820 0.0724 0.0484 0.3083 385 TYR A O 2371 C CB . TYR A 385 ? 1.6237 1.5074 1.9671 0.0710 0.0615 0.3384 385 TYR A CB 2372 C CG . TYR A 385 ? 1.6637 1.5195 2.0502 0.0704 0.0710 0.3407 385 TYR A CG 2373 C CD1 . TYR A 385 ? 1.7306 1.5625 2.1532 0.0766 0.0786 0.3279 385 TYR A CD1 2374 C CD2 . TYR A 385 ? 1.6812 1.5326 2.0730 0.0632 0.0740 0.3568 385 TYR A CD2 2375 C CE1 . TYR A 385 ? 1.9141 1.7119 2.3720 0.0748 0.0886 0.3273 385 TYR A CE1 2376 C CE2 . TYR A 385 ? 1.7863 1.6077 2.2177 0.0593 0.0817 0.3588 385 TYR A CE2 2377 C CZ . TYR A 385 ? 1.9405 1.7320 2.4028 0.0648 0.0888 0.3424 385 TYR A CZ 2378 O OH . TYR A 385 ? 2.1233 1.8759 2.6206 0.0602 0.0981 0.3403 385 TYR A OH 2379 N N . ILE A 386 ? 1.5618 1.4702 1.7906 0.0627 0.0540 0.2939 386 ILE A N 2380 C CA . ILE A 386 ? 1.4012 1.3199 1.5909 0.0602 0.0464 0.2852 386 ILE A CA 2381 C C . ILE A 386 ? 1.3739 1.3039 1.5225 0.0574 0.0413 0.3034 386 ILE A C 2382 O O . ILE A 386 ? 1.2596 1.1888 1.4009 0.0583 0.0492 0.3145 386 ILE A O 2383 C CB . ILE A 386 ? 1.4175 1.3253 1.5810 0.0578 0.0540 0.2547 386 ILE A CB 2384 C CG1 . ILE A 386 ? 1.4840 1.3804 1.6812 0.0595 0.0596 0.2359 386 ILE A CG1 2385 C CG2 . ILE A 386 ? 1.3702 1.2823 1.4894 0.0536 0.0476 0.2458 386 ILE A CG2 2386 C CD1 . ILE A 386 ? 1.4477 1.3326 1.6297 0.0567 0.0685 0.2116 386 ILE A CD1 2387 N N . ALA A 387 ? 1.3492 1.2902 1.4705 0.0527 0.0284 0.3069 387 ALA A N 2388 C CA . ALA A 387 ? 1.4052 1.3540 1.4762 0.0476 0.0222 0.3214 387 ALA A CA 2389 C C . ALA A 387 ? 1.4052 1.3466 1.4183 0.0393 0.0181 0.3015 387 ALA A C 2390 O O . ALA A 387 ? 1.5807 1.5214 1.6009 0.0349 0.0113 0.2862 387 ALA A O 2391 C CB . ALA A 387 ? 1.4391 1.4092 1.5286 0.0458 0.0059 0.3534 387 ALA A CB 2392 N N . ALA A 388 ? 1.3615 1.2951 1.3173 0.0372 0.0240 0.3018 388 ALA A N 2393 C CA . ALA A 388 ? 1.4475 1.3691 1.3411 0.0270 0.0183 0.2863 388 ALA A CA 2394 C C . ALA A 388 ? 1.6409 1.5820 1.5204 0.0159 -0.0038 0.3095 388 ALA A C 2395 O O . ALA A 388 ? 1.7063 1.6624 1.5958 0.0194 -0.0053 0.3369 388 ALA A O 2396 C CB . ALA A 388 ? 1.4629 1.3635 1.3002 0.0316 0.0380 0.2760 388 ALA A CB 2397 N N . GLU A 389 ? 1.7980 1.7411 1.6570 0.0013 -0.0221 0.3010 389 GLU A N 2398 C CA . GLU A 389 ? 1.8771 1.8495 1.7453 -0.0111 -0.0495 0.3255 389 GLU A CA 2399 C C . GLU A 389 ? 1.8953 1.8596 1.7023 -0.0330 -0.0666 0.3118 389 GLU A C 2400 O O . GLU A 389 ? 2.1268 2.0782 1.9341 -0.0391 -0.0668 0.2883 389 GLU A O 2401 C CB . GLU A 389 ? 1.9533 1.9489 1.9026 -0.0062 -0.0580 0.3343 389 GLU A CB 2402 C CG . GLU A 389 ? 2.0776 2.1117 2.0619 -0.0116 -0.0828 0.3698 389 GLU A CG 2403 C CD . GLU A 389 ? 2.0943 2.1406 2.1096 0.0014 -0.0785 0.4018 389 GLU A CD 2404 O OE1 . GLU A 389 ? 2.0453 2.0921 2.0123 -0.0035 -0.0813 0.4161 389 GLU A OE1 2405 O OE2 . GLU A 389 ? 1.9959 2.0487 2.0824 0.0161 -0.0708 0.4126 389 GLU A OE2 2406 N N . GLU A 390 ? 1.8072 1.7785 1.5610 -0.0466 -0.0819 0.3268 390 GLU A N 2407 C CA . GLU A 390 ? 1.9149 1.8777 1.6073 -0.0726 -0.1024 0.3139 390 GLU A CA 2408 C C . GLU A 390 ? 2.0577 2.0635 1.7917 -0.0891 -0.1372 0.3369 390 GLU A C 2409 O O . GLU A 390 ? 2.3152 2.3530 2.0487 -0.0970 -0.1587 0.3689 390 GLU A O 2410 C CB . GLU A 390 ? 1.9735 1.9162 1.5730 -0.0827 -0.1011 0.3128 390 GLU A CB 2411 C CG . GLU A 390 ? 2.1108 2.0078 1.6599 -0.0688 -0.0657 0.2863 390 GLU A CG 2412 C CD . GLU A 390 ? 2.3483 2.2257 1.8044 -0.0766 -0.0605 0.2869 390 GLU A CD 2413 O OE1 . GLU A 390 ? 2.5683 2.4389 1.9619 -0.1027 -0.0830 0.2815 390 GLU A OE1 2414 O OE2 . GLU A 390 ? 2.3039 2.1733 1.7473 -0.0582 -0.0338 0.2931 390 GLU A OE2 2415 N N . GLU A 391 ? 2.0819 2.0911 1.8551 -0.0937 -0.1417 0.3230 391 GLU A N 2416 C CA . GLU A 391 ? 2.0955 2.1457 1.9109 -0.1104 -0.1721 0.3417 391 GLU A CA 2417 C C . GLU A 391 ? 2.1428 2.1716 1.8879 -0.1422 -0.1890 0.3178 391 GLU A C 2418 O O . GLU A 391 ? 2.0617 2.0398 1.7393 -0.1449 -0.1712 0.2849 391 GLU A O 2419 C CB . GLU A 391 ? 2.2069 2.2706 2.1103 -0.0934 -0.1599 0.3393 391 GLU A CB 2420 C CG . GLU A 391 ? 2.4154 2.5334 2.4050 -0.0896 -0.1777 0.3749 391 GLU A CG 2421 C CD . GLU A 391 ? 2.5259 2.6500 2.5881 -0.0759 -0.1624 0.3653 391 GLU A CD 2422 O OE1 . GLU A 391 ? 2.3696 2.4778 2.4167 -0.0873 -0.1597 0.3394 391 GLU A OE1 2423 O OE2 . GLU A 391 ? 2.5491 2.6916 2.6827 -0.0535 -0.1516 0.3838 391 GLU A OE2 2424 N N . ASP A 392 ? 2.1408 2.2066 1.9008 -0.1671 -0.2233 0.3354 392 ASP A N 2425 C CA . ASP A 392 ? 2.1031 2.1492 1.8162 -0.1987 -0.2390 0.3113 392 ASP A CA 2426 C C . ASP A 392 ? 2.1140 2.1695 1.8994 -0.1920 -0.2303 0.3027 392 ASP A C 2427 O O . ASP A 392 ? 2.2473 2.3371 2.1183 -0.1692 -0.2223 0.3227 392 ASP A O 2428 C CB . ASP A 392 ? 2.1920 2.2774 1.8855 -0.2335 -0.2834 0.3359 392 ASP A CB 2429 C CG . ASP A 392 ? 2.3166 2.3857 1.9183 -0.2460 -0.2929 0.3393 392 ASP A CG 2430 O OD1 . ASP A 392 ? 2.4659 2.4908 2.0184 -0.2274 -0.2623 0.3207 392 ASP A OD1 2431 O OD2 . ASP A 392 ? 2.2939 2.3967 1.8723 -0.2752 -0.3310 0.3619 392 ASP A OD2 2432 N N . TRP A 393 ? 2.2091 2.2320 1.9601 -0.2113 -0.2299 0.2733 393 TRP A N 2433 C CA . TRP A 393 ? 2.1752 2.2064 1.9911 -0.2054 -0.2194 0.2658 393 TRP A CA 2434 C C . TRP A 393 ? 2.2230 2.2673 2.0378 -0.2419 -0.2469 0.2641 393 TRP A C 2435 O O . TRP A 393 ? 2.2363 2.2482 1.9720 -0.2727 -0.2626 0.2469 393 TRP A O 2436 C CB . TRP A 393 ? 2.1318 2.1077 1.9249 -0.1851 -0.1818 0.2315 393 TRP A CB 2437 C CG . TRP A 393 ? 2.0068 1.9919 1.8659 -0.1732 -0.1664 0.2260 393 TRP A CG 2438 C CD1 . TRP A 393 ? 1.9193 1.8697 1.7607 -0.1804 -0.1541 0.1999 393 TRP A CD1 2439 C CD2 . TRP A 393 ? 2.0504 2.0801 2.0010 -0.1516 -0.1597 0.2474 393 TRP A CD2 2440 N NE1 . TRP A 393 ? 1.9439 1.9174 1.8576 -0.1655 -0.1407 0.2043 393 TRP A NE1 2441 C CE2 . TRP A 393 ? 1.9510 1.9713 1.9309 -0.1473 -0.1428 0.2314 393 TRP A CE2 2442 C CE3 . TRP A 393 ? 2.2108 2.2840 2.2201 -0.1347 -0.1644 0.2787 393 TRP A CE3 2443 C CZ2 . TRP A 393 ? 1.8707 1.9230 1.9313 -0.1272 -0.1293 0.2433 393 TRP A CZ2 2444 C CZ3 . TRP A 393 ? 2.2880 2.3894 2.3808 -0.1136 -0.1502 0.2899 393 TRP A CZ3 2445 C CH2 . TRP A 393 ? 2.0209 2.1112 2.1358 -0.1103 -0.1324 0.2708 393 TRP A CH2 2446 N N . ASP A 394 ? 2.1664 2.2566 2.0681 -0.2391 -0.2513 0.2818 394 ASP A N 2447 C CA . ASP A 394 ? 2.2969 2.4018 2.2092 -0.2729 -0.2734 0.2809 394 ASP A CA 2448 C C . ASP A 394 ? 2.3648 2.4467 2.3050 -0.2638 -0.2467 0.2591 394 ASP A C 2449 O O . ASP A 394 ? 2.5720 2.6862 2.5921 -0.2397 -0.2303 0.2722 394 ASP A O 2450 C CB . ASP A 394 ? 2.1600 2.3452 2.1500 -0.2849 -0.3051 0.3243 394 ASP A CB 2451 C CG . ASP A 394 ? 2.1571 2.3601 2.1461 -0.3284 -0.3355 0.3260 394 ASP A CG 2452 O OD1 . ASP A 394 ? 1.9948 2.1791 1.9995 -0.3324 -0.3205 0.3077 394 ASP A OD1 2453 O OD2 . ASP A 394 ? 2.3165 2.5520 2.2871 -0.3604 -0.3754 0.3467 394 ASP A OD2 2454 N N . TYR A 395 ? 2.2666 2.2910 2.1388 -0.2836 -0.2421 0.2266 395 TYR A N 2455 C CA . TYR A 395 ? 2.1156 2.1092 2.0006 -0.2761 -0.2159 0.2048 395 TYR A CA 2456 C C . TYR A 395 ? 2.1219 2.1622 2.0794 -0.2929 -0.2278 0.2218 395 TYR A C 2457 O O . TYR A 395 ? 2.1061 2.1457 2.1060 -0.2769 -0.2034 0.2165 395 TYR A O 2458 C CB . TYR A 395 ? 2.0565 1.9733 1.8485 -0.2934 -0.2083 0.1687 395 TYR A CB 2459 C CG . TYR A 395 ? 2.0534 1.9154 1.7821 -0.2680 -0.1812 0.1469 395 TYR A CG 2460 C CD1 . TYR A 395 ? 1.9865 1.8262 1.7321 -0.2339 -0.1453 0.1348 395 TYR A CD1 2461 C CD2 . TYR A 395 ? 2.2349 2.0673 1.8840 -0.2802 -0.1914 0.1386 395 TYR A CD2 2462 C CE1 . TYR A 395 ? 2.0532 1.8477 1.7464 -0.2118 -0.1210 0.1179 395 TYR A CE1 2463 C CE2 . TYR A 395 ? 2.2734 2.0578 1.8671 -0.2563 -0.1638 0.1204 395 TYR A CE2 2464 C CZ . TYR A 395 ? 2.1497 1.9169 1.7687 -0.2220 -0.1289 0.1112 395 TYR A CZ 2465 O OH . TYR A 395 ? 1.9763 1.7016 1.5458 -0.1991 -0.1022 0.0967 395 TYR A OH 2466 N N . ALA A 396 ? 2.1088 2.1927 2.0812 -0.3259 -0.2654 0.2442 396 ALA A N 2467 C CA . ALA A 396 ? 2.1610 2.2982 2.2101 -0.3420 -0.2775 0.2658 396 ALA A CA 2468 C C . ALA A 396 ? 2.1435 2.3625 2.2582 -0.3481 -0.3082 0.3096 396 ALA A C 2469 O O . ALA A 396 ? 2.2152 2.4586 2.3135 -0.3878 -0.3477 0.3233 396 ALA A O 2470 C CB . ALA A 396 ? 2.3321 2.4372 2.3372 -0.3865 -0.2943 0.2482 396 ALA A CB 2471 N N . PRO A 397 ? 2.0796 2.3395 2.2678 -0.3089 -0.2901 0.3322 397 PRO A N 2472 C CA . PRO A 397 ? 2.1024 2.4381 2.3627 -0.3029 -0.3110 0.3771 397 PRO A CA 2473 C C . PRO A 397 ? 2.0757 2.4777 2.3908 -0.3379 -0.3460 0.4087 397 PRO A C 2474 O O . PRO A 397 ? 2.2230 2.6177 2.4841 -0.3824 -0.3806 0.4041 397 PRO A O 2475 C CB . PRO A 397 ? 2.1173 2.4699 2.4546 -0.2552 -0.2727 0.3857 397 PRO A CB 2476 C CG . PRO A 397 ? 2.2506 2.5289 2.5243 -0.2340 -0.2396 0.3452 397 PRO A CG 2477 C CD . PRO A 397 ? 2.1508 2.3787 2.3517 -0.2661 -0.2454 0.3136 397 PRO A CD 2478 N N . LEU A 398 ? 1.9847 2.4509 2.4060 -0.3189 -0.3367 0.4409 398 LEU A N 2479 C CA . LEU A 398 ? 2.1837 2.7300 2.6724 -0.3479 -0.3727 0.4825 398 LEU A CA 2480 C C . LEU A 398 ? 2.2735 2.8079 2.7244 -0.4008 -0.3984 0.4683 398 LEU A C 2481 O O . LEU A 398 ? 2.4622 3.0533 2.9380 -0.4388 -0.4411 0.4984 398 LEU A O 2482 C CB . LEU A 398 ? 2.2124 2.8286 2.8276 -0.3148 -0.3513 0.5195 398 LEU A CB 2483 C CG . LEU A 398 ? 2.1708 2.8513 2.8704 -0.2818 -0.3519 0.5660 398 LEU A CG 2484 C CD1 . LEU A 398 ? 2.1147 2.8591 2.8276 -0.3117 -0.4051 0.6092 398 LEU A CD1 2485 C CD2 . LEU A 398 ? 2.0968 2.7310 2.7758 -0.2361 -0.3185 0.5504 398 LEU A CD2 2486 N N . VAL A 399 ? 2.1737 2.6335 2.5617 -0.4056 -0.3751 0.4240 399 VAL A N 2487 C CA . VAL A 399 ? 2.2457 2.6947 2.6172 -0.4514 -0.3918 0.4132 399 VAL A CA 2488 C C . VAL A 399 ? 2.3126 2.7033 2.5731 -0.5008 -0.4239 0.3850 399 VAL A C 2489 O O . VAL A 399 ? 2.1077 2.4128 2.2763 -0.4953 -0.4052 0.3431 399 VAL A O 2490 C CB . VAL A 399 ? 2.1919 2.6168 2.5936 -0.4335 -0.3500 0.3954 399 VAL A CB 2491 C CG1 . VAL A 399 ? 2.0072 2.3390 2.3261 -0.4099 -0.3148 0.3486 399 VAL A CG1 2492 C CG2 . VAL A 399 ? 2.2915 2.7361 2.7169 -0.4792 -0.3690 0.4027 399 VAL A CG2 2493 N N . LEU A 400 ? 2.4890 2.9302 2.7630 -0.5486 -0.4722 0.4107 400 LEU A N 2494 C CA . LEU A 400 ? 2.5107 2.9070 2.6918 -0.6070 -0.5088 0.3883 400 LEU A CA 2495 C C . LEU A 400 ? 2.3948 2.7855 2.5984 -0.6431 -0.5122 0.3821 400 LEU A C 2496 O O . LEU A 400 ? 2.1696 2.6243 2.4778 -0.6342 -0.5027 0.4116 400 LEU A O 2497 C CB . LEU A 400 ? 2.6267 3.0872 2.8089 -0.6450 -0.5658 0.4230 400 LEU A CB 2498 C CG . LEU A 400 ? 2.6888 3.1413 2.7981 -0.6469 -0.5894 0.4248 400 LEU A CG 2499 C CD1 . LEU A 400 ? 2.5331 3.0381 2.7111 -0.5921 -0.5715 0.4577 400 LEU A CD1 2500 C CD2 . LEU A 400 ? 2.6379 3.1365 2.7254 -0.7093 -0.6534 0.4484 400 LEU A CD2 2501 N N . ALA A 401 ? 2.4049 2.7168 2.5093 -0.6843 -0.5244 0.3444 401 ALA A N 2502 C CA . ALA A 401 ? 2.5594 2.8622 2.6736 -0.7308 -0.5378 0.3399 401 ALA A CA 2503 C C . ALA A 401 ? 2.8072 3.0766 2.8307 -0.7961 -0.5869 0.3249 401 ALA A C 2504 O O . ALA A 401 ? 2.6986 2.8791 2.6403 -0.8254 -0.5827 0.2849 401 ALA A O 2505 C CB . ALA A 401 ? 2.6091 2.8286 2.6923 -0.7111 -0.4909 0.3019 401 ALA A CB 2506 N N . PRO A 402 ? 3.1725 3.5133 3.2111 -0.8202 -0.6341 0.3584 402 PRO A N 2507 C CA . PRO A 402 ? 3.5451 3.8584 3.4846 -0.8780 -0.6834 0.3453 402 PRO A CA 2508 C C . PRO A 402 ? 3.7469 3.9791 3.6067 -0.9373 -0.6977 0.3070 402 PRO A C 2509 O O . PRO A 402 ? 3.5701 3.7805 3.4673 -0.9397 -0.6748 0.2984 402 PRO A O 2510 C CB . PRO A 402 ? 3.4704 3.9085 3.4969 -0.9035 -0.7350 0.4051 402 PRO A CB 2511 C CG . PRO A 402 ? 3.2828 3.7914 3.4164 -0.8367 -0.7034 0.4411 402 PRO A CG 2512 C CD . PRO A 402 ? 3.1986 3.6602 3.3619 -0.7964 -0.6449 0.4167 402 PRO A CD 2513 N N . ASP A 403 ? 3.9572 4.1436 3.7049 -0.9849 -0.7349 0.2848 403 ASP A N 2514 C CA . ASP A 403 ? 3.9802 4.0642 3.6197 -1.0407 -0.7463 0.2379 403 ASP A CA 2515 C C . ASP A 403 ? 4.0733 4.0329 3.6348 -1.0054 -0.6885 0.1836 403 ASP A C 2516 O O . ASP A 403 ? 3.9539 3.9125 3.5789 -0.9545 -0.6414 0.1854 403 ASP A O 2517 C CB . ASP A 403 ? 3.7695 3.8889 3.4727 -1.0969 -0.7757 0.2557 403 ASP A CB 2518 C CG . ASP A 403 ? 3.5854 3.8207 3.3502 -1.1444 -0.8405 0.3068 403 ASP A CG 2519 O OD1 . ASP A 403 ? 3.4264 3.7286 3.2079 -1.1235 -0.8578 0.3366 403 ASP A OD1 2520 O OD2 . ASP A 403 ? 3.4425 3.7032 3.2417 -1.2031 -0.8743 0.3196 403 ASP A OD2 2521 N N . ASP A 404 ? 4.1296 3.9850 3.5516 -1.0332 -0.6924 0.1364 404 ASP A N 2522 C CA . ASP A 404 ? 3.8947 3.6233 3.2323 -1.0074 -0.6408 0.0835 404 ASP A CA 2523 C C . ASP A 404 ? 3.6127 3.2947 2.9727 -1.0348 -0.6302 0.0696 404 ASP A C 2524 O O . ASP A 404 ? 3.4226 2.9918 2.7093 -1.0299 -0.5956 0.0260 404 ASP A O 2525 C CB . ASP A 404 ? 4.0959 3.7297 3.2785 -1.0296 -0.6475 0.0395 404 ASP A CB 2526 C CG . ASP A 404 ? 4.0774 3.7577 3.2377 -1.0004 -0.6550 0.0560 404 ASP A CG 2527 O OD1 . ASP A 404 ? 3.7814 3.4948 2.9986 -0.9346 -0.6184 0.0715 404 ASP A OD1 2528 O OD2 . ASP A 404 ? 4.1327 3.8169 3.2178 -1.0454 -0.6987 0.0543 404 ASP A OD2 2529 N N . ARG A 405 ? 3.4151 3.1895 2.8822 -1.0634 -0.6604 0.1109 405 ARG A N 2530 C CA . ARG A 405 ? 3.3223 3.0901 2.8541 -1.0767 -0.6465 0.1155 405 ARG A CA 2531 C C . ARG A 405 ? 3.2190 2.9196 2.7506 -1.0149 -0.5801 0.0921 405 ARG A C 2532 O O . ARG A 405 ? 3.1380 2.7342 2.6070 -1.0276 -0.5578 0.0553 405 ARG A O 2533 C CB . ARG A 405 ? 3.3235 3.2328 3.0056 -1.0789 -0.6692 0.1766 405 ARG A CB 2534 C CG . ARG A 405 ? 3.1373 3.1242 2.9152 -1.0034 -0.6342 0.2081 405 ARG A CG 2535 C CD . ARG A 405 ? 3.0383 3.1640 2.9615 -1.0026 -0.6542 0.2689 405 ARG A CD 2536 N NE . ARG A 405 ? 3.2361 3.3965 3.2045 -1.0678 -0.6911 0.2883 405 ARG A NE 2537 C CZ . ARG A 405 ? 3.1007 3.2915 3.1587 -1.0681 -0.6726 0.3076 405 ARG A CZ 2538 N NH1 . ARG A 405 ? 2.9715 3.1616 3.0813 -1.0059 -0.6171 0.3091 405 ARG A NH1 2539 N NH2 . ARG A 405 ? 3.0025 3.2259 3.0971 -1.1333 -0.7109 0.3265 405 ARG A NH2 2540 N N . SER A 406 ? 3.2290 2.9870 2.8248 -0.9490 -0.5503 0.1134 406 SER A N 2541 C CA . SER A 406 ? 3.2210 2.9627 2.8645 -0.8896 -0.4939 0.1110 406 SER A CA 2542 C C . SER A 406 ? 3.1628 2.7835 2.7095 -0.8586 -0.4491 0.0636 406 SER A C 2543 O O . SER A 406 ? 3.3457 2.8730 2.7834 -0.8884 -0.4552 0.0260 406 SER A O 2544 C CB . SER A 406 ? 3.0820 2.9219 2.8190 -0.8320 -0.4790 0.1474 406 SER A CB 2545 O OG . SER A 406 ? 2.9554 2.9120 2.8008 -0.8493 -0.5103 0.1961 406 SER A OG 2546 N N . TYR A 407 ? 2.9546 2.5796 2.5451 -0.7981 -0.4029 0.0673 407 TYR A N 2547 C CA . TYR A 407 ? 2.9385 2.4740 2.4586 -0.7561 -0.3587 0.0330 407 TYR A CA 2548 C C . TYR A 407 ? 2.7170 2.3055 2.2672 -0.6974 -0.3404 0.0472 407 TYR A C 2549 O O . TYR A 407 ? 2.4516 1.9838 1.9412 -0.6616 -0.3112 0.0235 407 TYR A O 2550 C CB . TYR A 407 ? 3.1928 2.6813 2.7368 -0.7430 -0.3220 0.0257 407 TYR A CB 2551 C CG . TYR A 407 ? 3.4532 2.8686 2.9528 -0.6905 -0.2720 0.0008 407 TYR A CG 2552 C CD1 . TYR A 407 ? 3.5802 2.9339 2.9880 -0.6737 -0.2612 -0.0280 407 TYR A CD1 2553 C CD2 . TYR A 407 ? 3.3768 2.7888 2.9276 -0.6573 -0.2351 0.0086 407 TYR A CD2 2554 C CE1 . TYR A 407 ? 3.7040 2.9982 3.0788 -0.6247 -0.2155 -0.0466 407 TYR A CE1 2555 C CE2 . TYR A 407 ? 3.5679 2.9197 3.0823 -0.6100 -0.1920 -0.0101 407 TYR A CE2 2556 C CZ . TYR A 407 ? 3.7645 3.0590 3.1940 -0.5936 -0.1825 -0.0370 407 TYR A CZ 2557 O OH . TYR A 407 ? 3.9116 3.1523 3.3110 -0.5464 -0.1399 -0.0521 407 TYR A OH 2558 N N . LYS A 408 ? 2.6494 2.3461 2.2957 -0.6889 -0.3575 0.0873 408 LYS A N 2559 C CA . LYS A 408 ? 2.5729 2.3263 2.2516 -0.6422 -0.3489 0.1049 408 LYS A CA 2560 C C . LYS A 408 ? 2.7181 2.4884 2.3461 -0.6643 -0.3856 0.1077 408 LYS A C 2561 O O . LYS A 408 ? 2.7129 2.4647 2.2959 -0.6334 -0.3722 0.0978 408 LYS A O 2562 C CB . LYS A 408 ? 2.3931 2.2475 2.1971 -0.6156 -0.3431 0.1456 408 LYS A CB 2563 C CG . LYS A 408 ? 2.4226 2.3701 2.3075 -0.6517 -0.3830 0.1848 408 LYS A CG 2564 C CD . LYS A 408 ? 2.2851 2.3246 2.2840 -0.6102 -0.3672 0.2221 408 LYS A CD 2565 C CE . LYS A 408 ? 2.2655 2.3798 2.3621 -0.6357 -0.3822 0.2568 408 LYS A CE 2566 N NZ . LYS A 408 ? 2.0850 2.2868 2.2918 -0.5943 -0.3636 0.2929 408 LYS A NZ 2567 N N . SER A 409 ? 2.9087 2.7169 2.5446 -0.7190 -0.4328 0.1234 409 SER A N 2568 C CA . SER A 409 ? 3.1373 2.9489 2.7056 -0.7517 -0.4726 0.1220 409 SER A CA 2569 C C . SER A 409 ? 3.0648 2.7543 2.4998 -0.7654 -0.4583 0.0708 409 SER A C 2570 O O . SER A 409 ? 3.2680 2.8988 2.6532 -0.8125 -0.4715 0.0484 409 SER A O 2571 C CB . SER A 409 ? 3.4159 3.2914 3.0206 -0.8135 -0.5280 0.1493 409 SER A CB 2572 O OG . SER A 409 ? 3.4513 3.4406 3.1870 -0.7987 -0.5371 0.1989 409 SER A OG 2573 N N . GLN A 410 ? 2.8014 2.4512 2.1817 -0.7231 -0.4287 0.0530 410 GLN A N 2574 C CA . GLN A 410 ? 2.7946 2.3275 2.0681 -0.7163 -0.3967 0.0062 410 GLN A CA 2575 C C . GLN A 410 ? 2.7490 2.2709 2.0254 -0.6500 -0.3510 0.0021 410 GLN A C 2576 O O . GLN A 410 ? 2.8570 2.3048 2.0420 -0.6365 -0.3287 -0.0280 410 GLN A O 2577 C CB . GLN A 410 ? 2.9402 2.4149 2.2208 -0.7306 -0.3786 -0.0119 410 GLN A CB 2578 C CG . GLN A 410 ? 3.2144 2.5614 2.3785 -0.7464 -0.3589 -0.0601 410 GLN A CG 2579 C CD . GLN A 410 ? 3.3745 2.6710 2.5637 -0.7490 -0.3345 -0.0707 410 GLN A CD 2580 O OE1 . GLN A 410 ? 3.4468 2.6960 2.6345 -0.7038 -0.2880 -0.0834 410 GLN A OE1 2581 N NE2 . GLN A 410 ? 3.3597 2.6725 2.5790 -0.8019 -0.3666 -0.0613 410 GLN A NE2 2582 N N . TYR A 411 ? 2.6734 2.2669 2.0546 -0.6097 -0.3356 0.0318 411 TYR A N 2583 C CA . TYR A 411 ? 2.5948 2.1997 1.9969 -0.5489 -0.2995 0.0363 411 TYR A CA 2584 C C . TYR A 411 ? 2.5301 2.2193 1.9705 -0.5406 -0.3244 0.0694 411 TYR A C 2585 O O . TYR A 411 ? 2.2888 1.9725 1.6977 -0.5107 -0.3104 0.0678 411 TYR A O 2586 C CB . TYR A 411 ? 2.5175 2.1440 2.0064 -0.5113 -0.2666 0.0468 411 TYR A CB 2587 C CG . TYR A 411 ? 2.5500 2.0915 2.0022 -0.4947 -0.2267 0.0170 411 TYR A CG 2588 C CD1 . TYR A 411 ? 2.6318 2.1270 2.0692 -0.5291 -0.2301 0.0033 411 TYR A CD1 2589 C CD2 . TYR A 411 ? 2.3954 1.9066 1.8341 -0.4448 -0.1861 0.0062 411 TYR A CD2 2590 C CE1 . TYR A 411 ? 2.5218 1.9403 1.9293 -0.5126 -0.1937 -0.0197 411 TYR A CE1 2591 C CE2 . TYR A 411 ? 2.2888 1.7288 1.6998 -0.4287 -0.1512 -0.0157 411 TYR A CE2 2592 C CZ . TYR A 411 ? 2.4101 1.8035 1.8057 -0.4615 -0.1548 -0.0280 411 TYR A CZ 2593 O OH . TYR A 411 ? 2.4883 1.8110 1.8594 -0.4447 -0.1202 -0.0462 411 TYR A OH 2594 N N . LEU A 412 ? 2.6008 2.3676 2.1116 -0.5686 -0.3610 0.1014 412 LEU A N 2595 C CA . LEU A 412 ? 2.6102 2.4692 2.1767 -0.5676 -0.3913 0.1415 412 LEU A CA 2596 C C . LEU A 412 ? 2.7272 2.5955 2.2306 -0.6200 -0.4411 0.1461 412 LEU A C 2597 O O . LEU A 412 ? 2.7129 2.5412 2.1262 -0.6211 -0.4425 0.1297 412 LEU A O 2598 C CB . LEU A 412 ? 2.3935 2.3385 2.0859 -0.5643 -0.3993 0.1785 412 LEU A CB 2599 C CG . LEU A 412 ? 2.1586 2.1319 1.9414 -0.5154 -0.3607 0.1899 412 LEU A CG 2600 C CD1 . LEU A 412 ? 2.0328 1.9258 1.7731 -0.4865 -0.3151 0.1541 412 LEU A CD1 2601 C CD2 . LEU A 412 ? 2.0942 2.1316 1.9724 -0.5336 -0.3739 0.2174 412 LEU A CD2 2602 N N . ASN A 413 ? 2.7287 2.6531 2.2809 -0.6635 -0.4815 0.1700 413 ASN A N 2603 C CA . ASN A 413 ? 2.8539 2.8006 2.3584 -0.7199 -0.5359 0.1799 413 ASN A CA 2604 C C . ASN A 413 ? 3.0496 2.9094 2.4108 -0.7360 -0.5360 0.1410 413 ASN A C 2605 O O . ASN A 413 ? 3.2415 3.0145 2.5199 -0.7660 -0.5313 0.1008 413 ASN A O 2606 C CB . ASN A 413 ? 2.8203 2.7805 2.3499 -0.7768 -0.5687 0.1840 413 ASN A CB 2607 C CG . ASN A 413 ? 2.7581 2.8366 2.4263 -0.7782 -0.5913 0.2379 413 ASN A CG 2608 O OD1 . ASN A 413 ? 2.7105 2.8048 2.4446 -0.7883 -0.5859 0.2443 413 ASN A OD1 2609 N ND2 . ASN A 413 ? 2.7315 2.8935 2.4454 -0.7676 -0.6154 0.2788 413 ASN A ND2 2610 N N . ASN A 414 ? 2.9929 2.8746 2.3267 -0.7144 -0.5385 0.1539 414 ASN A N 2611 C CA . ASN A 414 ? 3.0444 2.8526 2.2445 -0.7215 -0.5337 0.1219 414 ASN A CA 2612 C C . ASN A 414 ? 3.2643 3.0267 2.3558 -0.7900 -0.5740 0.0983 414 ASN A C 2613 O O . ASN A 414 ? 3.2778 3.1058 2.3963 -0.8360 -0.6269 0.1267 414 ASN A O 2614 C CB . ASN A 414 ? 2.9040 2.7677 2.1133 -0.6928 -0.5387 0.1528 414 ASN A CB 2615 C CG . ASN A 414 ? 3.0102 2.8253 2.0853 -0.7172 -0.5524 0.1326 414 ASN A CG 2616 O OD1 . ASN A 414 ? 2.9513 2.8066 1.9960 -0.7618 -0.6025 0.1517 414 ASN A OD1 2617 N ND2 . ASN A 414 ? 3.1161 2.8447 2.1080 -0.6893 -0.5077 0.0942 414 ASN A ND2 2618 N N . GLY A 415 ? 3.4202 3.0710 2.3882 -0.7959 -0.5487 0.0475 415 GLY A N 2619 C CA . GLY A 415 ? 3.5618 3.1427 2.4153 -0.8608 -0.5775 0.0130 415 GLY A CA 2620 C C . GLY A 415 ? 3.6738 3.1662 2.3725 -0.8701 -0.5666 -0.0264 415 GLY A C 2621 O O . GLY A 415 ? 3.6548 3.1517 2.3318 -0.8276 -0.5416 -0.0210 415 GLY A O 2622 N N . PRO A 416 ? 3.8073 3.2143 2.3952 -0.9261 -0.5829 -0.0674 416 PRO A N 2623 C CA . PRO A 416 ? 3.8846 3.2139 2.3145 -0.9493 -0.5838 -0.1032 416 PRO A CA 2624 C C . PRO A 416 ? 3.8476 3.0963 2.2209 -0.8899 -0.5161 -0.1344 416 PRO A C 2625 O O . PRO A 416 ? 3.8269 3.0330 2.0900 -0.8877 -0.5058 -0.1528 416 PRO A O 2626 C CB . PRO A 416 ? 4.0061 3.2491 2.3520 -1.0157 -0.6047 -0.1447 416 PRO A CB 2627 C CG . PRO A 416 ? 3.9040 3.1339 2.3446 -1.0000 -0.5802 -0.1471 416 PRO A CG 2628 C CD . PRO A 416 ? 3.7732 3.1327 2.3741 -0.9625 -0.5876 -0.0891 416 PRO A CD 2629 N N . GLN A 417 ? 3.7225 2.9538 2.1729 -0.8432 -0.4709 -0.1382 417 GLN A N 2630 C CA . GLN A 417 ? 3.6528 2.8257 2.0815 -0.7808 -0.4060 -0.1585 417 GLN A CA 2631 C C . GLN A 417 ? 3.3976 2.6139 1.9616 -0.7301 -0.3761 -0.1361 417 GLN A C 2632 O O . GLN A 417 ? 3.4098 2.5560 1.9710 -0.7026 -0.3310 -0.1619 417 GLN A O 2633 C CB . GLN A 417 ? 3.8660 2.8978 2.1673 -0.7932 -0.3719 -0.2176 417 GLN A CB 2634 C CG . GLN A 417 ? 3.8861 2.8555 2.1111 -0.7437 -0.3161 -0.2400 417 GLN A CG 2635 C CD . GLN A 417 ? 3.9887 2.8221 2.1265 -0.7368 -0.2672 -0.2929 417 GLN A CD 2636 O OE1 . GLN A 417 ? 3.8642 2.6545 1.9900 -0.6820 -0.2104 -0.3046 417 GLN A OE1 2637 N NE2 . GLN A 417 ? 4.2625 3.0277 2.3423 -0.7926 -0.2887 -0.3235 417 GLN A NE2 2638 N N . ARG A 418 ? 3.1610 2.4916 1.8418 -0.7181 -0.4010 -0.0876 418 ARG A N 2639 C CA . ARG A 418 ? 3.0422 2.4182 1.8454 -0.6661 -0.3709 -0.0653 418 ARG A CA 2640 C C . ARG A 418 ? 2.9310 2.4186 1.8279 -0.6368 -0.3847 -0.0159 418 ARG A C 2641 O O . ARG A 418 ? 2.8926 2.4641 1.8626 -0.6602 -0.4263 0.0193 418 ARG A O 2642 C CB . ARG A 418 ? 2.9945 2.3764 1.8700 -0.6866 -0.3797 -0.0634 418 ARG A CB 2643 C CG . ARG A 418 ? 3.0957 2.3832 1.8875 -0.7357 -0.3859 -0.1037 418 ARG A CG 2644 C CD . ARG A 418 ? 3.1210 2.3172 1.8979 -0.7055 -0.3325 -0.1359 418 ARG A CD 2645 N NE . ARG A 418 ? 3.3295 2.4531 2.0658 -0.7536 -0.3423 -0.1636 418 ARG A NE 2646 C CZ . ARG A 418 ? 3.3461 2.4972 2.1642 -0.7722 -0.3548 -0.1492 418 ARG A CZ 2647 N NH1 . ARG A 418 ? 3.2508 2.5007 2.1945 -0.7454 -0.3579 -0.1085 418 ARG A NH1 2648 N NH2 . ARG A 418 ? 3.3987 2.4760 2.1723 -0.8180 -0.3628 -0.1756 418 ARG A NH2 2649 N N . ILE A 419 ? 2.8889 2.3756 1.7850 -0.5858 -0.3487 -0.0123 419 ILE A N 2650 C CA . ILE A 419 ? 2.7495 2.3290 1.7340 -0.5520 -0.3535 0.0317 419 ILE A CA 2651 C C . ILE A 419 ? 2.7486 2.4089 1.8627 -0.5515 -0.3725 0.0653 419 ILE A C 2652 O O . ILE A 419 ? 2.6047 2.3469 1.7714 -0.5672 -0.4110 0.1030 419 ILE A O 2653 C CB . ILE A 419 ? 2.6351 2.1971 1.6346 -0.4910 -0.3015 0.0284 419 ILE A CB 2654 C CG1 . ILE A 419 ? 2.6507 2.1222 1.6115 -0.4733 -0.2565 -0.0118 419 ILE A CG1 2655 C CG2 . ILE A 419 ? 2.6922 2.2510 1.6220 -0.4802 -0.2970 0.0328 419 ILE A CG2 2656 C CD1 . ILE A 419 ? 2.8059 2.1825 1.6319 -0.4859 -0.2387 -0.0514 419 ILE A CD1 2657 N N . GLY A 420 ? 2.9157 2.5518 2.0791 -0.5322 -0.3434 0.0523 420 GLY A N 2658 C CA . GLY A 420 ? 2.9399 2.6398 2.2211 -0.5285 -0.3515 0.0782 420 GLY A CA 2659 C C . GLY A 420 ? 2.9314 2.7243 2.3183 -0.4954 -0.3546 0.1214 420 GLY A C 2660 O O . GLY A 420 ? 3.0907 2.9234 2.4708 -0.4918 -0.3715 0.1439 420 GLY A O 2661 N N . ARG A 421 ? 2.6171 2.4408 2.0989 -0.4711 -0.3365 0.1329 421 ARG A N 2662 C CA . ARG A 421 ? 2.3651 2.2770 1.9600 -0.4443 -0.3397 0.1737 421 ARG A CA 2663 C C . ARG A 421 ? 2.3193 2.2526 1.9309 -0.4013 -0.3217 0.1891 421 ARG A C 2664 O O . ARG A 421 ? 2.2476 2.2052 1.9323 -0.3632 -0.2963 0.1998 421 ARG A O 2665 C CB . ARG A 421 ? 2.2998 2.2896 1.9474 -0.4805 -0.3876 0.2097 421 ARG A CB 2666 C CG . ARG A 421 ? 2.1163 2.1908 1.8921 -0.4555 -0.3861 0.2493 421 ARG A CG 2667 C CD . ARG A 421 ? 2.2037 2.3626 2.0330 -0.4866 -0.4336 0.2917 421 ARG A CD 2668 N NE . ARG A 421 ? 2.3412 2.4944 2.1424 -0.5425 -0.4672 0.2846 421 ARG A NE 2669 C CZ . ARG A 421 ? 2.2964 2.4779 2.1643 -0.5586 -0.4713 0.2934 421 ARG A CZ 2670 N NH1 . ARG A 421 ? 2.2244 2.4424 2.1892 -0.5215 -0.4422 0.3090 421 ARG A NH1 2671 N NH2 . ARG A 421 ? 2.2836 2.4557 2.1193 -0.6137 -0.5041 0.2864 421 ARG A NH2 2672 N N . LYS A 422 ? 2.4479 2.3721 1.9913 -0.4093 -0.3353 0.1908 422 LYS A N 2673 C CA . LYS A 422 ? 2.4116 2.3676 1.9766 -0.3756 -0.3264 0.2140 422 LYS A CA 2674 C C . LYS A 422 ? 2.3453 2.2372 1.8134 -0.3623 -0.3025 0.1885 422 LYS A C 2675 O O . LYS A 422 ? 2.4991 2.3532 1.8720 -0.3922 -0.3173 0.1717 422 LYS A O 2676 C CB . LYS A 422 ? 2.5686 2.5997 2.1653 -0.3960 -0.3702 0.2564 422 LYS A CB 2677 C CG . LYS A 422 ? 2.4702 2.5464 2.1160 -0.3606 -0.3632 0.2897 422 LYS A CG 2678 C CD . LYS A 422 ? 2.4216 2.5793 2.1172 -0.3777 -0.4059 0.3381 422 LYS A CD 2679 C CE . LYS A 422 ? 2.4173 2.5945 2.1109 -0.3520 -0.4016 0.3639 422 LYS A CE 2680 N NZ . LYS A 422 ? 2.3334 2.5910 2.1340 -0.3343 -0.4155 0.4156 422 LYS A NZ 2681 N N . TYR A 423 ? 2.1514 2.0308 1.6430 -0.3187 -0.2649 0.1853 423 TYR A N 2682 C CA . TYR A 423 ? 2.2632 2.0845 1.6750 -0.3010 -0.2356 0.1626 423 TYR A CA 2683 C C . TYR A 423 ? 2.2706 2.1261 1.7247 -0.2641 -0.2202 0.1879 423 TYR A C 2684 O O . TYR A 423 ? 2.2572 2.1653 1.8047 -0.2464 -0.2225 0.2139 423 TYR A O 2685 C CB . TYR A 423 ? 2.3647 2.1198 1.7537 -0.2864 -0.1985 0.1259 423 TYR A CB 2686 C CG . TYR A 423 ? 2.5670 2.2706 1.9030 -0.3212 -0.2068 0.0964 423 TYR A CG 2687 C CD1 . TYR A 423 ? 2.5854 2.3191 1.9746 -0.3466 -0.2312 0.1043 423 TYR A CD1 2688 C CD2 . TYR A 423 ? 2.6602 2.2824 1.8957 -0.3277 -0.1872 0.0610 423 TYR A CD2 2689 C CE1 . TYR A 423 ? 2.5266 2.2117 1.8699 -0.3805 -0.2390 0.0788 423 TYR A CE1 2690 C CE2 . TYR A 423 ? 2.5475 2.1155 1.7349 -0.3597 -0.1930 0.0334 423 TYR A CE2 2691 C CZ . TYR A 423 ? 2.4842 2.0838 1.7258 -0.3875 -0.2202 0.0426 423 TYR A CZ 2692 O OH . TYR A 423 ? 2.4366 1.9828 1.6343 -0.4221 -0.2273 0.0172 423 TYR A OH 2693 N N . LYS A 424 ? 2.3276 2.1525 1.7139 -0.2531 -0.2036 0.1813 424 LYS A N 2694 C CA . LYS A 424 ? 2.2150 2.0647 1.6386 -0.2184 -0.1849 0.2034 424 LYS A CA 2695 C C . LYS A 424 ? 2.2185 2.0334 1.6602 -0.1852 -0.1426 0.1829 424 LYS A C 2696 O O . LYS A 424 ? 2.2697 2.0261 1.6447 -0.1829 -0.1191 0.1529 424 LYS A O 2697 C CB . LYS A 424 ? 2.2190 2.0608 1.5660 -0.2229 -0.1876 0.2119 424 LYS A CB 2698 C CG . LYS A 424 ? 2.1326 1.9941 1.5131 -0.1885 -0.1652 0.2340 424 LYS A CG 2699 C CD . LYS A 424 ? 2.2259 2.0895 1.5360 -0.1953 -0.1713 0.2495 424 LYS A CD 2700 C CE . LYS A 424 ? 2.2430 2.1742 1.6039 -0.2013 -0.2042 0.2959 424 LYS A CE 2701 N NZ . LYS A 424 ? 2.2552 2.1924 1.5491 -0.2072 -0.2101 0.3155 424 LYS A NZ 2702 N N . LYS A 425 ? 2.1217 1.9717 1.6536 -0.1601 -0.1331 0.1994 425 LYS A N 2703 C CA . LYS A 425 ? 2.0794 1.9058 1.6376 -0.1302 -0.0973 0.1842 425 LYS A CA 2704 C C . LYS A 425 ? 2.0235 1.8775 1.6294 -0.1026 -0.0839 0.2071 425 LYS A C 2705 O O . LYS A 425 ? 2.1348 2.0235 1.7535 -0.1053 -0.1007 0.2351 425 LYS A O 2706 C CB . LYS A 425 ? 2.0650 1.8977 1.6827 -0.1292 -0.0957 0.1752 425 LYS A CB 2707 C CG . LYS A 425 ? 2.1747 1.9793 1.7531 -0.1576 -0.1080 0.1540 425 LYS A CG 2708 C CD . LYS A 425 ? 2.1491 1.9430 1.7692 -0.1502 -0.0932 0.1395 425 LYS A CD 2709 C CE . LYS A 425 ? 2.1400 1.8787 1.7189 -0.1328 -0.0598 0.1138 425 LYS A CE 2710 N NZ . LYS A 425 ? 2.1282 1.8164 1.6133 -0.1433 -0.0543 0.0962 425 LYS A NZ 2711 N N . VAL A 426 ? 1.8950 1.7340 1.5269 -0.0777 -0.0547 0.1968 426 VAL A N 2712 C CA . VAL A 426 ? 1.8917 1.7522 1.5700 -0.0538 -0.0410 0.2160 426 VAL A CA 2713 C C . VAL A 426 ? 1.8982 1.7657 1.6455 -0.0374 -0.0276 0.2102 426 VAL A C 2714 O O . VAL A 426 ? 2.1772 2.0175 1.9133 -0.0269 -0.0060 0.1905 426 VAL A O 2715 C CB . VAL A 426 ? 1.8364 1.6720 1.4624 -0.0408 -0.0169 0.2134 426 VAL A CB 2716 C CG1 . VAL A 426 ? 1.7613 1.5535 1.3530 -0.0315 0.0099 0.1847 426 VAL A CG1 2717 C CG2 . VAL A 426 ? 1.7736 1.6349 1.4505 -0.0208 -0.0063 0.2369 426 VAL A CG2 2718 N N . ARG A 427 ? 1.8394 1.7425 1.6561 -0.0349 -0.0396 0.2278 427 ARG A N 2719 C CA . ARG A 427 ? 1.8872 1.7945 1.7637 -0.0209 -0.0265 0.2204 427 ARG A CA 2720 C C . ARG A 427 ? 1.7452 1.6627 1.6629 -0.0019 -0.0137 0.2344 427 ARG A C 2721 O O . ARG A 427 ? 1.6977 1.6246 1.6077 0.0004 -0.0168 0.2542 427 ARG A O 2722 C CB . ARG A 427 ? 1.9347 1.8699 1.8641 -0.0284 -0.0423 0.2277 427 ARG A CB 2723 C CG . ARG A 427 ? 1.9560 1.9055 1.8625 -0.0524 -0.0692 0.2353 427 ARG A CG 2724 C CD . ARG A 427 ? 1.7816 1.7775 1.7562 -0.0535 -0.0871 0.2629 427 ARG A CD 2725 N NE . ARG A 427 ? 1.7711 1.7745 1.8116 -0.0353 -0.0703 0.2602 427 ARG A NE 2726 C CZ . ARG A 427 ? 1.9520 1.9899 2.0603 -0.0308 -0.0765 0.2788 427 ARG A CZ 2727 N NH1 . ARG A 427 ? 2.2626 2.3374 2.3889 -0.0436 -0.1022 0.3053 427 ARG A NH1 2728 N NH2 . ARG A 427 ? 1.8099 1.8461 1.9676 -0.0135 -0.0567 0.2716 427 ARG A NH2 2729 N N . PHE A 428 ? 1.5583 1.4722 1.5165 0.0097 0.0005 0.2239 428 PHE A N 2730 C CA . PHE A 428 ? 1.4969 1.4211 1.5045 0.0231 0.0084 0.2367 428 PHE A CA 2731 C C . PHE A 428 ? 1.5441 1.4939 1.6089 0.0237 -0.0038 0.2541 428 PHE A C 2732 O O . PHE A 428 ? 1.7174 1.6730 1.8078 0.0219 -0.0052 0.2451 428 PHE A O 2733 C CB . PHE A 428 ? 1.5049 1.4145 1.5296 0.0323 0.0264 0.2175 428 PHE A CB 2734 C CG . PHE A 428 ? 1.6299 1.5201 1.6134 0.0362 0.0408 0.2062 428 PHE A CG 2735 C CD1 . PHE A 428 ? 1.7272 1.6183 1.7054 0.0427 0.0488 0.2191 428 PHE A CD1 2736 C CD2 . PHE A 428 ? 1.7334 1.6057 1.6882 0.0345 0.0480 0.1852 428 PHE A CD2 2737 C CE1 . PHE A 428 ? 1.7206 1.5985 1.6674 0.0486 0.0643 0.2119 428 PHE A CE1 2738 C CE2 . PHE A 428 ? 1.6318 1.4878 1.5549 0.0413 0.0634 0.1780 428 PHE A CE2 2739 C CZ . PHE A 428 ? 1.5969 1.4573 1.5171 0.0489 0.0719 0.1916 428 PHE A CZ 2740 N N . MET A 429 ? 1.5809 1.5471 1.6682 0.0273 -0.0109 0.2813 429 MET A N 2741 C CA . MET A 429 ? 1.6368 1.6241 1.7903 0.0343 -0.0161 0.3003 429 MET A CA 2742 C C . MET A 429 ? 1.6221 1.5975 1.8175 0.0488 0.0002 0.3046 429 MET A C 2743 O O . MET A 429 ? 1.4102 1.3730 1.5864 0.0509 0.0082 0.3065 429 MET A O 2744 C CB . MET A 429 ? 1.8631 1.8805 2.0211 0.0272 -0.0389 0.3324 429 MET A CB 2745 C CG . MET A 429 ? 2.1641 2.1974 2.2956 0.0093 -0.0589 0.3296 429 MET A CG 2746 S SD . MET A 429 ? 2.6497 2.7330 2.8239 0.0021 -0.0882 0.3705 429 MET A SD 2747 C CE . MET A 429 ? 2.0658 2.1657 2.3302 0.0176 -0.0773 0.3727 429 MET A CE 2748 N N . ALA A 430 ? 1.6621 1.6398 1.9141 0.0580 0.0065 0.3055 430 ALA A N 2749 C CA . ALA A 430 ? 1.7835 1.7416 2.0726 0.0692 0.0228 0.3043 430 ALA A CA 2750 C C . ALA A 430 ? 1.8884 1.8564 2.2273 0.0785 0.0195 0.3377 430 ALA A C 2751 O O . ALA A 430 ? 2.0259 2.0120 2.4068 0.0849 0.0149 0.3526 430 ALA A O 2752 C CB . ALA A 430 ? 1.8043 1.7472 2.1161 0.0743 0.0376 0.2780 430 ALA A CB 2753 N N . TYR A 431 ? 1.8236 1.7811 2.1624 0.0800 0.0230 0.3520 431 TYR A N 2754 C CA . TYR A 431 ? 1.8702 1.8341 2.2562 0.0890 0.0207 0.3873 431 TYR A CA 2755 C C . TYR A 431 ? 1.9137 1.8465 2.3491 0.0994 0.0394 0.3810 431 TYR A C 2756 O O . TYR A 431 ? 2.1600 2.0674 2.5874 0.0974 0.0528 0.3484 431 TYR A O 2757 C CB . TYR A 431 ? 1.8858 1.8574 2.2448 0.0837 0.0134 0.4126 431 TYR A CB 2758 C CG . TYR A 431 ? 1.9450 1.9484 2.2668 0.0754 -0.0075 0.4321 431 TYR A CG 2759 C CD1 . TYR A 431 ? 2.0371 2.0432 2.2970 0.0636 -0.0132 0.4098 431 TYR A CD1 2760 C CD2 . TYR A 431 ? 2.0595 2.0885 2.4055 0.0783 -0.0219 0.4731 431 TYR A CD2 2761 C CE1 . TYR A 431 ? 2.0680 2.0972 2.2857 0.0525 -0.0328 0.4240 431 TYR A CE1 2762 C CE2 . TYR A 431 ? 2.2626 2.3214 2.5676 0.0669 -0.0439 0.4904 431 TYR A CE2 2763 C CZ . TYR A 431 ? 2.1839 2.2407 2.4222 0.0529 -0.0493 0.4638 431 TYR A CZ 2764 O OH . TYR A 431 ? 2.2552 2.3354 2.4457 0.0385 -0.0713 0.4774 431 TYR A OH 2765 N N . THR A 432 ? 1.7938 1.7264 2.2772 0.1096 0.0403 0.4127 432 THR A N 2766 C CA . THR A 432 ? 1.5742 1.4703 2.1062 0.1200 0.0595 0.4078 432 THR A CA 2767 C C . THR A 432 ? 1.4743 1.3377 2.0049 0.1139 0.0690 0.4056 432 THR A C 2768 O O . THR A 432 ? 1.5418 1.3673 2.0889 0.1146 0.0850 0.3824 432 THR A O 2769 C CB . THR A 432 ? 1.6496 1.5545 2.2449 0.1373 0.0606 0.4418 432 THR A CB 2770 O OG1 . THR A 432 ? 1.6165 1.5630 2.2077 0.1356 0.0389 0.4822 432 THR A OG1 2771 C CG2 . THR A 432 ? 1.7825 1.6942 2.4032 0.1475 0.0682 0.4264 432 THR A CG2 2772 N N . ASP A 433 ? 1.4286 1.3053 1.9390 0.1066 0.0599 0.4295 433 ASP A N 2773 C CA . ASP A 433 ? 1.6302 1.4792 2.1480 0.0998 0.0691 0.4326 433 ASP A CA 2774 C C . ASP A 433 ? 1.7770 1.6454 2.2498 0.0877 0.0623 0.4422 433 ASP A C 2775 O O . ASP A 433 ? 1.8686 1.7651 2.2968 0.0847 0.0524 0.4398 433 ASP A O 2776 C CB . ASP A 433 ? 1.6957 1.5317 2.2685 0.1102 0.0730 0.4686 433 ASP A CB 2777 C CG . ASP A 433 ? 1.7732 1.6500 2.3485 0.1165 0.0569 0.5118 433 ASP A CG 2778 O OD1 . ASP A 433 ? 1.8753 1.7852 2.4206 0.1154 0.0438 0.5077 433 ASP A OD1 2779 O OD2 . ASP A 433 ? 1.7641 1.6402 2.3679 0.1206 0.0561 0.5503 433 ASP A OD2 2780 N N . GLU A 434 ? 1.8813 1.7330 2.3662 0.0807 0.0693 0.4532 434 GLU A N 2781 C CA . GLU A 434 ? 1.9261 1.7982 2.3773 0.0718 0.0669 0.4696 434 GLU A CA 2782 C C . GLU A 434 ? 1.8649 1.7742 2.2840 0.0759 0.0543 0.4982 434 GLU A C 2783 O O . GLU A 434 ? 1.6680 1.5963 2.0343 0.0712 0.0516 0.4893 434 GLU A O 2784 C CB . GLU A 434 ? 2.1306 1.9837 2.6151 0.0650 0.0752 0.4909 434 GLU A CB 2785 C CG . GLU A 434 ? 2.1989 2.0310 2.6844 0.0506 0.0836 0.4641 434 GLU A CG 2786 C CD . GLU A 434 ? 2.3159 2.1752 2.7537 0.0435 0.0834 0.4520 434 GLU A CD 2787 O OE1 . GLU A 434 ? 2.2478 2.1322 2.6668 0.0425 0.0845 0.4786 434 GLU A OE1 2788 O OE2 . GLU A 434 ? 2.1613 2.0163 2.5802 0.0402 0.0839 0.4167 434 GLU A OE2 2789 N N . THR A 435 ? 1.9021 1.8205 2.3513 0.0844 0.0469 0.5326 435 THR A N 2790 C CA . THR A 435 ? 1.8326 1.7878 2.2495 0.0858 0.0308 0.5586 435 THR A CA 2791 C C . THR A 435 ? 1.8529 1.8215 2.2468 0.0863 0.0205 0.5338 435 THR A C 2792 O O . THR A 435 ? 1.8693 1.8224 2.2909 0.0912 0.0254 0.5088 435 THR A O 2793 C CB . THR A 435 ? 1.8475 1.8156 2.3069 0.0949 0.0218 0.6057 435 THR A CB 2794 O OG1 . THR A 435 ? 1.8064 1.8082 2.2480 0.0965 0.0024 0.6152 435 THR A OG1 2795 C CG2 . THR A 435 ? 1.5750 1.5113 2.1076 0.1060 0.0327 0.6079 435 THR A CG2 2796 N N . PHE A 436 ? 1.8736 1.8703 2.2157 0.0804 0.0065 0.5417 436 PHE A N 2797 C CA . PHE A 436 ? 1.9543 1.9640 2.2760 0.0778 -0.0052 0.5210 436 PHE A CA 2798 C C . PHE A 436 ? 2.0338 2.0780 2.3615 0.0777 -0.0276 0.5560 436 PHE A C 2799 O O . PHE A 436 ? 2.3532 2.4185 2.6241 0.0668 -0.0424 0.5629 436 PHE A O 2800 C CB . PHE A 436 ? 1.9587 1.9661 2.2081 0.0674 -0.0033 0.4900 436 PHE A CB 2801 C CG . PHE A 436 ? 1.8683 1.8486 2.1151 0.0676 0.0156 0.4546 436 PHE A CG 2802 C CD1 . PHE A 436 ? 1.8720 1.8392 2.1287 0.0679 0.0302 0.4601 436 PHE A CD1 2803 C CD2 . PHE A 436 ? 1.7941 1.7655 2.0263 0.0656 0.0176 0.4181 436 PHE A CD2 2804 C CE1 . PHE A 436 ? 1.7182 1.6669 1.9729 0.0658 0.0439 0.4304 436 PHE A CE1 2805 C CE2 . PHE A 436 ? 1.6182 1.5692 1.8457 0.0650 0.0325 0.3888 436 PHE A CE2 2806 C CZ . PHE A 436 ? 1.5614 1.5025 1.8004 0.0647 0.0446 0.3952 436 PHE A CZ 2807 N N . LYS A 437 ? 1.8730 1.9230 2.2685 0.0894 -0.0301 0.5792 437 LYS A N 2808 C CA . LYS A 437 ? 1.9858 2.0707 2.3960 0.0892 -0.0511 0.5950 437 LYS A CA 2809 C C . LYS A 437 ? 1.8689 1.9473 2.3492 0.1036 -0.0422 0.5873 437 LYS A C 2810 O O . LYS A 437 ? 1.5890 1.6397 2.1207 0.1174 -0.0236 0.5899 437 LYS A O 2811 C CB . LYS A 437 ? 2.2591 2.3832 2.6609 0.0848 -0.0747 0.6448 437 LYS A CB 2812 C CG . LYS A 437 ? 2.4977 2.6335 2.9723 0.1005 -0.0763 0.6940 437 LYS A CG 2813 C CD . LYS A 437 ? 2.4472 2.6194 2.8937 0.0925 -0.0987 0.7422 437 LYS A CD 2814 C CE . LYS A 437 ? 2.3750 2.5275 2.7877 0.0897 -0.0858 0.7525 437 LYS A CE 2815 N NZ . LYS A 437 ? 2.1474 2.2620 2.5193 0.0845 -0.0634 0.7050 437 LYS A NZ 2816 N N . THR A 438 ? 2.0459 2.1467 2.5223 0.0988 -0.0539 0.5746 438 THR A N 2817 C CA . THR A 438 ? 2.0442 2.1452 2.5788 0.1112 -0.0447 0.5637 438 THR A CA 2818 C C . THR A 438 ? 1.8093 1.8719 2.3316 0.1119 -0.0220 0.5118 438 THR A C 2819 O O . THR A 438 ? 1.5619 1.5871 2.0708 0.1127 -0.0049 0.4925 438 THR A O 2820 C CB . THR A 438 ? 2.2690 2.3751 2.8877 0.1328 -0.0380 0.6021 438 THR A CB 2821 O OG1 . THR A 438 ? 2.3628 2.4285 2.9943 0.1408 -0.0191 0.6046 438 THR A OG1 2822 C CG2 . THR A 438 ? 2.2026 2.3619 2.8374 0.1308 -0.0666 0.6559 438 THR A CG2 2823 N N . ARG A 439 ? 1.8367 1.9127 2.3645 0.1100 -0.0238 0.4931 439 ARG A N 2824 C CA . ARG A 439 ? 1.9303 1.9788 2.4402 0.1083 -0.0063 0.4464 439 ARG A CA 2825 C C . ARG A 439 ? 2.0102 2.0684 2.5734 0.1200 0.0041 0.4405 439 ARG A C 2826 O O . ARG A 439 ? 2.1819 2.2712 2.8003 0.1303 -0.0025 0.4739 439 ARG A O 2827 C CB . ARG A 439 ? 1.8564 1.9113 2.2952 0.0883 -0.0191 0.4233 439 ARG A CB 2828 C CG . ARG A 439 ? 1.9019 1.9806 2.2957 0.0741 -0.0431 0.4462 439 ARG A CG 2829 C CD . ARG A 439 ? 2.0214 2.1288 2.3907 0.0581 -0.0638 0.4430 439 ARG A CD 2830 N NE . ARG A 439 ? 2.2554 2.3692 2.5536 0.0394 -0.0826 0.4469 439 ARG A NE 2831 C CZ . ARG A 439 ? 2.3243 2.4634 2.6132 0.0338 -0.1022 0.4825 439 ARG A CZ 2832 N NH1 . ARG A 439 ? 2.3634 2.5266 2.7162 0.0468 -0.1069 0.5214 439 ARG A NH1 2833 N NH2 . ARG A 439 ? 2.3776 2.5163 2.5911 0.0158 -0.1161 0.4797 439 ARG A NH2 2834 N N . GLU A 440 ? 1.9487 1.9829 2.4959 0.1189 0.0209 0.4007 440 GLU A N 2835 C CA . GLU A 440 ? 1.8231 1.8655 2.4110 0.1288 0.0343 0.3907 440 GLU A CA 2836 C C . GLU A 440 ? 1.7433 1.8249 2.3121 0.1135 0.0143 0.3921 440 GLU A C 2837 O O . GLU A 440 ? 1.7426 1.8267 2.2518 0.0946 -0.0031 0.3847 440 GLU A O 2838 C CB . GLU A 440 ? 1.9410 1.9394 2.5162 0.1332 0.0617 0.3485 440 GLU A CB 2839 C CG . GLU A 440 ? 2.1368 2.0979 2.6584 0.1230 0.0652 0.3235 440 GLU A CG 2840 C CD . GLU A 440 ? 2.3006 2.2372 2.8416 0.1298 0.0707 0.3391 440 GLU A CD 2841 O OE1 . GLU A 440 ? 2.3861 2.2895 2.9600 0.1417 0.0919 0.3302 440 GLU A OE1 2842 O OE2 . GLU A 440 ? 2.1041 2.0520 2.6256 0.1225 0.0548 0.3604 440 GLU A OE2 2843 N N . ALA A 441 ? 1.8929 2.0031 2.5118 0.1210 0.0182 0.4017 441 ALA A N 2844 C CA . ALA A 441 ? 2.0865 2.2463 2.7061 0.1049 -0.0068 0.4175 441 ALA A CA 2845 C C . ALA A 441 ? 2.0393 2.1943 2.5985 0.0824 -0.0141 0.3860 441 ALA A C 2846 O O . ALA A 441 ? 1.7326 1.8571 2.2715 0.0844 0.0067 0.3515 441 ALA A O 2847 C CB . ALA A 441 ? 1.8439 2.0458 2.5477 0.1202 -0.0022 0.4472 441 ALA A CB 2848 N N . ILE A 442 ? 2.2104 2.3942 2.7395 0.0600 -0.0445 0.3995 442 ILE A N 2849 C CA . ILE A 442 ? 2.5409 2.7161 3.0069 0.0358 -0.0552 0.3735 442 ILE A CA 2850 C C . ILE A 442 ? 2.6997 2.8792 3.1913 0.0373 -0.0389 0.3557 442 ILE A C 2851 O O . ILE A 442 ? 2.6565 2.8592 3.2172 0.0538 -0.0257 0.3708 442 ILE A O 2852 C CB . ILE A 442 ? 2.6505 2.8554 3.0819 0.0099 -0.0926 0.3947 442 ILE A CB 2853 C CG1 . ILE A 442 ? 2.5628 2.7472 2.9183 -0.0168 -0.1032 0.3659 442 ILE A CG1 2854 C CG2 . ILE A 442 ? 2.7182 2.9833 3.2187 0.0092 -0.1122 0.4373 442 ILE A CG2 2855 C CD1 . ILE A 442 ? 1.9900 2.1846 2.2887 -0.0434 -0.1357 0.3770 442 ILE A CD1 2856 N N . GLN A 443 ? 2.8410 2.9962 3.2783 0.0224 -0.0364 0.3246 443 GLN A N 2857 C CA . GLN A 443 ? 2.4648 2.6170 2.9169 0.0242 -0.0173 0.3051 443 GLN A CA 2858 C C . GLN A 443 ? 2.2960 2.4745 2.7439 0.0005 -0.0343 0.3082 443 GLN A C 2859 O O . GLN A 443 ? 2.1293 2.2832 2.5157 -0.0185 -0.0419 0.2872 443 GLN A O 2860 C CB . GLN A 443 ? 2.3041 2.4061 2.7057 0.0286 0.0040 0.2679 443 GLN A CB 2861 C CG . GLN A 443 ? 2.1909 2.2721 2.6209 0.0528 0.0312 0.2595 443 GLN A CG 2862 C CD . GLN A 443 ? 2.3825 2.4948 2.8894 0.0692 0.0407 0.2829 443 GLN A CD 2863 O OE1 . GLN A 443 ? 2.3136 2.4557 2.8535 0.0666 0.0429 0.2901 443 GLN A OE1 2864 N NE2 . GLN A 443 ? 2.5116 2.6187 3.0511 0.0866 0.0468 0.2978 443 GLN A NE2 2865 N N . HIS A 444 ? 2.1624 2.3894 2.6769 0.0012 -0.0390 0.3345 444 HIS A N 2866 C CA . HIS A 444 ? 2.4190 2.6705 2.9317 -0.0243 -0.0544 0.3365 444 HIS A CA 2867 C C . HIS A 444 ? 2.3035 2.5175 2.7834 -0.0234 -0.0298 0.3018 444 HIS A C 2868 O O . HIS A 444 ? 2.2418 2.4378 2.6715 -0.0464 -0.0400 0.2855 444 HIS A O 2869 C CB . HIS A 444 ? 2.7436 3.0594 3.3415 -0.0236 -0.0607 0.3721 444 HIS A CB 2870 C CG . HIS A 444 ? 2.9494 3.2973 3.5423 -0.0586 -0.0896 0.3824 444 HIS A CG 2871 N ND1 . HIS A 444 ? 2.9036 3.3077 3.5335 -0.0757 -0.1232 0.4200 444 HIS A ND1 2872 C CD2 . HIS A 444 ? 2.7505 3.0808 3.3052 -0.0818 -0.0911 0.3607 444 HIS A CD2 2873 C CE1 . HIS A 444 ? 2.6827 3.1017 3.2962 -0.1100 -0.1451 0.4192 444 HIS A CE1 2874 N NE2 . HIS A 444 ? 2.6186 2.9912 3.1870 -0.1137 -0.1250 0.3832 444 HIS A NE2 2875 N N . GLU A 445 ? 2.1891 2.3872 2.6930 0.0029 0.0027 0.2902 445 GLU A N 2876 C CA . GLU A 445 ? 2.1989 2.3621 2.6706 0.0061 0.0273 0.2588 445 GLU A CA 2877 C C . GLU A 445 ? 2.1601 2.2764 2.5501 -0.0058 0.0204 0.2327 445 GLU A C 2878 O O . GLU A 445 ? 2.0682 2.1750 2.4216 -0.0261 0.0114 0.2230 445 GLU A O 2879 C CB . GLU A 445 ? 2.2023 2.3536 2.7066 0.0350 0.0617 0.2500 445 GLU A CB 2880 C CG . GLU A 445 ? 2.2076 2.4015 2.7911 0.0490 0.0771 0.2723 445 GLU A CG 2881 C CD . GLU A 445 ? 2.2647 2.4627 2.8545 0.0483 0.1004 0.2599 445 GLU A CD 2882 O OE1 . GLU A 445 ? 2.4192 2.5773 2.9578 0.0484 0.1158 0.2299 445 GLU A OE1 2883 O OE2 . GLU A 445 ? 1.9353 2.1792 2.5834 0.0479 0.1039 0.2824 445 GLU A OE2 2884 N N . SER A 446 ? 2.1799 2.2676 2.5443 0.0064 0.0248 0.2239 446 SER A N 2885 C CA . SER A 446 ? 1.9692 2.0162 2.2632 -0.0011 0.0219 0.2023 446 SER A CA 2886 C C . SER A 446 ? 1.7195 1.7652 1.9797 -0.0137 -0.0032 0.2128 446 SER A C 2887 O O . SER A 446 ? 1.5753 1.6092 1.8241 -0.0042 -0.0034 0.2157 446 SER A O 2888 C CB . SER A 446 ? 2.1880 2.2037 2.4693 0.0172 0.0441 0.1837 446 SER A CB 2889 O OG . SER A 446 ? 2.4112 2.4305 2.7207 0.0315 0.0452 0.1962 446 SER A OG 2890 N N . GLY A 447 ? 1.5799 1.6360 1.8209 -0.0369 -0.0236 0.2177 447 GLY A N 2891 C CA . GLY A 447 ? 1.6399 1.7016 1.8500 -0.0535 -0.0505 0.2303 447 GLY A CA 2892 C C . GLY A 447 ? 1.5422 1.5753 1.7008 -0.0493 -0.0521 0.2247 447 GLY A C 2893 O O . GLY A 447 ? 1.5218 1.5654 1.7031 -0.0349 -0.0512 0.2396 447 GLY A O 2894 N N . ILE A 448 ? 1.5590 1.5558 1.6501 -0.0616 -0.0532 0.2050 448 ILE A N 2895 C CA . ILE A 448 ? 1.6456 1.6156 1.6812 -0.0595 -0.0537 0.2001 448 ILE A CA 2896 C C . ILE A 448 ? 1.7589 1.7101 1.7974 -0.0351 -0.0301 0.1921 448 ILE A C 2897 O O . ILE A 448 ? 1.6558 1.5983 1.6706 -0.0287 -0.0292 0.1975 448 ILE A O 2898 C CB . ILE A 448 ? 1.6372 1.5691 1.5986 -0.0783 -0.0577 0.1803 448 ILE A CB 2899 C CG1 . ILE A 448 ? 1.6748 1.5828 1.5798 -0.0746 -0.0561 0.1784 448 ILE A CG1 2900 C CG2 . ILE A 448 ? 1.4073 1.3088 1.3573 -0.0742 -0.0374 0.1570 448 ILE A CG2 2901 C CD1 . ILE A 448 ? 1.6477 1.5375 1.4857 -0.0992 -0.0742 0.1743 448 ILE A CD1 2902 N N . LEU A 449 ? 1.6836 1.6304 1.7504 -0.0237 -0.0118 0.1803 449 LEU A N 2903 C CA . LEU A 449 ? 1.6024 1.5312 1.6703 -0.0054 0.0086 0.1698 449 LEU A CA 2904 C C . LEU A 449 ? 1.6543 1.5960 1.7520 0.0068 0.0084 0.1865 449 LEU A C 2905 O O . LEU A 449 ? 1.7522 1.7207 1.8943 0.0084 0.0000 0.2051 449 LEU A O 2906 C CB . LEU A 449 ? 1.4775 1.4066 1.5755 0.0020 0.0246 0.1579 449 LEU A CB 2907 C CG . LEU A 449 ? 1.6029 1.5221 1.6802 -0.0099 0.0261 0.1450 449 LEU A CG 2908 C CD1 . LEU A 449 ? 1.6974 1.6445 1.8022 -0.0243 0.0108 0.1579 449 LEU A CD1 2909 C CD2 . LEU A 449 ? 1.6123 1.5229 1.6997 -0.0004 0.0458 0.1306 449 LEU A CD2 2910 N N . GLY A 450 ? 1.7202 1.6438 1.7965 0.0154 0.0181 0.1823 450 GLY A N 2911 C CA . GLY A 450 ? 1.6560 1.5856 1.7648 0.0276 0.0228 0.1951 450 GLY A CA 2912 C C . GLY A 450 ? 1.5701 1.5002 1.7249 0.0376 0.0361 0.1877 450 GLY A C 2913 O O . GLY A 450 ? 1.7959 1.7237 1.9534 0.0359 0.0426 0.1731 450 GLY A O 2914 N N . PRO A 451 ? 1.4529 1.3828 1.6413 0.0475 0.0415 0.1973 451 PRO A N 2915 C CA . PRO A 451 ? 1.5103 1.4345 1.7410 0.0572 0.0556 0.1903 451 PRO A CA 2916 C C . PRO A 451 ? 1.5006 1.4048 1.7135 0.0572 0.0700 0.1637 451 PRO A C 2917 O O . PRO A 451 ? 1.4233 1.3177 1.5974 0.0525 0.0700 0.1544 451 PRO A O 2918 C CB . PRO A 451 ? 1.6972 1.6155 1.9505 0.0641 0.0571 0.2053 451 PRO A CB 2919 C CG . PRO A 451 ? 1.5968 1.5123 1.8082 0.0581 0.0501 0.2104 451 PRO A CG 2920 C CD . PRO A 451 ? 1.4472 1.3770 1.6292 0.0493 0.0366 0.2147 451 PRO A CD 2921 N N . LEU A 452 ? 1.4316 1.3304 1.6725 0.0632 0.0830 0.1531 452 LEU A N 2922 C CA . LEU A 452 ? 1.5002 1.3838 1.7204 0.0611 0.0951 0.1285 452 LEU A CA 2923 C C . LEU A 452 ? 1.4118 1.2747 1.6255 0.0609 0.1013 0.1184 452 LEU A C 2924 O O . LEU A 452 ? 1.5764 1.4257 1.8167 0.0658 0.1105 0.1148 452 LEU A O 2925 C CB . LEU A 452 ? 1.6515 1.5372 1.8972 0.0666 0.1088 0.1196 452 LEU A CB 2926 C CG . LEU A 452 ? 1.6691 1.5490 1.8887 0.0623 0.1190 0.0988 452 LEU A CG 2927 C CD1 . LEU A 452 ? 1.5296 1.4005 1.7717 0.0703 0.1393 0.0861 452 LEU A CD1 2928 C CD2 . LEU A 452 ? 1.5106 1.3770 1.6867 0.0550 0.1164 0.0863 452 LEU A CD2 2929 N N . LEU A 453 ? 1.3092 1.1685 1.4891 0.0547 0.0973 0.1136 453 LEU A N 2930 C CA . LEU A 453 ? 1.3811 1.2263 1.5586 0.0512 0.1004 0.1064 453 LEU A CA 2931 C C . LEU A 453 ? 1.4329 1.2668 1.5970 0.0470 0.1094 0.0836 453 LEU A C 2932 O O . LEU A 453 ? 1.6035 1.4434 1.7435 0.0450 0.1105 0.0758 453 LEU A O 2933 C CB . LEU A 453 ? 1.2790 1.1307 1.4343 0.0476 0.0931 0.1160 453 LEU A CB 2934 C CG . LEU A 453 ? 1.2755 1.1357 1.4388 0.0507 0.0861 0.1385 453 LEU A CG 2935 C CD1 . LEU A 453 ? 1.2754 1.1460 1.4450 0.0542 0.0806 0.1484 453 LEU A CD1 2936 C CD2 . LEU A 453 ? 1.3071 1.1742 1.4415 0.0495 0.0837 0.1463 453 LEU A CD2 2937 N N . TYR A 454 ? 1.3727 1.1877 1.5500 0.0447 0.1161 0.0730 454 TYR A N 2938 C CA . TYR A 454 ? 1.4218 1.2238 1.5797 0.0388 0.1245 0.0500 454 TYR A CA 2939 C C . TYR A 454 ? 1.4501 1.2375 1.6025 0.0271 0.1203 0.0433 454 TYR A C 2940 O O . TYR A 454 ? 1.5619 1.3436 1.7363 0.0263 0.1162 0.0551 454 TYR A O 2941 C CB . TYR A 454 ? 1.5459 1.3340 1.7230 0.0470 0.1409 0.0390 454 TYR A CB 2942 C CG . TYR A 454 ? 1.7499 1.5176 1.9032 0.0409 0.1535 0.0125 454 TYR A CG 2943 C CD1 . TYR A 454 ? 1.8478 1.6262 1.9676 0.0362 0.1547 0.0029 454 TYR A CD1 2944 C CD2 . TYR A 454 ? 1.8757 1.6103 2.0366 0.0392 0.1649 -0.0031 454 TYR A CD2 2945 C CE1 . TYR A 454 ? 2.0477 1.8084 2.1394 0.0294 0.1658 -0.0206 454 TYR A CE1 2946 C CE2 . TYR A 454 ? 2.0130 1.7249 2.1431 0.0317 0.1769 -0.0301 454 TYR A CE2 2947 C CZ . TYR A 454 ? 2.0586 1.7857 2.1527 0.0266 0.1769 -0.0384 454 TYR A CZ 2948 O OH . TYR A 454 ? 2.0033 1.7095 2.0607 0.0179 0.1883 -0.0643 454 TYR A OH 2949 N N . GLY A 455 ? 1.4370 1.2208 1.5600 0.0161 0.1198 0.0269 455 GLY A N 2950 C CA . GLY A 455 ? 1.3919 1.1594 1.5081 0.0003 0.1151 0.0162 455 GLY A CA 2951 C C . GLY A 455 ? 1.4635 1.2321 1.5414 -0.0123 0.1131 -0.0014 455 GLY A C 2952 O O . GLY A 455 ? 1.3866 1.1797 1.4450 -0.0111 0.1076 0.0055 455 GLY A O 2953 N N . GLU A 456 ? 1.5193 1.2586 1.5845 -0.0247 0.1178 -0.0238 456 GLU A N 2954 C CA . GLU A 456 ? 1.6422 1.3786 1.6651 -0.0409 0.1147 -0.0428 456 GLU A CA 2955 C C . GLU A 456 ? 1.5682 1.3247 1.5828 -0.0604 0.0927 -0.0333 456 GLU A C 2956 O O . GLU A 456 ? 1.6679 1.4272 1.7103 -0.0646 0.0840 -0.0195 456 GLU A O 2957 C CB . GLU A 456 ? 1.8388 1.5303 1.8472 -0.0487 0.1288 -0.0724 456 GLU A CB 2958 C CG . GLU A 456 ? 1.9847 1.6569 2.0053 -0.0283 0.1542 -0.0815 456 GLU A CG 2959 C CD . GLU A 456 ? 2.1617 1.7824 2.1723 -0.0333 0.1721 -0.1100 456 GLU A CD 2960 O OE1 . GLU A 456 ? 2.2893 1.8839 2.3232 -0.0383 0.1700 -0.1097 456 GLU A OE1 2961 O OE2 . GLU A 456 ? 2.0989 1.7026 2.0770 -0.0322 0.1898 -0.1326 456 GLU A OE2 2962 N N . VAL A 457 ? 1.4687 1.2424 1.4483 -0.0726 0.0834 -0.0376 457 VAL A N 2963 C CA . VAL A 457 ? 1.4139 1.2111 1.3903 -0.0932 0.0609 -0.0265 457 VAL A CA 2964 C C . VAL A 457 ? 1.6003 1.3692 1.5873 -0.1135 0.0548 -0.0379 457 VAL A C 2965 O O . VAL A 457 ? 1.7232 1.4478 1.6983 -0.1177 0.0676 -0.0641 457 VAL A O 2966 C CB . VAL A 457 ? 1.3418 1.1601 1.2773 -0.1069 0.0499 -0.0299 457 VAL A CB 2967 C CG1 . VAL A 457 ? 1.3634 1.2049 1.2917 -0.0866 0.0574 -0.0168 457 VAL A CG1 2968 C CG2 . VAL A 457 ? 1.5381 1.3220 1.4298 -0.1233 0.0558 -0.0632 457 VAL A CG2 2969 N N . GLY A 458 ? 1.7158 1.5085 1.7282 -0.1248 0.0377 -0.0170 458 GLY A N 2970 C CA . GLY A 458 ? 1.6058 1.3743 1.6351 -0.1463 0.0301 -0.0226 458 GLY A CA 2971 C C . GLY A 458 ? 1.4788 1.2332 1.5517 -0.1308 0.0407 -0.0093 458 GLY A C 2972 O O . GLY A 458 ? 1.4212 1.1849 1.5241 -0.1419 0.0304 0.0079 458 GLY A O 2973 N N . ASP A 459 ? 1.5655 1.3008 1.6420 -0.1060 0.0607 -0.0153 459 ASP A N 2974 C CA . ASP A 459 ? 1.5884 1.3144 1.7032 -0.0857 0.0723 -0.0003 459 ASP A CA 2975 C C . ASP A 459 ? 1.4604 1.2261 1.6024 -0.0766 0.0644 0.0334 459 ASP A C 2976 O O . ASP A 459 ? 1.3889 1.1920 1.5208 -0.0746 0.0565 0.0464 459 ASP A O 2977 C CB . ASP A 459 ? 1.6861 1.4062 1.7970 -0.0605 0.0901 -0.0061 459 ASP A CB 2978 C CG . ASP A 459 ? 1.8486 1.5215 1.9639 -0.0554 0.1087 -0.0276 459 ASP A CG 2979 O OD1 . ASP A 459 ? 1.8643 1.4998 1.9665 -0.0733 0.1103 -0.0496 459 ASP A OD1 2980 O OD2 . ASP A 459 ? 1.9331 1.6068 2.0649 -0.0330 0.1223 -0.0220 459 ASP A OD2 2981 N N . THR A 460 ? 1.4042 1.1602 1.5797 -0.0688 0.0692 0.0486 460 THR A N 2982 C CA . THR A 460 ? 1.4317 1.2216 1.6289 -0.0608 0.0643 0.0800 460 THR A CA 2983 C C . THR A 460 ? 1.4956 1.2808 1.7095 -0.0384 0.0751 0.0923 460 THR A C 2984 O O . THR A 460 ? 1.7383 1.4932 1.9718 -0.0360 0.0823 0.0891 460 THR A O 2985 C CB . THR A 460 ? 1.4951 1.2846 1.7201 -0.0790 0.0556 0.0944 460 THR A CB 2986 O OG1 . THR A 460 ? 1.6532 1.4198 1.8676 -0.1061 0.0472 0.0728 460 THR A OG1 2987 C CG2 . THR A 460 ? 1.4586 1.2952 1.6933 -0.0772 0.0483 0.1226 460 THR A CG2 2988 N N . LEU A 461 ? 1.4380 1.2513 1.6436 -0.0225 0.0762 0.1070 461 LEU A N 2989 C CA . LEU A 461 ? 1.3666 1.1810 1.5861 -0.0052 0.0821 0.1230 461 LEU A CA 2990 C C . LEU A 461 ? 1.4670 1.2943 1.7089 -0.0059 0.0792 0.1509 461 LEU A C 2991 O O . LEU A 461 ? 1.4822 1.3258 1.7292 -0.0171 0.0736 0.1608 461 LEU A O 2992 C CB . LEU A 461 ? 1.2509 1.0827 1.4476 0.0094 0.0845 0.1241 461 LEU A CB 2993 C CG . LEU A 461 ? 1.3395 1.1571 1.5225 0.0125 0.0904 0.1009 461 LEU A CG 2994 C CD1 . LEU A 461 ? 1.4799 1.3085 1.6335 0.0058 0.0874 0.0888 461 LEU A CD1 2995 C CD2 . LEU A 461 ? 1.4283 1.2515 1.6102 0.0271 0.0942 0.1059 461 LEU A CD2 2996 N N . LEU A 462 ? 1.4409 1.2640 1.6982 0.0058 0.0829 0.1661 462 LEU A N 2997 C CA . LEU A 462 ? 1.3399 1.1694 1.6205 0.0046 0.0819 0.1933 462 LEU A CA 2998 C C . LEU A 462 ? 1.3288 1.1703 1.6067 0.0202 0.0835 0.2133 462 LEU A C 2999 O O . LEU A 462 ? 1.2927 1.1212 1.5904 0.0269 0.0849 0.2208 462 LEU A O 3000 C CB . LEU A 462 ? 1.2866 1.0848 1.5988 -0.0054 0.0833 0.1913 462 LEU A CB 3001 C CG . LEU A 462 ? 1.2098 1.0162 1.5428 -0.0188 0.0796 0.2119 462 LEU A CG 3002 C CD1 . LEU A 462 ? 1.2388 1.0060 1.6035 -0.0282 0.0821 0.2104 462 LEU A CD1 3003 C CD2 . LEU A 462 ? 1.1525 0.9884 1.4855 -0.0072 0.0811 0.2437 462 LEU A CD2 3004 N N . ILE A 463 ? 1.3749 1.2413 1.6274 0.0256 0.0834 0.2230 463 ILE A N 3005 C CA . ILE A 463 ? 1.4278 1.3040 1.6604 0.0375 0.0832 0.2328 463 ILE A CA 3006 C C . ILE A 463 ? 1.4249 1.3140 1.6619 0.0399 0.0843 0.2626 463 ILE A C 3007 O O . ILE A 463 ? 1.4966 1.4023 1.7177 0.0404 0.0889 0.2728 463 ILE A O 3008 C CB . ILE A 463 ? 1.4435 1.3309 1.6366 0.0421 0.0848 0.2210 463 ILE A CB 3009 C CG1 . ILE A 463 ? 1.5482 1.4256 1.7361 0.0384 0.0844 0.1940 463 ILE A CG1 3010 C CG2 . ILE A 463 ? 1.5347 1.4258 1.7031 0.0502 0.0826 0.2260 463 ILE A CG2 3011 C CD1 . ILE A 463 ? 1.7503 1.6113 1.9531 0.0402 0.0836 0.1820 463 ILE A CD1 3012 N N . ILE A 464 ? 1.4151 1.2973 1.6749 0.0425 0.0816 0.2787 464 ILE A N 3013 C CA . ILE A 464 ? 1.3856 1.2822 1.6414 0.0461 0.0816 0.3093 464 ILE A CA 3014 C C . ILE A 464 ? 1.4104 1.3177 1.6314 0.0537 0.0766 0.3131 464 ILE A C 3015 O O . ILE A 464 ? 1.3649 1.2689 1.5955 0.0570 0.0692 0.3125 464 ILE A O 3016 C CB . ILE A 464 ? 1.3683 1.2553 1.6660 0.0444 0.0806 0.3321 464 ILE A CB 3017 C CG1 . ILE A 464 ? 1.4384 1.3059 1.7702 0.0329 0.0841 0.3231 464 ILE A CG1 3018 C CG2 . ILE A 464 ? 1.3317 1.2379 1.6193 0.0463 0.0825 0.3651 464 ILE A CG2 3019 C CD1 . ILE A 464 ? 1.4238 1.2611 1.7797 0.0325 0.0841 0.3020 464 ILE A CD1 3020 N N . PHE A 465 ? 1.4319 1.3520 1.6126 0.0558 0.0812 0.3176 465 PHE A N 3021 C CA . PHE A 465 ? 1.4241 1.3488 1.5592 0.0593 0.0771 0.3142 465 PHE A CA 3022 C C . PHE A 465 ? 1.5586 1.4953 1.6716 0.0607 0.0776 0.3420 465 PHE A C 3023 O O . PHE A 465 ? 1.6574 1.6015 1.7661 0.0621 0.0892 0.3557 465 PHE A O 3024 C CB . PHE A 465 ? 1.3741 1.2961 1.4725 0.0613 0.0858 0.2937 465 PHE A CB 3025 C CG . PHE A 465 ? 1.4451 1.3656 1.4877 0.0635 0.0859 0.2912 465 PHE A CG 3026 C CD1 . PHE A 465 ? 1.4615 1.3751 1.4859 0.0601 0.0749 0.2767 465 PHE A CD1 3027 C CD2 . PHE A 465 ? 1.5614 1.4860 1.5683 0.0680 0.0982 0.3027 465 PHE A CD2 3028 C CE1 . PHE A 465 ? 1.5253 1.4325 1.4937 0.0581 0.0736 0.2719 465 PHE A CE1 3029 C CE2 . PHE A 465 ? 1.6319 1.5475 1.5792 0.0687 0.0999 0.2966 465 PHE A CE2 3030 C CZ . PHE A 465 ? 1.5872 1.4923 1.5139 0.0622 0.0863 0.2802 465 PHE A CZ 3031 N N . LYS A 466 ? 1.5480 1.4897 1.6478 0.0598 0.0649 0.3523 466 LYS A N 3032 C CA . LYS A 466 ? 1.5648 1.5183 1.6294 0.0593 0.0633 0.3771 466 LYS A CA 3033 C C . LYS A 466 ? 1.5071 1.4565 1.5091 0.0562 0.0589 0.3610 466 LYS A C 3034 O O . LYS A 466 ? 1.5398 1.4829 1.5408 0.0529 0.0498 0.3407 466 LYS A O 3035 C CB . LYS A 466 ? 1.6020 1.5672 1.6975 0.0583 0.0493 0.4071 466 LYS A CB 3036 C CG . LYS A 466 ? 1.7194 1.6993 1.7771 0.0566 0.0475 0.4370 466 LYS A CG 3037 C CD . LYS A 466 ? 1.7601 1.7554 1.8493 0.0561 0.0323 0.4725 466 LYS A CD 3038 C CE . LYS A 466 ? 1.8606 1.8721 1.8969 0.0522 0.0283 0.4999 466 LYS A CE 3039 N NZ . LYS A 466 ? 1.8643 1.8938 1.9318 0.0530 0.0175 0.5438 466 LYS A NZ 3040 N N . ASN A 467 ? 1.5060 1.4566 1.4541 0.0564 0.0665 0.3698 467 ASN A N 3041 C CA . ASN A 467 ? 1.5891 1.5302 1.4708 0.0503 0.0608 0.3554 467 ASN A CA 3042 C C . ASN A 467 ? 1.6381 1.5932 1.4918 0.0420 0.0443 0.3800 467 ASN A C 3043 O O . ASN A 467 ? 1.8246 1.7862 1.6512 0.0438 0.0528 0.4010 467 ASN A O 3044 C CB . ASN A 467 ? 1.6306 1.5552 1.4588 0.0566 0.0842 0.3410 467 ASN A CB 3045 C CG . ASN A 467 ? 1.6349 1.5407 1.3844 0.0490 0.0810 0.3253 467 ASN A CG 3046 O OD1 . ASN A 467 ? 1.5363 1.4373 1.2759 0.0375 0.0612 0.3128 467 ASN A OD1 3047 N ND2 . ASN A 467 ? 1.7265 1.6204 1.4190 0.0545 0.1016 0.3257 467 ASN A ND2 3048 N N . GLN A 468 ? 1.6206 1.5838 1.4819 0.0325 0.0205 0.3802 468 GLN A N 3049 C CA . GLN A 468 ? 1.8116 1.7898 1.6344 0.0211 0.0010 0.4012 468 GLN A CA 3050 C C . GLN A 468 ? 1.9358 1.8970 1.6897 0.0072 -0.0078 0.3745 468 GLN A C 3051 O O . GLN A 468 ? 2.0217 1.9826 1.7940 0.0000 -0.0216 0.3589 468 GLN A O 3052 C CB . GLN A 468 ? 1.8914 1.8968 1.7766 0.0192 -0.0217 0.4277 468 GLN A CB 3053 C CG . GLN A 468 ? 1.9120 1.9236 1.8732 0.0326 -0.0119 0.4472 468 GLN A CG 3054 C CD . GLN A 468 ? 2.0076 2.0409 2.0334 0.0341 -0.0308 0.4718 468 GLN A CD 3055 O OE1 . GLN A 468 ? 2.0894 2.1406 2.1370 0.0364 -0.0378 0.5093 468 GLN A OE1 3056 N NE2 . GLN A 468 ? 1.8887 1.9217 1.9468 0.0338 -0.0377 0.4533 468 GLN A NE2 3057 N N . ALA A 469 ? 2.0336 1.9782 1.7076 0.0030 0.0022 0.3689 469 ALA A N 3058 C CA . ALA A 469 ? 2.1082 2.0221 1.7071 -0.0090 0.0022 0.3370 469 ALA A CA 3059 C C . ALA A 469 ? 2.2022 2.0891 1.7279 -0.0020 0.0308 0.3280 469 ALA A C 3060 O O . ALA A 469 ? 2.5070 2.4010 2.0554 0.0147 0.0534 0.3423 469 ALA A O 3061 C CB . ALA A 469 ? 2.1045 2.0006 1.7328 -0.0061 0.0070 0.3064 469 ALA A CB 3062 N N . SER A 470 ? 2.0611 1.9156 1.5014 -0.0142 0.0320 0.3041 470 SER A N 3063 C CA . SER A 470 ? 2.1644 1.9925 1.5246 -0.0079 0.0599 0.2988 470 SER A CA 3064 C C . SER A 470 ? 2.2592 2.0560 1.6107 0.0140 0.1005 0.2772 470 SER A C 3065 O O . SER A 470 ? 2.6216 2.4063 1.9271 0.0257 0.1292 0.2813 470 SER A O 3066 C CB . SER A 470 ? 2.1584 1.9631 1.4187 -0.0319 0.0448 0.2864 470 SER A CB 3067 O OG . SER A 470 ? 2.1103 1.8939 1.3603 -0.0491 0.0263 0.2586 470 SER A OG 3068 N N . ARG A 471 ? 2.1557 1.9421 1.5519 0.0206 0.1042 0.2574 471 ARG A N 3069 C CA . ARG A 471 ? 2.1175 1.8803 1.5135 0.0421 0.1403 0.2419 471 ARG A CA 3070 C C . ARG A 471 ? 2.0677 1.8614 1.5551 0.0588 0.1483 0.2572 471 ARG A C 3071 O O . ARG A 471 ? 2.0346 1.8509 1.5864 0.0531 0.1262 0.2623 471 ARG A O 3072 C CB . ARG A 471 ? 2.1985 1.9191 1.5652 0.0379 0.1433 0.2066 471 ARG A CB 3073 C CG . ARG A 471 ? 2.3374 2.0407 1.7248 0.0619 0.1766 0.1952 471 ARG A CG 3074 C CD . ARG A 471 ? 2.4196 2.0666 1.7431 0.0610 0.1916 0.1625 471 ARG A CD 3075 N NE . ARG A 471 ? 2.7144 2.3264 1.9409 0.0521 0.2001 0.1528 471 ARG A NE 3076 C CZ . ARG A 471 ? 2.8666 2.4694 2.0419 0.0238 0.1710 0.1459 471 ARG A CZ 3077 N NH1 . ARG A 471 ? 2.8372 2.4656 2.0560 0.0039 0.1332 0.1495 471 ARG A NH1 3078 N NH2 . ARG A 471 ? 3.1382 2.7072 2.2179 0.0148 0.1800 0.1360 471 ARG A NH2 3079 N N . PRO A 472 ? 2.1250 1.9197 1.6179 0.0791 0.1808 0.2645 472 PRO A N 3080 C CA . PRO A 472 ? 2.1572 1.9735 1.7284 0.0930 0.1900 0.2714 472 PRO A CA 3081 C C . PRO A 472 ? 2.1110 1.9168 1.7145 0.0892 0.1769 0.2485 472 PRO A C 3082 O O . PRO A 472 ? 2.3483 2.1214 1.9163 0.0936 0.1894 0.2254 472 PRO A O 3083 C CB . PRO A 472 ? 2.1883 1.9936 1.7359 0.1143 0.2295 0.2724 472 PRO A CB 3084 C CG . PRO A 472 ? 2.2402 2.0356 1.7161 0.1127 0.2412 0.2813 472 PRO A CG 3085 C CD . PRO A 472 ? 2.1603 1.9436 1.5912 0.0887 0.2092 0.2724 472 PRO A CD 3086 N N . TYR A 473 ? 1.8318 1.6623 1.4992 0.0813 0.1535 0.2553 473 TYR A N 3087 C CA . TYR A 473 ? 1.7547 1.5808 1.4591 0.0793 0.1442 0.2371 473 TYR A CA 3088 C C . TYR A 473 ? 1.6881 1.5414 1.4656 0.0863 0.1462 0.2491 473 TYR A C 3089 O O . TYR A 473 ? 1.7047 1.5794 1.5058 0.0900 0.1514 0.2719 473 TYR A O 3090 C CB . TYR A 473 ? 1.6989 1.5265 1.4089 0.0616 0.1148 0.2306 473 TYR A CB 3091 C CG . TYR A 473 ? 1.7783 1.5793 1.4178 0.0489 0.1076 0.2165 473 TYR A CG 3092 C CD1 . TYR A 473 ? 1.9015 1.6643 1.4897 0.0522 0.1243 0.1930 473 TYR A CD1 3093 C CD2 . TYR A 473 ? 1.8870 1.6996 1.5100 0.0326 0.0837 0.2274 473 TYR A CD2 3094 C CE1 . TYR A 473 ? 2.0866 1.8179 1.6042 0.0371 0.1174 0.1771 473 TYR A CE1 3095 C CE2 . TYR A 473 ? 2.0435 1.8318 1.5973 0.0162 0.0736 0.2138 473 TYR A CE2 3096 C CZ . TYR A 473 ? 2.0682 1.8131 1.5669 0.0173 0.0906 0.1867 473 TYR A CZ 3097 O OH . TYR A 473 ? 1.9575 1.6718 1.3827 -0.0022 0.0805 0.1704 473 TYR A OH 3098 N N . ASN A 474 ? 1.6040 1.4557 1.4145 0.0864 0.1419 0.2344 474 ASN A N 3099 C CA . ASN A 474 ? 1.6218 1.4970 1.4986 0.0877 0.1385 0.2425 474 ASN A CA 3100 C C . ASN A 474 ? 1.5207 1.3941 1.4287 0.0814 0.1251 0.2257 474 ASN A C 3101 O O . ASN A 474 ? 1.4619 1.3187 1.3462 0.0762 0.1181 0.2093 474 ASN A O 3102 C CB . ASN A 474 ? 1.7047 1.5930 1.5984 0.1004 0.1596 0.2535 474 ASN A CB 3103 C CG . ASN A 474 ? 1.5440 1.4164 1.4138 0.1115 0.1758 0.2393 474 ASN A CG 3104 O OD1 . ASN A 474 ? 1.4900 1.3342 1.3171 0.1104 0.1757 0.2210 474 ASN A OD1 3105 N ND2 . ASN A 474 ? 1.4310 1.3221 1.3308 0.1218 0.1897 0.2503 474 ASN A ND2 3106 N N . ILE A 475 ? 1.5808 1.4703 1.5400 0.0801 0.1218 0.2300 475 ILE A N 3107 C CA . ILE A 475 ? 1.6416 1.5275 1.6217 0.0763 0.1153 0.2122 475 ILE A CA 3108 C C . ILE A 475 ? 1.6520 1.5479 1.6544 0.0799 0.1226 0.2105 475 ILE A C 3109 O O . ILE A 475 ? 1.4987 1.4117 1.5370 0.0771 0.1220 0.2223 475 ILE A O 3110 C CB . ILE A 475 ? 1.6708 1.5591 1.6852 0.0672 0.0998 0.2083 475 ILE A CB 3111 C CG1 . ILE A 475 ? 1.7577 1.6570 1.8019 0.0648 0.0954 0.2281 475 ILE A CG1 3112 C CG2 . ILE A 475 ? 1.6195 1.4971 1.6135 0.0625 0.0903 0.1971 475 ILE A CG2 3113 C CD1 . ILE A 475 ? 1.9737 1.8707 2.0494 0.0595 0.0834 0.2248 475 ILE A CD1 3114 N N . TYR A 476 ? 1.5756 1.4605 1.5574 0.0841 0.1276 0.1966 476 TYR A N 3115 C CA . TYR A 476 ? 1.4738 1.3684 1.4765 0.0843 0.1283 0.1921 476 TYR A CA 3116 C C . TYR A 476 ? 1.4375 1.3199 1.4368 0.0778 0.1198 0.1723 476 TYR A C 3117 O O . TYR A 476 ? 1.2644 1.1289 1.2381 0.0765 0.1179 0.1621 476 TYR A O 3118 C CB . TYR A 476 ? 1.4090 1.3059 1.3963 0.0977 0.1447 0.1991 476 TYR A CB 3119 C CG . TYR A 476 ? 1.4412 1.3654 1.4635 0.0982 0.1453 0.2106 476 TYR A CG 3120 C CD1 . TYR A 476 ? 1.5805 1.5091 1.6105 0.0954 0.1399 0.2026 476 TYR A CD1 3121 C CD2 . TYR A 476 ? 1.5597 1.5081 1.6072 0.1000 0.1505 0.2318 476 TYR A CD2 3122 C CE1 . TYR A 476 ? 1.8085 1.7666 1.8695 0.0930 0.1371 0.2152 476 TYR A CE1 3123 C CE2 . TYR A 476 ? 1.7309 1.7095 1.8140 0.0974 0.1485 0.2449 476 TYR A CE2 3124 C CZ . TYR A 476 ? 1.8057 1.7896 1.8946 0.0933 0.1405 0.2365 476 TYR A CZ 3125 O OH . TYR A 476 ? 1.8502 1.8680 1.9733 0.0879 0.1350 0.2515 476 TYR A OH 3126 N N . PRO A 477 ? 1.4377 1.3307 1.4623 0.0716 0.1140 0.1673 477 PRO A N 3127 C CA . PRO A 477 ? 1.4384 1.3216 1.4563 0.0671 0.1097 0.1503 477 PRO A CA 3128 C C . PRO A 477 ? 1.6086 1.4972 1.6182 0.0720 0.1152 0.1507 477 PRO A C 3129 O O . PRO A 477 ? 1.6268 1.5351 1.6525 0.0736 0.1165 0.1627 477 PRO A O 3130 C CB . PRO A 477 ? 1.3414 1.2294 1.3888 0.0563 0.1006 0.1437 477 PRO A CB 3131 C CG . PRO A 477 ? 1.3246 1.2286 1.3950 0.0536 0.0996 0.1575 477 PRO A CG 3132 C CD . PRO A 477 ? 1.4391 1.3500 1.4985 0.0643 0.1087 0.1751 477 PRO A CD 3133 N N . HIS A 478 ? 1.8270 1.7003 1.8143 0.0738 0.1179 0.1405 478 HIS A N 3134 C CA . HIS A 478 ? 1.9295 1.8073 1.9111 0.0778 0.1219 0.1420 478 HIS A CA 3135 C C . HIS A 478 ? 1.8243 1.7087 1.8156 0.0661 0.1128 0.1303 478 HIS A C 3136 O O . HIS A 478 ? 1.5171 1.3912 1.5080 0.0590 0.1091 0.1167 478 HIS A O 3137 C CB . HIS A 478 ? 1.9081 1.7621 1.8584 0.0876 0.1332 0.1407 478 HIS A CB 3138 C CG . HIS A 478 ? 1.9458 1.7937 1.8868 0.0871 0.1345 0.1361 478 HIS A CG 3139 N ND1 . HIS A 478 ? 1.8085 1.6350 1.7320 0.0812 0.1340 0.1234 478 HIS A ND1 3140 C CD2 . HIS A 478 ? 2.1592 2.0225 2.1075 0.0909 0.1356 0.1451 478 HIS A CD2 3141 C CE1 . HIS A 478 ? 1.8761 1.7025 1.7953 0.0820 0.1364 0.1244 478 HIS A CE1 3142 N NE2 . HIS A 478 ? 2.0172 1.8659 1.9499 0.0881 0.1369 0.1377 478 HIS A NE2 3143 N N . GLY A 479 ? 1.9081 1.8123 1.9088 0.0640 0.1094 0.1371 479 GLY A N 3144 C CA . GLY A 479 ? 1.9335 1.8444 1.9355 0.0519 0.1013 0.1265 479 GLY A CA 3145 C C . GLY A 479 ? 1.9004 1.8332 1.9230 0.0415 0.0913 0.1322 479 GLY A C 3146 O O . GLY A 479 ? 1.8798 1.8303 1.9007 0.0342 0.0840 0.1357 479 GLY A O 3147 N N . ILE A 480 ? 1.6908 1.6225 1.7318 0.0393 0.0899 0.1346 480 ILE A N 3148 C CA . ILE A 480 ? 1.6569 1.6065 1.7227 0.0283 0.0811 0.1428 480 ILE A CA 3149 C C . ILE A 480 ? 1.7376 1.7137 1.8190 0.0371 0.0842 0.1687 480 ILE A C 3150 O O . ILE A 480 ? 1.8553 1.8280 1.9280 0.0545 0.0969 0.1789 480 ILE A O 3151 C CB . ILE A 480 ? 1.5474 1.4826 1.6300 0.0227 0.0799 0.1373 480 ILE A CB 3152 C CG1 . ILE A 480 ? 1.6399 1.5487 1.7122 0.0220 0.0827 0.1167 480 ILE A CG1 3153 C CG2 . ILE A 480 ? 1.4070 1.3523 1.5119 0.0050 0.0690 0.1392 480 ILE A CG2 3154 C CD1 . ILE A 480 ? 1.7312 1.6268 1.8195 0.0248 0.0850 0.1184 480 ILE A CD1 3155 N N . THR A 481 ? 1.5910 1.5919 1.6959 0.0238 0.0734 0.1788 481 THR A N 3156 C CA . THR A 481 ? 1.5016 1.5386 1.6277 0.0291 0.0738 0.2060 481 THR A CA 3157 C C . THR A 481 ? 1.5258 1.5803 1.6855 0.0194 0.0694 0.2203 481 THR A C 3158 O O . THR A 481 ? 1.7435 1.8259 1.9251 0.0292 0.0764 0.2459 481 THR A O 3159 C CB . THR A 481 ? 1.5477 1.6105 1.6745 0.0175 0.0598 0.2104 481 THR A CB 3160 O OG1 . THR A 481 ? 1.6083 1.6665 1.7360 -0.0090 0.0427 0.1940 481 THR A OG1 3161 C CG2 . THR A 481 ? 1.6259 1.6756 1.7212 0.0275 0.0648 0.2017 481 THR A CG2 3162 N N . ASP A 482 ? 1.6338 1.6714 1.7995 0.0007 0.0597 0.2052 482 ASP A N 3163 C CA . ASP A 482 ? 1.7074 1.7567 1.9065 -0.0117 0.0549 0.2186 482 ASP A CA 3164 C C . ASP A 482 ? 1.6767 1.7024 1.8764 -0.0009 0.0670 0.2187 482 ASP A C 3165 O O . ASP A 482 ? 1.9417 1.9374 2.1382 -0.0091 0.0639 0.2013 482 ASP A O 3166 C CB . ASP A 482 ? 1.8087 1.8501 2.0143 -0.0415 0.0362 0.2030 482 ASP A CB 3167 C CG . ASP A 482 ? 1.9523 2.0091 2.1966 -0.0596 0.0283 0.2198 482 ASP A CG 3168 O OD1 . ASP A 482 ? 2.0521 2.0988 2.3120 -0.0527 0.0380 0.2290 482 ASP A OD1 3169 O OD2 . ASP A 482 ? 2.0057 2.0847 2.2644 -0.0832 0.0109 0.2245 482 ASP A OD2 3170 N N . VAL A 483 ? 1.4956 1.5339 1.6975 0.0181 0.0818 0.2389 483 VAL A N 3171 C CA . VAL A 483 ? 1.4508 1.4718 1.6494 0.0272 0.0922 0.2432 483 VAL A CA 3172 C C . VAL A 483 ? 1.4738 1.5210 1.6982 0.0315 0.1013 0.2730 483 VAL A C 3173 O O . VAL A 483 ? 1.4173 1.4822 1.6364 0.0495 0.1168 0.2900 483 VAL A O 3174 C CB . VAL A 483 ? 1.4629 1.4609 1.6235 0.0460 0.1038 0.2328 483 VAL A CB 3175 C CG1 . VAL A 483 ? 1.5044 1.4846 1.6605 0.0489 0.1077 0.2350 483 VAL A CG1 3176 C CG2 . VAL A 483 ? 1.4839 1.4615 1.6225 0.0426 0.0970 0.2072 483 VAL A CG2 3177 N N . ARG A 484 ? 1.4844 1.5311 1.7368 0.0152 0.0936 0.2793 484 ARG A N 3178 C CA . ARG A 484 ? 1.5048 1.5769 1.7874 0.0147 0.1008 0.3091 484 ARG A CA 3179 C C . ARG A 484 ? 1.3566 1.4035 1.6387 0.0132 0.1028 0.3098 484 ARG A C 3180 O O . ARG A 484 ? 1.2209 1.2361 1.4944 0.0063 0.0940 0.2888 484 ARG A O 3181 C CB . ARG A 484 ? 1.6392 1.7415 1.9650 -0.0084 0.0872 0.3227 484 ARG A CB 3182 C CG . ARG A 484 ? 1.5889 1.6668 1.9262 -0.0363 0.0676 0.3036 484 ARG A CG 3183 C CD . ARG A 484 ? 1.5781 1.6878 1.9499 -0.0620 0.0512 0.3149 484 ARG A CD 3184 N NE . ARG A 484 ? 1.7148 1.7957 2.0957 -0.0920 0.0341 0.2968 484 ARG A NE 3185 C CZ . ARG A 484 ? 1.9339 1.9906 2.3344 -0.1027 0.0349 0.3007 484 ARG A CZ 3186 N NH1 . ARG A 484 ? 2.0869 2.1488 2.4990 -0.0865 0.0505 0.3236 484 ARG A NH1 3187 N NH2 . ARG A 484 ? 1.9534 1.9771 2.3594 -0.1296 0.0212 0.2816 484 ARG A NH2 3188 N N . PRO A 485 ? 1.4044 1.4665 1.6956 0.0214 0.1159 0.3361 485 PRO A N 3189 C CA . PRO A 485 ? 1.5304 1.5760 1.8290 0.0178 0.1166 0.3455 485 PRO A CA 3190 C C . PRO A 485 ? 1.5801 1.6172 1.9173 -0.0075 0.1010 0.3431 485 PRO A C 3191 O O . PRO A 485 ? 1.6280 1.6829 1.9863 -0.0224 0.0917 0.3418 485 PRO A O 3192 C CB . PRO A 485 ? 1.6137 1.6891 1.9218 0.0276 0.1341 0.3790 485 PRO A CB 3193 C CG . PRO A 485 ? 1.5295 1.6415 1.8547 0.0301 0.1392 0.3895 485 PRO A CG 3194 C CD . PRO A 485 ? 1.4341 1.5327 1.7326 0.0349 0.1324 0.3616 485 PRO A CD 3195 N N . LEU A 486 ? 1.4965 1.5064 1.8427 -0.0130 0.0978 0.3436 486 LEU A N 3196 C CA . LEU A 486 ? 1.4791 1.4629 1.8510 -0.0355 0.0841 0.3299 486 LEU A CA 3197 C C . LEU A 486 ? 1.4779 1.4786 1.8912 -0.0608 0.0758 0.3439 486 LEU A C 3198 O O . LEU A 486 ? 1.4623 1.4520 1.8822 -0.0815 0.0620 0.3240 486 LEU A O 3199 C CB . LEU A 486 ? 1.3636 1.3106 1.7387 -0.0326 0.0845 0.3277 486 LEU A CB 3200 C CG . LEU A 486 ? 1.3240 1.2298 1.7162 -0.0497 0.0753 0.3056 486 LEU A CG 3201 C CD1 . LEU A 486 ? 1.2315 1.1196 1.6011 -0.0541 0.0686 0.2687 486 LEU A CD1 3202 C CD2 . LEU A 486 ? 1.2856 1.1617 1.6860 -0.0401 0.0797 0.3117 486 LEU A CD2 3203 N N . TYR A 487 ? 1.3549 1.3826 1.7946 -0.0617 0.0836 0.3779 487 TYR A N 3204 C CA . TYR A 487 ? 1.4409 1.4789 1.9249 -0.0897 0.0739 0.3917 487 TYR A CA 3205 C C . TYR A 487 ? 1.5992 1.6920 2.1068 -0.0972 0.0724 0.4122 487 TYR A C 3206 O O . TYR A 487 ? 1.7301 1.8366 2.2756 -0.1255 0.0596 0.4220 487 TYR A O 3207 C CB . TYR A 487 ? 1.3854 1.4110 1.8964 -0.0941 0.0801 0.4173 487 TYR A CB 3208 C CG . TYR A 487 ? 1.4590 1.4308 1.9612 -0.0918 0.0785 0.4008 487 TYR A CG 3209 C CD1 . TYR A 487 ? 1.4237 1.3818 1.8915 -0.0660 0.0864 0.3932 487 TYR A CD1 3210 C CD2 . TYR A 487 ? 1.6511 1.5854 2.1825 -0.1157 0.0698 0.3953 487 TYR A CD2 3211 C CE1 . TYR A 487 ? 1.5469 1.4619 2.0153 -0.0624 0.0853 0.3838 487 TYR A CE1 3212 C CE2 . TYR A 487 ? 1.7858 1.6699 2.3154 -0.1104 0.0717 0.3836 487 TYR A CE2 3213 C CZ . TYR A 487 ? 1.7271 1.6049 2.2279 -0.0825 0.0795 0.3796 487 TYR A CZ 3214 O OH . TYR A 487 ? 1.7863 1.6200 2.2933 -0.0761 0.0815 0.3725 487 TYR A OH 3215 N N . SER A 488 ? 1.6214 1.7449 2.1082 -0.0724 0.0855 0.4194 488 SER A N 3216 C CA . SER A 488 ? 1.6298 1.8090 2.1419 -0.0728 0.0880 0.4425 488 SER A CA 3217 C C . SER A 488 ? 1.5201 1.7050 1.9960 -0.0527 0.0911 0.4243 488 SER A C 3218 O O . SER A 488 ? 1.4304 1.5778 1.8633 -0.0400 0.0922 0.3962 488 SER A O 3219 C CB . SER A 488 ? 1.7681 1.9817 2.2985 -0.0566 0.1114 0.4821 488 SER A CB 3220 O OG . SER A 488 ? 1.5561 1.8245 2.1382 -0.0689 0.1116 0.5152 488 SER A OG 3221 N N . ARG A 489 ? 1.4245 1.6574 1.9210 -0.0497 0.0927 0.4423 489 ARG A N 3222 C CA . ARG A 489 ? 1.5262 1.7661 1.9905 -0.0212 0.1062 0.4364 489 ARG A CA 3223 C C . ARG A 489 ? 1.6666 1.9274 2.1309 0.0060 0.1364 0.4647 489 ARG A C 3224 O O . ARG A 489 ? 1.7707 2.0011 2.2055 0.0174 0.1485 0.4598 489 ARG A O 3225 C CB . ARG A 489 ? 1.6399 1.9130 2.1189 -0.0286 0.0924 0.4371 489 ARG A CB 3226 C CG . ARG A 489 ? 1.8280 2.0693 2.2860 -0.0510 0.0667 0.4019 489 ARG A CG 3227 C CD . ARG A 489 ? 1.9786 2.2458 2.4320 -0.0510 0.0557 0.3988 489 ARG A CD 3228 N NE . ARG A 489 ? 2.0051 2.3310 2.5072 -0.0705 0.0401 0.4270 489 ARG A NE 3229 C CZ . ARG A 489 ? 1.7751 2.1300 2.3254 -0.0973 0.0283 0.4491 489 ARG A CZ 3230 N NH1 . ARG A 489 ? 1.5155 1.8459 2.0776 -0.1099 0.0308 0.4495 489 ARG A NH1 3231 N NH2 . ARG A 489 ? 1.5591 1.9720 2.1497 -0.1130 0.0125 0.4744 489 ARG A NH2 3232 N N . ARG A 490 ? 1.7836 2.0961 2.2803 0.0163 0.1491 0.4954 490 ARG A N 3233 C CA . ARG A 490 ? 1.8464 2.1781 2.3397 0.0452 0.1832 0.5219 490 ARG A CA 3234 C C . ARG A 490 ? 1.9262 2.2084 2.3564 0.0659 0.2003 0.5025 490 ARG A C 3235 O O . ARG A 490 ? 2.0208 2.2870 2.4451 0.0604 0.2033 0.5079 490 ARG A O 3236 C CB . ARG A 490 ? 1.8375 2.2091 2.3853 0.0322 0.1887 0.5603 490 ARG A CB 3237 C CG . ARG A 490 ? 1.8325 2.1759 2.3887 0.0047 0.1717 0.5549 490 ARG A CG 3238 C CD . ARG A 490 ? 2.0340 2.4185 2.6500 -0.0121 0.1754 0.5953 490 ARG A CD 3239 N NE . ARG A 490 ? 2.0569 2.4773 2.6797 0.0150 0.2109 0.6297 490 ARG A NE 3240 C CZ . ARG A 490 ? 1.9504 2.4288 2.6130 0.0264 0.2255 0.6596 490 ARG A CZ 3241 N NH1 . ARG A 490 ? 1.9896 2.5008 2.6900 0.0112 0.2041 0.6615 490 ARG A NH1 3242 N NH2 . ARG A 490 ? 1.8844 2.3895 2.5487 0.0535 0.2624 0.6890 490 ARG A NH2 3243 N N . LEU A 491 ? 1.9459 2.2043 2.3296 0.0876 0.2099 0.4813 491 LEU A N 3244 C CA . LEU A 491 ? 1.8628 2.0711 2.1828 0.1007 0.2185 0.4572 491 LEU A CA 3245 C C . LEU A 491 ? 1.9733 2.1841 2.2745 0.1174 0.2467 0.4778 491 LEU A C 3246 O O . LEU A 491 ? 2.0252 2.2630 2.3340 0.1374 0.2736 0.4997 491 LEU A O 3247 C CB . LEU A 491 ? 2.0842 2.2683 2.3615 0.1188 0.2242 0.4329 491 LEU A CB 3248 C CG . LEU A 491 ? 2.1853 2.3852 2.4847 0.1132 0.2085 0.4258 491 LEU A CG 3249 C CD1 . LEU A 491 ? 1.9615 2.1953 2.2784 0.1367 0.2313 0.4491 491 LEU A CD1 3250 C CD2 . LEU A 491 ? 2.2408 2.3972 2.4968 0.1112 0.1950 0.3891 491 LEU A CD2 3251 N N . PRO A 492 ? 2.1263 2.3101 2.4030 0.1100 0.2420 0.4728 492 PRO A N 3252 C CA . PRO A 492 ? 2.1744 2.3697 2.4415 0.1205 0.2664 0.4992 492 PRO A CA 3253 C C . PRO A 492 ? 1.9528 2.1456 2.1753 0.1504 0.3018 0.5036 492 PRO A C 3254 O O . PRO A 492 ? 1.5516 1.7199 1.7353 0.1651 0.3081 0.4803 492 PRO A O 3255 C CB . PRO A 492 ? 2.4040 2.5662 2.6444 0.1086 0.2518 0.4901 492 PRO A CB 3256 C CG . PRO A 492 ? 2.4034 2.5567 2.6797 0.0847 0.2201 0.4747 492 PRO A CG 3257 C CD . PRO A 492 ? 2.4152 2.5687 2.6894 0.0892 0.2145 0.4529 492 PRO A CD 3258 N N . LYS A 493 ? 2.1964 2.4138 2.4270 0.1582 0.3261 0.5350 493 LYS A N 3259 C CA . LYS A 493 ? 2.3056 2.5235 2.4959 0.1864 0.3665 0.5459 493 LYS A CA 3260 C C . LYS A 493 ? 2.1728 2.4045 2.3739 0.2093 0.3875 0.5459 493 LYS A C 3261 O O . LYS A 493 ? 2.0326 2.3123 2.3026 0.2072 0.3865 0.5697 493 LYS A O 3262 C CB . LYS A 493 ? 2.4204 2.5888 2.5234 0.1930 0.3735 0.5247 493 LYS A CB 3263 C CG . LYS A 493 ? 2.4158 2.5776 2.5096 0.1744 0.3573 0.5342 493 LYS A CG 3264 C CD . LYS A 493 ? 2.5168 2.7175 2.6433 0.1740 0.3763 0.5768 493 LYS A CD 3265 C CE . LYS A 493 ? 2.6389 2.8318 2.7005 0.1949 0.4140 0.5873 493 LYS A CE 3266 N NZ . LYS A 493 ? 2.5268 2.6878 2.5239 0.1866 0.4040 0.5803 493 LYS A NZ 3267 N N . GLY A 494 ? 2.1292 2.3189 2.2641 0.2298 0.4053 0.5208 494 GLY A N 3268 C CA . GLY A 494 ? 1.9918 2.1868 2.1280 0.2581 0.4347 0.5239 494 GLY A CA 3269 C C . GLY A 494 ? 1.9096 2.0941 2.0587 0.2562 0.4144 0.5027 494 GLY A C 3270 O O . GLY A 494 ? 1.8564 2.0739 2.0511 0.2707 0.4259 0.5205 494 GLY A O 3271 N N . VAL A 495 ? 1.7984 1.9424 1.9127 0.2380 0.3836 0.4690 495 VAL A N 3272 C CA . VAL A 495 ? 1.8306 1.9455 1.9279 0.2394 0.3701 0.4406 495 VAL A CA 3273 C C . VAL A 495 ? 1.7228 1.8721 1.8814 0.2309 0.3486 0.4475 495 VAL A C 3274 O O . VAL A 495 ? 1.5513 1.7233 1.7501 0.2049 0.3179 0.4505 495 VAL A O 3275 C CB . VAL A 495 ? 1.8367 1.9038 1.8844 0.2210 0.3433 0.4052 495 VAL A CB 3276 C CG1 . VAL A 495 ? 2.1116 2.1273 2.0772 0.2344 0.3650 0.3856 495 VAL A CG1 3277 C CG2 . VAL A 495 ? 1.6910 1.7733 1.7661 0.1938 0.3144 0.4102 495 VAL A CG2 3278 N N . LYS A 496 ? 1.7118 1.8592 1.8715 0.2518 0.3640 0.4478 496 LYS A N 3279 C CA . LYS A 496 ? 1.6885 1.8766 1.9071 0.2466 0.3468 0.4615 496 LYS A CA 3280 C C . LYS A 496 ? 1.6287 1.7932 1.8345 0.2240 0.3106 0.4319 496 LYS A C 3281 O O . LYS A 496 ? 1.7038 1.8990 1.9505 0.2138 0.2906 0.4394 496 LYS A O 3282 C CB . LYS A 496 ? 1.8657 2.0679 2.1000 0.2790 0.3770 0.4803 496 LYS A CB 3283 C CG . LYS A 496 ? 2.0058 2.2804 2.3162 0.2880 0.3900 0.5269 496 LYS A CG 3284 C CD . LYS A 496 ? 2.1128 2.3899 2.4243 0.3301 0.4371 0.5470 496 LYS A CD 3285 C CE . LYS A 496 ? 2.0032 2.3232 2.3723 0.3437 0.4358 0.5727 496 LYS A CE 3286 N NZ . LYS A 496 ? 1.9489 2.3504 2.4016 0.3497 0.4455 0.6229 496 LYS A NZ 3287 N N . HIS A 497 ? 1.5912 1.7042 1.7405 0.2156 0.3025 0.4000 497 HIS A N 3288 C CA . HIS A 497 ? 1.5417 1.6355 1.6830 0.1915 0.2684 0.3734 497 HIS A CA 3289 C C . HIS A 497 ? 1.5567 1.6092 1.6517 0.1797 0.2593 0.3491 497 HIS A C 3290 O O . HIS A 497 ? 1.6248 1.6456 1.6704 0.1920 0.2782 0.3414 497 HIS A O 3291 C CB . HIS A 497 ? 1.6650 1.7427 1.7942 0.1985 0.2649 0.3594 497 HIS A CB 3292 C CG . HIS A 497 ? 1.8343 1.8905 1.9502 0.1764 0.2352 0.3318 497 HIS A CG 3293 N ND1 . HIS A 497 ? 1.9424 2.0163 2.0869 0.1507 0.2080 0.3290 497 HIS A ND1 3294 C CD2 . HIS A 497 ? 1.9852 2.0028 2.0631 0.1767 0.2307 0.3066 497 HIS A CD2 3295 C CE1 . HIS A 497 ? 2.1237 2.1713 2.2474 0.1382 0.1901 0.3029 497 HIS A CE1 3296 N NE2 . HIS A 497 ? 2.1688 2.1851 2.2540 0.1530 0.2026 0.2901 497 HIS A NE2 3297 N N . LEU A 498 ? 1.5030 1.5561 1.6142 0.1555 0.2298 0.3374 498 LEU A N 3298 C CA . LEU A 498 ? 1.4442 1.4753 1.5365 0.1409 0.2165 0.3250 498 LEU A CA 3299 C C . LEU A 498 ? 1.5093 1.4947 1.5449 0.1427 0.2148 0.2977 498 LEU A C 3300 O O . LEU A 498 ? 1.5245 1.4929 1.5355 0.1366 0.2105 0.2932 498 LEU A O 3301 C CB . LEU A 498 ? 1.2746 1.3190 1.4069 0.1170 0.1889 0.3209 498 LEU A CB 3302 C CG . LEU A 498 ? 1.2350 1.2647 1.3710 0.0995 0.1716 0.3129 498 LEU A CG 3303 C CD1 . LEU A 498 ? 1.1303 1.1495 1.2440 0.1038 0.1806 0.3225 498 LEU A CD1 3304 C CD2 . LEU A 498 ? 1.3407 1.3970 1.5299 0.0811 0.1570 0.3242 498 LEU A CD2 3305 N N . LYS A 499 ? 1.4689 1.4374 1.4868 0.1496 0.2169 0.2826 499 LYS A N 3306 C CA . LYS A 499 ? 1.5556 1.4813 1.5228 0.1498 0.2153 0.2572 499 LYS A CA 3307 C C . LYS A 499 ? 1.5616 1.4611 1.4772 0.1613 0.2358 0.2563 499 LYS A C 3308 O O . LYS A 499 ? 1.4559 1.3237 1.3282 0.1539 0.2291 0.2386 499 LYS A O 3309 C CB . LYS A 499 ? 1.7491 1.6649 1.7125 0.1577 0.2188 0.2480 499 LYS A CB 3310 C CG . LYS A 499 ? 1.9514 1.8360 1.8884 0.1473 0.2046 0.2221 499 LYS A CG 3311 C CD . LYS A 499 ? 2.2884 2.1742 2.2356 0.1525 0.2051 0.2196 499 LYS A CD 3312 C CE . LYS A 499 ? 2.7555 2.6307 2.7012 0.1360 0.1845 0.2000 499 LYS A CE 3313 N NZ . LYS A 499 ? 2.9065 2.7924 2.8684 0.1370 0.1806 0.2012 499 LYS A NZ 3314 N N . ASP A 500 ? 1.6644 1.5789 1.5847 0.1785 0.2609 0.2765 500 ASP A N 3315 C CA . ASP A 500 ? 1.8311 1.7200 1.6986 0.1922 0.2865 0.2764 500 ASP A CA 3316 C C . ASP A 500 ? 1.8803 1.7830 1.7436 0.1850 0.2852 0.2904 500 ASP A C 3317 O O . ASP A 500 ? 2.0702 1.9466 1.8773 0.1888 0.2982 0.2851 500 ASP A O 3318 C CB . ASP A 500 ? 2.0698 1.9657 1.9434 0.2188 0.3204 0.2918 500 ASP A CB 3319 C CG . ASP A 500 ? 2.4073 2.2827 2.2778 0.2292 0.3255 0.2800 500 ASP A CG 3320 O OD1 . ASP A 500 ? 2.5829 2.4205 2.4185 0.2192 0.3126 0.2542 500 ASP A OD1 3321 O OD2 . ASP A 500 ? 2.6635 2.5634 2.5700 0.2475 0.3425 0.2994 500 ASP A OD2 3322 N N . PHE A 501 ? 1.8582 1.7998 1.7779 0.1735 0.2696 0.3085 501 PHE A N 3323 C CA . PHE A 501 ? 1.8139 1.7707 1.7378 0.1657 0.2672 0.3262 501 PHE A CA 3324 C C . PHE A 501 ? 1.8820 1.8149 1.7733 0.1493 0.2448 0.3115 501 PHE A C 3325 O O . PHE A 501 ? 1.7284 1.6613 1.6461 0.1344 0.2188 0.3006 501 PHE A O 3326 C CB . PHE A 501 ? 1.8087 1.8101 1.8049 0.1569 0.2582 0.3508 501 PHE A CB 3327 C CG . PHE A 501 ? 1.9151 1.9294 1.9217 0.1466 0.2532 0.3704 501 PHE A CG 3328 C CD1 . PHE A 501 ? 1.8981 1.9131 1.8710 0.1571 0.2760 0.3868 501 PHE A CD1 3329 C CD2 . PHE A 501 ? 1.9940 2.0175 2.0428 0.1268 0.2272 0.3729 501 PHE A CD2 3330 C CE1 . PHE A 501 ? 1.9342 1.9618 1.9164 0.1474 0.2709 0.4077 501 PHE A CE1 3331 C CE2 . PHE A 501 ? 1.7959 1.8286 1.8575 0.1181 0.2230 0.3934 501 PHE A CE2 3332 C CZ . PHE A 501 ? 1.9111 1.9478 1.9402 0.1282 0.2440 0.4122 501 PHE A CZ 3333 N N . PRO A 502 ? 1.8993 1.8133 1.7329 0.1522 0.2556 0.3124 502 PRO A N 3334 C CA . PRO A 502 ? 1.8304 1.7231 1.6208 0.1382 0.2371 0.3020 502 PRO A CA 3335 C C . PRO A 502 ? 1.8081 1.7236 1.6210 0.1272 0.2234 0.3253 502 PRO A C 3336 O O . PRO A 502 ? 1.8346 1.7719 1.6602 0.1331 0.2389 0.3509 502 PRO A O 3337 C CB . PRO A 502 ? 1.8102 1.6709 1.5210 0.1479 0.2600 0.2926 502 PRO A CB 3338 C CG . PRO A 502 ? 1.8628 1.7374 1.5829 0.1692 0.2949 0.3094 502 PRO A CG 3339 C CD . PRO A 502 ? 1.8479 1.7623 1.6518 0.1712 0.2905 0.3258 502 PRO A CD 3340 N N . ILE A 503 ? 1.8381 1.7489 1.6580 0.1120 0.1954 0.3184 503 ILE A N 3341 C CA . ILE A 503 ? 1.8187 1.7484 1.6669 0.1020 0.1798 0.3410 503 ILE A CA 3342 C C . ILE A 503 ? 1.8272 1.7469 1.6127 0.0980 0.1779 0.3472 503 ILE A C 3343 O O . ILE A 503 ? 1.8549 1.7544 1.5993 0.0899 0.1637 0.3287 503 ILE A O 3344 C CB . ILE A 503 ? 1.7091 1.6400 1.6030 0.0900 0.1526 0.3327 503 ILE A CB 3345 C CG1 . ILE A 503 ? 1.6329 1.5728 1.5846 0.0908 0.1531 0.3260 503 ILE A CG1 3346 C CG2 . ILE A 503 ? 1.7083 1.6517 1.6235 0.0814 0.1364 0.3559 503 ILE A CG2 3347 C CD1 . ILE A 503 ? 1.5010 1.4593 1.4743 0.0996 0.1739 0.3399 503 ILE A CD1 3348 N N . LEU A 504 ? 1.7236 1.6589 1.5008 0.1019 0.1913 0.3742 504 LEU A N 3349 C CA . LEU A 504 ? 1.8369 1.7631 1.5441 0.0983 0.1925 0.3810 504 LEU A CA 3350 C C . LEU A 504 ? 1.9185 1.8485 1.6251 0.0819 0.1592 0.3872 504 LEU A C 3351 O O . LEU A 504 ? 1.9386 1.8849 1.7112 0.0770 0.1416 0.3985 504 LEU A O 3352 C CB . LEU A 504 ? 1.8497 1.7939 1.5480 0.1075 0.2178 0.4105 504 LEU A CB 3353 C CG . LEU A 504 ? 1.9361 1.8609 1.5786 0.1234 0.2525 0.3964 504 LEU A CG 3354 C CD1 . LEU A 504 ? 1.9696 1.9179 1.6643 0.1393 0.2799 0.4121 504 LEU A CD1 3355 C CD2 . LEU A 504 ? 2.0443 1.9545 1.5986 0.1231 0.2657 0.4014 504 LEU A CD2 3356 N N . PRO A 505 ? 1.9559 1.8699 1.5882 0.0728 0.1505 0.3795 505 PRO A N 3357 C CA . PRO A 505 ? 1.8671 1.7917 1.5010 0.0568 0.1174 0.3899 505 PRO A CA 3358 C C . PRO A 505 ? 1.9512 1.9068 1.6362 0.0573 0.1111 0.4295 505 PRO A C 3359 O O . PRO A 505 ? 2.0374 2.0030 1.6954 0.0606 0.1252 0.4539 505 PRO A O 3360 C CB . PRO A 505 ? 1.9852 1.8919 1.5210 0.0469 0.1156 0.3831 505 PRO A CB 3361 C CG . PRO A 505 ? 2.0823 1.9729 1.5693 0.0612 0.1535 0.3789 505 PRO A CG 3362 C CD . PRO A 505 ? 2.0802 1.9668 1.6226 0.0763 0.1717 0.3642 505 PRO A CD 3363 N N . GLY A 506 ? 1.9608 1.9289 1.7207 0.0551 0.0933 0.4360 506 GLY A N 3364 C CA . GLY A 506 ? 2.0205 2.0121 1.8339 0.0546 0.0847 0.4733 506 GLY A CA 3365 C C . GLY A 506 ? 1.8762 1.8738 1.7622 0.0623 0.0984 0.4831 506 GLY A C 3366 O O . GLY A 506 ? 1.8232 1.8343 1.7573 0.0612 0.0923 0.5132 506 GLY A O 3367 N N . GLU A 507 ? 1.8673 1.8547 1.7613 0.0687 0.1159 0.4594 507 GLU A N 3368 C CA . GLU A 507 ? 1.8912 1.8853 1.8521 0.0720 0.1262 0.4658 507 GLU A CA 3369 C C . GLU A 507 ? 1.7784 1.7616 1.7878 0.0688 0.1129 0.4421 507 GLU A C 3370 O O . GLU A 507 ? 1.6706 1.6419 1.6587 0.0671 0.1019 0.4173 507 GLU A O 3371 C CB . GLU A 507 ? 2.0957 2.0934 2.0424 0.0807 0.1539 0.4616 507 GLU A CB 3372 C CG . GLU A 507 ? 2.7000 2.7014 2.5800 0.0873 0.1739 0.4745 507 GLU A CG 3373 C CD . GLU A 507 ? 2.8671 2.8894 2.7559 0.0858 0.1800 0.5163 507 GLU A CD 3374 O OE1 . GLU A 507 ? 3.1047 3.1309 2.9988 0.0780 0.1599 0.5344 507 GLU A OE1 3375 O OE2 . GLU A 507 ? 2.6810 2.7179 2.5714 0.0932 0.2057 0.5339 507 GLU A OE2 3376 N N . ILE A 508 ? 1.8287 1.8149 1.9015 0.0666 0.1143 0.4506 508 ILE A N 3377 C CA . ILE A 508 ? 1.7683 1.7418 1.8868 0.0629 0.1053 0.4282 508 ILE A CA 3378 C C . ILE A 508 ? 1.8001 1.7759 1.9380 0.0625 0.1182 0.4162 508 ILE A C 3379 O O . ILE A 508 ? 1.9490 1.9400 2.0970 0.0628 0.1317 0.4365 508 ILE A O 3380 C CB . ILE A 508 ? 1.7392 1.7073 1.9156 0.0583 0.0941 0.4450 508 ILE A CB 3381 C CG1 . ILE A 508 ? 2.0154 1.9938 2.2201 0.0555 0.1022 0.4817 508 ILE A CG1 3382 C CG2 . ILE A 508 ? 1.5379 1.5052 1.7052 0.0599 0.0777 0.4495 508 ILE A CG2 3383 C CD1 . ILE A 508 ? 1.8823 1.8479 2.1498 0.0505 0.0958 0.4983 508 ILE A CD1 3384 N N . PHE A 509 ? 1.6603 1.6251 1.8039 0.0614 0.1140 0.3859 509 PHE A N 3385 C CA . PHE A 509 ? 1.6503 1.6210 1.8173 0.0586 0.1218 0.3772 509 PHE A CA 3386 C C . PHE A 509 ? 1.7311 1.6874 1.9319 0.0503 0.1111 0.3549 509 PHE A C 3387 O O . PHE A 509 ? 1.8652 1.8067 2.0558 0.0515 0.1025 0.3343 509 PHE A O 3388 C CB . PHE A 509 ? 1.5139 1.4916 1.6422 0.0679 0.1352 0.3659 509 PHE A CB 3389 C CG . PHE A 509 ? 1.4993 1.4961 1.6566 0.0666 0.1455 0.3725 509 PHE A CG 3390 C CD1 . PHE A 509 ? 1.5480 1.5609 1.7497 0.0579 0.1472 0.3976 509 PHE A CD1 3391 C CD2 . PHE A 509 ? 1.4856 1.4865 1.6289 0.0734 0.1527 0.3567 509 PHE A CD2 3392 C CE1 . PHE A 509 ? 1.6351 1.6714 1.8677 0.0541 0.1541 0.4064 509 PHE A CE1 3393 C CE2 . PHE A 509 ? 1.4214 1.4467 1.5960 0.0721 0.1602 0.3671 509 PHE A CE2 3394 C CZ . PHE A 509 ? 1.5833 1.6283 1.8030 0.0617 0.1601 0.3920 509 PHE A CZ 3395 N N . LYS A 510 ? 1.6553 1.6173 1.8947 0.0405 0.1124 0.3597 510 LYS A N 3396 C CA . LYS A 510 ? 1.5235 1.4689 1.7926 0.0291 0.1030 0.3392 510 LYS A CA 3397 C C . LYS A 510 ? 1.5022 1.4579 1.7669 0.0252 0.1036 0.3213 510 LYS A C 3398 O O . LYS A 510 ? 1.4969 1.4757 1.7758 0.0209 0.1086 0.3347 510 LYS A O 3399 C CB . LYS A 510 ? 1.3976 1.3337 1.7128 0.0163 0.0998 0.3553 510 LYS A CB 3400 C CG . LYS A 510 ? 1.4267 1.3534 1.7505 0.0216 0.0990 0.3770 510 LYS A CG 3401 C CD . LYS A 510 ? 1.6291 1.5599 1.9906 0.0119 0.1025 0.4082 510 LYS A CD 3402 C CE . LYS A 510 ? 1.6330 1.5499 2.0132 0.0157 0.1004 0.4321 510 LYS A CE 3403 N NZ . LYS A 510 ? 1.5043 1.3856 1.9123 0.0139 0.0940 0.4168 510 LYS A NZ 3404 N N . TYR A 511 ? 1.4322 1.3730 1.6801 0.0266 0.0981 0.2935 511 TYR A N 3405 C CA . TYR A 511 ? 1.3653 1.3135 1.6012 0.0253 0.0974 0.2758 511 TYR A CA 3406 C C . TYR A 511 ? 1.4476 1.3776 1.7013 0.0102 0.0871 0.2532 511 TYR A C 3407 O O . TYR A 511 ? 1.4123 1.3167 1.6698 0.0095 0.0839 0.2402 511 TYR A O 3408 C CB . TYR A 511 ? 1.3933 1.3337 1.5888 0.0385 0.1000 0.2607 511 TYR A CB 3409 C CG . TYR A 511 ? 1.4083 1.3585 1.5694 0.0527 0.1112 0.2720 511 TYR A CG 3410 C CD1 . TYR A 511 ? 1.4032 1.3482 1.5457 0.0585 0.1129 0.2833 511 TYR A CD1 3411 C CD2 . TYR A 511 ? 1.4975 1.4588 1.6400 0.0605 0.1201 0.2691 511 TYR A CD2 3412 C CE1 . TYR A 511 ? 1.5404 1.4879 1.6408 0.0697 0.1238 0.2885 511 TYR A CE1 3413 C CE2 . TYR A 511 ? 1.5685 1.5303 1.6744 0.0745 0.1338 0.2751 511 TYR A CE2 3414 C CZ . TYR A 511 ? 1.5814 1.5342 1.6624 0.0783 0.1360 0.2828 511 TYR A CZ 3415 O OH . TYR A 511 ? 1.4813 1.4294 1.5176 0.0908 0.1513 0.2850 511 TYR A OH 3416 N N . LYS A 512 ? 1.5775 1.5214 1.8407 -0.0016 0.0825 0.2492 512 LYS A N 3417 C CA . LYS A 512 ? 1.5149 1.4417 1.7814 -0.0176 0.0725 0.2240 512 LYS A CA 3418 C C . LYS A 512 ? 1.4839 1.4204 1.7212 -0.0120 0.0717 0.2084 512 LYS A C 3419 O O . LYS A 512 ? 1.4791 1.4451 1.7158 -0.0106 0.0720 0.2202 512 LYS A O 3420 C CB . LYS A 512 ? 1.4830 1.4179 1.7805 -0.0413 0.0633 0.2314 512 LYS A CB 3421 C CG . LYS A 512 ? 1.3862 1.3041 1.6799 -0.0629 0.0513 0.2054 512 LYS A CG 3422 C CD . LYS A 512 ? 1.4599 1.3634 1.7841 -0.0897 0.0423 0.2081 512 LYS A CD 3423 C CE . LYS A 512 ? 1.5172 1.4049 1.8300 -0.1162 0.0284 0.1815 512 LYS A CE 3424 N NZ . LYS A 512 ? 1.3491 1.1897 1.6732 -0.1390 0.0245 0.1650 512 LYS A NZ 3425 N N . TRP A 513 ? 1.4461 1.3594 1.6624 -0.0073 0.0723 0.1852 513 TRP A N 3426 C CA . TRP A 513 ? 1.4490 1.3665 1.6387 -0.0051 0.0711 0.1687 513 TRP A CA 3427 C C . TRP A 513 ? 1.4935 1.3972 1.6828 -0.0242 0.0623 0.1476 513 TRP A C 3428 O O . TRP A 513 ? 1.5763 1.4508 1.7598 -0.0260 0.0647 0.1272 513 TRP A O 3429 C CB . TRP A 513 ? 1.4291 1.3313 1.5951 0.0094 0.0776 0.1565 513 TRP A CB 3430 C CG . TRP A 513 ? 1.4661 1.3745 1.6206 0.0254 0.0847 0.1711 513 TRP A CG 3431 C CD1 . TRP A 513 ? 1.5200 1.4468 1.6753 0.0321 0.0899 0.1928 513 TRP A CD1 3432 C CD2 . TRP A 513 ? 1.5020 1.3978 1.6386 0.0351 0.0878 0.1643 513 TRP A CD2 3433 N NE1 . TRP A 513 ? 1.5531 1.4746 1.6855 0.0449 0.0962 0.1971 513 TRP A NE1 3434 C CE2 . TRP A 513 ? 1.6303 1.5341 1.7522 0.0453 0.0929 0.1803 513 TRP A CE2 3435 C CE3 . TRP A 513 ? 1.4251 1.3051 1.5573 0.0354 0.0871 0.1469 513 TRP A CE3 3436 C CZ2 . TRP A 513 ? 1.7543 1.6491 1.8543 0.0522 0.0938 0.1783 513 TRP A CZ2 3437 C CZ3 . TRP A 513 ? 1.4600 1.3366 1.5783 0.0434 0.0883 0.1481 513 TRP A CZ3 3438 C CH2 . TRP A 513 ? 1.5986 1.4818 1.6995 0.0501 0.0899 0.1630 513 TRP A CH2 3439 N N . THR A 514 ? 1.4974 1.4225 1.6925 -0.0389 0.0526 0.1530 514 THR A N 3440 C CA . THR A 514 ? 1.6452 1.5564 1.8314 -0.0605 0.0424 0.1315 514 THR A CA 3441 C C . THR A 514 ? 1.6080 1.5270 1.7613 -0.0556 0.0419 0.1191 514 THR A C 3442 O O . THR A 514 ? 1.4970 1.4435 1.6451 -0.0424 0.0442 0.1347 514 THR A O 3443 C CB . THR A 514 ? 1.9717 1.9022 2.1806 -0.0851 0.0277 0.1433 514 THR A CB 3444 O OG1 . THR A 514 ? 2.0739 2.0108 2.3173 -0.0841 0.0309 0.1665 514 THR A OG1 3445 C CG2 . THR A 514 ? 2.1555 2.0537 2.3537 -0.1118 0.0181 0.1164 514 THR A CG2 3446 N N . VAL A 515 ? 1.6429 1.5348 1.7734 -0.0652 0.0413 0.0915 515 VAL A N 3447 C CA . VAL A 515 ? 1.4514 1.3454 1.5475 -0.0622 0.0425 0.0774 515 VAL A CA 3448 C C . VAL A 515 ? 1.4495 1.3523 1.5265 -0.0865 0.0274 0.0680 515 VAL A C 3449 O O . VAL A 515 ? 1.6380 1.5228 1.7172 -0.1087 0.0193 0.0556 515 VAL A O 3450 C CB . VAL A 515 ? 1.3500 1.2083 1.4307 -0.0540 0.0561 0.0534 515 VAL A CB 3451 C CG1 . VAL A 515 ? 1.3629 1.2160 1.4068 -0.0619 0.0558 0.0333 515 VAL A CG1 3452 C CG2 . VAL A 515 ? 1.3440 1.2048 1.4311 -0.0300 0.0677 0.0636 515 VAL A CG2 3453 N N . THR A 516 ? 1.3439 1.2720 1.4002 -0.0834 0.0232 0.0738 516 THR A N 3454 C CA . THR A 516 ? 1.4811 1.4289 1.5193 -0.1064 0.0052 0.0724 516 THR A CA 3455 C C . THR A 516 ? 1.5504 1.4979 1.5502 -0.1018 0.0088 0.0618 516 THR A C 3456 O O . THR A 516 ? 1.6921 1.6477 1.6914 -0.0789 0.0201 0.0726 516 THR A O 3457 C CB . THR A 516 ? 1.5759 1.5748 1.6374 -0.1034 -0.0056 0.1068 516 THR A CB 3458 O OG1 . THR A 516 ? 1.6520 1.6578 1.7371 -0.0762 0.0095 0.1258 516 THR A OG1 3459 C CG2 . THR A 516 ? 1.6992 1.7191 1.7845 -0.1301 -0.0254 0.1174 516 THR A CG2 3460 N N . VAL A 517 ? 1.5531 1.4926 1.5183 -0.1244 -0.0012 0.0428 517 VAL A N 3461 C CA . VAL A 517 ? 1.6184 1.5595 1.5441 -0.1195 0.0038 0.0350 517 VAL A CA 3462 C C . VAL A 517 ? 1.7353 1.7142 1.6713 -0.1001 0.0038 0.0655 517 VAL A C 3463 O O . VAL A 517 ? 1.9213 1.8928 1.8421 -0.0827 0.0180 0.0639 517 VAL A O 3464 C CB . VAL A 517 ? 1.4463 1.3873 1.3281 -0.1480 -0.0112 0.0189 517 VAL A CB 3465 C CG1 . VAL A 517 ? 1.4871 1.3783 1.3487 -0.1650 -0.0052 -0.0172 517 VAL A CG1 3466 C CG2 . VAL A 517 ? 1.3540 1.3429 1.2478 -0.1668 -0.0388 0.0449 517 VAL A CG2 3467 N N . GLU A 518 ? 1.6364 1.6545 1.6011 -0.1023 -0.0101 0.0943 518 GLU A N 3468 C CA . GLU A 518 ? 1.7243 1.7757 1.6960 -0.0843 -0.0089 0.1229 518 GLU A CA 3469 C C . GLU A 518 ? 1.8347 1.8726 1.8215 -0.0529 0.0132 0.1309 518 GLU A C 3470 O O . GLU A 518 ? 2.5904 2.6488 2.5846 -0.0356 0.0177 0.1544 518 GLU A O 3471 C CB . GLU A 518 ? 1.7811 1.8835 1.7804 -0.0940 -0.0289 0.1547 518 GLU A CB 3472 C CG . GLU A 518 ? 2.0193 2.1295 2.0202 -0.1285 -0.0516 0.1466 518 GLU A CG 3473 C CD . GLU A 518 ? 2.3212 2.4386 2.3688 -0.1306 -0.0528 0.1584 518 GLU A CD 3474 O OE1 . GLU A 518 ? 2.3353 2.4374 2.4042 -0.1070 -0.0335 0.1620 518 GLU A OE1 3475 O OE2 . GLU A 518 ? 2.4351 2.5753 2.4979 -0.1578 -0.0743 0.1655 518 GLU A OE2 3476 N N . ASP A 519 ? 1.7522 1.7552 1.7423 -0.0460 0.0267 0.1123 519 ASP A N 3477 C CA . ASP A 519 ? 1.9134 1.9001 1.9063 -0.0211 0.0453 0.1152 519 ASP A CA 3478 C C . ASP A 519 ? 1.8177 1.7691 1.7915 -0.0197 0.0571 0.0888 519 ASP A C 3479 O O . ASP A 519 ? 1.6984 1.6339 1.6769 -0.0044 0.0697 0.0878 519 ASP A O 3480 C CB . ASP A 519 ? 2.0573 2.0475 2.0814 -0.0081 0.0512 0.1306 519 ASP A CB 3481 C CG . ASP A 519 ? 2.3061 2.2831 2.3485 -0.0197 0.0476 0.1204 519 ASP A CG 3482 O OD1 . ASP A 519 ? 2.2632 2.2175 2.2938 -0.0333 0.0455 0.0970 519 ASP A OD1 3483 O OD2 . ASP A 519 ? 2.4387 2.4262 2.5076 -0.0144 0.0488 0.1366 519 ASP A OD2 3484 N N . GLY A 520 ? 1.7062 1.6471 1.6580 -0.0367 0.0529 0.0683 520 GLY A N 3485 C CA . GLY A 520 ? 1.6649 1.5760 1.5982 -0.0361 0.0661 0.0434 520 GLY A CA 3486 C C . GLY A 520 ? 1.7036 1.6178 1.5993 -0.0418 0.0680 0.0363 520 GLY A C 3487 O O . GLY A 520 ? 1.5589 1.4988 1.4409 -0.0490 0.0555 0.0504 520 GLY A O 3488 N N . PRO A 521 ? 1.6483 1.5393 1.5288 -0.0382 0.0841 0.0169 521 PRO A N 3489 C CA . PRO A 521 ? 1.5265 1.4208 1.3748 -0.0379 0.0917 0.0147 521 PRO A CA 3490 C C . PRO A 521 ? 1.5142 1.4173 1.3246 -0.0579 0.0803 0.0078 521 PRO A C 3491 O O . PRO A 521 ? 1.5353 1.4317 1.3419 -0.0741 0.0700 -0.0044 521 PRO A O 3492 C CB . PRO A 521 ? 1.4720 1.3404 1.3206 -0.0312 0.1126 -0.0054 521 PRO A CB 3493 C CG . PRO A 521 ? 1.4447 1.2987 1.3301 -0.0246 0.1147 -0.0089 521 PRO A CG 3494 C CD . PRO A 521 ? 1.5569 1.4189 1.4516 -0.0353 0.0967 -0.0026 521 PRO A CD 3495 N N . THR A 522 ? 1.5893 1.5076 1.3710 -0.0587 0.0806 0.0171 522 THR A N 3496 C CA . THR A 522 ? 1.7552 1.6807 1.4912 -0.0796 0.0707 0.0086 522 THR A CA 3497 C C . THR A 522 ? 1.9145 1.8180 1.6138 -0.0807 0.0913 -0.0137 522 THR A C 3498 O O . THR A 522 ? 1.9924 1.8803 1.7078 -0.0649 0.1123 -0.0191 522 THR A O 3499 C CB . THR A 522 ? 1.7219 1.6852 1.4459 -0.0827 0.0541 0.0382 522 THR A CB 3500 O OG1 . THR A 522 ? 1.6595 1.6258 1.3797 -0.0664 0.0685 0.0524 522 THR A OG1 3501 C CG2 . THR A 522 ? 1.7875 1.7770 1.5514 -0.0788 0.0370 0.0638 522 THR A CG2 3502 N N . LYS A 523 ? 2.0644 1.9695 1.7136 -0.1005 0.0847 -0.0252 523 LYS A N 3503 C CA . LYS A 523 ? 2.1851 2.0691 1.7893 -0.1041 0.1056 -0.0483 523 LYS A CA 3504 C C . LYS A 523 ? 2.0014 1.8940 1.6109 -0.0856 0.1246 -0.0329 523 LYS A C 3505 O O . LYS A 523 ? 2.1546 2.0268 1.7596 -0.0773 0.1505 -0.0492 523 LYS A O 3506 C CB . LYS A 523 ? 2.4649 2.3568 2.0072 -0.1305 0.0903 -0.0561 523 LYS A CB 3507 C CG . LYS A 523 ? 2.6953 2.5887 2.2345 -0.1544 0.0630 -0.0631 523 LYS A CG 3508 C CD . LYS A 523 ? 2.7357 2.6652 2.3271 -0.1499 0.0389 -0.0295 523 LYS A CD 3509 C CE . LYS A 523 ? 2.8920 2.8688 2.4751 -0.1516 0.0202 0.0064 523 LYS A CE 3510 N NZ . LYS A 523 ? 2.7538 2.7633 2.3937 -0.1399 0.0051 0.0406 523 LYS A NZ 3511 N N . SER A 524 ? 1.8534 1.7754 1.4759 -0.0790 0.1130 -0.0004 524 SER A N 3512 C CA . SER A 524 ? 2.0313 1.9584 1.6636 -0.0629 0.1293 0.0169 524 SER A CA 3513 C C . SER A 524 ? 2.0942 2.0064 1.7771 -0.0448 0.1425 0.0163 524 SER A C 3514 O O . SER A 524 ? 1.9715 1.8785 1.6628 -0.0350 0.1614 0.0191 524 SER A O 3515 C CB . SER A 524 ? 2.1355 2.0924 1.7690 -0.0600 0.1140 0.0528 524 SER A CB 3516 O OG . SER A 524 ? 2.3947 2.3647 1.9823 -0.0682 0.1163 0.0614 524 SER A OG 3517 N N . ASP A 525 ? 2.1482 2.0560 1.8642 -0.0424 0.1314 0.0141 525 ASP A N 3518 C CA . ASP A 525 ? 2.0076 1.9059 1.7698 -0.0271 0.1377 0.0181 525 ASP A CA 3519 C C . ASP A 525 ? 1.8262 1.7043 1.6004 -0.0217 0.1588 -0.0019 525 ASP A C 3520 O O . ASP A 525 ? 1.6473 1.5109 1.4036 -0.0288 0.1667 -0.0246 525 ASP A O 3521 C CB . ASP A 525 ? 1.9479 1.8487 1.7381 -0.0269 0.1211 0.0224 525 ASP A CB 3522 C CG . ASP A 525 ? 2.0242 1.9472 1.8240 -0.0219 0.1067 0.0511 525 ASP A CG 3523 O OD1 . ASP A 525 ? 2.0018 1.9218 1.8236 -0.0079 0.1118 0.0649 525 ASP A OD1 3524 O OD2 . ASP A 525 ? 1.9584 1.9014 1.7440 -0.0322 0.0905 0.0604 525 ASP A OD2 3525 N N . PRO A 526 ? 1.9730 1.8498 1.7773 -0.0096 0.1684 0.0073 526 PRO A N 3526 C CA . PRO A 526 ? 2.0361 1.9006 1.8625 -0.0034 0.1863 -0.0069 526 PRO A CA 3527 C C . PRO A 526 ? 1.8031 1.6543 1.6474 -0.0040 0.1798 -0.0201 526 PRO A C 3528 O O . PRO A 526 ? 1.5653 1.4180 1.4387 0.0010 0.1687 -0.0103 526 PRO A O 3529 C CB . PRO A 526 ? 2.3124 2.1825 2.1717 0.0056 0.1880 0.0102 526 PRO A CB 3530 C CG . PRO A 526 ? 2.1876 2.0637 2.0443 0.0061 0.1706 0.0287 526 PRO A CG 3531 C CD . PRO A 526 ? 2.2326 2.1174 2.0524 -0.0021 0.1634 0.0306 526 PRO A CD 3532 N N . ARG A 527 ? 1.9618 1.7972 1.7849 -0.0109 0.1875 -0.0423 527 ARG A N 3533 C CA . ARG A 527 ? 2.0440 1.8642 1.8722 -0.0176 0.1767 -0.0543 527 ARG A CA 3534 C C . ARG A 527 ? 1.7067 1.5179 1.5837 -0.0065 0.1787 -0.0521 527 ARG A C 3535 O O . ARG A 527 ? 1.4895 1.2794 1.3786 -0.0025 0.1931 -0.0679 527 ARG A O 3536 C CB . ARG A 527 ? 2.4430 2.2406 2.2306 -0.0303 0.1854 -0.0817 527 ARG A CB 3537 C CG . ARG A 527 ? 2.7228 2.5328 2.4570 -0.0467 0.1747 -0.0816 527 ARG A CG 3538 C CD . ARG A 527 ? 2.9577 2.7419 2.6427 -0.0637 0.1801 -0.1112 527 ARG A CD 3539 N NE . ARG A 527 ? 3.3342 3.0957 3.0294 -0.0741 0.1691 -0.1254 527 ARG A NE 3540 C CZ . ARG A 527 ? 3.7233 3.4445 3.4147 -0.0748 0.1864 -0.1531 527 ARG A CZ 3541 N NH1 . ARG A 527 ? 3.9897 3.6898 3.6669 -0.0641 0.2176 -0.1706 527 ARG A NH1 3542 N NH2 . ARG A 527 ? 3.8549 3.5553 3.5579 -0.0861 0.1740 -0.1624 527 ARG A NH2 3543 N N . CYS A 528 ? 1.6285 1.4550 1.5308 -0.0011 0.1647 -0.0313 528 CYS A N 3544 C CA . CYS A 528 ? 1.6208 1.4454 1.5661 0.0094 0.1641 -0.0230 528 CYS A CA 3545 C C . CYS A 528 ? 1.4905 1.3321 1.4486 0.0154 0.1551 -0.0012 528 CYS A C 3546 O O . CYS A 528 ? 1.3100 1.1558 1.2885 0.0226 0.1618 0.0053 528 CYS A O 3547 C CB . CYS A 528 ? 1.8276 1.6424 1.7950 0.0188 0.1847 -0.0319 528 CYS A CB 3548 S SG . CYS A 528 ? 2.2841 2.0865 2.2984 0.0274 0.1844 -0.0298 528 CYS A SG 3549 N N . LEU A 529 ? 1.4763 1.3269 1.4233 0.0121 0.1404 0.0104 529 LEU A N 3550 C CA . LEU A 529 ? 1.4116 1.2712 1.3602 0.0179 0.1355 0.0284 529 LEU A CA 3551 C C . LEU A 529 ? 1.3545 1.2117 1.3291 0.0246 0.1316 0.0368 529 LEU A C 3552 O O . LEU A 529 ? 1.3836 1.2385 1.3739 0.0251 0.1256 0.0374 529 LEU A O 3553 C CB . LEU A 529 ? 1.3326 1.2029 1.2635 0.0157 0.1248 0.0406 529 LEU A CB 3554 C CG . LEU A 529 ? 1.3019 1.1783 1.2276 0.0066 0.1143 0.0372 529 LEU A CG 3555 C CD1 . LEU A 529 ? 1.4103 1.2845 1.3625 0.0087 0.1078 0.0411 529 LEU A CD1 3556 C CD2 . LEU A 529 ? 1.2662 1.1610 1.1749 0.0043 0.1053 0.0526 529 LEU A CD2 3557 N N . THR A 530 ? 1.2951 1.1524 1.2723 0.0279 0.1341 0.0443 530 THR A N 3558 C CA . THR A 530 ? 1.4166 1.2718 1.4110 0.0316 0.1283 0.0525 530 THR A CA 3559 C C . THR A 530 ? 1.5061 1.3588 1.4876 0.0349 0.1207 0.0637 530 THR A C 3560 O O . THR A 530 ? 1.5994 1.4528 1.5619 0.0360 0.1214 0.0685 530 THR A O 3561 C CB . THR A 530 ? 1.3498 1.2065 1.3563 0.0304 0.1318 0.0548 530 THR A CB 3562 O OG1 . THR A 530 ? 1.4620 1.3123 1.4585 0.0295 0.1248 0.0642 530 THR A OG1 3563 C CG2 . THR A 530 ? 1.2727 1.1323 1.2698 0.0272 0.1425 0.0504 530 THR A CG2 3564 N N . ARG A 531 ? 1.4376 1.2888 1.4310 0.0377 0.1151 0.0695 531 ARG A N 3565 C CA . ARG A 531 ? 1.4143 1.2627 1.3975 0.0427 0.1115 0.0801 531 ARG A CA 3566 C C . ARG A 531 ? 1.6047 1.4502 1.5975 0.0433 0.1065 0.0850 531 ARG A C 3567 O O . ARG A 531 ? 1.7408 1.5892 1.7505 0.0399 0.1044 0.0824 531 ARG A O 3568 C CB . ARG A 531 ? 1.3167 1.1751 1.3060 0.0437 0.1088 0.0837 531 ARG A CB 3569 C CG . ARG A 531 ? 1.4476 1.3136 1.4262 0.0405 0.1097 0.0812 531 ARG A CG 3570 C CD . ARG A 531 ? 1.6100 1.4734 1.5685 0.0467 0.1139 0.0908 531 ARG A CD 3571 N NE . ARG A 531 ? 1.8107 1.6811 1.7565 0.0432 0.1151 0.0899 531 ARG A NE 3572 C CZ . ARG A 531 ? 2.0055 1.8923 1.9478 0.0429 0.1108 0.0994 531 ARG A CZ 3573 N NH1 . ARG A 531 ? 1.8130 1.7137 1.7681 0.0461 0.1057 0.1112 531 ARG A NH1 3574 N NH2 . ARG A 531 ? 2.3712 2.2642 2.2981 0.0386 0.1111 0.0994 531 ARG A NH2 3575 N N . TYR A 532 ? 1.6012 1.4438 1.5841 0.0481 0.1053 0.0942 532 TYR A N 3576 C CA . TYR A 532 ? 1.6389 1.4786 1.6217 0.0475 0.1000 0.1004 532 TYR A CA 3577 C C . TYR A 532 ? 1.6724 1.5171 1.6576 0.0532 0.1002 0.1113 532 TYR A C 3578 O O . TYR A 532 ? 1.6775 1.5291 1.6668 0.0570 0.1042 0.1146 532 TYR A O 3579 C CB . TYR A 532 ? 1.6233 1.4460 1.5761 0.0444 0.0999 0.0990 532 TYR A CB 3580 C CG . TYR A 532 ? 1.5785 1.3848 1.5005 0.0518 0.1091 0.1012 532 TYR A CG 3581 C CD1 . TYR A 532 ? 1.7889 1.5894 1.6948 0.0583 0.1126 0.1087 532 TYR A CD1 3582 C CD2 . TYR A 532 ? 1.5992 1.3959 1.5095 0.0541 0.1165 0.0977 532 TYR A CD2 3583 C CE1 . TYR A 532 ? 2.0575 1.8422 1.9380 0.0686 0.1255 0.1117 532 TYR A CE1 3584 C CE2 . TYR A 532 ? 1.9089 1.6897 1.7959 0.0641 0.1275 0.1024 532 TYR A CE2 3585 C CZ . TYR A 532 ? 2.1512 1.9253 2.0241 0.0723 0.1331 0.1088 532 TYR A CZ 3586 O OH . TYR A 532 ? 2.2816 2.0386 2.1336 0.0856 0.1484 0.1143 532 TYR A OH 3587 N N . TYR A 533 ? 1.6971 1.5416 1.6811 0.0525 0.0952 0.1191 533 TYR A N 3588 C CA . TYR A 533 ? 1.5063 1.3546 1.4864 0.0578 0.0974 0.1322 533 TYR A CA 3589 C C . TYR A 533 ? 1.4370 1.2737 1.3837 0.0572 0.0962 0.1366 533 TYR A C 3590 O O . TYR A 533 ? 1.2707 1.1061 1.2146 0.0491 0.0861 0.1352 533 TYR A O 3591 C CB . TYR A 533 ? 1.4882 1.3502 1.5047 0.0562 0.0923 0.1403 533 TYR A CB 3592 C CG . TYR A 533 ? 1.5316 1.3968 1.5659 0.0519 0.0831 0.1441 533 TYR A CG 3593 C CD1 . TYR A 533 ? 1.4270 1.2917 1.4698 0.0477 0.0794 0.1349 533 TYR A CD1 3594 C CD2 . TYR A 533 ? 1.6314 1.5037 1.6781 0.0528 0.0787 0.1606 533 TYR A CD2 3595 C CE1 . TYR A 533 ? 1.4553 1.3287 1.5216 0.0455 0.0713 0.1426 533 TYR A CE1 3596 C CE2 . TYR A 533 ? 1.5986 1.4777 1.6660 0.0503 0.0695 0.1688 533 TYR A CE2 3597 C CZ . TYR A 533 ? 1.5676 1.4484 1.6465 0.0472 0.0657 0.1601 533 TYR A CZ 3598 O OH . TYR A 533 ? 1.5106 1.4036 1.6174 0.0463 0.0569 0.1718 533 TYR A OH 3599 N N . SER A 534 ? 1.4089 1.2381 1.3297 0.0652 0.1069 0.1423 534 SER A N 3600 C CA . SER A 534 ? 1.4893 1.3029 1.3690 0.0643 0.1084 0.1448 534 SER A CA 3601 C C . SER A 534 ? 1.6288 1.4468 1.4969 0.0736 0.1193 0.1593 534 SER A C 3602 O O . SER A 534 ? 1.4746 1.3134 1.3761 0.0788 0.1225 0.1715 534 SER A O 3603 C CB . SER A 534 ? 1.4267 1.2103 1.2641 0.0633 0.1151 0.1311 534 SER A CB 3604 O OG . SER A 534 ? 1.4325 1.1971 1.2247 0.0576 0.1135 0.1298 534 SER A OG 3605 N N . SER A 535 ? 1.6884 1.4854 1.5069 0.0739 0.1252 0.1575 535 SER A N 3606 C CA . SER A 535 ? 1.6191 1.4160 1.4140 0.0824 0.1384 0.1703 535 SER A CA 3607 C C . SER A 535 ? 1.6312 1.4029 1.3884 0.0960 0.1623 0.1644 535 SER A C 3608 O O . SER A 535 ? 1.6046 1.3422 1.3121 0.0922 0.1658 0.1497 535 SER A O 3609 C CB . SER A 535 ? 1.5867 1.3769 1.3453 0.0713 0.1273 0.1731 535 SER A CB 3610 O OG . SER A 535 ? 1.5530 1.3468 1.2902 0.0793 0.1407 0.1878 535 SER A OG 3611 N N . PHE A 536 ? 1.7569 1.5446 1.5384 0.1115 0.1792 0.1770 536 PHE A N 3612 C CA . PHE A 536 ? 1.8508 1.6192 1.6093 0.1293 0.2053 0.1755 536 PHE A CA 3613 C C . PHE A 536 ? 1.9452 1.7055 1.6691 0.1424 0.2289 0.1856 536 PHE A C 3614 O O . PHE A 536 ? 2.1106 1.8771 1.8434 0.1616 0.2531 0.1971 536 PHE A O 3615 C CB . PHE A 536 ? 1.7876 1.5801 1.5957 0.1385 0.2089 0.1836 536 PHE A CB 3616 C CG . PHE A 536 ? 1.9718 1.7633 1.7980 0.1267 0.1905 0.1704 536 PHE A CG 3617 C CD1 . PHE A 536 ? 2.2721 2.0309 2.0699 0.1272 0.1948 0.1550 536 PHE A CD1 3618 C CD2 . PHE A 536 ? 2.0614 1.8803 1.9298 0.1143 0.1705 0.1725 536 PHE A CD2 3619 C CE1 . PHE A 536 ? 2.4393 2.1988 2.2527 0.1158 0.1795 0.1445 536 PHE A CE1 3620 C CE2 . PHE A 536 ? 2.2393 2.0563 2.1203 0.1043 0.1569 0.1597 536 PHE A CE2 3621 C CZ . PHE A 536 ? 2.3082 2.0981 2.1624 0.1050 0.1612 0.1468 536 PHE A CZ 3622 N N . VAL A 537 ? 1.9686 1.7169 1.6524 0.1317 0.2219 0.1826 537 VAL A N 3623 C CA . VAL A 537 ? 1.9971 1.7311 1.6327 0.1411 0.2441 0.1884 537 VAL A CA 3624 C C . VAL A 537 ? 2.0566 1.7350 1.6232 0.1435 0.2592 0.1647 537 VAL A C 3625 O O . VAL A 537 ? 2.1493 1.8037 1.6724 0.1588 0.2888 0.1643 537 VAL A O 3626 C CB . VAL A 537 ? 2.0840 1.8328 1.7061 0.1265 0.2274 0.1986 537 VAL A CB 3627 C CG1 . VAL A 537 ? 2.2183 1.9399 1.7657 0.1303 0.2468 0.1969 537 VAL A CG1 3628 C CG2 . VAL A 537 ? 1.8567 1.6540 1.5461 0.1280 0.2206 0.2247 537 VAL A CG2 3629 N N . ASN A 538 ? 2.0561 1.7127 1.6134 0.1281 0.2403 0.1451 538 ASN A N 3630 C CA . ASN A 538 ? 2.2762 1.8760 1.7768 0.1276 0.2525 0.1212 538 ASN A CA 3631 C C . ASN A 538 ? 2.2401 1.8347 1.7657 0.1147 0.2324 0.1088 538 ASN A C 3632 O O . ASN A 538 ? 1.9991 1.5799 1.5025 0.0912 0.2094 0.0953 538 ASN A O 3633 C CB . ASN A 538 ? 2.4391 2.0003 1.8583 0.1124 0.2506 0.1061 538 ASN A CB 3634 C CG . ASN A 538 ? 2.4893 1.9820 1.8418 0.1144 0.2712 0.0804 538 ASN A CG 3635 O OD1 . ASN A 538 ? 2.4486 1.9217 1.8174 0.1174 0.2741 0.0710 538 ASN A OD1 3636 N ND2 . ASN A 538 ? 2.5075 1.9606 1.7813 0.1120 0.2864 0.0689 538 ASN A ND2 3637 N N . MET A 539 ? 2.3730 1.9806 1.9444 0.1300 0.2421 0.1156 539 MET A N 3638 C CA . MET A 539 ? 2.3551 1.9770 1.9690 0.1205 0.2230 0.1122 539 MET A CA 3639 C C . MET A 539 ? 2.2264 1.8329 1.8231 0.0942 0.1976 0.0956 539 MET A C 3640 O O . MET A 539 ? 1.8477 1.4863 1.4877 0.0827 0.1755 0.0992 539 MET A O 3641 C CB . MET A 539 ? 2.4734 2.0822 2.1020 0.1386 0.2424 0.1137 539 MET A CB 3642 C CG . MET A 539 ? 2.4977 2.1284 2.1715 0.1304 0.2244 0.1142 539 MET A CG 3643 S SD . MET A 539 ? 3.2822 2.9080 2.9784 0.1526 0.2450 0.1238 539 MET A SD 3644 C CE . MET A 539 ? 3.1669 2.7171 2.7977 0.1590 0.2694 0.1063 539 MET A CE 3645 N N . GLU A 540 ? 2.4168 1.9737 1.9508 0.0844 0.2018 0.0778 540 GLU A N 3646 C CA . GLU A 540 ? 2.6305 2.1695 2.1467 0.0572 0.1786 0.0625 540 GLU A CA 3647 C C . GLU A 540 ? 2.4426 1.9724 1.9118 0.0346 0.1608 0.0559 540 GLU A C 3648 O O . GLU A 540 ? 2.4746 2.0137 1.9502 0.0103 0.1339 0.0520 540 GLU A O 3649 C CB . GLU A 540 ? 2.7911 2.2784 2.2805 0.0564 0.1912 0.0461 540 GLU A CB 3650 C CG . GLU A 540 ? 2.8285 2.2523 2.2462 0.0631 0.2169 0.0309 540 GLU A CG 3651 C CD . GLU A 540 ? 3.0075 2.4398 2.4191 0.0899 0.2431 0.0428 540 GLU A CD 3652 O OE1 . GLU A 540 ? 3.2037 2.6516 2.6544 0.1159 0.2632 0.0568 540 GLU A OE1 3653 O OE2 . GLU A 540 ? 3.0862 2.5147 2.4568 0.0841 0.2425 0.0409 540 GLU A OE2 3654 N N . ARG A 541 ? 2.1805 1.6946 1.6027 0.0419 0.1753 0.0564 541 ARG A N 3655 C CA . ARG A 541 ? 2.0927 1.6054 1.4700 0.0195 0.1557 0.0539 541 ARG A CA 3656 C C . ARG A 541 ? 2.0117 1.5875 1.4509 0.0130 0.1291 0.0754 541 ARG A C 3657 O O . ARG A 541 ? 1.8924 1.4836 1.3385 -0.0107 0.0998 0.0759 541 ARG A O 3658 C CB . ARG A 541 ? 2.1343 1.6242 1.4514 0.0310 0.1789 0.0536 541 ARG A CB 3659 C CG . ARG A 541 ? 2.0858 1.5040 1.3289 0.0363 0.2074 0.0298 541 ARG A CG 3660 C CD . ARG A 541 ? 2.1595 1.5339 1.3308 0.0027 0.1880 0.0068 541 ARG A CD 3661 N NE . ARG A 541 ? 2.4216 1.7861 1.5227 -0.0095 0.1845 0.0047 541 ARG A NE 3662 C CZ . ARG A 541 ? 2.6121 1.9373 1.6477 0.0062 0.2180 -0.0034 541 ARG A CZ 3663 N NH1 . ARG A 541 ? 2.6640 1.9595 1.7029 0.0380 0.2590 -0.0074 541 ARG A NH1 3664 N NH2 . ARG A 541 ? 2.7646 2.0828 1.7320 -0.0087 0.2115 -0.0052 541 ARG A NH2 3665 N N . ASP A 542 ? 1.9791 1.5902 1.4670 0.0345 0.1406 0.0938 542 ASP A N 3666 C CA . ASP A 542 ? 2.0425 1.7076 1.5927 0.0331 0.1218 0.1147 542 ASP A CA 3667 C C . ASP A 542 ? 2.1140 1.8001 1.7174 0.0225 0.1014 0.1131 542 ASP A C 3668 O O . ASP A 542 ? 2.0804 1.8018 1.7223 0.0142 0.0808 0.1261 542 ASP A O 3669 C CB . ASP A 542 ? 2.0963 1.7871 1.6875 0.0567 0.1408 0.1316 542 ASP A CB 3670 C CG . ASP A 542 ? 2.0995 1.7775 1.6463 0.0696 0.1643 0.1381 542 ASP A CG 3671 O OD1 . ASP A 542 ? 2.1297 1.7761 1.6082 0.0606 0.1664 0.1278 542 ASP A OD1 3672 O OD2 . ASP A 542 ? 2.0721 1.7721 1.6515 0.0879 0.1813 0.1539 542 ASP A OD2 3673 N N . LEU A 543 ? 2.2081 1.8730 1.8155 0.0246 0.1093 0.0990 543 LEU A N 3674 C CA . LEU A 543 ? 2.2114 1.8887 1.8540 0.0107 0.0913 0.0946 543 LEU A CA 3675 C C . LEU A 543 ? 2.3159 1.9755 1.9209 -0.0158 0.0715 0.0850 543 LEU A C 3676 O O . LEU A 543 ? 2.4001 2.0908 2.0331 -0.0310 0.0476 0.0941 543 LEU A O 3677 C CB . LEU A 543 ? 1.9987 1.6614 1.6578 0.0203 0.1056 0.0857 543 LEU A CB 3678 C CG . LEU A 543 ? 2.0362 1.6940 1.7046 0.0013 0.0908 0.0766 543 LEU A CG 3679 C CD1 . LEU A 543 ? 2.0872 1.7723 1.8125 0.0083 0.0916 0.0810 543 LEU A CD1 3680 C CD2 . LEU A 543 ? 2.1852 1.7905 1.8015 -0.0082 0.0984 0.0591 543 LEU A CD2 3681 N N . ALA A 544 ? 2.2183 1.8277 1.7617 -0.0220 0.0816 0.0673 544 ALA A N 3682 C CA . ALA A 544 ? 2.1324 1.7205 1.6404 -0.0513 0.0620 0.0555 544 ALA A CA 3683 C C . ALA A 544 ? 2.1213 1.7280 1.6044 -0.0684 0.0396 0.0646 544 ALA A C 3684 O O . ALA A 544 ? 2.4568 2.0619 1.9203 -0.0967 0.0152 0.0610 544 ALA A O 3685 C CB . ALA A 544 ? 2.1578 1.6796 1.6028 -0.0547 0.0798 0.0326 544 ALA A CB 3686 N N . SER A 545 ? 2.0012 1.6305 1.4898 -0.0525 0.0461 0.0797 545 SER A N 3687 C CA . SER A 545 ? 2.0696 1.7279 1.5481 -0.0665 0.0231 0.0957 545 SER A CA 3688 C C . SER A 545 ? 2.0024 1.7201 1.5595 -0.0695 -0.0002 0.1188 545 SER A C 3689 O O . SER A 545 ? 2.0464 1.7903 1.6017 -0.0865 -0.0257 0.1335 545 SER A O 3690 C CB . SER A 545 ? 2.1000 1.7538 1.5428 -0.0508 0.0405 0.1038 545 SER A CB 3691 O OG . SER A 545 ? 2.0193 1.6173 1.3772 -0.0532 0.0585 0.0831 545 SER A OG 3692 N N . GLY A 546 ? 1.8479 1.5853 1.4710 -0.0530 0.0090 0.1224 546 GLY A N 3693 C CA . GLY A 546 ? 1.8904 1.6765 1.5888 -0.0534 -0.0076 0.1406 546 GLY A CA 3694 C C . GLY A 546 ? 1.9058 1.7131 1.6653 -0.0296 0.0075 0.1490 546 GLY A C 3695 O O . GLY A 546 ? 1.7111 1.5501 1.5324 -0.0272 -0.0002 0.1595 546 GLY A O 3696 N N . LEU A 547 ? 1.9647 1.7542 1.7069 -0.0123 0.0299 0.1446 547 LEU A N 3697 C CA . LEU A 547 ? 1.9285 1.7366 1.7214 0.0064 0.0421 0.1528 547 LEU A CA 3698 C C . LEU A 547 ? 1.7183 1.5197 1.5366 0.0133 0.0534 0.1392 547 LEU A C 3699 O O . LEU A 547 ? 1.6719 1.4539 1.4723 0.0243 0.0716 0.1309 547 LEU A O 3700 C CB . LEU A 547 ? 2.0225 1.8253 1.7958 0.0208 0.0590 0.1607 547 LEU A CB 3701 C CG . LEU A 547 ? 2.0006 1.8242 1.7792 0.0237 0.0550 0.1835 547 LEU A CG 3702 C CD1 . LEU A 547 ? 1.8333 1.6895 1.6639 0.0185 0.0354 0.2019 547 LEU A CD1 3703 C CD2 . LEU A 547 ? 1.9676 1.7744 1.6781 0.0171 0.0554 0.1852 547 LEU A CD2 3704 N N . ILE A 548 ? 1.4731 1.2922 1.3324 0.0071 0.0431 0.1389 548 ILE A N 3705 C CA . ILE A 548 ? 1.5188 1.3462 1.4192 0.0173 0.0532 0.1342 548 ILE A CA 3706 C C . ILE A 548 ? 1.6324 1.4876 1.5873 0.0167 0.0445 0.1431 548 ILE A C 3707 O O . ILE A 548 ? 1.6042 1.4766 1.5718 0.0089 0.0292 0.1559 548 ILE A O 3708 C CB . ILE A 548 ? 1.4281 1.2385 1.3194 0.0153 0.0610 0.1184 548 ILE A CB 3709 C CG1 . ILE A 548 ? 1.4594 1.2581 1.3263 -0.0022 0.0500 0.1125 548 ILE A CG1 3710 C CG2 . ILE A 548 ? 1.5384 1.3287 1.4060 0.0275 0.0789 0.1122 548 ILE A CG2 3711 C CD1 . ILE A 548 ? 1.5357 1.3613 1.4470 -0.0110 0.0383 0.1174 548 ILE A CD1 3712 N N . GLY A 549 ? 1.6726 1.5309 1.6570 0.0253 0.0551 0.1367 549 GLY A N 3713 C CA . GLY A 549 ? 1.7268 1.6023 1.7603 0.0277 0.0552 0.1379 549 GLY A CA 3714 C C . GLY A 549 ? 1.6968 1.5638 1.7339 0.0332 0.0689 0.1234 549 GLY A C 3715 O O . GLY A 549 ? 1.7495 1.6027 1.7574 0.0357 0.0758 0.1172 549 GLY A O 3716 N N . PRO A 550 ? 1.6651 1.5407 1.7370 0.0358 0.0739 0.1190 550 PRO A N 3717 C CA . PRO A 550 ? 1.5690 1.4376 1.6380 0.0381 0.0853 0.1046 550 PRO A CA 3718 C C . PRO A 550 ? 1.5811 1.4468 1.6633 0.0433 0.0911 0.1013 550 PRO A C 3719 O O . PRO A 550 ? 1.5797 1.4485 1.6873 0.0463 0.0890 0.1092 550 PRO A O 3720 C CB . PRO A 550 ? 1.5566 1.4352 1.6522 0.0366 0.0890 0.1012 550 PRO A CB 3721 C CG . PRO A 550 ? 1.6005 1.4931 1.7319 0.0394 0.0826 0.1151 550 PRO A CG 3722 C CD . PRO A 550 ? 1.6619 1.5542 1.7760 0.0371 0.0703 0.1278 550 PRO A CD 3723 N N . LEU A 551 ? 1.5014 1.3611 1.5671 0.0429 0.0975 0.0909 551 LEU A N 3724 C CA . LEU A 551 ? 1.3931 1.2501 1.4674 0.0428 0.1008 0.0853 551 LEU A CA 3725 C C . LEU A 551 ? 1.3494 1.2031 1.4145 0.0395 0.1080 0.0701 551 LEU A C 3726 O O . LEU A 551 ? 1.4618 1.3167 1.5031 0.0381 0.1094 0.0680 551 LEU A O 3727 C CB . LEU A 551 ? 1.3098 1.1688 1.3719 0.0435 0.0975 0.0940 551 LEU A CB 3728 C CG . LEU A 551 ? 1.3481 1.2080 1.4158 0.0387 0.0978 0.0890 551 LEU A CG 3729 C CD1 . LEU A 551 ? 1.3620 1.2154 1.4580 0.0356 0.0969 0.0882 551 LEU A CD1 3730 C CD2 . LEU A 551 ? 1.4755 1.3451 1.5314 0.0403 0.0957 0.1006 551 LEU A CD2 3731 N N . LEU A 552 ? 1.3294 1.1764 1.4111 0.0382 0.1135 0.0599 552 LEU A N 3732 C CA . LEU A 552 ? 1.3429 1.1843 1.4099 0.0337 0.1213 0.0436 552 LEU A CA 3733 C C . LEU A 552 ? 1.5027 1.3376 1.5612 0.0255 0.1179 0.0361 552 LEU A C 3734 O O . LEU A 552 ? 1.6970 1.5202 1.7740 0.0235 0.1180 0.0331 552 LEU A O 3735 C CB . LEU A 552 ? 1.1671 1.0025 1.2531 0.0379 0.1339 0.0344 552 LEU A CB 3736 C CG . LEU A 552 ? 1.0863 0.9350 1.1813 0.0421 0.1342 0.0445 552 LEU A CG 3737 C CD1 . LEU A 552 ? 1.0397 0.8915 1.1651 0.0485 0.1465 0.0428 552 LEU A CD1 3738 C CD2 . LEU A 552 ? 1.1093 0.9626 1.1732 0.0376 0.1345 0.0426 552 LEU A CD2 3739 N N . ILE A 553 ? 1.4261 1.2690 1.4586 0.0196 0.1136 0.0353 553 ILE A N 3740 C CA . ILE A 553 ? 1.5050 1.3453 1.5272 0.0076 0.1081 0.0272 553 ILE A CA 3741 C C . ILE A 553 ? 1.6031 1.4345 1.6010 0.0017 0.1165 0.0082 553 ILE A C 3742 O O . ILE A 553 ? 1.6590 1.4998 1.6373 0.0038 0.1198 0.0099 553 ILE A O 3743 C CB . ILE A 553 ? 1.5470 1.4074 1.5582 0.0041 0.0969 0.0416 553 ILE A CB 3744 C CG1 . ILE A 553 ? 1.6100 1.4784 1.6421 0.0112 0.0925 0.0602 553 ILE A CG1 3745 C CG2 . ILE A 553 ? 1.6107 1.4737 1.6103 -0.0125 0.0880 0.0340 553 ILE A CG2 3746 C CD1 . ILE A 553 ? 1.7182 1.6049 1.7405 0.0177 0.0898 0.0776 553 ILE A CD1 3747 N N . CYS A 554 ? 1.6148 1.4252 1.6120 -0.0057 0.1217 -0.0099 554 CYS A N 3748 C CA . CYS A 554 ? 1.6063 1.4039 1.5771 -0.0095 0.1345 -0.0301 554 CYS A CA 3749 C C . CYS A 554 ? 1.5518 1.3347 1.4954 -0.0279 0.1293 -0.0477 554 CYS A C 3750 O O . CYS A 554 ? 1.4575 1.2369 1.4118 -0.0378 0.1167 -0.0450 554 CYS A O 3751 C CB . CYS A 554 ? 1.7338 1.5156 1.7263 0.0033 0.1540 -0.0380 554 CYS A CB 3752 S SG . CYS A 554 ? 2.0544 1.8607 2.0682 0.0183 0.1562 -0.0171 554 CYS A SG 3753 N N . TYR A 555 ? 1.6532 1.4286 1.5593 -0.0343 0.1381 -0.0648 555 TYR A N 3754 C CA . TYR A 555 ? 1.9166 1.6801 1.7846 -0.0562 0.1299 -0.0822 555 TYR A CA 3755 C C . TYR A 555 ? 2.0322 1.7530 1.9013 -0.0629 0.1402 -0.1070 555 TYR A C 3756 O O . TYR A 555 ? 2.2526 1.9534 2.1472 -0.0467 0.1600 -0.1124 555 TYR A O 3757 C CB . TYR A 555 ? 2.1262 1.8958 1.9466 -0.0617 0.1361 -0.0913 555 TYR A CB 3758 C CG . TYR A 555 ? 2.4905 2.2698 2.2711 -0.0866 0.1153 -0.0947 555 TYR A CG 3759 C CD1 . TYR A 555 ? 2.6116 2.3879 2.4017 -0.1040 0.0957 -0.0948 555 TYR A CD1 3760 C CD2 . TYR A 555 ? 2.4848 2.2790 2.2196 -0.0944 0.1140 -0.0953 555 TYR A CD2 3761 C CE1 . TYR A 555 ? 2.8714 2.6616 2.6287 -0.1297 0.0734 -0.0956 555 TYR A CE1 3762 C CE2 . TYR A 555 ? 2.7266 2.5343 2.4250 -0.1189 0.0918 -0.0956 555 TYR A CE2 3763 C CZ . TYR A 555 ? 3.0839 2.8909 2.7950 -0.1371 0.0707 -0.0958 555 TYR A CZ 3764 O OH . TYR A 555 ? 3.6275 3.4530 3.3063 -0.1644 0.0454 -0.0936 555 TYR A OH 3765 N N . LYS A 556 ? 2.1145 1.8210 1.9574 -0.0873 0.1265 -0.1209 556 LYS A N 3766 C CA . LYS A 556 ? 2.4903 2.1491 2.3333 -0.0976 0.1340 -0.1449 556 LYS A CA 3767 C C . LYS A 556 ? 2.8137 2.4284 2.6187 -0.0967 0.1614 -0.1790 556 LYS A C 3768 O O . LYS A 556 ? 3.0658 2.6382 2.8410 -0.1157 0.1637 -0.2064 556 LYS A O 3769 C CB . LYS A 556 ? 2.4908 2.1505 2.3218 -0.1280 0.1068 -0.1460 556 LYS A CB 3770 C CG . LYS A 556 ? 2.5414 2.1551 2.3881 -0.1402 0.1085 -0.1615 556 LYS A CG 3771 C CD . LYS A 556 ? 2.2903 1.9108 2.2008 -0.1232 0.1087 -0.1367 556 LYS A CD 3772 C CE . LYS A 556 ? 2.2357 1.8064 2.1640 -0.1335 0.1135 -0.1503 556 LYS A CE 3773 N NZ . LYS A 556 ? 2.0481 1.6223 2.0360 -0.1104 0.1210 -0.1263 556 LYS A NZ 3774 N N . GLU A 557 ? 2.9491 2.5720 2.7556 -0.0750 0.1837 -0.1776 557 GLU A N 3775 C CA . GLU A 557 ? 3.1135 2.6996 2.8863 -0.0702 0.2146 -0.2069 557 GLU A CA 3776 C C . GLU A 557 ? 3.0922 2.6309 2.8965 -0.0572 0.2383 -0.2214 557 GLU A C 3777 O O . GLU A 557 ? 3.2542 2.7421 3.0235 -0.0666 0.2545 -0.2534 557 GLU A O 3778 C CB . GLU A 557 ? 3.1323 2.7468 2.9032 -0.0513 0.2321 -0.1968 557 GLU A CB 3779 C CG . GLU A 557 ? 3.1639 2.7850 2.9946 -0.0220 0.2524 -0.1818 557 GLU A CG 3780 C CD . GLU A 557 ? 3.0286 2.6998 2.8861 -0.0110 0.2419 -0.1504 557 GLU A CD 3781 O OE1 . GLU A 557 ? 2.9610 2.6596 2.8021 -0.0231 0.2171 -0.1366 557 GLU A OE1 3782 O OE2 . GLU A 557 ? 2.9537 2.6364 2.8504 0.0093 0.2585 -0.1387 557 GLU A OE2 3783 N N . ARG A 571 ? 1.8477 1.7701 2.2218 0.1073 0.2081 0.0950 571 ARG A N 3784 C CA . ARG A 571 ? 1.8865 1.8065 2.2088 0.0920 0.2024 0.0810 571 ARG A CA 3785 C C . ARG A 571 ? 1.7928 1.7412 2.1113 0.0781 0.1793 0.0981 571 ARG A C 3786 O O . ARG A 571 ? 1.7311 1.6931 2.0642 0.0745 0.1585 0.1164 571 ARG A O 3787 C CB . ARG A 571 ? 1.8927 1.7795 2.1643 0.0846 0.1972 0.0607 571 ARG A CB 3788 C CG . ARG A 571 ? 2.0977 1.9530 2.3550 0.0905 0.2203 0.0365 571 ARG A CG 3789 C CD . ARG A 571 ? 2.2281 2.0538 2.4539 0.0830 0.2111 0.0230 571 ARG A CD 3790 N NE . ARG A 571 ? 2.6446 2.4593 2.9023 0.0895 0.2060 0.0333 571 ARG A NE 3791 C CZ . ARG A 571 ? 2.7263 2.5106 2.9715 0.0853 0.2050 0.0217 571 ARG A CZ 3792 N NH1 . ARG A 571 ? 2.8435 2.6076 3.0440 0.0734 0.2068 -0.0012 571 ARG A NH1 3793 N NH2 . ARG A 571 ? 2.3311 2.1062 2.6090 0.0912 0.2010 0.0348 571 ARG A NH2 3794 N N . ASN A 572 ? 1.6540 1.6082 1.9494 0.0692 0.1836 0.0918 572 ASN A N 3795 C CA . ASN A 572 ? 1.6893 1.6667 1.9849 0.0548 0.1668 0.1063 572 ASN A CA 3796 C C . ASN A 572 ? 1.7723 1.7340 2.0174 0.0401 0.1475 0.1016 572 ASN A C 3797 O O . ASN A 572 ? 1.8362 1.7842 2.0447 0.0346 0.1535 0.0897 572 ASN A O 3798 C CB . ASN A 572 ? 1.6036 1.5978 1.9107 0.0531 0.1843 0.1065 572 ASN A CB 3799 C CG . ASN A 572 ? 1.5762 1.6077 1.9475 0.0594 0.1900 0.1279 572 ASN A CG 3800 O OD1 . ASN A 572 ? 1.6327 1.6876 2.0315 0.0527 0.1685 0.1485 572 ASN A OD1 3801 N ND2 . ASN A 572 ? 1.5663 1.6054 1.9622 0.0724 0.2195 0.1246 572 ASN A ND2 3802 N N . VAL A 573 ? 1.6013 1.5651 1.8439 0.0343 0.1259 0.1126 573 VAL A N 3803 C CA . VAL A 573 ? 1.4638 1.4081 1.6571 0.0234 0.1122 0.1071 573 VAL A CA 3804 C C . VAL A 573 ? 1.5423 1.4961 1.7287 0.0065 0.0959 0.1173 573 VAL A C 3805 O O . VAL A 573 ? 1.6875 1.6581 1.8923 0.0009 0.0795 0.1321 573 VAL A O 3806 C CB . VAL A 573 ? 1.3803 1.3100 1.5578 0.0278 0.1025 0.1072 573 VAL A CB 3807 C CG1 . VAL A 573 ? 1.3761 1.2890 1.5074 0.0179 0.0899 0.1053 573 VAL A CG1 3808 C CG2 . VAL A 573 ? 1.3163 1.2287 1.4865 0.0382 0.1165 0.0931 573 VAL A CG2 3809 N N . ILE A 574 ? 1.5055 1.4470 1.6637 -0.0028 0.0998 0.1099 574 ILE A N 3810 C CA . ILE A 574 ? 1.4086 1.3459 1.5479 -0.0220 0.0849 0.1150 574 ILE A CA 3811 C C . ILE A 574 ? 1.3404 1.2424 1.4257 -0.0239 0.0794 0.1053 574 ILE A C 3812 O O . ILE A 574 ? 1.2586 1.1410 1.3189 -0.0159 0.0915 0.0951 574 ILE A O 3813 C CB . ILE A 574 ? 1.4517 1.3950 1.5975 -0.0318 0.0944 0.1156 574 ILE A CB 3814 C CG1 . ILE A 574 ? 1.5477 1.5313 1.7484 -0.0382 0.0923 0.1321 574 ILE A CG1 3815 C CG2 . ILE A 574 ? 1.4125 1.3327 1.5222 -0.0513 0.0829 0.1142 574 ILE A CG2 3816 C CD1 . ILE A 574 ? 1.6998 1.7104 1.9486 -0.0209 0.0997 0.1400 574 ILE A CD1 3817 N N . LEU A 575 ? 1.3515 1.2469 1.4189 -0.0338 0.0618 0.1098 575 LEU A N 3818 C CA . LEU A 575 ? 1.4562 1.3154 1.4701 -0.0361 0.0592 0.1011 575 LEU A CA 3819 C C . LEU A 575 ? 1.5234 1.3614 1.5058 -0.0578 0.0484 0.0990 575 LEU A C 3820 O O . LEU A 575 ? 1.5631 1.4120 1.5483 -0.0740 0.0300 0.1063 575 LEU A O 3821 C CB . LEU A 575 ? 1.3521 1.2098 1.3557 -0.0278 0.0524 0.1042 575 LEU A CB 3822 C CG . LEU A 575 ? 1.4144 1.2443 1.3679 -0.0386 0.0424 0.1010 575 LEU A CG 3823 C CD1 . LEU A 575 ? 1.2936 1.0852 1.2022 -0.0309 0.0564 0.0893 575 LEU A CD1 3824 C CD2 . LEU A 575 ? 1.5612 1.4031 1.5140 -0.0375 0.0299 0.1108 575 LEU A CD2 3825 N N . PHE A 576 ? 1.4817 1.2877 1.4329 -0.0592 0.0591 0.0898 576 PHE A N 3826 C CA . PHE A 576 ? 1.5324 1.3076 1.4492 -0.0798 0.0515 0.0853 576 PHE A CA 3827 C C . PHE A 576 ? 1.6742 1.4106 1.5374 -0.0785 0.0499 0.0763 576 PHE A C 3828 O O . PHE A 576 ? 1.7456 1.4497 1.5791 -0.0654 0.0656 0.0690 576 PHE A O 3829 C CB . PHE A 576 ? 1.5639 1.3192 1.4741 -0.0815 0.0658 0.0818 576 PHE A CB 3830 C CG . PHE A 576 ? 1.6316 1.4197 1.5860 -0.0904 0.0667 0.0909 576 PHE A CG 3831 C CD1 . PHE A 576 ? 1.6519 1.4702 1.6409 -0.0738 0.0800 0.0948 576 PHE A CD1 3832 C CD2 . PHE A 576 ? 1.7095 1.4973 1.6697 -0.1166 0.0553 0.0954 576 PHE A CD2 3833 C CE1 . PHE A 576 ? 1.7370 1.5855 1.7655 -0.0801 0.0852 0.1035 576 PHE A CE1 3834 C CE2 . PHE A 576 ? 1.7409 1.5634 1.7468 -0.1243 0.0585 0.1068 576 PHE A CE2 3835 C CZ . PHE A 576 ? 1.7101 1.5634 1.7501 -0.1044 0.0751 0.1110 576 PHE A CZ 3836 N N . SER A 577 ? 1.7931 1.5340 1.6436 -0.0914 0.0318 0.0786 577 SER A N 3837 C CA . SER A 577 ? 1.9632 1.6671 1.7578 -0.0902 0.0323 0.0697 577 SER A CA 3838 C C . SER A 577 ? 2.1374 1.8095 1.8852 -0.1186 0.0168 0.0615 577 SER A C 3839 O O . SER A 577 ? 2.1799 1.8774 1.9416 -0.1412 -0.0065 0.0692 577 SER A O 3840 C CB . SER A 577 ? 1.7549 1.4832 1.5585 -0.0756 0.0290 0.0778 577 SER A CB 3841 O OG . SER A 577 ? 1.6931 1.3863 1.4454 -0.0665 0.0389 0.0699 577 SER A OG 3842 N N . VAL A 578 ? 2.2107 1.8260 1.9029 -0.1173 0.0306 0.0463 578 VAL A N 3843 C CA . VAL A 578 ? 2.0601 1.6312 1.6892 -0.1400 0.0208 0.0331 578 VAL A CA 3844 C C . VAL A 578 ? 1.9915 1.5558 1.5816 -0.1288 0.0226 0.0312 578 VAL A C 3845 O O . VAL A 578 ? 1.8699 1.4169 1.4447 -0.1020 0.0457 0.0284 578 VAL A O 3846 C CB . VAL A 578 ? 2.0374 1.5427 1.6247 -0.1464 0.0369 0.0166 578 VAL A CB 3847 C CG1 . VAL A 578 ? 1.9709 1.4270 1.5114 -0.1210 0.0647 0.0056 578 VAL A CG1 3848 C CG2 . VAL A 578 ? 2.0479 1.5209 1.5950 -0.1855 0.0168 0.0055 578 VAL A CG2 3849 N N . PHE A 579 ? 1.9692 1.5532 1.5473 -0.1495 -0.0025 0.0363 579 PHE A N 3850 C CA . PHE A 579 ? 2.0865 1.6612 1.6199 -0.1431 -0.0016 0.0351 579 PHE A CA 3851 C C . PHE A 579 ? 2.1965 1.7086 1.6445 -0.1644 -0.0025 0.0138 579 PHE A C 3852 O O . PHE A 579 ? 2.2441 1.7494 1.6719 -0.1994 -0.0272 0.0091 579 PHE A O 3853 C CB . PHE A 579 ? 2.0782 1.7120 1.6455 -0.1502 -0.0272 0.0561 579 PHE A CB 3854 C CG . PHE A 579 ? 2.0135 1.6992 1.6576 -0.1265 -0.0218 0.0743 579 PHE A CG 3855 C CD1 . PHE A 579 ? 1.9244 1.6114 1.5761 -0.0964 -0.0001 0.0771 579 PHE A CD1 3856 C CD2 . PHE A 579 ? 2.0091 1.7407 1.7179 -0.1348 -0.0368 0.0883 579 PHE A CD2 3857 C CE1 . PHE A 579 ? 1.8859 1.6144 1.6032 -0.0778 0.0042 0.0911 579 PHE A CE1 3858 C CE2 . PHE A 579 ? 1.9234 1.6955 1.6976 -0.1128 -0.0290 0.1020 579 PHE A CE2 3859 C CZ . PHE A 579 ? 1.9266 1.6945 1.7023 -0.0856 -0.0094 0.1019 579 PHE A CZ 3860 N N . ASP A 580 ? 2.1482 1.6135 1.5459 -0.1441 0.0253 0.0010 580 ASP A N 3861 C CA . ASP A 580 ? 2.3186 1.7174 1.6270 -0.1618 0.0291 -0.0218 580 ASP A CA 3862 C C . ASP A 580 ? 2.3310 1.7388 1.5913 -0.1709 0.0160 -0.0192 580 ASP A C 3863 O O . ASP A 580 ? 2.3607 1.7486 1.5834 -0.1485 0.0397 -0.0224 580 ASP A O 3864 C CB . ASP A 580 ? 2.4857 1.8207 1.7569 -0.1364 0.0688 -0.0382 580 ASP A CB 3865 C CG . ASP A 580 ? 2.7533 2.0074 1.9286 -0.1558 0.0763 -0.0660 580 ASP A CG 3866 O OD1 . ASP A 580 ? 2.6549 1.8769 1.8077 -0.1893 0.0597 -0.0796 580 ASP A OD1 3867 O OD2 . ASP A 580 ? 2.9827 2.2045 2.1039 -0.1384 0.0996 -0.0744 580 ASP A OD2 3868 N N . GLU A 581 ? 2.2156 1.6561 1.4782 -0.2040 -0.0215 -0.0109 581 GLU A N 3869 C CA . GLU A 581 ? 2.2439 1.6955 1.4575 -0.2172 -0.0386 -0.0058 581 GLU A CA 3870 C C . GLU A 581 ? 2.4547 1.8295 1.5602 -0.2234 -0.0206 -0.0336 581 GLU A C 3871 O O . GLU A 581 ? 2.6568 2.0347 1.7149 -0.2230 -0.0220 -0.0300 581 GLU A O 3872 C CB . GLU A 581 ? 2.2120 1.7082 1.4422 -0.2560 -0.0845 0.0081 581 GLU A CB 3873 C CG . GLU A 581 ? 2.1554 1.7366 1.4824 -0.2441 -0.1010 0.0422 581 GLU A CG 3874 C CD . GLU A 581 ? 2.2200 1.8362 1.5461 -0.2273 -0.1022 0.0625 581 GLU A CD 3875 O OE1 . GLU A 581 ? 2.2661 1.8497 1.5117 -0.2322 -0.0978 0.0530 581 GLU A OE1 3876 O OE2 . GLU A 581 ? 2.1574 1.8326 1.5635 -0.2095 -0.1064 0.0885 581 GLU A OE2 3877 N N . ASN A 582 ? 2.5674 1.8720 1.6342 -0.2285 -0.0020 -0.0602 582 ASN A N 3878 C CA . ASN A 582 ? 2.6949 1.9124 1.6607 -0.2270 0.0263 -0.0904 582 ASN A CA 3879 C C . ASN A 582 ? 2.8812 2.0912 1.8282 -0.1856 0.0643 -0.0871 582 ASN A C 3880 O O . ASN A 582 ? 3.0402 2.1974 1.8973 -0.1868 0.0815 -0.1054 582 ASN A O 3881 C CB . ASN A 582 ? 2.7248 1.8738 1.6784 -0.2273 0.0476 -0.1130 582 ASN A CB 3882 C CG . ASN A 582 ? 2.9293 2.0115 1.8012 -0.2723 0.0313 -0.1414 582 ASN A CG 3883 O OD1 . ASN A 582 ? 3.1104 2.1169 1.8880 -0.2746 0.0525 -0.1683 582 ASN A OD1 3884 N ND2 . ASN A 582 ? 3.0073 2.1166 1.9135 -0.3095 -0.0062 -0.1357 582 ASN A ND2 3885 N N . ARG A 583 ? 2.7591 2.0190 1.7889 -0.1499 0.0791 -0.0646 583 ARG A N 3886 C CA . ARG A 583 ? 2.6608 1.9446 1.6965 -0.1157 0.1030 -0.0497 583 ARG A CA 3887 C C . ARG A 583 ? 2.4225 1.7933 1.5505 -0.1023 0.0869 -0.0166 583 ARG A C 3888 O O . ARG A 583 ? 2.3134 1.7087 1.5000 -0.0708 0.1072 -0.0036 583 ARG A O 3889 C CB . ARG A 583 ? 2.7021 1.9358 1.7183 -0.0791 0.1525 -0.0604 583 ARG A CB 3890 C CG . ARG A 583 ? 2.5951 1.8063 1.6535 -0.0667 0.1676 -0.0658 583 ARG A CG 3891 C CD . ARG A 583 ? 2.7978 1.9463 1.8178 -0.0351 0.2160 -0.0786 583 ARG A CD 3892 N NE . ARG A 583 ? 2.8570 2.0471 1.9454 0.0056 0.2402 -0.0553 583 ARG A NE 3893 C CZ . ARG A 583 ? 3.0049 2.2290 2.1714 0.0177 0.2375 -0.0408 583 ARG A CZ 3894 N NH1 . ARG A 583 ? 3.0818 2.3048 2.2720 -0.0052 0.2144 -0.0459 583 ARG A NH1 3895 N NH2 . ARG A 583 ? 2.9936 2.2552 2.2146 0.0515 0.2576 -0.0198 583 ARG A NH2 3896 N N . SER A 584 ? 2.3183 1.7341 1.4579 -0.1280 0.0491 -0.0027 584 SER A N 3897 C CA . SER A 584 ? 2.2872 1.7705 1.4783 -0.1160 0.0381 0.0275 584 SER A CA 3898 C C . SER A 584 ? 2.2904 1.7514 1.4172 -0.1008 0.0625 0.0265 584 SER A C 3899 O O . SER A 584 ? 2.2898 1.6870 1.3312 -0.1061 0.0805 0.0017 584 SER A O 3900 C CB . SER A 584 ? 2.3320 1.8605 1.5373 -0.1484 -0.0069 0.0430 584 SER A CB 3901 O OG . SER A 584 ? 2.2762 1.8716 1.5486 -0.1355 -0.0181 0.0749 584 SER A OG 3902 N N . TRP A 585 ? 2.1941 1.7030 1.3591 -0.0816 0.0663 0.0525 585 TRP A N 3903 C CA . TRP A 585 ? 2.3385 1.8342 1.4388 -0.0740 0.0833 0.0559 585 TRP A CA 3904 C C . TRP A 585 ? 2.4938 1.9994 1.5406 -0.1091 0.0475 0.0602 585 TRP A C 3905 O O . TRP A 585 ? 2.7616 2.2394 1.7215 -0.1168 0.0545 0.0534 585 TRP A O 3906 C CB . TRP A 585 ? 2.2848 1.8305 1.4436 -0.0461 0.0964 0.0857 585 TRP A CB 3907 C CG . TRP A 585 ? 2.2091 1.7593 1.4243 -0.0122 0.1284 0.0895 585 TRP A CG 3908 C CD1 . TRP A 585 ? 2.2151 1.8008 1.5186 -0.0027 0.1218 0.0999 585 TRP A CD1 3909 C CD2 . TRP A 585 ? 2.2243 1.7502 1.4150 0.0162 0.1709 0.0873 585 TRP A CD2 3910 N NE1 . TRP A 585 ? 2.3394 1.9247 1.6729 0.0267 0.1536 0.1038 585 TRP A NE1 3911 C CE2 . TRP A 585 ? 2.2593 1.8107 1.5294 0.0398 0.1843 0.0980 585 TRP A CE2 3912 C CE3 . TRP A 585 ? 2.3737 1.8586 1.4822 0.0240 0.1999 0.0776 585 TRP A CE3 3913 C CZ2 . TRP A 585 ? 2.3017 1.8453 1.5790 0.0704 0.2232 0.1027 585 TRP A CZ2 3914 C CZ3 . TRP A 585 ? 2.4907 1.9655 1.6072 0.0578 0.2431 0.0816 585 TRP A CZ3 3915 C CH2 . TRP A 585 ? 2.4095 1.9164 1.6132 0.0801 0.2529 0.0956 585 TRP A CH2 3916 N N . TYR A 586 ? 2.4216 1.9698 1.5220 -0.1302 0.0091 0.0731 586 TYR A N 3917 C CA . TYR A 586 ? 2.4948 2.0704 1.5682 -0.1627 -0.0306 0.0863 586 TYR A CA 3918 C C . TYR A 586 ? 2.6212 2.1489 1.6175 -0.2004 -0.0489 0.0579 586 TYR A C 3919 O O . TYR A 586 ? 2.7017 2.2389 1.6474 -0.2313 -0.0795 0.0633 586 TYR A O 3920 C CB . TYR A 586 ? 2.4333 2.0810 1.6091 -0.1651 -0.0611 0.1171 586 TYR A CB 3921 C CG . TYR A 586 ? 2.4003 2.0893 1.6520 -0.1307 -0.0438 0.1431 586 TYR A CG 3922 C CD1 . TYR A 586 ? 2.3286 2.0541 1.5825 -0.1254 -0.0502 0.1727 586 TYR A CD1 3923 C CD2 . TYR A 586 ? 2.4039 2.0943 1.7230 -0.1053 -0.0217 0.1386 586 TYR A CD2 3924 C CE1 . TYR A 586 ? 2.1317 1.8906 1.4551 -0.0967 -0.0347 0.1961 586 TYR A CE1 3925 C CE2 . TYR A 586 ? 2.2341 1.9591 1.6188 -0.0781 -0.0078 0.1605 586 TYR A CE2 3926 C CZ . TYR A 586 ? 2.0493 1.8070 1.4373 -0.0743 -0.0141 0.1888 586 TYR A CZ 3927 O OH . TYR A 586 ? 1.7774 1.5650 1.2307 -0.0502 -0.0007 0.2099 586 TYR A OH 3928 N N . LEU A 587 ? 2.7779 2.2526 1.7630 -0.1990 -0.0304 0.0286 587 LEU A N 3929 C CA . LEU A 587 ? 2.8965 2.3198 1.8174 -0.2367 -0.0471 -0.0001 587 LEU A CA 3930 C C . LEU A 587 ? 2.9623 2.3696 1.7835 -0.2694 -0.0688 -0.0054 587 LEU A C 3931 O O . LEU A 587 ? 2.9449 2.3657 1.7459 -0.3115 -0.1111 -0.0041 587 LEU A O 3932 C CB . LEU A 587 ? 3.0223 2.3626 1.8988 -0.2214 -0.0055 -0.0353 587 LEU A CB 3933 C CG . LEU A 587 ? 3.0206 2.2831 1.7950 -0.2069 0.0364 -0.0624 587 LEU A CG 3934 C CD1 . LEU A 587 ? 2.8712 2.0481 1.6005 -0.2122 0.0584 -0.0989 587 LEU A CD1 3935 C CD2 . LEU A 587 ? 2.8875 2.1637 1.6842 -0.1596 0.0776 -0.0481 587 LEU A CD2 3936 N N . THR A 588 ? 2.9703 2.3438 1.7256 -0.2488 -0.0357 -0.0132 588 THR A N 3937 C CA . THR A 588 ? 3.0034 2.3426 1.6424 -0.2729 -0.0417 -0.0257 588 THR A CA 3938 C C . THR A 588 ? 3.0523 2.4641 1.7036 -0.2994 -0.0903 0.0084 588 THR A C 3939 O O . THR A 588 ? 3.0695 2.4717 1.6502 -0.3437 -0.1261 0.0008 588 THR A O 3940 C CB . THR A 588 ? 2.8951 2.1946 1.4802 -0.2361 0.0110 -0.0344 588 THR A CB 3941 O OG1 . THR A 588 ? 2.9552 2.2543 1.4511 -0.2522 0.0026 -0.0295 588 THR A OG1 3942 C CG2 . THR A 588 ? 2.5980 1.9491 1.2878 -0.1878 0.0379 -0.0055 588 THR A CG2 3943 N N . GLU A 589 ? 2.9896 2.4728 1.7334 -0.2718 -0.0909 0.0466 589 GLU A N 3944 C CA . GLU A 589 ? 3.0125 2.5711 1.7871 -0.2874 -0.1319 0.0869 589 GLU A CA 3945 C C . GLU A 589 ? 2.9511 2.5434 1.7631 -0.3259 -0.1817 0.0941 589 GLU A C 3946 O O . GLU A 589 ? 2.9136 2.5338 1.6875 -0.3611 -0.2225 0.1091 589 GLU A O 3947 C CB . GLU A 589 ? 3.0131 2.6342 1.8879 -0.2487 -0.1195 0.1251 589 GLU A CB 3948 C CG . GLU A 589 ? 3.1331 2.8135 2.0097 -0.2555 -0.1455 0.1662 589 GLU A CG 3949 C CD . GLU A 589 ? 3.0999 2.8530 2.1021 -0.2315 -0.1532 0.2079 589 GLU A CD 3950 O OE1 . GLU A 589 ? 2.8860 2.6386 1.9458 -0.1954 -0.1195 0.2095 589 GLU A OE1 3951 O OE2 . GLU A 589 ? 3.2528 3.0637 2.2967 -0.2491 -0.1934 0.2403 589 GLU A OE2 3952 N N . ASN A 590 ? 2.8882 2.4801 1.7744 -0.3190 -0.1775 0.0853 590 ASN A N 3953 C CA . ASN A 590 ? 2.7915 2.4172 1.7272 -0.3518 -0.2189 0.0929 590 ASN A CA 3954 C C . ASN A 590 ? 3.0198 2.6004 1.8524 -0.4027 -0.2461 0.0670 590 ASN A C 3955 O O . ASN A 590 ? 3.1259 2.7518 1.9638 -0.4408 -0.2944 0.0865 590 ASN A O 3956 C CB . ASN A 590 ? 2.6024 2.2203 1.6177 -0.3345 -0.2009 0.0815 590 ASN A CB 3957 C CG . ASN A 590 ? 2.3783 2.0566 1.5094 -0.2960 -0.1894 0.1120 590 ASN A CG 3958 O OD1 . ASN A 590 ? 2.2903 2.0335 1.4708 -0.2941 -0.2116 0.1483 590 ASN A OD1 3959 N ND2 . ASN A 590 ? 2.1949 1.8502 1.3683 -0.2659 -0.1548 0.0979 590 ASN A ND2 3960 N N . ILE A 591 ? 3.1592 2.6502 1.9005 -0.4021 -0.2137 0.0241 591 ILE A N 3961 C CA . ILE A 591 ? 3.2038 2.6316 1.8329 -0.4496 -0.2317 -0.0093 591 ILE A CA 3962 C C . ILE A 591 ? 3.3542 2.8043 1.9047 -0.4801 -0.2648 0.0047 591 ILE A C 3963 O O . ILE A 591 ? 3.4255 2.8846 1.9387 -0.5315 -0.3114 0.0040 591 ILE A O 3964 C CB . ILE A 591 ? 3.1157 2.4338 1.6591 -0.4429 -0.1878 -0.0598 591 ILE A CB 3965 C CG1 . ILE A 591 ? 3.1735 2.4288 1.6001 -0.4995 -0.2139 -0.0928 591 ILE A CG1 3966 C CG2 . ILE A 591 ? 3.1352 2.4185 1.6325 -0.3996 -0.1367 -0.0674 591 ILE A CG2 3967 C CD1 . ILE A 591 ? 3.2252 2.3804 1.5129 -0.4976 -0.1765 -0.1344 591 ILE A CD1 3968 N N . GLN A 592 ? 3.3580 2.8181 1.8801 -0.4517 -0.2425 0.0186 592 GLN A N 3969 C CA . GLN A 592 ? 3.4539 2.9350 1.8954 -0.4791 -0.2716 0.0341 592 GLN A CA 3970 C C . GLN A 592 ? 3.3917 2.9800 1.9217 -0.4906 -0.3213 0.0887 592 GLN A C 3971 O O . GLN A 592 ? 3.4937 3.1254 2.0098 -0.4855 -0.3313 0.1204 592 GLN A O 3972 C CB . GLN A 592 ? 3.5285 2.9782 1.8993 -0.4467 -0.2277 0.0296 592 GLN A CB 3973 C CG . GLN A 592 ? 3.8051 3.1588 2.0169 -0.4698 -0.2098 -0.0170 592 GLN A CG 3974 C CD . GLN A 592 ? 4.0208 3.3773 2.1427 -0.4658 -0.2003 -0.0051 592 GLN A CD 3975 O OE1 . GLN A 592 ? 4.0665 3.4379 2.2165 -0.4207 -0.1612 0.0120 592 GLN A OE1 3976 N NE2 . GLN A 592 ? 4.2309 3.5739 2.2422 -0.5153 -0.2366 -0.0131 592 GLN A NE2 3977 N N . ARG A 593 ? 3.3021 2.9328 1.9241 -0.5057 -0.3511 0.1013 593 ARG A N 3978 C CA . ARG A 593 ? 3.2357 2.9694 1.9643 -0.5074 -0.3905 0.1550 593 ARG A CA 3979 C C . ARG A 593 ? 3.2055 2.9696 2.0031 -0.5377 -0.4257 0.1590 593 ARG A C 3980 O O . ARG A 593 ? 3.3364 3.1846 2.2114 -0.5503 -0.4660 0.2022 593 ARG A O 3981 C CB . ARG A 593 ? 3.2226 2.9968 2.0588 -0.4504 -0.3577 0.1824 593 ARG A CB 3982 C CG . ARG A 593 ? 3.2381 3.1068 2.1560 -0.4422 -0.3866 0.2407 593 ARG A CG 3983 C CD . ARG A 593 ? 3.2961 3.1973 2.3339 -0.3908 -0.3557 0.2614 593 ARG A CD 3984 N NE . ARG A 593 ? 3.1666 3.1152 2.3197 -0.3902 -0.3721 0.2770 593 ARG A NE 3985 C CZ . ARG A 593 ? 2.9266 2.8982 2.1846 -0.3513 -0.3476 0.2888 593 ARG A CZ 3986 N NH1 . ARG A 593 ? 2.9009 2.8541 2.1678 -0.3114 -0.3080 0.2873 593 ARG A NH1 3987 N NH2 . ARG A 593 ? 2.6282 2.6413 1.9813 -0.3535 -0.3623 0.3021 593 ARG A NH2 3988 N N . PHE A 594 ? 3.1471 2.8441 1.9197 -0.5485 -0.4092 0.1165 594 PHE A N 3989 C CA . PHE A 594 ? 3.0890 2.8108 1.9334 -0.5741 -0.4355 0.1190 594 PHE A CA 3990 C C . PHE A 594 ? 3.1497 2.8071 1.9017 -0.6293 -0.4566 0.0804 594 PHE A C 3991 O O . PHE A 594 ? 3.1616 2.8209 1.9635 -0.6493 -0.4691 0.0745 594 PHE A O 3992 C CB . PHE A 594 ? 3.1143 2.8269 2.0511 -0.5308 -0.3945 0.1115 594 PHE A CB 3993 C CG . PHE A 594 ? 3.1001 2.9010 2.1713 -0.4969 -0.3963 0.1569 594 PHE A CG 3994 C CD1 . PHE A 594 ? 3.0292 2.8570 2.1243 -0.4563 -0.3759 0.1799 594 PHE A CD1 3995 C CD2 . PHE A 594 ? 3.0946 2.9484 2.2690 -0.5052 -0.4157 0.1763 594 PHE A CD2 3996 C CE1 . PHE A 594 ? 2.9176 2.8182 2.1334 -0.4258 -0.3759 0.2192 594 PHE A CE1 3997 C CE2 . PHE A 594 ? 2.9733 2.9022 2.2680 -0.4724 -0.4135 0.2159 594 PHE A CE2 3998 C CZ . PHE A 594 ? 2.9125 2.8617 2.2262 -0.4329 -0.3936 0.2361 594 PHE A CZ 3999 N N . LEU A 595 ? 3.1998 2.7995 1.8163 -0.6557 -0.4608 0.0547 595 LEU A N 4000 C CA . LEU A 595 ? 3.2126 2.7219 1.7250 -0.6995 -0.4644 0.0057 595 LEU A CA 4001 C C . LEU A 595 ? 3.3293 2.8192 1.7123 -0.7512 -0.5014 -0.0037 595 LEU A C 4002 O O . LEU A 595 ? 3.3053 2.8084 1.6368 -0.7371 -0.4965 0.0093 595 LEU A O 4003 C CB . LEU A 595 ? 3.2472 2.6550 1.7047 -0.6613 -0.3994 -0.0395 595 LEU A CB 4004 C CG . LEU A 595 ? 3.2299 2.5568 1.6789 -0.6688 -0.3764 -0.0805 595 LEU A CG 4005 C CD1 . LEU A 595 ? 3.3404 2.6055 1.6844 -0.7364 -0.4099 -0.1137 595 LEU A CD1 4006 C CD2 . LEU A 595 ? 3.0576 2.4434 1.6523 -0.6497 -0.3775 -0.0555 595 LEU A CD2 4007 N N . PRO A 596 ? 3.4970 2.9545 1.8242 -0.8132 -0.5390 -0.0262 596 PRO A N 4008 C CA . PRO A 596 ? 3.7439 3.1657 1.9285 -0.8693 -0.5736 -0.0448 596 PRO A CA 4009 C C . PRO A 596 ? 3.8550 3.1993 1.9153 -0.8423 -0.5272 -0.0755 596 PRO A C 4010 O O . PRO A 596 ? 3.7992 3.0461 1.8120 -0.8169 -0.4730 -0.1203 596 PRO A O 4011 C CB . PRO A 596 ? 3.8385 3.1837 1.9705 -0.9221 -0.5878 -0.0882 596 PRO A CB 4012 C CG . PRO A 596 ? 3.6988 3.1018 1.9833 -0.9112 -0.5941 -0.0635 596 PRO A CG 4013 C CD . PRO A 596 ? 3.4619 2.9250 1.8640 -0.8380 -0.5563 -0.0298 596 PRO A CD 4014 N N . ASN A 597 ? 4.0062 3.3967 2.0184 -0.8468 -0.5476 -0.0485 597 ASN A N 4015 C CA . ASN A 597 ? 4.1004 3.4481 2.0291 -0.8073 -0.4997 -0.0604 597 ASN A CA 4016 C C . ASN A 597 ? 4.1136 3.3400 1.9776 -0.7760 -0.4307 -0.1175 597 ASN A C 4017 O O . ASN A 597 ? 4.3566 3.4824 2.0900 -0.8092 -0.4226 -0.1684 597 ASN A O 4018 C CB . ASN A 597 ? 4.2307 3.5926 2.0386 -0.8430 -0.5327 -0.0499 597 ASN A CB 4019 C CG . ASN A 597 ? 4.4786 3.7986 2.1697 -0.9226 -0.5836 -0.0791 597 ASN A CG 4020 O OD1 . ASN A 597 ? 4.7287 3.9552 2.3618 -0.9470 -0.5711 -0.1308 597 ASN A OD1 4021 N ND2 . ASN A 597 ? 4.4061 3.7938 2.0585 -0.9648 -0.6419 -0.0451 597 ASN A ND2 4022 N N . PRO A 598 ? 3.8735 3.1108 1.8341 -0.7118 -0.3813 -0.1074 598 PRO A N 4023 C CA . PRO A 598 ? 3.7965 2.9534 1.7694 -0.6726 -0.3211 -0.1441 598 PRO A CA 4024 C C . PRO A 598 ? 3.8829 2.9143 1.7108 -0.6664 -0.2701 -0.1993 598 PRO A C 4025 O O . PRO A 598 ? 3.8208 2.8156 1.6636 -0.6114 -0.2098 -0.2096 598 PRO A O 4026 C CB . PRO A 598 ? 3.7004 2.9237 1.7954 -0.6067 -0.2888 -0.1062 598 PRO A CB 4027 C CG . PRO A 598 ? 3.5801 2.9226 1.7664 -0.6189 -0.3416 -0.0501 598 PRO A CG 4028 C CD . PRO A 598 ? 3.7103 3.0540 1.7835 -0.6720 -0.3854 -0.0501 598 PRO A CD 4029 N N . ALA A 599 ? 3.9952 2.9603 1.6869 -0.7221 -0.2931 -0.2346 599 ALA A N 4030 C CA . ALA A 599 ? 4.1509 2.9876 1.6956 -0.7192 -0.2436 -0.2909 599 ALA A CA 4031 C C . ALA A 599 ? 4.1921 2.9416 1.7617 -0.6950 -0.1964 -0.3279 599 ALA A C 4032 O O . ALA A 599 ? 4.1064 2.8398 1.7194 -0.6332 -0.1378 -0.3272 599 ALA A O 4033 C CB . ALA A 599 ? 4.2012 2.9835 1.5897 -0.7895 -0.2822 -0.3222 599 ALA A CB 4034 N N . GLY A 600 ? 4.3115 3.0105 1.8599 -0.7440 -0.2236 -0.3559 600 GLY A N 4035 C CA . GLY A 600 ? 4.2823 2.8927 1.8474 -0.7296 -0.1846 -0.3908 600 GLY A CA 4036 C C . GLY A 600 ? 4.1301 2.8026 1.8572 -0.6748 -0.1620 -0.3579 600 GLY A C 4037 O O . GLY A 600 ? 3.9234 2.6418 1.7496 -0.6918 -0.1936 -0.3403 600 GLY A O 4038 N N . VAL A 601 ? 4.2006 2.8732 1.9500 -0.6101 -0.1062 -0.3501 601 VAL A N 4039 C CA . VAL A 601 ? 4.0695 2.8106 1.9659 -0.5535 -0.0832 -0.3148 601 VAL A CA 4040 C C . VAL A 601 ? 3.9714 2.6598 1.9256 -0.5380 -0.0563 -0.3324 601 VAL A C 4041 O O . VAL A 601 ? 3.8005 2.5240 1.8287 -0.5651 -0.0927 -0.3208 601 VAL A O 4042 C CB . VAL A 601 ? 4.0928 2.8615 1.9970 -0.4938 -0.0376 -0.2957 601 VAL A CB 4043 C CG1 . VAL A 601 ? 3.9393 2.8209 1.8884 -0.4977 -0.0770 -0.2487 601 VAL A CG1 4044 C CG2 . VAL A 601 ? 4.1573 2.8251 1.9163 -0.4851 0.0093 -0.3351 601 VAL A CG2 4045 N N . GLN A 602 ? 4.0368 2.6425 1.9566 -0.4956 0.0071 -0.3581 602 GLN A N 4046 C CA . GLN A 602 ? 4.0305 2.5872 2.0074 -0.4712 0.0399 -0.3698 602 GLN A CA 4047 C C . GLN A 602 ? 3.8844 2.5374 2.0197 -0.4384 0.0338 -0.3272 602 GLN A C 4048 O O . GLN A 602 ? 3.6536 2.3507 1.8582 -0.4680 -0.0069 -0.3130 602 GLN A O 4049 C CB . GLN A 602 ? 4.1213 2.5950 2.0448 -0.5244 0.0200 -0.4054 602 GLN A CB 4050 C CG . GLN A 602 ? 4.3635 2.7140 2.1240 -0.5531 0.0378 -0.4571 602 GLN A CG 4051 C CD . GLN A 602 ? 4.5875 2.9489 2.2717 -0.6259 -0.0249 -0.4660 602 GLN A CD 4052 O OE1 . GLN A 602 ? 4.6605 3.0435 2.3821 -0.6740 -0.0732 -0.4615 602 GLN A OE1 4053 N NE2 . GLN A 602 ? 4.7465 3.0961 2.3239 -0.6355 -0.0251 -0.4766 602 GLN A NE2 4054 N N . LEU A 603 ? 3.9962 2.6801 2.1849 -0.3786 0.0752 -0.3073 603 LEU A N 4055 C CA . LEU A 603 ? 4.0676 2.8257 2.3951 -0.3405 0.0812 -0.2727 603 LEU A CA 4056 C C . LEU A 603 ? 4.1732 2.8772 2.5307 -0.3431 0.0932 -0.2882 603 LEU A C 4057 O O . LEU A 603 ? 4.2610 3.0164 2.7033 -0.3588 0.0622 -0.2699 603 LEU A O 4058 C CB . LEU A 603 ? 4.1119 2.8885 2.4698 -0.2781 0.1308 -0.2567 603 LEU A CB 4059 C CG . LEU A 603 ? 4.0150 2.8508 2.4963 -0.2278 0.1532 -0.2257 603 LEU A CG 4060 C CD1 . LEU A 603 ? 3.8420 2.6238 2.3558 -0.2095 0.1824 -0.2378 603 LEU A CD1 4061 C CD2 . LEU A 603 ? 3.7721 2.7217 2.3605 -0.2319 0.1118 -0.1863 603 LEU A CD2 4062 N N . GLU A 604 ? 4.2439 2.8437 2.5328 -0.3254 0.1410 -0.3203 604 GLU A N 4063 C CA . GLU A 604 ? 4.2162 2.7444 2.5120 -0.3325 0.1546 -0.3396 604 GLU A CA 4064 C C . GLU A 604 ? 4.0631 2.5574 2.3040 -0.4016 0.1077 -0.3615 604 GLU A C 4065 O O . GLU A 604 ? 4.0955 2.5557 2.2342 -0.4373 0.0906 -0.3839 604 GLU A O 4066 C CB . GLU A 604 ? 4.4285 2.8490 2.6605 -0.2953 0.2195 -0.3675 604 GLU A CB 4067 C CG . GLU A 604 ? 4.8403 3.1508 2.9232 -0.3211 0.2351 -0.4133 604 GLU A CG 4068 C CD . GLU A 604 ? 4.9708 3.3097 2.9882 -0.3179 0.2347 -0.4119 604 GLU A CD 4069 O OE1 . GLU A 604 ? 4.9770 3.3926 3.0571 -0.2746 0.2498 -0.3796 604 GLU A OE1 4070 O OE2 . GLU A 604 ? 5.0475 3.3311 2.9484 -0.3606 0.2190 -0.4428 604 GLU A OE2 4071 N N . ASP A 605 ? 3.8142 2.3281 2.1285 -0.4213 0.0843 -0.3512 605 ASP A N 4072 C CA . ASP A 605 ? 3.7629 2.2515 2.0466 -0.4871 0.0396 -0.3668 605 ASP A CA 4073 C C . ASP A 605 ? 3.6128 2.1425 2.0073 -0.4893 0.0265 -0.3440 605 ASP A C 4074 O O . ASP A 605 ? 3.1508 1.7893 1.6497 -0.4746 0.0062 -0.3055 605 ASP A O 4075 C CB . ASP A 605 ? 3.8051 2.3647 2.0695 -0.5328 -0.0182 -0.3549 605 ASP A CB 4076 C CG . ASP A 605 ? 3.8515 2.3951 2.0956 -0.6038 -0.0684 -0.3664 605 ASP A CG 4077 O OD1 . ASP A 605 ? 3.9780 2.4180 2.1108 -0.6413 -0.0666 -0.4075 605 ASP A OD1 4078 O OD2 . ASP A 605 ? 3.7330 2.3665 2.0729 -0.6229 -0.1088 -0.3343 605 ASP A OD2 4079 N N . PRO A 606 ? 3.8972 2.3367 2.2671 -0.5073 0.0401 -0.3678 606 PRO A N 4080 C CA . PRO A 606 ? 3.9467 2.4152 2.4107 -0.5165 0.0273 -0.3482 606 PRO A CA 4081 C C . PRO A 606 ? 3.7954 2.3970 2.3596 -0.5346 -0.0234 -0.3082 606 PRO A C 4082 O O . PRO A 606 ? 3.5828 2.2690 2.2333 -0.4919 -0.0152 -0.2761 606 PRO A O 4083 C CB . PRO A 606 ? 4.1485 2.5084 2.5358 -0.5706 0.0189 -0.3844 606 PRO A CB 4084 C CG . PRO A 606 ? 4.0957 2.3410 2.3525 -0.5635 0.0550 -0.4272 606 PRO A CG 4085 C CD . PRO A 606 ? 4.0584 2.3572 2.3066 -0.5196 0.0716 -0.4152 606 PRO A CD 4086 N N . GLU A 607 ? 3.8910 2.5104 2.4424 -0.5967 -0.0740 -0.3098 607 GLU A N 4087 C CA . GLU A 607 ? 3.7033 2.4430 2.3549 -0.6164 -0.1202 -0.2709 607 GLU A CA 4088 C C . GLU A 607 ? 3.5806 2.4228 2.2705 -0.5915 -0.1349 -0.2419 607 GLU A C 4089 O O . GLU A 607 ? 3.6365 2.5682 2.4322 -0.5628 -0.1365 -0.2070 607 GLU A O 4090 C CB . GLU A 607 ? 3.7349 2.4705 2.3668 -0.6911 -0.1716 -0.2769 607 GLU A CB 4091 C CG . GLU A 607 ? 3.9184 2.6884 2.4925 -0.7355 -0.2194 -0.2780 607 GLU A CG 4092 C CD . GLU A 607 ? 4.1366 2.7941 2.5600 -0.7628 -0.2125 -0.3251 607 GLU A CD 4093 O OE1 . GLU A 607 ? 4.2980 2.8456 2.6594 -0.7842 -0.1950 -0.3601 607 GLU A OE1 4094 O OE2 . GLU A 607 ? 4.1047 2.7808 2.4679 -0.7643 -0.2243 -0.3274 607 GLU A OE2 4095 N N . PHE A 608 ? 3.4361 2.2627 2.0396 -0.6015 -0.1433 -0.2559 608 PHE A N 4096 C CA . PHE A 608 ? 3.2784 2.2009 1.9153 -0.5840 -0.1613 -0.2261 608 PHE A CA 4097 C C . PHE A 608 ? 3.1478 2.1247 1.8751 -0.5201 -0.1280 -0.2002 608 PHE A C 4098 O O . PHE A 608 ? 3.0264 2.1033 1.8458 -0.5099 -0.1488 -0.1641 608 PHE A O 4099 C CB . PHE A 608 ? 3.4584 2.3399 1.9799 -0.5895 -0.1582 -0.2472 608 PHE A CB 4100 C CG . PHE A 608 ? 3.3583 2.3125 1.9095 -0.5472 -0.1498 -0.2201 608 PHE A CG 4101 C CD1 . PHE A 608 ? 3.2006 2.2547 1.7951 -0.5641 -0.1947 -0.1859 608 PHE A CD1 4102 C CD2 . PHE A 608 ? 3.2366 2.1588 1.7734 -0.4911 -0.0966 -0.2269 608 PHE A CD2 4103 C CE1 . PHE A 608 ? 2.9043 2.0192 1.5253 -0.5267 -0.1862 -0.1605 608 PHE A CE1 4104 C CE2 . PHE A 608 ? 2.9167 1.9035 1.4811 -0.4557 -0.0894 -0.2015 608 PHE A CE2 4105 C CZ . PHE A 608 ? 2.8327 1.9129 1.4375 -0.4741 -0.1341 -0.1692 608 PHE A CZ 4106 N N . GLN A 609 ? 3.1291 2.0391 1.8304 -0.4781 -0.0762 -0.2182 609 GLN A N 4107 C CA . GLN A 609 ? 3.1049 2.0608 1.8812 -0.4186 -0.0436 -0.1957 609 GLN A CA 4108 C C . GLN A 609 ? 3.0352 2.0799 1.9364 -0.4102 -0.0597 -0.1614 609 GLN A C 4109 O O . GLN A 609 ? 2.8299 1.9497 1.7990 -0.3772 -0.0569 -0.1343 609 GLN A O 4110 C CB . GLN A 609 ? 3.1671 2.0369 1.9071 -0.3803 0.0117 -0.2176 609 GLN A CB 4111 C CG . GLN A 609 ? 3.3211 2.1358 1.9638 -0.3640 0.0392 -0.2390 609 GLN A CG 4112 C CD . GLN A 609 ? 3.5252 2.3112 2.1795 -0.3045 0.0953 -0.2387 609 GLN A CD 4113 O OE1 . GLN A 609 ? 3.7066 2.4365 2.3704 -0.2887 0.1246 -0.2484 609 GLN A OE1 4114 N NE2 . GLN A 609 ? 3.4475 2.2736 2.1036 -0.2715 0.1103 -0.2249 609 GLN A NE2 4115 N N . ALA A 610 ? 3.0751 2.1091 2.0033 -0.4420 -0.0763 -0.1631 610 ALA A N 4116 C CA . ALA A 610 ? 2.9754 2.0916 2.0144 -0.4415 -0.0937 -0.1319 610 ALA A CA 4117 C C . ALA A 610 ? 2.9850 2.2062 2.0808 -0.4485 -0.1305 -0.1005 610 ALA A C 4118 O O . ALA A 610 ? 2.9272 2.2195 2.1111 -0.4182 -0.1254 -0.0735 610 ALA A O 4119 C CB . ALA A 610 ? 2.8972 1.9831 1.9446 -0.4833 -0.1095 -0.1389 610 ALA A CB 4120 N N . SER A 611 ? 3.0699 2.2975 2.1124 -0.4875 -0.1659 -0.1038 611 SER A N 4121 C CA . SER A 611 ? 3.0417 2.3673 2.1337 -0.5004 -0.2059 -0.0712 611 SER A CA 4122 C C . SER A 611 ? 2.9520 2.3431 2.1029 -0.4515 -0.1910 -0.0455 611 SER A C 4123 O O . SER A 611 ? 2.8036 2.2802 2.0191 -0.4534 -0.2178 -0.0134 611 SER A O 4124 C CB . SER A 611 ? 3.0713 2.3800 2.0730 -0.5440 -0.2400 -0.0820 611 SER A CB 4125 O OG . SER A 611 ? 2.8775 2.2777 1.9201 -0.5477 -0.2732 -0.0480 611 SER A OG 4126 N N . ASN A 612 ? 2.8739 2.2229 2.0037 -0.4084 -0.1477 -0.0587 612 ASN A N 4127 C CA . ASN A 612 ? 2.8135 2.2037 1.9699 -0.3663 -0.1312 -0.0417 612 ASN A CA 4128 C C . ASN A 612 ? 2.7406 2.1381 1.9626 -0.3222 -0.0959 -0.0359 612 ASN A C 4129 O O . ASN A 612 ? 2.8415 2.2646 2.0893 -0.2843 -0.0761 -0.0244 612 ASN A O 4130 C CB . ASN A 612 ? 2.8473 2.1799 1.9031 -0.3592 -0.1135 -0.0626 612 ASN A CB 4131 C CG . ASN A 612 ? 2.9229 2.2047 1.8818 -0.4087 -0.1384 -0.0855 612 ASN A CG 4132 O OD1 . ASN A 612 ? 2.8986 2.2257 1.8518 -0.4417 -0.1797 -0.0708 612 ASN A OD1 4133 N ND2 . ASN A 612 ? 2.9996 2.1858 1.8821 -0.4153 -0.1141 -0.1210 612 ASN A ND2 4134 N N . ILE A 613 ? 2.6379 2.0130 1.8859 -0.3294 -0.0891 -0.0429 613 ILE A N 4135 C CA . ILE A 613 ? 2.4559 1.8423 1.7661 -0.2923 -0.0599 -0.0353 613 ILE A CA 4136 C C . ILE A 613 ? 2.3718 1.8327 1.7747 -0.2997 -0.0805 -0.0100 613 ILE A C 4137 O O . ILE A 613 ? 2.4109 1.8682 1.8336 -0.3259 -0.0920 -0.0104 613 ILE A O 4138 C CB . ILE A 613 ? 2.4629 1.7703 1.7374 -0.2894 -0.0322 -0.0582 613 ILE A CB 4139 C CG1 . ILE A 613 ? 2.5791 1.8072 1.7546 -0.2857 -0.0118 -0.0850 613 ILE A CG1 4140 C CG2 . ILE A 613 ? 2.2976 1.6225 1.6341 -0.2495 -0.0032 -0.0469 613 ILE A CG2 4141 C CD1 . ILE A 613 ? 2.7948 1.9318 1.9079 -0.3088 -0.0017 -0.1130 613 ILE A CD1 4142 N N . MET A 614 ? 2.2209 1.7484 1.6805 -0.2766 -0.0836 0.0128 614 MET A N 4143 C CA . MET A 614 ? 2.2326 1.8335 1.7796 -0.2803 -0.1010 0.0382 614 MET A CA 4144 C C . MET A 614 ? 2.3371 1.9483 1.9410 -0.2509 -0.0741 0.0424 614 MET A C 4145 O O . MET A 614 ? 2.4108 2.0241 2.0249 -0.2154 -0.0507 0.0434 614 MET A O 4146 C CB . MET A 614 ? 2.1435 1.8068 1.7225 -0.2715 -0.1179 0.0614 614 MET A CB 4147 C CG . MET A 614 ? 2.2317 1.8955 1.7581 -0.3040 -0.1495 0.0626 614 MET A CG 4148 S SD . MET A 614 ? 2.3356 2.0046 1.8620 -0.3586 -0.1858 0.0632 614 MET A SD 4149 C CE . MET A 614 ? 2.3500 1.9922 1.7782 -0.3956 -0.2163 0.0532 614 MET A CE 4150 N N . HIS A 615 ? 2.3186 1.9374 1.9580 -0.2679 -0.0784 0.0459 615 HIS A N 4151 C CA . HIS A 615 ? 2.1733 1.8034 1.8634 -0.2449 -0.0549 0.0509 615 HIS A CA 4152 C C . HIS A 615 ? 2.0095 1.7184 1.7814 -0.2371 -0.0646 0.0760 615 HIS A C 4153 O O . HIS A 615 ? 2.0130 1.7606 1.8177 -0.2632 -0.0891 0.0902 615 HIS A O 4154 C CB . HIS A 615 ? 2.2381 1.8299 1.9182 -0.2681 -0.0519 0.0423 615 HIS A CB 4155 C CG . HIS A 615 ? 2.4092 1.9162 2.0074 -0.2775 -0.0418 0.0169 615 HIS A CG 4156 N ND1 . HIS A 615 ? 2.4774 1.9501 2.0117 -0.3060 -0.0610 0.0030 615 HIS A ND1 4157 C CD2 . HIS A 615 ? 2.4718 1.9191 2.0404 -0.2615 -0.0130 0.0033 615 HIS A CD2 4158 C CE1 . HIS A 615 ? 2.5540 1.9452 2.0211 -0.3062 -0.0419 -0.0206 615 HIS A CE1 4159 N NE2 . HIS A 615 ? 2.5172 1.8925 2.0071 -0.2782 -0.0124 -0.0194 615 HIS A NE2 4160 N N . SER A 616 ? 1.8921 1.6246 1.6971 -0.2020 -0.0457 0.0821 616 SER A N 4161 C CA . SER A 616 ? 1.8555 1.6553 1.7287 -0.1910 -0.0534 0.1040 616 SER A CA 4162 C C . SER A 616 ? 1.9480 1.7702 1.8696 -0.1602 -0.0291 0.1085 616 SER A C 4163 O O . SER A 616 ? 2.2413 2.0348 2.1404 -0.1380 -0.0078 0.0971 616 SER A O 4164 C CB . SER A 616 ? 1.7276 1.5418 1.5866 -0.1840 -0.0655 0.1106 616 SER A CB 4165 O OG . SER A 616 ? 1.5349 1.3407 1.3914 -0.1510 -0.0436 0.1065 616 SER A OG 4166 N N . ILE A 617 ? 1.8516 1.7263 1.8396 -0.1595 -0.0326 0.1261 617 ILE A N 4167 C CA . ILE A 617 ? 1.6551 1.5562 1.6891 -0.1305 -0.0123 0.1312 617 ILE A CA 4168 C C . ILE A 617 ? 1.6111 1.5428 1.6686 -0.1190 -0.0223 0.1442 617 ILE A C 4169 O O . ILE A 617 ? 1.5868 1.5554 1.6747 -0.1323 -0.0431 0.1624 617 ILE A O 4170 C CB . ILE A 617 ? 1.5650 1.5030 1.6585 -0.1314 -0.0033 0.1426 617 ILE A CB 4171 C CG1 . ILE A 617 ? 1.5850 1.5199 1.6768 -0.1620 -0.0139 0.1454 617 ILE A CG1 4172 C CG2 . ILE A 617 ? 1.4523 1.3807 1.5515 -0.1071 0.0258 0.1333 617 ILE A CG2 4173 C CD1 . ILE A 617 ? 1.6135 1.5026 1.6682 -0.1644 0.0030 0.1302 617 ILE A CD1 4174 N N . ASN A 618 ? 1.6283 1.5449 1.6719 -0.0954 -0.0086 0.1371 618 ASN A N 4175 C CA . ASN A 618 ? 1.6106 1.5511 1.6774 -0.0821 -0.0142 0.1498 618 ASN A CA 4176 C C . ASN A 618 ? 1.5921 1.5394 1.6365 -0.0993 -0.0405 0.1605 618 ASN A C 4177 O O . ASN A 618 ? 1.5574 1.5420 1.6395 -0.0976 -0.0535 0.1812 618 ASN A O 4178 C CB . ASN A 618 ? 1.5341 1.5175 1.6729 -0.0695 -0.0071 0.1648 618 ASN A CB 4179 C CG . ASN A 618 ? 1.4955 1.4673 1.6452 -0.0468 0.0201 0.1525 618 ASN A CG 4180 O OD1 . ASN A 618 ? 1.3315 1.2709 1.4430 -0.0441 0.0324 0.1353 618 ASN A OD1 4181 N ND2 . ASN A 618 ? 1.6124 1.6097 1.8132 -0.0304 0.0297 0.1619 618 ASN A ND2 4182 N N . GLY A 619 ? 1.6555 1.5643 1.6356 -0.1157 -0.0472 0.1466 619 GLY A N 4183 C CA . GLY A 619 ? 1.7462 1.6546 1.6900 -0.1356 -0.0719 0.1529 619 GLY A CA 4184 C C . GLY A 619 ? 1.8419 1.7866 1.8129 -0.1641 -0.0995 0.1692 619 GLY A C 4185 O O . GLY A 619 ? 1.9300 1.8819 1.8735 -0.1842 -0.1248 0.1776 619 GLY A O 4186 N N . TYR A 620 ? 1.7714 1.7417 1.7960 -0.1668 -0.0951 0.1755 620 TYR A N 4187 C CA . TYR A 620 ? 1.7308 1.7397 1.7885 -0.1959 -0.1202 0.1930 620 TYR A CA 4188 C C . TYR A 620 ? 1.7479 1.7230 1.7727 -0.2219 -0.1215 0.1764 620 TYR A C 4189 O O . TYR A 620 ? 1.7247 1.6676 1.7393 -0.2103 -0.0966 0.1598 620 TYR A O 4190 C CB . TYR A 620 ? 1.7058 1.7710 1.8530 -0.1817 -0.1126 0.2153 620 TYR A CB 4191 C CG . TYR A 620 ? 1.7850 1.8931 1.9798 -0.1628 -0.1178 0.2397 620 TYR A CG 4192 C CD1 . TYR A 620 ? 1.7875 1.8758 1.9674 -0.1356 -0.1025 0.2334 620 TYR A CD1 4193 C CD2 . TYR A 620 ? 1.9380 2.1082 2.1982 -0.1719 -0.1375 0.2720 620 TYR A CD2 4194 C CE1 . TYR A 620 ? 1.8426 1.9660 2.0681 -0.1184 -0.1062 0.2573 620 TYR A CE1 4195 C CE2 . TYR A 620 ? 1.9716 2.1799 2.2805 -0.1519 -0.1404 0.2976 620 TYR A CE2 4196 C CZ . TYR A 620 ? 1.8342 2.0157 2.1233 -0.1256 -0.1244 0.2892 620 TYR A CZ 4197 O OH . TYR A 620 ? 1.9692 2.1834 2.3063 -0.1065 -0.1267 0.3154 620 TYR A OH 4198 N N . VAL A 621 ? 1.8207 1.8029 1.8285 -0.2589 -0.1515 0.1822 621 VAL A N 4199 C CA . VAL A 621 ? 1.9408 1.8864 1.9174 -0.2873 -0.1539 0.1667 621 VAL A CA 4200 C C . VAL A 621 ? 1.9775 1.9796 2.0209 -0.3117 -0.1724 0.1908 621 VAL A C 4201 O O . VAL A 621 ? 1.8582 1.9266 1.9669 -0.3063 -0.1849 0.2196 621 VAL A O 4202 C CB . VAL A 621 ? 2.0110 1.8992 1.8954 -0.3169 -0.1715 0.1457 621 VAL A CB 4203 C CG1 . VAL A 621 ? 1.8369 1.6607 1.6540 -0.2920 -0.1454 0.1196 621 VAL A CG1 4204 C CG2 . VAL A 621 ? 2.0166 1.9397 1.8919 -0.3417 -0.2093 0.1627 621 VAL A CG2 4205 N N . PHE A 622 ? 1.9795 1.9547 2.0096 -0.3370 -0.1720 0.1807 622 PHE A N 4206 C CA . PHE A 622 ? 2.0119 2.0319 2.0917 -0.3716 -0.1945 0.2014 622 PHE A CA 4207 C C . PHE A 622 ? 2.0442 2.1478 2.2255 -0.3545 -0.1914 0.2353 622 PHE A C 4208 O O . PHE A 622 ? 2.0070 2.1679 2.2276 -0.3622 -0.2170 0.2616 622 PHE A O 4209 C CB . PHE A 622 ? 1.9801 2.0008 2.0201 -0.4157 -0.2372 0.2044 622 PHE A CB 4210 C CG . PHE A 622 ? 2.0273 1.9701 1.9837 -0.4484 -0.2425 0.1744 622 PHE A CG 4211 C CD1 . PHE A 622 ? 2.0710 2.0064 2.0423 -0.4816 -0.2485 0.1750 622 PHE A CD1 4212 C CD2 . PHE A 622 ? 2.0769 1.9507 1.9404 -0.4449 -0.2385 0.1458 622 PHE A CD2 4213 C CE1 . PHE A 622 ? 2.1224 1.9776 2.0157 -0.5115 -0.2512 0.1463 622 PHE A CE1 4214 C CE2 . PHE A 622 ? 2.1543 1.9487 1.9386 -0.4728 -0.2393 0.1165 622 PHE A CE2 4215 C CZ . PHE A 622 ? 2.1806 1.9631 1.9791 -0.5062 -0.2458 0.1160 622 PHE A CZ 4216 N N . ASP A 623 ? 2.1124 2.2216 2.3344 -0.3302 -0.1583 0.2352 623 ASP A N 4217 C CA . ASP A 623 ? 2.0759 2.2576 2.3931 -0.3129 -0.1476 0.2646 623 ASP A CA 4218 C C . ASP A 623 ? 2.0141 2.2503 2.3728 -0.3005 -0.1649 0.2895 623 ASP A C 4219 O O . ASP A 623 ? 2.1385 2.4449 2.5744 -0.3057 -0.1767 0.3227 623 ASP A O 4220 C CB . ASP A 623 ? 2.3108 2.5284 2.6761 -0.3462 -0.1582 0.2832 623 ASP A CB 4221 C CG . ASP A 623 ? 2.5580 2.7398 2.9143 -0.3424 -0.1270 0.2683 623 ASP A CG 4222 O OD1 . ASP A 623 ? 2.7202 2.8799 3.0681 -0.3053 -0.0930 0.2548 623 ASP A OD1 4223 O OD2 . ASP A 623 ? 2.6997 2.8766 3.0579 -0.3776 -0.1371 0.2718 623 ASP A OD2 4224 N N . SER A 624 ? 1.9048 2.1089 2.2127 -0.2846 -0.1666 0.2759 624 SER A N 4225 C CA . SER A 624 ? 1.8151 2.0624 2.1604 -0.2652 -0.1754 0.2985 624 SER A CA 4226 C C . SER A 624 ? 1.8377 2.0538 2.1729 -0.2223 -0.1401 0.2815 624 SER A C 4227 O O . SER A 624 ? 1.8979 2.0523 2.1677 -0.2169 -0.1245 0.2509 624 SER A O 4228 C CB . SER A 624 ? 1.9091 2.1458 2.1985 -0.2879 -0.2104 0.2992 624 SER A CB 4229 O OG . SER A 624 ? 1.9901 2.2861 2.3342 -0.2760 -0.2251 0.3326 624 SER A OG 4230 N N . LEU A 625 ? 1.8255 2.0841 2.2262 -0.1929 -0.1285 0.3026 625 LEU A N 4231 C CA . LEU A 625 ? 1.7817 2.0252 2.2012 -0.1528 -0.0898 0.2913 625 LEU A CA 4232 C C . LEU A 625 ? 1.8601 2.1261 2.3314 -0.1470 -0.0656 0.2954 625 LEU A C 4233 O O . LEU A 625 ? 1.9270 2.1699 2.3714 -0.1638 -0.0603 0.2808 625 LEU A O 4234 C CB . LEU A 625 ? 1.7014 1.8758 2.0440 -0.1407 -0.0729 0.2563 625 LEU A CB 4235 C CG . LEU A 625 ? 1.4506 1.5920 1.7828 -0.1185 -0.0364 0.2332 625 LEU A CG 4236 C CD1 . LEU A 625 ? 1.4040 1.5729 1.7984 -0.0873 -0.0108 0.2427 625 LEU A CD1 4237 C CD2 . LEU A 625 ? 1.3241 1.4065 1.5834 -0.1100 -0.0284 0.2058 625 LEU A CD2 4238 N N . GLN A 626 ? 1.8717 2.1823 2.4181 -0.1224 -0.0495 0.3169 626 GLN A N 4239 C CA . GLN A 626 ? 1.8271 2.1558 2.4208 -0.1082 -0.0178 0.3191 626 GLN A CA 4240 C C . GLN A 626 ? 1.7580 2.0699 2.3635 -0.0681 0.0150 0.3091 626 GLN A C 4241 O O . GLN A 626 ? 1.7991 2.1053 2.4030 -0.0538 0.0085 0.3129 626 GLN A O 4242 C CB . GLN A 626 ? 1.9389 2.3425 2.6213 -0.1162 -0.0264 0.3580 626 GLN A CB 4243 C CG . GLN A 626 ? 2.0262 2.4534 2.7071 -0.1603 -0.0595 0.3707 626 GLN A CG 4244 C CD . GLN A 626 ? 2.3489 2.8601 3.1234 -0.1686 -0.0760 0.4161 626 GLN A CD 4245 O OE1 . GLN A 626 ? 2.4567 3.0094 3.2963 -0.1637 -0.0560 0.4334 626 GLN A OE1 4246 N NE2 . GLN A 626 ? 2.4384 2.9785 3.2215 -0.1814 -0.1126 0.4381 626 GLN A NE2 4247 N N . LEU A 627 ? 1.6633 1.9654 2.2780 -0.0517 0.0501 0.2963 627 LEU A N 4248 C CA . LEU A 627 ? 1.5918 1.8768 2.2179 -0.0165 0.0832 0.2852 627 LEU A CA 4249 C C . LEU A 627 ? 1.6556 1.9828 2.3553 0.0009 0.1127 0.3029 627 LEU A C 4250 O O . LEU A 627 ? 1.5604 1.9066 2.2737 -0.0112 0.1216 0.3070 627 LEU A O 4251 C CB . LEU A 627 ? 1.5330 1.7595 2.0876 -0.0123 0.1012 0.2488 627 LEU A CB 4252 C CG . LEU A 627 ? 1.5146 1.7002 1.9943 -0.0337 0.0772 0.2311 627 LEU A CG 4253 C CD1 . LEU A 627 ? 1.5102 1.6691 1.9483 -0.0450 0.0891 0.2130 627 LEU A CD1 4254 C CD2 . LEU A 627 ? 1.4880 1.6352 1.9282 -0.0183 0.0776 0.2145 627 LEU A CD2 4255 N N . SER A 628 ? 1.7613 2.1028 2.5108 0.0298 0.1297 0.3149 628 SER A N 4256 C CA . SER A 628 ? 1.9134 2.2808 2.7227 0.0537 0.1685 0.3242 628 SER A CA 4257 C C . SER A 628 ? 1.8899 2.2023 2.6548 0.0765 0.2065 0.2884 628 SER A C 4258 O O . SER A 628 ? 1.8645 2.1302 2.5830 0.0840 0.2037 0.2667 628 SER A O 4259 C CB . SER A 628 ? 2.0152 2.4330 2.9142 0.0743 0.1710 0.3613 628 SER A CB 4260 O OG . SER A 628 ? 1.8647 2.3491 2.8380 0.0686 0.1738 0.3947 628 SER A OG 4261 N N . VAL A 629 ? 1.6246 1.9441 2.4009 0.0844 0.2403 0.2830 629 VAL A N 4262 C CA . VAL A 629 ? 1.5092 1.7879 2.2588 0.1092 0.2822 0.2548 629 VAL A CA 4263 C C . VAL A 629 ? 1.5233 1.8356 2.3323 0.1294 0.3233 0.2684 629 VAL A C 4264 O O . VAL A 629 ? 1.4753 1.8394 2.3302 0.1179 0.3210 0.2943 629 VAL A O 4265 C CB . VAL A 629 ? 1.4720 1.7056 2.1372 0.0955 0.2863 0.2214 629 VAL A CB 4266 C CG1 . VAL A 629 ? 1.4196 1.5964 2.0204 0.0978 0.2762 0.1929 629 VAL A CG1 4267 C CG2 . VAL A 629 ? 1.4281 1.6822 2.0797 0.0641 0.2617 0.2317 629 VAL A CG2 4268 N N . CYS A 630 ? 1.5776 1.8577 2.3830 0.1588 0.3619 0.2499 630 CYS A N 4269 C CA . CYS A 630 ? 1.6901 1.9891 2.5391 0.1830 0.4102 0.2556 630 CYS A CA 4270 C C . CYS A 630 ? 1.4976 1.7838 2.2940 0.1724 0.4312 0.2354 630 CYS A C 4271 O O . CYS A 630 ? 1.5655 1.7981 2.2812 0.1670 0.4339 0.2005 630 CYS A O 4272 C CB . CYS A 630 ? 2.1464 2.4014 2.9957 0.2165 0.4453 0.2367 630 CYS A CB 4273 S SG . CYS A 630 ? 2.8237 3.0898 3.7434 0.2369 0.4313 0.2638 630 CYS A SG 4274 N N . LEU A 631 ? 1.3881 1.7257 2.2306 0.1684 0.4455 0.2595 631 LEU A N 4275 C CA . LEU A 631 ? 1.4639 1.7894 2.2569 0.1601 0.4690 0.2428 631 LEU A CA 4276 C C . LEU A 631 ? 1.5894 1.8676 2.3430 0.1879 0.5172 0.2109 631 LEU A C 4277 O O . LEU A 631 ? 1.5287 1.8107 2.3308 0.2184 0.5499 0.2160 631 LEU A O 4278 C CB . LEU A 631 ? 1.3837 1.7747 2.2384 0.1511 0.4791 0.2770 631 LEU A CB 4279 C CG . LEU A 631 ? 1.4423 1.8692 2.3679 0.1831 0.5302 0.2949 631 LEU A CG 4280 C CD1 . LEU A 631 ? 1.4609 1.8871 2.3564 0.1847 0.5715 0.2857 631 LEU A CD1 4281 C CD2 . LEU A 631 ? 1.4592 1.9651 2.4928 0.1801 0.5142 0.3447 631 LEU A CD2 4282 N N . HIS A 632 ? 1.7266 1.9586 2.3903 0.1761 0.5197 0.1783 632 HIS A N 4283 C CA . HIS A 632 ? 1.8064 1.9811 2.4059 0.1927 0.5538 0.1401 632 HIS A CA 4284 C C . HIS A 632 ? 1.8270 1.9456 2.3746 0.1900 0.5293 0.1123 632 HIS A C 4285 O O . HIS A 632 ? 1.8492 1.9196 2.3173 0.1847 0.5351 0.0792 632 HIS A O 4286 C CB . HIS A 632 ? 1.9099 2.0903 2.5543 0.2268 0.6086 0.1419 632 HIS A CB 4287 C CG . HIS A 632 ? 1.9286 2.1579 2.6096 0.2308 0.6415 0.1639 632 HIS A CG 4288 N ND1 . HIS A 632 ? 1.8960 2.1274 2.5232 0.2109 0.6446 0.1580 632 HIS A ND1 4289 C CD2 . HIS A 632 ? 1.9392 2.2190 2.7080 0.2530 0.6745 0.1942 632 HIS A CD2 4290 C CE1 . HIS A 632 ? 2.1852 2.4660 2.8646 0.2193 0.6777 0.1834 632 HIS A CE1 4291 N NE2 . HIS A 632 ? 2.2235 2.5360 2.9904 0.2450 0.6967 0.2057 632 HIS A NE2 4292 N N . GLU A 633 ? 1.9129 2.0402 2.5052 0.1922 0.5015 0.1275 633 GLU A N 4293 C CA . GLU A 633 ? 2.0425 2.1220 2.5895 0.1868 0.4753 0.1058 633 GLU A CA 4294 C C . GLU A 633 ? 1.9013 1.9655 2.3779 0.1580 0.4431 0.0930 633 GLU A C 4295 O O . GLU A 633 ? 1.8240 1.9205 2.3112 0.1385 0.4162 0.1129 633 GLU A O 4296 C CB . GLU A 633 ? 2.3461 2.4431 2.9518 0.1913 0.4477 0.1294 633 GLU A CB 4297 C CG . GLU A 633 ? 2.6402 2.6938 3.1997 0.1818 0.4174 0.1115 633 GLU A CG 4298 C CD . GLU A 633 ? 2.9576 3.0404 3.5415 0.1655 0.3714 0.1369 633 GLU A CD 4299 O OE1 . GLU A 633 ? 3.1053 3.2228 3.7596 0.1759 0.3659 0.1665 633 GLU A OE1 4300 O OE2 . GLU A 633 ? 2.9184 2.9899 3.4505 0.1425 0.3416 0.1284 633 GLU A OE2 4301 N N . VAL A 634 ? 1.7734 1.7867 2.1787 0.1553 0.4467 0.0599 634 VAL A N 4302 C CA . VAL A 634 ? 1.6733 1.6698 2.0093 0.1323 0.4232 0.0467 634 VAL A CA 4303 C C . VAL A 634 ? 1.6380 1.6100 1.9525 0.1228 0.3872 0.0400 634 VAL A C 4304 O O . VAL A 634 ? 1.6250 1.5713 1.9481 0.1346 0.3909 0.0298 634 VAL A O 4305 C CB . VAL A 634 ? 1.6777 1.6407 1.9467 0.1334 0.4510 0.0174 634 VAL A CB 4306 C CG1 . VAL A 634 ? 1.6489 1.5687 1.9069 0.1504 0.4739 -0.0081 634 VAL A CG1 4307 C CG2 . VAL A 634 ? 1.6805 1.6269 1.8803 0.1110 0.4244 0.0065 634 VAL A CG2 4308 N N . ALA A 635 ? 1.6097 1.5872 1.8958 0.1024 0.3554 0.0459 635 ALA A N 4309 C CA . ALA A 635 ? 1.5212 1.4884 1.7994 0.0929 0.3192 0.0487 635 ALA A CA 4310 C C . ALA A 635 ? 1.4609 1.4056 1.6736 0.0764 0.2990 0.0359 635 ALA A C 4311 O O . ALA A 635 ? 1.5324 1.4827 1.7162 0.0668 0.3021 0.0364 635 ALA A O 4312 C CB . ALA A 635 ? 1.4457 1.4503 1.7750 0.0867 0.2973 0.0780 635 ALA A CB 4313 N N . TYR A 636 ? 1.3520 1.2735 1.5449 0.0739 0.2799 0.0274 636 TYR A N 4314 C CA . TYR A 636 ? 1.3987 1.3091 1.5462 0.0596 0.2559 0.0248 636 TYR A CA 4315 C C . TYR A 636 ? 1.4486 1.3734 1.6176 0.0530 0.2294 0.0440 636 TYR A C 4316 O O . TYR A 636 ? 1.6695 1.5978 1.8707 0.0586 0.2206 0.0516 636 TYR A O 4317 C CB . TYR A 636 ? 1.3899 1.2710 1.5049 0.0587 0.2485 0.0074 636 TYR A CB 4318 C CG . TYR A 636 ? 1.6041 1.4630 1.6724 0.0561 0.2631 -0.0155 636 TYR A CG 4319 C CD1 . TYR A 636 ? 1.6567 1.5176 1.7108 0.0589 0.2891 -0.0237 636 TYR A CD1 4320 C CD2 . TYR A 636 ? 1.8205 1.6569 1.8571 0.0493 0.2503 -0.0287 636 TYR A CD2 4321 C CE1 . TYR A 636 ? 1.8165 1.6546 1.8197 0.0543 0.3011 -0.0464 636 TYR A CE1 4322 C CE2 . TYR A 636 ? 1.8926 1.7088 1.8831 0.0429 0.2595 -0.0502 636 TYR A CE2 4323 C CZ . TYR A 636 ? 1.8912 1.7068 1.8617 0.0451 0.2846 -0.0600 636 TYR A CZ 4324 O OH . TYR A 636 ? 1.8809 1.6748 1.7981 0.0365 0.2927 -0.0826 636 TYR A OH 4325 N N . TRP A 637 ? 1.3903 1.3196 1.5377 0.0408 0.2171 0.0515 637 TRP A N 4326 C CA . TRP A 637 ? 1.3644 1.2998 1.5202 0.0322 0.1932 0.0658 637 TRP A CA 4327 C C . TRP A 637 ? 1.4136 1.3275 1.5263 0.0264 0.1771 0.0613 637 TRP A C 4328 O O . TRP A 637 ? 1.4985 1.4034 1.5777 0.0209 0.1787 0.0588 637 TRP A O 4329 C CB . TRP A 637 ? 1.4618 1.4167 1.6326 0.0217 0.1927 0.0796 637 TRP A CB 4330 C CG . TRP A 637 ? 1.6447 1.6285 1.8677 0.0271 0.2050 0.0904 637 TRP A CG 4331 C CD1 . TRP A 637 ? 1.7498 1.7408 1.9901 0.0398 0.2320 0.0848 637 TRP A CD1 4332 C CD2 . TRP A 637 ? 1.7388 1.7508 2.0060 0.0202 0.1917 0.1105 637 TRP A CD2 4333 N NE1 . TRP A 637 ? 1.7618 1.7860 2.0609 0.0442 0.2388 0.1023 637 TRP A NE1 4334 C CE2 . TRP A 637 ? 1.6866 1.7271 2.0047 0.0310 0.2120 0.1196 637 TRP A CE2 4335 C CE3 . TRP A 637 ? 1.8614 1.8773 2.1283 0.0050 0.1645 0.1219 637 TRP A CE3 4336 C CZ2 . TRP A 637 ? 1.6756 1.7543 2.0502 0.0270 0.2040 0.1431 637 TRP A CZ2 4337 C CZ3 . TRP A 637 ? 1.8839 1.9348 2.2000 -0.0020 0.1544 0.1427 637 TRP A CZ3 4338 C CH2 . TRP A 637 ? 1.8001 1.8852 2.1729 0.0090 0.1728 0.1549 637 TRP A CH2 4339 N N . TYR A 638 ? 1.3044 1.2118 1.4207 0.0288 0.1628 0.0629 638 TYR A N 4340 C CA . TYR A 638 ? 1.2132 1.1033 1.2947 0.0259 0.1503 0.0609 638 TYR A CA 4341 C C . TYR A 638 ? 1.2704 1.1602 1.3473 0.0171 0.1359 0.0718 638 TYR A C 4342 O O . TYR A 638 ? 1.3442 1.2411 1.4394 0.0156 0.1244 0.0800 638 TYR A O 4343 C CB . TYR A 638 ? 1.1642 1.0476 1.2516 0.0325 0.1451 0.0577 638 TYR A CB 4344 C CG . TYR A 638 ? 1.3536 1.2339 1.4528 0.0393 0.1599 0.0460 638 TYR A CG 4345 C CD1 . TYR A 638 ? 1.5517 1.4197 1.6204 0.0378 0.1663 0.0323 638 TYR A CD1 4346 C CD2 . TYR A 638 ? 1.4057 1.2943 1.5457 0.0470 0.1682 0.0488 638 TYR A CD2 4347 C CE1 . TYR A 638 ? 1.6773 1.5357 1.7486 0.0415 0.1805 0.0176 638 TYR A CE1 4348 C CE2 . TYR A 638 ? 1.4481 1.3256 1.5956 0.0545 0.1859 0.0353 638 TYR A CE2 4349 C CZ . TYR A 638 ? 1.5369 1.3966 1.6463 0.0506 0.1921 0.0176 638 TYR A CZ 4350 O OH . TYR A 638 ? 1.5391 1.3809 1.6458 0.0550 0.2096 0.0002 638 TYR A OH 4351 N N . ILE A 639 ? 1.2972 1.1770 1.3476 0.0104 0.1370 0.0723 639 ILE A N 4352 C CA . ILE A 639 ? 1.2834 1.1534 1.3209 -0.0004 0.1258 0.0791 639 ILE A CA 4353 C C . ILE A 639 ? 1.3799 1.2249 1.3797 0.0029 0.1217 0.0767 639 ILE A C 4354 O O . ILE A 639 ? 1.4617 1.3011 1.4452 0.0105 0.1287 0.0730 639 ILE A O 4355 C CB . ILE A 639 ? 1.2397 1.1111 1.2762 -0.0104 0.1328 0.0828 639 ILE A CB 4356 C CG1 . ILE A 639 ? 1.1086 1.0090 1.1857 -0.0107 0.1421 0.0868 639 ILE A CG1 4357 C CG2 . ILE A 639 ? 1.2670 1.1214 1.2876 -0.0252 0.1211 0.0878 639 ILE A CG2 4358 C CD1 . ILE A 639 ? 1.1147 1.0178 1.1864 -0.0150 0.1569 0.0886 639 ILE A CD1 4359 N N . LEU A 640 ? 1.4128 1.2438 1.3981 -0.0032 0.1108 0.0796 640 LEU A N 4360 C CA . LEU A 640 ? 1.4266 1.2314 1.3763 0.0017 0.1110 0.0782 640 LEU A CA 4361 C C . LEU A 640 ? 1.5007 1.2826 1.4271 -0.0096 0.1026 0.0786 640 LEU A C 4362 O O . LEU A 640 ? 1.5340 1.3249 1.4698 -0.0189 0.0901 0.0810 640 LEU A O 4363 C CB . LEU A 640 ? 1.3152 1.1257 1.2668 0.0138 0.1098 0.0781 640 LEU A CB 4364 C CG . LEU A 640 ? 1.2358 1.0569 1.2025 0.0135 0.0994 0.0815 640 LEU A CG 4365 C CD1 . LEU A 640 ? 1.2781 1.1010 1.2438 0.0250 0.1016 0.0827 640 LEU A CD1 4366 C CD2 . LEU A 640 ? 1.2049 1.0509 1.2113 0.0102 0.0962 0.0840 640 LEU A CD2 4367 N N . SER A 641 ? 1.5595 1.3103 1.4541 -0.0097 0.1094 0.0768 641 SER A N 4368 C CA . SER A 641 ? 1.6121 1.3299 1.4730 -0.0184 0.1045 0.0732 641 SER A CA 4369 C C . SER A 641 ? 1.6385 1.3461 1.4796 -0.0033 0.1084 0.0726 641 SER A C 4370 O O . SER A 641 ? 1.6207 1.3334 1.4652 0.0131 0.1187 0.0761 641 SER A O 4371 C CB . SER A 641 ? 1.6921 1.3738 1.5277 -0.0239 0.1134 0.0713 641 SER A CB 4372 O OG . SER A 641 ? 1.7735 1.4156 1.5702 -0.0325 0.1105 0.0642 641 SER A OG 4373 N N . ILE A 642 ? 1.6843 1.3810 1.5052 -0.0101 0.0996 0.0699 642 ILE A N 4374 C CA . ILE A 642 ? 1.7254 1.4172 1.5294 0.0034 0.1038 0.0714 642 ILE A CA 4375 C C . ILE A 642 ? 1.7280 1.3938 1.4921 -0.0085 0.0966 0.0658 642 ILE A C 4376 O O . ILE A 642 ? 1.6709 1.3490 1.4401 -0.0265 0.0789 0.0663 642 ILE A O 4377 C CB . ILE A 642 ? 1.7830 1.5146 1.6240 0.0122 0.0989 0.0791 642 ILE A CB 4378 C CG1 . ILE A 642 ? 1.7354 1.4638 1.5637 0.0277 0.1073 0.0836 642 ILE A CG1 4379 C CG2 . ILE A 642 ? 1.7483 1.5030 1.6095 -0.0002 0.0817 0.0830 642 ILE A CG2 4380 C CD1 . ILE A 642 ? 1.9239 1.6385 1.7424 0.0427 0.1241 0.0851 642 ILE A CD1 4381 N N . GLY A 643 ? 1.8144 1.4446 1.5379 0.0016 0.1108 0.0612 643 GLY A N 4382 C CA . GLY A 643 ? 2.0706 1.6648 1.7424 -0.0102 0.1079 0.0518 643 GLY A CA 4383 C C . GLY A 643 ? 2.3491 1.9131 1.9991 -0.0345 0.0993 0.0413 643 GLY A C 4384 O O . GLY A 643 ? 2.4565 1.9857 2.0577 -0.0499 0.0942 0.0306 643 GLY A O 4385 N N . ALA A 644 ? 2.3398 1.9172 2.0240 -0.0398 0.0974 0.0445 644 ALA A N 4386 C CA . ALA A 644 ? 2.0328 1.5810 1.7025 -0.0627 0.0921 0.0371 644 ALA A CA 4387 C C . ALA A 644 ? 2.0036 1.4937 1.6343 -0.0523 0.1149 0.0288 644 ALA A C 4388 O O . ALA A 644 ? 2.0507 1.5349 1.6983 -0.0441 0.1269 0.0337 644 ALA A O 4389 C CB . ALA A 644 ? 1.5590 1.1446 1.2805 -0.0704 0.0853 0.0462 644 ALA A CB 4390 N N . GLN A 645 ? 1.9787 1.4257 1.5559 -0.0515 0.1218 0.0175 645 GLN A N 4391 C CA . GLN A 645 ? 2.1532 1.5427 1.6906 -0.0346 0.1486 0.0101 645 GLN A CA 4392 C C . GLN A 645 ? 2.2528 1.6066 1.7938 -0.0321 0.1636 0.0109 645 GLN A C 4393 O O . GLN A 645 ? 2.0326 1.3843 1.5854 -0.0553 0.1513 0.0100 645 GLN A O 4394 C CB . GLN A 645 ? 2.3687 1.7076 1.8378 -0.0482 0.1485 -0.0081 645 GLN A CB 4395 C CG . GLN A 645 ? 2.6459 2.0012 2.0959 -0.0353 0.1508 -0.0068 645 GLN A CG 4396 C CD . GLN A 645 ? 2.6059 2.0364 2.1112 -0.0279 0.1355 0.0112 645 GLN A CD 4397 O OE1 . GLN A 645 ? 2.5416 1.9960 2.0401 -0.0413 0.1164 0.0128 645 GLN A OE1 4398 N NE2 . GLN A 645 ? 2.3239 1.7893 1.8813 -0.0065 0.1445 0.0254 645 GLN A NE2 4399 N N . THR A 646 ? 2.5162 1.8465 2.0511 -0.0027 0.1906 0.0163 646 THR A N 4400 C CA . THR A 646 ? 2.5671 1.8526 2.0976 0.0080 0.2121 0.0201 646 THR A CA 4401 C C . THR A 646 ? 2.3318 1.6422 1.9057 0.0042 0.2078 0.0346 646 THR A C 4402 O O . THR A 646 ? 2.2682 1.5854 1.8631 0.0282 0.2240 0.0505 646 THR A O 4403 C CB . THR A 646 ? 2.6367 1.8340 2.1058 -0.0034 0.2258 0.0005 646 THR A CB 4404 O OG1 . THR A 646 ? 2.7429 1.9279 2.1912 -0.0430 0.2011 -0.0146 646 THR A OG1 4405 C CG2 . THR A 646 ? 2.5018 1.6566 1.9221 0.0171 0.2492 -0.0100 646 THR A CG2 4406 N N . ASP A 647 ? 2.1791 1.5036 1.7660 -0.0254 0.1872 0.0314 647 ASP A N 4407 C CA . ASP A 647 ? 2.1716 1.5080 1.7904 -0.0307 0.1877 0.0443 647 ASP A CA 4408 C C . ASP A 647 ? 2.1175 1.5292 1.7896 -0.0241 0.1783 0.0599 647 ASP A C 4409 O O . ASP A 647 ? 2.1316 1.5868 1.8201 -0.0147 0.1708 0.0609 647 ASP A O 4410 C CB . ASP A 647 ? 2.3429 1.6490 1.9483 -0.0666 0.1751 0.0347 647 ASP A CB 4411 C CG . ASP A 647 ? 2.6649 1.9307 2.2700 -0.0683 0.1898 0.0427 647 ASP A CG 4412 O OD1 . ASP A 647 ? 2.5850 1.8825 2.2242 -0.0518 0.1980 0.0618 647 ASP A OD1 4413 O OD2 . ASP A 647 ? 3.1465 2.3461 2.7143 -0.0866 0.1935 0.0300 647 ASP A OD2 4414 N N . PHE A 648 ? 1.9344 1.3580 1.6307 -0.0290 0.1804 0.0719 648 PHE A N 4415 C CA . PHE A 648 ? 1.7449 1.2331 1.4837 -0.0281 0.1719 0.0824 648 PHE A CA 4416 C C . PHE A 648 ? 1.7914 1.3034 1.5501 -0.0567 0.1546 0.0786 648 PHE A C 4417 O O . PHE A 648 ? 1.8939 1.3736 1.6365 -0.0806 0.1477 0.0712 648 PHE A O 4418 C CB . PHE A 648 ? 1.7939 1.2914 1.5477 -0.0141 0.1853 0.1004 648 PHE A CB 4419 C CG . PHE A 648 ? 2.0117 1.4828 1.7654 -0.0309 0.1903 0.1076 648 PHE A CG 4420 C CD1 . PHE A 648 ? 2.0878 1.5871 1.8653 -0.0543 0.1801 0.1090 648 PHE A CD1 4421 C CD2 . PHE A 648 ? 2.0144 1.4356 1.7492 -0.0215 0.2073 0.1164 648 PHE A CD2 4422 C CE1 . PHE A 648 ? 1.9820 1.4603 1.7628 -0.0706 0.1854 0.1183 648 PHE A CE1 4423 C CE2 . PHE A 648 ? 2.0200 1.4161 1.7567 -0.0374 0.2124 0.1253 648 PHE A CE2 4424 C CZ . PHE A 648 ? 1.9838 1.4091 1.7430 -0.0630 0.2010 0.1262 648 PHE A CZ 4425 N N . LEU A 649 ? 1.7970 1.3657 1.5919 -0.0551 0.1479 0.0842 649 LEU A N 4426 C CA . LEU A 649 ? 1.9042 1.5019 1.7270 -0.0781 0.1352 0.0854 649 LEU A CA 4427 C C . LEU A 649 ? 2.0307 1.6564 1.8821 -0.0795 0.1437 0.0982 649 LEU A C 4428 O O . LEU A 649 ? 2.3499 1.9804 2.1996 -0.0618 0.1567 0.1059 649 LEU A O 4429 C CB . LEU A 649 ? 1.8986 1.5385 1.7429 -0.0763 0.1219 0.0816 649 LEU A CB 4430 C CG . LEU A 649 ? 1.9394 1.5539 1.7549 -0.0848 0.1097 0.0708 649 LEU A CG 4431 C CD1 . LEU A 649 ? 1.9893 1.6462 1.8275 -0.0795 0.0978 0.0711 649 LEU A CD1 4432 C CD2 . LEU A 649 ? 1.9981 1.5884 1.8023 -0.1163 0.0975 0.0673 649 LEU A CD2 4433 N N . SER A 650 ? 2.0045 1.6512 1.8822 -0.1012 0.1364 0.1025 650 SER A N 4434 C CA . SER A 650 ? 2.0310 1.7130 1.9392 -0.1014 0.1464 0.1150 650 SER A CA 4435 C C . SER A 650 ? 2.0113 1.7417 1.9611 -0.1125 0.1364 0.1169 650 SER A C 4436 O O . SER A 650 ? 2.4156 2.1527 2.3850 -0.1362 0.1288 0.1232 650 SER A O 4437 C CB . SER A 650 ? 1.9774 1.6309 1.8794 -0.1161 0.1551 0.1256 650 SER A CB 4438 O OG . SER A 650 ? 1.8343 1.4579 1.7098 -0.0987 0.1696 0.1310 650 SER A OG 4439 N N . VAL A 651 ? 1.7008 1.4647 1.6666 -0.0955 0.1364 0.1131 651 VAL A N 4440 C CA . VAL A 651 ? 1.7047 1.5138 1.7135 -0.1009 0.1289 0.1165 651 VAL A CA 4441 C C . VAL A 651 ? 1.7026 1.5478 1.7520 -0.1099 0.1395 0.1300 651 VAL A C 4442 O O . VAL A 651 ? 1.5856 1.4285 1.6287 -0.1058 0.1566 0.1355 651 VAL A O 4443 C CB . VAL A 651 ? 1.7053 1.5343 1.7209 -0.0794 0.1293 0.1093 651 VAL A CB 4444 C CG1 . VAL A 651 ? 1.5965 1.3912 1.5723 -0.0698 0.1235 0.0994 651 VAL A CG1 4445 C CG2 . VAL A 651 ? 1.8280 1.6767 1.8514 -0.0626 0.1486 0.1095 651 VAL A CG2 4446 N N . PHE A 652 ? 1.6951 1.5764 1.7872 -0.1217 0.1297 0.1380 652 PHE A N 4447 C CA . PHE A 652 ? 1.6493 1.5611 1.7813 -0.1372 0.1363 0.1542 652 PHE A CA 4448 C C . PHE A 652 ? 1.5955 1.5580 1.7739 -0.1219 0.1540 0.1620 652 PHE A C 4449 O O . PHE A 652 ? 1.5735 1.5387 1.7446 -0.1095 0.1768 0.1620 652 PHE A O 4450 C CB . PHE A 652 ? 1.7801 1.6959 1.9296 -0.1680 0.1126 0.1624 652 PHE A CB 4451 C CG . PHE A 652 ? 2.0546 1.9858 2.2331 -0.1910 0.1172 0.1793 652 PHE A CG 4452 C CD1 . PHE A 652 ? 2.4353 2.3457 2.5961 -0.1894 0.1374 0.1828 652 PHE A CD1 4453 C CD2 . PHE A 652 ? 2.1497 2.1202 2.3766 -0.2152 0.1007 0.1952 652 PHE A CD2 4454 C CE1 . PHE A 652 ? 2.7435 2.6690 2.9334 -0.2117 0.1428 0.2010 652 PHE A CE1 4455 C CE2 . PHE A 652 ? 2.4026 2.3913 2.6617 -0.2387 0.1048 0.2136 652 PHE A CE2 4456 C CZ . PHE A 652 ? 2.5706 2.5355 2.8110 -0.2369 0.1269 0.2161 652 PHE A CZ 4457 N N . PHE A 653 ? 1.5537 1.5546 1.7775 -0.1222 0.1447 0.1693 653 PHE A N 4458 C CA . PHE A 653 ? 1.4419 1.4917 1.7187 -0.1077 0.1641 0.1795 653 PHE A CA 4459 C C . PHE A 653 ? 1.3618 1.4418 1.6755 -0.1213 0.1777 0.1986 653 PHE A C 4460 O O . PHE A 653 ? 1.2122 1.2883 1.5124 -0.1128 0.2026 0.1977 653 PHE A O 4461 C CB . PHE A 653 ? 1.4686 1.5092 1.7234 -0.0799 0.1889 0.1653 653 PHE A CB 4462 C CG . PHE A 653 ? 1.5674 1.6011 1.8157 -0.0618 0.1828 0.1524 653 PHE A CG 4463 C CD1 . PHE A 653 ? 1.6075 1.6018 1.8059 -0.0583 0.1707 0.1373 653 PHE A CD1 4464 C CD2 . PHE A 653 ? 1.6166 1.6828 1.9114 -0.0467 0.1916 0.1573 653 PHE A CD2 4465 C CE1 . PHE A 653 ? 1.6642 1.6536 1.8594 -0.0429 0.1657 0.1275 653 PHE A CE1 4466 C CE2 . PHE A 653 ? 1.5945 1.6510 1.8847 -0.0305 0.1868 0.1467 653 PHE A CE2 4467 C CZ . PHE A 653 ? 1.5175 1.5364 1.7576 -0.0298 0.1731 0.1319 653 PHE A CZ 4468 N N . SER A 654 ? 1.4364 1.5501 1.7978 -0.1427 0.1611 0.2175 654 SER A N 4469 C CA . SER A 654 ? 1.5670 1.7134 1.9707 -0.1625 0.1691 0.2400 654 SER A CA 4470 C C . SER A 654 ? 1.5188 1.7059 1.9625 -0.1415 0.2056 0.2506 654 SER A C 4471 O O . SER A 654 ? 1.4456 1.6738 1.9389 -0.1255 0.2135 0.2590 654 SER A O 4472 C CB . SER A 654 ? 1.7342 1.9181 2.1885 -0.1895 0.1399 0.2600 654 SER A CB 4473 O OG . SER A 654 ? 2.0093 2.2000 2.4800 -0.2229 0.1327 0.2764 654 SER A OG 4474 N N . GLY A 655 ? 1.5836 1.7585 2.0051 -0.1411 0.2294 0.2514 655 GLY A N 4475 C CA . GLY A 655 ? 1.6703 1.8808 2.1212 -0.1226 0.2676 0.2608 655 GLY A CA 4476 C C . GLY A 655 ? 1.6901 1.8874 2.1122 -0.0885 0.2905 0.2393 655 GLY A C 4477 O O . GLY A 655 ? 1.7593 1.9886 2.2151 -0.0685 0.3192 0.2434 655 GLY A O 4478 N N . TYR A 656 ? 1.6102 1.7586 1.9692 -0.0826 0.2789 0.2162 656 TYR A N 4479 C CA . TYR A 656 ? 1.5056 1.6376 1.8346 -0.0558 0.2934 0.1945 656 TYR A CA 4480 C C . TYR A 656 ? 1.6614 1.7498 1.9176 -0.0510 0.2971 0.1767 656 TYR A C 4481 O O . TYR A 656 ? 1.8899 1.9469 2.1113 -0.0641 0.2773 0.1750 656 TYR A O 4482 C CB . TYR A 656 ? 1.3607 1.4906 1.7047 -0.0485 0.2720 0.1866 656 TYR A CB 4483 C CG . TYR A 656 ? 1.4525 1.6215 1.8542 -0.0308 0.2905 0.1944 656 TYR A CG 4484 C CD1 . TYR A 656 ? 1.6334 1.8084 2.0329 -0.0102 0.3283 0.1875 656 TYR A CD1 4485 C CD2 . TYR A 656 ? 1.5099 1.7095 1.9676 -0.0339 0.2722 0.2096 656 TYR A CD2 4486 C CE1 . TYR A 656 ? 1.8405 2.0473 2.2944 0.0098 0.3508 0.1944 656 TYR A CE1 4487 C CE2 . TYR A 656 ? 1.7106 1.9479 2.2284 -0.0140 0.2918 0.2205 656 TYR A CE2 4488 C CZ . TYR A 656 ? 1.7919 2.0308 2.3089 0.0091 0.3329 0.2123 656 TYR A CZ 4489 O OH . TYR A 656 ? 1.8127 2.0839 2.3898 0.0320 0.3567 0.2226 656 TYR A OH 4490 N N . THR A 657 ? 1.6405 1.7263 1.8730 -0.0320 0.3230 0.1639 657 THR A N 4491 C CA . THR A 657 ? 1.5326 1.5833 1.6977 -0.0282 0.3238 0.1490 657 THR A CA 4492 C C . THR A 657 ? 1.5628 1.5958 1.7032 -0.0110 0.3234 0.1254 657 THR A C 4493 O O . THR A 657 ? 1.5682 1.6138 1.7273 0.0044 0.3435 0.1167 657 THR A O 4494 C CB . THR A 657 ? 1.5689 1.6270 1.7100 -0.0272 0.3524 0.1547 657 THR A CB 4495 O OG1 . THR A 657 ? 1.7162 1.8100 1.9009 -0.0181 0.3812 0.1612 657 THR A OG1 4496 C CG2 . THR A 657 ? 1.5564 1.6104 1.6932 -0.0469 0.3450 0.1749 657 THR A CG2 4497 N N . PHE A 658 ? 1.4900 1.4922 1.5893 -0.0136 0.3017 0.1160 658 PHE A N 4498 C CA . PHE A 658 ? 1.5214 1.5041 1.5951 -0.0017 0.2952 0.0953 658 PHE A CA 4499 C C . PHE A 658 ? 1.5005 1.4621 1.5127 -0.0001 0.2971 0.0846 658 PHE A C 4500 O O . PHE A 658 ? 1.4790 1.4335 1.4644 -0.0084 0.2933 0.0953 658 PHE A O 4501 C CB . PHE A 658 ? 1.4312 1.4022 1.5172 -0.0048 0.2666 0.0946 658 PHE A CB 4502 C CG . PHE A 658 ? 1.4197 1.3736 1.4872 -0.0182 0.2477 0.1044 658 PHE A CG 4503 C CD1 . PHE A 658 ? 1.4777 1.4058 1.5000 -0.0166 0.2383 0.0987 658 PHE A CD1 4504 C CD2 . PHE A 658 ? 1.4495 1.4122 1.5461 -0.0329 0.2394 0.1197 658 PHE A CD2 4505 C CE1 . PHE A 658 ? 1.6064 1.5140 1.6127 -0.0259 0.2248 0.1078 658 PHE A CE1 4506 C CE2 . PHE A 658 ? 1.5656 1.5036 1.6410 -0.0457 0.2240 0.1259 658 PHE A CE2 4507 C CZ . PHE A 658 ? 1.5972 1.5056 1.6273 -0.0404 0.2187 0.1198 658 PHE A CZ 4508 N N . LYS A 659 ? 1.4744 1.4264 1.4662 0.0097 0.3025 0.0649 659 LYS A N 4509 C CA . LYS A 659 ? 1.4109 1.3473 1.3462 0.0089 0.3011 0.0544 659 LYS A CA 4510 C C . LYS A 659 ? 1.5398 1.4599 1.4650 0.0072 0.2729 0.0527 659 LYS A C 4511 O O . LYS A 659 ? 1.6078 1.5207 1.5479 0.0125 0.2640 0.0414 659 LYS A O 4512 C CB . LYS A 659 ? 1.3470 1.2773 1.2629 0.0169 0.3202 0.0318 659 LYS A CB 4513 C CG . LYS A 659 ? 1.3436 1.2693 1.1994 0.0124 0.3321 0.0249 659 LYS A CG 4514 C CD . LYS A 659 ? 1.3953 1.3079 1.2269 0.0185 0.3532 -0.0017 659 LYS A CD 4515 C CE . LYS A 659 ? 1.4381 1.3540 1.2208 0.0157 0.3791 -0.0058 659 LYS A CE 4516 N NZ . LYS A 659 ? 1.3728 1.3025 1.1810 0.0257 0.4163 -0.0039 659 LYS A NZ 4517 N N . HIS A 660 ? 1.6250 1.5394 1.5278 0.0009 0.2611 0.0663 660 HIS A N 4518 C CA . HIS A 660 ? 1.6408 1.5413 1.5273 0.0010 0.2389 0.0676 660 HIS A CA 4519 C C . HIS A 660 ? 1.7737 1.6739 1.6135 -0.0004 0.2378 0.0649 660 HIS A C 4520 O O . HIS A 660 ? 1.6221 1.5274 1.4382 -0.0044 0.2446 0.0778 660 HIS A O 4521 C CB . HIS A 660 ? 1.5773 1.4692 1.4716 -0.0034 0.2291 0.0860 660 HIS A CB 4522 C CG . HIS A 660 ? 1.6599 1.5365 1.5488 -0.0001 0.2099 0.0876 660 HIS A CG 4523 N ND1 . HIS A 660 ? 1.8037 1.6644 1.6851 -0.0014 0.2032 0.1025 660 HIS A ND1 4524 C CD2 . HIS A 660 ? 1.7806 1.6540 1.6709 0.0053 0.1983 0.0773 660 HIS A CD2 4525 C CE1 . HIS A 660 ? 1.8549 1.7047 1.7333 0.0046 0.1900 0.1009 660 HIS A CE1 4526 N NE2 . HIS A 660 ? 1.9312 1.7908 1.8158 0.0079 0.1860 0.0867 660 HIS A NE2 4527 N N . LYS A 661 ? 1.9111 1.8068 1.7388 0.0011 0.2289 0.0496 661 LYS A N 4528 C CA . LYS A 661 ? 1.9500 1.8480 1.7338 -0.0040 0.2220 0.0462 661 LYS A CA 4529 C C . LYS A 661 ? 1.8355 1.7416 1.5787 -0.0099 0.2383 0.0454 661 LYS A C 4530 O O . LYS A 661 ? 1.3953 1.3099 1.1130 -0.0137 0.2352 0.0640 661 LYS A O 4531 C CB . LYS A 661 ? 2.1307 2.0298 1.9101 -0.0034 0.2009 0.0637 661 LYS A CB 4532 C CG . LYS A 661 ? 2.6203 2.5233 2.3885 -0.0035 0.2024 0.0885 661 LYS A CG 4533 C CD . LYS A 661 ? 2.8190 2.7117 2.6175 -0.0007 0.2092 0.0986 661 LYS A CD 4534 C CE . LYS A 661 ? 3.0901 2.9859 2.8753 -0.0045 0.2214 0.1170 661 LYS A CE 4535 N NZ . LYS A 661 ? 3.0673 2.9589 2.8818 -0.0077 0.2337 0.1194 661 LYS A NZ 4536 N N . MET A 662 ? 1.9688 1.8705 1.7057 -0.0094 0.2569 0.0241 662 MET A N 4537 C CA . MET A 662 ? 2.0756 1.9823 1.7809 -0.0120 0.2818 0.0193 662 MET A CA 4538 C C . MET A 662 ? 1.9713 1.8927 1.6738 -0.0135 0.2926 0.0444 662 MET A C 4539 O O . MET A 662 ? 2.1045 2.0330 1.7619 -0.0195 0.3013 0.0490 662 MET A O 4540 C CB . MET A 662 ? 2.3185 2.2185 1.9642 -0.0216 0.2808 0.0004 662 MET A CB 4541 C CG . MET A 662 ? 2.6284 2.5090 2.2641 -0.0193 0.3014 -0.0316 662 MET A CG 4542 S SD . MET A 662 ? 3.2007 3.0814 2.8181 -0.0133 0.3459 -0.0413 662 MET A SD 4543 C CE . MET A 662 ? 2.8774 2.7666 2.4114 -0.0286 0.3470 -0.0368 662 MET A CE 4544 N N . VAL A 663 ? 1.7075 1.6323 1.4563 -0.0097 0.2918 0.0607 663 VAL A N 4545 C CA . VAL A 663 ? 1.5599 1.4956 1.3168 -0.0125 0.3055 0.0830 663 VAL A CA 4546 C C . VAL A 663 ? 1.5301 1.4700 1.3447 -0.0098 0.3124 0.0871 663 VAL A C 4547 O O . VAL A 663 ? 1.4097 1.3424 1.2556 -0.0063 0.2984 0.0801 663 VAL A O 4548 C CB . VAL A 663 ? 1.6152 1.5474 1.3660 -0.0163 0.2884 0.1082 663 VAL A CB 4549 C CG1 . VAL A 663 ? 1.5407 1.4830 1.2758 -0.0216 0.3047 0.1302 663 VAL A CG1 4550 C CG2 . VAL A 663 ? 1.9175 1.8456 1.6359 -0.0165 0.2666 0.1069 663 VAL A CG2 4551 N N . TYR A 664 ? 1.5953 1.5495 1.4243 -0.0128 0.3326 0.1015 664 TYR A N 4552 C CA . TYR A 664 ? 1.5637 1.5291 1.4513 -0.0135 0.3383 0.1091 664 TYR A CA 4553 C C . TYR A 664 ? 1.4995 1.4574 1.4089 -0.0237 0.3208 0.1304 664 TYR A C 4554 O O . TYR A 664 ? 1.5081 1.4619 1.3967 -0.0304 0.3226 0.1482 664 TYR A O 4555 C CB . TYR A 664 ? 1.5646 1.5531 1.4662 -0.0107 0.3719 0.1114 664 TYR A CB 4556 C CG . TYR A 664 ? 1.6496 1.6401 1.5630 0.0022 0.3871 0.0879 664 TYR A CG 4557 C CD1 . TYR A 664 ? 1.7636 1.7454 1.7076 0.0077 0.3696 0.0764 664 TYR A CD1 4558 C CD2 . TYR A 664 ? 1.6989 1.6965 1.5916 0.0097 0.4204 0.0775 664 TYR A CD2 4559 C CE1 . TYR A 664 ? 1.9506 1.9298 1.9090 0.0206 0.3837 0.0569 664 TYR A CE1 4560 C CE2 . TYR A 664 ? 1.9377 1.9291 1.8414 0.0233 0.4366 0.0545 664 TYR A CE2 4561 C CZ . TYR A 664 ? 2.0113 1.9931 1.9506 0.0291 0.4178 0.0450 664 TYR A CZ 4562 O OH . TYR A 664 ? 1.8275 1.7992 1.7824 0.0435 0.4333 0.0247 664 TYR A OH 4563 N N . GLU A 665 ? 1.4487 1.4008 1.3948 -0.0252 0.3036 0.1280 665 GLU A N 4564 C CA . GLU A 665 ? 1.5492 1.4855 1.5090 -0.0364 0.2864 0.1429 665 GLU A CA 4565 C C . GLU A 665 ? 1.6910 1.6406 1.7035 -0.0471 0.2838 0.1510 665 GLU A C 4566 O O . GLU A 665 ? 1.6286 1.6051 1.6774 -0.0435 0.2945 0.1480 665 GLU A O 4567 C CB . GLU A 665 ? 1.5274 1.4357 1.4672 -0.0329 0.2625 0.1364 665 GLU A CB 4568 C CG . GLU A 665 ? 1.7854 1.6807 1.6790 -0.0267 0.2590 0.1389 665 GLU A CG 4569 C CD . GLU A 665 ? 2.1249 2.0152 1.9990 -0.0326 0.2677 0.1610 665 GLU A CD 4570 O OE1 . GLU A 665 ? 2.4400 2.3204 2.3333 -0.0430 0.2689 0.1749 665 GLU A OE1 4571 O OE2 . GLU A 665 ? 2.1477 2.0434 1.9860 -0.0283 0.2721 0.1661 665 GLU A OE2 4572 N N . ASP A 666 ? 1.8188 1.7477 1.8342 -0.0604 0.2687 0.1618 666 ASP A N 4573 C CA . ASP A 666 ? 1.7808 1.7180 1.8359 -0.0790 0.2648 0.1757 666 ASP A CA 4574 C C . ASP A 666 ? 1.6223 1.5383 1.6818 -0.0846 0.2392 0.1672 666 ASP A C 4575 O O . ASP A 666 ? 1.4880 1.4208 1.5858 -0.0957 0.2295 0.1701 666 ASP A O 4576 C CB . ASP A 666 ? 2.1148 2.0339 2.1548 -0.0926 0.2706 0.1948 666 ASP A CB 4577 C CG . ASP A 666 ? 2.1943 2.1189 2.2738 -0.1174 0.2658 0.2107 666 ASP A CG 4578 O OD1 . ASP A 666 ? 2.3444 2.2805 2.4570 -0.1263 0.2508 0.2065 666 ASP A OD1 4579 O OD2 . ASP A 666 ? 2.0020 1.9191 2.0786 -0.1297 0.2758 0.2290 666 ASP A OD2 4580 N N . THR A 667 ? 1.5759 1.4578 1.5959 -0.0766 0.2289 0.1584 667 THR A N 4581 C CA . THR A 667 ? 1.7636 1.6157 1.7752 -0.0818 0.2076 0.1510 667 THR A CA 4582 C C . THR A 667 ? 1.7062 1.5319 1.6796 -0.0657 0.2024 0.1414 667 THR A C 4583 O O . THR A 667 ? 1.7431 1.5480 1.6884 -0.0610 0.2082 0.1485 667 THR A O 4584 C CB . THR A 667 ? 1.9891 1.8108 1.9969 -0.1027 0.2013 0.1612 667 THR A CB 4585 O OG1 . THR A 667 ? 2.1586 1.9727 2.1530 -0.1039 0.2173 0.1758 667 THR A OG1 4586 C CG2 . THR A 667 ? 2.2022 2.0461 2.2523 -0.1249 0.1923 0.1674 667 THR A CG2 4587 N N . LEU A 668 ? 1.7054 1.5341 1.6818 -0.0576 0.1910 0.1284 668 LEU A N 4588 C CA . LEU A 668 ? 1.6397 1.4528 1.5885 -0.0419 0.1863 0.1201 668 LEU A CA 4589 C C . LEU A 668 ? 1.6703 1.4448 1.5984 -0.0446 0.1757 0.1190 668 LEU A C 4590 O O . LEU A 668 ? 1.7150 1.4776 1.6509 -0.0587 0.1658 0.1170 668 LEU A O 4591 C CB . LEU A 668 ? 1.6642 1.4989 1.6288 -0.0326 0.1811 0.1079 668 LEU A CB 4592 C CG . LEU A 668 ? 1.7341 1.5557 1.6842 -0.0221 0.1699 0.0992 668 LEU A CG 4593 C CD1 . LEU A 668 ? 1.8319 1.6459 1.7537 -0.0097 0.1738 0.1002 668 LEU A CD1 4594 C CD2 . LEU A 668 ? 1.8207 1.6658 1.7968 -0.0173 0.1663 0.0907 668 LEU A CD2 4595 N N . THR A 669 ? 1.7349 1.4910 1.6361 -0.0308 0.1781 0.1206 669 THR A N 4596 C CA . THR A 669 ? 1.8287 1.5430 1.7064 -0.0283 0.1745 0.1207 669 THR A CA 4597 C C . THR A 669 ? 1.8167 1.5265 1.6843 -0.0141 0.1676 0.1121 669 THR A C 4598 O O . THR A 669 ? 1.9647 1.6905 1.8292 0.0006 0.1696 0.1143 669 THR A O 4599 C CB . THR A 669 ? 1.6769 1.3681 1.5360 -0.0233 0.1860 0.1357 669 THR A CB 4600 O OG1 . THR A 669 ? 1.5853 1.3089 1.4469 -0.0159 0.1930 0.1441 669 THR A OG1 4601 C CG2 . THR A 669 ? 1.4874 1.1517 1.3476 -0.0425 0.1895 0.1421 669 THR A CG2 4602 N N . LEU A 670 ? 1.7367 1.4253 1.5977 -0.0204 0.1591 0.1035 670 LEU A N 4603 C CA . LEU A 670 ? 1.6794 1.3687 1.5340 -0.0092 0.1530 0.0962 670 LEU A CA 4604 C C . LEU A 670 ? 1.8851 1.5325 1.7094 -0.0020 0.1564 0.0941 670 LEU A C 4605 O O . LEU A 670 ? 1.9236 1.5412 1.7304 -0.0138 0.1515 0.0860 670 LEU A O 4606 C CB . LEU A 670 ? 1.6462 1.3586 1.5209 -0.0187 0.1403 0.0884 670 LEU A CB 4607 C CG . LEU A 670 ? 1.6819 1.4362 1.5854 -0.0139 0.1417 0.0890 670 LEU A CG 4608 C CD1 . LEU A 670 ? 1.7860 1.5616 1.7115 -0.0161 0.1308 0.0838 670 LEU A CD1 4609 C CD2 . LEU A 670 ? 1.6975 1.4591 1.5924 0.0028 0.1484 0.0913 670 LEU A CD2 4610 N N . PHE A 671 ? 1.8620 1.5091 1.6799 0.0175 0.1653 0.1019 671 PHE A N 4611 C CA . PHE A 671 ? 1.8830 1.4982 1.6781 0.0315 0.1732 0.1026 671 PHE A CA 4612 C C . PHE A 671 ? 1.8356 1.4585 1.6281 0.0338 0.1658 0.0934 671 PHE A C 4613 O O . PHE A 671 ? 1.9866 1.6482 1.8015 0.0340 0.1568 0.0924 671 PHE A O 4614 C CB . PHE A 671 ? 1.9933 1.6244 1.7953 0.0522 0.1820 0.1182 671 PHE A CB 4615 C CG . PHE A 671 ? 2.0672 1.6726 1.8603 0.0578 0.1947 0.1320 671 PHE A CG 4616 C CD1 . PHE A 671 ? 2.0732 1.6553 1.8605 0.0414 0.1963 0.1306 671 PHE A CD1 4617 C CD2 . PHE A 671 ? 2.0582 1.6641 1.8524 0.0798 0.2053 0.1496 671 PHE A CD2 4618 C CE1 . PHE A 671 ? 2.2624 1.8177 2.0426 0.0467 0.2090 0.1457 671 PHE A CE1 4619 C CE2 . PHE A 671 ? 2.1446 1.7266 1.9336 0.0869 0.2176 0.1661 671 PHE A CE2 4620 C CZ . PHE A 671 ? 2.2732 1.8275 2.0537 0.0704 0.2199 0.1638 671 PHE A CZ 4621 N N . PRO A 672 ? 1.7538 1.3372 1.5166 0.0362 0.1713 0.0869 672 PRO A N 4622 C CA . PRO A 672 ? 1.8563 1.4422 1.6095 0.0433 0.1696 0.0821 672 PRO A CA 4623 C C . PRO A 672 ? 1.8837 1.5197 1.6675 0.0463 0.1587 0.0853 672 PRO A C 4624 O O . PRO A 672 ? 1.9958 1.6519 1.7940 0.0318 0.1447 0.0798 672 PRO A O 4625 C CB . PRO A 672 ? 1.9993 1.5604 1.7370 0.0668 0.1897 0.0905 672 PRO A CB 4626 C CG . PRO A 672 ? 2.0784 1.5938 1.7969 0.0627 0.2002 0.0901 672 PRO A CG 4627 C CD . PRO A 672 ? 1.9152 1.4447 1.6488 0.0393 0.1861 0.0869 672 PRO A CD 4628 N N . PHE A 673 ? 1.8401 1.4966 1.6364 0.0642 0.1649 0.0953 673 PHE A N 4629 C CA . PHE A 673 ? 1.7954 1.4898 1.6156 0.0643 0.1545 0.0960 673 PHE A CA 4630 C C . PHE A 673 ? 1.8632 1.5944 1.7129 0.0649 0.1498 0.1016 673 PHE A C 4631 O O . PHE A 673 ? 1.7356 1.4939 1.6036 0.0704 0.1463 0.1064 673 PHE A O 4632 C CB . PHE A 673 ? 1.7950 1.4866 1.6058 0.0771 0.1608 0.1002 673 PHE A CB 4633 C CG . PHE A 673 ? 1.8956 1.5442 1.6663 0.0755 0.1679 0.0919 673 PHE A CG 4634 C CD1 . PHE A 673 ? 2.0129 1.6459 1.7669 0.0555 0.1560 0.0796 673 PHE A CD1 4635 C CD2 . PHE A 673 ? 1.9045 1.5276 1.6529 0.0932 0.1871 0.0965 673 PHE A CD2 4636 C CE1 . PHE A 673 ? 2.0512 1.6414 1.7607 0.0498 0.1604 0.0696 673 PHE A CE1 4637 C CE2 . PHE A 673 ? 1.9769 1.5536 1.6802 0.0909 0.1959 0.0854 673 PHE A CE2 4638 C CZ . PHE A 673 ? 2.0412 1.5997 1.7215 0.0674 0.1813 0.0706 673 PHE A CZ 4639 N N . SER A 674 ? 2.1621 1.8918 2.0135 0.0570 0.1499 0.1003 674 SER A N 4640 C CA . SER A 674 ? 2.2251 1.9855 2.0972 0.0520 0.1448 0.1000 674 SER A CA 4641 C C . SER A 674 ? 1.9247 1.6964 1.8126 0.0388 0.1365 0.0894 674 SER A C 4642 O O . SER A 674 ? 1.5655 1.3230 1.4487 0.0303 0.1325 0.0849 674 SER A O 4643 C CB . SER A 674 ? 2.4046 2.1624 2.2702 0.0521 0.1516 0.1074 674 SER A CB 4644 O OG . SER A 674 ? 2.2032 1.9329 2.0561 0.0439 0.1561 0.1056 674 SER A OG 4645 N N . GLY A 675 ? 1.7771 1.5745 1.6840 0.0371 0.1340 0.0863 675 GLY A N 4646 C CA . GLY A 675 ? 1.7196 1.5302 1.6474 0.0287 0.1305 0.0788 675 GLY A CA 4647 C C . GLY A 675 ? 1.8520 1.6782 1.7852 0.0272 0.1364 0.0754 675 GLY A C 4648 O O . GLY A 675 ? 2.0794 1.9160 2.0107 0.0310 0.1360 0.0742 675 GLY A O 4649 N N . GLU A 676 ? 1.7776 1.6058 1.7155 0.0202 0.1420 0.0745 676 GLU A N 4650 C CA . GLU A 676 ? 1.7066 1.5481 1.6440 0.0189 0.1508 0.0709 676 GLU A CA 4651 C C . GLU A 676 ? 1.5615 1.4171 1.5248 0.0164 0.1563 0.0630 676 GLU A C 4652 O O . GLU A 676 ? 1.3927 1.2519 1.3784 0.0129 0.1537 0.0653 676 GLU A O 4653 C CB . GLU A 676 ? 1.8569 1.6924 1.7754 0.0159 0.1582 0.0795 676 GLU A CB 4654 C CG . GLU A 676 ? 1.9701 1.8062 1.8658 0.0217 0.1577 0.0864 676 GLU A CG 4655 C CD . GLU A 676 ? 2.3946 2.2448 2.2914 0.0245 0.1518 0.0790 676 GLU A CD 4656 O OE1 . GLU A 676 ? 2.2765 2.1371 2.1757 0.0206 0.1558 0.0674 676 GLU A OE1 4657 O OE2 . GLU A 676 ? 2.6997 2.5488 2.5952 0.0304 0.1442 0.0846 676 GLU A OE2 4658 N N . THR A 677 ? 1.6520 1.5157 1.6111 0.0182 0.1642 0.0544 677 THR A N 4659 C CA . THR A 677 ? 1.6282 1.5002 1.6104 0.0204 0.1727 0.0446 677 THR A CA 4660 C C . THR A 677 ? 1.5826 1.4628 1.5608 0.0186 0.1910 0.0411 677 THR A C 4661 O O . THR A 677 ? 1.6202 1.4989 1.5671 0.0165 0.1963 0.0374 677 THR A O 4662 C CB . THR A 677 ? 1.6547 1.5213 1.6320 0.0235 0.1684 0.0342 677 THR A CB 4663 O OG1 . THR A 677 ? 1.4542 1.3208 1.4438 0.0262 0.1816 0.0212 677 THR A OG1 4664 C CG2 . THR A 677 ? 1.6798 1.5443 1.6220 0.0203 0.1631 0.0344 677 THR A CG2 4665 N N . VAL A 678 ? 1.4539 1.3461 1.4641 0.0190 0.2003 0.0448 678 VAL A N 4666 C CA . VAL A 678 ? 1.4427 1.3470 1.4551 0.0173 0.2200 0.0468 678 VAL A CA 4667 C C . VAL A 678 ? 1.3446 1.2599 1.3858 0.0254 0.2400 0.0396 678 VAL A C 4668 O O . VAL A 678 ? 1.4478 1.3608 1.5127 0.0326 0.2379 0.0344 678 VAL A O 4669 C CB . VAL A 678 ? 1.4518 1.3656 1.4815 0.0086 0.2173 0.0636 678 VAL A CB 4670 C CG1 . VAL A 678 ? 1.4414 1.3383 1.4421 0.0017 0.2033 0.0713 678 VAL A CG1 4671 C CG2 . VAL A 678 ? 1.4413 1.3687 1.5170 0.0081 0.2097 0.0707 678 VAL A CG2 4672 N N . PHE A 679 ? 1.2827 1.2103 1.3252 0.0254 0.2613 0.0417 679 PHE A N 4673 C CA . PHE A 679 ? 1.4070 1.3411 1.4706 0.0364 0.2865 0.0329 679 PHE A CA 4674 C C . PHE A 679 ? 1.5173 1.4790 1.6182 0.0385 0.3077 0.0467 679 PHE A C 4675 O O . PHE A 679 ? 1.6579 1.6272 1.7397 0.0330 0.3207 0.0519 679 PHE A O 4676 C CB . PHE A 679 ? 1.5116 1.4263 1.5250 0.0379 0.2996 0.0123 679 PHE A CB 4677 C CG . PHE A 679 ? 1.7406 1.6512 1.7620 0.0498 0.3300 -0.0023 679 PHE A CG 4678 C CD1 . PHE A 679 ? 1.6046 1.5000 1.6479 0.0601 0.3332 -0.0143 679 PHE A CD1 4679 C CD2 . PHE A 679 ? 2.0228 1.9412 2.0262 0.0512 0.3581 -0.0042 679 PHE A CD2 4680 C CE1 . PHE A 679 ? 1.6646 1.5488 1.7128 0.0728 0.3647 -0.0292 679 PHE A CE1 4681 C CE2 . PHE A 679 ? 2.1024 2.0125 2.1081 0.0640 0.3908 -0.0196 679 PHE A CE2 4682 C CZ . PHE A 679 ? 1.9939 1.8849 2.0223 0.0754 0.3945 -0.0330 679 PHE A CZ 4683 N N . MET A 680 ? 1.5703 1.5496 1.7273 0.0471 0.3122 0.0547 680 MET A N 4684 C CA . MET A 680 ? 1.6771 1.6912 1.8828 0.0473 0.3268 0.0743 680 MET A CA 4685 C C . MET A 680 ? 1.8751 1.8983 2.0982 0.0638 0.3650 0.0687 680 MET A C 4686 O O . MET A 680 ? 1.8566 1.8891 2.1264 0.0787 0.3755 0.0713 680 MET A O 4687 C CB . MET A 680 ? 1.7192 1.7563 1.9826 0.0452 0.3067 0.0932 680 MET A CB 4688 C CG . MET A 680 ? 1.8147 1.8414 2.0597 0.0283 0.2713 0.0986 680 MET A CG 4689 S SD . MET A 680 ? 1.7713 1.8149 2.0221 0.0054 0.2601 0.1189 680 MET A SD 4690 C CE . MET A 680 ? 1.8871 1.9390 2.1234 0.0086 0.2952 0.1184 680 MET A CE 4691 N N . SER A 681 ? 2.1322 2.1518 2.3172 0.0623 0.3876 0.0621 681 SER A N 4692 C CA . SER A 681 ? 2.2090 2.2456 2.4171 0.0764 0.4274 0.0633 681 SER A CA 4693 C C . SER A 681 ? 2.0838 2.1655 2.3665 0.0727 0.4215 0.0948 681 SER A C 4694 O O . SER A 681 ? 2.0923 2.1899 2.3759 0.0542 0.4059 0.1120 681 SER A O 4695 C CB . SER A 681 ? 2.3711 2.4030 2.5251 0.0708 0.4486 0.0576 681 SER A CB 4696 O OG . SER A 681 ? 2.5573 2.6036 2.7291 0.0862 0.4916 0.0572 681 SER A OG 4697 N N . MET A 682 ? 1.7889 1.8899 2.1345 0.0884 0.4304 0.1036 682 MET A N 4698 C CA . MET A 682 ? 1.6687 1.8123 2.0856 0.0808 0.4097 0.1343 682 MET A CA 4699 C C . MET A 682 ? 1.6697 1.8615 2.1685 0.0954 0.4353 0.1588 682 MET A C 4700 O O . MET A 682 ? 1.4347 1.6481 1.9927 0.1038 0.4250 0.1742 682 MET A O 4701 C CB . MET A 682 ? 1.5687 1.6993 1.9930 0.0782 0.3745 0.1331 682 MET A CB 4702 C CG . MET A 682 ? 1.5042 1.6795 2.0014 0.0721 0.3543 0.1640 682 MET A CG 4703 S SD . MET A 682 ? 1.7391 1.8949 2.2104 0.0528 0.3035 0.1630 682 MET A SD 4704 C CE . MET A 682 ? 1.5575 1.6959 1.9702 0.0264 0.2901 0.1582 682 MET A CE 4705 N N . GLU A 683 ? 1.7852 1.9982 2.2900 0.0974 0.4675 0.1665 683 GLU A N 4706 C CA . GLU A 683 ? 1.8518 2.1122 2.4336 0.1146 0.5000 0.1899 683 GLU A CA 4707 C C . GLU A 683 ? 1.8702 2.1875 2.5085 0.0943 0.4891 0.2266 683 GLU A C 4708 O O . GLU A 683 ? 2.1519 2.5131 2.8469 0.1048 0.5210 0.2481 683 GLU A O 4709 C CB . GLU A 683 ? 1.9983 2.2410 2.5511 0.1375 0.5539 0.1710 683 GLU A CB 4710 C CG . GLU A 683 ? 2.3263 2.5670 2.8270 0.1255 0.5731 0.1672 683 GLU A CG 4711 C CD . GLU A 683 ? 2.5589 2.7585 2.9739 0.1027 0.5424 0.1480 683 GLU A CD 4712 O OE1 . GLU A 683 ? 2.4740 2.6790 2.8952 0.0807 0.5009 0.1602 683 GLU A OE1 4713 O OE2 . GLU A 683 ? 2.8197 2.9821 3.1604 0.1065 0.5604 0.1215 683 GLU A OE2 4714 N N . ASN A 684 ? 1.8516 2.1680 2.4770 0.0649 0.4450 0.2342 684 ASN A N 4715 C CA . ASN A 684 ? 1.8094 2.1728 2.4822 0.0392 0.4297 0.2668 684 ASN A CA 4716 C C . ASN A 684 ? 1.7665 2.1697 2.5077 0.0261 0.3924 0.2935 684 ASN A C 4717 O O . ASN A 684 ? 1.7254 2.1041 2.4363 0.0080 0.3517 0.2861 684 ASN A O 4718 C CB . ASN A 684 ? 1.7325 2.0644 2.3390 0.0117 0.4107 0.2581 684 ASN A CB 4719 C CG . ASN A 684 ? 1.6893 2.0615 2.3360 -0.0148 0.4051 0.2887 684 ASN A CG 4720 O OD1 . ASN A 684 ? 1.6421 2.0685 2.3590 -0.0098 0.4274 0.3151 684 ASN A OD1 4721 N ND2 . ASN A 684 ? 1.6657 2.0107 2.2698 -0.0431 0.3767 0.2863 684 ASN A ND2 4722 N N . PRO A 685 ? 1.6576 2.1244 2.4905 0.0344 0.4066 0.3264 685 PRO A N 4723 C CA . PRO A 685 ? 1.6169 2.1328 2.5261 0.0267 0.3756 0.3571 685 PRO A CA 4724 C C . PRO A 685 ? 1.7823 2.3185 2.6994 -0.0166 0.3293 0.3758 685 PRO A C 4725 O O . PRO A 685 ? 2.0310 2.5498 2.9086 -0.0399 0.3268 0.3705 685 PRO A O 4726 C CB . PRO A 685 ? 1.5230 2.1046 2.5248 0.0466 0.4129 0.3893 685 PRO A CB 4727 C CG . PRO A 685 ? 1.5054 2.0854 2.4823 0.0416 0.4458 0.3859 685 PRO A CG 4728 C CD . PRO A 685 ? 1.5461 2.0482 2.4163 0.0486 0.4545 0.3410 685 PRO A CD 4729 N N . GLY A 686 ? 1.8140 2.3865 2.7823 -0.0280 0.2938 0.3988 686 GLY A N 4730 C CA . GLY A 686 ? 1.7388 2.3324 2.7168 -0.0722 0.2472 0.4172 686 GLY A CA 4731 C C . GLY A 686 ? 1.6355 2.1854 2.5549 -0.0892 0.2021 0.3986 686 GLY A C 4732 O O . GLY A 686 ? 1.6453 2.1512 2.5199 -0.0665 0.2061 0.3734 686 GLY A O 4733 N N . LEU A 687 ? 1.5370 2.0982 2.4559 -0.1300 0.1597 0.4112 687 LEU A N 4734 C CA . LEU A 687 ? 1.5227 2.0352 2.3740 -0.1478 0.1204 0.3904 687 LEU A CA 4735 C C . LEU A 687 ? 1.6230 2.0688 2.3889 -0.1654 0.1189 0.3609 687 LEU A C 4736 O O . LEU A 687 ? 1.9327 2.3811 2.6979 -0.1965 0.1109 0.3689 687 LEU A O 4737 C CB . LEU A 687 ? 1.5235 2.0748 2.4068 -0.1829 0.0720 0.4155 687 LEU A CB 4738 C CG . LEU A 687 ? 1.5181 2.0778 2.4063 -0.1738 0.0453 0.4206 687 LEU A CG 4739 C CD1 . LEU A 687 ? 1.5009 2.0368 2.3369 -0.2150 -0.0042 0.4144 687 LEU A CD1 4740 C CD2 . LEU A 687 ? 1.5148 2.0269 2.3607 -0.1343 0.0675 0.3933 687 LEU A CD2 4741 N N . TRP A 688 ? 1.5603 1.9466 2.2569 -0.1456 0.1260 0.3288 688 TRP A N 4742 C CA . TRP A 688 ? 1.6003 1.9225 2.2169 -0.1556 0.1277 0.3018 688 TRP A CA 4743 C C . TRP A 688 ? 1.5799 1.8552 2.1350 -0.1697 0.0941 0.2835 688 TRP A C 4744 O O . TRP A 688 ? 1.5547 1.8229 2.1002 -0.1529 0.0858 0.2760 688 TRP A O 4745 C CB . TRP A 688 ? 1.6471 1.9414 2.2327 -0.1228 0.1670 0.2814 688 TRP A CB 4746 C CG . TRP A 688 ? 1.7569 2.0963 2.3987 -0.1097 0.2025 0.2992 688 TRP A CG 4747 C CD1 . TRP A 688 ? 1.8136 2.1828 2.4997 -0.0777 0.2312 0.3047 688 TRP A CD1 4748 C CD2 . TRP A 688 ? 1.8372 2.1972 2.4990 -0.1281 0.2154 0.3155 688 TRP A CD2 4749 N NE1 . TRP A 688 ? 1.8756 2.2827 2.6054 -0.0732 0.2634 0.3221 688 TRP A NE1 4750 C CE2 . TRP A 688 ? 1.8472 2.2521 2.5644 -0.1044 0.2537 0.3303 688 TRP A CE2 4751 C CE3 . TRP A 688 ? 1.8969 2.2388 2.5349 -0.1619 0.2003 0.3193 688 TRP A CE3 4752 C CZ2 . TRP A 688 ? 1.8156 2.2525 2.5653 -0.1135 0.2772 0.3502 688 TRP A CZ2 4753 C CZ3 . TRP A 688 ? 1.9320 2.3041 2.6042 -0.1724 0.2220 0.3396 688 TRP A CZ3 4754 C CH2 . TRP A 688 ? 1.8334 2.2548 2.5610 -0.1484 0.2598 0.3555 688 TRP A CH2 4755 N N . ILE A 689 ? 1.5236 1.7661 2.0386 -0.2013 0.0765 0.2776 689 ILE A N 4756 C CA . ILE A 689 ? 1.5126 1.7072 1.9660 -0.2192 0.0462 0.2606 689 ILE A CA 4757 C C . ILE A 689 ? 1.4780 1.6087 1.8592 -0.1978 0.0628 0.2307 689 ILE A C 4758 O O . ILE A 689 ? 1.5134 1.6082 1.8597 -0.2023 0.0760 0.2214 689 ILE A O 4759 C CB . ILE A 689 ? 1.7147 1.9031 2.1628 -0.2652 0.0199 0.2691 689 ILE A CB 4760 C CG1 . ILE A 689 ? 1.8355 1.9559 2.2027 -0.2844 -0.0038 0.2450 689 ILE A CG1 4761 C CG2 . ILE A 689 ? 1.6877 1.8863 2.1607 -0.2756 0.0416 0.2806 689 ILE A CG2 4762 C CD1 . ILE A 689 ? 1.9258 2.0474 2.2896 -0.3316 -0.0414 0.2530 689 ILE A CD1 4763 N N . LEU A 690 ? 1.5848 1.7059 1.9496 -0.1730 0.0634 0.2191 690 LEU A N 4764 C CA . LEU A 690 ? 1.6167 1.6831 1.9174 -0.1543 0.0753 0.1937 690 LEU A CA 4765 C C . LEU A 690 ? 1.6822 1.7029 1.9258 -0.1724 0.0504 0.1808 690 LEU A C 4766 O O . LEU A 690 ? 1.7072 1.7325 1.9462 -0.1748 0.0296 0.1812 690 LEU A O 4767 C CB . LEU A 690 ? 1.6099 1.6844 1.9190 -0.1211 0.0887 0.1869 690 LEU A CB 4768 C CG . LEU A 690 ? 1.6045 1.6329 1.8552 -0.1078 0.0853 0.1656 690 LEU A CG 4769 C CD1 . LEU A 690 ? 1.5928 1.5776 1.7923 -0.1036 0.1010 0.1498 690 LEU A CD1 4770 C CD2 . LEU A 690 ? 1.4724 1.5143 1.7421 -0.0809 0.0938 0.1632 690 LEU A CD2 4771 N N . GLY A 691 ? 1.7593 1.7347 1.9588 -0.1846 0.0544 0.1705 691 GLY A N 4772 C CA . GLY A 691 ? 1.8312 1.7525 1.9696 -0.1992 0.0379 0.1552 691 GLY A CA 4773 C C . GLY A 691 ? 1.8981 1.7714 1.9903 -0.1815 0.0594 0.1402 691 GLY A C 4774 O O . GLY A 691 ? 1.9482 1.8295 2.0432 -0.1533 0.0776 0.1363 691 GLY A O 4775 N N . CYS A 692 ? 1.8822 1.7054 1.9326 -0.1987 0.0571 0.1327 692 CYS A N 4776 C CA . CYS A 692 ? 1.9771 1.7585 1.9919 -0.1834 0.0783 0.1249 692 CYS A CA 4777 C C . CYS A 692 ? 2.0952 1.8474 2.1017 -0.2085 0.0799 0.1299 692 CYS A C 4778 O O . CYS A 692 ? 2.0708 1.8043 2.0671 -0.2383 0.0608 0.1281 692 CYS A O 4779 C CB . CYS A 692 ? 1.9292 1.6640 1.8899 -0.1679 0.0786 0.1081 692 CYS A CB 4780 S SG . CYS A 692 ? 1.9349 1.6221 1.8471 -0.1923 0.0560 0.0947 692 CYS A SG 4781 N N . HIS A 693 ? 2.3671 2.1148 2.3768 -0.1988 0.1016 0.1371 693 HIS A N 4782 C CA . HIS A 693 ? 2.6295 2.3428 2.6296 -0.2224 0.1045 0.1434 693 HIS A CA 4783 C C . HIS A 693 ? 2.6696 2.3066 2.6103 -0.2214 0.1079 0.1300 693 HIS A C 4784 O O . HIS A 693 ? 3.0161 2.6179 2.9421 -0.2220 0.1226 0.1359 693 HIS A O 4785 C CB . HIS A 693 ? 2.8275 2.5769 2.8692 -0.2266 0.1210 0.1639 693 HIS A CB 4786 C CG . HIS A 693 ? 2.9647 2.6978 2.9880 -0.2054 0.1461 0.1689 693 HIS A CG 4787 N ND1 . HIS A 693 ? 2.9733 2.7513 3.0258 -0.1930 0.1650 0.1823 693 HIS A ND1 4788 C CD2 . HIS A 693 ? 3.1205 2.7990 3.1004 -0.1961 0.1557 0.1652 693 HIS A CD2 4789 C CE1 . HIS A 693 ? 3.2099 2.9638 3.2345 -0.1785 0.1824 0.1865 693 HIS A CE1 4790 N NE2 . HIS A 693 ? 3.3296 3.0249 3.3137 -0.1791 0.1768 0.1780 693 HIS A NE2 4791 N N . ASN A 694 ? 2.4809 2.0940 2.3888 -0.2178 0.0956 0.1134 694 ASN A N 4792 C CA . ASN A 694 ? 2.5220 2.0644 2.3776 -0.2325 0.0901 0.0986 694 ASN A CA 4793 C C . ASN A 694 ? 2.6505 2.2049 2.5198 -0.2727 0.0641 0.0991 694 ASN A C 4794 O O . ASN A 694 ? 2.6634 2.2713 2.5626 -0.2762 0.0475 0.1032 694 ASN A O 4795 C CB . ASN A 694 ? 2.5219 2.0406 2.3368 -0.2120 0.0889 0.0816 694 ASN A CB 4796 C CG . ASN A 694 ? 2.7129 2.2469 2.5303 -0.1722 0.1081 0.0846 694 ASN A CG 4797 O OD1 . ASN A 694 ? 2.7617 2.3472 2.6177 -0.1592 0.1142 0.0962 694 ASN A OD1 4798 N ND2 . ASN A 694 ? 2.7219 2.2116 2.4972 -0.1533 0.1178 0.0739 694 ASN A ND2 4799 N N . SER A 695 ? 2.9300 2.4379 2.7816 -0.3041 0.0596 0.0974 695 SER A N 4800 C CA . SER A 695 ? 2.9508 2.4691 2.8124 -0.3480 0.0306 0.0980 695 SER A CA 4801 C C . SER A 695 ? 3.0021 2.4492 2.7955 -0.3704 0.0157 0.0735 695 SER A C 4802 O O . SER A 695 ? 3.0527 2.5023 2.8421 -0.4099 -0.0121 0.0708 695 SER A O 4803 C CB . SER A 695 ? 2.8305 2.3677 2.7362 -0.3766 0.0301 0.1178 695 SER A CB 4804 O OG . SER A 695 ? 2.5163 2.1418 2.4920 -0.3704 0.0286 0.1397 695 SER A OG 4805 N N . ASP A 696 ? 2.9835 2.3684 2.7229 -0.3448 0.0352 0.0566 696 ASP A N 4806 C CA . ASP A 696 ? 2.8898 2.2203 2.5625 -0.3491 0.0277 0.0318 696 ASP A CA 4807 C C . ASP A 696 ? 2.6685 2.0604 2.3549 -0.3504 0.0033 0.0330 696 ASP A C 4808 O O . ASP A 696 ? 2.5470 1.9583 2.2379 -0.3878 -0.0263 0.0342 696 ASP A O 4809 C CB . ASP A 696 ? 3.1276 2.4073 2.7607 -0.3077 0.0585 0.0213 696 ASP A CB 4810 C CG . ASP A 696 ? 3.2614 2.5927 2.9419 -0.2670 0.0791 0.0403 696 ASP A CG 4811 O OD1 . ASP A 696 ? 3.1995 2.5649 2.9265 -0.2711 0.0833 0.0590 696 ASP A OD1 4812 O OD2 . ASP A 696 ? 3.1910 2.5282 2.8600 -0.2322 0.0915 0.0369 696 ASP A OD2 4813 N N . PHE A 697 ? 2.4313 1.8563 2.1282 -0.3111 0.0147 0.0356 697 PHE A N 4814 C CA . PHE A 697 ? 2.2720 1.7483 1.9791 -0.3073 -0.0046 0.0378 697 PHE A CA 4815 C C . PHE A 697 ? 2.2297 1.7753 1.9938 -0.3353 -0.0321 0.0565 697 PHE A C 4816 O O . PHE A 697 ? 2.2936 1.8435 2.0402 -0.3653 -0.0602 0.0535 697 PHE A O 4817 C CB . PHE A 697 ? 2.2001 1.7130 1.9293 -0.2619 0.0129 0.0437 697 PHE A CB 4818 C CG . PHE A 697 ? 2.3479 1.8059 2.0315 -0.2314 0.0395 0.0306 697 PHE A CG 4819 C CD1 . PHE A 697 ? 2.5048 1.9062 2.1222 -0.2327 0.0407 0.0113 697 PHE A CD1 4820 C CD2 . PHE A 697 ? 2.4883 1.9536 2.1954 -0.2008 0.0642 0.0393 697 PHE A CD2 4821 C CE1 . PHE A 697 ? 2.6232 1.9778 2.2054 -0.2019 0.0683 0.0026 697 PHE A CE1 4822 C CE2 . PHE A 697 ? 2.4599 1.8814 2.1324 -0.1724 0.0878 0.0321 697 PHE A CE2 4823 C CZ . PHE A 697 ? 2.4989 1.8662 2.1125 -0.1717 0.0910 0.0146 697 PHE A CZ 4824 N N . ARG A 698 ? 2.2432 1.8419 2.0738 -0.3264 -0.0234 0.0767 698 ARG A N 4825 C CA . ARG A 698 ? 2.2772 1.9601 2.1777 -0.3342 -0.0408 0.0994 698 ARG A CA 4826 C C . ARG A 698 ? 2.3682 2.0751 2.2845 -0.3810 -0.0754 0.1089 698 ARG A C 4827 O O . ARG A 698 ? 2.4132 2.1931 2.3984 -0.3881 -0.0870 0.1329 698 ARG A O 4828 C CB . ARG A 698 ? 2.2832 2.0125 2.2466 -0.3129 -0.0185 0.1174 698 ARG A CB 4829 C CG . ARG A 698 ? 2.3998 2.1258 2.3875 -0.3371 -0.0136 0.1284 698 ARG A CG 4830 C CD . ARG A 698 ? 2.4480 2.2430 2.5085 -0.3220 0.0012 0.1512 698 ARG A CD 4831 N NE . ARG A 698 ? 2.6998 2.5225 2.8046 -0.3554 -0.0068 0.1703 698 ARG A NE 4832 C CZ . ARG A 698 ? 2.7968 2.6808 2.9556 -0.3780 -0.0292 0.1895 698 ARG A CZ 4833 N NH1 . ARG A 698 ? 2.4829 2.4065 2.6577 -0.3702 -0.0466 0.1929 698 ARG A NH1 4834 N NH2 . ARG A 698 ? 2.9931 2.9012 3.1937 -0.4089 -0.0343 0.2084 698 ARG A NH2 4835 N N . ASN A 699 ? 2.3864 2.0328 2.2395 -0.4128 -0.0914 0.0907 699 ASN A N 4836 C CA . ASN A 699 ? 2.3381 2.0046 2.1897 -0.4583 -0.1305 0.0960 699 ASN A CA 4837 C C . ASN A 699 ? 2.3931 2.0039 2.1590 -0.4691 -0.1448 0.0712 699 ASN A C 4838 O O . ASN A 699 ? 2.5788 2.1674 2.3082 -0.5137 -0.1737 0.0637 699 ASN A O 4839 C CB . ASN A 699 ? 2.3951 2.0487 2.2613 -0.5026 -0.1418 0.1019 699 ASN A CB 4840 C CG . ASN A 699 ? 2.4367 1.9900 2.2351 -0.5108 -0.1238 0.0764 699 ASN A CG 4841 O OD1 . ASN A 699 ? 2.3142 1.8274 2.0900 -0.4729 -0.0906 0.0656 699 ASN A OD1 4842 N ND2 . ASN A 699 ? 2.5371 2.0491 2.3043 -0.5613 -0.1459 0.0678 699 ASN A ND2 4843 N N . ARG A 700 ? 2.3308 1.9174 2.0627 -0.4289 -0.1228 0.0582 700 ARG A N 4844 C CA . ARG A 700 ? 2.3421 1.8967 2.0049 -0.4279 -0.1321 0.0407 700 ARG A CA 4845 C C . ARG A 700 ? 2.2967 1.9285 2.0079 -0.4008 -0.1384 0.0612 700 ARG A C 4846 O O . ARG A 700 ? 2.3713 1.9909 2.0458 -0.3779 -0.1321 0.0528 700 ARG A O 4847 C CB . ARG A 700 ? 2.4117 1.8841 2.0074 -0.3995 -0.0984 0.0145 700 ARG A CB 4848 C CG . ARG A 700 ? 2.5664 1.9527 2.1126 -0.4201 -0.0864 -0.0058 700 ARG A CG 4849 C CD . ARG A 700 ? 2.7553 2.0773 2.2631 -0.3805 -0.0461 -0.0216 700 ARG A CD 4850 N NE . ARG A 700 ? 3.2009 2.4248 2.6415 -0.3997 -0.0348 -0.0457 700 ARG A NE 4851 C CZ . ARG A 700 ? 3.4807 2.6609 2.9286 -0.3949 -0.0119 -0.0459 700 ARG A CZ 4852 N NH1 . ARG A 700 ? 3.4812 2.7085 2.9973 -0.3722 0.0020 -0.0234 700 ARG A NH1 4853 N NH2 . ARG A 700 ? 3.5950 2.6800 2.9783 -0.4130 -0.0018 -0.0687 700 ARG A NH2 4854 N N . GLY A 701 ? 2.1405 1.8503 1.9359 -0.4043 -0.1498 0.0892 701 GLY A N 4855 C CA . GLY A 701 ? 1.9540 1.7337 1.8133 -0.3704 -0.1441 0.1105 701 GLY A CA 4856 C C . GLY A 701 ? 1.9389 1.7118 1.8258 -0.3339 -0.1066 0.1084 701 GLY A C 4857 O O . GLY A 701 ? 1.9141 1.6459 1.7863 -0.3404 -0.0916 0.0988 701 GLY A O 4858 N N . MET A 702 ? 1.9389 1.7496 1.8631 -0.2970 -0.0920 0.1177 702 MET A N 4859 C CA . MET A 702 ? 1.9210 1.7227 1.8600 -0.2611 -0.0575 0.1131 702 MET A CA 4860 C C . MET A 702 ? 1.8114 1.6631 1.8231 -0.2565 -0.0469 0.1315 702 MET A C 4861 O O . MET A 702 ? 1.8303 1.6636 1.8439 -0.2466 -0.0238 0.1275 702 MET A O 4862 C CB . MET A 702 ? 1.9347 1.6608 1.8114 -0.2563 -0.0374 0.0906 702 MET A CB 4863 C CG . MET A 702 ? 1.8889 1.6096 1.7762 -0.2194 -0.0059 0.0883 702 MET A CG 4864 S SD . MET A 702 ? 1.8984 1.6013 1.7515 -0.1839 0.0072 0.0775 702 MET A SD 4865 C CE . MET A 702 ? 2.1016 1.7259 1.8930 -0.1790 0.0284 0.0596 702 MET A CE 4866 N N . THR A 703 ? 1.6433 1.5596 1.7149 -0.2630 -0.0625 0.1537 703 THR A N 4867 C CA . THR A 703 ? 1.6500 1.6177 1.7930 -0.2489 -0.0461 0.1715 703 THR A CA 4868 C C . THR A 703 ? 1.7698 1.8001 1.9706 -0.2361 -0.0549 0.1922 703 THR A C 4869 O O . THR A 703 ? 1.9092 1.9539 2.1040 -0.2491 -0.0818 0.1996 703 THR A O 4870 C CB . THR A 703 ? 1.6778 1.6643 1.8542 -0.2791 -0.0517 0.1848 703 THR A CB 4871 O OG1 . THR A 703 ? 1.8449 1.8497 2.0244 -0.3161 -0.0877 0.1953 703 THR A OG1 4872 C CG2 . THR A 703 ? 1.7724 1.6983 1.9028 -0.2875 -0.0365 0.1682 703 THR A CG2 4873 N N . ALA A 704 ? 1.7424 1.8075 1.9970 -0.2100 -0.0307 0.2019 704 ALA A N 4874 C CA . ALA A 704 ? 1.5976 1.7226 1.9192 -0.1940 -0.0318 0.2242 704 ALA A CA 4875 C C . ALA A 704 ? 1.5558 1.7270 1.9460 -0.1912 -0.0137 0.2425 704 ALA A C 4876 O O . ALA A 704 ? 1.5307 1.6841 1.9102 -0.1989 0.0014 0.2359 704 ALA A O 4877 C CB . ALA A 704 ? 1.4918 1.6027 1.8030 -0.1578 -0.0136 0.2133 704 ALA A CB 4878 N N . LEU A 705 ? 1.5672 1.7984 2.0294 -0.1797 -0.0137 0.2677 705 LEU A N 4879 C CA . LEU A 705 ? 1.6050 1.8831 2.1368 -0.1714 0.0092 0.2865 705 LEU A CA 4880 C C . LEU A 705 ? 1.6071 1.8955 2.1693 -0.1293 0.0415 0.2851 705 LEU A C 4881 O O . LEU A 705 ? 1.7827 2.0617 2.3361 -0.1114 0.0373 0.2809 705 LEU A O 4882 C CB . LEU A 705 ? 1.7513 2.0964 2.3522 -0.1961 -0.0154 0.3217 705 LEU A CB 4883 C CG . LEU A 705 ? 1.9497 2.2793 2.5140 -0.2433 -0.0512 0.3207 705 LEU A CG 4884 C CD1 . LEU A 705 ? 2.0388 2.3666 2.5759 -0.2568 -0.0884 0.3230 705 LEU A CD1 4885 C CD2 . LEU A 705 ? 1.9961 2.3797 2.6228 -0.2734 -0.0613 0.3491 705 LEU A CD2 4886 N N . LEU A 706 ? 1.4746 1.7787 2.0690 -0.1146 0.0749 0.2877 706 LEU A N 4887 C CA . LEU A 706 ? 1.4126 1.7152 2.0242 -0.0764 0.1100 0.2803 706 LEU A CA 4888 C C . LEU A 706 ? 1.4830 1.8443 2.1776 -0.0642 0.1342 0.3064 706 LEU A C 4889 O O . LEU A 706 ? 1.6134 1.9855 2.3175 -0.0718 0.1521 0.3098 706 LEU A O 4890 C CB . LEU A 706 ? 1.3897 1.6386 1.9363 -0.0679 0.1335 0.2498 706 LEU A CB 4891 C CG . LEU A 706 ? 1.3886 1.6135 1.9192 -0.0351 0.1671 0.2302 706 LEU A CG 4892 C CD1 . LEU A 706 ? 1.4841 1.6585 1.9410 -0.0403 0.1737 0.2049 706 LEU A CD1 4893 C CD2 . LEU A 706 ? 1.3587 1.6185 1.9443 -0.0152 0.2033 0.2413 706 LEU A CD2 4894 N N . LYS A 707 ? 1.4733 1.8733 2.2300 -0.0445 0.1365 0.3271 707 LYS A N 4895 C CA . LYS A 707 ? 1.5626 2.0201 2.4045 -0.0280 0.1637 0.3542 707 LYS A CA 4896 C C . LYS A 707 ? 1.6383 2.0720 2.4780 0.0112 0.2110 0.3361 707 LYS A C 4897 O O . LYS A 707 ? 1.6380 2.0360 2.4523 0.0318 0.2154 0.3189 707 LYS A O 4898 C CB . LYS A 707 ? 1.6606 2.1828 2.5844 -0.0287 0.1416 0.3942 707 LYS A CB 4899 C CG . LYS A 707 ? 1.7911 2.3841 2.8121 -0.0182 0.1657 0.4296 707 LYS A CG 4900 C CD . LYS A 707 ? 1.9128 2.5781 3.0237 -0.0182 0.1427 0.4753 707 LYS A CD 4901 C CE . LYS A 707 ? 2.0515 2.7102 3.1855 0.0179 0.1515 0.4797 707 LYS A CE 4902 N NZ . LYS A 707 ? 2.0771 2.7013 3.2111 0.0615 0.2056 0.4591 707 LYS A NZ 4903 N N . VAL A 708 ? 1.5992 2.0511 2.4628 0.0190 0.2463 0.3398 708 VAL A N 4904 C CA . VAL A 708 ? 1.5495 1.9788 2.4063 0.0532 0.2950 0.3215 708 VAL A CA 4905 C C . VAL A 708 ? 1.5315 2.0223 2.4842 0.0744 0.3248 0.3539 708 VAL A C 4906 O O . VAL A 708 ? 1.4585 1.9944 2.4511 0.0614 0.3323 0.3759 708 VAL A O 4907 C CB . VAL A 708 ? 1.4587 1.8542 2.2525 0.0462 0.3172 0.2971 708 VAL A CB 4908 C CG1 . VAL A 708 ? 1.4459 1.7771 2.1677 0.0657 0.3372 0.2581 708 VAL A CG1 4909 C CG2 . VAL A 708 ? 1.4290 1.8130 2.1802 0.0084 0.2820 0.2957 708 VAL A CG2 4910 N N . SER A 709 ? 1.5181 2.0111 2.5106 0.1070 0.3429 0.3588 709 SER A N 4911 C CA . SER A 709 ? 1.5672 2.1158 2.6547 0.1337 0.3774 0.3903 709 SER A CA 4912 C C . SER A 709 ? 1.6694 2.1914 2.7755 0.1782 0.4188 0.3799 709 SER A C 4913 O O . SER A 709 ? 1.8409 2.3082 2.8986 0.1863 0.4110 0.3545 709 SER A O 4914 C CB . SER A 709 ? 1.6028 2.2259 2.7755 0.1185 0.3421 0.4381 709 SER A CB 4915 O OG . SER A 709 ? 1.8747 2.5638 3.1343 0.1299 0.3720 0.4719 709 SER A OG 4916 N N . SER A 710 ? 1.6273 2.1887 2.8072 0.2065 0.4632 0.4014 710 SER A N 4917 C CA . SER A 710 ? 1.6604 2.1914 2.8583 0.2517 0.5144 0.3896 710 SER A CA 4918 C C . SER A 710 ? 1.7544 2.2812 2.9986 0.2751 0.5056 0.4044 710 SER A C 4919 O O . SER A 710 ? 1.8989 2.4907 3.2300 0.2760 0.4845 0.4502 710 SER A O 4920 C CB . SER A 710 ? 1.5816 2.1624 2.8533 0.2763 0.5664 0.4138 710 SER A CB 4921 O OG . SER A 710 ? 1.4776 2.0884 2.7356 0.2495 0.5646 0.4188 710 SER A OG 4922 N N . CYS A 711 ? 1.8303 2.2820 3.0193 0.2943 0.5240 0.3675 711 CYS A N 4923 C CA . CYS A 711 ? 2.0024 2.4365 3.2254 0.3168 0.5188 0.3773 711 CYS A CA 4924 C C . CYS A 711 ? 2.1167 2.5232 3.3767 0.3634 0.5802 0.3717 711 CYS A C 4925 O O . CYS A 711 ? 2.2093 2.6389 3.5024 0.3816 0.6255 0.3775 711 CYS A O 4926 C CB . CYS A 711 ? 2.1410 2.5074 3.2738 0.2990 0.4870 0.3414 711 CYS A CB 4927 S SG . CYS A 711 ? 2.5101 2.8836 3.5689 0.2480 0.4353 0.3297 711 CYS A SG 4928 N N . ASP A 712 ? 2.1409 2.4963 3.3950 0.3826 0.5833 0.3609 712 ASP A N 4929 C CA . ASP A 712 ? 2.3007 2.6165 3.5862 0.4276 0.6418 0.3529 712 ASP A CA 4930 C C . ASP A 712 ? 2.5427 2.7678 3.7744 0.4386 0.6480 0.3174 712 ASP A C 4931 O O . ASP A 712 ? 2.6930 2.8955 3.9766 0.4754 0.6824 0.3268 712 ASP A O 4932 C CB . ASP A 712 ? 2.1022 2.4902 3.5189 0.4588 0.6577 0.4112 712 ASP A CB 4933 C CG . ASP A 712 ? 2.0841 2.5184 3.5521 0.4776 0.7063 0.4261 712 ASP A CG 4934 O OD1 . ASP A 712 ? 2.0531 2.5552 3.5406 0.4522 0.6848 0.4483 712 ASP A OD1 4935 O OD2 . ASP A 712 ? 2.0648 2.4650 3.5524 0.5177 0.7681 0.4151 712 ASP A OD2 4936 N N . LYS A 713 ? 2.5880 2.7616 3.7200 0.4077 0.6172 0.2782 713 LYS A N 4937 C CA . LYS A 713 ? 2.5718 2.6595 3.6444 0.4105 0.6184 0.2421 713 LYS A CA 4938 C C . LYS A 713 ? 2.8504 2.8927 3.9654 0.4531 0.6703 0.2394 713 LYS A C 4939 O O . LYS A 713 ? 3.1734 3.1552 4.2689 0.4588 0.6681 0.2242 713 LYS A O 4940 C CB . LYS A 713 ? 2.4558 2.4819 3.4115 0.3866 0.6201 0.1862 713 LYS A CB 4941 C CG . LYS A 713 ? 2.2553 2.3094 3.1573 0.3458 0.5720 0.1828 713 LYS A CG 4942 C CD . LYS A 713 ? 2.1292 2.1578 2.9908 0.3233 0.5241 0.1761 713 LYS A CD 4943 C CE . LYS A 713 ? 1.9701 2.0566 2.9013 0.3200 0.4851 0.2236 713 LYS A CE 4944 N NZ . LYS A 713 ? 1.9266 1.9893 2.8061 0.2950 0.4399 0.2144 713 LYS A NZ 4945 N N . LYS B 46 ? 2.6031 2.7151 3.0675 0.1445 0.4799 -0.1248 1693 LYS B N 4946 C CA . LYS B 46 ? 2.4779 2.5773 2.9206 0.1098 0.4518 -0.0980 1693 LYS B CA 4947 C C . LYS B 46 ? 2.2273 2.3719 2.7118 0.0972 0.4430 -0.0558 1693 LYS B C 4948 O O . LYS B 46 ? 1.9910 2.1668 2.5341 0.1150 0.4495 -0.0424 1693 LYS B O 4949 C CB . LYS B 46 ? 2.5818 2.6181 3.0151 0.1024 0.4277 -0.1054 1693 LYS B CB 4950 C CG . LYS B 46 ? 2.5610 2.5545 2.9407 0.0991 0.4271 -0.1412 1693 LYS B CG 4951 C CD . LYS B 46 ? 2.6040 2.5733 2.9942 0.1278 0.4429 -0.1796 1693 LYS B CD 4952 C CE . LYS B 46 ? 2.4509 2.4140 2.7830 0.1295 0.4549 -0.2174 1693 LYS B CE 4953 N NZ . LYS B 46 ? 2.1882 2.1515 2.5275 0.1614 0.4801 -0.2535 1693 LYS B NZ 4954 N N . LYS B 47 ? 2.1869 2.3333 2.6411 0.0664 0.4270 -0.0358 1694 LYS B N 4955 C CA . LYS B 47 ? 2.1447 2.3393 2.6225 0.0486 0.4228 -0.0017 1694 LYS B CA 4956 C C . LYS B 47 ? 2.0683 2.2604 2.5762 0.0330 0.3940 0.0283 1694 LYS B C 4957 O O . LYS B 47 ? 2.0746 2.2218 2.5726 0.0302 0.3746 0.0267 1694 LYS B O 4958 C CB . LYS B 47 ? 2.1795 2.3784 2.6046 0.0233 0.4243 0.0025 1694 LYS B CB 4959 C CG . LYS B 47 ? 2.2103 2.4267 2.6034 0.0349 0.4528 -0.0185 1694 LYS B CG 4960 C CD . LYS B 47 ? 2.1651 2.4242 2.5491 0.0159 0.4628 0.0043 1694 LYS B CD 4961 C CE . LYS B 47 ? 2.1385 2.4432 2.5245 0.0363 0.4981 -0.0059 1694 LYS B CE 4962 N NZ . LYS B 47 ? 2.0936 2.4535 2.4971 0.0203 0.5105 0.0246 1694 LYS B NZ 4963 N N . THR B 48 ? 1.9881 2.2313 2.5317 0.0218 0.3914 0.0562 1695 THR B N 4964 C CA . THR B 48 ? 1.8025 2.0505 2.3623 -0.0013 0.3618 0.0858 1695 THR B CA 4965 C C . THR B 48 ? 1.6426 1.8871 2.1591 -0.0358 0.3524 0.0959 1695 THR B C 4966 O O . THR B 48 ? 1.5684 1.8566 2.1004 -0.0481 0.3607 0.1102 1695 THR B O 4967 C CB . THR B 48 ? 1.7743 2.0838 2.4082 0.0061 0.3601 0.1116 1695 THR B CB 4968 O OG1 . THR B 48 ? 1.7529 2.0679 2.4312 0.0423 0.3733 0.1025 1695 THR B OG1 4969 C CG2 . THR B 48 ? 1.6795 1.9902 2.3260 -0.0167 0.3251 0.1392 1695 THR B CG2 4970 N N . ARG B 49 ? 1.6979 1.8897 2.1623 -0.0509 0.3362 0.0892 1696 ARG B N 4971 C CA . ARG B 49 ? 1.7842 1.9654 2.2120 -0.0826 0.3229 0.1010 1696 ARG B CA 4972 C C . ARG B 49 ? 1.8051 2.0144 2.2689 -0.1004 0.3004 0.1282 1696 ARG B C 4973 O O . ARG B 49 ? 1.7831 1.9959 2.2781 -0.0918 0.2850 0.1373 1696 ARG B O 4974 C CB . ARG B 49 ? 1.7813 1.9017 2.1518 -0.0915 0.3099 0.0896 1696 ARG B CB 4975 C CG . ARG B 49 ? 1.8396 1.9301 2.1798 -0.0738 0.3253 0.0624 1696 ARG B CG 4976 C CD . ARG B 49 ? 1.8849 1.9860 2.1942 -0.0760 0.3455 0.0524 1696 ARG B CD 4977 N NE . ARG B 49 ? 1.9082 1.9792 2.1834 -0.0621 0.3545 0.0257 1696 ARG B NE 4978 C CZ . ARG B 49 ? 1.9903 2.0763 2.2645 -0.0426 0.3760 0.0056 1696 ARG B CZ 4979 N NH1 . ARG B 49 ? 2.0822 2.2150 2.3877 -0.0319 0.3951 0.0097 1696 ARG B NH1 4980 N NH2 . ARG B 49 ? 1.9814 2.0368 2.2220 -0.0341 0.3785 -0.0194 1696 ARG B NH2 4981 N N . HIS B 50 ? 1.8266 2.0559 2.2864 -0.1260 0.2975 0.1420 1697 HIS B N 4982 C CA . HIS B 50 ? 1.7765 2.0405 2.2742 -0.1462 0.2765 0.1666 1697 HIS B CA 4983 C C . HIS B 50 ? 1.7468 1.9807 2.1989 -0.1799 0.2619 0.1707 1697 HIS B C 4984 O O . HIS B 50 ? 1.7710 1.9949 2.1939 -0.1881 0.2779 0.1656 1697 HIS B O 4985 C CB . HIS B 50 ? 1.9238 2.2573 2.4814 -0.1414 0.2951 0.1800 1697 HIS B CB 4986 C CG . HIS B 50 ? 1.8986 2.2826 2.5190 -0.1496 0.2752 0.2049 1697 HIS B CG 4987 N ND1 . HIS B 50 ? 1.8786 2.3251 2.5691 -0.1282 0.2895 0.2155 1697 HIS B ND1 4988 C CD2 . HIS B 50 ? 1.8215 2.2055 2.4454 -0.1764 0.2414 0.2211 1697 HIS B CD2 4989 C CE1 . HIS B 50 ? 1.8881 2.3741 2.6268 -0.1419 0.2641 0.2395 1697 HIS B CE1 4990 N NE2 . HIS B 50 ? 1.8552 2.3038 2.5525 -0.1721 0.2336 0.2425 1697 HIS B NE2 4991 N N . TYR B 51 ? 1.7967 2.0134 2.2393 -0.1985 0.2317 0.1796 1698 TYR B N 4992 C CA . TYR B 51 ? 1.8937 2.0731 2.2887 -0.2288 0.2175 0.1796 1698 TYR B CA 4993 C C . TYR B 51 ? 1.9586 2.1633 2.3793 -0.2576 0.1902 0.1981 1698 TYR B C 4994 O O . TYR B 51 ? 2.0557 2.2723 2.4950 -0.2567 0.1669 0.2064 1698 TYR B O 4995 C CB . TYR B 51 ? 1.8566 1.9710 2.1897 -0.2251 0.2088 0.1643 1698 TYR B CB 4996 C CG . TYR B 51 ? 1.7604 1.8465 2.0607 -0.2063 0.2335 0.1458 1698 TYR B CG 4997 C CD1 . TYR B 51 ? 1.7969 1.8602 2.0595 -0.2175 0.2452 0.1405 1698 TYR B CD1 4998 C CD2 . TYR B 51 ? 1.7265 1.8094 2.0358 -0.1778 0.2443 0.1343 1698 TYR B CD2 4999 C CE1 . TYR B 51 ? 1.8030 1.8456 2.0359 -0.2006 0.2652 0.1249 1698 TYR B CE1 5000 C CE2 . TYR B 51 ? 1.6694 1.7289 1.9492 -0.1629 0.2640 0.1158 1698 TYR B CE2 5001 C CZ . TYR B 51 ? 1.6902 1.7321 1.9312 -0.1743 0.2737 0.1115 1698 TYR B CZ 5002 O OH . TYR B 51 ? 1.5884 1.6116 1.7997 -0.1600 0.2904 0.0945 1698 TYR B OH 5003 N N . PHE B 52 ? 1.7750 1.9894 2.1985 -0.2837 0.1924 0.2058 1699 PHE B N 5004 C CA . PHE B 52 ? 1.6358 1.8620 2.0735 -0.3174 0.1631 0.2193 1699 PHE B CA 5005 C C . PHE B 52 ? 1.5831 1.7389 1.9502 -0.3368 0.1475 0.2062 1699 PHE B C 5006 O O . PHE B 52 ? 1.5248 1.6460 1.8578 -0.3479 0.1600 0.2003 1699 PHE B O 5007 C CB . PHE B 52 ? 1.6611 1.9393 2.1500 -0.3379 0.1715 0.2373 1699 PHE B CB 5008 C CG . PHE B 52 ? 1.7235 2.0788 2.2889 -0.3189 0.1838 0.2524 1699 PHE B CG 5009 C CD1 . PHE B 52 ? 1.8058 2.1828 2.3993 -0.2959 0.1725 0.2545 1699 PHE B CD1 5010 C CD2 . PHE B 52 ? 1.7753 2.1817 2.3853 -0.3219 0.2089 0.2659 1699 PHE B CD2 5011 C CE1 . PHE B 52 ? 1.9237 2.3705 2.5905 -0.2749 0.1857 0.2683 1699 PHE B CE1 5012 C CE2 . PHE B 52 ? 1.8192 2.2990 2.5012 -0.3014 0.2236 0.2793 1699 PHE B CE2 5013 C CZ . PHE B 52 ? 1.9243 2.4236 2.6358 -0.2771 0.2118 0.2797 1699 PHE B CZ 5014 N N . ILE B 53 ? 1.5265 1.6613 1.8709 -0.3371 0.1218 0.2024 1700 ILE B N 5015 C CA . ILE B 53 ? 1.5660 1.6348 1.8407 -0.3503 0.1065 0.1883 1700 ILE B CA 5016 C C . ILE B 53 ? 1.7121 1.7924 1.9924 -0.3775 0.0691 0.1959 1700 ILE B C 5017 O O . ILE B 53 ? 1.7188 1.8520 2.0485 -0.3738 0.0542 0.2109 1700 ILE B O 5018 C CB . ILE B 53 ? 1.4407 1.4742 1.6762 -0.3223 0.1117 0.1761 1700 ILE B CB 5019 C CG1 . ILE B 53 ? 1.3936 1.3654 1.5674 -0.3186 0.1277 0.1587 1700 ILE B CG1 5020 C CG2 . ILE B 53 ? 1.4671 1.4927 1.6841 -0.3274 0.0813 0.1789 1700 ILE B CG2 5021 C CD1 . ILE B 53 ? 1.3393 1.2819 1.4816 -0.2926 0.1344 0.1486 1700 ILE B CD1 5022 N N . ALA B 54 ? 1.8113 1.8420 2.0415 -0.4039 0.0536 0.1852 1701 ALA B N 5023 C CA . ALA B 54 ? 1.7949 1.8260 2.0159 -0.4328 0.0153 0.1868 1701 ALA B CA 5024 C C . ALA B 54 ? 1.7911 1.7467 1.9277 -0.4387 0.0057 0.1654 1701 ALA B C 5025 O O . ALA B 54 ? 1.6967 1.6048 1.7918 -0.4228 0.0299 0.1524 1701 ALA B O 5026 C CB . ALA B 54 ? 1.7382 1.7968 2.0005 -0.4692 0.0037 0.1970 1701 ALA B CB 5027 N N . ALA B 55 ? 1.8216 1.7693 1.9333 -0.4604 -0.0292 0.1618 1702 ALA B N 5028 C CA . ALA B 55 ? 1.8331 1.7110 1.8616 -0.4676 -0.0404 0.1399 1702 ALA B CA 5029 C C . ALA B 55 ? 1.9652 1.8131 1.9758 -0.5078 -0.0615 0.1292 1702 ALA B C 5030 O O . ALA B 55 ? 2.0887 1.9710 2.1256 -0.5349 -0.0940 0.1363 1702 ALA B O 5031 C CB . ALA B 55 ? 1.7818 1.6686 1.7834 -0.4587 -0.0639 0.1418 1702 ALA B CB 5032 N N . VAL B 56 ? 2.0899 1.8736 2.0580 -0.5119 -0.0442 0.1126 1703 VAL B N 5033 C CA . VAL B 56 ? 2.2369 1.9843 2.1943 -0.5501 -0.0591 0.1028 1703 VAL B CA 5034 C C . VAL B 56 ? 2.3321 1.9994 2.2033 -0.5577 -0.0704 0.0742 1703 VAL B C 5035 O O . VAL B 56 ? 2.4956 2.1285 2.3150 -0.5290 -0.0543 0.0629 1703 VAL B O 5036 C CB . VAL B 56 ? 2.1971 1.9314 2.1811 -0.5524 -0.0295 0.1094 1703 VAL B CB 5037 C CG1 . VAL B 56 ? 2.1967 2.0120 2.2682 -0.5555 -0.0222 0.1368 1703 VAL B CG1 5038 C CG2 . VAL B 56 ? 2.0455 1.7363 1.9881 -0.5173 0.0056 0.1005 1703 VAL B CG2 5039 N N . GLU B 57 ? 2.2348 1.8728 2.0923 -0.5965 -0.0973 0.0622 1704 GLU B N 5040 C CA . GLU B 57 ? 2.2485 1.8017 2.0228 -0.6061 -0.1065 0.0310 1704 GLU B CA 5041 C C . GLU B 57 ? 2.2444 1.7348 2.0104 -0.6149 -0.0851 0.0229 1704 GLU B C 5042 O O . GLU B 57 ? 2.2088 1.7183 2.0306 -0.6397 -0.0858 0.0376 1704 GLU B O 5043 C CB . GLU B 57 ? 2.4295 1.9821 2.1853 -0.6437 -0.1530 0.0183 1704 GLU B CB 5044 C CG . GLU B 57 ? 2.6326 2.2248 2.3660 -0.6327 -0.1769 0.0202 1704 GLU B CG 5045 C CD . GLU B 57 ? 2.8715 2.4599 2.5761 -0.6709 -0.2261 0.0049 1704 GLU B CD 5046 O OE1 . GLU B 57 ? 3.0804 2.6168 2.7646 -0.7052 -0.2413 -0.0158 1704 GLU B OE1 5047 O OE2 . GLU B 57 ? 2.7695 2.4058 2.4704 -0.6671 -0.2512 0.0137 1704 GLU B OE2 5048 N N . ARG B 58 ? 2.2646 1.6829 1.9638 -0.5936 -0.0651 0.0022 1705 ARG B N 5049 C CA . ARG B 58 ? 2.2525 1.6034 1.9367 -0.5953 -0.0426 -0.0053 1705 ARG B CA 5050 C C . ARG B 58 ? 2.4384 1.6960 2.0384 -0.5969 -0.0473 -0.0399 1705 ARG B C 5051 O O . ARG B 58 ? 2.6123 1.8571 2.1578 -0.5929 -0.0641 -0.0595 1705 ARG B O 5052 C CB . ARG B 58 ? 2.0939 1.4532 1.7896 -0.5556 -0.0018 0.0087 1705 ARG B CB 5053 C CG . ARG B 58 ? 2.1742 1.6014 1.9472 -0.5528 0.0143 0.0397 1705 ARG B CG 5054 C CD . ARG B 58 ? 2.2119 1.6403 1.9812 -0.5122 0.0515 0.0473 1705 ARG B CD 5055 N NE . ARG B 58 ? 2.2784 1.6263 1.9898 -0.5001 0.0663 0.0296 1705 ARG B NE 5056 C CZ . ARG B 58 ? 2.4284 1.7415 2.1440 -0.4981 0.0867 0.0365 1705 ARG B CZ 5057 N NH1 . ARG B 58 ? 2.5782 1.9309 2.3499 -0.5074 0.0968 0.0613 1705 ARG B NH1 5058 N NH2 . ARG B 58 ? 2.4630 1.7024 2.1262 -0.4851 0.0983 0.0199 1705 ARG B NH2 5059 N N . LEU B 59 ? 2.4736 1.6658 2.0627 -0.6014 -0.0311 -0.0464 1706 LEU B N 5060 C CA . LEU B 59 ? 2.5312 1.6339 2.0441 -0.5863 -0.0201 -0.0759 1706 LEU B CA 5061 C C . LEU B 59 ? 2.5230 1.6253 2.0244 -0.5382 0.0191 -0.0679 1706 LEU B C 5062 O O . LEU B 59 ? 2.4173 1.5566 1.9698 -0.5260 0.0407 -0.0418 1706 LEU B O 5063 C CB . LEU B 59 ? 2.5821 1.6081 2.0904 -0.6133 -0.0220 -0.0864 1706 LEU B CB 5064 C CG . LEU B 59 ? 2.6122 1.5643 2.0569 -0.6392 -0.0502 -0.1249 1706 LEU B CG 5065 C CD1 . LEU B 59 ? 2.5603 1.5697 2.0266 -0.6752 -0.0923 -0.1244 1706 LEU B CD1 5066 C CD2 . LEU B 59 ? 2.5658 1.4254 1.9994 -0.6600 -0.0471 -0.1383 1706 LEU B CD2 5067 N N . TRP B 60 ? 2.5864 1.6503 2.0209 -0.5118 0.0278 -0.0901 1707 TRP B N 5068 C CA . TRP B 60 ? 2.5771 1.6287 1.9955 -0.4679 0.0646 -0.0862 1707 TRP B CA 5069 C C . TRP B 60 ? 2.6114 1.5736 1.9670 -0.4529 0.0796 -0.1122 1707 TRP B C 5070 O O . TRP B 60 ? 2.6806 1.5896 1.9801 -0.4658 0.0634 -0.1416 1707 TRP B O 5071 C CB . TRP B 60 ? 2.6445 1.7485 2.0535 -0.4397 0.0709 -0.0807 1707 TRP B CB 5072 C CG . TRP B 60 ? 2.5618 1.6919 1.9941 -0.4021 0.1046 -0.0626 1707 TRP B CG 5073 C CD1 . TRP B 60 ? 2.6161 1.7508 2.0193 -0.3684 0.1231 -0.0657 1707 TRP B CD1 5074 C CD2 . TRP B 60 ? 2.3785 1.5383 1.8681 -0.3966 0.1217 -0.0383 1707 TRP B CD2 5075 N NE1 . TRP B 60 ? 2.4712 1.6357 1.9121 -0.3441 0.1480 -0.0463 1707 TRP B NE1 5076 C CE2 . TRP B 60 ? 2.3160 1.4960 1.8068 -0.3599 0.1474 -0.0302 1707 TRP B CE2 5077 C CE3 . TRP B 60 ? 2.3024 1.4757 1.8416 -0.4197 0.1179 -0.0220 1707 TRP B CE3 5078 C CZ2 . TRP B 60 ? 2.2166 1.4279 1.7515 -0.3458 0.1669 -0.0092 1707 TRP B CZ2 5079 C CZ3 . TRP B 60 ? 2.3222 1.5266 1.9026 -0.4037 0.1402 0.0003 1707 TRP B CZ3 5080 C CH2 . TRP B 60 ? 2.2567 1.4791 1.8328 -0.3670 0.1633 0.0053 1707 TRP B CH2 5081 N N . ASP B 61 ? 2.6280 1.5766 1.9924 -0.4227 0.1114 -0.1014 1708 ASP B N 5082 C CA . ASP B 61 ? 2.8736 1.7381 2.1996 -0.4107 0.1279 -0.1181 1708 ASP B CA 5083 C C . ASP B 61 ? 2.8671 1.7514 2.2081 -0.3698 0.1612 -0.1004 1708 ASP B C 5084 O O . ASP B 61 ? 2.7578 1.7152 2.1419 -0.3595 0.1673 -0.0766 1708 ASP B O 5085 C CB . ASP B 61 ? 3.1243 1.9505 2.4817 -0.4411 0.1207 -0.1108 1708 ASP B CB 5086 C CG . ASP B 61 ? 3.2393 2.1113 2.6622 -0.4337 0.1390 -0.0733 1708 ASP B CG 5087 O OD1 . ASP B 61 ? 3.0728 2.0271 2.5417 -0.4349 0.1366 -0.0512 1708 ASP B OD1 5088 O OD2 . ASP B 61 ? 3.4434 2.2671 2.8695 -0.4247 0.1568 -0.0661 1708 ASP B OD2 5089 N N . TYR B 62 ? 2.9144 1.7328 2.2203 -0.3462 0.1820 -0.1129 1709 TYR B N 5090 C CA . TYR B 62 ? 2.7695 1.5963 2.0966 -0.3115 0.2121 -0.0934 1709 TYR B CA 5091 C C . TYR B 62 ? 2.8635 1.5941 2.1554 -0.3022 0.2246 -0.1100 1709 TYR B C 5092 O O . TYR B 62 ? 2.7508 1.4519 2.0149 -0.2662 0.2483 -0.1176 1709 TYR B O 5093 C CB . TYR B 62 ? 2.5898 1.4687 1.9101 -0.2776 0.2277 -0.0897 1709 TYR B CB 5094 C CG . TYR B 62 ? 2.5116 1.4359 1.8153 -0.2871 0.2097 -0.0985 1709 TYR B CG 5095 C CD1 . TYR B 62 ? 2.5315 1.4220 1.7891 -0.3109 0.1863 -0.1245 1709 TYR B CD1 5096 C CD2 . TYR B 62 ? 2.3165 1.3144 1.6480 -0.2714 0.2156 -0.0809 1709 TYR B CD2 5097 C CE1 . TYR B 62 ? 2.3848 1.3183 1.6260 -0.3177 0.1693 -0.1289 1709 TYR B CE1 5098 C CE2 . TYR B 62 ? 2.2379 1.2737 1.5550 -0.2777 0.2004 -0.0853 1709 TYR B CE2 5099 C CZ . TYR B 62 ? 2.2239 1.2298 1.4955 -0.3003 0.1771 -0.1077 1709 TYR B CZ 5100 O OH . TYR B 62 ? 1.9580 1.0049 1.2148 -0.3056 0.1608 -0.1083 1709 TYR B OH 5101 N N . GLY B 63 ? 3.0021 1.6842 2.2981 -0.3368 0.2074 -0.1158 1710 GLY B N 5102 C CA . GLY B 63 ? 3.0793 1.6627 2.3494 -0.3369 0.2143 -0.1305 1710 GLY B CA 5103 C C . GLY B 63 ? 3.2624 1.8438 2.5785 -0.3255 0.2330 -0.0972 1710 GLY B C 5104 O O . GLY B 63 ? 2.9747 1.5465 2.3263 -0.3561 0.2226 -0.0805 1710 GLY B O 5105 N N . MET B 64 ? 3.6778 2.2644 2.9895 -0.2809 0.2607 -0.0885 1711 MET B N 5106 C CA . MET B 64 ? 3.7275 2.3623 3.0857 -0.2572 0.2801 -0.0508 1711 MET B CA 5107 C C . MET B 64 ? 3.6155 2.2396 3.0164 -0.2705 0.2827 -0.0189 1711 MET B C 5108 O O . MET B 64 ? 3.3318 1.9848 2.7656 -0.3061 0.2666 -0.0047 1711 MET B O 5109 C CB . MET B 64 ? 3.7271 2.3589 3.0672 -0.2063 0.3077 -0.0519 1711 MET B CB 5110 C CG . MET B 64 ? 3.7393 2.2797 3.0529 -0.1816 0.3260 -0.0612 1711 MET B CG 5111 S SD . MET B 64 ? 3.4935 2.0379 2.7995 -0.1203 0.3599 -0.0555 1711 MET B SD 5112 C CE . MET B 64 ? 3.3424 1.9593 2.7123 -0.1078 0.3676 -0.0059 1711 MET B CE 5113 N N . SER B 65 ? 3.7216 2.3074 3.1226 -0.2396 0.3042 -0.0057 1712 SER B N 5114 C CA . SER B 65 ? 3.9319 2.5233 3.3730 -0.2394 0.3127 0.0326 1712 SER B CA 5115 C C . SER B 65 ? 4.2861 2.8018 3.7164 -0.2088 0.3328 0.0404 1712 SER B C 5116 O O . SER B 65 ? 4.5064 3.0226 3.9670 -0.2055 0.3406 0.0753 1712 SER B O 5117 C CB . SER B 65 ? 3.5914 2.2851 3.0685 -0.2254 0.3186 0.0604 1712 SER B CB 5118 O OG . SER B 65 ? 3.1714 1.9016 2.6318 -0.1937 0.3275 0.0468 1712 SER B OG 5119 N N . SER B 66 ? 4.2809 2.7327 3.6681 -0.1853 0.3419 0.0097 1713 SER B N 5120 C CA . SER B 66 ? 3.9875 2.3621 3.3647 -0.1532 0.3620 0.0145 1713 SER B CA 5121 C C . SER B 66 ? 3.8789 2.1385 3.2151 -0.1650 0.3582 -0.0205 1713 SER B C 5122 O O . SER B 66 ? 3.7175 1.9577 3.0151 -0.1816 0.3456 -0.0592 1713 SER B O 5123 C CB . SER B 66 ? 3.9714 2.3776 3.3426 -0.1005 0.3849 0.0167 1713 SER B CB 5124 O OG . SER B 66 ? 4.0742 2.4678 3.4015 -0.0875 0.3884 -0.0223 1713 SER B OG 5125 N N . SER B 79 ? 3.9777 1.8238 2.8659 -0.4890 0.1056 -0.4323 1726 SER B N 5126 C CA . SER B 79 ? 3.8293 1.7656 2.7387 -0.4422 0.1358 -0.3996 1726 SER B CA 5127 C C . SER B 79 ? 3.7306 1.7959 2.6716 -0.4576 0.1165 -0.3748 1726 SER B C 5128 O O . SER B 79 ? 3.7744 1.8554 2.6758 -0.4825 0.0873 -0.4008 1726 SER B O 5129 C CB . SER B 79 ? 3.7443 1.6724 2.7102 -0.4124 0.1691 -0.3595 1726 SER B CB 5130 O OG . SER B 79 ? 3.7356 1.7012 2.7787 -0.4476 0.1555 -0.3192 1726 SER B OG 5131 N N . VAL B 80 ? 3.5684 1.7202 2.5787 -0.4437 0.1316 -0.3260 1727 VAL B N 5132 C CA . VAL B 80 ? 3.2410 1.5145 2.2789 -0.4336 0.1306 -0.2994 1727 VAL B CA 5133 C C . VAL B 80 ? 3.1987 1.5457 2.2415 -0.4702 0.0932 -0.3011 1727 VAL B C 5134 O O . VAL B 80 ? 3.3455 1.6934 2.4207 -0.5168 0.0635 -0.2974 1727 VAL B O 5135 C CB . VAL B 80 ? 3.0294 1.3682 2.1484 -0.4216 0.1493 -0.2477 1727 VAL B CB 5136 C CG1 . VAL B 80 ? 2.8416 1.1712 1.9556 -0.3665 0.1900 -0.2365 1727 VAL B CG1 5137 C CG2 . VAL B 80 ? 3.0579 1.3697 2.2303 -0.4594 0.1371 -0.2280 1727 VAL B CG2 5138 N N . PRO B 81 ? 3.0653 1.4792 2.0835 -0.4487 0.0956 -0.3014 1728 PRO B N 5139 C CA . PRO B 81 ? 3.0342 1.5265 2.0501 -0.4700 0.0654 -0.2999 1728 PRO B CA 5140 C C . PRO B 81 ? 3.0687 1.6561 2.1628 -0.5006 0.0422 -0.2639 1728 PRO B C 5141 O O . PRO B 81 ? 2.9651 1.6043 2.1254 -0.4900 0.0591 -0.2272 1728 PRO B O 5142 C CB . PRO B 81 ? 2.8782 1.4120 1.8615 -0.4244 0.0903 -0.2973 1728 PRO B CB 5143 C CG . PRO B 81 ? 2.8410 1.3507 1.8396 -0.3833 0.1316 -0.2842 1728 PRO B CG 5144 C CD . PRO B 81 ? 2.9884 1.3954 1.9705 -0.3949 0.1328 -0.3056 1728 PRO B CD 5145 N N . GLN B 82 ? 3.2674 1.8802 2.3489 -0.5355 0.0037 -0.2761 1729 GLN B N 5146 C CA . GLN B 82 ? 3.2895 1.9894 2.4406 -0.5674 -0.0231 -0.2471 1729 GLN B CA 5147 C C . GLN B 82 ? 3.1115 1.9071 2.2870 -0.5389 -0.0122 -0.2195 1729 GLN B C 5148 O O . GLN B 82 ? 2.8480 1.6611 2.0439 -0.5028 0.0220 -0.2003 1729 GLN B O 5149 C CB . GLN B 82 ? 3.4834 2.1722 2.6101 -0.6153 -0.0711 -0.2718 1729 GLN B CB 5150 C CG . GLN B 82 ? 3.3802 2.1145 2.5853 -0.6639 -0.1015 -0.2496 1729 GLN B CG 5151 C CD . GLN B 82 ? 3.2958 2.0321 2.4778 -0.7100 -0.1524 -0.2729 1729 GLN B CD 5152 O OE1 . GLN B 82 ? 3.0195 1.8266 2.2643 -0.7424 -0.1803 -0.2506 1729 GLN B OE1 5153 N NE2 . GLN B 82 ? 3.4503 2.1111 2.5420 -0.7124 -0.1646 -0.3180 1729 GLN B NE2 5154 N N . PHE B 83 ? 3.1483 2.0024 2.3223 -0.5562 -0.0429 -0.2178 1730 PHE B N 5155 C CA . PHE B 83 ? 2.9246 1.8680 2.1196 -0.5355 -0.0409 -0.1932 1730 PHE B CA 5156 C C . PHE B 83 ? 2.8069 1.8400 2.0898 -0.5547 -0.0568 -0.1578 1730 PHE B C 5157 O O . PHE B 83 ? 2.6722 1.7393 2.0173 -0.5422 -0.0342 -0.1303 1730 PHE B O 5158 C CB . PHE B 83 ? 2.9335 1.8843 2.1223 -0.4865 0.0011 -0.1818 1730 PHE B CB 5159 C CG . PHE B 83 ? 2.9684 1.8606 2.0718 -0.4600 0.0172 -0.2110 1730 PHE B CG 5160 C CD1 . PHE B 83 ? 3.0324 1.9305 2.0734 -0.4613 -0.0011 -0.2284 1730 PHE B CD1 5161 C CD2 . PHE B 83 ? 2.9595 1.7952 2.0457 -0.4310 0.0526 -0.2187 1730 PHE B CD2 5162 C CE1 . PHE B 83 ? 3.2091 2.0560 2.1693 -0.4343 0.0179 -0.2547 1730 PHE B CE1 5163 C CE2 . PHE B 83 ? 2.9568 1.7421 1.9678 -0.4033 0.0712 -0.2447 1730 PHE B CE2 5164 C CZ . PHE B 83 ? 3.1198 1.9108 2.0667 -0.4048 0.0552 -0.2633 1730 PHE B CZ 5165 N N . LYS B 84 ? 2.7400 1.8140 2.0271 -0.5831 -0.0954 -0.1582 1731 LYS B N 5166 C CA . LYS B 84 ? 2.5937 1.7592 1.9628 -0.5960 -0.1098 -0.1243 1731 LYS B CA 5167 C C . LYS B 84 ? 2.5689 1.7846 1.9406 -0.5540 -0.0870 -0.1056 1731 LYS B C 5168 O O . LYS B 84 ? 2.7350 1.9564 2.0545 -0.5419 -0.0961 -0.1144 1731 LYS B O 5169 C CB . LYS B 84 ? 2.5760 1.7724 1.9451 -0.6356 -0.1594 -0.1301 1731 LYS B CB 5170 C CG . LYS B 84 ? 2.4406 1.6910 1.8966 -0.6747 -0.1839 -0.1082 1731 LYS B CG 5171 C CD . LYS B 84 ? 2.4805 1.7252 1.9196 -0.7228 -0.2354 -0.1270 1731 LYS B CD 5172 C CE . LYS B 84 ? 2.3720 1.6846 1.8031 -0.7267 -0.2708 -0.1198 1731 LYS B CE 5173 N NZ . LYS B 84 ? 2.3092 1.5891 1.6666 -0.7547 -0.3141 -0.1525 1731 LYS B NZ 5174 N N . LYS B 85 ? 2.3794 1.6237 1.8047 -0.5310 -0.0556 -0.0817 1732 LYS B N 5175 C CA . LYS B 85 ? 2.2877 1.5913 1.7360 -0.4978 -0.0387 -0.0596 1732 LYS B CA 5176 C C . LYS B 85 ? 2.2475 1.6329 1.7831 -0.5095 -0.0494 -0.0292 1732 LYS B C 5177 O O . LYS B 85 ? 2.1526 1.5455 1.7305 -0.5395 -0.0623 -0.0243 1732 LYS B O 5178 C CB . LYS B 85 ? 2.1054 1.3840 1.5436 -0.4598 0.0035 -0.0578 1732 LYS B CB 5179 C CG . LYS B 85 ? 2.0859 1.3333 1.4530 -0.4314 0.0172 -0.0733 1732 LYS B CG 5180 C CD . LYS B 85 ? 2.0340 1.2551 1.3966 -0.3974 0.0572 -0.0720 1732 LYS B CD 5181 C CE . LYS B 85 ? 2.0795 1.2722 1.3759 -0.3685 0.0744 -0.0857 1732 LYS B CE 5182 N NZ . LYS B 85 ? 1.9815 1.1120 1.2414 -0.3457 0.1045 -0.1014 1732 LYS B NZ 5183 N N . VAL B 86 ? 2.2642 1.7095 1.8267 -0.4870 -0.0448 -0.0092 1733 VAL B N 5184 C CA . VAL B 86 ? 2.2125 1.7363 1.8593 -0.4898 -0.0490 0.0196 1733 VAL B CA 5185 C C . VAL B 86 ? 2.1547 1.6976 1.8338 -0.4557 -0.0122 0.0339 1733 VAL B C 5186 O O . VAL B 86 ? 2.2557 1.7721 1.8949 -0.4287 0.0076 0.0271 1733 VAL B O 5187 C CB . VAL B 86 ? 2.1558 1.7388 1.8170 -0.4903 -0.0761 0.0337 1733 VAL B CB 5188 C CG1 . VAL B 86 ? 2.1371 1.7812 1.8707 -0.5174 -0.1008 0.0518 1733 VAL B CG1 5189 C CG2 . VAL B 86 ? 2.1977 1.7484 1.7816 -0.4976 -0.1003 0.0149 1733 VAL B CG2 5190 N N . VAL B 87 ? 2.0615 1.6503 1.8110 -0.4573 -0.0026 0.0530 1734 VAL B N 5191 C CA . VAL B 87 ? 1.9816 1.5910 1.7600 -0.4260 0.0298 0.0644 1734 VAL B CA 5192 C C . VAL B 87 ? 1.9928 1.6757 1.8459 -0.4235 0.0288 0.0868 1734 VAL B C 5193 O O . VAL B 87 ? 2.0330 1.7523 1.9233 -0.4479 0.0058 0.0960 1734 VAL B O 5194 C CB . VAL B 87 ? 1.8879 1.4638 1.6673 -0.4226 0.0564 0.0612 1734 VAL B CB 5195 C CG1 . VAL B 87 ? 1.8409 1.4283 1.6290 -0.3876 0.0865 0.0668 1734 VAL B CG1 5196 C CG2 . VAL B 87 ? 1.9231 1.4226 1.6387 -0.4306 0.0561 0.0396 1734 VAL B CG2 5197 N N . PHE B 88 ? 1.9134 1.6173 1.7886 -0.3937 0.0541 0.0946 1735 PHE B N 5198 C CA . PHE B 88 ? 1.9074 1.6725 1.8525 -0.3858 0.0639 0.1124 1735 PHE B CA 5199 C C . PHE B 88 ? 1.9658 1.7307 1.9354 -0.3946 0.0822 0.1158 1735 PHE B C 5200 O O . PHE B 88 ? 1.9290 1.6541 1.8683 -0.3838 0.1033 0.1074 1735 PHE B O 5201 C CB . PHE B 88 ? 1.7763 1.5561 1.7299 -0.3515 0.0834 0.1155 1735 PHE B CB 5202 C CG . PHE B 88 ? 1.7706 1.5687 1.7224 -0.3421 0.0667 0.1216 1735 PHE B CG 5203 C CD1 . PHE B 88 ? 1.8045 1.6606 1.8120 -0.3434 0.0521 0.1388 1735 PHE B CD1 5204 C CD2 . PHE B 88 ? 1.7740 1.5338 1.6702 -0.3310 0.0662 0.1128 1735 PHE B CD2 5205 C CE1 . PHE B 88 ? 1.8027 1.6759 1.8096 -0.3338 0.0355 0.1483 1735 PHE B CE1 5206 C CE2 . PHE B 88 ? 1.8257 1.6034 1.7192 -0.3225 0.0514 0.1224 1735 PHE B CE2 5207 C CZ . PHE B 88 ? 1.8396 1.6726 1.7877 -0.3240 0.0350 0.1407 1735 PHE B CZ 5208 N N . GLN B 89 ? 2.0079 1.8203 2.0335 -0.4135 0.0744 0.1304 1736 GLN B N 5209 C CA . GLN B 89 ? 2.0333 1.8542 2.0880 -0.4246 0.0918 0.1389 1736 GLN B CA 5210 C C . GLN B 89 ? 1.8971 1.7841 2.0141 -0.4083 0.1111 0.1551 1736 GLN B C 5211 O O . GLN B 89 ? 1.6683 1.6106 1.8329 -0.4070 0.1001 0.1663 1736 GLN B O 5212 C CB . GLN B 89 ? 2.1711 1.9857 2.2375 -0.4653 0.0704 0.1427 1736 GLN B CB 5213 C CG . GLN B 89 ? 2.1543 1.9568 2.2351 -0.4802 0.0885 0.1512 1736 GLN B CG 5214 C CD . GLN B 89 ? 2.2164 1.9392 2.2351 -0.4783 0.0991 0.1362 1736 GLN B CD 5215 O OE1 . GLN B 89 ? 2.2324 1.9009 2.2122 -0.4992 0.0804 0.1224 1736 GLN B OE1 5216 N NE2 . GLN B 89 ? 2.1445 1.8598 2.1536 -0.4523 0.1290 0.1385 1736 GLN B NE2 5217 N N . GLU B 90 ? 2.0112 1.8909 2.1250 -0.3944 0.1401 0.1558 1737 GLU B N 5218 C CA . GLU B 90 ? 2.1531 2.0881 2.3146 -0.3769 0.1633 0.1672 1737 GLU B CA 5219 C C . GLU B 90 ? 2.1324 2.1107 2.3461 -0.4036 0.1605 0.1861 1737 GLU B C 5220 O O . GLU B 90 ? 2.2612 2.2150 2.4650 -0.4252 0.1643 0.1912 1737 GLU B O 5221 C CB . GLU B 90 ? 2.2314 2.1412 2.3629 -0.3559 0.1922 0.1608 1737 GLU B CB 5222 C CG . GLU B 90 ? 2.2171 2.1774 2.3856 -0.3386 0.2193 0.1697 1737 GLU B CG 5223 C CD . GLU B 90 ? 2.1177 2.1165 2.3136 -0.3103 0.2252 0.1648 1737 GLU B CD 5224 O OE1 . GLU B 90 ? 2.0527 2.0954 2.2953 -0.3134 0.2136 0.1737 1737 GLU B OE1 5225 O OE2 . GLU B 90 ? 2.0486 2.0339 2.2217 -0.2850 0.2410 0.1526 1737 GLU B OE2 5226 N N . PHE B 91 ? 1.9002 1.9426 2.1721 -0.4027 0.1532 0.1983 1738 PHE B N 5227 C CA . PHE B 91 ? 1.8469 1.9410 2.1778 -0.4274 0.1517 0.2190 1738 PHE B CA 5228 C C . PHE B 91 ? 1.7197 1.8685 2.0935 -0.4076 0.1852 0.2312 1738 PHE B C 5229 O O . PHE B 91 ? 1.6193 1.7507 1.9636 -0.3802 0.2094 0.2209 1738 PHE B O 5230 C CB . PHE B 91 ? 2.0175 2.1494 2.3885 -0.4474 0.1181 0.2277 1738 PHE B CB 5231 C CG . PHE B 91 ? 2.2141 2.3038 2.5582 -0.4867 0.0881 0.2232 1738 PHE B CG 5232 C CD1 . PHE B 91 ? 2.3244 2.3476 2.5999 -0.4873 0.0699 0.2022 1738 PHE B CD1 5233 C CD2 . PHE B 91 ? 2.2804 2.3937 2.6659 -0.5234 0.0798 0.2390 1738 PHE B CD2 5234 C CE1 . PHE B 91 ? 2.3852 2.3640 2.6303 -0.5224 0.0432 0.1937 1738 PHE B CE1 5235 C CE2 . PHE B 91 ? 2.4142 2.4817 2.7731 -0.5613 0.0512 0.2315 1738 PHE B CE2 5236 C CZ . PHE B 91 ? 2.4378 2.4360 2.7240 -0.5601 0.0328 0.2071 1738 PHE B CZ 5237 N N . THR B 92 ? 1.7211 1.9363 2.1625 -0.4219 0.1869 0.2526 1739 THR B N 5238 C CA . THR B 92 ? 1.6389 1.9065 2.1180 -0.4063 0.2226 0.2658 1739 THR B CA 5239 C C . THR B 92 ? 1.6407 1.9913 2.1935 -0.3894 0.2296 0.2784 1739 THR B C 5240 O O . THR B 92 ? 1.6306 1.9918 2.1826 -0.3534 0.2440 0.2674 1739 THR B O 5241 C CB . THR B 92 ? 1.6171 1.8822 2.1003 -0.4339 0.2363 0.2828 1739 THR B CB 5242 O OG1 . THR B 92 ? 1.5262 1.7974 1.9922 -0.4092 0.2736 0.2831 1739 THR B OG1 5243 C CG2 . THR B 92 ? 1.5848 1.9182 2.1454 -0.4623 0.2300 0.3096 1739 THR B CG2 5244 N N . ASP B 93 ? 1.7560 2.1655 2.3748 -0.4140 0.2207 0.3016 1740 ASP B N 5245 C CA . ASP B 93 ? 1.9041 2.3937 2.5967 -0.3954 0.2249 0.3143 1740 ASP B CA 5246 C C . ASP B 93 ? 1.9428 2.4377 2.6524 -0.4048 0.1834 0.3145 1740 ASP B C 5247 O O . ASP B 93 ? 1.9568 2.3943 2.6180 -0.4272 0.1538 0.3038 1740 ASP B O 5248 C CB . ASP B 93 ? 2.0552 2.6241 2.8212 -0.4074 0.2465 0.3423 1740 ASP B CB 5249 C CG . ASP B 93 ? 2.2519 2.8144 3.0285 -0.4575 0.2317 0.3598 1740 ASP B CG 5250 O OD1 . ASP B 93 ? 2.4445 2.9515 3.1846 -0.4849 0.1972 0.3504 1740 ASP B OD1 5251 O OD2 . ASP B 93 ? 2.2492 2.8622 3.0713 -0.4694 0.2555 0.3830 1740 ASP B OD2 5252 N N . GLY B 94 ? 1.8923 2.4540 2.6668 -0.3847 0.1822 0.3261 1741 GLY B N 5253 C CA . GLY B 94 ? 1.8736 2.4517 2.6712 -0.3915 0.1425 0.3316 1741 GLY B CA 5254 C C . GLY B 94 ? 1.9578 2.5348 2.7620 -0.4418 0.1049 0.3417 1741 GLY B C 5255 O O . GLY B 94 ? 1.9864 2.5408 2.7680 -0.4546 0.0669 0.3365 1741 GLY B O 5256 N N . SER B 95 ? 1.9872 2.5869 2.8203 -0.4710 0.1159 0.3559 1742 SER B N 5257 C CA . SER B 95 ? 1.9223 2.5187 2.7663 -0.5232 0.0828 0.3652 1742 SER B CA 5258 C C . SER B 95 ? 1.9399 2.4378 2.6934 -0.5439 0.0594 0.3404 1742 SER B C 5259 O O . SER B 95 ? 2.0163 2.4992 2.7674 -0.5858 0.0253 0.3413 1742 SER B O 5260 C CB . SER B 95 ? 1.8991 2.5300 2.7872 -0.5478 0.1070 0.3859 1742 SER B CB 5261 O OG . SER B 95 ? 1.8840 2.6048 2.8503 -0.5247 0.1371 0.4077 1742 SER B OG 5262 N N . PHE B 96 ? 1.9339 2.3659 2.6146 -0.5147 0.0776 0.3178 1743 PHE B N 5263 C CA . PHE B 96 ? 1.9033 2.2409 2.4970 -0.5287 0.0644 0.2943 1743 PHE B CA 5264 C C . PHE B 96 ? 1.9137 2.2329 2.5127 -0.5738 0.0575 0.3018 1743 PHE B C 5265 O O . PHE B 96 ? 1.9123 2.1910 2.4840 -0.6076 0.0238 0.2926 1743 PHE B O 5266 C CB . PHE B 96 ? 1.9440 2.2542 2.5013 -0.5322 0.0249 0.2807 1743 PHE B CB 5267 C CG . PHE B 96 ? 1.9717 2.2825 2.5122 -0.4886 0.0325 0.2728 1743 PHE B CG 5268 C CD1 . PHE B 96 ? 2.0266 2.4096 2.6309 -0.4691 0.0275 0.2893 1743 PHE B CD1 5269 C CD2 . PHE B 96 ? 1.9596 2.1996 2.4248 -0.4669 0.0449 0.2505 1743 PHE B CD2 5270 C CE1 . PHE B 96 ? 2.0366 2.4156 2.6285 -0.4294 0.0350 0.2835 1743 PHE B CE1 5271 C CE2 . PHE B 96 ? 2.0898 2.3295 2.5437 -0.4292 0.0520 0.2448 1743 PHE B CE2 5272 C CZ . PHE B 96 ? 2.1345 2.4408 2.6508 -0.4108 0.0470 0.2611 1743 PHE B CZ 5273 N N . THR B 97 ? 1.8953 2.2474 2.5325 -0.5746 0.0899 0.3195 1744 THR B N 5274 C CA . THR B 97 ? 1.9799 2.3176 2.6298 -0.6166 0.0881 0.3317 1744 THR B CA 5275 C C . THR B 97 ? 2.1265 2.3791 2.7025 -0.6116 0.1099 0.3181 1744 THR B C 5276 O O . THR B 97 ? 2.2806 2.4577 2.8019 -0.6320 0.0880 0.3006 1744 THR B O 5277 C CB . THR B 97 ? 1.9193 2.3502 2.6640 -0.6304 0.1039 0.3654 1744 THR B CB 5278 O OG1 . THR B 97 ? 2.0137 2.4245 2.7703 -0.6753 0.1004 0.3788 1744 THR B OG1 5279 C CG2 . THR B 97 ? 1.9666 2.4409 2.7293 -0.5898 0.1523 0.3752 1744 THR B CG2 5280 N N . GLN B 98 ? 2.1439 2.4067 2.7145 -0.5827 0.1514 0.3244 1745 GLN B N 5281 C CA . GLN B 98 ? 2.0648 2.2504 2.5619 -0.5697 0.1707 0.3109 1745 GLN B CA 5282 C C . GLN B 98 ? 2.1407 2.2761 2.5754 -0.5425 0.1586 0.2813 1745 GLN B C 5283 O O . GLN B 98 ? 2.3699 2.5438 2.8213 -0.5174 0.1556 0.2761 1745 GLN B O 5284 C CB . GLN B 98 ? 1.9067 2.1213 2.4071 -0.5396 0.2153 0.3220 1745 GLN B CB 5285 C CG . GLN B 98 ? 2.0890 2.3842 2.6627 -0.5504 0.2375 0.3537 1745 GLN B CG 5286 C CD . GLN B 98 ? 2.3180 2.5905 2.8978 -0.5877 0.2429 0.3751 1745 GLN B CD 5287 O OE1 . GLN B 98 ? 2.5438 2.8782 3.1872 -0.6067 0.2561 0.4045 1745 GLN B OE1 5288 N NE2 . GLN B 98 ? 2.4059 2.5892 2.9222 -0.5981 0.2338 0.3621 1745 GLN B NE2 5289 N N . PRO B 99 ? 2.1539 2.2039 2.5197 -0.5478 0.1510 0.2632 1746 PRO B N 5290 C CA . PRO B 99 ? 2.1625 2.1691 2.4676 -0.5133 0.1547 0.2391 1746 PRO B CA 5291 C C . PRO B 99 ? 2.0921 2.0866 2.3730 -0.4867 0.1912 0.2412 1746 PRO B C 5292 O O . PRO B 99 ? 2.2123 2.2029 2.5017 -0.5019 0.2066 0.2577 1746 PRO B O 5293 C CB . PRO B 99 ? 2.1766 2.1011 2.4232 -0.5333 0.1296 0.2200 1746 PRO B CB 5294 C CG . PRO B 99 ? 2.2366 2.1689 2.5187 -0.5792 0.1050 0.2308 1746 PRO B CG 5295 C CD . PRO B 99 ? 2.2292 2.2209 2.5742 -0.5878 0.1283 0.2600 1746 PRO B CD 5296 N N . LEU B 100 ? 1.8916 1.8829 2.1448 -0.4491 0.2044 0.2268 1747 LEU B N 5297 C CA . LEU B 100 ? 1.9156 1.8942 2.1406 -0.4250 0.2354 0.2268 1747 LEU B CA 5298 C C . LEU B 100 ? 2.0360 1.9335 2.1970 -0.4270 0.2343 0.2162 1747 LEU B C 5299 O O . LEU B 100 ? 2.2861 2.1426 2.4037 -0.4104 0.2266 0.1960 1747 LEU B O 5300 C CB . LEU B 100 ? 1.8337 1.8443 2.0594 -0.3854 0.2520 0.2161 1747 LEU B CB 5301 C CG . LEU B 100 ? 1.9078 1.9093 2.1017 -0.3609 0.2815 0.2141 1747 LEU B CG 5302 C CD1 . LEU B 100 ? 1.7000 1.7682 1.9306 -0.3452 0.3090 0.2254 1747 LEU B CD1 5303 C CD2 . LEU B 100 ? 1.9623 1.9206 2.1052 -0.3344 0.2811 0.1913 1747 LEU B CD2 5304 N N . TYR B 101 ? 2.1077 1.9846 2.2679 -0.4478 0.2424 0.2323 1748 TYR B N 5305 C CA . TYR B 101 ? 2.2013 2.0131 2.3112 -0.4442 0.2522 0.2311 1748 TYR B CA 5306 C C . TYR B 101 ? 2.1458 1.9401 2.2120 -0.4062 0.2633 0.2136 1748 TYR B C 5307 O O . TYR B 101 ? 2.1674 2.0069 2.2442 -0.3820 0.2814 0.2151 1748 TYR B O 5308 C CB . TYR B 101 ? 2.6273 2.4626 2.7596 -0.4535 0.2759 0.2599 1748 TYR B CB 5309 C CG . TYR B 101 ? 2.9465 2.7212 3.0415 -0.4574 0.2861 0.2701 1748 TYR B CG 5310 C CD1 . TYR B 101 ? 2.9779 2.6964 3.0170 -0.4339 0.2876 0.2540 1748 TYR B CD1 5311 C CD2 . TYR B 101 ? 3.0100 2.7871 3.1302 -0.4838 0.2954 0.2992 1748 TYR B CD2 5312 C CE1 . TYR B 101 ? 3.0274 2.6929 3.0367 -0.4346 0.2970 0.2656 1748 TYR B CE1 5313 C CE2 . TYR B 101 ? 3.1936 2.9143 3.2824 -0.4859 0.3050 0.3118 1748 TYR B CE2 5314 C CZ . TYR B 101 ? 3.2745 2.9391 3.3076 -0.4600 0.3053 0.2946 1748 TYR B CZ 5315 O OH . TYR B 101 ? 3.5512 3.1598 3.5551 -0.4588 0.3144 0.3083 1748 TYR B OH 5316 N N . ARG B 102 ? 2.2469 1.9773 2.2653 -0.4006 0.2526 0.1960 1749 ARG B N 5317 C CA . ARG B 102 ? 2.2467 1.9636 2.2289 -0.3665 0.2628 0.1816 1749 ARG B CA 5318 C C . ARG B 102 ? 2.1963 1.8861 2.1506 -0.3552 0.2818 0.1918 1749 ARG B C 5319 O O . ARG B 102 ? 2.1618 1.7944 2.0910 -0.3658 0.2788 0.1950 1749 ARG B O 5320 C CB . ARG B 102 ? 2.2319 1.9090 2.1814 -0.3596 0.2451 0.1585 1749 ARG B CB 5321 C CG . ARG B 102 ? 2.3442 2.0634 2.3131 -0.3465 0.2375 0.1482 1749 ARG B CG 5322 C CD . ARG B 102 ? 2.2759 1.9905 2.2514 -0.3661 0.2110 0.1415 1749 ARG B CD 5323 N NE . ARG B 102 ? 2.3696 2.0930 2.3369 -0.3473 0.2032 0.1284 1749 ARG B NE 5324 C CZ . ARG B 102 ? 2.3534 2.0345 2.2762 -0.3330 0.2010 0.1135 1749 ARG B CZ 5325 N NH1 . ARG B 102 ? 2.1608 1.7860 2.0411 -0.3321 0.2062 0.1071 1749 ARG B NH1 5326 N NH2 . ARG B 102 ? 2.3126 2.0085 2.2356 -0.3182 0.1948 0.1064 1749 ARG B NH2 5327 N N . GLY B 103 ? 2.1132 1.8453 2.0728 -0.3333 0.3008 0.1971 1750 GLY B N 5328 C CA . GLY B 103 ? 2.0250 1.7497 1.9646 -0.3230 0.3194 0.2124 1750 GLY B CA 5329 C C . GLY B 103 ? 2.0160 1.6904 1.9111 -0.3036 0.3180 0.2010 1750 GLY B C 5330 O O . GLY B 103 ? 2.2572 1.9022 2.1371 -0.2995 0.3045 0.1815 1750 GLY B O 5331 N N . GLU B 104 ? 1.9061 1.5735 1.7807 -0.2908 0.3323 0.2149 1751 GLU B N 5332 C CA . GLU B 104 ? 1.9291 1.5585 1.7670 -0.2688 0.3319 0.2061 1751 GLU B CA 5333 C C . GLU B 104 ? 2.0297 1.6841 1.8648 -0.2477 0.3280 0.1827 1751 GLU B C 5334 O O . GLU B 104 ? 2.0143 1.6358 1.8299 -0.2374 0.3202 0.1676 1751 GLU B O 5335 C CB . GLU B 104 ? 1.8771 1.5081 1.6975 -0.2561 0.3467 0.2272 1751 GLU B CB 5336 C CG . GLU B 104 ? 2.0469 1.6307 1.8620 -0.2728 0.3493 0.2504 1751 GLU B CG 5337 C CD . GLU B 104 ? 2.1529 1.7681 1.9964 -0.2956 0.3584 0.2750 1751 GLU B CD 5338 O OE1 . GLU B 104 ? 2.2494 1.9275 2.1130 -0.2931 0.3658 0.2744 1751 GLU B OE1 5339 O OE2 . GLU B 104 ? 2.2419 1.8191 2.0893 -0.3156 0.3594 0.2954 1751 GLU B OE2 5340 N N . LEU B 105 ? 2.1991 1.9108 2.0553 -0.2417 0.3346 0.1800 1752 LEU B N 5341 C CA . LEU B 105 ? 2.2359 1.9734 2.0981 -0.2250 0.3306 0.1580 1752 LEU B CA 5342 C C . LEU B 105 ? 2.2532 1.9552 2.1079 -0.2256 0.3152 0.1413 1752 LEU B C 5343 O O . LEU B 105 ? 2.2413 1.9200 2.0732 -0.2102 0.3135 0.1322 1752 LEU B O 5344 C CB . LEU B 105 ? 2.0607 1.8525 1.9588 -0.2287 0.3348 0.1560 1752 LEU B CB 5345 C CG . LEU B 105 ? 1.8249 1.6682 1.7332 -0.2215 0.3530 0.1650 1752 LEU B CG 5346 C CD1 . LEU B 105 ? 1.5989 1.4459 1.4752 -0.1998 0.3610 0.1610 1752 LEU B CD1 5347 C CD2 . LEU B 105 ? 1.9027 1.7552 1.8257 -0.2425 0.3616 0.1913 1752 LEU B CD2 5348 N N . ASN B 106 ? 2.2276 1.9292 2.1017 -0.2435 0.3041 0.1389 1753 ASN B N 5349 C CA . ASN B 106 ? 2.2733 1.9447 2.1371 -0.2457 0.2891 0.1245 1753 ASN B CA 5350 C C . ASN B 106 ? 2.1811 1.7990 2.0245 -0.2640 0.2794 0.1265 1753 ASN B C 5351 O O . ASN B 106 ? 2.1321 1.7413 1.9815 -0.2813 0.2644 0.1215 1753 ASN B O 5352 C CB . ASN B 106 ? 2.3378 2.0445 2.2312 -0.2474 0.2798 0.1163 1753 ASN B CB 5353 C CG . ASN B 106 ? 2.2412 1.9995 2.1747 -0.2553 0.2855 0.1266 1753 ASN B CG 5354 O OD1 . ASN B 106 ? 2.1853 1.9496 2.1281 -0.2705 0.2912 0.1421 1753 ASN B OD1 5355 N ND2 . ASN B 106 ? 2.1613 1.9573 2.1214 -0.2445 0.2849 0.1192 1753 ASN B ND2 5356 N N . GLU B 107 ? 2.0806 1.6611 1.8987 -0.2593 0.2872 0.1331 1754 GLU B N 5357 C CA . GLU B 107 ? 2.1319 1.6532 1.9276 -0.2738 0.2802 0.1326 1754 GLU B CA 5358 C C . GLU B 107 ? 2.0756 1.5639 1.8435 -0.2640 0.2721 0.1131 1754 GLU B C 5359 O O . GLU B 107 ? 2.2206 1.6701 1.9720 -0.2789 0.2602 0.1040 1754 GLU B O 5360 C CB . GLU B 107 ? 2.2024 1.6916 1.9809 -0.2674 0.2926 0.1471 1754 GLU B CB 5361 C CG . GLU B 107 ? 2.4258 1.8543 2.1907 -0.2880 0.2865 0.1501 1754 GLU B CG 5362 C CD . GLU B 107 ? 2.7224 2.1090 2.4672 -0.2763 0.2986 0.1636 1754 GLU B CD 5363 O OE1 . GLU B 107 ? 2.8323 2.2475 2.5875 -0.2687 0.3111 0.1843 1754 GLU B OE1 5364 O OE2 . GLU B 107 ? 2.8841 2.2088 2.6014 -0.2736 0.2959 0.1539 1754 GLU B OE2 5365 N N . HIS B 108 ? 1.9356 1.4421 1.6986 -0.2396 0.2786 0.1066 1755 HIS B N 5366 C CA . HIS B 108 ? 1.9770 1.4571 1.7142 -0.2257 0.2763 0.0920 1755 HIS B CA 5367 C C . HIS B 108 ? 1.9612 1.4492 1.6993 -0.2336 0.2624 0.0799 1755 HIS B C 5368 O O . HIS B 108 ? 1.9085 1.3650 1.6176 -0.2278 0.2595 0.0686 1755 HIS B O 5369 C CB . HIS B 108 ? 2.0515 1.5575 1.7923 -0.2002 0.2869 0.0919 1755 HIS B CB 5370 C CG . HIS B 108 ? 1.9537 1.5165 1.7262 -0.1978 0.2871 0.0929 1755 HIS B CG 5371 N ND1 . HIS B 108 ? 1.9614 1.5470 1.7457 -0.1915 0.2821 0.0830 1755 HIS B ND1 5372 C CD2 . HIS B 108 ? 1.9027 1.5019 1.6965 -0.2002 0.2928 0.1022 1755 HIS B CD2 5373 C CE1 . HIS B 108 ? 1.9179 1.5481 1.7305 -0.1892 0.2844 0.0842 1755 HIS B CE1 5374 N NE2 . HIS B 108 ? 2.0617 1.7024 1.8789 -0.1939 0.2914 0.0948 1755 HIS B NE2 5375 N N . LEU B 109 ? 1.8904 1.4221 1.6612 -0.2446 0.2549 0.0835 1756 LEU B N 5376 C CA . LEU B 109 ? 1.8961 1.4402 1.6718 -0.2519 0.2398 0.0763 1756 LEU B CA 5377 C C . LEU B 109 ? 2.0250 1.5224 1.7663 -0.2665 0.2265 0.0670 1756 LEU B C 5378 O O . LEU B 109 ? 1.8629 1.3521 1.5841 -0.2624 0.2189 0.0580 1756 LEU B O 5379 C CB . LEU B 109 ? 1.8356 1.4290 1.6547 -0.2647 0.2328 0.0846 1756 LEU B CB 5380 C CG . LEU B 109 ? 1.7783 1.4159 1.6242 -0.2466 0.2379 0.0839 1756 LEU B CG 5381 C CD1 . LEU B 109 ? 1.6462 1.2873 1.4873 -0.2259 0.2552 0.0829 1756 LEU B CD1 5382 C CD2 . LEU B 109 ? 1.8886 1.5762 1.7803 -0.2549 0.2347 0.0922 1756 LEU B CD2 5383 N N . GLY B 110 ? 2.2026 1.6679 1.9355 -0.2840 0.2243 0.0693 1757 GLY B N 5384 C CA . GLY B 110 ? 2.2112 1.6218 1.9067 -0.2986 0.2127 0.0571 1757 GLY B CA 5385 C C . GLY B 110 ? 2.2219 1.6521 1.9227 -0.3165 0.1903 0.0521 1757 GLY B C 5386 O O . GLY B 110 ? 2.3460 1.8177 2.0872 -0.3332 0.1806 0.0626 1757 GLY B O 5387 N N . LEU B 111 ? 2.1074 1.5129 1.7686 -0.3107 0.1833 0.0378 1758 LEU B N 5388 C CA . LEU B 111 ? 2.0797 1.4980 1.7343 -0.3266 0.1596 0.0325 1758 LEU B CA 5389 C C . LEU B 111 ? 1.9689 1.4529 1.6660 -0.3212 0.1538 0.0452 1758 LEU B C 5390 O O . LEU B 111 ? 1.9151 1.4200 1.6171 -0.3347 0.1323 0.0462 1758 LEU B O 5391 C CB . LEU B 111 ? 2.2283 1.6042 1.8234 -0.3167 0.1582 0.0153 1758 LEU B CB 5392 C CG . LEU B 111 ? 2.3993 1.7401 1.9538 -0.3401 0.1346 -0.0009 1758 LEU B CG 5393 C CD1 . LEU B 111 ? 2.5840 1.8998 2.0820 -0.3221 0.1387 -0.0145 1758 LEU B CD1 5394 C CD2 . LEU B 111 ? 2.3534 1.7383 1.9384 -0.3654 0.1065 0.0068 1758 LEU B CD2 5395 N N . LEU B 112 ? 1.8830 1.3981 1.6101 -0.3007 0.1722 0.0545 1759 LEU B N 5396 C CA . LEU B 112 ? 1.7650 1.3364 1.5345 -0.2927 0.1698 0.0650 1759 LEU B CA 5397 C C . LEU B 112 ? 1.8150 1.4292 1.6350 -0.3097 0.1618 0.0769 1759 LEU B C 5398 O O . LEU B 112 ? 1.8896 1.4976 1.7202 -0.3234 0.1659 0.0806 1759 LEU B O 5399 C CB . LEU B 112 ? 1.6888 1.2748 1.4719 -0.2667 0.1917 0.0675 1759 LEU B CB 5400 C CG . LEU B 112 ? 1.7559 1.3404 1.5242 -0.2460 0.1974 0.0646 1759 LEU B CG 5401 C CD1 . LEU B 112 ? 1.8409 1.3803 1.5545 -0.2444 0.1955 0.0547 1759 LEU B CD1 5402 C CD2 . LEU B 112 ? 1.7634 1.3574 1.5460 -0.2260 0.2178 0.0652 1759 LEU B CD2 5403 N N . GLY B 113 ? 1.7756 1.4348 1.6292 -0.3076 0.1515 0.0848 1760 GLY B N 5404 C CA . GLY B 113 ? 1.6495 1.3621 1.5615 -0.3141 0.1503 0.0979 1760 GLY B CA 5405 C C . GLY B 113 ? 1.5530 1.2889 1.4898 -0.2906 0.1743 0.1003 1760 GLY B C 5406 O O . GLY B 113 ? 1.5233 1.2377 1.4357 -0.2716 0.1868 0.0927 1760 GLY B O 5407 N N . PRO B 114 ? 1.5245 1.3068 1.5102 -0.2917 0.1806 0.1102 1761 PRO B N 5408 C CA . PRO B 114 ? 1.5633 1.3608 1.5625 -0.2749 0.2048 0.1099 1761 PRO B CA 5409 C C . PRO B 114 ? 1.5312 1.3448 1.5425 -0.2487 0.2140 0.1043 1761 PRO B C 5410 O O . PRO B 114 ? 1.4087 1.2347 1.4347 -0.2429 0.2030 0.1059 1761 PRO B O 5411 C CB . PRO B 114 ? 1.6326 1.4774 1.6797 -0.2862 0.2079 0.1229 1761 PRO B CB 5412 C CG . PRO B 114 ? 1.6001 1.4729 1.6771 -0.2953 0.1864 0.1296 1761 PRO B CG 5413 C CD . PRO B 114 ? 1.5310 1.3600 1.5638 -0.3047 0.1661 0.1223 1761 PRO B CD 5414 N N . TYR B 115 ? 1.6165 1.4290 1.6215 -0.2338 0.2333 0.0986 1762 TYR B N 5415 C CA . TYR B 115 ? 1.6281 1.4555 1.6471 -0.2109 0.2431 0.0908 1762 TYR B CA 5416 C C . TYR B 115 ? 1.6009 1.4749 1.6701 -0.2062 0.2435 0.0962 1762 TYR B C 5417 O O . TYR B 115 ? 1.7318 1.6367 1.8237 -0.2093 0.2541 0.1014 1762 TYR B O 5418 C CB . TYR B 115 ? 1.7361 1.5634 1.7426 -0.1999 0.2620 0.0844 1762 TYR B CB 5419 C CG . TYR B 115 ? 1.6671 1.4541 1.6308 -0.1966 0.2644 0.0788 1762 TYR B CG 5420 C CD1 . TYR B 115 ? 1.4858 1.2486 1.4331 -0.1891 0.2583 0.0726 1762 TYR B CD1 5421 C CD2 . TYR B 115 ? 1.7322 1.5083 1.6747 -0.1996 0.2742 0.0822 1762 TYR B CD2 5422 C CE1 . TYR B 115 ? 1.5586 1.2899 1.4718 -0.1842 0.2624 0.0687 1762 TYR B CE1 5423 C CE2 . TYR B 115 ? 1.6693 1.4111 1.5770 -0.1939 0.2768 0.0789 1762 TYR B CE2 5424 C CZ . TYR B 115 ? 1.6584 1.3794 1.5529 -0.1858 0.2712 0.0715 1762 TYR B CZ 5425 O OH . TYR B 115 ? 1.8092 1.5009 1.6737 -0.1783 0.2754 0.0693 1762 TYR B OH 5426 N N . ILE B 116 ? 1.4401 1.3197 1.5272 -0.1982 0.2331 0.0970 1763 ILE B N 5427 C CA . ILE B 116 ? 1.4123 1.3324 1.5499 -0.1852 0.2362 0.1001 1763 ILE B CA 5428 C C . ILE B 116 ? 1.4741 1.3874 1.6131 -0.1623 0.2504 0.0853 1763 ILE B C 5429 O O . ILE B 116 ? 1.6174 1.5061 1.7455 -0.1549 0.2447 0.0815 1763 ILE B O 5430 C CB . ILE B 116 ? 1.3654 1.2956 1.5257 -0.1874 0.2159 0.1119 1763 ILE B CB 5431 C CG1 . ILE B 116 ? 1.4732 1.3994 1.6191 -0.2129 0.1960 0.1226 1763 ILE B CG1 5432 C CG2 . ILE B 116 ? 1.2736 1.2502 1.4927 -0.1742 0.2198 0.1186 1763 ILE B CG2 5433 C CD1 . ILE B 116 ? 1.5958 1.5444 1.7685 -0.2163 0.1740 0.1368 1763 ILE B CD1 5434 N N . ARG B 117 ? 1.4953 1.4304 1.6465 -0.1522 0.2687 0.0771 1764 ARG B N 5435 C CA . ARG B 117 ? 1.5419 1.4698 1.6907 -0.1324 0.2813 0.0589 1764 ARG B CA 5436 C C . ARG B 117 ? 1.5748 1.5317 1.7701 -0.1137 0.2894 0.0537 1764 ARG B C 5437 O O . ARG B 117 ? 1.7704 1.7633 2.0006 -0.1145 0.2912 0.0649 1764 ARG B O 5438 C CB . ARG B 117 ? 1.4842 1.4102 1.6021 -0.1323 0.2959 0.0496 1764 ARG B CB 5439 C CG . ARG B 117 ? 1.4850 1.3814 1.5605 -0.1472 0.2903 0.0554 1764 ARG B CG 5440 C CD . ARG B 117 ? 1.5931 1.5064 1.6608 -0.1579 0.2997 0.0648 1764 ARG B CD 5441 N NE . ARG B 117 ? 1.6653 1.5499 1.6913 -0.1657 0.3005 0.0673 1764 ARG B NE 5442 C CZ . ARG B 117 ? 1.6492 1.5172 1.6479 -0.1554 0.3051 0.0569 1764 ARG B CZ 5443 N NH1 . ARG B 117 ? 1.5911 1.4647 1.5972 -0.1395 0.3080 0.0407 1764 ARG B NH1 5444 N NH2 . ARG B 117 ? 1.7399 1.5844 1.7057 -0.1616 0.3057 0.0630 1764 ARG B NH2 5445 N N . ALA B 118 ? 1.4834 1.4244 1.6819 -0.0970 0.2943 0.0370 1765 ALA B N 5446 C CA . ALA B 118 ? 1.4745 1.4332 1.7148 -0.0763 0.3032 0.0281 1765 ALA B CA 5447 C C . ALA B 118 ? 1.5159 1.4472 1.7473 -0.0622 0.3088 0.0041 1765 ALA B C 5448 O O . ALA B 118 ? 1.5798 1.4783 1.7876 -0.0687 0.2994 0.0018 1765 ALA B O 5449 C CB . ALA B 118 ? 1.4503 1.4156 1.7297 -0.0741 0.2893 0.0461 1765 ALA B CB 5450 N N . GLU B 119 ? 1.5118 1.4569 1.7626 -0.0434 0.3242 -0.0145 1766 GLU B N 5451 C CA . GLU B 119 ? 1.5799 1.4960 1.8318 -0.0299 0.3266 -0.0389 1766 GLU B CA 5452 C C . GLU B 119 ? 1.6592 1.5598 1.9540 -0.0195 0.3186 -0.0320 1766 GLU B C 5453 O O . GLU B 119 ? 1.7999 1.7169 2.1213 -0.0216 0.3108 -0.0078 1766 GLU B O 5454 C CB . GLU B 119 ? 1.5975 1.5281 1.8436 -0.0142 0.3459 -0.0661 1766 GLU B CB 5455 C CG . GLU B 119 ? 1.7992 1.7288 1.9940 -0.0239 0.3491 -0.0772 1766 GLU B CG 5456 C CD . GLU B 119 ? 2.0782 2.0341 2.2590 -0.0106 0.3695 -0.0977 1766 GLU B CD 5457 O OE1 . GLU B 119 ? 2.3626 2.3207 2.5670 0.0094 0.3807 -0.1175 1766 GLU B OE1 5458 O OE2 . GLU B 119 ? 2.0510 2.0243 2.1958 -0.0192 0.3752 -0.0934 1766 GLU B OE2 5459 N N . VAL B 120 ? 1.5860 1.4546 1.8888 -0.0094 0.3187 -0.0513 1767 VAL B N 5460 C CA . VAL B 120 ? 1.5465 1.3925 1.8863 -0.0031 0.3085 -0.0386 1767 VAL B CA 5461 C C . VAL B 120 ? 1.5236 1.3858 1.9135 0.0192 0.3167 -0.0368 1767 VAL B C 5462 O O . VAL B 120 ? 1.5180 1.3910 1.9385 0.0207 0.3073 -0.0098 1767 VAL B O 5463 C CB . VAL B 120 ? 1.6215 1.4225 1.9587 -0.0041 0.3027 -0.0529 1767 VAL B CB 5464 C CG1 . VAL B 120 ? 1.7759 1.5671 2.0662 -0.0232 0.2972 -0.0578 1767 VAL B CG1 5465 C CG2 . VAL B 120 ? 1.6728 1.4582 2.0306 0.0155 0.3146 -0.0847 1767 VAL B CG2 5466 N N . GLU B 121 ? 1.6031 1.4689 2.0013 0.0376 0.3342 -0.0649 1768 GLU B N 5467 C CA . GLU B 121 ? 1.8943 1.7768 2.3440 0.0624 0.3445 -0.0628 1768 GLU B CA 5468 C C . GLU B 121 ? 1.8793 1.8166 2.3519 0.0608 0.3451 -0.0335 1768 GLU B C 5469 O O . GLU B 121 ? 1.7245 1.6829 2.2481 0.0797 0.3493 -0.0216 1768 GLU B O 5470 C CB . GLU B 121 ? 2.1068 1.9815 2.5576 0.0846 0.3656 -0.1020 1768 GLU B CB 5471 C CG . GLU B 121 ? 2.2103 2.0269 2.6601 0.0892 0.3612 -0.1283 1768 GLU B CG 5472 C CD . GLU B 121 ? 2.2719 2.0547 2.7689 0.0962 0.3490 -0.1091 1768 GLU B CD 5473 O OE1 . GLU B 121 ? 2.1212 1.9208 2.6665 0.1151 0.3527 -0.0908 1768 GLU B OE1 5474 O OE2 . GLU B 121 ? 2.2287 1.9686 2.7169 0.0830 0.3356 -0.1105 1768 GLU B OE2 5475 N N . ASP B 122 ? 1.9751 1.9320 2.4123 0.0370 0.3387 -0.0203 1769 ASP B N 5476 C CA . ASP B 122 ? 1.8158 1.8244 2.2650 0.0280 0.3391 0.0032 1769 ASP B CA 5477 C C . ASP B 122 ? 1.7367 1.7632 2.2226 0.0226 0.3200 0.0378 1769 ASP B C 5478 O O . ASP B 122 ? 1.7914 1.7900 2.2908 0.0257 0.3052 0.0482 1769 ASP B O 5479 C CB . ASP B 122 ? 1.7330 1.7452 2.1298 0.0021 0.3360 0.0056 1769 ASP B CB 5480 C CG . ASP B 122 ? 1.8578 1.8714 2.2186 0.0062 0.3555 -0.0215 1769 ASP B CG 5481 O OD1 . ASP B 122 ? 2.0946 2.0916 2.4555 0.0249 0.3675 -0.0491 1769 ASP B OD1 5482 O OD2 . ASP B 122 ? 1.8359 1.8656 2.1656 -0.0104 0.3578 -0.0149 1769 ASP B OD2 5483 N N . ASN B 123 ? 1.5413 1.6162 2.0428 0.0132 0.3196 0.0565 1770 ASN B N 5484 C CA . ASN B 123 ? 1.4832 1.5813 2.0112 0.0016 0.2976 0.0890 1770 ASN B CA 5485 C C . ASN B 123 ? 1.5541 1.6595 2.0443 -0.0300 0.2853 0.1004 1770 ASN B C 5486 O O . ASN B 123 ? 1.7371 1.8534 2.2029 -0.0391 0.2989 0.0906 1770 ASN B O 5487 C CB . ASN B 123 ? 1.4714 1.6260 2.0641 0.0179 0.3050 0.1035 1770 ASN B CB 5488 C CG . ASN B 123 ? 1.7102 1.8556 2.3498 0.0498 0.3102 0.1011 1770 ASN B CG 5489 O OD1 . ASN B 123 ? 1.7556 1.8500 2.3806 0.0560 0.3043 0.0924 1770 ASN B OD1 5490 N ND2 . ASN B 123 ? 1.8930 2.0874 2.5929 0.0710 0.3222 0.1099 1770 ASN B ND2 5491 N N . ILE B 124 ? 1.5089 1.6058 1.9918 -0.0465 0.2596 0.1211 1771 ILE B N 5492 C CA . ILE B 124 ? 1.4389 1.5423 1.8906 -0.0765 0.2460 0.1320 1771 ILE B CA 5493 C C . ILE B 124 ? 1.4886 1.6389 1.9843 -0.0847 0.2282 0.1587 1771 ILE B C 5494 O O . ILE B 124 ? 1.4813 1.6404 2.0108 -0.0729 0.2148 0.1739 1771 ILE B O 5495 C CB . ILE B 124 ? 1.3804 1.4338 1.7763 -0.0923 0.2304 0.1306 1771 ILE B CB 5496 C CG1 . ILE B 124 ? 1.4105 1.4221 1.7766 -0.0808 0.2452 0.1072 1771 ILE B CG1 5497 C CG2 . ILE B 124 ? 1.4235 1.4746 1.7803 -0.1208 0.2226 0.1338 1771 ILE B CG2 5498 C CD1 . ILE B 124 ? 1.5880 1.5542 1.9097 -0.0910 0.2325 0.1078 1771 ILE B CD1 5499 N N . MET B 125 ? 1.5257 1.7081 2.0242 -0.1052 0.2276 0.1659 1772 MET B N 5500 C CA . MET B 125 ? 1.5412 1.7677 2.0769 -0.1203 0.2057 0.1911 1772 MET B CA 5501 C C . MET B 125 ? 1.5164 1.7330 2.0126 -0.1565 0.1900 0.1949 1772 MET B C 5502 O O . MET B 125 ? 1.4916 1.7125 1.9745 -0.1695 0.2042 0.1886 1772 MET B O 5503 C CB . MET B 125 ? 1.6142 1.9067 2.2209 -0.1065 0.2204 0.2013 1772 MET B CB 5504 C CG . MET B 125 ? 1.7211 2.0664 2.3770 -0.1206 0.1948 0.2299 1772 MET B CG 5505 S SD . MET B 125 ? 1.8494 2.2798 2.5987 -0.1005 0.2138 0.2452 1772 MET B SD 5506 C CE . MET B 125 ? 2.0453 2.5336 2.8300 -0.1389 0.1829 0.2746 1772 MET B CE 5507 N N . VAL B 126 ? 1.4517 1.6522 1.9270 -0.1722 0.1605 0.2053 1773 VAL B N 5508 C CA . VAL B 126 ? 1.4985 1.6850 1.9363 -0.2059 0.1431 0.2068 1773 VAL B CA 5509 C C . VAL B 126 ? 1.6558 1.8908 2.1351 -0.2233 0.1147 0.2295 1773 VAL B C 5510 O O . VAL B 126 ? 1.7699 2.0066 2.2504 -0.2214 0.0901 0.2413 1773 VAL B O 5511 C CB . VAL B 126 ? 1.5184 1.6414 1.8853 -0.2124 0.1327 0.1957 1773 VAL B CB 5512 C CG1 . VAL B 126 ? 1.6822 1.7804 2.0042 -0.2438 0.1234 0.1900 1773 VAL B CG1 5513 C CG2 . VAL B 126 ? 1.4810 1.5656 1.8215 -0.1902 0.1579 0.1769 1773 VAL B CG2 5514 N N . THR B 127 ? 1.6782 1.9567 2.1949 -0.2397 0.1187 0.2374 1774 THR B N 5515 C CA . THR B 127 ? 1.6338 1.9609 2.1905 -0.2645 0.0901 0.2580 1774 THR B CA 5516 C C . THR B 127 ? 1.6034 1.8895 2.1021 -0.3025 0.0675 0.2509 1774 THR B C 5517 O O . THR B 127 ? 1.4249 1.6905 1.9013 -0.3205 0.0803 0.2418 1774 THR B O 5518 C CB . THR B 127 ? 1.6444 2.0424 2.2762 -0.2649 0.1061 0.2722 1774 THR B CB 5519 O OG1 . THR B 127 ? 1.6371 2.0304 2.2706 -0.2397 0.1463 0.2591 1774 THR B OG1 5520 C CG2 . THR B 127 ? 1.5808 2.0464 2.2892 -0.2496 0.0929 0.2956 1774 THR B CG2 5521 N N . PHE B 128 ? 1.6377 1.9100 2.1104 -0.3127 0.0344 0.2552 1775 PHE B N 5522 C CA . PHE B 128 ? 1.6894 1.9072 2.0904 -0.3405 0.0134 0.2423 1775 PHE B CA 5523 C C . PHE B 128 ? 1.7715 2.0183 2.1869 -0.3766 -0.0245 0.2533 1775 PHE B C 5524 O O . PHE B 128 ? 1.7025 2.0012 2.1624 -0.3750 -0.0483 0.2727 1775 PHE B O 5525 C CB . PHE B 128 ? 1.6994 1.8702 2.0436 -0.3232 0.0072 0.2348 1775 PHE B CB 5526 C CG . PHE B 128 ? 1.7838 1.9051 2.0546 -0.3478 -0.0169 0.2231 1775 PHE B CG 5527 C CD1 . PHE B 128 ? 1.7938 1.8666 2.0170 -0.3682 -0.0093 0.2040 1775 PHE B CD1 5528 C CD2 . PHE B 128 ? 1.8002 1.9209 2.0460 -0.3485 -0.0459 0.2310 1775 PHE B CD2 5529 C CE1 . PHE B 128 ? 1.8086 1.8320 1.9625 -0.3881 -0.0294 0.1903 1775 PHE B CE1 5530 C CE2 . PHE B 128 ? 1.8279 1.9021 1.9999 -0.3693 -0.0661 0.2174 1775 PHE B CE2 5531 C CZ . PHE B 128 ? 1.8461 1.8705 1.9725 -0.3886 -0.0574 0.1955 1775 PHE B CZ 5532 N N . ARG B 129 ? 1.8645 2.0754 2.2422 -0.4090 -0.0312 0.2405 1776 ARG B N 5533 C CA . ARG B 129 ? 1.8596 2.0886 2.2460 -0.4496 -0.0677 0.2458 1776 ARG B CA 5534 C C . ARG B 129 ? 1.8401 1.9985 2.1410 -0.4731 -0.0889 0.2242 1776 ARG B C 5535 O O . ARG B 129 ? 1.7633 1.8619 2.0162 -0.4790 -0.0712 0.2056 1776 ARG B O 5536 C CB . ARG B 129 ? 1.8753 2.1376 2.3152 -0.4737 -0.0579 0.2541 1776 ARG B CB 5537 C CG . ARG B 129 ? 1.9056 2.2105 2.3832 -0.5136 -0.0972 0.2665 1776 ARG B CG 5538 C CD . ARG B 129 ? 1.8619 2.2621 2.4336 -0.5030 -0.1034 0.2953 1776 ARG B CD 5539 N NE . ARG B 129 ? 1.8868 2.3357 2.5283 -0.5086 -0.0775 0.3094 1776 ARG B NE 5540 C CZ . ARG B 129 ? 2.0456 2.5339 2.7354 -0.5478 -0.0942 0.3222 1776 ARG B CZ 5541 N NH1 . ARG B 129 ? 2.0757 2.5589 2.7512 -0.5858 -0.1397 0.3200 1776 ARG B NH1 5542 N NH2 . ARG B 129 ? 2.1147 2.6488 2.8671 -0.5502 -0.0656 0.3374 1776 ARG B NH2 5543 N N . ASN B 130 ? 1.8979 2.0657 2.1807 -0.4856 -0.1272 0.2274 1777 ASN B N 5544 C CA . ASN B 130 ? 1.9909 2.0963 2.1902 -0.5074 -0.1504 0.2057 1777 ASN B CA 5545 C C . ASN B 130 ? 2.0593 2.1629 2.2673 -0.5537 -0.1742 0.1998 1777 ASN B C 5546 O O . ASN B 130 ? 2.0864 2.2261 2.3122 -0.5804 -0.2143 0.2072 1777 ASN B O 5547 C CB . ASN B 130 ? 2.0948 2.2106 2.2633 -0.4992 -0.1805 0.2118 1777 ASN B CB 5548 C CG . ASN B 130 ? 2.2195 2.2694 2.2922 -0.5176 -0.2015 0.1869 1777 ASN B CG 5549 O OD1 . ASN B 130 ? 2.2572 2.2612 2.2969 -0.5451 -0.2043 0.1660 1777 ASN B OD1 5550 N ND2 . ASN B 130 ? 2.2277 2.2717 2.2546 -0.5019 -0.2156 0.1897 1777 ASN B ND2 5551 N N . GLN B 131 ? 2.0562 2.1176 2.2534 -0.5636 -0.1498 0.1874 1778 GLN B N 5552 C CA . GLN B 131 ? 1.9922 2.0372 2.1939 -0.6078 -0.1672 0.1804 1778 GLN B CA 5553 C C . GLN B 131 ? 1.9809 1.9476 2.0916 -0.6267 -0.1889 0.1509 1778 GLN B C 5554 O O . GLN B 131 ? 2.0150 1.9337 2.1051 -0.6563 -0.1924 0.1360 1778 GLN B O 5555 C CB . GLN B 131 ? 1.9838 2.0106 2.2073 -0.6080 -0.1300 0.1816 1778 GLN B CB 5556 C CG . GLN B 131 ? 2.0929 2.2021 2.4143 -0.6099 -0.1178 0.2101 1778 GLN B CG 5557 C CD . GLN B 131 ? 2.2517 2.3416 2.5886 -0.6175 -0.0853 0.2128 1778 GLN B CD 5558 O OE1 . GLN B 131 ? 2.3898 2.4072 2.6662 -0.6096 -0.0653 0.1951 1778 GLN B OE1 5559 N NE2 . GLN B 131 ? 2.1851 2.3425 2.6044 -0.6320 -0.0790 0.2372 1778 GLN B NE2 5560 N N . ALA B 132 ? 1.9281 1.8795 1.9829 -0.6087 -0.2018 0.1428 1779 ALA B N 5561 C CA . ALA B 132 ? 2.0330 1.9080 1.9929 -0.6206 -0.2172 0.1126 1779 ALA B CA 5562 C C . ALA B 132 ? 2.1559 2.0491 2.0971 -0.6518 -0.2692 0.1082 1779 ALA B C 5563 O O . ALA B 132 ? 2.1031 2.0672 2.1131 -0.6720 -0.2958 0.1288 1779 ALA B O 5564 C CB . ALA B 132 ? 1.9374 1.7708 1.8330 -0.5806 -0.1920 0.1028 1779 ALA B CB 5565 N N . SER B 133 ? 2.2786 2.1085 2.1256 -0.6552 -0.2828 0.0808 1780 SER B N 5566 C CA . SER B 133 ? 2.3384 2.1728 2.1446 -0.6828 -0.3320 0.0701 1780 SER B CA 5567 C C . SER B 133 ? 2.4754 2.3553 2.2655 -0.6566 -0.3464 0.0876 1780 SER B C 5568 O O . SER B 133 ? 2.5659 2.5079 2.3867 -0.6730 -0.3863 0.1041 1780 SER B O 5569 C CB . SER B 133 ? 2.3123 2.0501 2.0193 -0.6990 -0.3368 0.0288 1780 SER B CB 5570 O OG . SER B 133 ? 2.3885 2.1214 2.0339 -0.7183 -0.3805 0.0134 1780 SER B OG 5571 N N . ARG B 134 ? 2.5113 2.3630 2.2577 -0.6163 -0.3144 0.0869 1781 ARG B N 5572 C CA . ARG B 134 ? 2.4671 2.3508 2.1899 -0.5910 -0.3249 0.1039 1781 ARG B CA 5573 C C . ARG B 134 ? 2.3390 2.2762 2.1356 -0.5549 -0.2975 0.1369 1781 ARG B C 5574 O O . ARG B 134 ? 2.2169 2.1502 2.0600 -0.5431 -0.2625 0.1394 1781 ARG B O 5575 C CB . ARG B 134 ? 2.5508 2.3648 2.1679 -0.5722 -0.3097 0.0807 1781 ARG B CB 5576 C CG . ARG B 134 ? 2.9311 2.6680 2.4678 -0.5988 -0.3193 0.0397 1781 ARG B CG 5577 C CD . ARG B 134 ? 3.2085 2.9522 2.6983 -0.6326 -0.3726 0.0269 1781 ARG B CD 5578 N NE . ARG B 134 ? 3.3331 2.9941 2.7107 -0.6384 -0.3736 -0.0134 1781 ARG B NE 5579 C CZ . ARG B 134 ? 3.2851 2.8743 2.6303 -0.6594 -0.3678 -0.0482 1781 ARG B CZ 5580 N NH1 . ARG B 134 ? 3.2038 2.7928 2.6195 -0.6796 -0.3612 -0.0459 1781 ARG B NH1 5581 N NH2 . ARG B 134 ? 3.3394 2.8550 2.5800 -0.6590 -0.3670 -0.0846 1781 ARG B NH2 5582 N N . PRO B 135 ? 2.3191 2.3037 2.1241 -0.5363 -0.3131 0.1621 1782 PRO B N 5583 C CA . PRO B 135 ? 2.2205 2.2495 2.0932 -0.5001 -0.2875 0.1921 1782 PRO B CA 5584 C C . PRO B 135 ? 2.2565 2.2327 2.0979 -0.4670 -0.2394 0.1826 1782 PRO B C 5585 O O . PRO B 135 ? 2.3931 2.3186 2.1514 -0.4595 -0.2342 0.1674 1782 PRO B O 5586 C CB . PRO B 135 ? 2.1456 2.2189 2.0104 -0.4898 -0.3182 0.2177 1782 PRO B CB 5587 C CG . PRO B 135 ? 2.2025 2.2306 1.9629 -0.5082 -0.3436 0.1947 1782 PRO B CG 5588 C CD . PRO B 135 ? 2.3059 2.3019 2.0539 -0.5469 -0.3548 0.1641 1782 PRO B CD 5589 N N . TYR B 136 ? 2.1472 2.1362 2.0525 -0.4488 -0.2053 0.1902 1783 TYR B N 5590 C CA . TYR B 136 ? 2.0437 1.9987 1.9367 -0.4144 -0.1623 0.1874 1783 TYR B CA 5591 C C . TYR B 136 ? 1.9764 1.9809 1.9520 -0.3857 -0.1433 0.2130 1783 TYR B C 5592 O O . TYR B 136 ? 1.9419 2.0076 1.9860 -0.3902 -0.1605 0.2333 1783 TYR B O 5593 C CB . TYR B 136 ? 1.9395 1.8354 1.8028 -0.4183 -0.1322 0.1602 1783 TYR B CB 5594 C CG . TYR B 136 ? 2.0164 1.8549 1.8027 -0.4440 -0.1454 0.1319 1783 TYR B CG 5595 C CD1 . TYR B 136 ? 2.2196 2.0375 1.9329 -0.4501 -0.1693 0.1241 1783 TYR B CD1 5596 C CD2 . TYR B 136 ? 2.0374 1.8389 1.8210 -0.4606 -0.1325 0.1125 1783 TYR B CD2 5597 C CE1 . TYR B 136 ? 2.3330 2.0942 1.9731 -0.4725 -0.1807 0.0942 1783 TYR B CE1 5598 C CE2 . TYR B 136 ? 2.1706 1.9132 1.8858 -0.4831 -0.1438 0.0851 1783 TYR B CE2 5599 C CZ . TYR B 136 ? 2.2699 1.9914 1.9132 -0.4887 -0.1676 0.0741 1783 TYR B CZ 5600 O OH . TYR B 136 ? 2.2816 1.9404 1.8546 -0.5092 -0.1771 0.0432 1783 TYR B OH 5601 N N . SER B 137 ? 1.9637 1.9416 1.9334 -0.3566 -0.1085 0.2110 1784 SER B N 5602 C CA . SER B 137 ? 2.0402 2.0535 2.0787 -0.3269 -0.0891 0.2309 1784 SER B CA 5603 C C . SER B 137 ? 1.9619 1.9482 2.0130 -0.3116 -0.0485 0.2159 1784 SER B C 5604 O O . SER B 137 ? 1.7732 1.7186 1.7853 -0.3239 -0.0365 0.1939 1784 SER B O 5605 C CB . SER B 137 ? 2.1342 2.1497 2.1576 -0.3039 -0.0941 0.2507 1784 SER B CB 5606 O OG . SER B 137 ? 1.8825 1.9479 1.9812 -0.2829 -0.0949 0.2774 1784 SER B OG 5607 N N . PHE B 138 ? 1.9640 1.9729 2.0696 -0.2848 -0.0285 0.2274 1785 PHE B N 5608 C CA . PHE B 138 ? 1.9067 1.8919 2.0201 -0.2695 0.0075 0.2126 1785 PHE B CA 5609 C C . PHE B 138 ? 1.9324 1.8787 2.0110 -0.2482 0.0245 0.2097 1785 PHE B C 5610 O O . PHE B 138 ? 2.0662 1.9673 2.0845 -0.2533 0.0319 0.1944 1785 PHE B O 5611 C CB . PHE B 138 ? 1.8654 1.8949 2.0568 -0.2553 0.0226 0.2203 1785 PHE B CB 5612 C CG . PHE B 138 ? 1.9175 1.9248 2.1107 -0.2428 0.0571 0.2027 1785 PHE B CG 5613 C CD1 . PHE B 138 ? 1.8910 1.8610 2.0394 -0.2575 0.0678 0.1836 1785 PHE B CD1 5614 C CD2 . PHE B 138 ? 1.8884 1.9110 2.1272 -0.2159 0.0780 0.2050 1785 PHE B CD2 5615 C CE1 . PHE B 138 ? 1.8135 1.7669 1.9623 -0.2456 0.0972 0.1696 1785 PHE B CE1 5616 C CE2 . PHE B 138 ? 1.8330 1.8369 2.0691 -0.2053 0.1071 0.1874 1785 PHE B CE2 5617 C CZ . PHE B 138 ? 1.8307 1.8026 2.0216 -0.2202 0.1160 0.1710 1785 PHE B CZ 5618 N N . TYR B 139 ? 1.8454 1.8092 1.9654 -0.2241 0.0317 0.2247 1786 TYR B N 5619 C CA . TYR B 139 ? 1.9329 1.8639 2.0284 -0.2054 0.0452 0.2270 1786 TYR B CA 5620 C C . TYR B 139 ? 1.9863 1.8757 2.0539 -0.1993 0.0737 0.2054 1786 TYR B C 5621 O O . TYR B 139 ? 1.8574 1.7164 1.8734 -0.2127 0.0774 0.1889 1786 TYR B O 5622 C CB . TYR B 139 ? 1.9869 1.9034 2.0276 -0.2120 0.0250 0.2387 1786 TYR B CB 5623 C CG . TYR B 139 ? 1.9892 1.8796 2.0119 -0.1935 0.0380 0.2484 1786 TYR B CG 5624 C CD1 . TYR B 139 ? 1.9983 1.9084 2.0602 -0.1762 0.0320 0.2752 1786 TYR B CD1 5625 C CD2 . TYR B 139 ? 1.9742 1.8215 1.9438 -0.1935 0.0563 0.2331 1786 TYR B CD2 5626 C CE1 . TYR B 139 ? 2.0712 1.9565 2.1196 -0.1618 0.0441 0.2867 1786 TYR B CE1 5627 C CE2 . TYR B 139 ? 2.0546 1.8823 2.0125 -0.1788 0.0687 0.2443 1786 TYR B CE2 5628 C CZ . TYR B 139 ? 2.0215 1.8672 2.0185 -0.1642 0.0625 0.2713 1786 TYR B CZ 5629 O OH . TYR B 139 ? 1.8193 1.6444 1.8080 -0.1518 0.0753 0.2849 1786 TYR B OH 5630 N N . SER B 140 ? 2.0623 1.9508 2.1666 -0.1782 0.0927 0.2061 1787 SER B N 5631 C CA . SER B 140 ? 1.9740 1.8254 2.0547 -0.1683 0.1144 0.1943 1787 SER B CA 5632 C C . SER B 140 ? 1.8617 1.7092 1.9603 -0.1517 0.1140 0.2137 1787 SER B C 5633 O O . SER B 140 ? 1.7845 1.6544 1.9027 -0.1488 0.0958 0.2363 1787 SER B O 5634 C CB . SER B 140 ? 1.8062 1.6572 1.9133 -0.1610 0.1369 0.1749 1787 SER B CB 5635 O OG . SER B 140 ? 1.7048 1.5627 1.8596 -0.1410 0.1473 0.1781 1787 SER B OG 5636 N N . SER B 141 ? 1.7664 1.5864 1.8598 -0.1418 0.1327 0.2070 1788 SER B N 5637 C CA . SER B 141 ? 1.7530 1.5676 1.8761 -0.1262 0.1354 0.2243 1788 SER B CA 5638 C C . SER B 141 ? 1.6795 1.5162 1.8695 -0.1117 0.1381 0.2248 1788 SER B C 5639 O O . SER B 141 ? 1.8342 1.6909 2.0573 -0.1035 0.1250 0.2470 1788 SER B O 5640 C CB . SER B 141 ? 1.8829 1.6651 1.9921 -0.1216 0.1550 0.2151 1788 SER B CB 5641 O OG . SER B 141 ? 2.1810 1.9450 2.2331 -0.1305 0.1547 0.2197 1788 SER B OG 5642 N N . LEU B 142 ? 1.5653 1.4003 1.7724 -0.1080 0.1550 0.2004 1789 LEU B N 5643 C CA . LEU B 142 ? 1.5956 1.4430 1.8610 -0.0905 0.1650 0.1937 1789 LEU B CA 5644 C C . LEU B 142 ? 1.7286 1.6158 2.0410 -0.0830 0.1539 0.2082 1789 LEU B C 5645 O O . LEU B 142 ? 2.0172 1.9114 2.3813 -0.0635 0.1606 0.2099 1789 LEU B O 5646 C CB . LEU B 142 ? 1.5479 1.3940 1.8101 -0.0913 0.1828 0.1641 1789 LEU B CB 5647 C CG . LEU B 142 ? 1.6496 1.4680 1.8639 -0.1016 0.1927 0.1471 1789 LEU B CG 5648 C CD1 . LEU B 142 ? 1.6910 1.5171 1.9086 -0.1002 0.2078 0.1221 1789 LEU B CD1 5649 C CD2 . LEU B 142 ? 1.7652 1.5525 1.9784 -0.0956 0.1984 0.1493 1789 LEU B CD2 5650 N N . ILE B 143 ? 1.6827 1.5954 1.9782 -0.0985 0.1371 0.2174 1790 ILE B N 5651 C CA . ILE B 143 ? 1.6268 1.5866 1.9651 -0.0972 0.1241 0.2311 1790 ILE B CA 5652 C C . ILE B 143 ? 1.6342 1.6133 2.0259 -0.0773 0.1135 0.2582 1790 ILE B C 5653 O O . ILE B 143 ? 1.6949 1.6938 2.0843 -0.0831 0.0896 0.2833 1790 ILE B O 5654 C CB . ILE B 143 ? 1.6066 1.5788 1.9034 -0.1233 0.1036 0.2359 1790 ILE B CB 5655 C CG1 . ILE B 143 ? 1.5746 1.5944 1.9079 -0.1313 0.0968 0.2376 1790 ILE B CG1 5656 C CG2 . ILE B 143 ? 1.6606 1.6249 1.9249 -0.1295 0.0807 0.2586 1790 ILE B CG2 5657 C CD1 . ILE B 143 ? 1.5755 1.5916 1.8624 -0.1601 0.0870 0.2280 1790 ILE B CD1 5658 N N . SER B 144 ? 1.5849 1.5583 2.0243 -0.0535 0.1306 0.2525 1791 SER B N 5659 C CA . SER B 144 ? 1.5827 1.5536 2.0668 -0.0313 0.1255 0.2764 1791 SER B CA 5660 C C . SER B 144 ? 1.5769 1.5982 2.1271 -0.0154 0.1166 0.2955 1791 SER B C 5661 O O . SER B 144 ? 1.4902 1.5378 2.0747 -0.0076 0.1307 0.2798 1791 SER B O 5662 C CB . SER B 144 ? 1.7080 1.6366 2.2088 -0.0136 0.1482 0.2587 1791 SER B CB 5663 O OG . SER B 144 ? 1.8135 1.6978 2.2656 -0.0252 0.1525 0.2519 1791 SER B OG 5664 N N . TYR B 145 ? 1.6931 1.7285 2.2624 -0.0086 0.0949 0.3308 1792 TYR B N 5665 C CA . TYR B 145 ? 1.7286 1.8219 2.3571 0.0025 0.0780 0.3573 1792 TYR B CA 5666 C C . TYR B 145 ? 1.6916 1.7936 2.3971 0.0381 0.0868 0.3713 1792 TYR B C 5667 O O . TYR B 145 ? 1.6581 1.7243 2.3817 0.0567 0.1116 0.3515 1792 TYR B O 5668 C CB . TYR B 145 ? 1.7252 1.8423 2.3273 -0.0140 0.0429 0.3896 1792 TYR B CB 5669 C CG . TYR B 145 ? 1.8732 1.9878 2.4058 -0.0481 0.0324 0.3745 1792 TYR B CG 5670 C CD1 . TYR B 145 ? 1.9061 2.0335 2.4332 -0.0629 0.0442 0.3464 1792 TYR B CD1 5671 C CD2 . TYR B 145 ? 2.0544 2.1512 2.5250 -0.0648 0.0124 0.3878 1792 TYR B CD2 5672 C CE1 . TYR B 145 ? 1.8803 1.9985 2.3452 -0.0933 0.0355 0.3321 1792 TYR B CE1 5673 C CE2 . TYR B 145 ? 2.2343 2.3226 2.6394 -0.0943 0.0044 0.3706 1792 TYR B CE2 5674 C CZ . TYR B 145 ? 2.0617 2.1585 2.4659 -0.1083 0.0156 0.3428 1792 TYR B CZ 5675 O OH . TYR B 145 ? 2.0618 2.1441 2.4029 -0.1362 0.0078 0.3266 1792 TYR B OH 5676 N N . GLU B 146 ? 1.7302 1.8805 2.4815 0.0477 0.0653 0.4051 1793 GLU B N 5677 C CA . GLU B 146 ? 1.9930 2.1606 2.8251 0.0837 0.0736 0.4196 1793 GLU B CA 5678 C C . GLU B 146 ? 2.1562 2.3075 3.0105 0.1026 0.0577 0.4594 1793 GLU B C 5679 O O . GLU B 146 ? 2.0766 2.1738 2.9392 0.1204 0.0743 0.4551 1793 GLU B O 5680 C CB . GLU B 146 ? 2.1392 2.3818 3.0279 0.0880 0.0691 0.4260 1793 GLU B CB 5681 C CG . GLU B 146 ? 2.5697 2.8379 3.5481 0.1286 0.0826 0.4375 1793 GLU B CG 5682 C CD . GLU B 146 ? 2.7873 2.9906 3.7791 0.1573 0.1092 0.4216 1793 GLU B CD 5683 O OE1 . GLU B 146 ? 2.7642 2.9213 3.7172 0.1506 0.1329 0.3829 1793 GLU B OE1 5684 O OE2 . GLU B 146 ? 3.0006 3.1983 4.0435 0.1863 0.1049 0.4489 1793 GLU B OE2 5685 N N . GLU B 147 ? 2.2510 2.4496 3.1169 0.0985 0.0252 0.4983 1794 GLU B N 5686 C CA . GLU B 147 ? 2.0759 2.2691 2.9600 0.1150 0.0051 0.5440 1794 GLU B CA 5687 C C . GLU B 147 ? 1.9701 2.2376 2.9132 0.1270 -0.0238 0.5846 1794 GLU B C 5688 O O . GLU B 147 ? 1.7993 2.1185 2.8001 0.1368 -0.0187 0.5782 1794 GLU B O 5689 C CB . GLU B 147 ? 1.9917 2.1276 2.9125 0.1463 0.0293 0.5439 1794 GLU B CB 5690 C CG . GLU B 147 ? 2.0960 2.1993 3.0037 0.1524 0.0141 0.5847 1794 GLU B CG 5691 C CD . GLU B 147 ? 2.1117 2.1583 3.0671 0.1836 0.0362 0.5879 1794 GLU B CD 5692 O OE1 . GLU B 147 ? 2.1603 2.1912 3.1547 0.2009 0.0633 0.5538 1794 GLU B OE1 5693 O OE2 . GLU B 147 ? 1.9693 1.9854 2.9216 0.1904 0.0267 0.6241 1794 GLU B OE2 5694 N N . ASP B 148 ? 1.9436 2.2189 2.8717 0.1261 -0.0537 0.6275 1795 ASP B N 5695 C CA . ASP B 148 ? 1.9965 2.3381 2.9823 0.1414 -0.0843 0.6736 1795 ASP B CA 5696 C C . ASP B 148 ? 2.1018 2.4931 3.1865 0.1706 -0.0713 0.6724 1795 ASP B C 5697 O O . ASP B 148 ? 2.1933 2.5557 3.3330 0.2053 -0.0439 0.6678 1795 ASP B O 5698 C CB . ASP B 148 ? 2.0509 2.3671 3.0400 0.1609 -0.0983 0.7205 1795 ASP B CB 5699 C CG . ASP B 148 ? 2.2440 2.6055 3.3306 0.1997 -0.1093 0.7630 1795 ASP B CG 5700 O OD1 . ASP B 148 ? 2.2720 2.7120 3.3932 0.1975 -0.1382 0.7860 1795 ASP B OD1 5701 O OD2 . ASP B 148 ? 2.3188 2.6366 3.4507 0.2331 -0.0890 0.7735 1795 ASP B OD2 5702 N N . PRO B 155 ? 2.6955 3.1594 3.2545 -0.0344 -0.3026 0.7543 1802 PRO B N 5703 C CA . PRO B 155 ? 2.7062 3.1720 3.2142 -0.0727 -0.3084 0.7105 1802 PRO B CA 5704 C C . PRO B 155 ? 2.7125 3.1185 3.2009 -0.0796 -0.2633 0.6595 1802 PRO B C 5705 O O . PRO B 155 ? 2.6943 3.1195 3.2383 -0.0808 -0.2488 0.6368 1802 PRO B O 5706 C CB . PRO B 155 ? 2.5533 3.1004 3.1407 -0.0781 -0.3347 0.7188 1802 PRO B CB 5707 C CG . PRO B 155 ? 2.4666 3.0573 3.1405 -0.0411 -0.3452 0.7691 1802 PRO B CG 5708 C CD . PRO B 155 ? 2.5181 3.0587 3.1549 -0.0192 -0.3359 0.7964 1802 PRO B CD 5709 N N . ARG B 156 ? 2.5756 2.9152 2.9866 -0.0845 -0.2421 0.6431 1803 ARG B N 5710 C CA . ARG B 156 ? 2.4566 2.7396 2.8574 -0.0849 -0.1982 0.6008 1803 ARG B CA 5711 C C . ARG B 156 ? 2.4669 2.7206 2.7919 -0.1177 -0.1921 0.5563 1803 ARG B C 5712 O O . ARG B 156 ? 2.5338 2.7495 2.7747 -0.1293 -0.1920 0.5505 1803 ARG B O 5713 C CB . ARG B 156 ? 2.2943 2.5199 2.6846 -0.0623 -0.1689 0.6109 1803 ARG B CB 5714 C CG . ARG B 156 ? 2.1925 2.3862 2.6407 -0.0421 -0.1284 0.5889 1803 ARG B CG 5715 C CD . ARG B 156 ? 2.2860 2.4552 2.7097 -0.0602 -0.1044 0.5383 1803 ARG B CD 5716 N NE . ARG B 156 ? 2.2064 2.3771 2.7027 -0.0424 -0.0773 0.5192 1803 ARG B NE 5717 C CZ . ARG B 156 ? 1.9110 2.0836 2.4107 -0.0544 -0.0613 0.4824 1803 ARG B CZ 5718 N NH1 . ARG B 156 ? 1.7558 1.9257 2.1948 -0.0848 -0.0698 0.4605 1803 ARG B NH1 5719 N NH2 . ARG B 156 ? 1.6300 1.8057 2.1924 -0.0353 -0.0362 0.4677 1803 ARG B NH2 5720 N N . LYS B 157 ? 2.3769 2.6484 2.7345 -0.1304 -0.1853 0.5275 1804 LYS B N 5721 C CA . LYS B 157 ? 2.4036 2.6385 2.7128 -0.1543 -0.1663 0.4815 1804 LYS B CA 5722 C C . LYS B 157 ? 2.2691 2.5392 2.5855 -0.1850 -0.1843 0.4609 1804 LYS B C 5723 O O . LYS B 157 ? 2.0302 2.3591 2.4200 -0.1830 -0.1984 0.4756 1804 LYS B O 5724 C CB . LYS B 157 ? 2.4607 2.6306 2.6759 -0.1614 -0.1512 0.4651 1804 LYS B CB 5725 C CG . LYS B 157 ? 2.0988 2.2199 2.3234 -0.1384 -0.1112 0.4587 1804 LYS B CG 5726 C CD . LYS B 157 ? 1.9732 2.0380 2.1127 -0.1472 -0.0946 0.4411 1804 LYS B CD 5727 C CE . LYS B 157 ? 1.9428 1.9836 2.0377 -0.1701 -0.0841 0.3994 1804 LYS B CE 5728 N NZ . LYS B 157 ? 1.6915 1.7207 1.8295 -0.1651 -0.0547 0.3726 1804 LYS B NZ 5729 N N . ASN B 158 ? 2.2355 2.4693 2.4819 -0.2121 -0.1815 0.4282 1805 ASN B N 5730 C CA . ASN B 158 ? 2.1937 2.4436 2.4521 -0.2394 -0.1857 0.4033 1805 ASN B CA 5731 C C . ASN B 158 ? 2.3654 2.5701 2.5370 -0.2707 -0.1899 0.3707 1805 ASN B C 5732 O O . ASN B 158 ? 2.5537 2.7015 2.6577 -0.2668 -0.1718 0.3555 1805 ASN B O 5733 C CB . ASN B 158 ? 2.0697 2.3152 2.3849 -0.2259 -0.1472 0.3866 1805 ASN B CB 5734 C CG . ASN B 158 ? 1.9822 2.1632 2.2384 -0.2334 -0.1168 0.3508 1805 ASN B CG 5735 O OD1 . ASN B 158 ? 1.9225 2.1005 2.1802 -0.2515 -0.1085 0.3289 1805 ASN B OD1 5736 N ND2 . ASN B 158 ? 1.9335 2.0653 2.1401 -0.2199 -0.1008 0.3476 1805 ASN B ND2 5737 N N . PHE B 159 ? 2.3302 2.5613 2.5100 -0.3010 -0.2127 0.3605 1806 PHE B N 5738 C CA . PHE B 159 ? 2.1427 2.3329 2.2724 -0.3299 -0.2071 0.3250 1806 PHE B CA 5739 C C . PHE B 159 ? 2.0656 2.3023 2.2569 -0.3545 -0.2204 0.3228 1806 PHE B C 5740 O O . PHE B 159 ? 2.0346 2.3387 2.2974 -0.3522 -0.2405 0.3489 1806 PHE B O 5741 C CB . PHE B 159 ? 2.2300 2.3701 2.2521 -0.3485 -0.2239 0.3071 1806 PHE B CB 5742 C CG . PHE B 159 ? 2.3816 2.5535 2.3755 -0.3737 -0.2748 0.3167 1806 PHE B CG 5743 C CD1 . PHE B 159 ? 2.3349 2.5605 2.3801 -0.4003 -0.3068 0.3220 1806 PHE B CD1 5744 C CD2 . PHE B 159 ? 2.3437 2.4890 2.2512 -0.3733 -0.2907 0.3178 1806 PHE B CD2 5745 C CE1 . PHE B 159 ? 2.2024 2.4555 2.2171 -0.4255 -0.3560 0.3283 1806 PHE B CE1 5746 C CE2 . PHE B 159 ? 2.2950 2.4664 2.1663 -0.3968 -0.3381 0.3233 1806 PHE B CE2 5747 C CZ . PHE B 159 ? 2.2074 2.4322 2.1321 -0.4237 -0.3724 0.3277 1806 PHE B CZ 5748 N N . VAL B 160 ? 1.9707 2.1749 2.1416 -0.3763 -0.2075 0.2950 1807 VAL B N 5749 C CA . VAL B 160 ? 1.9210 2.1687 2.1479 -0.4043 -0.2220 0.2954 1807 VAL B CA 5750 C C . VAL B 160 ? 1.9579 2.1842 2.1338 -0.4470 -0.2528 0.2760 1807 VAL B C 5751 O O . VAL B 160 ? 1.8132 1.9730 1.9221 -0.4591 -0.2404 0.2472 1807 VAL B O 5752 C CB . VAL B 160 ? 1.8660 2.1193 2.1483 -0.3970 -0.1841 0.2888 1807 VAL B CB 5753 C CG1 . VAL B 160 ? 1.9125 2.2313 2.2875 -0.3689 -0.1735 0.3160 1807 VAL B CG1 5754 C CG2 . VAL B 160 ? 1.8378 2.0205 2.0663 -0.3818 -0.1455 0.2649 1807 VAL B CG2 5755 N N . LYS B 161 ? 2.1323 2.4177 2.3453 -0.4690 -0.2942 0.2928 1808 LYS B N 5756 C CA . LYS B 161 ? 2.2300 2.5073 2.4059 -0.5136 -0.3331 0.2771 1808 LYS B CA 5757 C C . LYS B 161 ? 2.1642 2.4150 2.3545 -0.5391 -0.3149 0.2560 1808 LYS B C 5758 O O . LYS B 161 ? 2.1864 2.4521 2.4350 -0.5231 -0.2792 0.2625 1808 LYS B O 5759 C CB . LYS B 161 ? 2.2086 2.5702 2.4429 -0.5305 -0.3807 0.3048 1808 LYS B CB 5760 C CG . LYS B 161 ? 2.0768 2.4786 2.3215 -0.4992 -0.3946 0.3358 1808 LYS B CG 5761 C CD . LYS B 161 ? 2.0267 2.5001 2.3014 -0.5207 -0.4504 0.3587 1808 LYS B CD 5762 C CE . LYS B 161 ? 2.0208 2.5301 2.3059 -0.4854 -0.4605 0.3932 1808 LYS B CE 5763 N NZ . LYS B 161 ? 2.0047 2.5912 2.3237 -0.5020 -0.5161 0.4207 1808 LYS B NZ 5764 N N . PRO B 162 ? 2.0711 2.2782 2.2044 -0.5777 -0.3380 0.2301 1809 PRO B N 5765 C CA . PRO B 162 ? 1.9552 2.1393 2.1079 -0.6067 -0.3262 0.2142 1809 PRO B CA 5766 C C . PRO B 162 ? 1.8432 2.1076 2.1112 -0.6144 -0.3221 0.2408 1809 PRO B C 5767 O O . PRO B 162 ? 1.7551 2.0963 2.0867 -0.6034 -0.3384 0.2694 1809 PRO B O 5768 C CB . PRO B 162 ? 2.0549 2.2046 2.1471 -0.6511 -0.3694 0.1907 1809 PRO B CB 5769 C CG . PRO B 162 ? 2.0533 2.2114 2.0898 -0.6433 -0.4027 0.1938 1809 PRO B CG 5770 C CD . PRO B 162 ? 2.0689 2.2338 2.1068 -0.5931 -0.3707 0.2112 1809 PRO B CD 5771 N N . ASN B 163 ? 1.8445 2.0937 2.1407 -0.6307 -0.2987 0.2338 1810 ASN B N 5772 C CA . ASN B 163 ? 1.9606 2.2876 2.3645 -0.6427 -0.2941 0.2591 1810 ASN B CA 5773 C C . ASN B 163 ? 1.9781 2.3824 2.4572 -0.6020 -0.2785 0.2900 1810 ASN B C 5774 O O . ASN B 163 ? 2.0295 2.5177 2.5998 -0.6099 -0.2895 0.3161 1810 ASN B O 5775 C CB . ASN B 163 ? 2.1231 2.4921 2.5614 -0.6941 -0.3448 0.2647 1810 ASN B CB 5776 C CG . ASN B 163 ? 2.1216 2.4529 2.5608 -0.7388 -0.3443 0.2496 1810 ASN B CG 5777 O OD1 . ASN B 163 ? 2.1476 2.4501 2.5948 -0.7306 -0.3029 0.2466 1810 ASN B OD1 5778 N ND2 . ASN B 163 ? 2.0378 2.3717 2.4717 -0.7876 -0.3927 0.2416 1810 ASN B ND2 5779 N N . GLU B 164 ? 2.0103 2.3869 2.4544 -0.5589 -0.2533 0.2874 1811 GLU B N 5780 C CA . GLU B 164 ? 2.0597 2.4977 2.5672 -0.5186 -0.2406 0.3139 1811 GLU B CA 5781 C C . GLU B 164 ? 2.0264 2.4405 2.5394 -0.4799 -0.1871 0.3089 1811 GLU B C 5782 O O . GLU B 164 ? 1.9923 2.3339 2.4398 -0.4772 -0.1640 0.2848 1811 GLU B O 5783 C CB . GLU B 164 ? 2.0795 2.5173 2.5485 -0.5029 -0.2690 0.3216 1811 GLU B CB 5784 C CG . GLU B 164 ? 2.0921 2.6052 2.6370 -0.4716 -0.2734 0.3552 1811 GLU B CG 5785 C CD . GLU B 164 ? 2.2313 2.7603 2.7467 -0.4728 -0.3176 0.3689 1811 GLU B CD 5786 O OE1 . GLU B 164 ? 2.3271 2.9053 2.8678 -0.5045 -0.3611 0.3799 1811 GLU B OE1 5787 O OE2 . GLU B 164 ? 2.1536 2.6479 2.6213 -0.4433 -0.3097 0.3701 1811 GLU B OE2 5788 N N . THR B 165 ? 1.9946 2.4702 2.5860 -0.4498 -0.1683 0.3308 1812 THR B N 5789 C CA . THR B 165 ? 1.9292 2.3882 2.5305 -0.4127 -0.1194 0.3250 1812 THR B CA 5790 C C . THR B 165 ? 2.0524 2.5162 2.6599 -0.3705 -0.1136 0.3352 1812 THR B C 5791 O O . THR B 165 ? 2.1671 2.6915 2.8316 -0.3602 -0.1336 0.3604 1812 THR B O 5792 C CB . THR B 165 ? 1.8119 2.3358 2.5020 -0.4079 -0.0937 0.3394 1812 THR B CB 5793 O OG1 . THR B 165 ? 1.8367 2.3984 2.5618 -0.4505 -0.1163 0.3480 1812 THR B OG1 5794 C CG2 . THR B 165 ? 1.6762 2.1606 2.3456 -0.3907 -0.0460 0.3219 1812 THR B CG2 5795 N N . LYS B 166 ? 2.1045 2.5052 2.6566 -0.3467 -0.0871 0.3174 1813 LYS B N 5796 C CA . LYS B 166 ? 2.1302 2.5321 2.6992 -0.3043 -0.0715 0.3261 1813 LYS B CA 5797 C C . LYS B 166 ? 2.1190 2.5006 2.6976 -0.2780 -0.0250 0.3115 1813 LYS B C 5798 O O . LYS B 166 ? 2.0862 2.4346 2.6329 -0.2905 -0.0049 0.2919 1813 LYS B O 5799 C CB . LYS B 166 ? 2.0394 2.3900 2.5381 -0.2966 -0.0867 0.3229 1813 LYS B CB 5800 C CG . LYS B 166 ? 1.8719 2.2458 2.4067 -0.2620 -0.0899 0.3459 1813 LYS B CG 5801 C CD . LYS B 166 ? 1.8202 2.1422 2.2832 -0.2554 -0.1009 0.3451 1813 LYS B CD 5802 C CE . LYS B 166 ? 1.8070 2.1669 2.2952 -0.2431 -0.1311 0.3773 1813 LYS B CE 5803 N NZ . LYS B 166 ? 1.6808 2.0360 2.2033 -0.2025 -0.1109 0.3915 1813 LYS B NZ 5804 N N . THR B 167 ? 2.0416 2.4429 2.6643 -0.2412 -0.0093 0.3214 1814 THR B N 5805 C CA . THR B 167 ? 1.8753 2.2594 2.5078 -0.2139 0.0321 0.3063 1814 THR B CA 5806 C C . THR B 167 ? 1.9444 2.2868 2.5543 -0.1836 0.0397 0.3033 1814 THR B C 5807 O O . THR B 167 ? 2.1025 2.4621 2.7356 -0.1703 0.0203 0.3240 1814 THR B O 5808 C CB . THR B 167 ? 1.8647 2.3184 2.5854 -0.1971 0.0500 0.3191 1814 THR B CB 5809 O OG1 . THR B 167 ? 1.8969 2.3297 2.6141 -0.1753 0.0911 0.2990 1814 THR B OG1 5810 C CG2 . THR B 167 ? 1.7294 2.2306 2.5159 -0.1704 0.0361 0.3456 1814 THR B CG2 5811 N N . TYR B 168 ? 1.8514 2.1389 2.4162 -0.1743 0.0662 0.2793 1815 TYR B N 5812 C CA . TYR B 168 ? 1.7325 1.9824 2.2866 -0.1452 0.0784 0.2750 1815 TYR B CA 5813 C C . TYR B 168 ? 1.6788 1.9166 2.2463 -0.1233 0.1162 0.2540 1815 TYR B C 5814 O O . TYR B 168 ? 1.5350 1.7567 2.0722 -0.1354 0.1331 0.2348 1815 TYR B O 5815 C CB . TYR B 168 ? 1.7831 1.9710 2.2597 -0.1556 0.0698 0.2659 1815 TYR B CB 5816 C CG . TYR B 168 ? 1.9267 2.1088 2.3571 -0.1863 0.0382 0.2724 1815 TYR B CG 5817 C CD1 . TYR B 168 ? 1.9283 2.0972 2.3211 -0.2153 0.0365 0.2573 1815 TYR B CD1 5818 C CD2 . TYR B 168 ? 1.9279 2.1116 2.3458 -0.1857 0.0108 0.2924 1815 TYR B CD2 5819 C CE1 . TYR B 168 ? 1.8724 2.0286 2.2183 -0.2431 0.0077 0.2588 1815 TYR B CE1 5820 C CE2 . TYR B 168 ? 1.8971 2.0720 2.2637 -0.2134 -0.0181 0.2945 1815 TYR B CE2 5821 C CZ . TYR B 168 ? 1.8470 2.0066 2.1777 -0.2419 -0.0193 0.2757 1815 TYR B CZ 5822 O OH . TYR B 168 ? 1.8679 2.0135 2.1456 -0.2688 -0.0477 0.2739 1815 TYR B OH 5823 N N . PHE B 169 ? 1.6970 1.9405 2.3081 -0.0908 0.1284 0.2579 1816 PHE B N 5824 C CA . PHE B 169 ? 1.6839 1.9207 2.3151 -0.0657 0.1630 0.2373 1816 PHE B CA 5825 C C . PHE B 169 ? 1.6315 1.8278 2.2654 -0.0390 0.1682 0.2346 1816 PHE B C 5826 O O . PHE B 169 ? 1.7231 1.9309 2.3900 -0.0269 0.1515 0.2581 1816 PHE B O 5827 C CB . PHE B 169 ? 1.7566 2.0602 2.4614 -0.0519 0.1752 0.2466 1816 PHE B CB 5828 C CG . PHE B 169 ? 1.7749 2.0766 2.5106 -0.0175 0.2088 0.2285 1816 PHE B CG 5829 C CD1 . PHE B 169 ? 1.7944 2.0824 2.5018 -0.0171 0.2372 0.2011 1816 PHE B CD1 5830 C CD2 . PHE B 169 ? 1.8087 2.1228 2.6014 0.0153 0.2118 0.2391 1816 PHE B CD2 5831 C CE1 . PHE B 169 ? 1.7306 2.0164 2.4608 0.0144 0.2673 0.1812 1816 PHE B CE1 5832 C CE2 . PHE B 169 ? 1.8017 2.1091 2.6203 0.0478 0.2431 0.2187 1816 PHE B CE2 5833 C CZ . PHE B 169 ? 1.7613 2.0550 2.5465 0.0467 0.2707 0.1883 1816 PHE B CZ 5834 N N . TRP B 170 ? 1.5488 1.6982 2.1491 -0.0314 0.1894 0.2078 1817 TRP B N 5835 C CA . TRP B 170 ? 1.5388 1.6414 2.1369 -0.0115 0.1940 0.2027 1817 TRP B CA 5836 C C . TRP B 170 ? 1.5179 1.5848 2.0972 0.0000 0.2217 0.1684 1817 TRP B C 5837 O O . TRP B 170 ? 1.4097 1.4717 1.9499 -0.0145 0.2323 0.1493 1817 TRP B O 5838 C CB . TRP B 170 ? 1.5906 1.6575 2.1420 -0.0282 0.1715 0.2164 1817 TRP B CB 5839 C CG . TRP B 170 ? 1.6645 1.6906 2.1476 -0.0480 0.1767 0.1961 1817 TRP B CG 5840 C CD1 . TRP B 170 ? 1.8495 1.8270 2.3051 -0.0432 0.1872 0.1808 1817 TRP B CD1 5841 C CD2 . TRP B 170 ? 1.5320 1.5625 1.9704 -0.0748 0.1717 0.1898 1817 TRP B CD2 5842 N NE1 . TRP B 170 ? 1.8255 1.7812 2.2237 -0.0633 0.1895 0.1665 1817 TRP B NE1 5843 C CE2 . TRP B 170 ? 1.5278 1.5123 1.9134 -0.0819 0.1807 0.1714 1817 TRP B CE2 5844 C CE3 . TRP B 170 ? 1.5200 1.5876 1.9609 -0.0939 0.1603 0.1985 1817 TRP B CE3 5845 C CZ2 . TRP B 170 ? 1.3907 1.3635 1.7258 -0.1041 0.1798 0.1618 1817 TRP B CZ2 5846 C CZ3 . TRP B 170 ? 1.5477 1.5988 1.9363 -0.1184 0.1590 0.1876 1817 TRP B CZ3 5847 C CH2 . TRP B 170 ? 1.3850 1.3883 1.7214 -0.1216 0.1694 0.1696 1817 TRP B CH2 5848 N N . LYS B 171 ? 1.5740 1.6158 2.1816 0.0258 0.2322 0.1609 1818 LYS B N 5849 C CA . LYS B 171 ? 1.7233 1.7297 2.3134 0.0361 0.2552 0.1262 1818 LYS B CA 5850 C C . LYS B 171 ? 1.8042 1.7578 2.3402 0.0200 0.2492 0.1169 1818 LYS B C 5851 O O . LYS B 171 ? 1.9992 1.9254 2.5355 0.0192 0.2354 0.1339 1818 LYS B O 5852 C CB . LYS B 171 ? 1.8748 1.8699 2.5167 0.0698 0.2697 0.1171 1818 LYS B CB 5853 C CG . LYS B 171 ? 2.0266 1.9895 2.6510 0.0808 0.2931 0.0765 1818 LYS B CG 5854 C CD . LYS B 171 ? 2.0832 2.0259 2.7557 0.1141 0.3071 0.0635 1818 LYS B CD 5855 C CE . LYS B 171 ? 2.0159 1.9146 2.6609 0.1197 0.3240 0.0210 1818 LYS B CE 5856 N NZ . LYS B 171 ? 1.9761 1.8661 2.6636 0.1539 0.3443 -0.0008 1818 LYS B NZ 5857 N N . VAL B 172 ? 1.6345 1.5771 2.1264 0.0078 0.2601 0.0925 1819 VAL B N 5858 C CA . VAL B 172 ? 1.4874 1.3838 1.9349 -0.0038 0.2585 0.0797 1819 VAL B CA 5859 C C . VAL B 172 ? 1.5830 1.4415 2.0555 0.0144 0.2649 0.0669 1819 VAL B C 5860 O O . VAL B 172 ? 1.7954 1.6581 2.2996 0.0353 0.2795 0.0495 1819 VAL B O 5861 C CB . VAL B 172 ? 1.3322 1.2281 1.7360 -0.0148 0.2706 0.0547 1819 VAL B CB 5862 C CG1 . VAL B 172 ? 1.3511 1.2123 1.7082 -0.0323 0.2630 0.0526 1819 VAL B CG1 5863 C CG2 . VAL B 172 ? 1.2506 1.1883 1.6460 -0.0262 0.2717 0.0625 1819 VAL B CG2 5864 N N . GLN B 173 ? 1.5831 1.4043 2.0426 0.0067 0.2550 0.0756 1820 GLN B N 5865 C CA . GLN B 173 ? 1.7628 1.5420 2.2460 0.0190 0.2594 0.0649 1820 GLN B CA 5866 C C . GLN B 173 ? 1.8968 1.6466 2.3395 0.0042 0.2631 0.0411 1820 GLN B C 5867 O O . GLN B 173 ? 1.9650 1.7288 2.3649 -0.0123 0.2619 0.0385 1820 GLN B O 5868 C CB . GLN B 173 ? 1.8827 1.6461 2.3884 0.0205 0.2447 0.0996 1820 GLN B CB 5869 C CG . GLN B 173 ? 1.9677 1.7017 2.5254 0.0425 0.2485 0.1008 1820 GLN B CG 5870 C CD . GLN B 173 ? 2.0745 1.8339 2.6765 0.0679 0.2589 0.0928 1820 GLN B CD 5871 O OE1 . GLN B 173 ? 2.0002 1.8051 2.6164 0.0717 0.2538 0.1122 1820 GLN B OE1 5872 N NE2 . GLN B 173 ? 2.1823 1.9135 2.8074 0.0855 0.2736 0.0632 1820 GLN B NE2 5873 N N . HIS B 174 ? 1.9427 1.6529 2.4003 0.0094 0.2669 0.0241 1821 HIS B N 5874 C CA . HIS B 174 ? 1.8371 1.5222 2.2625 -0.0076 0.2659 0.0081 1821 HIS B CA 5875 C C . HIS B 174 ? 1.7709 1.4471 2.1790 -0.0247 0.2541 0.0389 1821 HIS B C 5876 O O . HIS B 174 ? 1.5830 1.2545 1.9575 -0.0406 0.2530 0.0335 1821 HIS B O 5877 C CB . HIS B 174 ? 2.0044 1.6502 2.4522 -0.0007 0.2710 -0.0202 1821 HIS B CB 5878 C CG . HIS B 174 ? 2.3395 1.9469 2.8226 -0.0003 0.2640 -0.0010 1821 HIS B CG 5879 N ND1 . HIS B 174 ? 2.4177 1.9999 2.8927 -0.0185 0.2577 0.0051 1821 HIS B ND1 5880 C CD2 . HIS B 174 ? 2.5270 2.1175 3.0568 0.0164 0.2632 0.0156 1821 HIS B CD2 5881 C CE1 . HIS B 174 ? 2.3538 1.9047 2.8674 -0.0147 0.2537 0.0254 1821 HIS B CE1 5882 N NE2 . HIS B 174 ? 2.4544 2.0078 3.0010 0.0070 0.2564 0.0323 1821 HIS B NE2 5883 N N . HIS B 175 ? 1.8015 1.4790 2.2330 -0.0193 0.2460 0.0717 1822 HIS B N 5884 C CA . HIS B 175 ? 1.6492 1.3231 2.0642 -0.0317 0.2350 0.1065 1822 HIS B CA 5885 C C . HIS B 175 ? 1.5308 1.2317 1.8952 -0.0467 0.2305 0.1137 1822 HIS B C 5886 O O . HIS B 175 ? 1.4863 1.1818 1.8234 -0.0587 0.2249 0.1330 1822 HIS B O 5887 C CB . HIS B 175 ? 1.7148 1.3817 2.1709 -0.0189 0.2270 0.1397 1822 HIS B CB 5888 C CG . HIS B 175 ? 1.9721 1.6720 2.4184 -0.0193 0.2146 0.1704 1822 HIS B CG 5889 N ND1 . HIS B 175 ? 2.1145 1.8147 2.5332 -0.0309 0.2039 0.2011 1822 HIS B ND1 5890 C CD2 . HIS B 175 ? 2.0531 1.7876 2.5170 -0.0091 0.2102 0.1761 1822 HIS B CD2 5891 C CE1 . HIS B 175 ? 2.0734 1.8055 2.4879 -0.0294 0.1914 0.2216 1822 HIS B CE1 5892 N NE2 . HIS B 175 ? 2.0281 1.7830 2.4729 -0.0172 0.1943 0.2079 1822 HIS B NE2 5893 N N . MET B 176 ? 1.5122 1.2399 1.8638 -0.0459 0.2346 0.0967 1823 MET B N 5894 C CA . MET B 176 ? 1.4609 1.2088 1.7666 -0.0604 0.2318 0.0982 1823 MET B CA 5895 C C . MET B 176 ? 1.4928 1.2421 1.7717 -0.0658 0.2424 0.0689 1823 MET B C 5896 O O . MET B 176 ? 1.4794 1.2435 1.7242 -0.0758 0.2424 0.0672 1823 MET B O 5897 C CB . MET B 176 ? 1.4683 1.2502 1.7815 -0.0589 0.2242 0.1125 1823 MET B CB 5898 C CG . MET B 176 ? 1.5851 1.3872 1.9468 -0.0407 0.2294 0.1069 1823 MET B CG 5899 S SD . MET B 176 ? 1.8062 1.6515 2.1945 -0.0378 0.2156 0.1349 1823 MET B SD 5900 C CE . MET B 176 ? 1.7303 1.5616 2.1570 -0.0243 0.2034 0.1657 1823 MET B CE 5901 N N . ALA B 177 ? 1.5720 1.3036 1.8657 -0.0598 0.2502 0.0466 1824 ALA B N 5902 C CA . ALA B 177 ? 1.4759 1.2095 1.7453 -0.0636 0.2582 0.0192 1824 ALA B CA 5903 C C . ALA B 177 ? 1.4700 1.1828 1.7215 -0.0747 0.2565 0.0160 1824 ALA B C 5904 O O . ALA B 177 ? 1.6149 1.3096 1.8769 -0.0790 0.2514 0.0340 1824 ALA B O 5905 C CB . ALA B 177 ? 1.5380 1.2700 1.8330 -0.0490 0.2672 -0.0081 1824 ALA B CB 5906 N N . PRO B 178 ? 1.3254 1.0442 1.5512 -0.0793 0.2609 -0.0043 1825 PRO B N 5907 C CA . PRO B 178 ? 1.3372 1.0434 1.5538 -0.0873 0.2599 -0.0156 1825 PRO B CA 5908 C C . PRO B 178 ? 1.3515 1.0365 1.6010 -0.0840 0.2589 -0.0354 1825 PRO B C 5909 O O . PRO B 178 ? 1.4262 1.1119 1.6877 -0.0733 0.2632 -0.0576 1825 PRO B O 5910 C CB . PRO B 178 ? 1.2486 0.9746 1.4314 -0.0888 0.2643 -0.0326 1825 PRO B CB 5911 C CG . PRO B 178 ? 1.2404 0.9850 1.4242 -0.0798 0.2701 -0.0362 1825 PRO B CG 5912 C CD . PRO B 178 ? 1.2072 0.9512 1.4059 -0.0795 0.2658 -0.0102 1825 PRO B CD 5913 N N . THR B 179 ? 1.3273 0.9937 1.5912 -0.0933 0.2542 -0.0281 1826 THR B N 5914 C CA . THR B 179 ? 1.5001 1.1432 1.7943 -0.0956 0.2510 -0.0486 1826 THR B CA 5915 C C . THR B 179 ? 1.5732 1.2283 1.8455 -0.0979 0.2502 -0.0813 1826 THR B C 5916 O O . THR B 179 ? 1.6373 1.3152 1.8754 -0.1027 0.2507 -0.0783 1826 THR B O 5917 C CB . THR B 179 ? 1.6107 1.2381 1.9240 -0.1099 0.2460 -0.0309 1826 THR B CB 5918 O OG1 . THR B 179 ? 1.6852 1.3240 1.9800 -0.1140 0.2479 0.0019 1826 THR B OG1 5919 C CG2 . THR B 179 ? 1.5973 1.1892 1.9605 -0.1097 0.2431 -0.0279 1826 THR B CG2 5920 N N . LYS B 180 ? 1.5805 1.2186 1.8709 -0.0942 0.2486 -0.1120 1827 LYS B N 5921 C CA . LYS B 180 ? 1.6339 1.2792 1.9057 -0.0991 0.2439 -0.1454 1827 LYS B CA 5922 C C . LYS B 180 ? 1.7320 1.3960 1.9854 -0.1143 0.2368 -0.1356 1827 LYS B C 5923 O O . LYS B 180 ? 1.9232 1.6053 2.1513 -0.1173 0.2324 -0.1555 1827 LYS B O 5924 C CB . LYS B 180 ? 1.6828 1.2945 1.9860 -0.1013 0.2376 -0.1743 1827 LYS B CB 5925 C CG . LYS B 180 ? 1.8543 1.4470 2.1884 -0.1207 0.2263 -0.1660 1827 LYS B CG 5926 C CD . LYS B 180 ? 2.0877 1.6425 2.4540 -0.1254 0.2185 -0.1975 1827 LYS B CD 5927 C CE . LYS B 180 ? 2.1189 1.6487 2.5303 -0.1446 0.2097 -0.1802 1827 LYS B CE 5928 N NZ . LYS B 180 ? 2.0673 1.5614 2.5056 -0.1549 0.1983 -0.2164 1827 LYS B NZ 5929 N N . ASP B 181 ? 1.6830 1.3444 1.9490 -0.1222 0.2364 -0.1037 1828 ASP B N 5930 C CA . ASP B 181 ? 1.6674 1.3437 1.9282 -0.1351 0.2315 -0.0922 1828 ASP B CA 5931 C C . ASP B 181 ? 1.6733 1.3735 1.8969 -0.1311 0.2382 -0.0711 1828 ASP B C 5932 O O . ASP B 181 ? 1.8482 1.5665 2.0588 -0.1369 0.2364 -0.0638 1828 ASP B O 5933 C CB . ASP B 181 ? 1.8075 1.4647 2.1088 -0.1461 0.2291 -0.0713 1828 ASP B CB 5934 C CG . ASP B 181 ? 2.1994 1.8257 2.5412 -0.1518 0.2216 -0.0929 1828 ASP B CG 5935 O OD1 . ASP B 181 ? 2.2211 1.8494 2.5604 -0.1569 0.2127 -0.1253 1828 ASP B OD1 5936 O OD2 . ASP B 181 ? 2.4937 2.0921 2.8685 -0.1511 0.2238 -0.0778 1828 ASP B OD2 5937 N N . GLU B 182 ? 1.6265 1.3272 1.8344 -0.1209 0.2455 -0.0619 1829 GLU B N 5938 C CA . GLU B 182 ? 1.7685 1.4844 1.9431 -0.1194 0.2509 -0.0415 1829 GLU B CA 5939 C C . GLU B 182 ? 1.8066 1.5441 1.9463 -0.1164 0.2520 -0.0550 1829 GLU B C 5940 O O . GLU B 182 ? 1.7071 1.4550 1.8441 -0.1199 0.2463 -0.0707 1829 GLU B O 5941 C CB . GLU B 182 ? 1.8625 1.5723 2.0344 -0.1135 0.2554 -0.0230 1829 GLU B CB 5942 C CG . GLU B 182 ? 1.9970 1.6862 2.2034 -0.1143 0.2536 -0.0074 1829 GLU B CG 5943 C CD . GLU B 182 ? 2.0296 1.7171 2.2243 -0.1148 0.2552 0.0234 1829 GLU B CD 5944 O OE1 . GLU B 182 ? 1.9961 1.6910 2.1626 -0.1192 0.2580 0.0354 1829 GLU B OE1 5945 O OE2 . GLU B 182 ? 1.8247 1.5030 2.0384 -0.1101 0.2534 0.0357 1829 GLU B OE2 5946 N N . PHE B 183 ? 1.8297 1.5748 1.9436 -0.1111 0.2581 -0.0460 1830 PHE B N 5947 C CA . PHE B 183 ? 1.7309 1.4947 1.8121 -0.1077 0.2612 -0.0535 1830 PHE B CA 5948 C C . PHE B 183 ? 1.7577 1.5268 1.8383 -0.1004 0.2669 -0.0619 1830 PHE B C 5949 O O . PHE B 183 ? 2.1134 1.8729 2.2155 -0.0980 0.2680 -0.0550 1830 PHE B O 5950 C CB . PHE B 183 ? 1.6536 1.4201 1.7070 -0.1097 0.2644 -0.0324 1830 PHE B CB 5951 C CG . PHE B 183 ? 1.9219 1.6944 1.9713 -0.1126 0.2612 -0.0291 1830 PHE B CG 5952 C CD1 . PHE B 183 ? 1.9668 1.7463 2.0367 -0.1160 0.2534 -0.0448 1830 PHE B CD1 5953 C CD2 . PHE B 183 ? 1.9079 1.6799 1.9350 -0.1118 0.2654 -0.0114 1830 PHE B CD2 5954 C CE1 . PHE B 183 ? 1.8039 1.5957 1.8764 -0.1191 0.2491 -0.0401 1830 PHE B CE1 5955 C CE2 . PHE B 183 ? 1.8190 1.6012 1.8476 -0.1118 0.2636 -0.0070 1830 PHE B CE2 5956 C CZ . PHE B 183 ? 1.7781 1.5734 1.8311 -0.1157 0.2550 -0.0201 1830 PHE B CZ 5957 N N . ASP B 184 ? 1.7289 1.5162 1.7869 -0.0962 0.2708 -0.0751 1831 ASP B N 5958 C CA . ASP B 184 ? 1.7354 1.5344 1.7942 -0.0878 0.2794 -0.0846 1831 ASP B CA 5959 C C . ASP B 184 ? 1.6832 1.4811 1.7556 -0.0873 0.2833 -0.0652 1831 ASP B C 5960 O O . ASP B 184 ? 1.6006 1.4048 1.6933 -0.0793 0.2887 -0.0710 1831 ASP B O 5961 C CB . ASP B 184 ? 1.8292 1.6516 1.8533 -0.0854 0.2854 -0.0894 1831 ASP B CB 5962 C CG . ASP B 184 ? 2.0328 1.8626 2.0419 -0.0843 0.2800 -0.1114 1831 ASP B CG 5963 O OD1 . ASP B 184 ? 2.0594 1.8850 2.0817 -0.0794 0.2790 -0.1368 1831 ASP B OD1 5964 O OD2 . ASP B 184 ? 2.2240 2.0633 2.2079 -0.0880 0.2761 -0.1036 1831 ASP B OD2 5965 N N . CYS B 185 ? 1.6490 1.4399 1.7098 -0.0952 0.2801 -0.0428 1832 CYS B N 5966 C CA . CYS B 185 ? 1.5870 1.3748 1.6586 -0.0977 0.2789 -0.0241 1832 CYS B CA 5967 C C . CYS B 185 ? 1.6456 1.4128 1.7188 -0.1039 0.2716 -0.0079 1832 CYS B C 5968 O O . CYS B 185 ? 1.7565 1.5141 1.8223 -0.1066 0.2697 -0.0088 1832 CYS B O 5969 C CB . CYS B 185 ? 1.8188 1.6195 1.8671 -0.1029 0.2828 -0.0126 1832 CYS B CB 5970 S SG . CYS B 185 ? 2.2150 2.0458 2.2581 -0.0970 0.2948 -0.0240 1832 CYS B SG 5971 N N . LYS B 186 ? 1.6891 1.4531 1.7726 -0.1057 0.2678 0.0079 1833 LYS B N 5972 C CA . LYS B 186 ? 1.6032 1.3510 1.6804 -0.1112 0.2620 0.0260 1833 LYS B CA 5973 C C . LYS B 186 ? 1.5192 1.2709 1.5766 -0.1180 0.2583 0.0401 1833 LYS B C 5974 O O . LYS B 186 ? 1.3761 1.1446 1.4465 -0.1175 0.2576 0.0405 1833 LYS B O 5975 C CB . LYS B 186 ? 1.5352 1.2745 1.6480 -0.1066 0.2578 0.0316 1833 LYS B CB 5976 C CG . LYS B 186 ? 1.4928 1.2145 1.6060 -0.1102 0.2558 0.0436 1833 LYS B CG 5977 C CD . LYS B 186 ? 1.6134 1.3264 1.7622 -0.1059 0.2513 0.0550 1833 LYS B CD 5978 C CE . LYS B 186 ? 1.6858 1.3821 1.8444 -0.1095 0.2513 0.0677 1833 LYS B CE 5979 N NZ . LYS B 186 ? 1.8000 1.4938 1.9244 -0.1158 0.2525 0.0860 1833 LYS B NZ 5980 N N . ALA B 187 ? 1.4940 1.2314 1.5211 -0.1246 0.2561 0.0507 1834 ALA B N 5981 C CA . ALA B 187 ? 1.4927 1.2294 1.5008 -0.1330 0.2496 0.0617 1834 ALA B CA 5982 C C . ALA B 187 ? 1.5282 1.2588 1.5400 -0.1348 0.2401 0.0774 1834 ALA B C 5983 O O . ALA B 187 ? 1.5734 1.2921 1.5855 -0.1314 0.2414 0.0836 1834 ALA B O 5984 C CB . ALA B 187 ? 1.7167 1.4383 1.6838 -0.1391 0.2527 0.0613 1834 ALA B CB 5985 N N . TRP B 188 ? 1.4586 1.2006 1.4746 -0.1407 0.2302 0.0857 1835 TRP B N 5986 C CA . TRP B 188 ? 1.5392 1.2809 1.5571 -0.1427 0.2179 0.1027 1835 TRP B CA 5987 C C . TRP B 188 ? 1.5979 1.3390 1.5858 -0.1563 0.2072 0.1067 1835 TRP B C 5988 O O . TRP B 188 ? 1.6405 1.3904 1.6289 -0.1629 0.2085 0.0993 1835 TRP B O 5989 C CB . TRP B 188 ? 1.5843 1.3482 1.6504 -0.1353 0.2126 0.1089 1835 TRP B CB 5990 C CG . TRP B 188 ? 1.7551 1.5143 1.8546 -0.1224 0.2201 0.1054 1835 TRP B CG 5991 C CD1 . TRP B 188 ? 1.9453 1.7114 2.0727 -0.1134 0.2301 0.0885 1835 TRP B CD1 5992 C CD2 . TRP B 188 ? 1.6876 1.4326 1.7963 -0.1177 0.2180 0.1189 1835 TRP B CD2 5993 N NE1 . TRP B 188 ? 1.7828 1.5360 1.9370 -0.1044 0.2329 0.0881 1835 TRP B NE1 5994 C CE2 . TRP B 188 ? 1.6705 1.4110 1.8166 -0.1073 0.2259 0.1086 1835 TRP B CE2 5995 C CE3 . TRP B 188 ? 1.7798 1.5150 1.8672 -0.1215 0.2106 0.1391 1835 TRP B CE3 5996 C CZ2 . TRP B 188 ? 1.7209 1.4455 1.8886 -0.1024 0.2261 0.1193 1835 TRP B CZ2 5997 C CZ3 . TRP B 188 ? 1.9658 1.6893 2.0731 -0.1153 0.2124 0.1522 1835 TRP B CZ3 5998 C CH2 . TRP B 188 ? 1.8741 1.5912 2.0236 -0.1066 0.2199 0.1430 1835 TRP B CH2 5999 N N . ALA B 189 ? 1.7021 1.4332 1.6642 -0.1612 0.1964 0.1188 1836 ALA B N 6000 C CA . ALA B 189 ? 1.7599 1.4851 1.6864 -0.1762 0.1833 0.1201 1836 ALA B CA 6001 C C . ALA B 189 ? 1.8445 1.5979 1.7968 -0.1835 0.1641 0.1319 1836 ALA B C 6002 O O . ALA B 189 ? 2.0794 1.8510 2.0662 -0.1743 0.1590 0.1452 1836 ALA B O 6003 C CB . ALA B 189 ? 1.8823 1.5822 1.7597 -0.1772 0.1820 0.1245 1836 ALA B CB 6004 N N . TYR B 190 ? 1.7735 1.5305 1.7126 -0.2001 0.1530 0.1281 1837 TYR B N 6005 C CA . TYR B 190 ? 1.8107 1.5962 1.7693 -0.2111 0.1304 0.1406 1837 TYR B CA 6006 C C . TYR B 190 ? 1.8131 1.5801 1.7233 -0.2321 0.1142 0.1356 1837 TYR B C 6007 O O . TYR B 190 ? 1.7991 1.5377 1.6778 -0.2399 0.1228 0.1207 1837 TYR B O 6008 C CB . TYR B 190 ? 1.8620 1.6862 1.8786 -0.2112 0.1317 0.1428 1837 TYR B CB 6009 C CG . TYR B 190 ? 2.0003 1.8240 2.0132 -0.2263 0.1367 0.1319 1837 TYR B CG 6010 C CD1 . TYR B 190 ? 1.9466 1.7766 1.9511 -0.2497 0.1179 0.1344 1837 TYR B CD1 6011 C CD2 . TYR B 190 ? 1.9579 1.7755 1.9769 -0.2182 0.1593 0.1205 1837 TYR B CD2 6012 C CE1 . TYR B 190 ? 1.7756 1.6028 1.7804 -0.2649 0.1232 0.1275 1837 TYR B CE1 6013 C CE2 . TYR B 190 ? 1.7917 1.6091 1.8076 -0.2313 0.1648 0.1149 1837 TYR B CE2 6014 C CZ . TYR B 190 ? 1.7671 1.5881 1.7776 -0.2547 0.1477 0.1193 1837 TYR B CZ 6015 O OH . TYR B 190 ? 1.7375 1.5559 1.7482 -0.2688 0.1543 0.1163 1837 TYR B OH 6016 N N . PHE B 191 ? 1.8316 1.6134 1.7354 -0.2408 0.0901 0.1478 1838 PHE B N 6017 C CA . PHE B 191 ? 1.9972 1.7584 1.8469 -0.2611 0.0707 0.1412 1838 PHE B CA 6018 C C . PHE B 191 ? 1.9830 1.7762 1.8420 -0.2692 0.0411 0.1585 1838 PHE B C 6019 O O . PHE B 191 ? 2.1392 1.9611 2.0360 -0.2541 0.0393 0.1775 1838 PHE B O 6020 C CB . PHE B 191 ? 2.1276 1.8451 1.9120 -0.2542 0.0811 0.1323 1838 PHE B CB 6021 C CG . PHE B 191 ? 2.0062 1.7305 1.7894 -0.2363 0.0846 0.1489 1838 PHE B CG 6022 C CD1 . PHE B 191 ? 1.8333 1.5599 1.6491 -0.2167 0.1069 0.1534 1838 PHE B CD1 6023 C CD2 . PHE B 191 ? 2.0489 1.7768 1.7973 -0.2403 0.0650 0.1606 1838 PHE B CD2 6024 C CE1 . PHE B 191 ? 1.7746 1.5048 1.5935 -0.2025 0.1105 0.1705 1838 PHE B CE1 6025 C CE2 . PHE B 191 ? 2.0788 1.8127 1.8270 -0.2242 0.0696 0.1799 1838 PHE B CE2 6026 C CZ . PHE B 191 ? 1.9775 1.7116 1.7636 -0.2058 0.0928 0.1855 1838 PHE B CZ 6027 N N . SER B 192 ? 1.8440 1.6307 1.6680 -0.2924 0.0169 0.1523 1839 SER B N 6028 C CA . SER B 192 ? 1.8362 1.6595 1.6705 -0.3017 -0.0154 0.1699 1839 SER B CA 6029 C C . SER B 192 ? 1.8509 1.6620 1.6359 -0.2915 -0.0219 0.1794 1839 SER B C 6030 O O . SER B 192 ? 1.6887 1.4558 1.4065 -0.2910 -0.0124 0.1644 1839 SER B O 6031 C CB . SER B 192 ? 1.9856 1.8122 1.8042 -0.3332 -0.0439 0.1607 1839 SER B CB 6032 O OG . SER B 192 ? 1.8872 1.7530 1.7138 -0.3403 -0.0771 0.1794 1839 SER B OG 6033 N N . ASP B 193 ? 1.9889 1.8413 1.8102 -0.2823 -0.0371 0.2061 1840 ASP B N 6034 C CA . ASP B 193 ? 2.2360 2.0869 2.0222 -0.2700 -0.0438 0.2246 1840 ASP B CA 6035 C C . ASP B 193 ? 2.2125 2.0877 1.9704 -0.2864 -0.0833 0.2362 1840 ASP B C 6036 O O . ASP B 193 ? 2.1849 2.0767 1.9310 -0.2763 -0.0956 0.2607 1840 ASP B O 6037 C CB . ASP B 193 ? 2.3831 2.2507 2.2229 -0.2425 -0.0267 0.2484 1840 ASP B CB 6038 C CG . ASP B 193 ? 2.4716 2.3933 2.3862 -0.2368 -0.0450 0.2741 1840 ASP B CG 6039 O OD1 . ASP B 193 ? 2.5102 2.4638 2.4496 -0.2538 -0.0675 0.2732 1840 ASP B OD1 6040 O OD2 . ASP B 193 ? 2.4791 2.4106 2.4311 -0.2145 -0.0359 0.2959 1840 ASP B OD2 6041 N N . VAL B 194 ? 2.1878 2.0636 1.9329 -0.3132 -0.1038 0.2185 1841 VAL B N 6042 C CA . VAL B 194 ? 2.2260 2.1186 1.9335 -0.3339 -0.1435 0.2220 1841 VAL B CA 6043 C C . VAL B 194 ? 2.1941 2.0421 1.8020 -0.3335 -0.1423 0.2093 1841 VAL B C 6044 O O . VAL B 194 ? 2.3643 2.2289 1.9381 -0.3311 -0.1630 0.2271 1841 VAL B O 6045 C CB . VAL B 194 ? 2.3699 2.2744 2.0973 -0.3652 -0.1658 0.2059 1841 VAL B CB 6046 C CG1 . VAL B 194 ? 2.5500 2.4402 2.2041 -0.3923 -0.2012 0.1911 1841 VAL B CG1 6047 C CG2 . VAL B 194 ? 2.4444 2.4165 2.2673 -0.3649 -0.1803 0.2316 1841 VAL B CG2 6048 N N . ASP B 195 ? 2.2159 2.0094 1.7772 -0.3341 -0.1172 0.1803 1842 ASP B N 6049 C CA . ASP B 195 ? 2.5047 2.2574 1.9836 -0.3225 -0.1017 0.1720 1842 ASP B CA 6050 C C . ASP B 195 ? 2.6712 2.3938 2.1662 -0.3027 -0.0585 0.1638 1842 ASP B C 6051 O O . ASP B 195 ? 2.8290 2.5173 2.3161 -0.3098 -0.0442 0.1376 1842 ASP B O 6052 C CB . ASP B 195 ? 2.6822 2.3944 2.0742 -0.3439 -0.1176 0.1404 1842 ASP B CB 6053 C CG . ASP B 195 ? 2.8470 2.5264 2.1490 -0.3297 -0.1040 0.1356 1842 ASP B CG 6054 O OD1 . ASP B 195 ? 2.8988 2.5526 2.1941 -0.3080 -0.0661 0.1338 1842 ASP B OD1 6055 O OD2 . ASP B 195 ? 2.8167 2.4983 2.0538 -0.3403 -0.1311 0.1337 1842 ASP B OD2 6056 N N . LEU B 196 ? 2.8927 2.6285 2.4131 -0.2785 -0.0392 0.1877 1843 LEU B N 6057 C CA . LEU B 196 ? 2.7987 2.5156 2.3483 -0.2598 -0.0010 0.1837 1843 LEU B CA 6058 C C . LEU B 196 ? 2.6199 2.2848 2.1075 -0.2601 0.0207 0.1542 1843 LEU B C 6059 O O . LEU B 196 ? 2.2376 1.8849 1.7502 -0.2530 0.0457 0.1420 1843 LEU B O 6060 C CB . LEU B 196 ? 2.8286 2.5615 2.4030 -0.2366 0.0139 0.2135 1843 LEU B CB 6061 C CG . LEU B 196 ? 2.7990 2.5790 2.4351 -0.2313 -0.0055 0.2462 1843 LEU B CG 6062 C CD1 . LEU B 196 ? 2.6790 2.4768 2.2714 -0.2336 -0.0315 0.2691 1843 LEU B CD1 6063 C CD2 . LEU B 196 ? 2.4450 2.2324 2.1450 -0.2098 0.0181 0.2635 1843 LEU B CD2 6064 N N . GLU B 197 ? 2.6614 2.3037 2.0686 -0.2681 0.0091 0.1426 1844 GLU B N 6065 C CA . GLU B 197 ? 2.5915 2.1819 1.9289 -0.2667 0.0276 0.1136 1844 GLU B CA 6066 C C . GLU B 197 ? 2.5435 2.1032 1.8613 -0.2895 0.0138 0.0822 1844 GLU B C 6067 O O . GLU B 197 ? 2.6272 2.1544 1.9500 -0.2864 0.0356 0.0635 1844 GLU B O 6068 C CB . GLU B 197 ? 2.6278 2.2064 1.8821 -0.2601 0.0268 0.1161 1844 GLU B CB 6069 C CG . GLU B 197 ? 2.7851 2.3231 1.9908 -0.2421 0.0635 0.1006 1844 GLU B CG 6070 C CD . GLU B 197 ? 3.0257 2.5245 2.1318 -0.2474 0.0590 0.0741 1844 GLU B CD 6071 O OE1 . GLU B 197 ? 3.1050 2.6176 2.1604 -0.2527 0.0375 0.0824 1844 GLU B OE1 6072 O OE2 . GLU B 197 ? 2.9499 2.4030 2.0270 -0.2448 0.0775 0.0446 1844 GLU B OE2 6073 N N . LYS B 198 ? 2.4210 1.9908 1.7176 -0.3130 -0.0230 0.0775 1845 LYS B N 6074 C CA . LYS B 198 ? 2.4093 1.9483 1.6876 -0.3393 -0.0402 0.0480 1845 LYS B CA 6075 C C . LYS B 198 ? 2.4211 1.9720 1.7787 -0.3500 -0.0377 0.0483 1845 LYS B C 6076 O O . LYS B 198 ? 2.3702 1.8797 1.7189 -0.3590 -0.0281 0.0250 1845 LYS B O 6077 C CB . LYS B 198 ? 2.3710 1.9217 1.6083 -0.3643 -0.0836 0.0435 1845 LYS B CB 6078 C CG . LYS B 198 ? 2.4481 1.9452 1.5803 -0.3700 -0.0877 0.0121 1845 LYS B CG 6079 C CD . LYS B 198 ? 2.5053 2.0136 1.6012 -0.4005 -0.1358 0.0031 1845 LYS B CD 6080 C CE . LYS B 198 ? 2.5408 1.9897 1.5282 -0.4084 -0.1415 -0.0345 1845 LYS B CE 6081 N NZ . LYS B 198 ? 2.6379 2.1026 1.5945 -0.4409 -0.1928 -0.0432 1845 LYS B NZ 6082 N N . ASP B 199 ? 2.3491 1.9557 1.7831 -0.3471 -0.0445 0.0755 1846 ASP B N 6083 C CA . ASP B 199 ? 2.2037 1.8314 1.7159 -0.3537 -0.0394 0.0798 1846 ASP B CA 6084 C C . ASP B 199 ? 2.0835 1.6916 1.6185 -0.3324 0.0000 0.0765 1846 ASP B C 6085 O O . ASP B 199 ? 2.0365 1.6735 1.6391 -0.3261 0.0111 0.0883 1846 ASP B O 6086 C CB . ASP B 199 ? 2.1196 1.8137 1.7038 -0.3540 -0.0576 0.1089 1846 ASP B CB 6087 C CG . ASP B 199 ? 2.1483 1.8695 1.7178 -0.3765 -0.1001 0.1145 1846 ASP B CG 6088 O OD1 . ASP B 199 ? 2.1472 1.8356 1.6576 -0.3987 -0.1189 0.0919 1846 ASP B OD1 6089 O OD2 . ASP B 199 ? 2.1349 1.9103 1.7532 -0.3714 -0.1156 0.1417 1846 ASP B OD2 6090 N N . VAL B 200 ? 2.0369 1.5978 1.5134 -0.3202 0.0208 0.0605 1847 VAL B N 6091 C CA . VAL B 200 ? 2.0937 1.6295 1.5817 -0.3044 0.0540 0.0529 1847 VAL B CA 6092 C C . VAL B 200 ? 2.2838 1.7611 1.7169 -0.3148 0.0573 0.0248 1847 VAL B C 6093 O O . VAL B 200 ? 2.4071 1.8673 1.8633 -0.3221 0.0650 0.0164 1847 VAL B O 6094 C CB . VAL B 200 ? 2.0045 1.5449 1.4893 -0.2755 0.0800 0.0649 1847 VAL B CB 6095 C CG1 . VAL B 200 ? 2.0309 1.5231 1.4652 -0.2611 0.1071 0.0473 1847 VAL B CG1 6096 C CG2 . VAL B 200 ? 1.8883 1.4650 1.4493 -0.2640 0.0928 0.0815 1847 VAL B CG2 6097 N N . HIS B 201 ? 2.3753 1.8210 1.7345 -0.3154 0.0511 0.0105 1848 HIS B N 6098 C CA . HIS B 201 ? 2.3892 1.7724 1.6910 -0.3223 0.0557 -0.0191 1848 HIS B CA 6099 C C . HIS B 201 ? 2.4263 1.8022 1.7497 -0.3544 0.0307 -0.0287 1848 HIS B C 6100 O O . HIS B 201 ? 2.5174 1.8523 1.8413 -0.3603 0.0411 -0.0435 1848 HIS B O 6101 C CB . HIS B 201 ? 2.4671 1.8216 1.6826 -0.3179 0.0515 -0.0340 1848 HIS B CB 6102 C CG . HIS B 201 ? 2.5649 1.9144 1.7560 -0.2855 0.0847 -0.0280 1848 HIS B CG 6103 N ND1 . HIS B 201 ? 2.6660 2.0623 1.8825 -0.2698 0.0911 0.0000 1848 HIS B ND1 6104 C CD2 . HIS B 201 ? 2.5727 1.8779 1.7230 -0.2659 0.1145 -0.0443 1848 HIS B CD2 6105 C CE1 . HIS B 201 ? 2.6820 2.0649 1.8745 -0.2443 0.1226 0.0010 1848 HIS B CE1 6106 N NE2 . HIS B 201 ? 2.7996 2.1298 1.9524 -0.2405 0.1377 -0.0255 1848 HIS B NE2 6107 N N . SER B 202 ? 2.3981 1.8178 1.7469 -0.3746 -0.0016 -0.0166 1849 SER B N 6108 C CA . SER B 202 ? 2.4735 1.9021 1.8606 -0.4067 -0.0261 -0.0190 1849 SER B CA 6109 C C . SER B 202 ? 2.4502 1.8815 1.8994 -0.4030 -0.0030 -0.0115 1849 SER B C 6110 O O . SER B 202 ? 2.4138 1.8064 1.8601 -0.4203 -0.0032 -0.0258 1849 SER B O 6111 C CB . SER B 202 ? 2.4714 1.9649 1.8978 -0.4221 -0.0596 0.0018 1849 SER B CB 6112 O OG . SER B 202 ? 2.3476 1.8392 1.7124 -0.4284 -0.0850 -0.0045 1849 SER B OG 6113 N N . GLY B 203 ? 2.3726 1.8463 1.8738 -0.3804 0.0168 0.0104 1850 GLY B N 6114 C CA . GLY B 203 ? 2.3653 1.8400 1.9129 -0.3704 0.0434 0.0163 1850 GLY B CA 6115 C C . GLY B 203 ? 2.2370 1.7724 1.8598 -0.3592 0.0523 0.0402 1850 GLY B C 6116 O O . GLY B 203 ? 2.2344 1.7771 1.8976 -0.3580 0.0680 0.0450 1850 GLY B O 6117 N N . LEU B 204 ? 2.1051 1.6830 1.7459 -0.3493 0.0437 0.0556 1851 LEU B N 6118 C CA . LEU B 204 ? 2.1189 1.7522 1.8323 -0.3411 0.0487 0.0756 1851 LEU B CA 6119 C C . LEU B 204 ? 2.1189 1.7599 1.8444 -0.3101 0.0745 0.0830 1851 LEU B C 6120 O O . LEU B 204 ? 2.2614 1.9189 1.9835 -0.2978 0.0702 0.0936 1851 LEU B O 6121 C CB . LEU B 204 ? 2.1451 1.8278 1.8890 -0.3538 0.0184 0.0912 1851 LEU B CB 6122 C CG . LEU B 204 ? 2.0990 1.7941 1.8554 -0.3878 -0.0112 0.0892 1851 LEU B CG 6123 C CD1 . LEU B 204 ? 2.1766 1.8249 1.8595 -0.4064 -0.0315 0.0693 1851 LEU B CD1 6124 C CD2 . LEU B 204 ? 1.9743 1.7356 1.7862 -0.3930 -0.0349 0.1114 1851 LEU B CD2 6125 N N . ILE B 205 ? 1.9580 1.5860 1.6960 -0.2986 0.1001 0.0782 1852 ILE B N 6126 C CA . ILE B 205 ? 1.9246 1.5725 1.6936 -0.2735 0.1211 0.0863 1852 ILE B CA 6127 C C . ILE B 205 ? 1.9619 1.6207 1.7680 -0.2712 0.1373 0.0855 1852 ILE B C 6128 O O . ILE B 205 ? 1.9292 1.5627 1.7202 -0.2823 0.1416 0.0771 1852 ILE B O 6129 C CB . ILE B 205 ? 1.9241 1.5403 1.6559 -0.2534 0.1415 0.0797 1852 ILE B CB 6130 C CG1 . ILE B 205 ? 2.1178 1.6876 1.7824 -0.2592 0.1383 0.0662 1852 ILE B CG1 6131 C CG2 . ILE B 205 ? 1.7806 1.4210 1.5353 -0.2345 0.1477 0.0926 1852 ILE B CG2 6132 C CD1 . ILE B 205 ? 2.2912 1.8238 1.9382 -0.2643 0.1495 0.0521 1852 ILE B CD1 6133 N N . GLY B 206 ? 1.9715 1.6653 1.8234 -0.2557 0.1471 0.0941 1853 GLY B N 6134 C CA . GLY B 206 ? 1.8842 1.5917 1.7673 -0.2472 0.1662 0.0926 1853 GLY B CA 6135 C C . GLY B 206 ? 1.6789 1.3992 1.5826 -0.2240 0.1804 0.0937 1853 GLY B C 6136 O O . GLY B 206 ? 1.6586 1.3818 1.5622 -0.2159 0.1746 0.0996 1853 GLY B O 6137 N N . PRO B 207 ? 1.6033 1.3298 1.5228 -0.2141 0.1984 0.0885 1854 PRO B N 6138 C CA . PRO B 207 ? 1.5861 1.3253 1.5288 -0.1947 0.2106 0.0862 1854 PRO B CA 6139 C C . PRO B 207 ? 1.5801 1.3595 1.5740 -0.1890 0.2132 0.0891 1854 PRO B C 6140 O O . PRO B 207 ? 1.6511 1.4514 1.6624 -0.1982 0.2130 0.0919 1854 PRO B O 6141 C CB . PRO B 207 ? 1.5545 1.2745 1.4755 -0.1884 0.2267 0.0767 1854 PRO B CB 6142 C CG . PRO B 207 ? 1.5799 1.2896 1.4846 -0.2032 0.2260 0.0769 1854 PRO B CG 6143 C CD . PRO B 207 ? 1.6681 1.3822 1.5752 -0.2212 0.2079 0.0835 1854 PRO B CD 6144 N N . LEU B 208 ? 1.5364 1.3253 1.5553 -0.1734 0.2169 0.0886 1855 LEU B N 6145 C CA . LEU B 208 ? 1.4903 1.3130 1.5584 -0.1639 0.2194 0.0904 1855 LEU B CA 6146 C C . LEU B 208 ? 1.4320 1.2500 1.5122 -0.1467 0.2324 0.0788 1855 LEU B C 6147 O O . LEU B 208 ? 1.5410 1.3473 1.6285 -0.1387 0.2295 0.0813 1855 LEU B O 6148 C CB . LEU B 208 ? 1.5336 1.3706 1.6252 -0.1643 0.2030 0.1055 1855 LEU B CB 6149 C CG . LEU B 208 ? 1.4979 1.3628 1.6430 -0.1485 0.2047 0.1099 1855 LEU B CG 6150 C CD1 . LEU B 208 ? 1.4175 1.3229 1.5994 -0.1542 0.1967 0.1212 1855 LEU B CD1 6151 C CD2 . LEU B 208 ? 1.5843 1.4337 1.7291 -0.1422 0.1945 0.1213 1855 LEU B CD2 6152 N N . LEU B 209 ? 1.3787 1.2059 1.4605 -0.1421 0.2463 0.0665 1856 LEU B N 6153 C CA . LEU B 209 ? 1.3925 1.2110 1.4736 -0.1296 0.2570 0.0514 1856 LEU B CA 6154 C C . LEU B 209 ? 1.4399 1.2760 1.5616 -0.1144 0.2630 0.0427 1856 LEU B C 6155 O O . LEU B 209 ? 1.6665 1.5305 1.8095 -0.1107 0.2697 0.0411 1856 LEU B O 6156 C CB . LEU B 209 ? 1.3714 1.1902 1.4263 -0.1320 0.2674 0.0425 1856 LEU B CB 6157 C CG . LEU B 209 ? 1.4969 1.2886 1.5103 -0.1402 0.2656 0.0455 1856 LEU B CG 6158 C CD1 . LEU B 209 ? 1.5851 1.3572 1.5839 -0.1495 0.2536 0.0575 1856 LEU B CD1 6159 C CD2 . LEU B 209 ? 1.6016 1.3985 1.5953 -0.1469 0.2727 0.0467 1856 LEU B CD2 6160 N N . VAL B 210 ? 1.3452 1.1646 1.4792 -0.1055 0.2619 0.0372 1857 VAL B N 6161 C CA . VAL B 210 ? 1.3068 1.1341 1.4763 -0.0899 0.2689 0.0241 1857 VAL B CA 6162 C C . VAL B 210 ? 1.3154 1.1348 1.4702 -0.0850 0.2782 0.0009 1857 VAL B C 6163 O O . VAL B 210 ? 1.4400 1.2393 1.5745 -0.0902 0.2750 -0.0019 1857 VAL B O 6164 C CB . VAL B 210 ? 1.2905 1.1026 1.4895 -0.0832 0.2611 0.0332 1857 VAL B CB 6165 C CG1 . VAL B 210 ? 1.2559 1.0672 1.4907 -0.0660 0.2694 0.0159 1857 VAL B CG1 6166 C CG2 . VAL B 210 ? 1.2874 1.1142 1.5004 -0.0871 0.2498 0.0571 1857 VAL B CG2 6167 N N . CYS B 211 ? 1.3050 1.1429 1.4695 -0.0749 0.2895 -0.0157 1858 CYS B N 6168 C CA . CYS B 211 ? 1.3890 1.2225 1.5335 -0.0712 0.2962 -0.0389 1858 CYS B CA 6169 C C . CYS B 211 ? 1.4598 1.2893 1.6299 -0.0556 0.3024 -0.0628 1858 CYS B C 6170 O O . CYS B 211 ? 1.4204 1.2553 1.6259 -0.0445 0.3055 -0.0607 1858 CYS B O 6171 C CB . CYS B 211 ? 1.5621 1.4190 1.6778 -0.0748 0.3051 -0.0397 1858 CYS B CB 6172 S SG . CYS B 211 ? 1.9322 1.7849 2.0167 -0.0929 0.2984 -0.0151 1858 CYS B SG 6173 N N . HIS B 212 ? 1.5270 1.3457 1.6795 -0.0546 0.3030 -0.0857 1859 HIS B N 6174 C CA . HIS B 212 ? 1.6436 1.4522 1.8124 -0.0416 0.3078 -0.1149 1859 HIS B CA 6175 C C . HIS B 212 ? 1.6673 1.5041 1.8331 -0.0279 0.3241 -0.1286 1859 HIS B C 6176 O O . HIS B 212 ? 1.6388 1.5027 1.7808 -0.0319 0.3307 -0.1188 1859 HIS B O 6177 C CB . HIS B 212 ? 1.8379 1.6323 1.9832 -0.0479 0.3012 -0.1361 1859 HIS B CB 6178 C CG . HIS B 212 ? 1.9269 1.6887 2.0955 -0.0544 0.2891 -0.1361 1859 HIS B CG 6179 N ND1 . HIS B 212 ? 1.7256 1.4792 1.8872 -0.0685 0.2792 -0.1163 1859 HIS B ND1 6180 C CD2 . HIS B 212 ? 2.1252 1.8602 2.3259 -0.0486 0.2867 -0.1521 1859 HIS B CD2 6181 C CE1 . HIS B 212 ? 1.8628 1.5897 2.0523 -0.0723 0.2717 -0.1180 1859 HIS B CE1 6182 N NE2 . HIS B 212 ? 2.1704 1.8833 2.3845 -0.0613 0.2751 -0.1393 1859 HIS B NE2 6183 N N . THR B 213 ? 1.7344 1.5643 1.9243 -0.0110 0.3321 -0.1510 1860 THR B N 6184 C CA . THR B 213 ? 1.8325 1.6934 2.0220 0.0051 0.3515 -0.1628 1860 THR B CA 6185 C C . THR B 213 ? 1.8064 1.6839 1.9459 0.0034 0.3584 -0.1824 1860 THR B C 6186 O O . THR B 213 ? 1.8137 1.6737 1.9263 -0.0062 0.3470 -0.1953 1860 THR B O 6187 C CB . THR B 213 ? 1.8887 1.7377 2.1181 0.0274 0.3609 -0.1815 1860 THR B CB 6188 O OG1 . THR B 213 ? 2.0627 1.8664 2.3108 0.0244 0.3469 -0.1900 1860 THR B OG1 6189 C CG2 . THR B 213 ? 1.7373 1.6120 2.0121 0.0379 0.3682 -0.1550 1860 THR B CG2 6190 N N . ASN B 214 ? 1.8067 1.7219 1.9355 0.0119 0.3765 -0.1807 1861 ASN B N 6191 C CA . ASN B 214 ? 1.8482 1.7868 1.9269 0.0098 0.3846 -0.1895 1861 ASN B CA 6192 C C . ASN B 214 ? 1.8323 1.7686 1.8773 -0.0104 0.3709 -0.1709 1861 ASN B C 6193 O O . ASN B 214 ? 1.9180 1.8645 1.9201 -0.0126 0.3715 -0.1804 1861 ASN B O 6194 C CB . ASN B 214 ? 1.9426 1.8711 1.9978 0.0225 0.3893 -0.2313 1861 ASN B CB 6195 C CG . ASN B 214 ? 2.1348 2.0847 2.2012 0.0459 0.4136 -0.2488 1861 ASN B CG 6196 O OD1 . ASN B 214 ? 2.1954 2.1851 2.2647 0.0504 0.4311 -0.2298 1861 ASN B OD1 6197 N ND2 . ASN B 214 ? 2.3548 2.2783 2.4300 0.0611 0.4160 -0.2851 1861 ASN B ND2 6198 N N . THR B 215 ? 1.7608 1.6845 1.8246 -0.0236 0.3588 -0.1436 1862 THR B N 6199 C CA . THR B 215 ? 1.7261 1.6452 1.7620 -0.0401 0.3480 -0.1247 1862 THR B CA 6200 C C . THR B 215 ? 1.7640 1.7072 1.7908 -0.0484 0.3554 -0.0960 1862 THR B C 6201 O O . THR B 215 ? 1.9191 1.8672 1.9114 -0.0563 0.3543 -0.0868 1862 THR B O 6202 C CB . THR B 215 ? 1.7951 1.6825 1.8491 -0.0503 0.3307 -0.1135 1862 THR B CB 6203 O OG1 . THR B 215 ? 2.2400 2.1228 2.2649 -0.0633 0.3225 -0.0980 1862 THR B OG1 6204 C CG2 . THR B 215 ? 1.7647 1.6520 1.8541 -0.0518 0.3301 -0.0920 1862 THR B CG2 6205 N N . LEU B 216 ? 1.7075 1.6651 1.7673 -0.0477 0.3614 -0.0804 1863 LEU B N 6206 C CA . LEU B 216 ? 1.6807 1.6619 1.7367 -0.0584 0.3678 -0.0539 1863 LEU B CA 6207 C C . LEU B 216 ? 1.8062 1.8249 1.8517 -0.0485 0.3893 -0.0596 1863 LEU B C 6208 O O . LEU B 216 ? 1.9207 1.9530 1.9815 -0.0311 0.4014 -0.0795 1863 LEU B O 6209 C CB . LEU B 216 ? 1.6287 1.6150 1.7257 -0.0643 0.3629 -0.0339 1863 LEU B CB 6210 C CG . LEU B 216 ? 1.7951 1.7470 1.9023 -0.0721 0.3429 -0.0273 1863 LEU B CG 6211 C CD1 . LEU B 216 ? 1.8889 1.8533 2.0415 -0.0711 0.3391 -0.0134 1863 LEU B CD1 6212 C CD2 . LEU B 216 ? 1.6979 1.6273 1.7733 -0.0896 0.3313 -0.0123 1863 LEU B CD2 6213 N N . ASN B 217 ? 1.9238 1.9578 1.9422 -0.0585 0.3953 -0.0418 1864 ASN B N 6214 C CA . ASN B 217 ? 2.0733 2.1438 2.0728 -0.0499 0.4168 -0.0443 1864 ASN B CA 6215 C C . ASN B 217 ? 2.1471 2.2565 2.1847 -0.0487 0.4338 -0.0279 1864 ASN B C 6216 O O . ASN B 217 ? 2.1405 2.2526 2.1998 -0.0654 0.4278 -0.0012 1864 ASN B O 6217 C CB . ASN B 217 ? 2.2218 2.2924 2.1773 -0.0607 0.4164 -0.0283 1864 ASN B CB 6218 C CG . ASN B 217 ? 2.5377 2.6416 2.4604 -0.0493 0.4363 -0.0355 1864 ASN B CG 6219 O OD1 . ASN B 217 ? 2.6256 2.7618 2.5494 -0.0528 0.4537 -0.0143 1864 ASN B OD1 6220 N ND2 . ASN B 217 ? 2.7523 2.8504 2.6460 -0.0360 0.4340 -0.0658 1864 ASN B ND2 6221 N N . PRO B 218 ? 2.2187 2.3598 2.2651 -0.0289 0.4552 -0.0443 1865 PRO B N 6222 C CA . PRO B 218 ? 2.1032 2.2853 2.1969 -0.0248 0.4716 -0.0293 1865 PRO B CA 6223 C C . PRO B 218 ? 2.1963 2.4032 2.2912 -0.0455 0.4768 0.0064 1865 PRO B C 6224 O O . PRO B 218 ? 2.0712 2.2768 2.1220 -0.0532 0.4806 0.0145 1865 PRO B O 6225 C CB . PRO B 218 ? 2.2089 2.4217 2.2925 0.0007 0.4986 -0.0534 1865 PRO B CB 6226 C CG . PRO B 218 ? 2.3334 2.5301 2.3524 0.0028 0.4973 -0.0718 1865 PRO B CG 6227 C CD . PRO B 218 ? 2.3841 2.5300 2.3921 -0.0106 0.4671 -0.0750 1865 PRO B CD 6228 N N . ALA B 219 ? 2.4450 2.6729 2.5916 -0.0551 0.4751 0.0285 1866 ALA B N 6229 C CA . ALA B 219 ? 2.5435 2.7948 2.7045 -0.0789 0.4774 0.0639 1866 ALA B CA 6230 C C . ALA B 219 ? 2.4142 2.6257 2.5367 -0.1027 0.4599 0.0789 1866 ALA B C 6231 O O . ALA B 219 ? 2.2604 2.4621 2.4025 -0.1257 0.4453 0.1007 1866 ALA B O 6232 C CB . ALA B 219 ? 2.4042 2.7123 2.5702 -0.0717 0.5096 0.0751 1866 ALA B CB 6233 N N . HIS B 220 ? 2.2789 2.4667 2.3478 -0.0962 0.4601 0.0656 1867 HIS B N 6234 C CA . HIS B 220 ? 2.1696 2.3271 2.1992 -0.1128 0.4503 0.0811 1867 HIS B CA 6235 C C . HIS B 220 ? 2.1547 2.2624 2.1845 -0.1278 0.4229 0.0838 1867 HIS B C 6236 O O . HIS B 220 ? 2.2725 2.3458 2.2644 -0.1317 0.4131 0.0840 1867 HIS B O 6237 C CB . HIS B 220 ? 2.1359 2.2873 2.1118 -0.0980 0.4561 0.0644 1867 HIS B CB 6238 C CG . HIS B 220 ? 2.3437 2.4779 2.2805 -0.1103 0.4531 0.0854 1867 HIS B CG 6239 N ND1 . HIS B 220 ? 2.4037 2.4917 2.3188 -0.1171 0.4322 0.0849 1867 HIS B ND1 6240 C CD2 . HIS B 220 ? 2.5274 2.6844 2.4454 -0.1161 0.4694 0.1101 1867 HIS B CD2 6241 C CE1 . HIS B 220 ? 2.6403 2.7214 2.5255 -0.1250 0.4351 0.1073 1867 HIS B CE1 6242 N NE2 . HIS B 220 ? 2.7037 2.8251 2.5893 -0.1254 0.4570 0.1237 1867 HIS B NE2 6243 N N . GLY B 221 ? 2.0145 2.1207 2.0859 -0.1357 0.4111 0.0875 1868 GLY B N 6244 C CA . GLY B 221 ? 1.8409 1.9017 1.9088 -0.1450 0.3863 0.0844 1868 GLY B CA 6245 C C . GLY B 221 ? 1.7292 1.7702 1.7863 -0.1260 0.3802 0.0572 1868 GLY B C 6246 O O . GLY B 221 ? 1.6036 1.6668 1.6729 -0.1075 0.3916 0.0402 1868 GLY B O 6247 N N . ARG B 222 ? 1.7629 1.7614 1.7975 -0.1301 0.3635 0.0524 1869 ARG B N 6248 C CA . ARG B 222 ? 1.8712 1.8511 1.9080 -0.1165 0.3551 0.0307 1869 ARG B CA 6249 C C . ARG B 222 ? 1.8150 1.7650 1.8132 -0.1131 0.3485 0.0200 1869 ARG B C 6250 O O . ARG B 222 ? 1.6912 1.6220 1.6627 -0.1231 0.3441 0.0324 1869 ARG B O 6251 C CB . ARG B 222 ? 2.1829 2.1496 2.2500 -0.1226 0.3396 0.0362 1869 ARG B CB 6252 C CG . ARG B 222 ? 2.5271 2.5286 2.6427 -0.1172 0.3444 0.0397 1869 ARG B CG 6253 C CD . ARG B 222 ? 2.7029 2.7315 2.8415 -0.1340 0.3450 0.0633 1869 ARG B CD 6254 N NE . ARG B 222 ? 2.8882 2.9536 3.0798 -0.1269 0.3473 0.0679 1869 ARG B NE 6255 C CZ . ARG B 222 ? 2.8586 2.9676 3.0837 -0.1336 0.3561 0.0843 1869 ARG B CZ 6256 N NH1 . ARG B 222 ? 3.0437 3.1630 3.2541 -0.1496 0.3641 0.0985 1869 ARG B NH1 6257 N NH2 . ARG B 222 ? 2.5001 2.6441 2.7773 -0.1239 0.3574 0.0886 1869 ARG B NH2 6258 N N . GLN B 223 ? 1.8181 1.7638 1.8174 -0.0990 0.3473 -0.0029 1870 GLN B N 6259 C CA . GLN B 223 ? 1.8868 1.8205 1.8538 -0.0930 0.3443 -0.0171 1870 GLN B CA 6260 C C . GLN B 223 ? 1.8147 1.7698 1.7503 -0.0924 0.3561 -0.0104 1870 GLN B C 6261 O O . GLN B 223 ? 1.8929 1.8779 1.8359 -0.0898 0.3710 -0.0062 1870 GLN B O 6262 C CB . GLN B 223 ? 2.1283 2.0276 2.0834 -0.1002 0.3290 -0.0118 1870 GLN B CB 6263 C CG . GLN B 223 ? 2.2892 2.1824 2.2187 -0.0944 0.3241 -0.0247 1870 GLN B CG 6264 C CD . GLN B 223 ? 2.1556 2.0400 2.1017 -0.0874 0.3165 -0.0480 1870 GLN B CD 6265 O OE1 . GLN B 223 ? 1.8176 1.7023 1.7485 -0.0839 0.3109 -0.0616 1870 GLN B OE1 6266 N NE2 . GLN B 223 ? 2.1758 2.0519 2.1549 -0.0864 0.3147 -0.0510 1870 GLN B NE2 6267 N N . VAL B 224 ? 1.7931 1.7360 1.6958 -0.0937 0.3502 -0.0074 1871 VAL B N 6268 C CA . VAL B 224 ? 1.8693 1.8294 1.7388 -0.0937 0.3594 0.0054 1871 VAL B CA 6269 C C . VAL B 224 ? 1.7391 1.6912 1.5755 -0.0891 0.3502 0.0017 1871 VAL B C 6270 O O . VAL B 224 ? 1.7866 1.7375 1.5987 -0.0921 0.3517 0.0218 1871 VAL B O 6271 C CB . VAL B 224 ? 1.9361 1.9362 1.8029 -0.0853 0.3785 -0.0001 1871 VAL B CB 6272 C CG1 . VAL B 224 ? 1.9919 2.0049 1.8425 -0.0699 0.3794 -0.0314 1871 VAL B CG1 6273 C CG2 . VAL B 224 ? 1.8326 1.8504 1.6759 -0.0910 0.3908 0.0264 1871 VAL B CG2 6274 N N . THR B 225 ? 1.6251 1.5721 1.4642 -0.0822 0.3400 -0.0224 1872 THR B N 6275 C CA . THR B 225 ? 1.6841 1.6333 1.4963 -0.0776 0.3296 -0.0289 1872 THR B CA 6276 C C . THR B 225 ? 1.6931 1.6159 1.5099 -0.0822 0.3158 -0.0183 1872 THR B C 6277 O O . THR B 225 ? 1.5997 1.5267 1.4019 -0.0785 0.3054 -0.0210 1872 THR B O 6278 C CB . THR B 225 ? 1.7065 1.6669 1.5186 -0.0696 0.3248 -0.0625 1872 THR B CB 6279 O OG1 . THR B 225 ? 1.6736 1.6194 1.5226 -0.0698 0.3249 -0.0769 1872 THR B OG1 6280 C CG2 . THR B 225 ? 1.8327 1.8254 1.6163 -0.0610 0.3379 -0.0717 1872 THR B CG2 6281 N N . VAL B 226 ? 1.6152 1.5135 1.4525 -0.0897 0.3157 -0.0061 1873 VAL B N 6282 C CA . VAL B 226 ? 1.5833 1.4560 1.4210 -0.0927 0.3075 0.0066 1873 VAL B CA 6283 C C . VAL B 226 ? 1.6577 1.5109 1.4971 -0.1016 0.3135 0.0270 1873 VAL B C 6284 O O . VAL B 226 ? 1.6579 1.5172 1.5116 -0.1070 0.3197 0.0270 1873 VAL B O 6285 C CB . VAL B 226 ? 1.6159 1.4747 1.4792 -0.0933 0.2980 -0.0072 1873 VAL B CB 6286 C CG1 . VAL B 226 ? 1.5927 1.4673 1.4697 -0.0892 0.2956 -0.0337 1873 VAL B CG1 6287 C CG2 . VAL B 226 ? 1.6531 1.4878 1.5341 -0.1006 0.2989 0.0019 1873 VAL B CG2 6288 N N . GLN B 227 ? 1.6782 1.5087 1.5038 -0.1028 0.3116 0.0439 1874 GLN B N 6289 C CA . GLN B 227 ? 1.6373 1.4409 1.4627 -0.1129 0.3145 0.0595 1874 GLN B CA 6290 C C . GLN B 227 ? 1.5995 1.3812 1.4408 -0.1158 0.3075 0.0521 1874 GLN B C 6291 O O . GLN B 227 ? 1.3381 1.1131 1.1808 -0.1091 0.3023 0.0470 1874 GLN B O 6292 C CB . GLN B 227 ? 1.6174 1.4012 1.4192 -0.1116 0.3171 0.0795 1874 GLN B CB 6293 C CG . GLN B 227 ? 1.7465 1.5533 1.5305 -0.1086 0.3245 0.0916 1874 GLN B CG 6294 C CD . GLN B 227 ? 1.9115 1.7080 1.6736 -0.0990 0.3235 0.1084 1874 GLN B CD 6295 O OE1 . GLN B 227 ? 1.8603 1.6658 1.6200 -0.0877 0.3163 0.1024 1874 GLN B OE1 6296 N NE2 . GLN B 227 ? 2.0166 1.7954 1.7657 -0.1037 0.3305 0.1313 1874 GLN B NE2 6297 N N . GLU B 228 ? 1.7599 1.5368 1.6158 -0.1257 0.3072 0.0525 1875 GLU B N 6298 C CA . GLU B 228 ? 1.7404 1.4987 1.6085 -0.1298 0.3002 0.0488 1875 GLU B CA 6299 C C . GLU B 228 ? 1.7737 1.4988 1.6233 -0.1384 0.2991 0.0612 1875 GLU B C 6300 O O . GLU B 228 ? 1.9406 1.6619 1.7824 -0.1468 0.3026 0.0716 1875 GLU B O 6301 C CB . GLU B 228 ? 1.7195 1.4941 1.6141 -0.1355 0.2986 0.0443 1875 GLU B CB 6302 C CG . GLU B 228 ? 1.7135 1.5137 1.6299 -0.1262 0.2999 0.0287 1875 GLU B CG 6303 C CD . GLU B 228 ? 1.7023 1.5230 1.6456 -0.1290 0.3021 0.0275 1875 GLU B CD 6304 O OE1 . GLU B 228 ? 1.6968 1.5286 1.6395 -0.1366 0.3072 0.0382 1875 GLU B OE1 6305 O OE2 . GLU B 228 ? 1.7074 1.5338 1.6754 -0.1232 0.2993 0.0175 1875 GLU B OE2 6306 N N . PHE B 229 ? 1.6423 1.3429 1.4849 -0.1367 0.2948 0.0597 1876 PHE B N 6307 C CA . PHE B 229 ? 1.5951 1.2593 1.4166 -0.1444 0.2930 0.0662 1876 PHE B CA 6308 C C . PHE B 229 ? 1.5893 1.2415 1.4121 -0.1461 0.2865 0.0615 1876 PHE B C 6309 O O . PHE B 229 ? 1.7109 1.3696 1.5410 -0.1363 0.2874 0.0572 1876 PHE B O 6310 C CB . PHE B 229 ? 1.6592 1.3001 1.4574 -0.1344 0.2990 0.0715 1876 PHE B CB 6311 C CG . PHE B 229 ? 1.7293 1.3738 1.5197 -0.1336 0.3046 0.0816 1876 PHE B CG 6312 C CD1 . PHE B 229 ? 1.8769 1.5184 1.6674 -0.1480 0.3051 0.0893 1876 PHE B CD1 6313 C CD2 . PHE B 229 ? 1.7833 1.4367 1.5678 -0.1190 0.3090 0.0859 1876 PHE B CD2 6314 C CE1 . PHE B 229 ? 2.1387 1.7842 1.9218 -0.1476 0.3119 0.1025 1876 PHE B CE1 6315 C CE2 . PHE B 229 ? 1.8814 1.5391 1.6562 -0.1172 0.3139 0.0987 1876 PHE B CE2 6316 C CZ . PHE B 229 ? 2.0733 1.7259 1.8463 -0.1314 0.3163 0.1077 1876 PHE B CZ 6317 N N . ALA B 230 ? 1.4350 1.0707 1.2503 -0.1596 0.2795 0.0634 1877 ALA B N 6318 C CA . ALA B 230 ? 1.4263 1.0514 1.2366 -0.1615 0.2722 0.0609 1877 ALA B CA 6319 C C . ALA B 230 ? 1.5466 1.1302 1.3190 -0.1654 0.2704 0.0600 1877 ALA B C 6320 O O . ALA B 230 ? 1.5471 1.1130 1.3063 -0.1804 0.2626 0.0601 1877 ALA B O 6321 C CB . ALA B 230 ? 1.2827 0.9317 1.1192 -0.1710 0.2620 0.0622 1877 ALA B CB 6322 N N . LEU B 231 ? 1.7263 1.2958 1.4824 -0.1520 0.2779 0.0583 1878 LEU B N 6323 C CA . LEU B 231 ? 1.7530 1.2829 1.4695 -0.1504 0.2803 0.0548 1878 LEU B CA 6324 C C . LEU B 231 ? 1.8259 1.3551 1.5312 -0.1531 0.2737 0.0539 1878 LEU B C 6325 O O . LEU B 231 ? 1.8512 1.4078 1.5805 -0.1485 0.2729 0.0584 1878 LEU B O 6326 C CB . LEU B 231 ? 1.7272 1.2448 1.4327 -0.1316 0.2954 0.0555 1878 LEU B CB 6327 C CG . LEU B 231 ? 1.8571 1.3806 1.5740 -0.1255 0.3015 0.0601 1878 LEU B CG 6328 C CD1 . LEU B 231 ? 1.9650 1.4672 1.6651 -0.1074 0.3146 0.0623 1878 LEU B CD1 6329 C CD2 . LEU B 231 ? 1.9037 1.4144 1.6168 -0.1412 0.2956 0.0619 1878 LEU B CD2 6330 N N . PHE B 232 ? 1.8594 1.3555 1.5263 -0.1608 0.2684 0.0483 1879 PHE B N 6331 C CA . PHE B 232 ? 1.7972 1.2932 1.4466 -0.1659 0.2590 0.0484 1879 PHE B CA 6332 C C . PHE B 232 ? 1.8489 1.3023 1.4436 -0.1619 0.2643 0.0389 1879 PHE B C 6333 O O . PHE B 232 ? 2.0676 1.4855 1.6349 -0.1709 0.2603 0.0291 1879 PHE B O 6334 C CB . PHE B 232 ? 1.8246 1.3343 1.4877 -0.1863 0.2388 0.0500 1879 PHE B CB 6335 C CG . PHE B 232 ? 1.8346 1.3319 1.4647 -0.1968 0.2240 0.0475 1879 PHE B CG 6336 C CD1 . PHE B 232 ? 1.9597 1.4170 1.5460 -0.2084 0.2170 0.0353 1879 PHE B CD1 6337 C CD2 . PHE B 232 ? 1.8639 1.3882 1.5059 -0.1957 0.2157 0.0575 1879 PHE B CD2 6338 C CE1 . PHE B 232 ? 2.0089 1.4558 1.5597 -0.2190 0.2009 0.0310 1879 PHE B CE1 6339 C CE2 . PHE B 232 ? 1.9413 1.4577 1.5497 -0.2051 0.2002 0.0572 1879 PHE B CE2 6340 C CZ . PHE B 232 ? 1.9481 1.4271 1.5089 -0.2171 0.1921 0.0429 1879 PHE B CZ 6341 N N . PHE B 233 ? 1.7951 1.2501 1.3736 -0.1483 0.2745 0.0417 1880 PHE B N 6342 C CA . PHE B 233 ? 1.9572 1.3730 1.4836 -0.1386 0.2859 0.0315 1880 PHE B CA 6343 C C . PHE B 233 ? 2.1158 1.5227 1.6008 -0.1459 0.2757 0.0283 1880 PHE B C 6344 O O . PHE B 233 ? 2.1956 1.6321 1.6918 -0.1439 0.2737 0.0408 1880 PHE B O 6345 C CB . PHE B 233 ? 1.9006 1.3250 1.4355 -0.1149 0.3096 0.0374 1880 PHE B CB 6346 C CG . PHE B 233 ? 1.9023 1.3397 1.4762 -0.1075 0.3169 0.0415 1880 PHE B CG 6347 C CD1 . PHE B 233 ? 1.8317 1.3093 1.4556 -0.1122 0.3102 0.0507 1880 PHE B CD1 6348 C CD2 . PHE B 233 ? 2.0217 1.4299 1.5806 -0.0949 0.3299 0.0360 1880 PHE B CD2 6349 C CE1 . PHE B 233 ? 1.7772 1.2686 1.4309 -0.1057 0.3154 0.0536 1880 PHE B CE1 6350 C CE2 . PHE B 233 ? 1.9661 1.3894 1.5587 -0.0877 0.3347 0.0425 1880 PHE B CE2 6351 C CZ . PHE B 233 ? 1.8792 1.3455 1.5171 -0.0939 0.3268 0.0509 1880 PHE B CZ 6352 N N . THR B 234 ? 2.1841 1.5492 1.6207 -0.1555 0.2679 0.0118 1881 THR B N 6353 C CA . THR B 234 ? 2.2135 1.5672 1.6000 -0.1625 0.2567 0.0058 1881 THR B CA 6354 C C . THR B 234 ? 2.2302 1.5286 1.5535 -0.1559 0.2666 -0.0160 1881 THR B C 6355 O O . THR B 234 ? 2.1456 1.4130 1.4700 -0.1487 0.2787 -0.0251 1881 THR B O 6356 C CB . THR B 234 ? 2.2029 1.5689 1.5968 -0.1894 0.2254 0.0062 1881 THR B CB 6357 O OG1 . THR B 234 ? 2.2239 1.6340 1.6841 -0.1936 0.2197 0.0228 1881 THR B OG1 6358 C CG2 . THR B 234 ? 2.0692 1.4457 1.4253 -0.1949 0.2107 0.0096 1881 THR B CG2 6359 N N . ILE B 235 ? 2.2946 1.5821 1.5626 -0.1554 0.2635 -0.0228 1882 ILE B N 6360 C CA . ILE B 235 ? 2.3418 1.5741 1.5387 -0.1596 0.2600 -0.0493 1882 ILE B CA 6361 C C . ILE B 235 ? 2.3170 1.5498 1.5080 -0.1915 0.2238 -0.0550 1882 ILE B C 6362 O O . ILE B 235 ? 2.3137 1.5860 1.5135 -0.2010 0.2063 -0.0408 1882 ILE B O 6363 C CB . ILE B 235 ? 2.3307 1.5550 1.4656 -0.1411 0.2767 -0.0540 1882 ILE B CB 6364 C CG1 . ILE B 235 ? 2.3032 1.5040 1.4270 -0.1112 0.3126 -0.0601 1882 ILE B CG1 6365 C CG2 . ILE B 235 ? 2.3979 1.5789 1.4544 -0.1541 0.2604 -0.0803 1882 ILE B CG2 6366 C CD1 . ILE B 235 ? 2.3511 1.5996 1.5358 -0.0927 0.3337 -0.0339 1882 ILE B CD1 6367 N N . PHE B 236 ? 2.3904 1.5826 1.5743 -0.2084 0.2121 -0.0730 1883 PHE B N 6368 C CA . PHE B 236 ? 2.5188 1.7079 1.6934 -0.2406 0.1771 -0.0811 1883 PHE B CA 6369 C C . PHE B 236 ? 2.6900 1.8276 1.7791 -0.2446 0.1705 -0.1097 1883 PHE B C 6370 O O . PHE B 236 ? 2.8419 1.9204 1.8922 -0.2351 0.1861 -0.1326 1883 PHE B O 6371 C CB . PHE B 236 ? 2.5174 1.6954 1.7374 -0.2611 0.1664 -0.0819 1883 PHE B CB 6372 C CG . PHE B 236 ? 2.4666 1.7048 1.7652 -0.2647 0.1632 -0.0550 1883 PHE B CG 6373 C CD1 . PHE B 236 ? 2.4158 1.6736 1.7565 -0.2424 0.1887 -0.0404 1883 PHE B CD1 6374 C CD2 . PHE B 236 ? 2.4067 1.6845 1.7375 -0.2891 0.1346 -0.0446 1883 PHE B CD2 6375 C CE1 . PHE B 236 ? 2.2392 1.5495 1.6466 -0.2447 0.1864 -0.0193 1883 PHE B CE1 6376 C CE2 . PHE B 236 ? 2.2780 1.6100 1.6796 -0.2892 0.1345 -0.0217 1883 PHE B CE2 6377 C CZ . PHE B 236 ? 2.2392 1.5850 1.6763 -0.2670 0.1608 -0.0107 1883 PHE B CZ 6378 N N . ASP B 237 ? 2.6843 1.8440 1.7418 -0.2564 0.1479 -0.1086 1884 ASP B N 6379 C CA . ASP B 237 ? 2.8613 1.9773 1.8293 -0.2582 0.1417 -0.1361 1884 ASP B CA 6380 C C . ASP B 237 ? 2.8045 1.9199 1.7552 -0.2945 0.0985 -0.1471 1884 ASP B C 6381 O O . ASP B 237 ? 2.8497 2.0137 1.8043 -0.3044 0.0758 -0.1304 1884 ASP B O 6382 C CB . ASP B 237 ? 3.0106 2.1538 1.9406 -0.2346 0.1578 -0.1244 1884 ASP B CB 6383 C CG . ASP B 237 ? 3.0733 2.1698 1.9028 -0.2298 0.1595 -0.1543 1884 ASP B CG 6384 O OD1 . ASP B 237 ? 3.1076 2.1844 1.8937 -0.2561 0.1263 -0.1742 1884 ASP B OD1 6385 O OD2 . ASP B 237 ? 3.0625 2.1445 1.8571 -0.1996 0.1940 -0.1580 1884 ASP B OD2 6386 N N . GLU B 238 ? 2.6455 1.7055 1.5784 -0.3148 0.0860 -0.1743 1885 GLU B N 6387 C CA . GLU B 238 ? 2.6653 1.7300 1.5981 -0.3536 0.0429 -0.1822 1885 GLU B CA 6388 C C . GLU B 238 ? 2.9277 1.9743 1.7716 -0.3635 0.0199 -0.2054 1885 GLU B C 6389 O O . GLU B 238 ? 3.2398 2.2503 2.0527 -0.3940 -0.0103 -0.2314 1885 GLU B O 6390 C CB . GLU B 238 ? 2.6603 1.6762 1.6166 -0.3760 0.0360 -0.1988 1885 GLU B CB 6391 C CG . GLU B 238 ? 2.6603 1.6988 1.7006 -0.3663 0.0577 -0.1736 1885 GLU B CG 6392 C CD . GLU B 238 ? 2.6948 1.7871 1.8132 -0.3947 0.0325 -0.1505 1885 GLU B CD 6393 O OE1 . GLU B 238 ? 2.6870 1.8256 1.8129 -0.4134 0.0019 -0.1415 1885 GLU B OE1 6394 O OE2 . GLU B 238 ? 2.6746 1.7650 1.8486 -0.3970 0.0444 -0.1398 1885 GLU B OE2 6395 N N . THR B 239 ? 2.9471 2.0182 1.7492 -0.3387 0.0340 -0.1959 1886 THR B N 6396 C CA . THR B 239 ? 3.1369 2.2163 1.8635 -0.3485 0.0076 -0.2058 1886 THR B CA 6397 C C . THR B 239 ? 3.1432 2.3038 1.9246 -0.3606 -0.0195 -0.1682 1886 THR B C 6398 O O . THR B 239 ? 3.3568 2.5382 2.1070 -0.3825 -0.0576 -0.1699 1886 THR B O 6399 C CB . THR B 239 ? 3.2080 2.2754 1.8578 -0.3147 0.0383 -0.2112 1886 THR B CB 6400 O OG1 . THR B 239 ? 3.2235 2.2308 1.8529 -0.2914 0.0767 -0.2337 1886 THR B OG1 6401 C CG2 . THR B 239 ? 3.2901 2.3423 1.8374 -0.3274 0.0109 -0.2352 1886 THR B CG2 6402 N N . LYS B 240 ? 2.9813 2.1870 1.8447 -0.3450 0.0002 -0.1345 1887 LYS B N 6403 C CA . LYS B 240 ? 2.9752 2.2514 1.9130 -0.3569 -0.0227 -0.1000 1887 LYS B CA 6404 C C . LYS B 240 ? 3.0026 2.2734 1.9940 -0.3893 -0.0471 -0.1083 1887 LYS B C 6405 O O . LYS B 240 ? 3.0617 2.2752 2.0130 -0.4074 -0.0564 -0.1413 1887 LYS B O 6406 C CB . LYS B 240 ? 3.0393 2.3546 2.0406 -0.3280 0.0102 -0.0672 1887 LYS B CB 6407 C CG . LYS B 240 ? 3.2169 2.5382 2.1715 -0.2976 0.0368 -0.0563 1887 LYS B CG 6408 C CD . LYS B 240 ? 3.1449 2.4146 2.0578 -0.2728 0.0775 -0.0769 1887 LYS B CD 6409 C CE . LYS B 240 ? 3.0438 2.3315 1.9266 -0.2429 0.1067 -0.0591 1887 LYS B CE 6410 N NZ . LYS B 240 ? 3.0337 2.2904 1.8113 -0.2362 0.1097 -0.0802 1887 LYS B NZ 6411 N N . SER B 241 ? 2.9872 2.3145 2.0684 -0.3963 -0.0557 -0.0791 1888 SER B N 6412 C CA . SER B 241 ? 2.9907 2.3250 2.1305 -0.4278 -0.0784 -0.0810 1888 SER B CA 6413 C C . SER B 241 ? 2.9908 2.3410 2.1083 -0.4618 -0.1269 -0.0883 1888 SER B C 6414 O O . SER B 241 ? 3.1706 2.4690 2.2139 -0.4773 -0.1420 -0.1209 1888 SER B O 6415 C CB . SER B 241 ? 2.9551 2.2220 2.0881 -0.4341 -0.0609 -0.1073 1888 SER B CB 6416 O OG . SER B 241 ? 2.6819 1.9599 1.8805 -0.4625 -0.0766 -0.1027 1888 SER B OG 6417 N N . TRP B 242 ? 2.8093 2.2309 1.9905 -0.4723 -0.1514 -0.0588 1889 TRP B N 6418 C CA . TRP B 242 ? 2.8442 2.2936 2.0243 -0.5075 -0.2010 -0.0607 1889 TRP B CA 6419 C C . TRP B 242 ? 3.0321 2.4233 2.1847 -0.5428 -0.2195 -0.0968 1889 TRP B C 6420 O O . TRP B 242 ? 3.2342 2.6292 2.3595 -0.5749 -0.2623 -0.1099 1889 TRP B O 6421 C CB . TRP B 242 ? 2.7154 2.2453 1.9987 -0.5156 -0.2169 -0.0246 1889 TRP B CB 6422 C CG . TRP B 242 ? 2.5936 2.1847 1.9071 -0.4886 -0.2123 0.0115 1889 TRP B CG 6423 C CD1 . TRP B 242 ? 2.6188 2.2041 1.9179 -0.4525 -0.1774 0.0227 1889 TRP B CD1 6424 C CD2 . TRP B 242 ? 2.5528 2.2204 1.9239 -0.4959 -0.2432 0.0430 1889 TRP B CD2 6425 N NE1 . TRP B 242 ? 2.6365 2.2836 1.9766 -0.4376 -0.1846 0.0581 1889 TRP B NE1 6426 C CE2 . TRP B 242 ? 2.5657 2.2641 1.9504 -0.4621 -0.2244 0.0714 1889 TRP B CE2 6427 C CE3 . TRP B 242 ? 2.5050 2.2190 1.9201 -0.5277 -0.2853 0.0509 1889 TRP B CE3 6428 C CZ2 . TRP B 242 ? 2.5317 2.3012 1.9711 -0.4567 -0.2455 0.1074 1889 TRP B CZ2 6429 C CZ3 . TRP B 242 ? 2.4697 2.2607 1.9414 -0.5215 -0.3063 0.0875 1889 TRP B CZ3 6430 C CH2 . TRP B 242 ? 2.4320 2.2477 1.9142 -0.4853 -0.2860 0.1150 1889 TRP B CH2 6431 N N . TYR B 243 ? 2.9052 2.2418 2.0648 -0.5372 -0.1882 -0.1121 1890 TYR B N 6432 C CA . TYR B 243 ? 2.8293 2.1044 1.9729 -0.5687 -0.2004 -0.1431 1890 TYR B CA 6433 C C . TYR B 243 ? 2.8544 2.0417 1.8932 -0.5642 -0.1930 -0.1855 1890 TYR B C 6434 O O . TYR B 243 ? 2.8146 1.9393 1.8373 -0.5501 -0.1609 -0.2022 1890 TYR B O 6435 C CB . TYR B 243 ? 2.7587 2.0294 1.9793 -0.5700 -0.1758 -0.1311 1890 TYR B CB 6436 C CG . TYR B 243 ? 2.7698 2.1258 2.0909 -0.5806 -0.1879 -0.0942 1890 TYR B CG 6437 C CD1 . TYR B 243 ? 2.8921 2.2937 2.2438 -0.6170 -0.2331 -0.0877 1890 TYR B CD1 6438 C CD2 . TYR B 243 ? 2.7283 2.1217 2.1143 -0.5537 -0.1548 -0.0665 1890 TYR B CD2 6439 C CE1 . TYR B 243 ? 2.8041 2.2876 2.2518 -0.6240 -0.2420 -0.0530 1890 TYR B CE1 6440 C CE2 . TYR B 243 ? 2.7199 2.1901 2.1959 -0.5607 -0.1632 -0.0349 1890 TYR B CE2 6441 C CZ . TYR B 243 ? 2.7180 2.2341 2.2266 -0.5943 -0.2051 -0.0273 1890 TYR B CZ 6442 O OH . TYR B 243 ? 2.5375 2.1329 2.1390 -0.5975 -0.2101 0.0051 1890 TYR B OH 6443 N N . PHE B 244 ? 2.9866 2.1724 1.9533 -0.5747 -0.2233 -0.2021 1891 PHE B N 6444 C CA . PHE B 244 ? 3.1204 2.2238 1.9825 -0.5784 -0.2258 -0.2480 1891 PHE B CA 6445 C C . PHE B 244 ? 3.1342 2.2105 1.9754 -0.6278 -0.2744 -0.2766 1891 PHE B C 6446 O O . PHE B 244 ? 2.9517 2.0315 1.7272 -0.6455 -0.3116 -0.2944 1891 PHE B O 6447 C CB . PHE B 244 ? 3.2826 2.3842 2.0569 -0.5471 -0.2130 -0.2537 1891 PHE B CB 6448 C CG . PHE B 244 ? 3.2179 2.2515 1.9385 -0.5113 -0.1646 -0.2749 1891 PHE B CG 6449 C CD1 . PHE B 244 ? 3.1874 2.1452 1.9081 -0.5163 -0.1478 -0.3019 1891 PHE B CD1 6450 C CD2 . PHE B 244 ? 3.1507 2.1976 1.8237 -0.4726 -0.1357 -0.2655 1891 PHE B CD2 6451 C CE1 . PHE B 244 ? 3.2012 2.0992 1.8765 -0.4814 -0.1037 -0.3198 1891 PHE B CE1 6452 C CE2 . PHE B 244 ? 3.1529 2.1428 1.7813 -0.4393 -0.0908 -0.2838 1891 PHE B CE2 6453 C CZ . PHE B 244 ? 3.1955 2.1118 1.8258 -0.4426 -0.0750 -0.3111 1891 PHE B CZ 6454 N N . THR B 245 ? 3.1493 2.2053 2.0568 -0.6500 -0.2728 -0.2760 1892 THR B N 6455 C CA . THR B 245 ? 3.2029 2.1918 2.0952 -0.6907 -0.2970 -0.3105 1892 THR B CA 6456 C C . THR B 245 ? 3.2959 2.1757 2.0883 -0.6708 -0.2699 -0.3566 1892 THR B C 6457 O O . THR B 245 ? 3.2206 2.0896 1.9305 -0.6417 -0.2578 -0.3703 1892 THR B O 6458 C CB . THR B 245 ? 2.9799 1.9876 1.9827 -0.7108 -0.2910 -0.2851 1892 THR B CB 6459 O OG1 . THR B 245 ? 2.7764 1.7896 1.8182 -0.6703 -0.2402 -0.2614 1892 THR B OG1 6460 C CG2 . THR B 245 ? 2.7629 1.8740 1.8535 -0.7360 -0.3248 -0.2476 1892 THR B CG2 6461 N N . GLU B 246 ? 3.2803 2.0811 2.0790 -0.6859 -0.2610 -0.3796 1893 GLU B N 6462 C CA . GLU B 246 ? 3.2402 1.9427 1.9750 -0.6555 -0.2205 -0.4115 1893 GLU B CA 6463 C C . GLU B 246 ? 3.3370 1.9255 2.0113 -0.6794 -0.2315 -0.4633 1893 GLU B C 6464 O O . GLU B 246 ? 3.3813 1.9481 2.0144 -0.7190 -0.2761 -0.4932 1893 GLU B O 6465 C CB . GLU B 246 ? 3.1472 1.8590 1.8200 -0.6033 -0.1850 -0.4105 1893 GLU B CB 6466 C CG . GLU B 246 ? 3.0620 1.8514 1.8134 -0.5713 -0.1533 -0.3602 1893 GLU B CG 6467 C CD . GLU B 246 ? 2.9971 1.8170 1.8590 -0.5903 -0.1532 -0.3290 1893 GLU B CD 6468 O OE1 . GLU B 246 ? 3.0192 1.7758 1.8944 -0.6114 -0.1544 -0.3455 1893 GLU B OE1 6469 O OE2 . GLU B 246 ? 2.8798 1.7858 1.8152 -0.5843 -0.1515 -0.2877 1893 GLU B OE2 6470 N N . ASN B 247 ? 3.2838 1.7999 1.9539 -0.6531 -0.1898 -0.4730 1894 ASN B N 6471 C CA . ASN B 247 ? 3.3095 1.7132 1.9513 -0.6724 -0.1913 -0.5122 1894 ASN B CA 6472 C C . ASN B 247 ? 3.4552 1.7661 1.9755 -0.6531 -0.1820 -0.5678 1894 ASN B C 6473 O O . ASN B 247 ? 3.5524 1.7790 2.0229 -0.6839 -0.2069 -0.6129 1894 ASN B O 6474 C CB . ASN B 247 ? 3.1632 1.5417 1.8741 -0.6524 -0.1506 -0.4871 1894 ASN B CB 6475 C CG . ASN B 247 ? 2.9806 1.4623 1.7991 -0.6526 -0.1450 -0.4294 1894 ASN B CG 6476 O OD1 . ASN B 247 ? 2.9371 1.4736 1.8125 -0.6935 -0.1807 -0.4116 1894 ASN B OD1 6477 N ND2 . ASN B 247 ? 2.7884 1.2990 1.6355 -0.6066 -0.1007 -0.4007 1894 ASN B ND2 6478 N N . THR B 264 ? 4.8939 3.4872 2.7868 -0.4312 -0.1152 -0.5792 1911 THR B N 6479 C CA . THR B 264 ? 4.8148 3.4176 2.7401 -0.3813 -0.0532 -0.5540 1911 THR B CA 6480 C C . THR B 264 ? 5.0961 3.6076 2.9325 -0.3477 -0.0105 -0.6017 1911 THR B C 6481 O O . THR B 264 ? 5.3288 3.8060 3.0480 -0.3436 -0.0157 -0.6401 1911 THR B O 6482 C CB . THR B 264 ? 4.6298 3.3310 2.5710 -0.3578 -0.0404 -0.5013 1911 THR B CB 6483 O OG1 . THR B 264 ? 4.5463 3.2545 2.5144 -0.3108 0.0196 -0.4799 1911 THR B OG1 6484 C CG2 . THR B 264 ? 4.6204 3.3394 2.4465 -0.3587 -0.0606 -0.5145 1911 THR B CG2 6485 N N . PHE B 265 ? 4.9705 3.4424 2.8625 -0.3240 0.0301 -0.6000 1912 PHE B N 6486 C CA . PHE B 265 ? 4.9184 3.3126 2.7455 -0.2832 0.0791 -0.6362 1912 PHE B CA 6487 C C . PHE B 265 ? 4.8989 3.3478 2.7485 -0.2307 0.1360 -0.5975 1912 PHE B C 6488 O O . PHE B 265 ? 5.0996 3.5781 2.8751 -0.2095 0.1503 -0.5962 1912 PHE B O 6489 C CB . PHE B 265 ? 4.6150 2.9156 2.4741 -0.2918 0.0840 -0.6668 1912 PHE B CB 6490 C CG . PHE B 265 ? 4.4674 2.6971 2.2803 -0.3403 0.0333 -0.7155 1912 PHE B CG 6491 C CD1 . PHE B 265 ? 4.4977 2.6659 2.1813 -0.3433 0.0214 -0.7722 1912 PHE B CD1 6492 C CD2 . PHE B 265 ? 4.1953 2.4174 2.0941 -0.3833 -0.0013 -0.7059 1912 PHE B CD2 6493 C CE1 . PHE B 265 ? 4.4382 2.5393 2.0814 -0.3902 -0.0271 -0.8187 1912 PHE B CE1 6494 C CE2 . PHE B 265 ? 4.2229 2.3810 2.0859 -0.4304 -0.0479 -0.7491 1912 PHE B CE2 6495 C CZ . PHE B 265 ? 4.3603 2.4566 2.0962 -0.4348 -0.0622 -0.8064 1912 PHE B CZ 6496 N N . LYS B 266 ? 4.6738 3.1379 2.6219 -0.2110 0.1672 -0.5658 1913 LYS B N 6497 C CA . LYS B 266 ? 4.3692 2.9100 2.3705 -0.1737 0.2082 -0.5159 1913 LYS B CA 6498 C C . LYS B 266 ? 4.1387 2.6944 2.2543 -0.1580 0.2351 -0.4833 1913 LYS B C 6499 O O . LYS B 266 ? 4.1181 2.6386 2.2379 -0.1214 0.2792 -0.4904 1913 LYS B O 6500 C CB . LYS B 266 ? 4.3260 2.8663 2.2418 -0.1298 0.2524 -0.5257 1913 LYS B CB 6501 C CG . LYS B 266 ? 4.0856 2.7230 2.0464 -0.1075 0.2761 -0.4699 1913 LYS B CG 6502 C CD . LYS B 266 ? 4.0001 2.6381 1.9287 -0.0557 0.3369 -0.4679 1913 LYS B CD 6503 C CE . LYS B 266 ? 3.7706 2.3961 1.7836 -0.0281 0.3755 -0.4549 1913 LYS B CE 6504 N NZ . LYS B 266 ? 3.4665 2.1605 1.6012 -0.0403 0.3659 -0.4037 1913 LYS B NZ 6505 N N . GLU B 267 ? 3.8149 2.4257 2.0216 -0.1857 0.2071 -0.4474 1914 GLU B N 6506 C CA . GLU B 267 ? 3.5049 2.1593 1.8205 -0.1726 0.2279 -0.4057 1914 GLU B CA 6507 C C . GLU B 267 ? 3.4510 2.0480 1.8187 -0.1730 0.2371 -0.4158 1914 GLU B C 6508 O O . GLU B 267 ? 3.3292 1.8417 1.6458 -0.1619 0.2511 -0.4551 1914 GLU B O 6509 C CB . GLU B 267 ? 3.4679 2.1727 1.7924 -0.1293 0.2737 -0.3769 1914 GLU B CB 6510 C CG . GLU B 267 ? 3.3355 2.1247 1.7635 -0.1274 0.2778 -0.3233 1914 GLU B CG 6511 C CD . GLU B 267 ? 3.2352 2.0211 1.7557 -0.1446 0.2656 -0.3107 1914 GLU B CD 6512 O OE1 . GLU B 267 ? 3.1938 1.9945 1.7423 -0.1816 0.2253 -0.3061 1914 GLU B OE1 6513 O OE2 . GLU B 267 ? 3.1365 1.9063 1.7017 -0.1218 0.2952 -0.3047 1914 GLU B OE2 6514 N N . ASN B 268 ? 3.3980 2.0437 1.8669 -0.1861 0.2280 -0.3785 1915 ASN B N 6515 C CA . ASN B 268 ? 3.3011 1.9210 1.8439 -0.1858 0.2375 -0.3696 1915 ASN B CA 6516 C C . ASN B 268 ? 2.9175 1.6122 1.5677 -0.1978 0.2285 -0.3231 1915 ASN B C 6517 O O . ASN B 268 ? 2.7238 1.4377 1.4275 -0.1718 0.2580 -0.3004 1915 ASN B O 6518 C CB . ASN B 268 ? 3.6254 2.1578 2.1413 -0.2133 0.2149 -0.4074 1915 ASN B CB 6519 C CG . ASN B 268 ? 3.6695 2.1640 2.2480 -0.2068 0.2310 -0.3994 1915 ASN B CG 6520 O OD1 . ASN B 268 ? 3.6075 2.1542 2.2717 -0.2122 0.2298 -0.3621 1915 ASN B OD1 6521 N ND2 . ASN B 268 ? 3.7324 2.1338 2.2663 -0.1946 0.2460 -0.4346 1915 ASN B ND2 6522 N N . TYR B 269 ? 2.8451 1.5813 1.5243 -0.2353 0.1887 -0.3105 1916 TYR B N 6523 C CA . TYR B 269 ? 2.8547 1.6493 1.6337 -0.2527 0.1757 -0.2736 1916 TYR B CA 6524 C C . TYR B 269 ? 2.7026 1.5817 1.5447 -0.2338 0.1913 -0.2315 1916 TYR B C 6525 O O . TYR B 269 ? 2.3561 1.2983 1.2379 -0.2517 0.1685 -0.2078 1916 TYR B O 6526 C CB . TYR B 269 ? 2.9380 1.7521 1.7348 -0.2988 0.1283 -0.2732 1916 TYR B CB 6527 C CG . TYR B 269 ? 3.0084 1.7648 1.7339 -0.3270 0.0982 -0.3124 1916 TYR B CG 6528 C CD1 . TYR B 269 ? 3.1479 1.8162 1.8458 -0.3346 0.1003 -0.3452 1916 TYR B CD1 6529 C CD2 . TYR B 269 ? 3.0014 1.7920 1.6909 -0.3485 0.0644 -0.3155 1916 TYR B CD2 6530 C CE1 . TYR B 269 ? 3.4025 2.0139 2.0345 -0.3635 0.0701 -0.3844 1916 TYR B CE1 6531 C CE2 . TYR B 269 ? 3.3188 2.0591 1.9416 -0.3771 0.0326 -0.3530 1916 TYR B CE2 6532 C CZ . TYR B 269 ? 3.5543 2.2034 2.1475 -0.3854 0.0353 -0.3892 1916 TYR B CZ 6533 O OH . TYR B 269 ? 3.8528 2.4471 2.3777 -0.4161 0.0019 -0.4302 1916 TYR B OH 6534 N N . ARG B 270 ? 2.8276 1.7069 1.6839 -0.1981 0.2296 -0.2221 1917 ARG B N 6535 C CA . ARG B 270 ? 2.7478 1.6985 1.6636 -0.1803 0.2458 -0.1858 1917 ARG B CA 6536 C C . ARG B 270 ? 2.6781 1.6291 1.6645 -0.1747 0.2584 -0.1708 1917 ARG B C 6537 O O . ARG B 270 ? 2.7740 1.6756 1.7516 -0.1564 0.2803 -0.1828 1917 ARG B O 6538 C CB . ARG B 270 ? 2.9246 1.8860 1.8021 -0.1446 0.2790 -0.1836 1917 ARG B CB 6539 C CG . ARG B 270 ? 2.9557 1.8771 1.7343 -0.1407 0.2790 -0.2138 1917 ARG B CG 6540 C CD . ARG B 270 ? 2.8492 1.7982 1.5946 -0.1081 0.3109 -0.2042 1917 ARG B CD 6541 N NE . ARG B 270 ? 2.7398 1.7629 1.5160 -0.1151 0.3000 -0.1708 1917 ARG B NE 6542 C CZ . ARG B 270 ? 2.7381 1.8168 1.5820 -0.1008 0.3174 -0.1368 1917 ARG B CZ 6543 N NH1 . ARG B 270 ? 2.7502 1.8245 1.6360 -0.0782 0.3461 -0.1311 1917 ARG B NH1 6544 N NH2 . ARG B 270 ? 2.7592 1.8973 1.6292 -0.1090 0.3051 -0.1081 1917 ARG B NH2 6545 N N . PHE B 271 ? 2.5665 1.5719 1.6214 -0.1903 0.2435 -0.1449 1918 PHE B N 6546 C CA . PHE B 271 ? 2.5624 1.5732 1.6812 -0.1886 0.2516 -0.1298 1918 PHE B CA 6547 C C . PHE B 271 ? 2.3364 1.4090 1.5067 -0.1667 0.2705 -0.1015 1918 PHE B C 6548 O O . PHE B 271 ? 2.3089 1.4355 1.5009 -0.1725 0.2603 -0.0852 1918 PHE B O 6549 C CB . PHE B 271 ? 2.6209 1.6398 1.7789 -0.2249 0.2215 -0.1248 1918 PHE B CB 6550 C CG . PHE B 271 ? 2.6991 1.6563 1.8118 -0.2519 0.1993 -0.1529 1918 PHE B CG 6551 C CD1 . PHE B 271 ? 2.7070 1.5871 1.7600 -0.2400 0.2127 -0.1818 1918 PHE B CD1 6552 C CD2 . PHE B 271 ? 2.5710 1.5469 1.7033 -0.2893 0.1647 -0.1510 1918 PHE B CD2 6553 C CE1 . PHE B 271 ? 2.6653 1.4843 1.6760 -0.2665 0.1908 -0.2103 1918 PHE B CE1 6554 C CE2 . PHE B 271 ? 2.5628 1.4835 1.6570 -0.3174 0.1418 -0.1771 1918 PHE B CE2 6555 C CZ . PHE B 271 ? 2.6520 1.4919 1.6840 -0.3069 0.1542 -0.2078 1918 PHE B CZ 6556 N N . HIS B 272 ? 2.2879 1.3513 1.4779 -0.1413 0.2970 -0.0958 1919 HIS B N 6557 C CA . HIS B 272 ? 2.2824 1.4019 1.5196 -0.1205 0.3149 -0.0714 1919 HIS B CA 6558 C C . HIS B 272 ? 2.1819 1.3341 1.4859 -0.1295 0.3080 -0.0525 1919 HIS B C 6559 O O . HIS B 272 ? 2.1654 1.3231 1.5006 -0.1125 0.3244 -0.0424 1919 HIS B O 6560 C CB . HIS B 272 ? 2.3377 1.4396 1.5567 -0.0858 0.3475 -0.0745 1919 HIS B CB 6561 C CG . HIS B 272 ? 2.4183 1.5075 1.5763 -0.0744 0.3576 -0.0877 1919 HIS B CG 6562 N ND1 . HIS B 272 ? 2.4153 1.4545 1.5068 -0.0874 0.3450 -0.1144 1919 HIS B ND1 6563 C CD2 . HIS B 272 ? 2.4606 1.5834 1.6127 -0.0531 0.3781 -0.0771 1919 HIS B CD2 6564 C CE1 . HIS B 272 ? 2.5931 1.6357 1.6357 -0.0725 0.3584 -0.1203 1919 HIS B CE1 6565 N NE2 . HIS B 272 ? 2.5315 1.6252 1.6112 -0.0515 0.3798 -0.0964 1919 HIS B NE2 6566 N N . ALA B 273 ? 2.1820 1.3607 1.5071 -0.1559 0.2831 -0.0470 1920 ALA B N 6567 C CA . ALA B 273 ? 2.1348 1.3304 1.5093 -0.1710 0.2730 -0.0358 1920 ALA B CA 6568 C C . ALA B 273 ? 1.9668 1.2268 1.3988 -0.1662 0.2749 -0.0141 1920 ALA B C 6569 O O . ALA B 273 ? 1.8274 1.1259 1.2685 -0.1643 0.2714 -0.0063 1920 ALA B O 6570 C CB . ALA B 273 ? 2.3835 1.5669 1.7505 -0.2038 0.2454 -0.0438 1920 ALA B CB 6571 N N . ILE B 274 ? 1.8616 1.1289 1.3301 -0.1643 0.2804 -0.0046 1921 ILE B N 6572 C CA . ILE B 274 ? 1.8122 1.1335 1.3343 -0.1616 0.2814 0.0124 1921 ILE B CA 6573 C C . ILE B 274 ? 1.8727 1.2057 1.4213 -0.1865 0.2645 0.0168 1921 ILE B C 6574 O O . ILE B 274 ? 1.8168 1.1191 1.3616 -0.1958 0.2636 0.0154 1921 ILE B O 6575 C CB . ILE B 274 ? 1.7580 1.0805 1.2963 -0.1389 0.3012 0.0200 1921 ILE B CB 6576 C CG1 . ILE B 274 ? 1.7424 1.0432 1.2498 -0.1149 0.3195 0.0139 1921 ILE B CG1 6577 C CG2 . ILE B 274 ? 1.5851 0.9635 1.1739 -0.1356 0.3015 0.0343 1921 ILE B CG2 6578 C CD1 . ILE B 274 ? 1.7339 1.0355 1.2565 -0.0906 0.3384 0.0219 1921 ILE B CD1 6579 N N . ASN B 275 ? 2.0095 1.3874 1.5872 -0.1969 0.2519 0.0239 1922 ASN B N 6580 C CA . ASN B 275 ? 2.1015 1.4962 1.7042 -0.2214 0.2346 0.0280 1922 ASN B CA 6581 C C . ASN B 275 ? 2.1351 1.4807 1.7043 -0.2412 0.2232 0.0164 1922 ASN B C 6582 O O . ASN B 275 ? 2.1747 1.5122 1.7600 -0.2586 0.2178 0.0200 1922 ASN B O 6583 C CB . ASN B 275 ? 2.0821 1.5071 1.7283 -0.2200 0.2419 0.0404 1922 ASN B CB 6584 C CG . ASN B 275 ? 1.9757 1.4459 1.6526 -0.2023 0.2506 0.0476 1922 ASN B CG 6585 O OD1 . ASN B 275 ? 2.0041 1.4773 1.6864 -0.1854 0.2651 0.0506 1922 ASN B OD1 6586 N ND2 . ASN B 275 ? 1.7287 1.2329 1.4264 -0.2061 0.2407 0.0504 1922 ASN B ND2 6587 N N . GLY B 276 ? 2.0272 1.3393 1.5483 -0.2381 0.2207 0.0021 1923 GLY B N 6588 C CA . GLY B 276 ? 2.0780 1.3360 1.5566 -0.2550 0.2094 -0.0148 1923 GLY B CA 6589 C C . GLY B 276 ? 2.1128 1.3118 1.5712 -0.2514 0.2216 -0.0229 1923 GLY B C 6590 O O . GLY B 276 ? 2.2629 1.4245 1.7086 -0.2744 0.2083 -0.0320 1923 GLY B O 6591 N N . TYR B 277 ? 2.0814 1.2700 1.5381 -0.2237 0.2455 -0.0193 1924 TYR B N 6592 C CA . TYR B 277 ? 2.1583 1.2866 1.5955 -0.2170 0.2576 -0.0254 1924 TYR B CA 6593 C C . TYR B 277 ? 2.1406 1.2339 1.5402 -0.1863 0.2790 -0.0360 1924 TYR B C 6594 O O . TYR B 277 ? 2.0203 1.1398 1.4387 -0.1604 0.2973 -0.0242 1924 TYR B O 6595 C CB . TYR B 277 ? 2.2608 1.4063 1.7417 -0.2145 0.2661 -0.0048 1924 TYR B CB 6596 C CG . TYR B 277 ? 2.3884 1.5399 1.8975 -0.2457 0.2506 0.0039 1924 TYR B CG 6597 C CD1 . TYR B 277 ? 2.6120 1.7143 2.0998 -0.2724 0.2351 -0.0089 1924 TYR B CD1 6598 C CD2 . TYR B 277 ? 2.3292 1.5359 1.8868 -0.2488 0.2521 0.0249 1924 TYR B CD2 6599 C CE1 . TYR B 277 ? 2.6902 1.8032 2.2107 -0.3028 0.2215 0.0022 1924 TYR B CE1 6600 C CE2 . TYR B 277 ? 2.3237 1.5416 1.9101 -0.2760 0.2412 0.0356 1924 TYR B CE2 6601 C CZ . TYR B 277 ? 2.3807 1.5540 1.9518 -0.3036 0.2260 0.0259 1924 TYR B CZ 6602 O OH . TYR B 277 ? 2.2122 1.4019 1.8181 -0.3323 0.2159 0.0392 1924 TYR B OH 6603 N N . ILE B 278 ? 2.2640 1.2976 1.6108 -0.1893 0.2767 -0.0592 1925 ILE B N 6604 C CA . ILE B 278 ? 2.4012 1.4019 1.7064 -0.1591 0.2983 -0.0724 1925 ILE B CA 6605 C C . ILE B 278 ? 2.2969 1.2504 1.6037 -0.1389 0.3180 -0.0706 1925 ILE B C 6606 O O . ILE B 278 ? 2.3090 1.2377 1.6337 -0.1543 0.3110 -0.0647 1925 ILE B O 6607 C CB . ILE B 278 ? 2.6199 1.5809 1.8612 -0.1684 0.2883 -0.1002 1925 ILE B CB 6608 C CG1 . ILE B 278 ? 2.9352 1.8696 2.1308 -0.1345 0.3142 -0.1139 1925 ILE B CG1 6609 C CG2 . ILE B 278 ? 2.6088 1.5104 1.8294 -0.1978 0.2688 -0.1177 1925 ILE B CG2 6610 C CD1 . ILE B 278 ? 3.2636 2.1615 2.3876 -0.1398 0.3073 -0.1424 1925 ILE B CD1 6611 N N . MET B 279 ? 2.2826 1.2270 1.5740 -0.1041 0.3430 -0.0728 1926 MET B N 6612 C CA . MET B 279 ? 2.3645 1.2904 1.6755 -0.0774 0.3639 -0.0607 1926 MET B CA 6613 C C . MET B 279 ? 2.4261 1.4009 1.7959 -0.0850 0.3578 -0.0325 1926 MET B C 6614 O O . MET B 279 ? 2.6423 1.6825 2.0415 -0.0930 0.3497 -0.0208 1926 MET B O 6615 C CB . MET B 279 ? 2.4898 1.3272 1.7657 -0.0751 0.3688 -0.0784 1926 MET B CB 6616 C CG . MET B 279 ? 2.7644 1.5514 1.9776 -0.0592 0.3807 -0.1087 1926 MET B CG 6617 S SD . MET B 279 ? 3.1107 1.9147 2.3203 -0.0071 0.4179 -0.1043 1926 MET B SD 6618 C CE . MET B 279 ? 3.0650 1.7751 2.1947 0.0091 0.4329 -0.1447 1926 MET B CE 6619 N N . ASP B 280 ? 2.3492 1.2935 1.7350 -0.0831 0.3614 -0.0210 1927 ASP B N 6620 C CA . ASP B 280 ? 2.3078 1.3062 1.7449 -0.0851 0.3589 0.0071 1927 ASP B CA 6621 C C . ASP B 280 ? 2.2786 1.2993 1.7409 -0.1197 0.3390 0.0171 1927 ASP B C 6622 O O . ASP B 280 ? 2.1559 1.2227 1.6558 -0.1197 0.3388 0.0390 1927 ASP B O 6623 C CB . ASP B 280 ? 2.3752 1.3595 1.8277 -0.0565 0.3764 0.0246 1927 ASP B CB 6624 C CG . ASP B 280 ? 2.4554 1.4702 1.9129 -0.0214 0.3947 0.0273 1927 ASP B CG 6625 O OD1 . ASP B 280 ? 2.7017 1.6963 2.1262 -0.0118 0.4027 0.0072 1927 ASP B OD1 6626 O OD2 . ASP B 280 ? 2.2946 1.3557 1.7878 -0.0044 0.4007 0.0492 1927 ASP B OD2 6627 N N . THR B 281 ? 2.4851 1.4772 1.9265 -0.1486 0.3224 0.0006 1928 THR B N 6628 C CA . THR B 281 ? 2.6876 1.6928 2.1534 -0.1838 0.3039 0.0094 1928 THR B CA 6629 C C . THR B 281 ? 2.4570 1.5435 1.9715 -0.1912 0.2989 0.0314 1928 THR B C 6630 O O . THR B 281 ? 2.2715 1.3678 1.8131 -0.2066 0.2956 0.0487 1928 THR B O 6631 C CB . THR B 281 ? 2.8911 1.8605 2.3278 -0.2154 0.2830 -0.0137 1928 THR B CB 6632 O OG1 . THR B 281 ? 2.8847 1.8673 2.2916 -0.2088 0.2795 -0.0322 1928 THR B OG1 6633 C CG2 . THR B 281 ? 2.6232 1.5011 2.0272 -0.2230 0.2831 -0.0287 1928 THR B CG2 6634 N N . LEU B 282 ? 2.2528 1.3951 1.7783 -0.1800 0.2998 0.0312 1929 LEU B N 6635 C CA . LEU B 282 ? 2.1645 1.3756 1.7319 -0.1888 0.2937 0.0463 1929 LEU B CA 6636 C C . LEU B 282 ? 2.0325 1.2598 1.6261 -0.1824 0.3028 0.0680 1929 LEU B C 6637 O O . LEU B 282 ? 1.9612 1.1972 1.5575 -0.1569 0.3159 0.0757 1929 LEU B O 6638 C CB . LEU B 282 ? 2.3680 1.6310 1.9460 -0.1742 0.2956 0.0441 1929 LEU B CB 6639 C CG . LEU B 282 ? 2.4008 1.7283 2.0195 -0.1845 0.2879 0.0545 1929 LEU B CG 6640 C CD1 . LEU B 282 ? 2.1838 1.5444 1.8070 -0.1860 0.2796 0.0469 1929 LEU B CD1 6641 C CD2 . LEU B 282 ? 2.4134 1.7763 2.0580 -0.1679 0.2992 0.0696 1929 LEU B CD2 6642 N N . PRO B 283 ? 2.0527 1.2922 1.6681 -0.2060 0.2953 0.0795 1930 PRO B N 6643 C CA . PRO B 283 ? 2.1961 1.4294 1.8254 -0.2071 0.3028 0.1007 1930 PRO B CA 6644 C C . PRO B 283 ? 2.1582 1.4554 1.8159 -0.1964 0.3095 0.1182 1930 PRO B C 6645 O O . PRO B 283 ? 2.3696 1.6630 2.0308 -0.1870 0.3190 0.1372 1930 PRO B O 6646 C CB . PRO B 283 ? 2.3714 1.5954 2.0126 -0.2421 0.2903 0.1036 1930 PRO B CB 6647 C CG . PRO B 283 ? 2.2248 1.5016 1.8829 -0.2528 0.2785 0.0946 1930 PRO B CG 6648 C CD . PRO B 283 ? 2.1335 1.4066 1.7679 -0.2321 0.2796 0.0764 1930 PRO B CD 6649 N N . GLY B 284 ? 1.9014 1.2541 1.5773 -0.1976 0.3043 0.1122 1931 GLY B N 6650 C CA . GLY B 284 ? 1.8594 1.2715 1.5627 -0.1956 0.3081 0.1255 1931 GLY B CA 6651 C C . GLY B 284 ? 1.7947 1.2523 1.5066 -0.1722 0.3138 0.1247 1931 GLY B C 6652 O O . GLY B 284 ? 1.8892 1.3941 1.6214 -0.1748 0.3106 0.1203 1931 GLY B O 6653 N N . LEU B 285 ? 1.6862 1.1320 1.3860 -0.1498 0.3216 0.1296 1932 LEU B N 6654 C CA . LEU B 285 ? 1.6482 1.1393 1.3588 -0.1306 0.3239 0.1279 1932 LEU B CA 6655 C C . LEU B 285 ? 1.6983 1.2128 1.4111 -0.1180 0.3299 0.1460 1932 LEU B C 6656 O O . LEU B 285 ? 1.7511 1.2632 1.4583 -0.0976 0.3336 0.1516 1932 LEU B O 6657 C CB . LEU B 285 ? 1.6398 1.1180 1.3421 -0.1143 0.3251 0.1156 1932 LEU B CB 6658 C CG . LEU B 285 ? 1.6617 1.1241 1.3578 -0.1256 0.3188 0.0987 1932 LEU B CG 6659 C CD1 . LEU B 285 ? 1.8065 1.2527 1.4896 -0.1090 0.3236 0.0895 1932 LEU B CD1 6660 C CD2 . LEU B 285 ? 1.5411 1.0478 1.2603 -0.1370 0.3108 0.0924 1932 LEU B CD2 6661 N N . VAL B 286 ? 1.7310 1.2720 1.4524 -0.1301 0.3307 0.1562 1933 VAL B N 6662 C CA . VAL B 286 ? 1.8899 1.4589 1.6091 -0.1207 0.3360 0.1746 1933 VAL B CA 6663 C C . VAL B 286 ? 1.9254 1.5521 1.6553 -0.1131 0.3331 0.1634 1933 VAL B C 6664 O O . VAL B 286 ? 2.0028 1.6563 1.7468 -0.1245 0.3314 0.1522 1933 VAL B O 6665 C CB . VAL B 286 ? 2.0921 1.6581 1.8121 -0.1381 0.3415 0.1946 1933 VAL B CB 6666 C CG1 . VAL B 286 ? 2.0389 1.6624 1.7724 -0.1458 0.3440 0.1939 1933 VAL B CG1 6667 C CG2 . VAL B 286 ? 2.0059 1.5468 1.7110 -0.1285 0.3482 0.2213 1933 VAL B CG2 6668 N N . MET B 287 ? 1.8425 1.4877 1.5675 -0.0939 0.3318 0.1664 1934 MET B N 6669 C CA . MET B 287 ? 1.7475 1.4422 1.4812 -0.0865 0.3264 0.1524 1934 MET B CA 6670 C C . MET B 287 ? 1.7742 1.4954 1.4987 -0.0690 0.3236 0.1634 1934 MET B C 6671 O O . MET B 287 ? 1.7370 1.4372 1.4550 -0.0562 0.3244 0.1783 1934 MET B O 6672 C CB . MET B 287 ? 1.7341 1.4254 1.4825 -0.0849 0.3207 0.1315 1934 MET B CB 6673 C CG . MET B 287 ? 1.8600 1.5066 1.6024 -0.0790 0.3229 0.1351 1934 MET B CG 6674 S SD . MET B 287 ? 1.9044 1.5541 1.6622 -0.0745 0.3187 0.1156 1934 MET B SD 6675 C CE . MET B 287 ? 1.6803 1.3803 1.4522 -0.0605 0.3124 0.1137 1934 MET B CE 6676 N N . ALA B 288 ? 1.7537 1.5212 1.4774 -0.0676 0.3197 0.1549 1935 ALA B N 6677 C CA . ALA B 288 ? 1.8167 1.6174 1.5268 -0.0538 0.3145 0.1651 1935 ALA B CA 6678 C C . ALA B 288 ? 1.7636 1.5809 1.4860 -0.0414 0.3028 0.1551 1935 ALA B C 6679 O O . ALA B 288 ? 1.9399 1.7544 1.6819 -0.0452 0.2992 0.1350 1935 ALA B O 6680 C CB . ALA B 288 ? 1.8082 1.6510 1.5068 -0.0581 0.3153 0.1576 1935 ALA B CB 6681 N N . GLN B 289 ? 1.6429 1.4810 1.3561 -0.0273 0.2964 0.1708 1936 GLN B N 6682 C CA . GLN B 289 ? 1.7141 1.5751 1.4449 -0.0172 0.2840 0.1626 1936 GLN B CA 6683 C C . GLN B 289 ? 1.8718 1.7801 1.6050 -0.0215 0.2704 0.1391 1936 GLN B C 6684 O O . GLN B 289 ? 1.8434 1.7795 1.5912 -0.0156 0.2567 0.1331 1936 GLN B O 6685 C CB . GLN B 289 ? 1.7657 1.6266 1.4944 0.0014 0.2815 0.1900 1936 GLN B CB 6686 C CG . GLN B 289 ? 1.9630 1.8695 1.6750 0.0105 0.2695 0.2032 1936 GLN B CG 6687 C CD . GLN B 289 ? 2.0445 1.9623 1.7696 0.0306 0.2619 0.2248 1936 GLN B CD 6688 O OE1 . GLN B 289 ? 2.0971 2.0197 1.8517 0.0357 0.2576 0.2162 1936 GLN B OE1 6689 N NE2 . GLN B 289 ? 2.1347 2.0581 1.8403 0.0431 0.2613 0.2556 1936 GLN B NE2 6690 N N . ASP B 290 ? 2.1466 2.0638 1.8673 -0.0323 0.2743 0.1246 1937 ASP B N 6691 C CA . ASP B 290 ? 2.2963 2.2457 2.0207 -0.0374 0.2638 0.0956 1937 ASP B CA 6692 C C . ASP B 290 ? 2.1668 2.0933 1.9149 -0.0486 0.2696 0.0745 1937 ASP B C 6693 O O . ASP B 290 ? 1.9479 1.8665 1.7229 -0.0501 0.2640 0.0649 1937 ASP B O 6694 C CB . ASP B 290 ? 2.7788 2.7576 2.4705 -0.0381 0.2655 0.0918 1937 ASP B CB 6695 C CG . ASP B 290 ? 3.2716 3.2492 2.9349 -0.0318 0.2745 0.1254 1937 ASP B CG 6696 O OD1 . ASP B 290 ? 3.5508 3.5197 3.2147 -0.0219 0.2712 0.1509 1937 ASP B OD1 6697 O OD2 . ASP B 290 ? 3.4924 3.4783 3.1345 -0.0361 0.2861 0.1278 1937 ASP B OD2 6698 N N . GLN B 291 ? 2.0527 1.9702 1.7923 -0.0561 0.2817 0.0716 1938 GLN B N 6699 C CA . GLN B 291 ? 1.8021 1.7060 1.5626 -0.0657 0.2864 0.0518 1938 GLN B CA 6700 C C . GLN B 291 ? 1.6651 1.5449 1.4536 -0.0680 0.2822 0.0478 1938 GLN B C 6701 O O . GLN B 291 ? 1.5397 1.3948 1.3292 -0.0654 0.2856 0.0650 1938 GLN B O 6702 C CB . GLN B 291 ? 1.7269 1.6177 1.4813 -0.0729 0.3011 0.0618 1938 GLN B CB 6703 C CG . GLN B 291 ? 2.1036 2.0156 1.8282 -0.0698 0.3087 0.0776 1938 GLN B CG 6704 C CD . GLN B 291 ? 2.3737 2.2959 2.0975 -0.0769 0.3227 0.0753 1938 GLN B CD 6705 O OE1 . GLN B 291 ? 2.6412 2.5623 2.3868 -0.0817 0.3245 0.0564 1938 GLN B OE1 6706 N NE2 . GLN B 291 ? 2.2421 2.1770 1.9432 -0.0768 0.3334 0.0971 1938 GLN B NE2 6707 N N . ARG B 292 ? 1.6461 1.5332 1.4561 -0.0717 0.2753 0.0249 1939 ARG B N 6708 C CA . ARG B 292 ? 1.5802 1.4466 1.4172 -0.0751 0.2735 0.0221 1939 ARG B CA 6709 C C . ARG B 292 ? 1.4976 1.3359 1.3366 -0.0815 0.2836 0.0279 1939 ARG B C 6710 O O . ARG B 292 ? 1.4644 1.3054 1.2958 -0.0856 0.2901 0.0263 1939 ARG B O 6711 C CB . ARG B 292 ? 1.7754 1.6537 1.6382 -0.0793 0.2636 -0.0015 1939 ARG B CB 6712 C CG . ARG B 292 ? 1.9760 1.8634 1.8411 -0.0830 0.2637 -0.0251 1939 ARG B CG 6713 C CD . ARG B 292 ? 2.1178 2.0145 2.0061 -0.0866 0.2511 -0.0487 1939 ARG B CD 6714 N NE . ARG B 292 ? 2.4955 2.3845 2.4107 -0.0897 0.2449 -0.0406 1939 ARG B NE 6715 C CZ . ARG B 292 ? 2.6313 2.5396 2.5548 -0.0891 0.2333 -0.0386 1939 ARG B CZ 6716 N NH1 . ARG B 292 ? 2.7003 2.6367 2.6048 -0.0861 0.2232 -0.0452 1939 ARG B NH1 6717 N NH2 . ARG B 292 ? 2.4978 2.4009 2.4496 -0.0915 0.2317 -0.0286 1939 ARG B NH2 6718 N N . ILE B 293 ? 1.4721 1.2857 1.3203 -0.0823 0.2852 0.0358 1940 ILE B N 6719 C CA . ILE B 293 ? 1.4752 1.2619 1.3231 -0.0895 0.2915 0.0406 1940 ILE B CA 6720 C C . ILE B 293 ? 1.5459 1.3256 1.4176 -0.0933 0.2881 0.0311 1940 ILE B C 6721 O O . ILE B 293 ? 1.5748 1.3577 1.4593 -0.0895 0.2846 0.0302 1940 ILE B O 6722 C CB . ILE B 293 ? 1.4289 1.1865 1.2591 -0.0867 0.2970 0.0583 1940 ILE B CB 6723 C CG1 . ILE B 293 ? 1.4547 1.2144 1.2628 -0.0838 0.3010 0.0719 1940 ILE B CG1 6724 C CG2 . ILE B 293 ? 1.4221 1.1501 1.2509 -0.0960 0.2998 0.0597 1940 ILE B CG2 6725 C CD1 . ILE B 293 ? 1.4010 1.1813 1.2032 -0.0713 0.2974 0.0785 1940 ILE B CD1 6726 N N . ARG B 294 ? 1.5843 1.3578 1.4651 -0.1007 0.2891 0.0263 1941 ARG B N 6727 C CA . ARG B 294 ? 1.5582 1.3179 1.4563 -0.1044 0.2868 0.0249 1941 ARG B CA 6728 C C . ARG B 294 ? 1.6062 1.3393 1.4880 -0.1098 0.2898 0.0367 1941 ARG B C 6729 O O . ARG B 294 ? 1.5771 1.3065 1.4482 -0.1156 0.2917 0.0409 1941 ARG B O 6730 C CB . ARG B 294 ? 1.4186 1.1900 1.3426 -0.1070 0.2833 0.0115 1941 ARG B CB 6731 C CG . ARG B 294 ? 1.4836 1.2565 1.4091 -0.1118 0.2859 0.0125 1941 ARG B CG 6732 C CD . ARG B 294 ? 1.5333 1.3114 1.4889 -0.1117 0.2830 0.0029 1941 ARG B CD 6733 N NE . ARG B 294 ? 1.5068 1.3061 1.4709 -0.1078 0.2868 -0.0101 1941 ARG B NE 6734 C CZ . ARG B 294 ? 1.6293 1.4420 1.5939 -0.1020 0.2866 -0.0268 1941 ARG B CZ 6735 N NH1 . ARG B 294 ? 1.6429 1.4525 1.6049 -0.1013 0.2806 -0.0307 1941 ARG B NH1 6736 N NH2 . ARG B 294 ? 1.6662 1.4973 1.6338 -0.0969 0.2922 -0.0401 1941 ARG B NH2 6737 N N . TRP B 295 ? 1.5955 1.3107 1.4741 -0.1084 0.2905 0.0421 1942 TRP B N 6738 C CA . TRP B 295 ? 1.5524 1.2396 1.4100 -0.1132 0.2920 0.0497 1942 TRP B CA 6739 C C . TRP B 295 ? 1.6771 1.3614 1.5473 -0.1179 0.2876 0.0494 1942 TRP B C 6740 O O . TRP B 295 ? 1.7660 1.4578 1.6537 -0.1139 0.2877 0.0488 1942 TRP B O 6741 C CB . TRP B 295 ? 1.4929 1.1604 1.3306 -0.1051 0.2984 0.0562 1942 TRP B CB 6742 C CG . TRP B 295 ? 1.6022 1.2714 1.4299 -0.0963 0.3029 0.0605 1942 TRP B CG 6743 C CD1 . TRP B 295 ? 1.6630 1.3571 1.5049 -0.0873 0.3026 0.0603 1942 TRP B CD1 6744 C CD2 . TRP B 295 ? 1.6011 1.2442 1.4026 -0.0950 0.3076 0.0676 1942 TRP B CD2 6745 N NE1 . TRP B 295 ? 1.5167 1.2052 1.3426 -0.0788 0.3067 0.0688 1942 TRP B NE1 6746 C CE2 . TRP B 295 ? 1.5311 1.1857 1.3325 -0.0829 0.3108 0.0738 1942 TRP B CE2 6747 C CE3 . TRP B 295 ? 1.7228 1.3326 1.5016 -0.1037 0.3080 0.0693 1942 TRP B CE3 6748 C CZ2 . TRP B 295 ? 1.6356 1.2678 1.4164 -0.0776 0.3160 0.0838 1942 TRP B CZ2 6749 C CZ3 . TRP B 295 ? 1.9318 1.5160 1.6900 -0.1005 0.3130 0.0766 1942 TRP B CZ3 6750 C CH2 . TRP B 295 ? 1.9662 1.5607 1.7260 -0.0866 0.3179 0.0849 1942 TRP B CH2 6751 N N . TYR B 296 ? 1.6933 1.3674 1.5556 -0.1273 0.2831 0.0518 1943 TYR B N 6752 C CA . TYR B 296 ? 1.5938 1.2667 1.4655 -0.1324 0.2765 0.0546 1943 TYR B CA 6753 C C . TYR B 296 ? 1.5752 1.2202 1.4140 -0.1340 0.2772 0.0601 1943 TYR B C 6754 O O . TYR B 296 ? 1.6763 1.3019 1.4896 -0.1408 0.2753 0.0601 1943 TYR B O 6755 C CB . TYR B 296 ? 1.5144 1.1997 1.3998 -0.1415 0.2695 0.0544 1943 TYR B CB 6756 C CG . TYR B 296 ? 1.6112 1.3243 1.5264 -0.1374 0.2717 0.0469 1943 TYR B CG 6757 C CD1 . TYR B 296 ? 1.6542 1.3790 1.5952 -0.1297 0.2721 0.0404 1943 TYR B CD1 6758 C CD2 . TYR B 296 ? 1.6130 1.3398 1.5302 -0.1415 0.2741 0.0458 1943 TYR B CD2 6759 C CE1 . TYR B 296 ? 1.6077 1.3538 1.5715 -0.1250 0.2743 0.0294 1943 TYR B CE1 6760 C CE2 . TYR B 296 ? 1.6240 1.3772 1.5634 -0.1358 0.2784 0.0373 1943 TYR B CE2 6761 C CZ . TYR B 296 ? 1.6339 1.3952 1.5947 -0.1269 0.2782 0.0272 1943 TYR B CZ 6762 O OH . TYR B 296 ? 1.4866 1.2698 1.4650 -0.1203 0.2827 0.0146 1943 TYR B OH 6763 N N . LEU B 297 ? 1.5410 1.1832 1.3796 -0.1280 0.2806 0.0644 1944 LEU B N 6764 C CA . LEU B 297 ? 1.5806 1.1977 1.3831 -0.1259 0.2851 0.0682 1944 LEU B CA 6765 C C . LEU B 297 ? 1.6929 1.3060 1.4863 -0.1317 0.2776 0.0748 1944 LEU B C 6766 O O . LEU B 297 ? 1.8848 1.5150 1.7056 -0.1308 0.2750 0.0817 1944 LEU B O 6767 C CB . LEU B 297 ? 1.5209 1.1399 1.3247 -0.1130 0.2981 0.0711 1944 LEU B CB 6768 C CG . LEU B 297 ? 1.6358 1.2587 1.4436 -0.1061 0.3036 0.0668 1944 LEU B CG 6769 C CD1 . LEU B 297 ? 1.6326 1.2732 1.4607 -0.0948 0.3124 0.0708 1944 LEU B CD1 6770 C CD2 . LEU B 297 ? 1.7824 1.3736 1.5521 -0.1046 0.3079 0.0646 1944 LEU B CD2 6771 N N . LEU B 298 ? 1.7001 1.2893 1.4541 -0.1379 0.2733 0.0731 1945 LEU B N 6772 C CA . LEU B 298 ? 1.7672 1.3543 1.5057 -0.1438 0.2636 0.0800 1945 LEU B CA 6773 C C . LEU B 298 ? 1.9077 1.4649 1.5913 -0.1421 0.2679 0.0772 1945 LEU B C 6774 O O . LEU B 298 ? 2.0832 1.6134 1.7370 -0.1435 0.2707 0.0662 1945 LEU B O 6775 C CB . LEU B 298 ? 1.6936 1.2904 1.4440 -0.1582 0.2455 0.0800 1945 LEU B CB 6776 C CG . LEU B 298 ? 1.6711 1.2704 1.4068 -0.1650 0.2312 0.0890 1945 LEU B CG 6777 C CD1 . LEU B 298 ? 1.6398 1.2583 1.4026 -0.1561 0.2343 0.1035 1945 LEU B CD1 6778 C CD2 . LEU B 298 ? 1.6150 1.2267 1.3636 -0.1802 0.2117 0.0893 1945 LEU B CD2 6779 N N . SER B 299 ? 1.8850 1.4457 1.5543 -0.1387 0.2690 0.0872 1946 SER B N 6780 C CA . SER B 299 ? 2.0059 1.5407 1.6160 -0.1389 0.2696 0.0837 1946 SER B CA 6781 C C . SER B 299 ? 1.9850 1.5263 1.5810 -0.1519 0.2482 0.0901 1946 SER B C 6782 O O . SER B 299 ? 1.8484 1.4161 1.4865 -0.1577 0.2358 0.1002 1946 SER B O 6783 C CB . SER B 299 ? 2.1244 1.6588 1.7185 -0.1232 0.2903 0.0914 1946 SER B CB 6784 O OG . SER B 299 ? 2.4271 1.9364 1.9587 -0.1218 0.2925 0.0858 1946 SER B OG 6785 N N . MET B 300 ? 2.0581 1.5766 1.5955 -0.1555 0.2433 0.0842 1947 MET B N 6786 C CA . MET B 300 ? 2.2609 1.7880 1.7837 -0.1700 0.2183 0.0896 1947 MET B CA 6787 C C . MET B 300 ? 2.4093 1.9153 1.8604 -0.1729 0.2120 0.0846 1947 MET B C 6788 O O . MET B 300 ? 2.4185 1.8902 1.8231 -0.1800 0.2078 0.0635 1947 MET B O 6789 C CB . MET B 300 ? 2.3493 1.8785 1.8954 -0.1872 0.1991 0.0805 1947 MET B CB 6790 C CG . MET B 300 ? 2.4279 1.9880 2.0002 -0.1999 0.1737 0.0936 1947 MET B CG 6791 S SD . MET B 300 ? 2.2198 1.8227 1.8741 -0.1923 0.1757 0.1120 1947 MET B SD 6792 C CE . MET B 300 ? 2.4180 2.0342 2.0641 -0.1813 0.1768 0.1357 1947 MET B CE 6793 N N . GLY B 301 ? 2.4660 1.9916 1.9078 -0.1679 0.2104 0.1042 1948 GLY B N 6794 C CA . GLY B 301 ? 2.5594 2.0752 1.9345 -0.1726 0.1985 0.1037 1948 GLY B CA 6795 C C . GLY B 301 ? 2.6105 2.1123 1.9307 -0.1565 0.2222 0.1053 1948 GLY B C 6796 O O . GLY B 301 ? 2.6080 2.1310 1.9504 -0.1435 0.2396 0.1274 1948 GLY B O 6797 N N . SER B 302 ? 2.7319 2.1973 1.9808 -0.1577 0.2232 0.0814 1949 SER B N 6798 C CA . SER B 302 ? 2.6831 2.1316 1.8654 -0.1417 0.2459 0.0780 1949 SER B CA 6799 C C . SER B 302 ? 2.4480 1.9131 1.6638 -0.1206 0.2800 0.0949 1949 SER B C 6800 O O . SER B 302 ? 2.2548 1.7183 1.5186 -0.1147 0.2932 0.0902 1949 SER B O 6801 C CB . SER B 302 ? 2.9259 2.3226 2.0453 -0.1412 0.2510 0.0420 1949 SER B CB 6802 O OG . SER B 302 ? 3.0806 2.4585 2.1543 -0.1622 0.2192 0.0245 1949 SER B OG 6803 N N . ASN B 303 ? 2.3826 1.8654 1.5725 -0.1100 0.2938 0.1156 1950 ASN B N 6804 C CA . ASN B 303 ? 2.4105 1.9175 1.6413 -0.0934 0.3240 0.1380 1950 ASN B CA 6805 C C . ASN B 303 ? 2.3863 1.8746 1.6110 -0.0753 0.3557 0.1216 1950 ASN B C 6806 O O . ASN B 303 ? 2.1849 1.6950 1.4422 -0.0612 0.3822 0.1389 1950 ASN B O 6807 C CB . ASN B 303 ? 2.5569 2.0883 1.7611 -0.0879 0.3313 0.1677 1950 ASN B CB 6808 C CG . ASN B 303 ? 2.7394 2.2970 1.9758 -0.1022 0.3027 0.1929 1950 ASN B CG 6809 O OD1 . ASN B 303 ? 2.8294 2.3952 2.1284 -0.1124 0.2850 0.1929 1950 ASN B OD1 6810 N ND2 . ASN B 303 ? 2.7567 2.3286 1.9502 -0.1014 0.2987 0.2155 1950 ASN B ND2 6811 N N . GLU B 304 ? 2.4868 1.9348 1.6738 -0.0766 0.3514 0.0892 1951 GLU B N 6812 C CA . GLU B 304 ? 2.5267 1.9506 1.7103 -0.0593 0.3774 0.0712 1951 GLU B CA 6813 C C . GLU B 304 ? 2.4356 1.8650 1.6907 -0.0639 0.3717 0.0694 1951 GLU B C 6814 O O . GLU B 304 ? 2.4811 1.9133 1.7653 -0.0483 0.3940 0.0695 1951 GLU B O 6815 C CB . GLU B 304 ? 2.6286 1.9990 1.7352 -0.0583 0.3751 0.0365 1951 GLU B CB 6816 C CG . GLU B 304 ? 2.7526 2.0972 1.8539 -0.0830 0.3400 0.0171 1951 GLU B CG 6817 C CD . GLU B 304 ? 2.9400 2.2245 1.9750 -0.0825 0.3397 -0.0193 1951 GLU B CD 6818 O OE1 . GLU B 304 ? 2.9233 2.1838 1.9192 -0.0595 0.3692 -0.0314 1951 GLU B OE1 6819 O OE2 . GLU B 304 ? 3.0137 2.2746 2.0385 -0.1053 0.3103 -0.0359 1951 GLU B OE2 6820 N N . ASN B 305 ? 2.3945 1.8280 1.6762 -0.0850 0.3416 0.0686 1952 ASN B N 6821 C CA . ASN B 305 ? 2.3436 1.7807 1.6846 -0.0921 0.3328 0.0647 1952 ASN B CA 6822 C C . ASN B 305 ? 2.1945 1.6659 1.6038 -0.0819 0.3485 0.0826 1952 ASN B C 6823 O O . ASN B 305 ? 2.2797 1.7689 1.7436 -0.0909 0.3362 0.0869 1952 ASN B O 6824 C CB . ASN B 305 ? 2.3432 1.7906 1.7047 -0.1153 0.2999 0.0667 1952 ASN B CB 6825 C CG . ASN B 305 ? 2.4068 1.8172 1.7349 -0.1299 0.2819 0.0423 1952 ASN B CG 6826 O OD1 . ASN B 305 ? 2.4034 1.7732 1.6807 -0.1238 0.2916 0.0218 1952 ASN B OD1 6827 N ND2 . ASN B 305 ? 2.4189 1.8428 1.7786 -0.1494 0.2561 0.0444 1952 ASN B ND2 6828 N N . ILE B 306 ? 2.0452 1.5274 1.4520 -0.0636 0.3755 0.0921 1953 ILE B N 6829 C CA . ILE B 306 ? 2.0031 1.5217 1.4763 -0.0570 0.3877 0.1106 1953 ILE B CA 6830 C C . ILE B 306 ? 1.9802 1.4933 1.4809 -0.0462 0.3989 0.0999 1953 ILE B C 6831 O O . ILE B 306 ? 1.9753 1.5063 1.4986 -0.0305 0.4209 0.1085 1953 ILE B O 6832 C CB . ILE B 306 ? 2.1424 1.6883 1.6158 -0.0479 0.4072 0.1348 1953 ILE B CB 6833 C CG1 . ILE B 306 ? 2.2101 1.7930 1.7556 -0.0426 0.4207 0.1528 1953 ILE B CG1 6834 C CG2 . ILE B 306 ? 2.0757 1.6010 1.4771 -0.0328 0.4280 0.1278 1953 ILE B CG2 6835 C CD1 . ILE B 306 ? 2.1826 1.7966 1.7458 -0.0413 0.4338 0.1821 1953 ILE B CD1 6836 N N . HIS B 307 ? 2.0167 1.5086 1.5190 -0.0558 0.3821 0.0838 1954 HIS B N 6837 C CA . HIS B 307 ? 1.9604 1.4412 1.4817 -0.0476 0.3879 0.0738 1954 HIS B CA 6838 C C . HIS B 307 ? 1.7982 1.3170 1.3842 -0.0410 0.3949 0.0866 1954 HIS B C 6839 O O . HIS B 307 ? 1.6595 1.2005 1.2885 -0.0533 0.3797 0.0913 1954 HIS B O 6840 C CB . HIS B 307 ? 1.9285 1.3834 1.4416 -0.0638 0.3662 0.0590 1954 HIS B CB 6841 C CG . HIS B 307 ? 2.0439 1.4584 1.4944 -0.0717 0.3577 0.0432 1954 HIS B CG 6842 N ND1 . HIS B 307 ? 2.2112 1.5792 1.6203 -0.0650 0.3646 0.0247 1954 HIS B ND1 6843 C CD2 . HIS B 307 ? 2.0234 1.4363 1.4442 -0.0856 0.3421 0.0430 1954 HIS B CD2 6844 C CE1 . HIS B 307 ? 2.1573 1.4951 1.5132 -0.0768 0.3523 0.0109 1954 HIS B CE1 6845 N NE2 . HIS B 307 ? 2.0389 1.4060 1.4000 -0.0891 0.3380 0.0224 1954 HIS B NE2 6846 N N . SER B 308 ? 1.8057 1.3320 1.3971 -0.0209 0.4179 0.0912 1955 SER B N 6847 C CA . SER B 308 ? 1.7947 1.3580 1.4450 -0.0136 0.4241 0.1025 1955 SER B CA 6848 C C . SER B 308 ? 1.7406 1.2934 1.4045 -0.0107 0.4173 0.0932 1955 SER B C 6849 O O . SER B 308 ? 1.7716 1.3038 1.4175 0.0065 0.4306 0.0881 1955 SER B O 6850 C CB . SER B 308 ? 1.8955 1.4782 1.5513 0.0071 0.4518 0.1145 1955 SER B CB 6851 O OG . SER B 308 ? 1.9288 1.5314 1.5836 0.0037 0.4598 0.1294 1955 SER B OG 6852 N N . ILE B 309 ? 1.6564 1.2240 1.3524 -0.0261 0.3977 0.0925 1956 ILE B N 6853 C CA . ILE B 309 ? 1.6266 1.1842 1.3293 -0.0271 0.3886 0.0853 1956 ILE B CA 6854 C C . ILE B 309 ? 1.7720 1.3605 1.5163 -0.0157 0.3927 0.0930 1956 ILE B C 6855 O O . ILE B 309 ? 1.7882 1.4166 1.5761 -0.0198 0.3887 0.1009 1956 ILE B O 6856 C CB . ILE B 309 ? 1.5610 1.1170 1.2691 -0.0485 0.3667 0.0792 1956 ILE B CB 6857 C CG1 . ILE B 309 ? 1.6169 1.1289 1.2811 -0.0548 0.3613 0.0675 1956 ILE B CG1 6858 C CG2 . ILE B 309 ? 1.5492 1.1323 1.2975 -0.0522 0.3571 0.0806 1956 ILE B CG2 6859 C CD1 . ILE B 309 ? 1.8650 1.3490 1.4826 -0.0546 0.3662 0.0622 1956 ILE B CD1 6860 N N . HIS B 310 ? 1.8745 1.4428 1.6052 -0.0021 0.3991 0.0908 1957 HIS B N 6861 C CA . HIS B 310 ? 1.8296 1.4259 1.5950 0.0107 0.4012 0.0997 1957 HIS B CA 6862 C C . HIS B 310 ? 1.8813 1.4657 1.6438 0.0067 0.3889 0.0970 1957 HIS B C 6863 O O . HIS B 310 ? 1.8338 1.3753 1.5614 0.0031 0.3874 0.0897 1957 HIS B O 6864 C CB . HIS B 310 ? 1.8288 1.4210 1.5894 0.0370 0.4236 0.1064 1957 HIS B CB 6865 C CG . HIS B 310 ? 1.8792 1.5015 1.6758 0.0525 0.4249 0.1180 1957 HIS B CG 6866 N ND1 . HIS B 310 ? 1.8487 1.4496 1.6336 0.0762 0.4381 0.1220 1957 HIS B ND1 6867 C CD2 . HIS B 310 ? 1.9568 1.6290 1.8006 0.0478 0.4130 0.1265 1957 HIS B CD2 6868 C CE1 . HIS B 310 ? 1.9596 1.5999 1.7845 0.0862 0.4339 0.1352 1957 HIS B CE1 6869 N NE2 . HIS B 310 ? 2.0750 1.7595 1.9344 0.0683 0.4179 0.1371 1957 HIS B NE2 6870 N N . PHE B 311 ? 1.8714 1.4954 1.6709 0.0061 0.3797 0.1035 1958 PHE B N 6871 C CA . PHE B 311 ? 1.8741 1.4956 1.6723 0.0056 0.3703 0.1053 1958 PHE B CA 6872 C C . PHE B 311 ? 1.8881 1.5290 1.7049 0.0272 0.3764 0.1185 1958 PHE B C 6873 O O . PHE B 311 ? 1.9670 1.6559 1.8212 0.0291 0.3702 0.1249 1958 PHE B O 6874 C CB . PHE B 311 ? 1.8913 1.5450 1.7121 -0.0120 0.3530 0.1010 1958 PHE B CB 6875 C CG . PHE B 311 ? 1.8470 1.4798 1.6494 -0.0311 0.3449 0.0908 1958 PHE B CG 6876 C CD1 . PHE B 311 ? 1.8311 1.4329 1.6072 -0.0358 0.3429 0.0898 1958 PHE B CD1 6877 C CD2 . PHE B 311 ? 1.7738 1.4200 1.5898 -0.0445 0.3387 0.0844 1958 PHE B CD2 6878 C CE1 . PHE B 311 ? 1.7608 1.3505 1.5266 -0.0542 0.3348 0.0822 1958 PHE B CE1 6879 C CE2 . PHE B 311 ? 1.7464 1.3786 1.5506 -0.0604 0.3306 0.0770 1958 PHE B CE2 6880 C CZ . PHE B 311 ? 1.7735 1.3799 1.5536 -0.0654 0.3285 0.0757 1958 PHE B CZ 6881 N N . SER B 312 ? 1.7450 1.3483 1.5375 0.0431 0.3871 0.1228 1959 SER B N 6882 C CA . SER B 312 ? 1.6337 1.2506 1.4434 0.0688 0.3959 0.1378 1959 SER B CA 6883 C C . SER B 312 ? 1.6658 1.3328 1.5079 0.0676 0.3800 0.1485 1959 SER B C 6884 O O . SER B 312 ? 1.5307 1.1988 1.3646 0.0527 0.3659 0.1458 1959 SER B O 6885 C CB . SER B 312 ? 1.6057 1.1656 1.3822 0.0834 0.4067 0.1398 1959 SER B CB 6886 O OG . SER B 312 ? 1.5740 1.1383 1.3643 0.1134 0.4221 0.1523 1959 SER B OG 6887 N N . GLY B 313 ? 1.8343 1.5466 1.7136 0.0824 0.3819 0.1602 1960 GLY B N 6888 C CA . GLY B 313 ? 2.1088 1.8727 2.0184 0.0830 0.3648 0.1707 1960 GLY B CA 6889 C C . GLY B 313 ? 1.9943 1.7849 1.9094 0.0581 0.3437 0.1597 1960 GLY B C 6890 O O . GLY B 313 ? 1.9513 1.7707 1.8729 0.0574 0.3287 0.1654 1960 GLY B O 6891 N N . HIS B 314 ? 1.8590 1.6399 1.7704 0.0392 0.3433 0.1441 1961 HIS B N 6892 C CA . HIS B 314 ? 1.7615 1.5569 1.6750 0.0170 0.3272 0.1305 1961 HIS B CA 6893 C C . HIS B 314 ? 1.7707 1.5789 1.7084 0.0059 0.3287 0.1224 1961 HIS B C 6894 O O . HIS B 314 ? 1.8532 1.6433 1.7873 0.0126 0.3444 0.1258 1961 HIS B O 6895 C CB . HIS B 314 ? 1.7903 1.5424 1.6652 0.0066 0.3282 0.1226 1961 HIS B CB 6896 C CG . HIS B 314 ? 2.0442 1.7851 1.8978 0.0134 0.3259 0.1327 1961 HIS B CG 6897 N ND1 . HIS B 314 ? 2.0829 1.8133 1.9161 -0.0003 0.3196 0.1276 1961 HIS B ND1 6898 C CD2 . HIS B 314 ? 2.1033 1.8428 1.9547 0.0331 0.3300 0.1502 1961 HIS B CD2 6899 C CE1 . HIS B 314 ? 2.0444 1.7673 1.8625 0.0090 0.3201 0.1424 1961 HIS B CE1 6900 N NE2 . HIS B 314 ? 2.1251 1.8518 1.9536 0.0297 0.3255 0.1564 1961 HIS B NE2 6901 N N . VAL B 315 ? 1.7171 1.5562 1.6791 -0.0099 0.3134 0.1126 1962 VAL B N 6902 C CA . VAL B 315 ? 1.5641 1.4089 1.5489 -0.0245 0.3128 0.1045 1962 VAL B CA 6903 C C . VAL B 315 ? 1.5702 1.3989 1.5409 -0.0414 0.3035 0.0882 1962 VAL B C 6904 O O . VAL B 315 ? 1.8103 1.6321 1.7581 -0.0420 0.2977 0.0834 1962 VAL B O 6905 C CB . VAL B 315 ? 1.4388 1.3311 1.4722 -0.0314 0.3011 0.1046 1962 VAL B CB 6906 C CG1 . VAL B 315 ? 1.4452 1.3613 1.5085 -0.0188 0.3126 0.1220 1962 VAL B CG1 6907 C CG2 . VAL B 315 ? 1.5001 1.4214 1.5381 -0.0345 0.2814 0.0977 1962 VAL B CG2 6908 N N . PHE B 316 ? 1.4837 1.3095 1.4712 -0.0541 0.3026 0.0816 1963 PHE B N 6909 C CA . PHE B 316 ? 1.5325 1.3527 1.5206 -0.0692 0.2917 0.0653 1963 PHE B CA 6910 C C . PHE B 316 ? 1.4689 1.3071 1.4970 -0.0821 0.2824 0.0570 1963 PHE B C 6911 O O . PHE B 316 ? 1.5175 1.3797 1.5786 -0.0831 0.2811 0.0634 1963 PHE B O 6912 C CB . PHE B 316 ? 1.4405 1.2249 1.4010 -0.0728 0.2985 0.0639 1963 PHE B CB 6913 C CG . PHE B 316 ? 1.4758 1.2420 1.4282 -0.0682 0.3117 0.0753 1963 PHE B CG 6914 C CD1 . PHE B 316 ? 1.5731 1.3235 1.5000 -0.0549 0.3232 0.0843 1963 PHE B CD1 6915 C CD2 . PHE B 316 ? 1.6213 1.3858 1.5911 -0.0759 0.3133 0.0777 1963 PHE B CD2 6916 C CE1 . PHE B 316 ? 1.9306 1.6637 1.8446 -0.0490 0.3370 0.0923 1963 PHE B CE1 6917 C CE2 . PHE B 316 ? 1.8246 1.5753 1.7823 -0.0708 0.3266 0.0892 1963 PHE B CE2 6918 C CZ . PHE B 316 ? 2.0273 1.7628 1.9551 -0.0571 0.3389 0.0950 1963 PHE B CZ 6919 N N . THR B 317 ? 1.3680 1.1943 1.3960 -0.0922 0.2762 0.0431 1964 THR B N 6920 C CA . THR B 317 ? 1.3594 1.1917 1.4240 -0.1041 0.2686 0.0349 1964 THR B CA 6921 C C . THR B 317 ? 1.3893 1.1934 1.4487 -0.1082 0.2747 0.0374 1964 THR B C 6922 O O . THR B 317 ? 1.3178 1.1035 1.3458 -0.1045 0.2790 0.0377 1964 THR B O 6923 C CB . THR B 317 ? 1.4356 1.2809 1.5078 -0.1106 0.2535 0.0123 1964 THR B CB 6924 O OG1 . THR B 317 ? 1.6531 1.5197 1.7068 -0.1034 0.2483 0.0105 1964 THR B OG1 6925 C CG2 . THR B 317 ? 1.3170 1.1742 1.4333 -0.1229 0.2431 0.0040 1964 THR B CG2 6926 N N . VAL B 318 ? 1.3364 1.1381 1.4283 -0.1164 0.2742 0.0416 1965 VAL B N 6927 C CA . VAL B 318 ? 1.3074 1.0854 1.3995 -0.1202 0.2766 0.0449 1965 VAL B CA 6928 C C . VAL B 318 ? 1.4447 1.2178 1.5710 -0.1295 0.2669 0.0319 1965 VAL B C 6929 O O . VAL B 318 ? 1.3307 1.1147 1.4921 -0.1376 0.2604 0.0273 1965 VAL B O 6930 C CB . VAL B 318 ? 1.2168 0.9862 1.3072 -0.1190 0.2884 0.0676 1965 VAL B CB 6931 C CG1 . VAL B 318 ? 1.2010 0.9466 1.2670 -0.1181 0.2905 0.0723 1965 VAL B CG1 6932 C CG2 . VAL B 318 ? 1.1902 0.9691 1.2610 -0.1092 0.2995 0.0790 1965 VAL B CG2 6933 N N . ARG B 319 ? 1.7087 1.4647 1.8254 -0.1281 0.2658 0.0261 1966 ARG B N 6934 C CA . ARG B 319 ? 1.8345 1.5782 1.9794 -0.1325 0.2594 0.0147 1966 ARG B CA 6935 C C . ARG B 319 ? 1.7569 1.4912 1.9396 -0.1404 0.2597 0.0291 1966 ARG B C 6936 O O . ARG B 319 ? 1.7738 1.5159 1.9864 -0.1486 0.2545 0.0235 1966 ARG B O 6937 C CB . ARG B 319 ? 2.1293 1.8607 2.2569 -0.1266 0.2613 0.0145 1966 ARG B CB 6938 C CG . ARG B 319 ? 2.3225 2.0497 2.4169 -0.1233 0.2682 0.0338 1966 ARG B CG 6939 C CD . ARG B 319 ? 2.5866 2.3047 2.6728 -0.1208 0.2669 0.0371 1966 ARG B CD 6940 N NE . ARG B 319 ? 2.9994 2.7064 3.0830 -0.1223 0.2686 0.0595 1966 ARG B NE 6941 C CZ . ARG B 319 ? 3.2923 2.9942 3.3550 -0.1215 0.2670 0.0696 1966 ARG B CZ 6942 N NH1 . ARG B 319 ? 3.5532 3.2603 3.6002 -0.1204 0.2647 0.0606 1966 ARG B NH1 6943 N NH2 . ARG B 319 ? 3.0172 2.7108 3.0744 -0.1228 0.2673 0.0900 1966 ARG B NH2 6944 N N . LYS B 320 ? 1.6289 1.3484 1.8101 -0.1389 0.2651 0.0491 1967 LYS B N 6945 C CA . LYS B 320 ? 1.7097 1.4168 1.9266 -0.1457 0.2661 0.0668 1967 LYS B CA 6946 C C . LYS B 320 ? 1.7160 1.4150 1.9805 -0.1551 0.2574 0.0522 1967 LYS B C 6947 O O . LYS B 320 ? 1.6045 1.2962 1.8742 -0.1531 0.2500 0.0267 1967 LYS B O 6948 C CB . LYS B 320 ? 1.7883 1.5044 2.0000 -0.1475 0.2769 0.0943 1967 LYS B CB 6949 C CG . LYS B 320 ? 1.9369 1.6575 2.0980 -0.1383 0.2856 0.1036 1967 LYS B CG 6950 C CD . LYS B 320 ? 2.0268 1.7339 2.1584 -0.1326 0.2819 0.1007 1967 LYS B CD 6951 C CE . LYS B 320 ? 2.1567 1.8520 2.2839 -0.1324 0.2842 0.1248 1967 LYS B CE 6952 N NZ . LYS B 320 ? 2.2531 1.9523 2.3481 -0.1299 0.2959 0.1437 1967 LYS B NZ 6953 N N . LYS B 321 ? 1.8473 1.5462 2.1467 -0.1657 0.2589 0.0679 1968 LYS B N 6954 C CA . LYS B 321 ? 1.9275 1.6145 2.2740 -0.1778 0.2488 0.0527 1968 LYS B CA 6955 C C . LYS B 321 ? 1.6913 1.3923 2.0366 -0.1815 0.2373 0.0181 1968 LYS B C 6956 O O . LYS B 321 ? 1.5409 1.2283 1.8818 -0.1773 0.2305 -0.0088 1968 LYS B O 6957 C CB . LYS B 321 ? 2.1832 1.8694 2.5715 -0.1913 0.2529 0.0795 1968 LYS B CB 6958 C CG . LYS B 321 ? 2.2444 1.9067 2.6443 -0.1893 0.2596 0.1082 1968 LYS B CG 6959 C CD . LYS B 321 ? 2.3283 1.9553 2.7663 -0.1928 0.2504 0.0955 1968 LYS B CD 6960 C CE . LYS B 321 ? 2.2444 1.8499 2.7150 -0.1976 0.2557 0.1306 1968 LYS B CE 6961 N NZ . LYS B 321 ? 2.0286 1.5943 2.5404 -0.1995 0.2473 0.1193 1968 LYS B NZ 6962 N N . GLU B 322 ? 1.6303 1.3605 1.9784 -0.1879 0.2355 0.0198 1969 GLU B N 6963 C CA . GLU B 322 ? 1.6526 1.4041 1.9893 -0.1892 0.2238 -0.0081 1969 GLU B CA 6964 C C . GLU B 322 ? 1.7578 1.5353 2.0514 -0.1767 0.2314 0.0008 1969 GLU B C 6965 O O . GLU B 322 ? 1.8003 1.5763 2.0748 -0.1687 0.2449 0.0246 1969 GLU B O 6966 C CB . GLU B 322 ? 1.6436 1.4121 2.0238 -0.2072 0.2124 -0.0117 1969 GLU B CB 6967 C CG . GLU B 322 ? 1.8821 1.6282 2.3144 -0.2225 0.2118 0.0007 1969 GLU B CG 6968 C CD . GLU B 322 ? 2.1896 1.9183 2.6536 -0.2375 0.1935 -0.0310 1969 GLU B CD 6969 O OE1 . GLU B 322 ? 2.3674 2.1194 2.8599 -0.2536 0.1811 -0.0371 1969 GLU B OE1 6970 O OE2 . GLU B 322 ? 2.4516 2.1441 2.9127 -0.2327 0.1913 -0.0501 1969 GLU B OE2 6971 N N . GLU B 323 ? 1.8525 1.6525 2.1293 -0.1748 0.2224 -0.0175 1970 GLU B N 6972 C CA . GLU B 323 ? 1.8105 1.6296 2.0469 -0.1615 0.2300 -0.0077 1970 GLU B CA 6973 C C . GLU B 323 ? 1.6501 1.4966 1.9013 -0.1619 0.2354 0.0151 1970 GLU B C 6974 O O . GLU B 323 ? 1.5452 1.4154 1.8305 -0.1724 0.2250 0.0122 1970 GLU B O 6975 C CB . GLU B 323 ? 2.0104 1.8408 2.2141 -0.1552 0.2213 -0.0316 1970 GLU B CB 6976 C CG . GLU B 323 ? 2.1527 1.9623 2.3219 -0.1451 0.2283 -0.0394 1970 GLU B CG 6977 C CD . GLU B 323 ? 2.0670 1.8888 2.2028 -0.1386 0.2230 -0.0602 1970 GLU B CD 6978 O OE1 . GLU B 323 ? 1.7949 1.6432 1.9218 -0.1382 0.2152 -0.0629 1970 GLU B OE1 6979 O OE2 . GLU B 323 ? 1.8154 1.6229 1.9349 -0.1331 0.2272 -0.0716 1970 GLU B OE2 6980 N N . TYR B 324 ? 1.5579 1.4010 1.7844 -0.1504 0.2518 0.0370 1971 TYR B N 6981 C CA . TYR B 324 ? 1.5867 1.4532 1.8211 -0.1453 0.2627 0.0601 1971 TYR B CA 6982 C C . TYR B 324 ? 1.6433 1.5182 1.8365 -0.1285 0.2686 0.0624 1971 TYR B C 6983 O O . TYR B 324 ? 1.6460 1.4980 1.7982 -0.1205 0.2729 0.0578 1971 TYR B O 6984 C CB . TYR B 324 ? 1.6238 1.4745 1.8582 -0.1436 0.2799 0.0840 1971 TYR B CB 6985 C CG . TYR B 324 ? 1.6983 1.5388 1.9749 -0.1589 0.2773 0.0901 1971 TYR B CG 6986 C CD1 . TYR B 324 ? 1.5561 1.3650 1.8303 -0.1631 0.2720 0.0808 1971 TYR B CD1 6987 C CD2 . TYR B 324 ? 1.9312 1.7943 2.2539 -0.1687 0.2812 0.1079 1971 TYR B CD2 6988 C CE1 . TYR B 324 ? 1.5786 1.3738 1.8936 -0.1760 0.2700 0.0888 1971 TYR B CE1 6989 C CE2 . TYR B 324 ? 1.9572 1.8083 2.3216 -0.1843 0.2793 0.1165 1971 TYR B CE2 6990 C CZ . TYR B 324 ? 1.7871 1.6016 2.1467 -0.1876 0.2734 0.1069 1971 TYR B CZ 6991 O OH . TYR B 324 ? 1.8761 1.6752 2.2799 -0.2022 0.2718 0.1180 1971 TYR B OH 6992 N N . LYS B 325 ? 1.5390 1.4464 1.7460 -0.1232 0.2689 0.0715 1972 LYS B N 6993 C CA . LYS B 325 ? 1.4100 1.3225 1.5815 -0.1053 0.2757 0.0769 1972 LYS B CA 6994 C C . LYS B 325 ? 1.3574 1.2655 1.5181 -0.0916 0.2978 0.0994 1972 LYS B C 6995 O O . LYS B 325 ? 1.3432 1.2749 1.5384 -0.0921 0.3055 0.1150 1972 LYS B O 6996 C CB . LYS B 325 ? 1.3551 1.3057 1.5425 -0.1033 0.2619 0.0733 1972 LYS B CB 6997 C CG . LYS B 325 ? 1.3988 1.3529 1.5538 -0.0830 0.2696 0.0831 1972 LYS B CG 6998 C CD . LYS B 325 ? 1.5082 1.4908 1.6616 -0.0814 0.2512 0.0745 1972 LYS B CD 6999 C CE . LYS B 325 ? 1.6631 1.6272 1.7856 -0.0884 0.2399 0.0519 1972 LYS B CE 7000 N NZ . LYS B 325 ? 1.8300 1.8244 1.9653 -0.0981 0.2166 0.0349 1972 LYS B NZ 7001 N N . MET B 326 ? 1.3676 1.2459 1.4804 -0.0798 0.3081 0.0999 1973 MET B N 7002 C CA . MET B 326 ? 1.4663 1.3286 1.5559 -0.0667 0.3295 0.1154 1973 MET B CA 7003 C C . MET B 326 ? 1.5279 1.3743 1.5767 -0.0492 0.3365 0.1155 1973 MET B C 7004 O O . MET B 326 ? 1.5236 1.3614 1.5530 -0.0500 0.3254 0.1042 1973 MET B O 7005 C CB . MET B 326 ? 1.5616 1.3897 1.6268 -0.0733 0.3343 0.1143 1973 MET B CB 7006 C CG . MET B 326 ? 1.6093 1.4402 1.7080 -0.0901 0.3276 0.1150 1973 MET B CG 7007 S SD . MET B 326 ? 1.7791 1.5802 1.8478 -0.0892 0.3418 0.1280 1973 MET B SD 7008 C CE . MET B 326 ? 1.8579 1.6860 1.9510 -0.0823 0.3627 0.1524 1973 MET B CE 7009 N N . ALA B 327 ? 1.5614 1.4010 1.5957 -0.0332 0.3561 0.1281 1974 ALA B N 7010 C CA . ALA B 327 ? 1.5927 1.4087 1.5881 -0.0154 0.3643 0.1280 1974 ALA B CA 7011 C C . ALA B 327 ? 1.5680 1.3387 1.5150 -0.0108 0.3781 0.1258 1974 ALA B C 7012 O O . ALA B 327 ? 1.5030 1.2415 1.4121 -0.0014 0.3817 0.1212 1974 ALA B O 7013 C CB . ALA B 327 ? 1.5653 1.4094 1.5822 0.0042 0.3741 0.1417 1974 ALA B CB 7014 N N . LEU B 328 ? 1.4619 1.2297 1.4100 -0.0183 0.3846 0.1295 1975 LEU B N 7015 C CA . LEU B 328 ? 1.5860 1.3154 1.4870 -0.0162 0.3950 0.1271 1975 LEU B CA 7016 C C . LEU B 328 ? 1.6251 1.3527 1.5315 -0.0345 0.3862 0.1267 1975 LEU B C 7017 O O . LEU B 328 ? 1.8343 1.5897 1.7801 -0.0413 0.3864 0.1365 1975 LEU B O 7018 C CB . LEU B 328 ? 1.7078 1.4402 1.6003 0.0018 0.4197 0.1386 1975 LEU B CB 7019 C CG . LEU B 328 ? 1.7850 1.4721 1.6168 0.0140 0.4339 0.1317 1975 LEU B CG 7020 C CD1 . LEU B 328 ? 1.8118 1.5073 1.6407 0.0380 0.4609 0.1414 1975 LEU B CD1 7021 C CD2 . LEU B 328 ? 1.7896 1.4530 1.5874 0.0001 0.4298 0.1275 1975 LEU B CD2 7022 N N . TYR B 329 ? 1.6353 1.3309 1.5058 -0.0428 0.3779 0.1171 1976 TYR B N 7023 C CA . TYR B 329 ? 1.7880 1.4801 1.6614 -0.0578 0.3692 0.1189 1976 TYR B CA 7024 C C . TYR B 329 ? 1.8036 1.4644 1.6253 -0.0567 0.3748 0.1188 1976 TYR B C 7025 O O . TYR B 329 ? 1.9130 1.5451 1.6968 -0.0557 0.3714 0.1075 1976 TYR B O 7026 C CB . TYR B 329 ? 1.8206 1.5139 1.7106 -0.0714 0.3490 0.1075 1976 TYR B CB 7027 C CG . TYR B 329 ? 1.8275 1.5262 1.7406 -0.0845 0.3395 0.1114 1976 TYR B CG 7028 C CD1 . TYR B 329 ? 1.9333 1.6125 1.8194 -0.0896 0.3364 0.1148 1976 TYR B CD1 7029 C CD2 . TYR B 329 ? 1.7786 1.5003 1.7405 -0.0915 0.3323 0.1114 1976 TYR B CD2 7030 C CE1 . TYR B 329 ? 2.0708 1.7546 1.9803 -0.0990 0.3278 0.1214 1976 TYR B CE1 7031 C CE2 . TYR B 329 ? 2.0411 1.7620 2.0259 -0.1017 0.3246 0.1154 1976 TYR B CE2 7032 C CZ . TYR B 329 ? 2.1246 1.8271 2.0844 -0.1043 0.3230 0.1220 1976 TYR B CZ 7033 O OH . TYR B 329 ? 2.0453 1.7469 2.0300 -0.1121 0.3153 0.1291 1976 TYR B OH 7034 N N . ASN B 330 ? 1.7358 1.4026 1.5557 -0.0579 0.3827 0.1321 1977 ASN B N 7035 C CA . ASN B 330 ? 1.6775 1.3190 1.4445 -0.0567 0.3873 0.1332 1977 ASN B CA 7036 C C . ASN B 330 ? 1.7330 1.3648 1.4938 -0.0725 0.3672 0.1311 1977 ASN B C 7037 O O . ASN B 330 ? 1.8703 1.5201 1.6710 -0.0818 0.3579 0.1394 1977 ASN B O 7038 C CB . ASN B 330 ? 1.6561 1.3123 1.4206 -0.0496 0.4065 0.1518 1977 ASN B CB 7039 C CG . ASN B 330 ? 1.7013 1.3842 1.4981 -0.0361 0.4257 0.1602 1977 ASN B CG 7040 O OD1 . ASN B 330 ? 1.8706 1.5497 1.6394 -0.0197 0.4472 0.1631 1977 ASN B OD1 7041 N ND2 . ASN B 330 ? 1.5048 1.2164 1.3610 -0.0426 0.4179 0.1638 1977 ASN B ND2 7042 N N . LEU B 331 ? 1.8118 1.4150 1.5254 -0.0756 0.3597 0.1199 1978 LEU B N 7043 C CA . LEU B 331 ? 1.8475 1.4459 1.5569 -0.0901 0.3395 0.1193 1978 LEU B CA 7044 C C . LEU B 331 ? 1.9304 1.5241 1.6053 -0.0910 0.3407 0.1312 1978 LEU B C 7045 O O . LEU B 331 ? 2.0593 1.6357 1.6848 -0.0830 0.3526 0.1283 1978 LEU B O 7046 C CB . LEU B 331 ? 1.8032 1.3776 1.4869 -0.0969 0.3268 0.1018 1978 LEU B CB 7047 C CG . LEU B 331 ? 1.7890 1.3744 1.5111 -0.1041 0.3150 0.0947 1978 LEU B CG 7048 C CD1 . LEU B 331 ? 1.9195 1.5319 1.6908 -0.0985 0.3216 0.0994 1978 LEU B CD1 7049 C CD2 . LEU B 331 ? 1.7916 1.3534 1.4899 -0.1044 0.3143 0.0805 1978 LEU B CD2 7050 N N . TYR B 332 ? 1.9214 1.5303 1.6210 -0.0995 0.3292 0.1452 1979 TYR B N 7051 C CA . TYR B 332 ? 2.0028 1.6079 1.6659 -0.1018 0.3254 0.1580 1979 TYR B CA 7052 C C . TYR B 332 ? 1.9707 1.5666 1.6204 -0.1141 0.3009 0.1494 1979 TYR B C 7053 O O . TYR B 332 ? 2.0692 1.6673 1.7492 -0.1199 0.2906 0.1382 1979 TYR B O 7054 C CB . TYR B 332 ? 2.1957 1.8237 1.8961 -0.1019 0.3297 0.1841 1979 TYR B CB 7055 C CG . TYR B 332 ? 2.3684 2.0082 2.0794 -0.0914 0.3551 0.1940 1979 TYR B CG 7056 C CD1 . TYR B 332 ? 2.4899 2.1253 2.1509 -0.0816 0.3735 0.2014 1979 TYR B CD1 7057 C CD2 . TYR B 332 ? 2.2647 1.9220 2.0346 -0.0909 0.3611 0.1949 1979 TYR B CD2 7058 C CE1 . TYR B 332 ? 2.3640 2.0154 2.0386 -0.0707 0.3992 0.2121 1979 TYR B CE1 7059 C CE2 . TYR B 332 ? 2.3229 1.9966 2.1079 -0.0823 0.3834 0.2056 1979 TYR B CE2 7060 C CZ . TYR B 332 ? 2.2697 1.9419 2.0094 -0.0717 0.4034 0.2152 1979 TYR B CZ 7061 O OH . TYR B 332 ? 2.0988 1.7923 1.8574 -0.0620 0.4277 0.2277 1979 TYR B OH 7062 N N . PRO B 333 ? 2.0323 1.6204 1.6357 -0.1182 0.2914 0.1546 1980 PRO B N 7063 C CA . PRO B 333 ? 2.1303 1.7161 1.7283 -0.1317 0.2653 0.1485 1980 PRO B CA 7064 C C . PRO B 333 ? 2.0393 1.6499 1.7006 -0.1366 0.2519 0.1614 1980 PRO B C 7065 O O . PRO B 333 ? 2.1773 1.8031 1.8636 -0.1326 0.2548 0.1830 1980 PRO B O 7066 C CB . PRO B 333 ? 2.3529 1.9323 1.8917 -0.1343 0.2572 0.1564 1980 PRO B CB 7067 C CG . PRO B 333 ? 2.3708 1.9385 1.8681 -0.1209 0.2829 0.1567 1980 PRO B CG 7068 C CD . PRO B 333 ? 2.1814 1.7648 1.7335 -0.1111 0.3035 0.1655 1980 PRO B CD 7069 N N . GLY B 334 ? 1.9665 1.5802 1.6547 -0.1441 0.2394 0.1486 1981 GLY B N 7070 C CA . GLY B 334 ? 2.0071 1.6433 1.7518 -0.1471 0.2267 0.1573 1981 GLY B CA 7071 C C . GLY B 334 ? 2.0363 1.6828 1.8370 -0.1411 0.2372 0.1539 1981 GLY B C 7072 O O . GLY B 334 ? 2.1261 1.7875 1.9711 -0.1424 0.2283 0.1547 1981 GLY B O 7073 N N . VAL B 335 ? 1.9835 1.6235 1.7823 -0.1341 0.2556 0.1493 1982 VAL B N 7074 C CA . VAL B 335 ? 1.9040 1.5546 1.7527 -0.1297 0.2639 0.1457 1982 VAL B CA 7075 C C . VAL B 335 ? 1.9428 1.5932 1.7998 -0.1306 0.2648 0.1248 1982 VAL B C 7076 O O . VAL B 335 ? 1.8977 1.5408 1.7386 -0.1264 0.2760 0.1159 1982 VAL B O 7077 C CB . VAL B 335 ? 1.8902 1.5425 1.7455 -0.1231 0.2812 0.1562 1982 VAL B CB 7078 C CG1 . VAL B 335 ? 1.8949 1.5497 1.7450 -0.1228 0.2809 0.1810 1982 VAL B CG1 7079 C CG2 . VAL B 335 ? 1.9104 1.5526 1.7279 -0.1172 0.2962 0.1478 1982 VAL B CG2 7080 N N . PHE B 336 ? 1.9740 1.6346 1.8569 -0.1348 0.2535 0.1191 1983 PHE B N 7081 C CA . PHE B 336 ? 1.9440 1.6077 1.8339 -0.1360 0.2547 0.1022 1983 PHE B CA 7082 C C . PHE B 336 ? 1.9370 1.6098 1.8589 -0.1296 0.2638 0.0955 1983 PHE B C 7083 O O . PHE B 336 ? 1.9920 1.6741 1.9520 -0.1275 0.2620 0.0980 1983 PHE B O 7084 C CB . PHE B 336 ? 1.8902 1.5670 1.7997 -0.1417 0.2423 0.0998 1983 PHE B CB 7085 C CG . PHE B 336 ? 1.7262 1.3991 1.6149 -0.1490 0.2400 0.0896 1983 PHE B CG 7086 C CD1 . PHE B 336 ? 1.6610 1.3288 1.5419 -0.1464 0.2501 0.0786 1983 PHE B CD1 7087 C CD2 . PHE B 336 ? 1.6472 1.3225 1.5264 -0.1596 0.2266 0.0932 1983 PHE B CD2 7088 C CE1 . PHE B 336 ? 1.5834 1.2452 1.4473 -0.1539 0.2486 0.0727 1983 PHE B CE1 7089 C CE2 . PHE B 336 ? 1.5342 1.2047 1.3989 -0.1692 0.2242 0.0856 1983 PHE B CE2 7090 C CZ . PHE B 336 ? 1.5056 1.1676 1.3626 -0.1662 0.2362 0.0760 1983 PHE B CZ 7091 N N . GLU B 337 ? 1.9100 1.5785 1.8160 -0.1264 0.2725 0.0869 1984 GLU B N 7092 C CA . GLU B 337 ? 1.9289 1.6074 1.8587 -0.1211 0.2798 0.0821 1984 GLU B CA 7093 C C . GLU B 337 ? 1.8435 1.5306 1.7766 -0.1195 0.2805 0.0675 1984 GLU B C 7094 O O . GLU B 337 ? 1.8895 1.5682 1.7944 -0.1190 0.2831 0.0646 1984 GLU B O 7095 C CB . GLU B 337 ? 1.8955 1.5687 1.8103 -0.1159 0.2911 0.0912 1984 GLU B CB 7096 C CG . GLU B 337 ? 2.1289 1.8180 2.0798 -0.1134 0.2958 0.0918 1984 GLU B CG 7097 C CD . GLU B 337 ? 2.4424 2.1386 2.4356 -0.1183 0.2883 0.0924 1984 GLU B CD 7098 O OE1 . GLU B 337 ? 2.7172 2.4064 2.7123 -0.1208 0.2839 0.1029 1984 GLU B OE1 7099 O OE2 . GLU B 337 ? 2.5160 2.2236 2.5399 -0.1192 0.2860 0.0820 1984 GLU B OE2 7100 N N . THR B 338 ? 1.7118 1.4140 1.6782 -0.1186 0.2780 0.0587 1985 THR B N 7101 C CA . THR B 338 ? 1.6498 1.3642 1.6184 -0.1169 0.2776 0.0448 1985 THR B CA 7102 C C . THR B 338 ? 1.5615 1.2861 1.5373 -0.1127 0.2808 0.0412 1985 THR B C 7103 O O . THR B 338 ? 1.4082 1.1395 1.4129 -0.1139 0.2790 0.0400 1985 THR B O 7104 C CB . THR B 338 ? 1.7407 1.4658 1.7374 -0.1177 0.2723 0.0341 1985 THR B CB 7105 O OG1 . THR B 338 ? 1.6000 1.3212 1.5945 -0.1208 0.2687 0.0409 1985 THR B OG1 7106 C CG2 . THR B 338 ? 1.7898 1.5301 1.7840 -0.1150 0.2734 0.0191 1985 THR B CG2 7107 N N . VAL B 339 ? 1.5625 1.2882 1.5145 -0.1085 0.2847 0.0412 1986 VAL B N 7108 C CA . VAL B 339 ? 1.6525 1.3942 1.6115 -0.1032 0.2856 0.0389 1986 VAL B CA 7109 C C . VAL B 339 ? 1.7530 1.5063 1.6979 -0.1000 0.2837 0.0316 1986 VAL B C 7110 O O . VAL B 339 ? 1.7104 1.4529 1.6308 -0.1001 0.2865 0.0345 1986 VAL B O 7111 C CB . VAL B 339 ? 1.5999 1.3349 1.5454 -0.0964 0.2943 0.0521 1986 VAL B CB 7112 C CG1 . VAL B 339 ? 1.6463 1.3815 1.6121 -0.0983 0.2978 0.0608 1986 VAL B CG1 7113 C CG2 . VAL B 339 ? 1.6156 1.3253 1.5228 -0.0941 0.3001 0.0576 1986 VAL B CG2 7114 N N . GLU B 340 ? 1.8264 1.6024 1.7866 -0.0982 0.2782 0.0235 1987 GLU B N 7115 C CA . GLU B 340 ? 1.8182 1.6112 1.7640 -0.0945 0.2748 0.0169 1987 GLU B CA 7116 C C . GLU B 340 ? 1.7308 1.5368 1.6716 -0.0863 0.2747 0.0269 1987 GLU B C 7117 O O . GLU B 340 ? 1.6817 1.4968 1.6445 -0.0853 0.2735 0.0311 1987 GLU B O 7118 C CB . GLU B 340 ? 1.8533 1.6644 1.8153 -0.0985 0.2661 -0.0038 1987 GLU B CB 7119 C CG . GLU B 340 ? 1.8795 1.6860 1.8368 -0.1007 0.2686 -0.0140 1987 GLU B CG 7120 C CD . GLU B 340 ? 1.9870 1.8094 1.9541 -0.1010 0.2628 -0.0377 1987 GLU B CD 7121 O OE1 . GLU B 340 ? 2.1109 1.9507 2.0782 -0.1005 0.2546 -0.0479 1987 GLU B OE1 7122 O OE2 . GLU B 340 ? 1.8374 1.6558 1.8114 -0.1010 0.2661 -0.0473 1987 GLU B OE2 7123 N N . MET B 341 ? 1.6813 1.4895 1.5963 -0.0799 0.2767 0.0333 1988 MET B N 7124 C CA . MET B 341 ? 1.6575 1.4807 1.5688 -0.0693 0.2756 0.0448 1988 MET B CA 7125 C C . MET B 341 ? 1.7300 1.5677 1.6183 -0.0646 0.2721 0.0473 1988 MET B C 7126 O O . MET B 341 ? 1.7285 1.5547 1.5954 -0.0675 0.2767 0.0474 1988 MET B O 7127 C CB . MET B 341 ? 1.6786 1.4774 1.5793 -0.0605 0.2872 0.0616 1988 MET B CB 7128 C CG . MET B 341 ? 1.6138 1.4007 1.4869 -0.0506 0.2923 0.0752 1988 MET B CG 7129 S SD . MET B 341 ? 1.7180 1.4538 1.5633 -0.0512 0.3054 0.0823 1988 MET B SD 7130 C CE . MET B 341 ? 1.6520 1.3770 1.5087 -0.0431 0.3144 0.0862 1988 MET B CE 7131 N N . LEU B 342 ? 1.7424 1.6078 1.6369 -0.0571 0.2641 0.0524 1989 LEU B N 7132 C CA . LEU B 342 ? 1.7399 1.6270 1.6133 -0.0513 0.2580 0.0570 1989 LEU B CA 7133 C C . LEU B 342 ? 1.7938 1.6768 1.6617 -0.0363 0.2627 0.0814 1989 LEU B C 7134 O O . LEU B 342 ? 2.1711 2.0699 2.0633 -0.0298 0.2593 0.0873 1989 LEU B O 7135 C CB . LEU B 342 ? 1.7946 1.7201 1.6839 -0.0557 0.2409 0.0407 1989 LEU B CB 7136 C CG . LEU B 342 ? 2.0409 2.0023 1.9125 -0.0534 0.2270 0.0357 1989 LEU B CG 7137 C CD1 . LEU B 342 ? 1.9812 1.9614 1.8671 -0.0653 0.2129 0.0059 1989 LEU B CD1 7138 C CD2 . LEU B 342 ? 2.1542 2.1417 2.0298 -0.0412 0.2187 0.0564 1989 LEU B CD2 7139 N N . PRO B 343 ? 1.6820 1.5428 1.5219 -0.0306 0.2717 0.0967 1990 PRO B N 7140 C CA . PRO B 343 ? 1.7220 1.5622 1.5580 -0.0155 0.2805 0.1187 1990 PRO B CA 7141 C C . PRO B 343 ? 1.9322 1.7982 1.7689 0.0013 0.2742 0.1384 1990 PRO B C 7142 O O . PRO B 343 ? 1.7394 1.6054 1.5528 0.0065 0.2739 0.1528 1990 PRO B O 7143 C CB . PRO B 343 ? 1.6280 1.4250 1.4373 -0.0195 0.2925 0.1253 1990 PRO B CB 7144 C CG . PRO B 343 ? 1.6695 1.4664 1.4774 -0.0370 0.2912 0.1065 1990 PRO B CG 7145 C CD . PRO B 343 ? 1.6771 1.5184 1.4940 -0.0398 0.2784 0.0934 1990 PRO B CD 7146 N N . SER B 344 ? 2.5676 2.4582 2.4344 0.0094 0.2693 0.1407 1991 SER B N 7147 C CA . SER B 344 ? 2.8032 2.7083 2.6824 0.0306 0.2694 0.1638 1991 SER B CA 7148 C C . SER B 344 ? 2.6537 2.5605 2.5078 0.0426 0.2668 0.1857 1991 SER B C 7149 O O . SER B 344 ? 2.0454 1.9831 1.8850 0.0371 0.2531 0.1843 1991 SER B O 7150 C CB . SER B 344 ? 2.9486 2.8159 2.8361 0.0422 0.2886 0.1708 1991 SER B CB 7151 O OG . SER B 344 ? 2.6214 2.5105 2.5360 0.0631 0.2909 0.1882 1991 SER B OG 7152 N N . LYS B 345 ? 2.6863 2.5582 2.5348 0.0599 0.2808 0.2059 1992 LYS B N 7153 C CA . LYS B 345 ? 2.3706 2.2310 2.1986 0.0744 0.2826 0.2323 1992 LYS B CA 7154 C C . LYS B 345 ? 2.1998 1.9995 1.9985 0.0662 0.2978 0.2322 1992 LYS B C 7155 O O . LYS B 345 ? 1.9137 1.6773 1.7115 0.0566 0.3083 0.2156 1992 LYS B O 7156 C CB . LYS B 345 ? 2.2528 2.1151 2.1024 0.1024 0.2877 0.2561 1992 LYS B CB 7157 C CG . LYS B 345 ? 2.2648 2.1781 2.1572 0.1094 0.2792 0.2527 1992 LYS B CG 7158 C CD . LYS B 345 ? 2.2142 2.1954 2.1179 0.1064 0.2536 0.2566 1992 LYS B CD 7159 C CE . LYS B 345 ? 1.9225 1.9538 1.8697 0.0998 0.2417 0.2433 1992 LYS B CE 7160 N NZ . LYS B 345 ? 1.6943 1.7349 1.6818 0.1207 0.2524 0.2583 1992 LYS B NZ 7161 N N . ALA B 346 ? 2.1712 1.9625 1.9460 0.0686 0.2976 0.2521 1993 ALA B N 7162 C CA . ALA B 346 ? 2.1231 1.8631 1.8727 0.0573 0.3095 0.2553 1993 ALA B CA 7163 C C . ALA B 346 ? 2.0596 1.7402 1.8088 0.0710 0.3244 0.2663 1993 ALA B C 7164 O O . ALA B 346 ? 2.0647 1.7479 1.8292 0.0948 0.3264 0.2804 1993 ALA B O 7165 C CB . ALA B 346 ? 2.1988 1.9537 1.9253 0.0551 0.3055 0.2764 1993 ALA B CB 7166 N N . GLY B 347 ? 1.9869 1.6144 1.7196 0.0563 0.3344 0.2591 1994 GLY B N 7167 C CA . GLY B 347 ? 2.1096 1.6719 1.8362 0.0665 0.3482 0.2642 1994 GLY B CA 7168 C C . GLY B 347 ? 2.1407 1.6582 1.8569 0.0478 0.3548 0.2396 1994 GLY B C 7169 O O . GLY B 347 ? 2.1312 1.6648 1.8450 0.0247 0.3492 0.2230 1994 GLY B O 7170 N N . ILE B 348 ? 2.0588 1.5201 1.7678 0.0591 0.3666 0.2372 1995 ILE B N 7171 C CA . ILE B 348 ? 1.9409 1.3523 1.6334 0.0425 0.3719 0.2152 1995 ILE B CA 7172 C C . ILE B 348 ? 1.9738 1.3841 1.6715 0.0555 0.3789 0.1969 1995 ILE B C 7173 O O . ILE B 348 ? 2.0420 1.4270 1.7401 0.0807 0.3906 0.2024 1995 ILE B O 7174 C CB . ILE B 348 ? 1.8953 1.2342 1.5680 0.0403 0.3794 0.2249 1995 ILE B CB 7175 C CG1 . ILE B 348 ? 2.0372 1.3177 1.6900 0.0307 0.3852 0.1997 1995 ILE B CG1 7176 C CG2 . ILE B 348 ? 1.7900 1.1124 1.4680 0.0709 0.3872 0.2502 1995 ILE B CG2 7177 C CD1 . ILE B 348 ? 2.2871 1.5001 1.9206 0.0129 0.3863 0.2015 1995 ILE B CD1 7178 N N . TRP B 349 ? 1.8517 1.2912 1.5546 0.0396 0.3730 0.1773 1996 TRP B N 7179 C CA . TRP B 349 ? 1.8300 1.2827 1.5415 0.0496 0.3791 0.1634 1996 TRP B CA 7180 C C . TRP B 349 ? 1.8471 1.2633 1.5361 0.0337 0.3819 0.1410 1996 TRP B C 7181 O O . TRP B 349 ? 1.9028 1.2878 1.5735 0.0129 0.3764 0.1353 1996 TRP B O 7182 C CB . TRP B 349 ? 1.7149 1.2370 1.4551 0.0452 0.3688 0.1616 1996 TRP B CB 7183 C CG . TRP B 349 ? 1.7816 1.3505 1.5442 0.0589 0.3622 0.1798 1996 TRP B CG 7184 C CD1 . TRP B 349 ? 1.9204 1.5211 1.6854 0.0493 0.3496 0.1878 1996 TRP B CD1 7185 C CD2 . TRP B 349 ? 1.7938 1.3895 1.5801 0.0844 0.3666 0.1922 1996 TRP B CD2 7186 N NE1 . TRP B 349 ? 1.8883 1.5326 1.6733 0.0664 0.3436 0.2038 1996 TRP B NE1 7187 C CE2 . TRP B 349 ? 1.8342 1.4777 1.6359 0.0879 0.3533 0.2076 1996 TRP B CE2 7188 C CE3 . TRP B 349 ? 1.9322 1.5193 1.7285 0.1055 0.3812 0.1923 1996 TRP B CE3 7189 C CZ2 . TRP B 349 ? 1.9327 1.6170 1.7626 0.1102 0.3511 0.2238 1996 TRP B CZ2 7190 C CZ3 . TRP B 349 ? 2.0382 1.6667 1.8661 0.1290 0.3819 0.2094 1996 TRP B CZ3 7191 C CH2 . TRP B 349 ? 1.9783 1.6557 1.8243 0.1305 0.3655 0.2253 1996 TRP B CH2 7192 N N . ARG B 350 ? 1.8301 1.2536 1.5211 0.0424 0.3897 0.1300 1997 ARG B N 7193 C CA . ARG B 350 ? 1.8540 1.2498 1.5205 0.0272 0.3905 0.1100 1997 ARG B CA 7194 C C . ARG B 350 ? 1.8163 1.2543 1.4974 0.0173 0.3858 0.1013 1997 ARG B C 7195 O O . ARG B 350 ? 1.6245 1.1115 1.3364 0.0262 0.3864 0.1081 1997 ARG B O 7196 C CB . ARG B 350 ? 2.0146 1.3490 1.6475 0.0416 0.4060 0.1001 1997 ARG B CB 7197 C CG . ARG B 350 ? 2.1288 1.4743 1.7674 0.0694 0.4241 0.1005 1997 ARG B CG 7198 C CD . ARG B 350 ? 2.3885 1.6865 1.9857 0.0725 0.4363 0.0806 1997 ARG B CD 7199 N NE . ARG B 350 ? 2.6055 1.8283 2.1656 0.0806 0.4448 0.0711 1997 ARG B NE 7200 C CZ . ARG B 350 ? 2.8008 1.9779 2.3237 0.0954 0.4614 0.0544 1997 ARG B CZ 7201 N NH1 . ARG B 350 ? 2.8564 2.0576 2.3726 0.1049 0.4733 0.0477 1997 ARG B NH1 7202 N NH2 . ARG B 350 ? 2.9070 2.0114 2.3973 0.1007 0.4669 0.0437 1997 ARG B NH2 7203 N N . VAL B 351 ? 1.9827 1.4002 1.6426 -0.0028 0.3796 0.0874 1998 VAL B N 7204 C CA . VAL B 351 ? 2.0392 1.4821 1.7046 -0.0122 0.3764 0.0796 1998 VAL B CA 7205 C C . VAL B 351 ? 2.1342 1.5332 1.7590 -0.0122 0.3838 0.0662 1998 VAL B C 7206 O O . VAL B 351 ? 2.2542 1.6085 1.8482 -0.0246 0.3784 0.0565 1998 VAL B O 7207 C CB . VAL B 351 ? 2.0128 1.4836 1.6948 -0.0364 0.3591 0.0774 1998 VAL B CB 7208 C CG1 . VAL B 351 ? 1.9015 1.3391 1.5632 -0.0558 0.3495 0.0725 1998 VAL B CG1 7209 C CG2 . VAL B 351 ? 2.0418 1.5346 1.7309 -0.0434 0.3565 0.0722 1998 VAL B CG2 7210 N N . GLU B 352 ? 2.0711 1.4848 1.6959 0.0010 0.3960 0.0659 1999 GLU B N 7211 C CA . GLU B 352 ? 2.0327 1.4076 1.6147 0.0094 0.4089 0.0543 1999 GLU B CA 7212 C C . GLU B 352 ? 1.9985 1.4069 1.5858 0.0085 0.4131 0.0564 1999 GLU B C 7213 O O . GLU B 352 ? 2.0149 1.4731 1.6446 0.0121 0.4144 0.0691 1999 GLU B O 7214 C CB . GLU B 352 ? 2.0243 1.3786 1.6003 0.0394 0.4302 0.0572 1999 GLU B CB 7215 C CG . GLU B 352 ? 2.1894 1.5979 1.8066 0.0592 0.4430 0.0728 1999 GLU B CG 7216 C CD . GLU B 352 ? 2.3648 1.7668 1.9930 0.0899 0.4607 0.0816 1999 GLU B CD 7217 O OE1 . GLU B 352 ? 2.4690 1.8145 2.0641 0.1010 0.4689 0.0731 1999 GLU B OE1 7218 O OE2 . GLU B 352 ? 2.3641 1.8179 2.0367 0.1032 0.4658 0.0976 1999 GLU B OE2 7219 N N . CYS B 353 ? 1.9154 1.2966 1.4596 0.0030 0.4147 0.0448 2000 CYS B N 7220 C CA . CYS B 353 ? 1.8217 1.2315 1.3655 0.0062 0.4232 0.0503 2000 CYS B CA 7221 C C . CYS B 353 ? 1.8159 1.2255 1.3522 0.0352 0.4512 0.0537 2000 CYS B C 7222 O O . CYS B 353 ? 2.0713 1.4364 1.5604 0.0479 0.4642 0.0403 2000 CYS B O 7223 C CB . CYS B 353 ? 1.7915 1.1790 1.2899 -0.0098 0.4136 0.0395 2000 CYS B CB 7224 S SG . CYS B 353 ? 1.8402 1.2467 1.3169 0.0031 0.4336 0.0465 2000 CYS B SG 7225 N N . LEU B 354 ? 1.7093 1.1692 1.2929 0.0456 0.4608 0.0708 2001 LEU B N 7226 C CA . LEU B 354 ? 1.7995 1.2690 1.3903 0.0749 0.4878 0.0778 2001 LEU B CA 7227 C C . LEU B 354 ? 1.9646 1.4208 1.5118 0.0897 0.5119 0.0734 2001 LEU B C 7228 O O . LEU B 354 ? 1.9866 1.4567 1.5419 0.1165 0.5386 0.0806 2001 LEU B O 7229 C CB . LEU B 354 ? 1.7470 1.2802 1.4052 0.0773 0.4882 0.0983 2001 LEU B CB 7230 C CG . LEU B 354 ? 1.7311 1.2784 1.4234 0.0975 0.4946 0.1067 2001 LEU B CG 7231 C CD1 . LEU B 354 ? 1.7968 1.4112 1.5548 0.0932 0.4898 0.1251 2001 LEU B CD1 7232 C CD2 . LEU B 354 ? 1.7664 1.2927 1.4367 0.1296 0.5237 0.1055 2001 LEU B CD2 7233 N N . ILE B 355 ? 1.9884 1.4212 1.4891 0.0736 0.5033 0.0627 2002 ILE B N 7234 C CA . ILE B 355 ? 2.0851 1.5074 1.5386 0.0872 0.5254 0.0586 2002 ILE B CA 7235 C C . ILE B 355 ? 2.1771 1.5344 1.5677 0.1009 0.5348 0.0337 2002 ILE B C 7236 O O . ILE B 355 ? 2.0523 1.3647 1.3972 0.0834 0.5164 0.0145 2002 ILE B O 7237 C CB . ILE B 355 ? 2.1529 1.5897 1.5858 0.0672 0.5148 0.0635 2002 ILE B CB 7238 C CG1 . ILE B 355 ? 2.0133 1.4227 1.4258 0.0391 0.4823 0.0506 2002 ILE B CG1 7239 C CG2 . ILE B 355 ? 2.2612 1.7616 1.7579 0.0620 0.5164 0.0907 2002 ILE B CG2 7240 C CD1 . ILE B 355 ? 2.0342 1.4502 1.4147 0.0234 0.4722 0.0540 2002 ILE B CD1 7241 N N . GLY B 356 ? 2.3673 1.7214 1.7610 0.1326 0.5636 0.0347 2003 GLY B N 7242 C CA . GLY B 356 ? 2.5116 1.8015 1.8543 0.1534 0.5785 0.0115 2003 GLY B CA 7243 C C . GLY B 356 ? 2.4799 1.7033 1.7534 0.1348 0.5606 -0.0171 2003 GLY B C 7244 O O . GLY B 356 ? 2.4591 1.6491 1.7361 0.1189 0.5389 -0.0258 2003 GLY B O 7245 N N . GLU B 357 ? 2.5161 1.7231 1.7270 0.1358 0.5693 -0.0307 2004 GLU B N 7246 C CA . GLU B 357 ? 2.5440 1.6860 1.6807 0.1201 0.5535 -0.0614 2004 GLU B CA 7247 C C . GLU B 357 ? 2.4355 1.5692 1.5923 0.0839 0.5145 -0.0624 2004 GLU B C 7248 O O . GLU B 357 ? 2.4051 1.4834 1.5444 0.0762 0.5026 -0.0809 2004 GLU B O 7249 C CB . GLU B 357 ? 2.7359 1.8833 1.8100 0.1185 0.5602 -0.0683 2004 GLU B CB 7250 C CG . GLU B 357 ? 2.9084 2.0261 1.9237 0.1532 0.5975 -0.0857 2004 GLU B CG 7251 C CD . GLU B 357 ? 3.0220 2.1881 2.0167 0.1641 0.6197 -0.0702 2004 GLU B CD 7252 O OE1 . GLU B 357 ? 2.9765 2.1820 1.9785 0.1400 0.6006 -0.0531 2004 GLU B OE1 7253 O OE2 . GLU B 357 ? 3.0640 2.2294 2.0365 0.1982 0.6580 -0.0733 2004 GLU B OE2 7254 N N . HIS B 358 ? 2.3360 1.5261 1.5349 0.0634 0.4969 -0.0408 2005 HIS B N 7255 C CA . HIS B 358 ? 2.2547 1.4518 1.4838 0.0315 0.4629 -0.0369 2005 HIS B CA 7256 C C . HIS B 358 ? 2.1668 1.3424 1.4311 0.0291 0.4551 -0.0378 2005 HIS B C 7257 O O . HIS B 358 ? 2.0429 1.2063 1.3148 0.0028 0.4289 -0.0416 2005 HIS B O 7258 C CB . HIS B 358 ? 2.3119 1.5782 1.5965 0.0215 0.4555 -0.0099 2005 HIS B CB 7259 C CG . HIS B 358 ? 2.5323 1.8133 1.7910 0.0015 0.4386 -0.0079 2005 HIS B CG 7260 N ND1 . HIS B 358 ? 2.6563 1.9798 1.9601 -0.0191 0.4176 0.0096 2005 HIS B ND1 7261 C CD2 . HIS B 358 ? 2.6037 1.8617 1.7944 -0.0004 0.4386 -0.0210 2005 HIS B CD2 7262 C CE1 . HIS B 358 ? 2.7115 2.0390 1.9798 -0.0318 0.4055 0.0100 2005 HIS B CE1 7263 N NE2 . HIS B 358 ? 2.7238 2.0137 1.9219 -0.0217 0.4169 -0.0081 2005 HIS B NE2 7264 N N . LEU B 359 ? 2.1141 1.2893 1.4017 0.0570 0.4782 -0.0314 2006 LEU B N 7265 C CA . LEU B 359 ? 2.0162 1.1760 1.3386 0.0596 0.4740 -0.0267 2006 LEU B CA 7266 C C . LEU B 359 ? 2.1602 1.2402 1.4361 0.0661 0.4781 -0.0500 2006 LEU B C 7267 O O . LEU B 359 ? 2.2062 1.2539 1.4845 0.0467 0.4593 -0.0549 2006 LEU B O 7268 C CB . LEU B 359 ? 1.8611 1.0638 1.2353 0.0874 0.4947 -0.0054 2006 LEU B CB 7269 C CG . LEU B 359 ? 1.7592 0.9938 1.1939 0.0815 0.4818 0.0135 2006 LEU B CG 7270 C CD1 . LEU B 359 ? 1.7404 0.9657 1.1954 0.1132 0.5013 0.0218 2006 LEU B CD1 7271 C CD2 . LEU B 359 ? 1.7523 0.9611 1.1822 0.0513 0.4545 0.0072 2006 LEU B CD2 7272 N N . HIS B 360 ? 2.2945 1.3425 1.5299 0.0937 0.5042 -0.0640 2007 HIS B N 7273 C CA . HIS B 360 ? 2.5470 1.5125 1.7361 0.1040 0.5116 -0.0890 2007 HIS B CA 7274 C C . HIS B 360 ? 2.5718 1.4947 1.6983 0.0762 0.4916 -0.1160 2007 HIS B C 7275 O O . HIS B 360 ? 2.8415 1.7067 1.9032 0.0861 0.5022 -0.1443 2007 HIS B O 7276 C CB . HIS B 360 ? 2.9006 1.8505 2.0694 0.1468 0.5491 -0.0953 2007 HIS B CB 7277 C CG . HIS B 360 ? 3.0389 2.0448 2.2739 0.1745 0.5682 -0.0658 2007 HIS B CG 7278 N ND1 . HIS B 360 ? 3.1478 2.1395 2.3843 0.2160 0.6009 -0.0657 2007 HIS B ND1 7279 C CD2 . HIS B 360 ? 2.9830 2.0600 2.2856 0.1666 0.5581 -0.0362 2007 HIS B CD2 7280 C CE1 . HIS B 360 ? 2.9776 2.0337 2.2825 0.2313 0.6086 -0.0354 2007 HIS B CE1 7281 N NE2 . HIS B 360 ? 2.9409 2.0478 2.2846 0.2009 0.5823 -0.0185 2007 HIS B NE2 7282 N N . ALA B 361 ? 2.4145 1.3701 1.5629 0.0417 0.4618 -0.1067 2008 ALA B N 7283 C CA . ALA B 361 ? 2.5384 1.4710 1.6439 0.0089 0.4349 -0.1253 2008 ALA B CA 7284 C C . ALA B 361 ? 2.4911 1.4389 1.6424 -0.0229 0.4061 -0.1127 2008 ALA B C 7285 O O . ALA B 361 ? 2.4281 1.3651 1.5607 -0.0548 0.3789 -0.1231 2008 ALA B O 7286 C CB . ALA B 361 ? 2.7099 1.6930 1.7993 0.0044 0.4327 -0.1193 2008 ALA B CB 7287 N N . GLY B 362 ? 2.4803 1.4593 1.6925 -0.0129 0.4128 -0.0890 2009 GLY B N 7288 C CA . GLY B 362 ? 2.3608 1.3580 1.6214 -0.0360 0.3925 -0.0735 2009 GLY B CA 7289 C C . GLY B 362 ? 2.2221 1.2983 1.5345 -0.0447 0.3835 -0.0500 2009 GLY B C 7290 O O . GLY B 362 ? 2.2160 1.3163 1.5275 -0.0685 0.3637 -0.0505 2009 GLY B O 7291 N N . MET B 363 ? 2.1298 1.2470 1.4882 -0.0254 0.3969 -0.0297 2010 MET B N 7292 C CA . MET B 363 ? 2.1575 1.3413 1.5658 -0.0372 0.3853 -0.0107 2010 MET B CA 7293 C C . MET B 363 ? 2.1938 1.3940 1.6471 -0.0342 0.3846 0.0057 2010 MET B C 7294 O O . MET B 363 ? 2.0839 1.3144 1.5676 -0.0536 0.3684 0.0146 2010 MET B O 7295 C CB . MET B 363 ? 2.1204 1.3541 1.5412 -0.0237 0.3966 -0.0015 2010 MET B CB 7296 C CG . MET B 363 ? 2.1287 1.3668 1.5170 -0.0386 0.3866 -0.0097 2010 MET B CG 7297 S SD . MET B 363 ? 2.0658 1.3638 1.4964 -0.0630 0.3637 0.0052 2010 MET B SD 7298 C CE . MET B 363 ? 1.9268 1.1991 1.3066 -0.0875 0.3420 -0.0100 2010 MET B CE 7299 N N . SER B 364 ? 2.3942 1.5726 1.8489 -0.0089 0.4024 0.0096 2011 SER B N 7300 C CA . SER B 364 ? 2.5779 1.7676 2.0693 -0.0035 0.4019 0.0270 2011 SER B CA 7301 C C . SER B 364 ? 2.5548 1.7399 2.0557 -0.0330 0.3815 0.0298 2011 SER B C 7302 O O . SER B 364 ? 2.8300 1.9721 2.3024 -0.0531 0.3712 0.0162 2011 SER B O 7303 C CB . SER B 364 ? 2.6700 1.8098 2.1478 0.0221 0.4193 0.0271 2011 SER B CB 7304 O OG . SER B 364 ? 2.4794 1.6303 1.9904 0.0273 0.4174 0.0474 2011 SER B OG 7305 N N . THR B 365 ? 2.2761 1.5085 1.8178 -0.0359 0.3757 0.0475 2012 THR B N 7306 C CA . THR B 365 ? 2.1310 1.3677 1.6861 -0.0606 0.3604 0.0535 2012 THR B CA 7307 C C . THR B 365 ? 2.0576 1.3373 1.6484 -0.0498 0.3627 0.0734 2012 THR B C 7308 O O . THR B 365 ? 2.1713 1.4946 1.7828 -0.0342 0.3679 0.0787 2012 THR B O 7309 C CB . THR B 365 ? 2.1099 1.3771 1.6707 -0.0851 0.3446 0.0466 2012 THR B CB 7310 O OG1 . THR B 365 ? 2.1900 1.4097 1.7161 -0.1029 0.3362 0.0306 2012 THR B OG1 7311 C CG2 . THR B 365 ? 2.0248 1.3331 1.6202 -0.1013 0.3336 0.0592 2012 THR B CG2 7312 N N . LEU B 366 ? 1.9055 1.1737 1.5032 -0.0588 0.3586 0.0852 2013 LEU B N 7313 C CA . LEU B 366 ? 1.8649 1.1657 1.4874 -0.0444 0.3622 0.1056 2013 LEU B CA 7314 C C . LEU B 366 ? 1.8594 1.2132 1.5071 -0.0601 0.3515 0.1148 2013 LEU B C 7315 O O . LEU B 366 ? 1.9177 1.2758 1.5664 -0.0841 0.3420 0.1087 2013 LEU B O 7316 C CB . LEU B 366 ? 1.8774 1.1281 1.4886 -0.0340 0.3700 0.1177 2013 LEU B CB 7317 C CG . LEU B 366 ? 1.9259 1.1413 1.5233 -0.0045 0.3855 0.1144 2013 LEU B CG 7318 C CD1 . LEU B 366 ? 1.8844 1.0664 1.4525 -0.0053 0.3900 0.0893 2013 LEU B CD1 7319 C CD2 . LEU B 366 ? 2.1326 1.2929 1.7213 0.0033 0.3915 0.1280 2013 LEU B CD2 7320 N N . PHE B 367 ? 1.8586 1.2544 1.5264 -0.0452 0.3531 0.1289 2014 PHE B N 7321 C CA . PHE B 367 ? 1.8708 1.3148 1.5569 -0.0555 0.3454 0.1377 2014 PHE B CA 7322 C C . PHE B 367 ? 1.9994 1.4597 1.6913 -0.0390 0.3484 0.1596 2014 PHE B C 7323 O O . PHE B 367 ? 1.9572 1.4206 1.6534 -0.0156 0.3535 0.1663 2014 PHE B O 7324 C CB . PHE B 367 ? 1.7311 1.2268 1.4366 -0.0598 0.3386 0.1252 2014 PHE B CB 7325 C CG . PHE B 367 ? 1.7868 1.3092 1.5060 -0.0396 0.3415 0.1239 2014 PHE B CG 7326 C CD1 . PHE B 367 ? 1.7627 1.2586 1.4734 -0.0259 0.3505 0.1193 2014 PHE B CD1 7327 C CD2 . PHE B 367 ? 1.7630 1.3394 1.5045 -0.0353 0.3353 0.1265 2014 PHE B CD2 7328 C CE1 . PHE B 367 ? 1.6845 1.2111 1.4140 -0.0086 0.3544 0.1209 2014 PHE B CE1 7329 C CE2 . PHE B 367 ? 1.5804 1.1848 1.3403 -0.0202 0.3361 0.1262 2014 PHE B CE2 7330 C CZ . PHE B 367 ? 1.5923 1.1738 1.3489 -0.0070 0.3462 0.1251 2014 PHE B CZ 7331 N N . LEU B 368 ? 2.0209 1.4933 1.7132 -0.0507 0.3456 0.1728 2015 LEU B N 7332 C CA . LEU B 368 ? 1.9248 1.4195 1.6194 -0.0365 0.3466 0.1954 2015 LEU B CA 7333 C C . LEU B 368 ? 1.8724 1.4323 1.5791 -0.0388 0.3389 0.1925 2015 LEU B C 7334 O O . LEU B 368 ? 1.7911 1.3708 1.4999 -0.0570 0.3361 0.1860 2015 LEU B O 7335 C CB . LEU B 368 ? 1.9748 1.4385 1.6581 -0.0450 0.3508 0.2171 2015 LEU B CB 7336 C CG . LEU B 368 ? 2.0831 1.5721 1.7655 -0.0286 0.3516 0.2451 2015 LEU B CG 7337 C CD1 . LEU B 368 ? 2.1456 1.6058 1.8270 -0.0016 0.3567 0.2588 2015 LEU B CD1 7338 C CD2 . LEU B 368 ? 2.2560 1.7382 1.9306 -0.0431 0.3549 0.2679 2015 LEU B CD2 7339 N N . VAL B 369 ? 1.9008 1.4938 1.6165 -0.0196 0.3356 0.1966 2016 VAL B N 7340 C CA . VAL B 369 ? 1.9548 1.6064 1.6761 -0.0179 0.3270 0.1986 2016 VAL B CA 7341 C C . VAL B 369 ? 1.8536 1.5127 1.5627 -0.0064 0.3275 0.2275 2016 VAL B C 7342 O O . VAL B 369 ? 1.6851 1.3379 1.3966 0.0140 0.3281 0.2441 2016 VAL B O 7343 C CB . VAL B 369 ? 2.1290 1.8189 1.8703 -0.0085 0.3191 0.1842 2016 VAL B CB 7344 C CG1 . VAL B 369 ? 2.1443 1.8334 1.8966 -0.0232 0.3179 0.1588 2016 VAL B CG1 7345 C CG2 . VAL B 369 ? 2.2922 1.9689 2.0430 0.0131 0.3229 0.1939 2016 VAL B CG2 7346 N N . TYR B 370 ? 1.8075 1.4796 1.5040 -0.0190 0.3286 0.2357 2017 TYR B N 7347 C CA . TYR B 370 ? 1.9025 1.5842 1.5840 -0.0103 0.3298 0.2659 2017 TYR B CA 7348 C C . TYR B 370 ? 1.9887 1.7342 1.6664 -0.0056 0.3192 0.2611 2017 TYR B C 7349 O O . TYR B 370 ? 2.0679 1.8417 1.7535 -0.0146 0.3138 0.2339 2017 TYR B O 7350 C CB . TYR B 370 ? 1.8796 1.5422 1.5486 -0.0278 0.3391 0.2805 2017 TYR B CB 7351 C CG . TYR B 370 ? 1.7900 1.4829 1.4609 -0.0475 0.3397 0.2614 2017 TYR B CG 7352 C CD1 . TYR B 370 ? 1.7525 1.4321 1.4383 -0.0609 0.3390 0.2346 2017 TYR B CD1 7353 C CD2 . TYR B 370 ? 1.8808 1.6166 1.5379 -0.0512 0.3419 0.2712 2017 TYR B CD2 7354 C CE1 . TYR B 370 ? 1.8666 1.5741 1.5585 -0.0764 0.3401 0.2190 2017 TYR B CE1 7355 C CE2 . TYR B 370 ? 1.8883 1.6524 1.5494 -0.0663 0.3452 0.2531 2017 TYR B CE2 7356 C CZ . TYR B 370 ? 1.8610 1.6104 1.5422 -0.0784 0.3440 0.2272 2017 TYR B CZ 7357 O OH . TYR B 370 ? 1.8156 1.5928 1.5058 -0.0909 0.3473 0.2103 2017 TYR B OH 7358 N N . SER B 371 ? 1.7530 1.5079 1.9535 -0.1934 0.3413 0.1114 2018 SER B N 7359 C CA . SER B 371 ? 1.7291 1.5071 1.9425 -0.2389 0.3190 0.0901 2018 SER B CA 7360 C C . SER B 371 ? 1.7336 1.4799 1.9005 -0.2283 0.3028 0.0643 2018 SER B C 7361 O O . SER B 371 ? 1.6284 1.3710 1.7742 -0.1920 0.3036 0.0716 2018 SER B O 7362 C CB . SER B 371 ? 1.6944 1.5752 1.9594 -0.2576 0.3024 0.1101 2018 SER B CB 7363 O OG . SER B 371 ? 1.7066 1.6106 1.9670 -0.3026 0.2749 0.0844 2018 SER B OG 7364 N N . ASN B 372 ? 1.8662 1.5820 2.0133 -0.2604 0.2929 0.0336 2019 ASN B N 7365 C CA . ASN B 372 ? 2.0594 1.7628 2.1688 -0.2567 0.2762 0.0099 2019 ASN B CA 7366 C C . ASN B 372 ? 2.0629 1.8153 2.1760 -0.2977 0.2515 -0.0056 2019 ASN B C 7367 O O . ASN B 372 ? 2.2092 1.9504 2.2871 -0.3000 0.2392 -0.0272 2019 ASN B O 7368 C CB . ASN B 372 ? 2.1428 1.7653 2.2098 -0.2423 0.2888 -0.0114 2019 ASN B CB 7369 C CG . ASN B 372 ? 2.4682 2.0327 2.5302 -0.2685 0.3062 -0.0263 2019 ASN B CG 7370 O OD1 . ASN B 372 ? 2.4994 2.0793 2.5877 -0.3052 0.3083 -0.0246 2019 ASN B OD1 7371 N ND2 . ASN B 372 ? 2.6966 2.1937 2.7258 -0.2496 0.3217 -0.0387 2019 ASN B ND2 7372 N N . LYS B 373 ? 2.0137 1.8278 2.1694 -0.3315 0.2439 0.0072 2020 LYS B N 7373 C CA . LYS B 373 ? 1.9904 1.8904 2.1595 -0.3629 0.2137 0.0078 2020 LYS B CA 7374 C C . LYS B 373 ? 1.9054 1.8749 2.0964 -0.3197 0.2060 0.0440 2020 LYS B C 7375 O O . LYS B 373 ? 1.9661 2.0253 2.1793 -0.3325 0.1830 0.0602 2020 LYS B O 7376 C CB . LYS B 373 ? 1.9954 1.9511 2.2046 -0.4214 0.2045 0.0096 2020 LYS B CB 7377 C CG . LYS B 373 ? 2.2328 2.1121 2.4019 -0.4753 0.2092 -0.0354 2020 LYS B CG 7378 C CD . LYS B 373 ? 2.3733 2.3195 2.5606 -0.5509 0.1860 -0.0468 2020 LYS B CD 7379 C CE . LYS B 373 ? 2.5017 2.3487 2.6265 -0.6046 0.1946 -0.1005 2020 LYS B CE 7380 N NZ . LYS B 373 ? 2.4640 2.3680 2.5842 -0.6892 0.1673 -0.1234 2020 LYS B NZ 7381 N N . CYS B 374 ? 1.8610 1.7852 2.0411 -0.2692 0.2274 0.0573 2021 CYS B N 7382 C CA . CYS B 374 ? 1.8017 1.7505 1.9793 -0.2251 0.2290 0.0821 2021 CYS B CA 7383 C C . CYS B 374 ? 1.8278 1.7020 1.9502 -0.2020 0.2340 0.0600 2021 CYS B C 7384 O O . CYS B 374 ? 1.8407 1.6628 1.9466 -0.1727 0.2541 0.0635 2021 CYS B O 7385 C CB . CYS B 374 ? 1.9929 1.9513 2.2010 -0.1885 0.2549 0.1178 2021 CYS B CB 7386 S SG . CYS B 374 ? 2.6228 2.5858 2.8158 -0.1337 0.2672 0.1460 2021 CYS B SG 7387 N N . GLN B 375 ? 1.9144 1.7860 2.0063 -0.2188 0.2162 0.0369 2022 GLN B N 7388 C CA . GLN B 375 ? 1.9905 1.8233 2.0414 -0.1945 0.2186 0.0278 2022 GLN B CA 7389 C C . GLN B 375 ? 1.9714 1.8674 2.0296 -0.1826 0.2067 0.0530 2022 GLN B C 7390 O O . GLN B 375 ? 2.0494 2.0159 2.1284 -0.2060 0.1868 0.0614 2022 GLN B O 7391 C CB . GLN B 375 ? 2.1270 1.9149 2.1389 -0.2143 0.2134 -0.0096 2022 GLN B CB 7392 C CG . GLN B 375 ? 2.0700 1.7861 2.0628 -0.2006 0.2317 -0.0250 2022 GLN B CG 7393 C CD . GLN B 375 ? 2.1356 1.8156 2.0911 -0.2029 0.2324 -0.0517 2022 GLN B CD 7394 O OE1 . GLN B 375 ? 2.1133 1.8111 2.0492 -0.2012 0.2234 -0.0550 2022 GLN B OE1 7395 N NE2 . GLN B 375 ? 2.0799 1.7090 2.0266 -0.2025 0.2471 -0.0666 2022 GLN B NE2 7396 N N . THR B 376 ? 1.7794 1.6523 1.8198 -0.1480 0.2197 0.0677 2023 THR B N 7397 C CA . THR B 376 ? 1.7325 1.6529 1.7753 -0.1291 0.2153 0.0969 2023 THR B CA 7398 C C . THR B 376 ? 1.7609 1.6246 1.7648 -0.1017 0.2324 0.0987 2023 THR B C 7399 O O . THR B 376 ? 1.8668 1.6653 1.8511 -0.0925 0.2501 0.0861 2023 THR B O 7400 C CB . THR B 376 ? 1.7505 1.7367 1.8428 -0.1094 0.2221 0.1407 2023 THR B CB 7401 O OG1 . THR B 376 ? 1.7803 1.8304 1.8793 -0.0943 0.2127 0.1727 2023 THR B OG1 7402 C CG2 . THR B 376 ? 1.7843 1.7172 1.8762 -0.0725 0.2568 0.1568 2023 THR B CG2 7403 N N . PRO B 377 ? 1.7457 1.6359 1.7362 -0.0914 0.2273 0.1158 2024 PRO B N 7404 C CA . PRO B 377 ? 1.7644 1.5929 1.7136 -0.0767 0.2435 0.1108 2024 PRO B CA 7405 C C . PRO B 377 ? 1.8564 1.6365 1.8015 -0.0448 0.2756 0.1317 2024 PRO B C 7406 O O . PRO B 377 ? 2.0639 1.8771 2.0356 -0.0190 0.2871 0.1680 2024 PRO B O 7407 C CB . PRO B 377 ? 1.8366 1.7107 1.7751 -0.0718 0.2326 0.1312 2024 PRO B CB 7408 C CG . PRO B 377 ? 1.7258 1.6874 1.7075 -0.0643 0.2207 0.1663 2024 PRO B CG 7409 C CD . PRO B 377 ? 1.7028 1.6817 1.7159 -0.0895 0.2100 0.1473 2024 PRO B CD 7410 N N . LEU B 378 ? 1.7910 1.4958 1.7017 -0.0470 0.2914 0.1101 2025 LEU B N 7411 C CA . LEU B 378 ? 1.7597 1.4035 1.6507 -0.0230 0.3249 0.1230 2025 LEU B CA 7412 C C . LEU B 378 ? 1.9311 1.5421 1.7964 0.0012 0.3495 0.1483 2025 LEU B C 7413 O O . LEU B 378 ? 1.8716 1.4197 1.7130 0.0224 0.3840 0.1592 2025 LEU B O 7414 C CB . LEU B 378 ? 1.6369 1.2191 1.4963 -0.0402 0.3304 0.0909 2025 LEU B CB 7415 C CG . LEU B 378 ? 1.6479 1.2664 1.5405 -0.0511 0.3141 0.0812 2025 LEU B CG 7416 C CD1 . LEU B 378 ? 1.8606 1.4373 1.7275 -0.0675 0.3129 0.0532 2025 LEU B CD1 7417 C CD2 . LEU B 378 ? 1.5178 1.1583 1.4413 -0.0289 0.3292 0.1085 2025 LEU B CD2 7418 N N . GLY B 379 ? 2.1439 1.7917 2.0089 -0.0019 0.3349 0.1577 2026 GLY B N 7419 C CA . GLY B 379 ? 2.0976 1.7324 1.9465 0.0260 0.3563 0.1929 2026 GLY B CA 7420 C C . GLY B 379 ? 2.1178 1.6740 1.9155 0.0147 0.3744 0.1782 2026 GLY B C 7421 O O . GLY B 379 ? 2.3229 1.8170 2.0927 0.0384 0.4108 0.2010 2026 GLY B O 7422 N N . MET B 380 ? 1.8402 1.3958 1.6258 -0.0213 0.3534 0.1418 2027 MET B N 7423 C CA . MET B 380 ? 1.7585 1.2652 1.5056 -0.0369 0.3657 0.1326 2027 MET B CA 7424 C C . MET B 380 ? 1.7806 1.3389 1.5295 -0.0330 0.3527 0.1507 2027 MET B C 7425 O O . MET B 380 ? 1.5743 1.1023 1.2943 -0.0405 0.3654 0.1535 2027 MET B O 7426 C CB . MET B 380 ? 1.6588 1.1458 1.3952 -0.0737 0.3544 0.0912 2027 MET B CB 7427 C CG . MET B 380 ? 1.8259 1.2291 1.5272 -0.0814 0.3820 0.0809 2027 MET B CG 7428 S SD . MET B 380 ? 1.9519 1.3487 1.6453 -0.1222 0.3656 0.0390 2027 MET B SD 7429 C CE . MET B 380 ? 1.9543 1.3543 1.6342 -0.1526 0.3640 0.0301 2027 MET B CE 7430 N N . ALA B 381 ? 1.9823 1.6212 1.7636 -0.0240 0.3276 0.1637 2028 ALA B N 7431 C CA . ALA B 381 ? 2.1327 1.8376 1.9143 -0.0189 0.3103 0.1850 2028 ALA B CA 7432 C C . ALA B 381 ? 2.2110 1.9013 1.9801 0.0193 0.3380 0.2359 2028 ALA B C 7433 O O . ALA B 381 ? 2.0351 1.6881 1.7701 0.0203 0.3550 0.2451 2028 ALA B O 7434 C CB . ALA B 381 ? 2.0991 1.8933 1.9174 -0.0249 0.2769 0.1857 2028 ALA B CB 7435 N N . SER B 382 ? 2.3208 2.0432 2.1200 0.0524 0.3450 0.2722 2029 SER B N 7436 C CA . SER B 382 ? 2.2437 1.9358 2.0356 0.0995 0.3830 0.3246 2029 SER B CA 7437 C C . SER B 382 ? 2.3515 1.9207 2.1131 0.1001 0.4244 0.3055 2029 SER B C 7438 O O . SER B 382 ? 2.1895 1.7316 1.9526 0.0727 0.4167 0.2636 2029 SER B O 7439 C CB . SER B 382 ? 2.2320 2.0062 2.0746 0.1346 0.3785 0.3679 2029 SER B CB 7440 O OG . SER B 382 ? 2.4010 2.1498 2.2656 0.1322 0.3868 0.3481 2029 SER B OG 7441 N N . GLY B 383 ? 2.7033 2.1944 2.4321 0.1301 0.4702 0.3367 2030 GLY B N 7442 C CA . GLY B 383 ? 3.0576 2.4198 2.7444 0.1254 0.5137 0.3162 2030 GLY B CA 7443 C C . GLY B 383 ? 3.1483 2.4925 2.8517 0.1505 0.5332 0.3215 2030 GLY B C 7444 O O . GLY B 383 ? 3.5709 2.8082 3.2356 0.1714 0.5847 0.3293 2030 GLY B O 7445 N N . HIS B 384 ? 2.7794 2.2208 2.5354 0.1471 0.4966 0.3166 2031 HIS B N 7446 C CA . HIS B 384 ? 2.5061 1.9412 2.2829 0.1703 0.5150 0.3237 2031 HIS B CA 7447 C C . HIS B 384 ? 2.4759 1.8081 2.2065 0.1396 0.5316 0.2733 2031 HIS B C 7448 O O . HIS B 384 ? 2.6562 1.9320 2.3729 0.1624 0.5677 0.2782 2031 HIS B O 7449 C CB . HIS B 384 ? 2.3335 1.8992 2.1794 0.1691 0.4734 0.3331 2031 HIS B CB 7450 C CG . HIS B 384 ? 2.4453 2.0067 2.3146 0.1884 0.4930 0.3385 2031 HIS B CG 7451 N ND1 . HIS B 384 ? 2.5179 2.0512 2.3791 0.1556 0.4824 0.2931 2031 HIS B ND1 7452 C CD2 . HIS B 384 ? 2.4494 2.0273 2.3471 0.2408 0.5280 0.3872 2031 HIS B CD2 7453 C CE1 . HIS B 384 ? 2.3518 1.8835 2.2326 0.1839 0.5087 0.3112 2031 HIS B CE1 7454 N NE2 . HIS B 384 ? 2.3884 1.9473 2.2934 0.2361 0.5378 0.3678 2031 HIS B NE2 7455 N N . ILE B 385 ? 2.2381 1.5511 1.9437 0.0891 0.5065 0.2275 2032 ILE B N 7456 C CA . ILE B 385 ? 2.2671 1.4808 1.9176 0.0560 0.5234 0.1848 2032 ILE B CA 7457 C C . ILE B 385 ? 2.4707 1.5837 2.0639 0.0541 0.5629 0.1909 2032 ILE B C 7458 O O . ILE B 385 ? 2.5487 1.6731 2.1354 0.0273 0.5468 0.1820 2032 ILE B O 7459 C CB . ILE B 385 ? 2.1004 1.3560 1.7593 0.0046 0.4780 0.1398 2032 ILE B CB 7460 C CG1 . ILE B 385 ? 2.0071 1.3453 1.7167 0.0063 0.4458 0.1347 2032 ILE B CG1 7461 C CG2 . ILE B 385 ? 2.1691 1.3403 1.7723 -0.0340 0.4901 0.1000 2032 ILE B CG2 7462 C CD1 . ILE B 385 ? 2.0468 1.4223 1.7661 -0.0345 0.4075 0.0969 2032 ILE B CD1 7463 N N . ARG B 386 ? 2.7059 1.7162 2.2558 0.0831 0.6188 0.2070 2033 ARG B N 7464 C CA . ARG B 386 ? 2.9878 1.8908 2.4821 0.0883 0.6659 0.2211 2033 ARG B CA 7465 C C . ARG B 386 ? 3.0888 1.9257 2.5314 0.0228 0.6615 0.1746 2033 ARG B C 7466 O O . ARG B 386 ? 2.8568 1.7099 2.2940 -0.0239 0.6312 0.1296 2033 ARG B O 7467 C CB . ARG B 386 ? 3.1985 1.9872 2.6489 0.1344 0.7354 0.2459 2033 ARG B CB 7468 C CG . ARG B 386 ? 3.2788 2.0944 2.7609 0.2058 0.7651 0.3165 2033 ARG B CG 7469 C CD . ARG B 386 ? 3.4065 2.1644 2.8787 0.2643 0.8216 0.3462 2033 ARG B CD 7470 N NE . ARG B 386 ? 3.4757 2.3699 3.0332 0.3215 0.8056 0.4017 2033 ARG B NE 7471 C CZ . ARG B 386 ? 3.3435 2.3527 2.9613 0.3129 0.7604 0.3920 2033 ARG B CZ 7472 N NH1 . ARG B 386 ? 3.1500 2.1559 2.7536 0.2559 0.7263 0.3318 2033 ARG B NH1 7473 N NH2 . ARG B 386 ? 3.3307 2.4637 3.0254 0.3607 0.7495 0.4460 2033 ARG B NH2 7474 N N . ASP B 387 ? 3.2757 2.0428 2.6826 0.0205 0.6934 0.1903 2034 ASP B N 7475 C CA . ASP B 387 ? 3.2094 1.9415 2.5832 -0.0433 0.6848 0.1557 2034 ASP B CA 7476 C C . ASP B 387 ? 3.1157 1.7784 2.4371 -0.1059 0.6856 0.0991 2034 ASP B C 7477 O O . ASP B 387 ? 2.9477 1.6493 2.2738 -0.1628 0.6523 0.0673 2034 ASP B O 7478 C CB . ASP B 387 ? 3.4310 2.0854 2.7705 -0.0326 0.7288 0.1872 2034 ASP B CB 7479 C CG . ASP B 387 ? 3.4332 2.1943 2.8208 -0.0248 0.6953 0.2140 2034 ASP B CG 7480 O OD1 . ASP B 387 ? 3.3109 2.2013 2.7576 -0.0177 0.6432 0.2133 2034 ASP B OD1 7481 O OD2 . ASP B 387 ? 3.7455 2.4555 3.1061 -0.0279 0.7237 0.2347 2034 ASP B OD2 7482 N N . PHE B 388 ? 3.0093 1.5776 2.2809 -0.0951 0.7231 0.0883 2035 PHE B N 7483 C CA . PHE B 388 ? 2.8795 1.4067 2.1031 -0.1520 0.7139 0.0347 2035 PHE B CA 7484 C C . PHE B 388 ? 2.7404 1.4020 2.0266 -0.1535 0.6533 0.0218 2035 PHE B C 7485 O O . PHE B 388 ? 2.5488 1.3277 1.9081 -0.1351 0.6138 0.0417 2035 PHE B O 7486 C CB . PHE B 388 ? 2.9284 1.3044 2.0679 -0.1395 0.7773 0.0256 2035 PHE B CB 7487 C CG . PHE B 388 ? 2.9173 1.3209 2.0788 -0.0850 0.7830 0.0413 2035 PHE B CG 7488 C CD1 . PHE B 388 ? 2.9322 1.3960 2.1571 -0.0095 0.7921 0.0966 2035 PHE B CD1 7489 C CD2 . PHE B 388 ? 2.9642 1.3436 2.0844 -0.1112 0.7780 0.0029 2035 PHE B CD2 7490 C CE1 . PHE B 388 ? 2.9206 1.4205 2.1733 0.0373 0.7979 0.1134 2035 PHE B CE1 7491 C CE2 . PHE B 388 ? 2.9696 1.3766 2.1115 -0.0616 0.7860 0.0191 2035 PHE B CE2 7492 C CZ . PHE B 388 ? 2.8968 1.3643 2.1081 0.0120 0.7970 0.0745 2035 PHE B CZ 7493 N N . GLN B 389 ? 2.7704 1.4107 2.0226 -0.1768 0.6478 -0.0111 2036 GLN B N 7494 C CA . GLN B 389 ? 2.6582 1.4116 1.9613 -0.1789 0.5963 -0.0223 2036 GLN B CA 7495 C C . GLN B 389 ? 2.4622 1.3396 1.8280 -0.2084 0.5377 -0.0299 2036 GLN B C 7496 O O . GLN B 389 ? 2.2776 1.2488 1.6940 -0.1999 0.4995 -0.0306 2036 GLN B O 7497 C CB . GLN B 389 ? 2.6544 1.4461 2.0005 -0.1137 0.6037 0.0095 2036 GLN B CB 7498 C CG . GLN B 389 ? 2.6651 1.5073 2.0714 -0.0584 0.6098 0.0588 2036 GLN B CG 7499 C CD . GLN B 389 ? 2.5379 1.4560 2.0044 -0.0068 0.6028 0.0893 2036 GLN B CD 7500 O OE1 . GLN B 389 ? 2.6317 1.5544 2.1221 0.0452 0.6296 0.1326 2036 GLN B OE1 7501 N NE2 . GLN B 389 ? 2.3343 1.3186 1.8289 -0.0214 0.5671 0.0708 2036 GLN B NE2 7502 N N . ILE B 390 ? 2.4568 1.3276 1.8164 -0.2422 0.5362 -0.0345 2037 ILE B N 7503 C CA . ILE B 390 ? 2.3523 1.3265 1.7603 -0.2740 0.4904 -0.0439 2037 ILE B CA 7504 C C . ILE B 390 ? 2.4877 1.4209 1.8486 -0.3436 0.4939 -0.0734 2037 ILE B C 7505 O O . ILE B 390 ? 2.5717 1.4247 1.8944 -0.3609 0.5280 -0.0703 2037 ILE B O 7506 C CB . ILE B 390 ? 2.2889 1.3238 1.7508 -0.2436 0.4823 -0.0130 2037 ILE B CB 7507 C CG1 . ILE B 390 ? 2.1264 1.2032 1.6300 -0.1829 0.4789 0.0166 2037 ILE B CG1 7508 C CG2 . ILE B 390 ? 2.1795 1.3142 1.6872 -0.2718 0.4423 -0.0229 2037 ILE B CG2 7509 C CD1 . ILE B 390 ? 2.0019 1.1321 1.5437 -0.1551 0.4727 0.0474 2037 ILE B CD1 7510 N N . THR B 391 ? 2.4722 1.4609 1.8349 -0.3851 0.4601 -0.0994 2038 THR B N 7511 C CA . THR B 391 ? 2.5836 1.5545 1.9068 -0.4590 0.4568 -0.1270 2038 THR B CA 7512 C C . THR B 391 ? 2.4215 1.5228 1.8100 -0.4859 0.4138 -0.1255 2038 THR B C 7513 O O . THR B 391 ? 2.0769 1.2759 1.5320 -0.4486 0.3851 -0.1096 2038 THR B O 7514 C CB . THR B 391 ? 2.7995 1.7201 2.0516 -0.5002 0.4574 -0.1605 2038 THR B CB 7515 O OG1 . THR B 391 ? 2.6373 1.5017 1.8634 -0.4511 0.4783 -0.1557 2038 THR B OG1 7516 C CG2 . THR B 391 ? 2.9996 1.8091 2.1673 -0.5692 0.4892 -0.1883 2038 THR B CG2 7517 N N . ALA B 392 ? 2.4744 1.5725 1.8414 -0.5520 0.4137 -0.1417 2039 ALA B N 7518 C CA . ALA B 392 ? 2.4300 1.6543 1.8578 -0.5826 0.3782 -0.1382 2039 ALA B CA 7519 C C . ALA B 392 ? 2.3815 1.6338 1.7782 -0.6582 0.3576 -0.1649 2039 ALA B C 7520 O O . ALA B 392 ? 2.4441 1.5969 1.7594 -0.6969 0.3768 -0.1910 2039 ALA B O 7521 C CB . ALA B 392 ? 2.5803 1.8024 2.0307 -0.5907 0.3971 -0.1221 2039 ALA B CB 7522 N N . SER B 393 ? 2.3880 1.7785 1.8481 -0.6785 0.3200 -0.1570 2040 SER B N 7523 C CA . SER B 393 ? 2.6041 2.0546 2.0496 -0.7565 0.2946 -0.1751 2040 SER B CA 7524 C C . SER B 393 ? 2.7134 2.1011 2.1269 -0.8200 0.3220 -0.1863 2040 SER B C 7525 O O . SER B 393 ? 3.1389 2.4916 2.4933 -0.8989 0.3221 -0.2142 2040 SER B O 7526 C CB . SER B 393 ? 2.6753 2.3025 2.2120 -0.7508 0.2527 -0.1523 2040 SER B CB 7527 O OG . SER B 393 ? 2.6330 2.3144 2.2281 -0.7549 0.2607 -0.1333 2040 SER B OG 7528 N N . GLY B 394 ? 2.5036 1.8769 1.9536 -0.7868 0.3459 -0.1640 2041 GLY B N 7529 C CA . GLY B 394 ? 2.5950 1.9025 2.0207 -0.8350 0.3789 -0.1664 2041 GLY B CA 7530 C C . GLY B 394 ? 2.5657 1.8873 2.0437 -0.7719 0.3961 -0.1333 2041 GLY B C 7531 O O . GLY B 394 ? 2.2878 1.6501 1.8052 -0.6990 0.3840 -0.1159 2041 GLY B O 7532 N N . GLN B 395 ? 2.7822 2.0683 2.2558 -0.8036 0.4251 -0.1250 2042 GLN B N 7533 C CA . GLN B 395 ? 2.7985 2.1040 2.3151 -0.7506 0.4416 -0.0925 2042 GLN B CA 7534 C C . GLN B 395 ? 2.8881 2.2274 2.4282 -0.8036 0.4566 -0.0821 2042 GLN B C 7535 O O . GLN B 395 ? 2.9725 2.2972 2.4872 -0.8870 0.4601 -0.1015 2042 GLN B O 7536 C CB . GLN B 395 ? 2.7602 1.9317 2.2261 -0.6962 0.4808 -0.0812 2042 GLN B CB 7537 C CG . GLN B 395 ? 2.9563 1.9696 2.3341 -0.7413 0.5246 -0.0984 2042 GLN B CG 7538 C CD . GLN B 395 ? 3.0625 1.9558 2.3974 -0.6752 0.5637 -0.0801 2042 GLN B CD 7539 O OE1 . GLN B 395 ? 3.1610 1.9983 2.4862 -0.6549 0.5998 -0.0533 2042 GLN B OE1 7540 N NE2 . GLN B 395 ? 3.0563 1.9191 2.3697 -0.6370 0.5573 -0.0894 2042 GLN B NE2 7541 N N . TYR B 396 ? 2.7393 2.1261 2.3254 -0.7575 0.4654 -0.0521 2043 TYR B N 7542 C CA . TYR B 396 ? 2.6957 2.1110 2.3058 -0.7927 0.4871 -0.0345 2043 TYR B CA 7543 C C . TYR B 396 ? 2.7322 2.0064 2.2841 -0.7810 0.5392 -0.0193 2043 TYR B C 7544 O O . TYR B 396 ? 2.5123 1.7714 2.0670 -0.7121 0.5515 0.0059 2043 TYR B O 7545 C CB . TYR B 396 ? 2.5709 2.1271 2.2620 -0.7495 0.4689 -0.0100 2043 TYR B CB 7546 C CG . TYR B 396 ? 2.6797 2.2595 2.3931 -0.7676 0.4982 0.0143 2043 TYR B CG 7547 C CD1 . TYR B 396 ? 2.9100 2.5460 2.6500 -0.8470 0.5014 0.0131 2043 TYR B CD1 7548 C CD2 . TYR B 396 ? 2.6610 2.2130 2.3680 -0.7088 0.5224 0.0401 2043 TYR B CD2 7549 C CE1 . TYR B 396 ? 3.1101 2.7690 2.8727 -0.8652 0.5321 0.0379 2043 TYR B CE1 7550 C CE2 . TYR B 396 ? 3.0001 2.5720 2.7222 -0.7243 0.5522 0.0643 2043 TYR B CE2 7551 C CZ . TYR B 396 ? 3.1564 2.7797 2.9080 -0.8012 0.5589 0.0637 2043 TYR B CZ 7552 O OH . TYR B 396 ? 3.3202 2.9652 3.0894 -0.8173 0.5920 0.0903 2043 TYR B OH 7553 N N . GLY B 397 ? 3.0021 2.1734 2.4982 -0.8509 0.5700 -0.0340 2044 GLY B N 7554 C CA . GLY B 397 ? 3.3295 2.3490 2.7623 -0.8482 0.6278 -0.0182 2044 GLY B CA 7555 C C . GLY B 397 ? 3.4943 2.4033 2.8761 -0.7757 0.6460 -0.0115 2044 GLY B C 7556 O O . GLY B 397 ? 3.6955 2.5714 3.0492 -0.7721 0.6313 -0.0371 2044 GLY B O 7557 N N . GLN B 398 ? 3.4977 2.3543 2.8672 -0.7178 0.6794 0.0261 2045 GLN B N 7558 C CA . GLN B 398 ? 3.4745 2.3129 2.8381 -0.6288 0.6762 0.0451 2045 GLN B CA 7559 C C . GLN B 398 ? 3.1359 2.1342 2.5747 -0.5853 0.6281 0.0546 2045 GLN B C 7560 O O . GLN B 398 ? 3.0329 2.1238 2.5163 -0.6088 0.6171 0.0600 2045 GLN B O 7561 C CB . GLN B 398 ? 3.5379 2.2640 2.8561 -0.5820 0.7293 0.0859 2045 GLN B CB 7562 C CG . GLN B 398 ? 3.6729 2.3542 2.9716 -0.5049 0.7329 0.1007 2045 GLN B CG 7563 C CD . GLN B 398 ? 3.6590 2.3704 2.9723 -0.4281 0.7407 0.1517 2045 GLN B CD 7564 O OE1 . GLN B 398 ? 3.7885 2.4201 3.0668 -0.4148 0.7874 0.1872 2045 GLN B OE1 7565 N NE2 . GLN B 398 ? 3.3465 2.1722 2.7077 -0.3792 0.6955 0.1565 2045 GLN B NE2 7566 N N . TRP B 399 ? 2.8392 1.8664 2.2907 -0.5244 0.6035 0.0563 2046 TRP B N 7567 C CA . TRP B 399 ? 2.6153 1.7784 2.1293 -0.4936 0.5573 0.0537 2046 TRP B CA 7568 C C . TRP B 399 ? 2.4565 1.6228 1.9704 -0.4935 0.5299 0.0253 2046 TRP B C 7569 O O . TRP B 399 ? 2.1967 1.4550 1.7519 -0.5090 0.4935 0.0063 2046 TRP B O 7570 C CB . TRP B 399 ? 2.6979 1.9671 2.2620 -0.5355 0.5419 0.0486 2046 TRP B CB 7571 C CG . TRP B 399 ? 2.7050 2.0710 2.3114 -0.4915 0.5293 0.0686 2046 TRP B CG 7572 C CD1 . TRP B 399 ? 2.6851 2.1693 2.3478 -0.4859 0.4991 0.0604 2046 TRP B CD1 7573 C CD2 . TRP B 399 ? 2.6450 1.9919 2.2325 -0.4469 0.5497 0.1000 2046 TRP B CD2 7574 N NE1 . TRP B 399 ? 2.4581 1.9868 2.1319 -0.4430 0.5023 0.0795 2046 TRP B NE1 7575 C CE2 . TRP B 399 ? 2.5499 2.0014 2.1772 -0.4208 0.5298 0.1035 2046 TRP B CE2 7576 C CE3 . TRP B 399 ? 2.6456 1.8969 2.1830 -0.4236 0.5846 0.1280 2046 TRP B CE3 7577 C CZ2 . TRP B 399 ? 2.6465 2.1105 2.2587 -0.3798 0.5402 0.1289 2046 TRP B CZ2 7578 C CZ3 . TRP B 399 ? 2.7000 1.9749 2.2300 -0.3795 0.5925 0.1593 2046 TRP B CZ3 7579 C CH2 . TRP B 399 ? 2.8251 2.2064 2.3893 -0.3611 0.5687 0.1574 2046 TRP B CH2 7580 N N . ALA B 400 ? 2.5924 1.6525 2.0567 -0.4726 0.5530 0.0266 2047 ALA B N 7581 C CA . ALA B 400 ? 2.8434 1.8763 2.2894 -0.4755 0.5397 0.0007 2047 ALA B CA 7582 C C . ALA B 400 ? 2.7337 1.8399 2.2194 -0.4171 0.5062 0.0055 2047 ALA B C 7583 O O . ALA B 400 ? 2.5382 1.6972 2.0547 -0.3711 0.4982 0.0298 2047 ALA B O 7584 C CB . ALA B 400 ? 3.0863 1.9658 2.4587 -0.4734 0.5874 0.0019 2047 ALA B CB 7585 N N . PRO B 401 ? 2.5947 1.7042 2.0755 -0.4235 0.4868 -0.0187 2048 PRO B N 7586 C CA . PRO B 401 ? 2.3414 1.4724 1.8395 -0.3685 0.4717 -0.0119 2048 PRO B CA 7587 C C . PRO B 401 ? 2.3800 1.4026 1.8324 -0.3332 0.5127 0.0071 2048 PRO B C 7588 O O . PRO B 401 ? 2.3804 1.2939 1.7754 -0.3594 0.5521 0.0027 2048 PRO B O 7589 C CB . PRO B 401 ? 2.3270 1.4767 1.8209 -0.3954 0.4481 -0.0419 2048 PRO B CB 7590 C CG . PRO B 401 ? 2.4704 1.5487 1.9109 -0.4601 0.4677 -0.0641 2048 PRO B CG 7591 C CD . PRO B 401 ? 2.5333 1.6290 1.9886 -0.4861 0.4784 -0.0522 2048 PRO B CD 7592 N N . LYS B 402 ? 2.3085 1.3605 1.7858 -0.2751 0.5059 0.0289 2049 LYS B N 7593 C CA . LYS B 402 ? 2.4593 1.4512 1.9172 -0.2264 0.5414 0.0653 2049 LYS B CA 7594 C C . LYS B 402 ? 2.4072 1.4823 1.9044 -0.2024 0.5239 0.0921 2049 LYS B C 7595 O O . LYS B 402 ? 2.3350 1.4755 1.8662 -0.1613 0.5037 0.1098 2049 LYS B O 7596 C CB . LYS B 402 ? 2.5136 1.3722 1.9063 -0.2446 0.5957 0.0707 2049 LYS B CB 7597 C CG . LYS B 402 ? 2.4976 1.3081 1.8781 -0.1864 0.6344 0.1200 2049 LYS B CG 7598 C CD . LYS B 402 ? 2.6534 1.3504 1.9794 -0.2074 0.6855 0.1315 2049 LYS B CD 7599 C CE . LYS B 402 ? 2.7837 1.4816 2.1161 -0.1486 0.7099 0.1897 2049 LYS B CE 7600 N NZ . LYS B 402 ? 3.0098 1.5603 2.2783 -0.1470 0.7779 0.2121 2049 LYS B NZ 7601 N N . LEU B 403 ? 2.4452 1.5210 1.9357 -0.2328 0.5312 0.0933 2050 LEU B N 7602 C CA . LEU B 403 ? 2.4669 1.6254 1.9876 -0.2179 0.5138 0.1124 2050 LEU B CA 7603 C C . LEU B 403 ? 2.4929 1.7613 2.0629 -0.2179 0.4662 0.0913 2050 LEU B C 7604 O O . LEU B 403 ? 2.4136 1.7516 2.0043 -0.2074 0.4500 0.0996 2050 LEU B O 7605 C CB . LEU B 403 ? 2.4787 1.6176 1.9836 -0.2565 0.5336 0.1145 2050 LEU B CB 7606 C CG . LEU B 403 ? 2.6851 1.7172 2.1405 -0.2612 0.5855 0.1403 2050 LEU B CG 7607 C CD1 . LEU B 403 ? 2.6964 1.7382 2.1513 -0.3109 0.5949 0.1349 2050 LEU B CD1 7608 C CD2 . LEU B 403 ? 2.7096 1.7262 2.1522 -0.2002 0.6066 0.1907 2050 LEU B CD2 7609 N N . ALA B 404 ? 2.4914 1.7656 2.0728 -0.2274 0.4486 0.0653 2051 ALA B N 7610 C CA . ALA B 404 ? 2.2299 1.5893 1.8534 -0.2294 0.4100 0.0441 2051 ALA B CA 7611 C C . ALA B 404 ? 1.9893 1.4004 1.6394 -0.1883 0.3889 0.0545 2051 ALA B C 7612 O O . ALA B 404 ? 1.7795 1.2474 1.4597 -0.1889 0.3624 0.0376 2051 ALA B O 7613 C CB . ALA B 404 ? 2.1436 1.4873 1.7634 -0.2587 0.4017 0.0161 2051 ALA B CB 7614 N N . ARG B 405 ? 2.0060 1.3998 1.6456 -0.1541 0.4020 0.0844 2052 ARG B N 7615 C CA . ARG B 405 ? 1.9716 1.4217 1.6374 -0.1219 0.3810 0.0967 2052 ARG B CA 7616 C C . ARG B 405 ? 1.8927 1.4156 1.5732 -0.1245 0.3572 0.0924 2052 ARG B C 7617 O O . ARG B 405 ? 1.8596 1.3854 1.5244 -0.1341 0.3657 0.0975 2052 ARG B O 7618 C CB . ARG B 405 ? 2.1553 1.5856 1.8111 -0.0826 0.4009 0.1380 2052 ARG B CB 7619 C CG . ARG B 405 ? 2.4350 1.7686 2.0504 -0.0782 0.4452 0.1563 2052 ARG B CG 7620 C CD . ARG B 405 ? 2.2914 1.5929 1.9008 -0.0307 0.4727 0.1977 2052 ARG B CD 7621 N NE . ARG B 405 ? 2.1863 1.3897 1.7660 -0.0366 0.5052 0.1842 2052 ARG B NE 7622 C CZ . ARG B 405 ? 2.1200 1.3246 1.7117 -0.0382 0.4961 0.1635 2052 ARG B CZ 7623 N NH1 . ARG B 405 ? 1.9728 1.2693 1.6111 -0.0327 0.4576 0.1574 2052 ARG B NH1 7624 N NH2 . ARG B 405 ? 2.2362 1.3446 1.7878 -0.0470 0.5281 0.1485 2052 ARG B NH2 7625 N N . LEU B 406 ? 2.0248 1.6007 1.7308 -0.1174 0.3309 0.0826 2053 LEU B N 7626 C CA . LEU B 406 ? 2.0260 1.6604 1.7358 -0.1219 0.3106 0.0732 2053 LEU B CA 7627 C C . LEU B 406 ? 2.0515 1.7099 1.7403 -0.1054 0.3129 0.1041 2053 LEU B C 7628 O O . LEU B 406 ? 1.9766 1.6381 1.6669 -0.0813 0.3170 0.1357 2053 LEU B O 7629 C CB . LEU B 406 ? 1.9009 1.5740 1.6360 -0.1221 0.2858 0.0557 2053 LEU B CB 7630 C CG . LEU B 406 ? 1.8377 1.5389 1.5715 -0.1378 0.2739 0.0275 2053 LEU B CG 7631 C CD1 . LEU B 406 ? 1.7686 1.4724 1.5275 -0.1438 0.2623 0.0035 2053 LEU B CD1 7632 C CD2 . LEU B 406 ? 1.7701 1.5124 1.4814 -0.1370 0.2624 0.0330 2053 LEU B CD2 7633 N N . HIS B 407 ? 2.1586 1.8370 1.8278 -0.1161 0.3127 0.0977 2054 HIS B N 7634 C CA . HIS B 407 ? 2.2078 1.9172 1.8481 -0.1043 0.3126 0.1242 2054 HIS B CA 7635 C C . HIS B 407 ? 2.1841 1.8549 1.8010 -0.0901 0.3417 0.1615 2054 HIS B C 7636 O O . HIS B 407 ? 2.1804 1.8802 1.7714 -0.0759 0.3423 0.1903 2054 HIS B O 7637 C CB . HIS B 407 ? 2.2518 2.0202 1.8976 -0.0913 0.2864 0.1382 2054 HIS B CB 7638 C CG . HIS B 407 ? 2.2732 2.0838 1.9150 -0.1120 0.2610 0.1038 2054 HIS B CG 7639 N ND1 . HIS B 407 ? 2.1390 1.9705 1.8075 -0.1204 0.2401 0.0851 2054 HIS B ND1 7640 C CD2 . HIS B 407 ? 2.3639 2.1885 1.9732 -0.1272 0.2589 0.0827 2054 HIS B CD2 7641 C CE1 . HIS B 407 ? 2.2581 2.1088 1.9082 -0.1417 0.2263 0.0528 2054 HIS B CE1 7642 N NE2 . HIS B 407 ? 2.5264 2.3723 2.1385 -0.1446 0.2381 0.0500 2054 HIS B NE2 7643 N N . TYR B 408 ? 2.1313 1.7341 1.7512 -0.0959 0.3671 0.1616 2055 TYR B N 7644 C CA . TYR B 408 ? 2.2372 1.7842 1.8293 -0.0856 0.4020 0.1956 2055 TYR B CA 7645 C C . TYR B 408 ? 2.5080 2.0757 2.0734 -0.0935 0.4098 0.2049 2055 TYR B C 7646 O O . TYR B 408 ? 2.6458 2.2310 2.2157 -0.1202 0.4054 0.1756 2055 TYR B O 7647 C CB . TYR B 408 ? 2.0713 1.5331 1.6600 -0.1048 0.4295 0.1833 2055 TYR B CB 7648 C CG . TYR B 408 ? 2.1413 1.5286 1.7019 -0.0812 0.4680 0.2225 2055 TYR B CG 7649 C CD1 . TYR B 408 ? 2.3069 1.7025 1.8729 -0.0372 0.4704 0.2572 2055 TYR B CD1 7650 C CD2 . TYR B 408 ? 2.3701 1.6793 1.8999 -0.1016 0.5057 0.2285 2055 TYR B CD2 7651 C CE1 . TYR B 408 ? 2.7779 2.1007 2.3182 -0.0061 0.5127 0.2992 2055 TYR B CE1 7652 C CE2 . TYR B 408 ? 2.8090 2.0332 2.3064 -0.0769 0.5489 0.2663 2055 TYR B CE2 7653 C CZ . TYR B 408 ? 2.9684 2.1972 2.4706 -0.0251 0.5541 0.3029 2055 TYR B CZ 7654 O OH . TYR B 408 ? 3.0080 2.1487 2.4788 0.0085 0.6033 0.3456 2055 TYR B OH 7655 N N . SER B 409 ? 2.5908 2.1634 2.1293 -0.0661 0.4222 0.2495 2056 SER B N 7656 C CA . SER B 409 ? 2.5795 2.1781 2.0855 -0.0679 0.4293 0.2648 2056 SER B CA 7657 C C . SER B 409 ? 2.7169 2.2404 2.2004 -0.0761 0.4738 0.2859 2056 SER B C 7658 O O . SER B 409 ? 2.8408 2.2895 2.3310 -0.0876 0.4971 0.2808 2056 SER B O 7659 C CB . SER B 409 ? 2.6555 2.3145 2.1411 -0.0342 0.4139 0.3055 2056 SER B CB 7660 O OG . SER B 409 ? 2.8492 2.4779 2.3411 0.0008 0.4305 0.3487 2056 SER B OG 7661 N N . GLY B 410 ? 2.9206 2.4598 2.3714 -0.0728 0.4875 0.3095 2057 GLY B N 7662 C CA . GLY B 410 ? 3.1855 2.6617 2.6181 -0.0933 0.5294 0.3208 2057 GLY B CA 7663 C C . GLY B 410 ? 3.2853 2.7763 2.7449 -0.1378 0.5238 0.2728 2057 GLY B C 7664 O O . GLY B 410 ? 3.4151 2.9448 2.9061 -0.1470 0.4930 0.2347 2057 GLY B O 7665 N N . SER B 411 ? 3.2109 2.6774 2.6613 -0.1642 0.5548 0.2782 2058 SER B N 7666 C CA . SER B 411 ? 3.0879 2.5757 2.5735 -0.2060 0.5522 0.2399 2058 SER B CA 7667 C C . SER B 411 ? 3.1497 2.5645 2.6488 -0.2388 0.5687 0.2291 2058 SER B C 7668 O O . SER B 411 ? 3.3704 2.8064 2.9044 -0.2747 0.5590 0.1968 2058 SER B O 7669 C CB . SER B 411 ? 3.0391 2.5578 2.5166 -0.2220 0.5747 0.2485 2058 SER B CB 7670 O OG . SER B 411 ? 3.1988 2.6677 2.6840 -0.2620 0.6085 0.2545 2058 SER B OG 7671 N N . ILE B 412 ? 3.0814 2.4110 2.5492 -0.2253 0.5953 0.2576 2059 ILE B N 7672 C CA . ILE B 412 ? 3.1763 2.4218 2.6427 -0.2487 0.6087 0.2425 2059 ILE B CA 7673 C C . ILE B 412 ? 3.1710 2.4358 2.6583 -0.2281 0.5743 0.2197 2059 ILE B C 7674 O O . ILE B 412 ? 3.2895 2.5124 2.7601 -0.1910 0.5813 0.2408 2059 ILE B O 7675 C CB . ILE B 412 ? 3.2299 2.3573 2.6484 -0.2415 0.6607 0.2804 2059 ILE B CB 7676 C CG1 . ILE B 412 ? 3.1851 2.2101 2.5881 -0.2615 0.6784 0.2607 2059 ILE B CG1 7677 C CG2 . ILE B 412 ? 3.1386 2.2736 2.5298 -0.1801 0.6710 0.3339 2059 ILE B CG2 7678 C CD1 . ILE B 412 ? 2.9239 1.9234 2.3217 -0.2125 0.6714 0.2691 2059 ILE B CD1 7679 N N . ASN B 413 ? 2.9630 2.2939 2.4891 -0.2492 0.5403 0.1809 2060 ASN B N 7680 C CA . ASN B 413 ? 2.7264 2.0873 2.2752 -0.2298 0.5064 0.1601 2060 ASN B CA 7681 C C . ASN B 413 ? 2.5664 1.9717 2.1531 -0.2611 0.4796 0.1188 2060 ASN B C 7682 O O . ASN B 413 ? 2.4599 1.9126 2.0685 -0.2896 0.4769 0.1063 2060 ASN B O 7683 C CB . ASN B 413 ? 2.7053 2.1336 2.2580 -0.1873 0.4819 0.1738 2060 ASN B CB 7684 C CG . ASN B 413 ? 2.7148 2.2245 2.2988 -0.1948 0.4494 0.1424 2060 ASN B CG 7685 O OD1 . ASN B 413 ? 2.5589 2.0884 2.1666 -0.1910 0.4246 0.1201 2060 ASN B OD1 7686 N ND2 . ASN B 413 ? 2.8670 2.4186 2.4487 -0.2033 0.4542 0.1421 2060 ASN B ND2 7687 N N . ALA B 414 ? 2.3478 1.7428 1.9433 -0.2507 0.4619 0.1034 2061 ALA B N 7688 C CA . ALA B 414 ? 2.1465 1.5787 1.7735 -0.2707 0.4355 0.0700 2061 ALA B CA 7689 C C . ALA B 414 ? 2.1619 1.5733 1.7896 -0.3229 0.4417 0.0497 2061 ALA B C 7690 O O . ALA B 414 ? 2.2394 1.6428 1.8613 -0.3564 0.4605 0.0543 2061 ALA B O 7691 C CB . ALA B 414 ? 2.0710 1.5930 1.7331 -0.2589 0.4091 0.0589 2061 ALA B CB 7692 N N . TRP B 415 ? 2.1208 1.5294 1.7548 -0.3327 0.4247 0.0281 2062 TRP B N 7693 C CA . TRP B 415 ? 2.0996 1.5085 1.7340 -0.3856 0.4209 0.0064 2062 TRP B CA 7694 C C . TRP B 415 ? 1.9685 1.4733 1.6483 -0.4122 0.4080 0.0036 2062 TRP B C 7695 O O . TRP B 415 ? 1.9440 1.5165 1.6573 -0.3816 0.3966 0.0106 2062 TRP B O 7696 C CB . TRP B 415 ? 2.0401 1.4465 1.6737 -0.3820 0.4000 -0.0132 2062 TRP B CB 7697 C CG . TRP B 415 ? 2.1690 1.5925 1.8007 -0.4370 0.3890 -0.0349 2062 TRP B CG 7698 C CD1 . TRP B 415 ? 2.3331 1.7032 1.9283 -0.4940 0.4077 -0.0450 2062 TRP B CD1 7699 C CD2 . TRP B 415 ? 2.0313 1.5352 1.6970 -0.4441 0.3563 -0.0473 2062 TRP B CD2 7700 N NE1 . TRP B 415 ? 2.2257 1.6481 1.8302 -0.5403 0.3838 -0.0646 2062 TRP B NE1 7701 C CE2 . TRP B 415 ? 2.0724 1.5811 1.7220 -0.5070 0.3520 -0.0632 2062 TRP B CE2 7702 C CE3 . TRP B 415 ? 1.8656 1.4353 1.5709 -0.4050 0.3318 -0.0452 2062 TRP B CE3 7703 C CZ2 . TRP B 415 ? 1.9282 1.5188 1.6034 -0.5273 0.3206 -0.0724 2062 TRP B CZ2 7704 C CZ3 . TRP B 415 ? 1.8884 1.5260 1.6181 -0.4211 0.3063 -0.0533 2062 TRP B CZ3 7705 C CH2 . TRP B 415 ? 1.8597 1.5138 1.5758 -0.4799 0.2991 -0.0647 2062 TRP B CH2 7706 N N . SER B 416 ? 1.9120 1.4217 1.5910 -0.4697 0.4130 -0.0055 2063 SER B N 7707 C CA . SER B 416 ? 1.8918 1.5105 1.6243 -0.4974 0.3982 -0.0055 2063 SER B CA 7708 C C . SER B 416 ? 2.0332 1.6609 1.7620 -0.5723 0.3982 -0.0174 2063 SER B C 7709 O O . SER B 416 ? 2.1315 1.6739 1.8154 -0.6112 0.4253 -0.0199 2063 SER B O 7710 C CB . SER B 416 ? 1.8868 1.5475 1.6429 -0.4781 0.4146 0.0159 2063 SER B CB 7711 O OG . SER B 416 ? 1.7875 1.5619 1.6026 -0.4882 0.4034 0.0203 2063 SER B OG 7712 N N . THR B 417 ? 2.0347 1.7656 1.8088 -0.5934 0.3689 -0.0231 2064 THR B N 7713 C CA . THR B 417 ? 2.1438 1.9199 1.9269 -0.6701 0.3619 -0.0309 2064 THR B CA 7714 C C . THR B 417 ? 2.2122 2.1358 2.0751 -0.6708 0.3484 -0.0113 2064 THR B C 7715 O O . THR B 417 ? 2.2468 2.2400 2.1526 -0.6157 0.3336 -0.0007 2064 THR B O 7716 C CB . THR B 417 ? 2.1614 1.9548 1.9290 -0.7007 0.3312 -0.0519 2064 THR B CB 7717 O OG1 . THR B 417 ? 2.3017 2.0435 2.0443 -0.6455 0.3231 -0.0592 2064 THR B OG1 7718 C CG2 . THR B 417 ? 2.2931 2.0103 2.0001 -0.7821 0.3424 -0.0748 2064 THR B CG2 7719 N N . LYS B 418 ? 2.3703 2.3435 2.2548 -0.7338 0.3556 -0.0054 2065 LYS B N 7720 C CA . LYS B 418 ? 2.4865 2.6213 2.4551 -0.7390 0.3391 0.0159 2065 LYS B CA 7721 C C . LYS B 418 ? 2.5493 2.7624 2.5314 -0.7930 0.3019 0.0060 2065 LYS B C 7722 O O . LYS B 418 ? 2.6947 3.0586 2.7506 -0.8021 0.2829 0.0275 2065 LYS B O 7723 C CB . LYS B 418 ? 2.5553 2.7391 2.5616 -0.7658 0.3670 0.0376 2065 LYS B CB 7724 C CG . LYS B 418 ? 2.7373 2.8741 2.7116 -0.8574 0.3819 0.0272 2065 LYS B CG 7725 C CD . LYS B 418 ? 2.7224 2.9602 2.7598 -0.8919 0.4009 0.0543 2065 LYS B CD 7726 C CE . LYS B 418 ? 2.7272 2.9256 2.7636 -0.8355 0.4403 0.0755 2065 LYS B CE 7727 N NZ . LYS B 418 ? 2.8388 3.0654 2.8982 -0.8909 0.4720 0.0943 2065 LYS B NZ 7728 N N . GLU B 419 ? 2.5279 2.6430 2.4373 -0.8252 0.2927 -0.0239 2066 GLU B N 7729 C CA . GLU B 419 ? 2.6184 2.8019 2.5258 -0.8727 0.2542 -0.0360 2066 GLU B CA 7730 C C . GLU B 419 ? 2.5319 2.8215 2.4944 -0.8055 0.2250 -0.0164 2066 GLU B C 7731 O O . GLU B 419 ? 2.3956 2.6355 2.3560 -0.7281 0.2353 -0.0120 2066 GLU B O 7732 C CB . GLU B 419 ? 2.8184 2.8592 2.6243 -0.9141 0.2568 -0.0744 2066 GLU B CB 7733 C CG . GLU B 419 ? 2.8731 2.8457 2.6416 -0.8492 0.2492 -0.0844 2066 GLU B CG 7734 C CD . GLU B 419 ? 3.0737 2.9541 2.7531 -0.8973 0.2427 -0.1195 2066 GLU B CD 7735 O OE1 . GLU B 419 ? 3.3174 3.1084 2.9351 -0.9682 0.2633 -0.1432 2066 GLU B OE1 7736 O OE2 . GLU B 419 ? 2.8487 2.7408 2.5156 -0.8646 0.2205 -0.1237 2066 GLU B OE2 7737 N N . PRO B 420 ? 2.5361 2.9749 2.5487 -0.8363 0.1897 -0.0018 2067 PRO B N 7738 C CA . PRO B 420 ? 2.3182 2.8839 2.4005 -0.7725 0.1676 0.0294 2067 PRO B CA 7739 C C . PRO B 420 ? 2.0813 2.5718 2.1299 -0.7012 0.1635 0.0217 2067 PRO B C 7740 O O . PRO B 420 ? 1.8093 2.2625 1.8752 -0.6289 0.1854 0.0312 2067 PRO B O 7741 C CB . PRO B 420 ? 2.4461 3.1580 2.5582 -0.8378 0.1268 0.0398 2067 PRO B CB 7742 C CG . PRO B 420 ? 2.5945 3.3011 2.6918 -0.9332 0.1348 0.0252 2067 PRO B CG 7743 C CD . PRO B 420 ? 2.6720 3.1716 2.6765 -0.9393 0.1696 -0.0121 2067 PRO B CD 7744 N N . PHE B 421 ? 2.0493 2.5199 2.0481 -0.7256 0.1368 0.0044 2068 PHE B N 7745 C CA . PHE B 421 ? 2.0292 2.4244 1.9897 -0.6679 0.1335 -0.0041 2068 PHE B CA 7746 C C . PHE B 421 ? 2.0676 2.2881 1.9327 -0.6829 0.1521 -0.0423 2068 PHE B C 7747 O O . PHE B 421 ? 2.0753 2.2493 1.8741 -0.7318 0.1402 -0.0669 2068 PHE B O 7748 C CB . PHE B 421 ? 1.9735 2.4672 1.9435 -0.6689 0.0954 0.0096 2068 PHE B CB 7749 C CG . PHE B 421 ? 2.0682 2.7499 2.1272 -0.6728 0.0736 0.0502 2068 PHE B CG 7750 C CD1 . PHE B 421 ? 2.0885 2.8399 2.2298 -0.6097 0.0925 0.0849 2068 PHE B CD1 7751 C CD2 . PHE B 421 ? 2.2472 3.0412 2.3062 -0.7393 0.0352 0.0554 2068 PHE B CD2 7752 C CE1 . PHE B 421 ? 2.2495 3.1799 2.4783 -0.6064 0.0777 0.1284 2068 PHE B CE1 7753 C CE2 . PHE B 421 ? 2.3207 3.3079 2.4709 -0.7407 0.0136 0.1004 2068 PHE B CE2 7754 C CZ . PHE B 421 ? 2.3152 3.3713 2.5542 -0.6705 0.0370 0.1392 2068 PHE B CZ 7755 N N . SER B 422 ? 2.0962 2.2220 1.9530 -0.6383 0.1834 -0.0451 2069 SER B N 7756 C CA . SER B 422 ? 2.1110 2.0813 1.8896 -0.6397 0.2064 -0.0714 2069 SER B CA 7757 C C . SER B 422 ? 2.0168 1.9386 1.7763 -0.5806 0.2032 -0.0734 2069 SER B C 7758 O O . SER B 422 ? 1.9516 1.9540 1.7505 -0.5465 0.1820 -0.0570 2069 SER B O 7759 C CB . SER B 422 ? 2.2814 2.1850 2.0612 -0.6240 0.2409 -0.0677 2069 SER B CB 7760 O OG . SER B 422 ? 2.3129 2.2749 2.1543 -0.5633 0.2446 -0.0444 2069 SER B OG 7761 N N . TRP B 423 ? 1.9189 1.7097 1.6194 -0.5684 0.2277 -0.0899 2070 TRP B N 7762 C CA . TRP B 423 ? 1.7481 1.4804 1.4295 -0.5145 0.2321 -0.0910 2070 TRP B CA 7763 C C . TRP B 423 ? 1.7218 1.3248 1.3547 -0.4992 0.2662 -0.0996 2070 TRP B C 7764 O O . TRP B 423 ? 1.8549 1.3953 1.4517 -0.5357 0.2875 -0.1088 2070 TRP B O 7765 C CB . TRP B 423 ? 1.8438 1.5833 1.4889 -0.5302 0.2119 -0.1016 2070 TRP B CB 7766 C CG . TRP B 423 ? 2.0373 1.7026 1.5999 -0.5944 0.2185 -0.1303 2070 TRP B CG 7767 C CD1 . TRP B 423 ? 2.1541 1.8749 1.6956 -0.6635 0.1957 -0.1423 2070 TRP B CD1 7768 C CD2 . TRP B 423 ? 2.1634 1.6843 1.6488 -0.5961 0.2517 -0.1508 2070 TRP B CD2 7769 N NE1 . TRP B 423 ? 2.3164 1.9235 1.7633 -0.7135 0.2139 -0.1749 2070 TRP B NE1 7770 C CE2 . TRP B 423 ? 2.3897 1.8686 1.8010 -0.6690 0.2516 -0.1794 2070 TRP B CE2 7771 C CE3 . TRP B 423 ? 2.0694 1.4960 1.5413 -0.5433 0.2830 -0.1457 2070 TRP B CE3 7772 C CZ2 . TRP B 423 ? 2.5492 1.8779 1.8676 -0.6860 0.2885 -0.2050 2070 TRP B CZ2 7773 C CZ3 . TRP B 423 ? 2.1859 1.4794 1.5770 -0.5550 0.3178 -0.1643 2070 TRP B CZ3 7774 C CH2 . TRP B 423 ? 2.4053 1.6426 1.7175 -0.6238 0.3235 -0.1947 2070 TRP B CH2 7775 N N . ILE B 424 ? 1.6778 1.2442 1.3125 -0.4445 0.2731 -0.0932 2071 ILE B N 7776 C CA . ILE B 424 ? 1.6617 1.1212 1.2570 -0.4224 0.3043 -0.0939 2071 ILE B CA 7777 C C . ILE B 424 ? 1.7092 1.1359 1.2888 -0.3851 0.3049 -0.0942 2071 ILE B C 7778 O O . ILE B 424 ? 1.6359 1.1257 1.2529 -0.3597 0.2835 -0.0871 2071 ILE B O 7779 C CB . ILE B 424 ? 1.5630 1.0291 1.1924 -0.3913 0.3167 -0.0756 2071 ILE B CB 7780 C CG1 . ILE B 424 ? 1.6690 1.0354 1.2591 -0.3694 0.3494 -0.0689 2071 ILE B CG1 7781 C CG2 . ILE B 424 ? 1.4172 0.9556 1.1032 -0.3456 0.2986 -0.0627 2071 ILE B CG2 7782 C CD1 . ILE B 424 ? 1.9083 1.2902 1.5266 -0.3386 0.3581 -0.0477 2071 ILE B CD1 7783 N N . LYS B 425 ? 1.8083 1.1335 1.3317 -0.3814 0.3335 -0.1006 2072 LYS B N 7784 C CA . LYS B 425 ? 1.8407 1.1332 1.3440 -0.3516 0.3388 -0.1010 2072 LYS B CA 7785 C C . LYS B 425 ? 1.9935 1.2052 1.4802 -0.3101 0.3747 -0.0870 2072 LYS B C 7786 O O . LYS B 425 ? 2.2325 1.3647 1.6797 -0.3189 0.4063 -0.0870 2072 LYS B O 7787 C CB . LYS B 425 ? 1.8009 1.0669 1.2425 -0.3942 0.3344 -0.1251 2072 LYS B CB 7788 C CG . LYS B 425 ? 1.7743 0.9460 1.1513 -0.3802 0.3627 -0.1338 2072 LYS B CG 7789 C CD . LYS B 425 ? 1.9248 1.0568 1.2216 -0.4373 0.3618 -0.1641 2072 LYS B CD 7790 C CE . LYS B 425 ? 2.2199 1.2593 1.4541 -0.4872 0.3900 -0.1850 2072 LYS B CE 7791 N NZ . LYS B 425 ? 2.4669 1.4646 1.6138 -0.5585 0.3877 -0.2209 2072 LYS B NZ 7792 N N . VAL B 426 ? 1.9110 1.1493 1.4325 -0.2643 0.3706 -0.0710 2073 VAL B N 7793 C CA . VAL B 426 ? 1.8808 1.0686 1.3987 -0.2208 0.4004 -0.0513 2073 VAL B CA 7794 C C . VAL B 426 ? 2.0784 1.2266 1.5642 -0.2071 0.4147 -0.0557 2073 VAL B C 7795 O O . VAL B 426 ? 2.2615 1.4624 1.7695 -0.2037 0.3916 -0.0584 2073 VAL B O 7796 C CB . VAL B 426 ? 1.6902 0.9523 1.2778 -0.1839 0.3836 -0.0277 2073 VAL B CB 7797 C CG1 . VAL B 426 ? 1.6805 0.9290 1.2819 -0.1390 0.4029 -0.0037 2073 VAL B CG1 7798 C CG2 . VAL B 426 ? 1.7654 1.0403 1.3666 -0.1882 0.3840 -0.0184 2073 VAL B CG2 7799 N N . ASP B 427 ? 2.2098 1.2597 1.6393 -0.1974 0.4573 -0.0551 2074 ASP B N 7800 C CA . ASP B 427 ? 2.3850 1.3977 1.7913 -0.1694 0.4801 -0.0506 2074 ASP B CA 7801 C C . ASP B 427 ? 2.4351 1.4850 1.9031 -0.1132 0.4899 -0.0130 2074 ASP B C 7802 O O . ASP B 427 ? 2.7047 1.7116 2.1678 -0.0874 0.5214 0.0081 2074 ASP B O 7803 C CB . ASP B 427 ? 2.5459 1.4279 1.8583 -0.1807 0.5291 -0.0665 2074 ASP B CB 7804 C CG . ASP B 427 ? 2.6013 1.4405 1.8721 -0.1620 0.5528 -0.0706 2074 ASP B CG 7805 O OD1 . ASP B 427 ? 2.4341 1.3278 1.7568 -0.1206 0.5492 -0.0467 2074 ASP B OD1 7806 O OD2 . ASP B 427 ? 2.8147 1.5604 1.9943 -0.1924 0.5779 -0.0993 2074 ASP B OD2 7807 N N . LEU B 428 ? 2.2650 1.3966 1.7910 -0.0958 0.4641 -0.0020 2075 LEU B N 7808 C CA . LEU B 428 ? 2.1563 1.3359 1.7432 -0.0512 0.4696 0.0331 2075 LEU B CA 7809 C C . LEU B 428 ? 2.3520 1.4712 1.9147 -0.0123 0.5182 0.0538 2075 LEU B C 7810 O O . LEU B 428 ? 2.2637 1.4263 1.8778 0.0275 0.5285 0.0892 2075 LEU B O 7811 C CB . LEU B 428 ? 1.9717 1.2434 1.6209 -0.0508 0.4331 0.0362 2075 LEU B CB 7812 C CG . LEU B 428 ? 1.8802 1.2167 1.5698 -0.0684 0.3967 0.0314 2075 LEU B CG 7813 C CD1 . LEU B 428 ? 1.8216 1.2138 1.5406 -0.0848 0.3640 0.0176 2075 LEU B CD1 7814 C CD2 . LEU B 428 ? 1.7974 1.1787 1.5326 -0.0430 0.3964 0.0602 2075 LEU B CD2 7815 N N . LEU B 429 ? 2.5112 1.5317 1.9926 -0.0268 0.5490 0.0313 2076 LEU B N 7816 C CA . LEU B 429 ? 2.4866 1.4188 1.9193 0.0060 0.6059 0.0424 2076 LEU B CA 7817 C C . LEU B 429 ? 2.4663 1.4549 1.9474 0.0421 0.6102 0.0670 2076 LEU B C 7818 O O . LEU B 429 ? 2.4935 1.5012 2.0158 0.0899 0.6374 0.1063 2076 LEU B O 7819 C CB . LEU B 429 ? 2.5705 1.4461 1.9949 0.0391 0.6480 0.0698 2076 LEU B CB 7820 C CG . LEU B 429 ? 2.8421 1.6277 2.2002 0.0033 0.6613 0.0459 2076 LEU B CG 7821 C CD1 . LEU B 429 ? 2.9015 1.6435 2.2641 0.0451 0.7027 0.0837 2076 LEU B CD1 7822 C CD2 . LEU B 429 ? 3.0419 1.7073 2.2933 -0.0338 0.6902 0.0038 2076 LEU B CD2 7823 N N . ALA B 430 ? 2.4213 1.4442 1.9010 0.0184 0.5826 0.0473 2077 ALA B N 7824 C CA . ALA B 430 ? 2.3796 1.4649 1.9098 0.0425 0.5799 0.0680 2077 ALA B CA 7825 C C . ALA B 430 ? 2.2721 1.4401 1.8454 0.0138 0.5272 0.0561 2077 ALA B C 7826 O O . ALA B 430 ? 2.2803 1.5020 1.8947 -0.0038 0.4908 0.0524 2077 ALA B O 7827 C CB . ALA B 430 ? 2.4134 1.5564 2.0201 0.0882 0.5949 0.1137 2077 ALA B CB 7828 N N . PRO B 431 ? 2.1954 1.3672 1.7539 0.0115 0.5277 0.0516 2078 PRO B N 7829 C CA . PRO B 431 ? 2.0216 1.2663 1.6267 -0.0018 0.4909 0.0520 2078 PRO B CA 7830 C C . PRO B 431 ? 2.0060 1.3359 1.7061 0.0081 0.4693 0.0749 2078 PRO B C 7831 O O . PRO B 431 ? 2.0646 1.4174 1.8059 0.0368 0.4909 0.1036 2078 PRO B O 7832 C CB . PRO B 431 ? 2.0228 1.2470 1.6031 0.0151 0.5183 0.0612 2078 PRO B CB 7833 C CG . PRO B 431 ? 2.1032 1.2283 1.5862 0.0152 0.5560 0.0437 2078 PRO B CG 7834 C CD . PRO B 431 ? 2.2748 1.3610 1.7483 0.0165 0.5676 0.0402 2078 PRO B CD 7835 N N . MET B 432 ? 1.9120 1.2889 1.6431 -0.0159 0.4294 0.0628 2079 MET B N 7836 C CA . MET B 432 ? 1.7857 1.2337 1.5911 -0.0170 0.4063 0.0752 2079 MET B CA 7837 C C . MET B 432 ? 1.8533 1.3344 1.6793 -0.0400 0.3736 0.0602 2079 MET B C 7838 O O . MET B 432 ? 1.9323 1.3952 1.7230 -0.0558 0.3606 0.0408 2079 MET B O 7839 C CB . MET B 432 ? 1.6603 1.1158 1.4737 -0.0165 0.4005 0.0771 2079 MET B CB 7840 C CG . MET B 432 ? 1.7875 1.2415 1.6142 0.0149 0.4297 0.1063 2079 MET B CG 7841 S SD . MET B 432 ? 2.0604 1.5249 1.8901 0.0124 0.4177 0.1090 2079 MET B SD 7842 C CE . MET B 432 ? 2.1801 1.5705 1.9670 0.0488 0.4694 0.1307 2079 MET B CE 7843 N N . ILE B 433 ? 1.9371 1.4673 1.8198 -0.0429 0.3622 0.0702 2080 ILE B N 7844 C CA . ILE B 433 ? 1.9064 1.4577 1.8085 -0.0621 0.3376 0.0562 2080 ILE B CA 7845 C C . ILE B 433 ? 1.7947 1.3652 1.7042 -0.0743 0.3178 0.0436 2080 ILE B C 7846 O O . ILE B 433 ? 1.7017 1.2995 1.6335 -0.0723 0.3160 0.0532 2080 ILE B O 7847 C CB . ILE B 433 ? 1.7567 1.3346 1.7045 -0.0680 0.3378 0.0663 2080 ILE B CB 7848 C CG1 . ILE B 433 ? 1.7506 1.3764 1.7466 -0.0708 0.3378 0.0824 2080 ILE B CG1 7849 C CG2 . ILE B 433 ? 1.6220 1.1779 1.5579 -0.0572 0.3574 0.0786 2080 ILE B CG2 7850 C CD1 . ILE B 433 ? 1.6867 1.3420 1.7258 -0.0937 0.3295 0.0824 2080 ILE B CD1 7851 N N . ILE B 434 ? 1.7479 1.3097 1.6384 -0.0848 0.3044 0.0259 2081 ILE B N 7852 C CA . ILE B 434 ? 1.7307 1.3081 1.6232 -0.0953 0.2898 0.0140 2081 ILE B CA 7853 C C . ILE B 434 ? 1.8168 1.4070 1.7260 -0.1049 0.2781 0.0018 2081 ILE B C 7854 O O . ILE B 434 ? 1.9789 1.5605 1.8778 -0.1029 0.2771 -0.0028 2081 ILE B O 7855 C CB . ILE B 434 ? 1.6759 1.2318 1.5302 -0.0991 0.2906 0.0058 2081 ILE B CB 7856 C CG1 . ILE B 434 ? 1.6094 1.1469 1.4329 -0.1037 0.2909 -0.0009 2081 ILE B CG1 7857 C CG2 . ILE B 434 ? 1.8139 1.3462 1.6507 -0.0886 0.3080 0.0174 2081 ILE B CG2 7858 C CD1 . ILE B 434 ? 1.5101 1.0131 1.2865 -0.1130 0.2995 -0.0074 2081 ILE B CD1 7859 N N . HIS B 435 ? 1.8611 1.4719 1.7932 -0.1149 0.2713 -0.0018 2082 HIS B N 7860 C CA . HIS B 435 ? 1.8113 1.4181 1.7529 -0.1254 0.2681 -0.0156 2082 HIS B CA 7861 C C . HIS B 435 ? 1.8106 1.4166 1.7371 -0.1281 0.2630 -0.0316 2082 HIS B C 7862 O O . HIS B 435 ? 1.8587 1.4483 1.7855 -0.1282 0.2686 -0.0415 2082 HIS B O 7863 C CB . HIS B 435 ? 1.7813 1.4074 1.7452 -0.1442 0.2633 -0.0176 2082 HIS B CB 7864 C CG . HIS B 435 ? 1.7857 1.4178 1.7749 -0.1451 0.2717 -0.0011 2082 HIS B CG 7865 N ND1 . HIS B 435 ? 1.8115 1.4744 1.8173 -0.1371 0.2736 0.0200 2082 HIS B ND1 7866 C CD2 . HIS B 435 ? 1.8494 1.4604 1.8516 -0.1511 0.2828 0.0006 2082 HIS B CD2 7867 C CE1 . HIS B 435 ? 1.7579 1.4252 1.7888 -0.1391 0.2845 0.0336 2082 HIS B CE1 7868 N NE2 . HIS B 435 ? 1.8804 1.5148 1.9084 -0.1496 0.2896 0.0216 2082 HIS B NE2 7869 N N . GLY B 436 ? 1.8250 1.4447 1.7377 -0.1284 0.2570 -0.0322 2083 GLY B N 7870 C CA . GLY B 436 ? 1.7622 1.3867 1.6621 -0.1309 0.2548 -0.0445 2083 GLY B CA 7871 C C . GLY B 436 ? 1.7417 1.3769 1.6256 -0.1323 0.2519 -0.0407 2083 GLY B C 7872 O O . GLY B 436 ? 1.7866 1.4242 1.6673 -0.1311 0.2516 -0.0292 2083 GLY B O 7873 N N . ILE B 437 ? 1.6841 1.3256 1.5596 -0.1333 0.2536 -0.0471 2084 ILE B N 7874 C CA . ILE B 437 ? 1.7319 1.3799 1.5913 -0.1392 0.2540 -0.0440 2084 ILE B CA 7875 C C . ILE B 437 ? 1.7745 1.4376 1.6261 -0.1432 0.2546 -0.0528 2084 ILE B C 7876 O O . ILE B 437 ? 1.7704 1.4379 1.6265 -0.1400 0.2597 -0.0635 2084 ILE B O 7877 C CB . ILE B 437 ? 1.6317 1.2778 1.4832 -0.1447 0.2568 -0.0410 2084 ILE B CB 7878 C CG1 . ILE B 437 ? 1.5881 1.2229 1.4182 -0.1544 0.2623 -0.0358 2084 ILE B CG1 7879 C CG2 . ILE B 437 ? 1.6896 1.3628 1.5546 -0.1438 0.2570 -0.0454 2084 ILE B CG2 7880 C CD1 . ILE B 437 ? 1.5167 1.1481 1.3341 -0.1718 0.2653 -0.0372 2084 ILE B CD1 7881 N N . LYS B 438 ? 1.6701 1.3387 1.5067 -0.1466 0.2531 -0.0457 2085 LYS B N 7882 C CA . LYS B 438 ? 1.6543 1.3373 1.4740 -0.1509 0.2549 -0.0515 2085 LYS B CA 7883 C C . LYS B 438 ? 1.7759 1.4599 1.5872 -0.1544 0.2647 -0.0446 2085 LYS B C 7884 O O . LYS B 438 ? 1.7935 1.4622 1.5979 -0.1565 0.2684 -0.0314 2085 LYS B O 7885 C CB . LYS B 438 ? 1.5379 1.2364 1.3444 -0.1529 0.2459 -0.0428 2085 LYS B CB 7886 C CG . LYS B 438 ? 1.4570 1.1667 1.2726 -0.1596 0.2336 -0.0499 2085 LYS B CG 7887 C CD . LYS B 438 ? 1.5407 1.2858 1.3391 -0.1670 0.2208 -0.0418 2085 LYS B CD 7888 C CE . LYS B 438 ? 1.6378 1.4149 1.4583 -0.1710 0.2061 -0.0277 2085 LYS B CE 7889 N NZ . LYS B 438 ? 1.8370 1.6246 1.6565 -0.1966 0.1941 -0.0504 2085 LYS B NZ 7890 N N . THR B 439 ? 1.9179 1.6167 1.7292 -0.1555 0.2728 -0.0532 2086 THR B N 7891 C CA . THR B 439 ? 1.9006 1.6121 1.7122 -0.1635 0.2833 -0.0464 2086 THR B CA 7892 C C . THR B 439 ? 1.8465 1.5689 1.6357 -0.1650 0.2936 -0.0444 2086 THR B C 7893 O O . THR B 439 ? 1.7070 1.4313 1.4780 -0.1592 0.2929 -0.0539 2086 THR B O 7894 C CB . THR B 439 ? 1.8923 1.6292 1.7323 -0.1619 0.2872 -0.0493 2086 THR B CB 7895 O OG1 . THR B 439 ? 1.9160 1.6503 1.7662 -0.1455 0.2880 -0.0594 2086 THR B OG1 7896 C CG2 . THR B 439 ? 1.8772 1.6121 1.7277 -0.1732 0.2792 -0.0434 2086 THR B CG2 7897 N N . GLN B 440 ? 1.8487 1.5758 1.6345 -0.1763 0.3043 -0.0327 2087 GLN B N 7898 C CA . GLN B 440 ? 1.8074 1.5422 1.5689 -0.1779 0.3175 -0.0251 2087 GLN B CA 7899 C C . GLN B 440 ? 1.8140 1.5653 1.5860 -0.1938 0.3341 -0.0156 2087 GLN B C 7900 O O . GLN B 440 ? 1.8414 1.5983 1.6366 -0.2097 0.3324 -0.0143 2087 GLN B O 7901 C CB . GLN B 440 ? 1.8041 1.5165 1.5368 -0.1749 0.3146 -0.0093 2087 GLN B CB 7902 C CG . GLN B 440 ? 1.9024 1.6268 1.6023 -0.1712 0.3236 -0.0004 2087 GLN B CG 7903 C CD . GLN B 440 ? 2.1149 1.8450 1.7914 -0.1607 0.3077 0.0048 2087 GLN B CD 7904 O OE1 . GLN B 440 ? 2.2366 1.9610 1.8972 -0.1536 0.3084 0.0304 2087 GLN B OE1 7905 N NE2 . GLN B 440 ? 2.2307 1.9735 1.9067 -0.1604 0.2941 -0.0173 2087 GLN B NE2 7906 N N . GLY B 441 ? 1.7759 1.5386 1.5282 -0.1929 0.3500 -0.0085 2088 GLY B N 7907 C CA . GLY B 441 ? 1.8587 1.6396 1.6206 -0.2109 0.3693 0.0042 2088 GLY B CA 7908 C C . GLY B 441 ? 1.9469 1.6968 1.6736 -0.2184 0.3826 0.0240 2088 GLY B C 7909 O O . GLY B 441 ? 1.9658 1.6781 1.6689 -0.2108 0.3752 0.0320 2088 GLY B O 7910 N N . ALA B 442 ? 1.9676 1.7353 1.6932 -0.2306 0.4052 0.0362 2089 ALA B N 7911 C CA . ALA B 442 ? 2.1965 1.9344 1.8847 -0.2344 0.4242 0.0597 2089 ALA B CA 7912 C C . ALA B 442 ? 2.4513 2.2225 2.1401 -0.2427 0.4513 0.0709 2089 ALA B C 7913 O O . ALA B 442 ? 2.5724 2.3838 2.3024 -0.2613 0.4596 0.0677 2089 ALA B O 7914 C CB . ALA B 442 ? 2.2510 1.9346 1.9341 -0.2561 0.4306 0.0714 2089 ALA B CB 7915 N N . ARG B 443 ? 2.5876 2.3497 2.2318 -0.2285 0.4653 0.0872 2090 ARG B N 7916 C CA . ARG B 443 ? 2.4023 2.1889 2.0382 -0.2351 0.4966 0.1029 2090 ARG B CA 7917 C C . ARG B 443 ? 2.3568 2.1164 2.0072 -0.2698 0.5163 0.1228 2090 ARG B C 7918 O O . ARG B 443 ? 2.2402 1.9426 1.8778 -0.2781 0.5114 0.1296 2090 ARG B O 7919 C CB . ARG B 443 ? 2.2911 2.0711 1.8634 -0.2108 0.5044 0.1168 2090 ARG B CB 7920 C CG . ARG B 443 ? 2.1179 1.9352 1.6705 -0.2031 0.5313 0.1183 2090 ARG B CG 7921 C CD . ARG B 443 ? 2.2685 2.0858 1.7497 -0.1788 0.5269 0.1169 2090 ARG B CD 7922 N NE . ARG B 443 ? 2.7216 2.5511 2.1597 -0.1748 0.5611 0.1379 2090 ARG B NE 7923 C CZ . ARG B 443 ? 2.6394 2.4895 2.0318 -0.1606 0.5768 0.1251 2090 ARG B CZ 7924 N NH1 . ARG B 443 ? 2.6041 2.4595 1.9825 -0.1496 0.5642 0.0881 2090 ARG B NH1 7925 N NH2 . ARG B 443 ? 2.3689 2.2270 1.7223 -0.1581 0.6103 0.1494 2090 ARG B NH2 7926 N N . GLN B 444 ? 2.4041 2.2033 2.0824 -0.2921 0.5406 0.1308 2091 GLN B N 7927 C CA . GLN B 444 ? 2.5374 2.3098 2.2212 -0.3325 0.5656 0.1511 2091 GLN B CA 7928 C C . GLN B 444 ? 2.5316 2.2997 2.1816 -0.3286 0.6018 0.1805 2091 GLN B C 7929 O O . GLN B 444 ? 2.7325 2.4495 2.3273 -0.3072 0.6090 0.1999 2091 GLN B O 7930 C CB . GLN B 444 ? 2.5528 2.3790 2.3007 -0.3739 0.5640 0.1416 2091 GLN B CB 7931 C CG . GLN B 444 ? 2.5634 2.3422 2.3173 -0.4106 0.5487 0.1300 2091 GLN B CG 7932 C CD . GLN B 444 ? 2.5885 2.3020 2.3181 -0.4548 0.5784 0.1472 2091 GLN B CD 7933 O OE1 . GLN B 444 ? 2.6606 2.4064 2.4240 -0.5070 0.5895 0.1487 2091 GLN B OE1 7934 N NE2 . GLN B 444 ? 2.5436 2.1667 2.2153 -0.4350 0.5933 0.1627 2091 GLN B NE2 7935 N N . LYS B 445 ? 2.3071 2.1330 1.9897 -0.3469 0.6263 0.1889 2092 LYS B N 7936 C CA . LYS B 445 ? 2.4794 2.3109 2.1221 -0.3282 0.6578 0.2127 2092 LYS B CA 7937 C C . LYS B 445 ? 2.4874 2.3736 2.1249 -0.2890 0.6520 0.1951 2092 LYS B C 7938 O O . LYS B 445 ? 2.6438 2.5062 2.2297 -0.2560 0.6354 0.1860 2092 LYS B O 7939 C CB . LYS B 445 ? 2.6327 2.4780 2.2952 -0.3667 0.6986 0.2399 2092 LYS B CB 7940 C CG . LYS B 445 ? 2.6521 2.5341 2.3857 -0.4213 0.6970 0.2330 2092 LYS B CG 7941 C CD . LYS B 445 ? 2.7084 2.5911 2.4508 -0.4646 0.7399 0.2631 2092 LYS B CD 7942 C CE . LYS B 445 ? 2.6213 2.5860 2.4461 -0.5198 0.7403 0.2593 2092 LYS B CE 7943 N NZ . LYS B 445 ? 2.5266 2.4547 2.3652 -0.5627 0.7103 0.2366 2092 LYS B NZ 7944 N N . PHE B 446 ? 2.4471 2.4059 2.1370 -0.2932 0.6667 0.1905 2093 PHE B N 7945 C CA . PHE B 446 ? 2.3501 2.3476 2.0384 -0.2549 0.6646 0.1692 2093 PHE B CA 7946 C C . PHE B 446 ? 2.3041 2.3573 2.0724 -0.2645 0.6493 0.1559 2093 PHE B C 7947 O O . PHE B 446 ? 2.3014 2.4293 2.1267 -0.2685 0.6720 0.1669 2093 PHE B O 7948 C CB . PHE B 446 ? 2.4339 2.4675 2.1020 -0.2369 0.7083 0.1833 2093 PHE B CB 7949 C CG . PHE B 446 ? 2.4661 2.4681 2.0829 -0.2471 0.7350 0.2138 2093 PHE B CG 7950 C CD1 . PHE B 446 ? 2.4259 2.3650 1.9636 -0.2322 0.7210 0.2178 2093 PHE B CD1 7951 C CD2 . PHE B 446 ? 2.5272 2.5691 2.1776 -0.2708 0.7754 0.2430 2093 PHE B CD2 7952 C CE1 . PHE B 446 ? 2.5866 2.4975 2.0762 -0.2369 0.7477 0.2525 2093 PHE B CE1 7953 C CE2 . PHE B 446 ? 2.7057 2.7131 2.3070 -0.2796 0.8043 0.2746 2093 PHE B CE2 7954 C CZ . PHE B 446 ? 2.8181 2.7569 2.3367 -0.2603 0.7908 0.2803 2093 PHE B CZ 7955 N N . SER B 447 ? 2.2122 2.2345 1.9863 -0.2675 0.6111 0.1366 2094 SER B N 7956 C CA . SER B 447 ? 2.1028 2.1722 1.9471 -0.2834 0.5912 0.1283 2094 SER B CA 7957 C C . SER B 447 ? 2.0089 2.0368 1.8369 -0.2644 0.5543 0.1023 2094 SER B C 7958 O O . SER B 447 ? 1.9263 1.8930 1.7247 -0.2765 0.5335 0.0977 2094 SER B O 7959 C CB . SER B 447 ? 2.1494 2.2260 2.0278 -0.3400 0.5906 0.1434 2094 SER B CB 7960 O OG . SER B 447 ? 2.0661 2.0759 1.8934 -0.3585 0.6085 0.1593 2094 SER B OG 7961 N N . SER B 448 ? 2.0805 2.1375 1.9255 -0.2311 0.5517 0.0874 2095 SER B N 7962 C CA . SER B 448 ? 2.1232 2.1470 1.9597 -0.2134 0.5205 0.0636 2095 SER B CA 7963 C C . SER B 448 ? 2.0255 2.0565 1.9031 -0.2441 0.4920 0.0638 2095 SER B C 7964 O O . SER B 448 ? 1.9569 2.0546 1.8940 -0.2629 0.4929 0.0749 2095 SER B O 7965 C CB . SER B 448 ? 2.2031 2.2531 2.0543 -0.1740 0.5319 0.0510 2095 SER B CB 7966 O OG . SER B 448 ? 2.0385 2.0421 1.8226 -0.1473 0.5448 0.0339 2095 SER B OG 7967 N N . LEU B 449 ? 1.9812 1.9477 1.8248 -0.2499 0.4678 0.0530 2096 LEU B N 7968 C CA . LEU B 449 ? 1.8996 1.8542 1.7633 -0.2806 0.4454 0.0506 2096 LEU B CA 7969 C C . LEU B 449 ? 1.8679 1.7831 1.7193 -0.2638 0.4165 0.0320 2096 LEU B C 7970 O O . LEU B 449 ? 1.7380 1.5915 1.5474 -0.2579 0.4086 0.0286 2096 LEU B O 7971 C CB . LEU B 449 ? 1.8857 1.7927 1.7212 -0.3152 0.4563 0.0632 2096 LEU B CB 7972 C CG . LEU B 449 ? 1.9040 1.8188 1.7655 -0.3658 0.4509 0.0647 2096 LEU B CG 7973 C CD1 . LEU B 449 ? 1.8015 1.8161 1.7246 -0.3870 0.4590 0.0755 2096 LEU B CD1 7974 C CD2 . LEU B 449 ? 1.9474 1.7842 1.7650 -0.3948 0.4691 0.0749 2096 LEU B CD2 7975 N N . TYR B 450 ? 1.8530 1.8108 1.7451 -0.2545 0.4032 0.0251 2097 TYR B N 7976 C CA . TYR B 450 ? 1.7405 1.6720 1.6279 -0.2328 0.3814 0.0095 2097 TYR B CA 7977 C C . TYR B 450 ? 1.7188 1.6945 1.6508 -0.2418 0.3638 0.0105 2097 TYR B C 7978 O O . TYR B 450 ? 1.6409 1.6894 1.6171 -0.2558 0.3686 0.0244 2097 TYR B O 7979 C CB . TYR B 450 ? 1.7471 1.6740 1.6211 -0.1938 0.3914 -0.0008 2097 TYR B CB 7980 C CG . TYR B 450 ? 1.7973 1.7833 1.7042 -0.1750 0.4166 0.0075 2097 TYR B CG 7981 C CD1 . TYR B 450 ? 1.9042 1.9444 1.8639 -0.1627 0.4149 0.0155 2097 TYR B CD1 7982 C CD2 . TYR B 450 ? 1.9189 1.9087 1.8029 -0.1651 0.4449 0.0109 2097 TYR B CD2 7983 C CE1 . TYR B 450 ? 2.0124 2.1114 2.0078 -0.1379 0.4427 0.0294 2097 TYR B CE1 7984 C CE2 . TYR B 450 ? 2.0476 2.0899 1.9621 -0.1427 0.4745 0.0207 2097 TYR B CE2 7985 C CZ . TYR B 450 ? 1.9983 2.0964 1.9719 -0.1272 0.4744 0.0313 2097 TYR B CZ 7986 O OH . TYR B 450 ? 1.9904 2.1468 2.0018 -0.0974 0.5076 0.0475 2097 TYR B OH 7987 N N . ILE B 451 ? 1.6475 1.5884 1.5693 -0.2347 0.3432 -0.0006 2098 ILE B N 7988 C CA . ILE B 451 ? 1.6246 1.6108 1.5828 -0.2370 0.3266 0.0029 2098 ILE B CA 7989 C C . ILE B 451 ? 1.5926 1.6007 1.5729 -0.1944 0.3331 0.0041 2098 ILE B C 7990 O O . ILE B 451 ? 1.6310 1.5863 1.5835 -0.1699 0.3373 -0.0092 2098 ILE B O 7991 C CB . ILE B 451 ? 1.6802 1.6222 1.6169 -0.2502 0.3049 -0.0069 2098 ILE B CB 7992 C CG1 . ILE B 451 ? 1.7333 1.6481 1.6456 -0.2968 0.3031 -0.0088 2098 ILE B CG1 7993 C CG2 . ILE B 451 ? 1.6008 1.5957 1.5720 -0.2405 0.2895 -0.0004 2098 ILE B CG2 7994 C CD1 . ILE B 451 ? 1.5856 1.4634 1.4739 -0.3167 0.2864 -0.0187 2098 ILE B CD1 7995 N N . SER B 452 ? 1.5261 1.6133 1.5561 -0.1872 0.3346 0.0217 2099 SER B N 7996 C CA . SER B 452 ? 1.7747 1.8855 1.8295 -0.1411 0.3534 0.0298 2099 SER B CA 7997 C C . SER B 452 ? 1.9295 2.0261 1.9912 -0.1153 0.3423 0.0304 2099 SER B C 7998 O O . SER B 452 ? 1.9374 1.9753 1.9769 -0.0854 0.3549 0.0179 2099 SER B O 7999 C CB . SER B 452 ? 1.8938 2.1067 2.0054 -0.1376 0.3682 0.0573 2099 SER B CB 8000 O OG . SER B 452 ? 2.3596 2.6005 2.5016 -0.0868 0.3902 0.0721 2099 SER B OG 8001 N N . GLN B 453 ? 2.0303 2.1817 2.1198 -0.1305 0.3196 0.0454 2100 GLN B N 8002 C CA . GLN B 453 ? 1.7989 1.9503 1.8969 -0.1091 0.3071 0.0531 2100 GLN B CA 8003 C C . GLN B 453 ? 1.6963 1.8331 1.7687 -0.1521 0.2761 0.0433 2100 GLN B C 8004 O O . GLN B 453 ? 1.6298 1.7885 1.6971 -0.1953 0.2663 0.0403 2100 GLN B O 8005 C CB . GLN B 453 ? 1.7422 1.9977 1.9006 -0.0825 0.3124 0.0893 2100 GLN B CB 8006 C CG . GLN B 453 ? 1.9157 2.1735 2.0863 -0.0453 0.3095 0.1063 2100 GLN B CG 8007 C CD . GLN B 453 ? 2.1398 2.4980 2.3732 -0.0027 0.3258 0.1495 2100 GLN B CD 8008 O OE1 . GLN B 453 ? 2.2234 2.5801 2.4745 0.0355 0.3627 0.1577 2100 GLN B OE1 8009 N NE2 . GLN B 453 ? 2.1840 2.6320 2.4488 -0.0071 0.3001 0.1792 2100 GLN B NE2 8010 N N . PHE B 454 ? 1.6377 1.7282 1.6888 -0.1416 0.2652 0.0371 2101 PHE B N 8011 C CA . PHE B 454 ? 1.6043 1.6739 1.6245 -0.1771 0.2415 0.0275 2101 PHE B CA 8012 C C . PHE B 454 ? 1.5870 1.6355 1.5989 -0.1550 0.2331 0.0323 2101 PHE B C 8013 O O . PHE B 454 ? 1.5996 1.6250 1.6226 -0.1151 0.2481 0.0374 2101 PHE B O 8014 C CB . PHE B 454 ? 1.5994 1.5889 1.5740 -0.2030 0.2445 0.0032 2101 PHE B CB 8015 C CG . PHE B 454 ? 1.5749 1.4862 1.5249 -0.1785 0.2531 -0.0102 2101 PHE B CG 8016 C CD1 . PHE B 454 ? 1.6003 1.4955 1.5563 -0.1523 0.2705 -0.0139 2101 PHE B CD1 8017 C CD2 . PHE B 454 ? 1.5711 1.4269 1.4891 -0.1856 0.2450 -0.0197 2101 PHE B CD2 8018 C CE1 . PHE B 454 ? 1.5978 1.4307 1.5304 -0.1395 0.2744 -0.0274 2101 PHE B CE1 8019 C CE2 . PHE B 454 ? 1.5862 1.3856 1.4895 -0.1674 0.2514 -0.0285 2101 PHE B CE2 8020 C CZ . PHE B 454 ? 1.5838 1.3754 1.4952 -0.1475 0.2635 -0.0327 2101 PHE B CZ 8021 N N . ILE B 455 ? 1.5933 1.6462 1.5813 -0.1828 0.2122 0.0305 2102 ILE B N 8022 C CA . ILE B 455 ? 1.6469 1.6750 1.6180 -0.1656 0.2049 0.0352 2102 ILE B CA 8023 C C . ILE B 455 ? 1.6520 1.5962 1.5697 -0.1887 0.2026 0.0113 2102 ILE B C 8024 O O . ILE B 455 ? 1.6801 1.5926 1.5748 -0.2184 0.2055 -0.0054 2102 ILE B O 8025 C CB . ILE B 455 ? 1.4881 1.6033 1.4722 -0.1721 0.1834 0.0594 2102 ILE B CB 8026 C CG1 . ILE B 455 ? 1.4421 1.5898 1.4007 -0.2319 0.1625 0.0480 2102 ILE B CG1 8027 C CG2 . ILE B 455 ? 1.3076 1.5125 1.3525 -0.1359 0.1903 0.0930 2102 ILE B CG2 8028 C CD1 . ILE B 455 ? 1.4253 1.4849 1.3162 -0.2646 0.1595 0.0195 2102 ILE B CD1 8029 N N . ILE B 456 ? 1.5399 1.4468 1.4380 -0.1730 0.2018 0.0127 2103 ILE B N 8030 C CA . ILE B 456 ? 1.5562 1.3903 1.4055 -0.1920 0.2040 -0.0060 2103 ILE B CA 8031 C C . ILE B 456 ? 1.6928 1.5235 1.5038 -0.2048 0.1932 -0.0044 2103 ILE B C 8032 O O . ILE B 456 ? 1.8855 1.7457 1.7074 -0.1822 0.1880 0.0139 2103 ILE B O 8033 C CB . ILE B 456 ? 1.4382 1.2060 1.2875 -0.1694 0.2208 -0.0140 2103 ILE B CB 8034 C CG1 . ILE B 456 ? 1.4393 1.1928 1.2918 -0.1799 0.2286 -0.0248 2103 ILE B CG1 8035 C CG2 . ILE B 456 ? 1.3248 1.0320 1.1347 -0.1737 0.2262 -0.0214 2103 ILE B CG2 8036 C CD1 . ILE B 456 ? 1.6411 1.3514 1.4975 -0.1613 0.2400 -0.0299 2103 ILE B CD1 8037 N N . MET B 457 ? 1.7189 1.5088 1.4796 -0.2415 0.1930 -0.0233 2104 MET B N 8038 C CA . MET B 457 ? 1.7564 1.5153 1.4601 -0.2576 0.1899 -0.0303 2104 MET B CA 8039 C C . MET B 457 ? 1.8591 1.5180 1.5236 -0.2520 0.2146 -0.0455 2104 MET B C 8040 O O . MET B 457 ? 1.8307 1.4530 1.5063 -0.2478 0.2290 -0.0516 2104 MET B O 8041 C CB . MET B 457 ? 1.7359 1.5299 1.4026 -0.3106 0.1719 -0.0408 2104 MET B CB 8042 C CG . MET B 457 ? 1.7820 1.6923 1.4831 -0.3141 0.1441 -0.0176 2104 MET B CG 8043 S SD . MET B 457 ? 2.2167 2.1808 1.8775 -0.3908 0.1190 -0.0325 2104 MET B SD 8044 C CE . MET B 457 ? 2.0462 2.1731 1.7915 -0.3875 0.0925 0.0033 2104 MET B CE 8045 N N . TYR B 458 ? 1.9255 1.5465 1.5457 -0.2482 0.2211 -0.0473 2105 TYR B N 8046 C CA . TYR B 458 ? 1.8849 1.4203 1.4740 -0.2333 0.2489 -0.0541 2105 TYR B CA 8047 C C . TYR B 458 ? 1.9056 1.4037 1.4294 -0.2406 0.2565 -0.0597 2105 TYR B C 8048 O O . TYR B 458 ? 1.8677 1.4129 1.3847 -0.2411 0.2391 -0.0498 2105 TYR B O 8049 C CB . TYR B 458 ? 1.8647 1.4010 1.5074 -0.1907 0.2585 -0.0376 2105 TYR B CB 8050 C CG . TYR B 458 ? 1.8851 1.4541 1.5489 -0.1664 0.2523 -0.0193 2105 TYR B CG 8051 C CD1 . TYR B 458 ? 1.7996 1.4358 1.5006 -0.1592 0.2335 -0.0054 2105 TYR B CD1 8052 C CD2 . TYR B 458 ? 1.9896 1.5208 1.6385 -0.1468 0.2702 -0.0118 2105 TYR B CD2 8053 C CE1 . TYR B 458 ? 1.7923 1.4479 1.5101 -0.1331 0.2337 0.0154 2105 TYR B CE1 8054 C CE2 . TYR B 458 ? 2.0891 1.6432 1.7561 -0.1252 0.2687 0.0074 2105 TYR B CE2 8055 C CZ . TYR B 458 ? 2.0364 1.6482 1.7354 -0.1184 0.2509 0.0209 2105 TYR B CZ 8056 O OH . TYR B 458 ? 2.3393 1.9629 2.0520 -0.0938 0.2551 0.0435 2105 TYR B OH 8057 N N . SER B 459 ? 1.9834 1.3959 1.4566 -0.2425 0.2857 -0.0728 2106 SER B N 8058 C CA . SER B 459 ? 2.1228 1.4869 1.5267 -0.2446 0.3013 -0.0792 2106 SER B CA 8059 C C . SER B 459 ? 2.2309 1.5279 1.6318 -0.2075 0.3396 -0.0712 2106 SER B C 8060 O O . SER B 459 ? 2.2596 1.5282 1.6881 -0.1918 0.3574 -0.0673 2106 SER B O 8061 C CB . SER B 459 ? 2.1847 1.5073 1.4993 -0.2971 0.3012 -0.1085 2106 SER B CB 8062 O OG . SER B 459 ? 2.1326 1.4491 1.3824 -0.3063 0.2992 -0.1127 2106 SER B OG 8063 N N . LEU B 460 ? 2.4203 1.7014 1.7889 -0.1924 0.3518 -0.0646 2107 LEU B N 8064 C CA . LEU B 460 ? 2.4454 1.6846 1.8216 -0.1531 0.3874 -0.0493 2107 LEU B CA 8065 C C . LEU B 460 ? 2.5892 1.7320 1.8709 -0.1605 0.4258 -0.0673 2107 LEU B C 8066 O O . LEU B 460 ? 2.7026 1.7983 1.9814 -0.1272 0.4649 -0.0553 2107 LEU B O 8067 C CB . LEU B 460 ? 2.4378 1.7249 1.8446 -0.1298 0.3796 -0.0263 2107 LEU B CB 8068 C CG . LEU B 460 ? 2.6204 1.9582 2.0007 -0.1502 0.3479 -0.0265 2107 LEU B CG 8069 C CD1 . LEU B 460 ? 2.7096 2.0048 1.9952 -0.1599 0.3633 -0.0349 2107 LEU B CD1 8070 C CD2 . LEU B 460 ? 2.3808 1.7901 1.8361 -0.1267 0.3285 0.0013 2107 LEU B CD2 8071 N N . ASP B 461 ? 2.7716 1.8864 1.9746 -0.2061 0.4160 -0.0959 2108 ASP B N 8072 C CA . ASP B 461 ? 2.9317 1.9369 2.0279 -0.2240 0.4547 -0.1222 2108 ASP B CA 8073 C C . ASP B 461 ? 2.8312 1.7829 1.9020 -0.2574 0.4618 -0.1453 2108 ASP B C 8074 O O . ASP B 461 ? 2.7717 1.6576 1.8489 -0.2319 0.5001 -0.1393 2108 ASP B O 8075 C CB . ASP B 461 ? 3.1335 2.1343 2.1379 -0.2572 0.4434 -0.1407 2108 ASP B CB 8076 C CG . ASP B 461 ? 3.1204 2.1689 2.0949 -0.3202 0.3984 -0.1637 2108 ASP B CG 8077 O OD1 . ASP B 461 ? 2.9760 2.1290 2.0311 -0.3230 0.3556 -0.1471 2108 ASP B OD1 8078 O OD2 . ASP B 461 ? 3.1800 2.1607 2.0474 -0.3684 0.4085 -0.1985 2108 ASP B OD2 8079 N N . GLY B 462 ? 2.7286 1.7167 1.7763 -0.3130 0.4252 -0.1665 2109 GLY B N 8080 C CA . GLY B 462 ? 2.6273 1.5755 1.6535 -0.3548 0.4275 -0.1883 2109 GLY B CA 8081 C C . GLY B 462 ? 2.6186 1.6195 1.6077 -0.4235 0.3856 -0.2118 2109 GLY B C 8082 O O . GLY B 462 ? 2.5160 1.5688 1.5479 -0.4525 0.3604 -0.2131 2109 GLY B O 8083 N N . LYS B 463 ? 2.8410 1.8375 1.7516 -0.4496 0.3778 -0.2276 2110 LYS B N 8084 C CA . LYS B 463 ? 3.1128 2.1534 1.9679 -0.5244 0.3404 -0.2531 2110 LYS B CA 8085 C C . LYS B 463 ? 2.9082 2.1138 1.8474 -0.5220 0.2814 -0.2242 2110 LYS B C 8086 O O . LYS B 463 ? 2.8273 2.1077 1.8285 -0.5444 0.2533 -0.2183 2110 LYS B O 8087 C CB . LYS B 463 ? 3.5421 2.4979 2.2553 -0.5646 0.3586 -0.2881 2110 LYS B CB 8088 C CG . LYS B 463 ? 3.7493 2.5253 2.3658 -0.5574 0.4285 -0.3153 2110 LYS B CG 8089 C CD . LYS B 463 ? 3.7707 2.4594 2.3967 -0.5663 0.4618 -0.3261 2110 LYS B CD 8090 C CE . LYS B 463 ? 3.7581 2.3910 2.2943 -0.6592 0.4581 -0.3716 2110 LYS B CE 8091 N NZ . LYS B 463 ? 3.8540 2.3467 2.2331 -0.6970 0.4987 -0.4155 2110 LYS B NZ 8092 N N . LYS B 464 ? 2.9111 2.1700 1.8522 -0.4916 0.2675 -0.2030 2111 LYS B N 8093 C CA . LYS B 464 ? 2.7884 2.1965 1.8094 -0.4774 0.2192 -0.1681 2111 LYS B CA 8094 C C . LYS B 464 ? 2.6073 2.0606 1.7509 -0.4146 0.2208 -0.1331 2111 LYS B C 8095 O O . LYS B 464 ? 2.4177 1.8315 1.5870 -0.3610 0.2473 -0.1170 2111 LYS B O 8096 C CB . LYS B 464 ? 2.8841 2.3455 1.8551 -0.4772 0.1983 -0.1553 2111 LYS B CB 8097 C CG . LYS B 464 ? 3.0684 2.4263 1.9351 -0.4689 0.2346 -0.1714 2111 LYS B CG 8098 C CD . LYS B 464 ? 3.0477 2.3736 1.9639 -0.3929 0.2678 -0.1420 2111 LYS B CD 8099 C CE . LYS B 464 ? 2.9200 2.3608 1.9318 -0.3490 0.2392 -0.0949 2111 LYS B CE 8100 N NZ . LYS B 464 ? 2.7031 2.1255 1.8091 -0.2900 0.2641 -0.0717 2111 LYS B NZ 8101 N N . TRP B 465 ? 2.5261 2.0649 1.7404 -0.4276 0.1924 -0.1230 2112 TRP B N 8102 C CA . TRP B 465 ? 2.3407 1.9174 1.6599 -0.3845 0.1931 -0.0994 2112 TRP B CA 8103 C C . TRP B 465 ? 2.3624 2.0378 1.7508 -0.3425 0.1712 -0.0609 2112 TRP B C 8104 O O . TRP B 465 ? 2.7982 2.5195 2.1570 -0.3439 0.1542 -0.0478 2112 TRP B O 8105 C CB . TRP B 465 ? 2.2839 1.9004 1.6336 -0.4232 0.1778 -0.1087 2112 TRP B CB 8106 C CG . TRP B 465 ? 2.4654 1.9789 1.7706 -0.4517 0.2066 -0.1385 2112 TRP B CG 8107 C CD1 . TRP B 465 ? 2.6848 2.1449 1.9062 -0.5159 0.2110 -0.1717 2112 TRP B CD1 8108 C CD2 . TRP B 465 ? 2.4742 1.9224 1.8132 -0.4181 0.2372 -0.1362 2112 TRP B CD2 8109 N NE1 . TRP B 465 ? 2.8782 2.2328 2.0795 -0.5192 0.2480 -0.1884 2112 TRP B NE1 8110 C CE2 . TRP B 465 ? 2.7333 2.0864 2.0083 -0.4574 0.2627 -0.1643 2112 TRP B CE2 8111 C CE3 . TRP B 465 ? 2.2376 1.6993 1.6514 -0.3612 0.2457 -0.1128 2112 TRP B CE3 8112 C CZ2 . TRP B 465 ? 2.6869 1.9645 1.9752 -0.4337 0.2966 -0.1630 2112 TRP B CZ2 8113 C CZ3 . TRP B 465 ? 2.1923 1.5888 1.6177 -0.3439 0.2738 -0.1145 2112 TRP B CZ3 8114 C CH2 . TRP B 465 ? 2.4387 1.7476 1.8043 -0.3762 0.2990 -0.1363 2112 TRP B CH2 8115 N N . GLN B 466 ? 2.2000 1.9042 1.6748 -0.3058 0.1738 -0.0426 2113 GLN B N 8116 C CA . GLN B 466 ? 2.1351 1.9121 1.6757 -0.2614 0.1631 -0.0066 2113 GLN B CA 8117 C C . GLN B 466 ? 2.2211 2.0440 1.8443 -0.2426 0.1602 0.0053 2113 GLN B C 8118 O O . GLN B 466 ? 2.4072 2.1857 2.0442 -0.2475 0.1741 -0.0114 2113 GLN B O 8119 C CB . GLN B 466 ? 2.0621 1.7796 1.6051 -0.2182 0.1886 0.0035 2113 GLN B CB 8120 C CG . GLN B 466 ? 2.1347 1.9068 1.7197 -0.1779 0.1829 0.0397 2113 GLN B CG 8121 C CD . GLN B 466 ? 2.3310 2.0593 1.8745 -0.1591 0.1993 0.0488 2113 GLN B CD 8122 O OE1 . GLN B 466 ? 2.4439 2.0949 1.9702 -0.1524 0.2258 0.0353 2113 GLN B OE1 8123 N NE2 . GLN B 466 ? 2.4756 2.2587 2.0030 -0.1490 0.1851 0.0756 2113 GLN B NE2 8124 N N . THR B 467 ? 2.2214 2.1293 1.8964 -0.2166 0.1462 0.0367 2114 THR B N 8125 C CA . THR B 467 ? 2.1429 2.0861 1.8911 -0.1920 0.1507 0.0489 2114 THR B CA 8126 C C . THR B 467 ? 2.1379 2.0467 1.9239 -0.1399 0.1725 0.0653 2114 THR B C 8127 O O . THR B 467 ? 2.1481 2.0559 1.9265 -0.1148 0.1761 0.0859 2114 THR B O 8128 C CB . THR B 467 ? 2.1767 2.2392 1.9652 -0.1945 0.1278 0.0756 2114 THR B CB 8129 O OG1 . THR B 467 ? 2.3371 2.4448 2.0832 -0.2500 0.1022 0.0639 2114 THR B OG1 8130 C CG2 . THR B 467 ? 2.1909 2.2784 2.0402 -0.1825 0.1370 0.0779 2114 THR B CG2 8131 N N . TYR B 468 ? 2.1620 2.0421 1.9846 -0.1275 0.1876 0.0559 2115 TYR B N 8132 C CA . TYR B 468 ? 1.9713 1.8082 1.8230 -0.0899 0.2094 0.0631 2115 TYR B CA 8133 C C . TYR B 468 ? 1.8583 1.7402 1.7590 -0.0546 0.2165 0.0888 2115 TYR B C 8134 O O . TYR B 468 ? 1.7768 1.6955 1.7076 -0.0543 0.2168 0.0882 2115 TYR B O 8135 C CB . TYR B 468 ? 1.8970 1.6715 1.7500 -0.0981 0.2226 0.0374 2115 TYR B CB 8136 C CG . TYR B 468 ? 1.8130 1.5484 1.6935 -0.0715 0.2418 0.0394 2115 TYR B CG 8137 C CD1 . TYR B 468 ? 1.8595 1.5567 1.7346 -0.0570 0.2535 0.0478 2115 TYR B CD1 8138 C CD2 . TYR B 468 ? 1.9230 1.6568 1.8301 -0.0658 0.2499 0.0310 2115 TYR B CD2 8139 C CE1 . TYR B 468 ? 1.9286 1.5870 1.8260 -0.0425 0.2713 0.0466 2115 TYR B CE1 8140 C CE2 . TYR B 468 ? 1.8925 1.5840 1.8144 -0.0503 0.2676 0.0273 2115 TYR B CE2 8141 C CZ . TYR B 468 ? 1.9055 1.5593 1.8233 -0.0415 0.2774 0.0343 2115 TYR B CZ 8142 O OH . TYR B 468 ? 1.9517 1.5613 1.8816 -0.0353 0.2950 0.0280 2115 TYR B OH 8143 N N . ARG B 469 ? 1.8466 1.7211 1.7513 -0.0230 0.2266 0.1137 2116 ARG B N 8144 C CA . ARG B 469 ? 1.9775 1.8629 1.9209 0.0206 0.2461 0.1414 2116 ARG B CA 8145 C C . ARG B 469 ? 1.9772 1.7714 1.9197 0.0349 0.2734 0.1316 2116 ARG B C 8146 O O . ARG B 469 ? 1.9821 1.7463 1.9133 0.0506 0.2841 0.1485 2116 ARG B O 8147 C CB . ARG B 469 ? 2.0692 2.0192 2.0159 0.0472 0.2389 0.1851 2116 ARG B CB 8148 C CG . ARG B 469 ? 1.9467 1.8790 1.9219 0.1016 0.2693 0.2207 2116 ARG B CG 8149 C CD . ARG B 469 ? 1.8706 1.9050 1.8631 0.1302 0.2572 0.2710 2116 ARG B CD 8150 N NE . ARG B 469 ? 1.8694 1.8916 1.8833 0.1887 0.2880 0.3163 2116 ARG B NE 8151 C CZ . ARG B 469 ? 2.0058 1.9719 1.9964 0.2075 0.3043 0.3336 2116 ARG B CZ 8152 N NH1 . ARG B 469 ? 2.0446 1.9607 1.9924 0.1739 0.2947 0.3078 2116 ARG B NH1 8153 N NH2 . ARG B 469 ? 2.0890 2.0440 2.0995 0.2631 0.3358 0.3794 2116 ARG B NH2 8154 N N . GLY B 470 ? 2.0267 1.7801 1.9790 0.0254 0.2843 0.1047 2117 GLY B N 8155 C CA . GLY B 470 ? 2.0641 1.7407 2.0193 0.0338 0.3098 0.0944 2117 GLY B CA 8156 C C . GLY B 470 ? 2.0172 1.6757 1.9855 0.0738 0.3356 0.1254 2117 GLY B C 8157 O O . GLY B 470 ? 1.8381 1.5542 1.8189 0.1016 0.3332 0.1593 2117 GLY B O 8158 N N . ASN B 471 ? 2.1045 1.6844 2.0700 0.0759 0.3616 0.1161 2118 ASN B N 8159 C CA . ASN B 471 ? 2.2493 1.7895 2.2207 0.1125 0.3936 0.1454 2118 ASN B CA 8160 C C . ASN B 471 ? 2.1885 1.7818 2.1812 0.1579 0.4033 0.1821 2118 ASN B C 8161 O O . ASN B 471 ? 1.6838 1.3400 1.6917 0.1579 0.3893 0.1789 2118 ASN B O 8162 C CB . ASN B 471 ? 2.2870 1.7271 2.2516 0.1029 0.4263 0.1230 2118 ASN B CB 8163 C CG . ASN B 471 ? 2.2352 1.6560 2.1963 0.0827 0.4284 0.0852 2118 ASN B CG 8164 O OD1 . ASN B 471 ? 2.2667 1.7332 2.2374 0.0972 0.4240 0.0875 2118 ASN B OD1 8165 N ND2 . ASN B 471 ? 2.3135 1.6736 2.2606 0.0475 0.4347 0.0520 2118 ASN B ND2 8166 N N . SER B 472 ? 2.5733 2.1482 2.5693 0.1972 0.4277 0.2218 2119 SER B N 8167 C CA . SER B 472 ? 2.9400 2.5632 2.9607 0.2516 0.4447 0.2688 2119 SER B CA 8168 C C . SER B 472 ? 3.0402 2.7136 3.0857 0.2592 0.4440 0.2606 2119 SER B C 8169 O O . SER B 472 ? 3.5596 3.1655 3.6025 0.2623 0.4743 0.2360 2119 SER B O 8170 C CB . SER B 472 ? 2.9440 2.4734 2.9621 0.2939 0.4981 0.2943 2119 SER B CB 8171 O OG . SER B 472 ? 2.6632 2.1736 2.6659 0.3003 0.5003 0.3213 2119 SER B OG 8172 N N . THR B 473 ? 2.5876 2.3802 2.6535 0.2586 0.4102 0.2807 2120 THR B N 8173 C CA . THR B 473 ? 2.1910 2.0459 2.2853 0.2614 0.4073 0.2764 2120 THR B CA 8174 C C . THR B 473 ? 2.0840 2.0656 2.2195 0.3025 0.3993 0.3359 2120 THR B C 8175 O O . THR B 473 ? 1.8208 1.8150 1.9888 0.3578 0.4358 0.3713 2120 THR B O 8176 C CB . THR B 473 ? 2.0383 1.9079 2.1158 0.1994 0.3709 0.2280 2120 THR B CB 8177 O OG1 . THR B 473 ? 2.3390 2.3117 2.4457 0.1928 0.3518 0.2362 2120 THR B OG1 8178 C CG2 . THR B 473 ? 1.8071 1.6806 1.8542 0.1626 0.3374 0.2181 2120 THR B CG2 8179 N N . GLY B 474 ? 2.0770 2.1497 2.2075 0.2760 0.3538 0.3486 2121 GLY B N 8180 C CA . GLY B 474 ? 2.2436 2.4599 2.4097 0.2993 0.3326 0.4029 2121 GLY B CA 8181 C C . GLY B 474 ? 2.3237 2.6119 2.4606 0.2438 0.2778 0.3921 2121 GLY B C 8182 O O . GLY B 474 ? 2.4540 2.7240 2.5549 0.2409 0.2672 0.4020 2121 GLY B O 8183 N N . THR B 475 ? 2.2212 2.5802 2.3676 0.1976 0.2475 0.3694 2122 THR B N 8184 C CA . THR B 475 ? 2.0320 2.4623 2.1475 0.1374 0.1976 0.3555 2122 THR B CA 8185 C C . THR B 475 ? 1.9269 2.2627 1.9890 0.0777 0.1869 0.2918 2122 THR B C 8186 O O . THR B 475 ? 1.6842 2.0078 1.6941 0.0403 0.1630 0.2755 2122 THR B O 8187 C CB . THR B 475 ? 2.1104 2.6830 2.2711 0.1172 0.1724 0.3726 2122 THR B CB 8188 O OG1 . THR B 475 ? 2.2386 2.8228 2.3589 0.0411 0.1358 0.3308 2122 THR B OG1 8189 C CG2 . THR B 475 ? 2.0489 2.6137 2.2617 0.1427 0.2055 0.3695 2122 THR B CG2 8190 N N . LEU B 476 ? 1.9436 2.2185 2.0183 0.0713 0.2068 0.2591 2123 LEU B N 8191 C CA . LEU B 476 ? 1.9217 2.1003 1.9561 0.0297 0.2065 0.2060 2123 LEU B CA 8192 C C . LEU B 476 ? 1.9243 2.0459 1.9814 0.0432 0.2359 0.1852 2123 LEU B C 8193 O O . LEU B 476 ? 1.8699 2.0412 1.9704 0.0714 0.2510 0.2060 2123 LEU B O 8194 C CB . LEU B 476 ? 1.8404 2.0606 1.8462 -0.0317 0.1727 0.1826 2123 LEU B CB 8195 C CG . LEU B 476 ? 1.8376 2.0997 1.8661 -0.0634 0.1665 0.1665 2123 LEU B CG 8196 C CD1 . LEU B 476 ? 1.6960 2.0590 1.7912 -0.0308 0.1742 0.2040 2123 LEU B CD1 8197 C CD2 . LEU B 476 ? 1.8251 1.9842 1.8360 -0.0757 0.1855 0.1259 2123 LEU B CD2 8198 N N . MET B 477 ? 1.9307 1.9539 1.9573 0.0244 0.2449 0.1469 2124 MET B N 8199 C CA . MET B 477 ? 1.8169 1.7837 1.8542 0.0351 0.2711 0.1266 2124 MET B CA 8200 C C . MET B 477 ? 1.7571 1.7496 1.7982 0.0041 0.2626 0.1053 2124 MET B C 8201 O O . MET B 477 ? 1.5546 1.5352 1.5679 -0.0373 0.2434 0.0824 2124 MET B O 8202 C CB . MET B 477 ? 1.8128 1.6744 1.8226 0.0322 0.2861 0.1011 2124 MET B CB 8203 C CG . MET B 477 ? 1.9323 1.7408 1.9538 0.0622 0.3211 0.0980 2124 MET B CG 8204 S SD . MET B 477 ? 2.2397 1.9633 2.2339 0.0335 0.3294 0.0518 2124 MET B SD 8205 C CE . MET B 477 ? 2.1593 1.8431 2.1613 0.0681 0.3719 0.0505 2124 MET B CE 8206 N N . VAL B 478 ? 1.7453 1.7671 1.8194 0.0291 0.2830 0.1162 2125 VAL B N 8207 C CA . VAL B 478 ? 1.6278 1.6832 1.7151 0.0116 0.2849 0.1050 2125 VAL B CA 8208 C C . VAL B 478 ? 1.6900 1.6562 1.7499 0.0069 0.3035 0.0711 2125 VAL B C 8209 O O . VAL B 478 ? 1.9131 1.8174 1.9660 0.0349 0.3293 0.0665 2125 VAL B O 8210 C CB . VAL B 478 ? 1.6003 1.7201 1.7354 0.0534 0.3091 0.1365 2125 VAL B CB 8211 C CG1 . VAL B 478 ? 1.4540 1.6512 1.6145 0.0295 0.3029 0.1381 2125 VAL B CG1 8212 C CG2 . VAL B 478 ? 1.6326 1.8158 1.7980 0.0899 0.3073 0.1816 2125 VAL B CG2 8213 N N . PHE B 479 ? 1.7395 1.6993 1.7813 -0.0298 0.2921 0.0484 2126 PHE B N 8214 C CA . PHE B 479 ? 1.8445 1.7325 1.8569 -0.0377 0.3043 0.0191 2126 PHE B CA 8215 C C . PHE B 479 ? 1.9914 1.9030 2.0123 -0.0352 0.3214 0.0161 2126 PHE B C 8216 O O . PHE B 479 ? 2.1335 2.1205 2.1844 -0.0394 0.3190 0.0339 2126 PHE B O 8217 C CB . PHE B 479 ? 1.7962 1.6483 1.7759 -0.0739 0.2835 -0.0002 2126 PHE B CB 8218 C CG . PHE B 479 ? 1.7852 1.6049 1.7519 -0.0739 0.2730 0.0010 2126 PHE B CG 8219 C CD1 . PHE B 479 ? 1.8142 1.5716 1.7670 -0.0655 0.2819 -0.0107 2126 PHE B CD1 8220 C CD2 . PHE B 479 ? 1.8455 1.6993 1.8113 -0.0855 0.2550 0.0137 2126 PHE B CD2 8221 C CE1 . PHE B 479 ? 1.7772 1.5086 1.7220 -0.0649 0.2759 -0.0066 2126 PHE B CE1 8222 C CE2 . PHE B 479 ? 1.8711 1.6939 1.8205 -0.0832 0.2493 0.0160 2126 PHE B CE2 8223 C CZ . PHE B 479 ? 1.9077 1.6699 1.8499 -0.0709 0.2612 0.0075 2126 PHE B CZ 8224 N N . PHE B 480 ? 2.0235 1.8748 2.0165 -0.0312 0.3389 -0.0061 2127 PHE B N 8225 C CA . PHE B 480 ? 2.0906 1.9572 2.0809 -0.0301 0.3571 -0.0110 2127 PHE B CA 8226 C C . PHE B 480 ? 2.1125 1.9498 2.0660 -0.0622 0.3460 -0.0323 2127 PHE B C 8227 O O . PHE B 480 ? 2.0351 1.8146 1.9543 -0.0701 0.3423 -0.0524 2127 PHE B O 8228 C CB . PHE B 480 ? 2.2531 2.0831 2.2365 0.0058 0.3944 -0.0152 2127 PHE B CB 8229 C CG . PHE B 480 ? 2.1820 2.0526 2.2083 0.0464 0.4127 0.0161 2127 PHE B CG 8230 C CD1 . PHE B 480 ? 2.2035 2.1726 2.2784 0.0557 0.4134 0.0469 2127 PHE B CD1 8231 C CD2 . PHE B 480 ? 2.2193 2.0352 2.2401 0.0750 0.4302 0.0189 2127 PHE B CD2 8232 C CE1 . PHE B 480 ? 2.3478 2.3706 2.4685 0.0979 0.4294 0.0837 2127 PHE B CE1 8233 C CE2 . PHE B 480 ? 2.2786 2.1335 2.3397 0.1197 0.4505 0.0552 2127 PHE B CE2 8234 C CZ . PHE B 480 ? 2.3487 2.3126 2.4615 0.1335 0.4489 0.0896 2127 PHE B CZ 8235 N N . GLY B 481 ? 2.1423 2.0264 2.1059 -0.0814 0.3412 -0.0238 2128 GLY B N 8236 C CA . GLY B 481 ? 2.1201 1.9818 2.0512 -0.1077 0.3349 -0.0354 2128 GLY B CA 8237 C C . GLY B 481 ? 2.0509 1.9010 1.9591 -0.0978 0.3588 -0.0445 2128 GLY B C 8238 O O . GLY B 481 ? 2.3455 2.1748 2.2469 -0.0722 0.3804 -0.0523 2128 GLY B O 8239 N N . ASN B 482 ? 1.7468 1.6036 1.6372 -0.1179 0.3588 -0.0431 2129 ASN B N 8240 C CA . ASN B 482 ? 1.7663 1.6043 1.6190 -0.1129 0.3779 -0.0533 2129 ASN B CA 8241 C C . ASN B 482 ? 1.7442 1.6244 1.6180 -0.0956 0.4083 -0.0428 2129 ASN B C 8242 O O . ASN B 482 ? 1.6407 1.5780 1.5659 -0.0918 0.4101 -0.0229 2129 ASN B O 8243 C CB . ASN B 482 ? 1.7248 1.5518 1.5477 -0.1367 0.3679 -0.0501 2129 ASN B CB 8244 C CG . ASN B 482 ? 1.7114 1.5118 1.5299 -0.1506 0.3417 -0.0499 2129 ASN B CG 8245 O OD1 . ASN B 482 ? 1.6034 1.4131 1.4511 -0.1559 0.3299 -0.0444 2129 ASN B OD1 8246 N ND2 . ASN B 482 ? 1.6629 1.4343 1.4437 -0.1551 0.3332 -0.0538 2129 ASN B ND2 8247 N N . VAL B 483 ? 1.7411 1.5985 1.5748 -0.0848 0.4326 -0.0546 2130 VAL B N 8248 C CA . VAL B 483 ? 1.8581 1.7552 1.7076 -0.0660 0.4686 -0.0425 2130 VAL B CA 8249 C C . VAL B 483 ? 1.8833 1.7773 1.6904 -0.0805 0.4799 -0.0431 2130 VAL B C 8250 O O . VAL B 483 ? 1.9684 1.8799 1.7678 -0.0646 0.5149 -0.0384 2130 VAL B O 8251 C CB . VAL B 483 ? 2.0273 1.8957 1.8677 -0.0272 0.5028 -0.0533 2130 VAL B CB 8252 C CG1 . VAL B 483 ? 2.0739 2.0077 1.9629 0.0018 0.5399 -0.0269 2130 VAL B CG1 8253 C CG2 . VAL B 483 ? 1.9957 1.8326 1.8508 -0.0164 0.4886 -0.0596 2130 VAL B CG2 8254 N N . ASP B 484 ? 1.9171 1.7888 1.6959 -0.1072 0.4532 -0.0454 2131 ASP B N 8255 C CA . ASP B 484 ? 2.0571 1.9279 1.7974 -0.1211 0.4607 -0.0381 2131 ASP B CA 8256 C C . ASP B 484 ? 1.9802 1.8355 1.7118 -0.1461 0.4325 -0.0283 2131 ASP B C 8257 O O . ASP B 484 ? 1.8318 1.6696 1.5772 -0.1522 0.4066 -0.0326 2131 ASP B O 8258 C CB . ASP B 484 ? 2.3784 2.2109 2.0467 -0.1105 0.4755 -0.0591 2131 ASP B CB 8259 C CG . ASP B 484 ? 2.6808 2.4708 2.3052 -0.1217 0.4446 -0.0775 2131 ASP B CG 8260 O OD1 . ASP B 484 ? 2.8760 2.6528 2.5273 -0.1229 0.4233 -0.0847 2131 ASP B OD1 8261 O OD2 . ASP B 484 ? 2.7769 2.5540 2.3414 -0.1296 0.4413 -0.0818 2131 ASP B OD2 8262 N N . SER B 485 ? 2.0037 1.8611 1.7080 -0.1567 0.4434 -0.0132 2132 SER B N 8263 C CA . SER B 485 ? 2.0013 1.8397 1.6940 -0.1755 0.4303 0.0043 2132 SER B CA 8264 C C . SER B 485 ? 2.1327 1.9351 1.7873 -0.1720 0.4049 0.0000 2132 SER B C 8265 O O . SER B 485 ? 2.1830 1.9683 1.8183 -0.1781 0.4021 0.0203 2132 SER B O 8266 C CB . SER B 485 ? 1.9270 1.7756 1.5954 -0.1817 0.4568 0.0248 2132 SER B CB 8267 O OG . SER B 485 ? 1.9050 1.7576 1.5289 -0.1638 0.4738 0.0145 2132 SER B OG 8268 N N . SER B 486 ? 2.1994 1.9920 1.8457 -0.1621 0.3888 -0.0227 2133 SER B N 8269 C CA . SER B 486 ? 2.2577 2.0347 1.8678 -0.1613 0.3655 -0.0252 2133 SER B CA 8270 C C . SER B 486 ? 2.4085 2.1747 2.0154 -0.1586 0.3502 -0.0533 2133 SER B C 8271 O O . SER B 486 ? 2.3812 2.1445 1.9744 -0.1630 0.3266 -0.0548 2133 SER B O 8272 C CB . SER B 486 ? 2.3431 2.1278 1.8940 -0.1597 0.3732 -0.0175 2133 SER B CB 8273 O OG . SER B 486 ? 2.5192 2.3056 2.0427 -0.1550 0.3926 -0.0404 2133 SER B OG 8274 N N . GLY B 487 ? 2.5962 2.3579 2.2154 -0.1510 0.3670 -0.0730 2134 GLY B N 8275 C CA . GLY B 487 ? 2.5915 2.3300 2.2139 -0.1483 0.3599 -0.0983 2134 GLY B CA 8276 C C . GLY B 487 ? 2.5189 2.2566 2.1856 -0.1516 0.3371 -0.0890 2134 GLY B C 8277 O O . GLY B 487 ? 2.5092 2.2603 2.2062 -0.1539 0.3346 -0.0681 2134 GLY B O 8278 N N . ILE B 488 ? 2.2742 1.9917 1.9403 -0.1547 0.3234 -0.1056 2135 ILE B N 8279 C CA . ILE B 488 ? 2.0211 1.7393 1.7160 -0.1594 0.3003 -0.0947 2135 ILE B CA 8280 C C . ILE B 488 ? 2.0617 1.7588 1.7836 -0.1562 0.2967 -0.1075 2135 ILE B C 8281 O O . ILE B 488 ? 2.1811 1.8664 1.8931 -0.1666 0.2835 -0.1187 2135 ILE B O 8282 C CB . ILE B 488 ? 1.7959 1.5289 1.4626 -0.1698 0.2804 -0.0850 2135 ILE B CB 8283 C CG1 . ILE B 488 ? 1.7370 1.4726 1.4317 -0.1720 0.2597 -0.0757 2135 ILE B CG1 8284 C CG2 . ILE B 488 ? 1.6161 1.3497 1.2285 -0.1809 0.2809 -0.1057 2135 ILE B CG2 8285 C CD1 . ILE B 488 ? 1.6959 1.4580 1.3839 -0.1709 0.2452 -0.0483 2135 ILE B CD1 8286 N N . LYS B 489 ? 2.0047 1.7028 1.7616 -0.1432 0.3082 -0.1025 2136 LYS B N 8287 C CA . LYS B 489 ? 1.9014 1.5789 1.6813 -0.1335 0.3119 -0.1100 2136 LYS B CA 8288 C C . LYS B 489 ? 1.9932 1.6670 1.7901 -0.1410 0.2909 -0.1022 2136 LYS B C 8289 O O . LYS B 489 ? 2.1764 1.8661 1.9848 -0.1446 0.2807 -0.0856 2136 LYS B O 8290 C CB . LYS B 489 ? 1.8209 1.5197 1.6378 -0.1150 0.3262 -0.0968 2136 LYS B CB 8291 C CG . LYS B 489 ? 1.8762 1.5527 1.7057 -0.0931 0.3453 -0.1020 2136 LYS B CG 8292 C CD . LYS B 489 ? 2.0666 1.7467 1.8904 -0.0721 0.3781 -0.1043 2136 LYS B CD 8293 C CE . LYS B 489 ? 2.0510 1.6974 1.8831 -0.0430 0.4058 -0.1058 2136 LYS B CE 8294 N NZ . LYS B 489 ? 2.0504 1.6336 1.8592 -0.0539 0.4014 -0.1251 2136 LYS B NZ 8295 N N . HIS B 490 ? 2.0364 1.6838 1.8324 -0.1443 0.2886 -0.1143 2137 HIS B N 8296 C CA . HIS B 490 ? 2.0534 1.6993 1.8696 -0.1493 0.2730 -0.1052 2137 HIS B CA 8297 C C . HIS B 490 ? 2.1539 1.7759 1.9909 -0.1368 0.2836 -0.1059 2137 HIS B C 8298 O O . HIS B 490 ? 2.5939 2.1825 2.4207 -0.1410 0.2930 -0.1213 2137 HIS B O 8299 C CB . HIS B 490 ? 1.9652 1.6137 1.7642 -0.1698 0.2583 -0.1132 2137 HIS B CB 8300 C CG . HIS B 490 ? 2.0295 1.6737 1.8517 -0.1761 0.2492 -0.1079 2137 HIS B CG 8301 N ND1 . HIS B 490 ? 2.2951 1.9407 2.1098 -0.1997 0.2396 -0.1194 2137 HIS B ND1 8302 C CD2 . HIS B 490 ? 2.0596 1.7010 1.9104 -0.1648 0.2491 -0.0922 2137 HIS B CD2 8303 C CE1 . HIS B 490 ? 2.4155 2.0619 2.2600 -0.2009 0.2357 -0.1085 2137 HIS B CE1 8304 N NE2 . HIS B 490 ? 2.3799 2.0206 2.2438 -0.1777 0.2426 -0.0921 2137 HIS B NE2 8305 N N . ASN B 491 ? 2.1061 1.7434 1.9675 -0.1232 0.2838 -0.0888 2138 ASN B N 8306 C CA . ASN B 491 ? 2.0014 1.6246 1.8823 -0.1067 0.2932 -0.0818 2138 ASN B CA 8307 C C . ASN B 491 ? 2.0609 1.6705 1.9490 -0.1142 0.2827 -0.0767 2138 ASN B C 8308 O O . ASN B 491 ? 2.1000 1.7254 1.9887 -0.1222 0.2693 -0.0682 2138 ASN B O 8309 C CB . ASN B 491 ? 1.9958 1.6557 1.8975 -0.0928 0.2931 -0.0631 2138 ASN B CB 8310 C CG . ASN B 491 ? 2.2557 1.9454 2.1600 -0.0866 0.3036 -0.0622 2138 ASN B CG 8311 O OD1 . ASN B 491 ? 2.4395 2.1222 2.3476 -0.0669 0.3250 -0.0636 2138 ASN B OD1 8312 N ND2 . ASN B 491 ? 2.2401 1.9595 2.1417 -0.1022 0.2933 -0.0580 2138 ASN B ND2 8313 N N . ILE B 492 ? 2.0499 1.6253 1.9417 -0.1112 0.2934 -0.0806 2139 ILE B N 8314 C CA . ILE B 492 ? 1.8932 1.4585 1.7964 -0.1181 0.2874 -0.0726 2139 ILE B CA 8315 C C . ILE B 492 ? 1.7625 1.3301 1.6796 -0.0974 0.2920 -0.0521 2139 ILE B C 8316 O O . ILE B 492 ? 1.6579 1.2239 1.5799 -0.0769 0.3046 -0.0450 2139 ILE B O 8317 C CB . ILE B 492 ? 1.8935 1.4236 1.7929 -0.1374 0.2939 -0.0870 2139 ILE B CB 8318 C CG1 . ILE B 492 ? 1.9966 1.4824 1.8746 -0.1375 0.3152 -0.1076 2139 ILE B CG1 8319 C CG2 . ILE B 492 ? 1.7821 1.3401 1.6807 -0.1639 0.2747 -0.0917 2139 ILE B CG2 8320 C CD1 . ILE B 492 ? 2.0912 1.5261 1.9594 -0.1611 0.3272 -0.1238 2139 ILE B CD1 8321 N N . PHE B 493 ? 1.7790 1.3555 1.7001 -0.1008 0.2829 -0.0403 2140 PHE B N 8322 C CA . PHE B 493 ? 1.8852 1.4627 1.8097 -0.0857 0.2857 -0.0215 2140 PHE B CA 8323 C C . PHE B 493 ? 2.1572 1.6992 2.0913 -0.0816 0.3008 -0.0158 2140 PHE B C 8324 O O . PHE B 493 ? 1.8656 1.3987 1.8057 -0.0935 0.3009 -0.0137 2140 PHE B O 8325 C CB . PHE B 493 ? 1.8232 1.4145 1.7361 -0.0917 0.2753 -0.0144 2140 PHE B CB 8326 C CG . PHE B 493 ? 1.7607 1.3743 1.6596 -0.1001 0.2652 -0.0199 2140 PHE B CG 8327 C CD1 . PHE B 493 ? 1.6102 1.2510 1.5104 -0.0965 0.2619 -0.0186 2140 PHE B CD1 8328 C CD2 . PHE B 493 ? 1.7174 1.3259 1.6038 -0.1107 0.2621 -0.0226 2140 PHE B CD2 8329 C CE1 . PHE B 493 ? 1.4902 1.1506 1.3789 -0.1106 0.2544 -0.0234 2140 PHE B CE1 8330 C CE2 . PHE B 493 ? 1.5834 1.2001 1.4531 -0.1205 0.2579 -0.0268 2140 PHE B CE2 8331 C CZ . PHE B 493 ? 1.5036 1.1454 1.3741 -0.1240 0.2534 -0.0289 2140 PHE B CZ 8332 N N . ASN B 494 ? 2.5750 2.0983 2.5123 -0.0628 0.3169 -0.0102 2141 ASN B N 8333 C CA . ASN B 494 ? 2.3808 1.8506 2.3213 -0.0594 0.3407 -0.0100 2141 ASN B CA 8334 C C . ASN B 494 ? 1.8857 1.3432 1.8326 -0.0617 0.3445 0.0060 2141 ASN B C 8335 O O . ASN B 494 ? 1.5450 0.9789 1.4980 -0.0859 0.3490 -0.0039 2141 ASN B O 8336 C CB . ASN B 494 ? 2.6640 2.1151 2.6059 -0.0260 0.3638 0.0041 2141 ASN B CB 8337 C CG . ASN B 494 ? 2.9534 2.4523 2.8987 -0.0097 0.3567 0.0070 2141 ASN B CG 8338 O OD1 . ASN B 494 ? 3.0971 2.5774 3.0383 -0.0017 0.3734 -0.0044 2141 ASN B OD1 8339 N ND2 . ASN B 494 ? 2.9670 2.5256 2.9171 -0.0065 0.3348 0.0223 2141 ASN B ND2 8340 N N . PRO B 495 ? 1.7345 1.2128 1.6790 -0.0384 0.3431 0.0318 2142 PRO B N 8341 C CA . PRO B 495 ? 1.7732 1.2644 1.7125 -0.0412 0.3368 0.0455 2142 PRO B CA 8342 C C . PRO B 495 ? 1.7460 1.2733 1.6749 -0.0555 0.3150 0.0335 2142 PRO B C 8343 O O . PRO B 495 ? 1.5971 1.1515 1.5187 -0.0539 0.3027 0.0274 2142 PRO B O 8344 C CB . PRO B 495 ? 1.7209 1.2252 1.6501 -0.0123 0.3411 0.0741 2142 PRO B CB 8345 C CG . PRO B 495 ? 1.5530 1.0831 1.4872 0.0038 0.3375 0.0753 2142 PRO B CG 8346 C CD . PRO B 495 ? 1.5951 1.0887 1.5397 -0.0061 0.3499 0.0521 2142 PRO B CD 8347 N N . PRO B 496 ? 1.7866 1.3128 1.7165 -0.0682 0.3141 0.0326 2143 PRO B N 8348 C CA . PRO B 496 ? 1.7344 1.2802 1.6573 -0.0801 0.3015 0.0216 2143 PRO B CA 8349 C C . PRO B 496 ? 1.8089 1.3600 1.7010 -0.0746 0.2987 0.0281 2143 PRO B C 8350 O O . PRO B 496 ? 1.9893 1.5285 1.8693 -0.0668 0.3093 0.0416 2143 PRO B O 8351 C CB . PRO B 496 ? 1.7258 1.2709 1.6714 -0.0923 0.3073 0.0233 2143 PRO B CB 8352 C CG . PRO B 496 ? 1.8745 1.3989 1.8291 -0.0861 0.3244 0.0395 2143 PRO B CG 8353 C CD . PRO B 496 ? 1.7902 1.2978 1.7304 -0.0688 0.3294 0.0466 2143 PRO B CD 8354 N N . ILE B 497 ? 1.8028 1.3664 1.6771 -0.0817 0.2872 0.0173 2144 ILE B N 8355 C CA . ILE B 497 ? 1.6830 1.2413 1.5174 -0.0853 0.2858 0.0171 2144 ILE B CA 8356 C C . ILE B 497 ? 1.6755 1.2070 1.4958 -0.0825 0.3014 0.0214 2144 ILE B C 8357 O O . ILE B 497 ? 1.5844 1.1165 1.4295 -0.0808 0.3075 0.0237 2144 ILE B O 8358 C CB . ILE B 497 ? 1.6442 1.2159 1.4623 -0.1004 0.2735 0.0038 2144 ILE B CB 8359 C CG1 . ILE B 497 ? 1.7316 1.3409 1.5579 -0.0994 0.2608 0.0072 2144 ILE B CG1 8360 C CG2 . ILE B 497 ? 1.5963 1.1422 1.3656 -0.1123 0.2783 -0.0019 2144 ILE B CG2 8361 C CD1 . ILE B 497 ? 1.8311 1.4659 1.6695 -0.1103 0.2518 -0.0028 2144 ILE B CD1 8362 N N . ILE B 498 ? 1.6882 1.2010 1.4665 -0.0809 0.3087 0.0246 2145 ILE B N 8363 C CA . ILE B 498 ? 1.6864 1.1695 1.4469 -0.0708 0.3312 0.0331 2145 ILE B CA 8364 C C . ILE B 498 ? 1.7682 1.2168 1.4632 -0.0814 0.3371 0.0203 2145 ILE B C 8365 O O . ILE B 498 ? 1.8580 1.3002 1.5080 -0.0876 0.3346 0.0185 2145 ILE B O 8366 C CB . ILE B 498 ? 1.7401 1.2253 1.5110 -0.0574 0.3416 0.0514 2145 ILE B CB 8367 C CG1 . ILE B 498 ? 1.6023 1.0641 1.3667 -0.0443 0.3697 0.0637 2145 ILE B CG1 8368 C CG2 . ILE B 498 ? 1.8274 1.3201 1.5629 -0.0575 0.3319 0.0555 2145 ILE B CG2 8369 C CD1 . ILE B 498 ? 1.5358 1.0022 1.3308 -0.0407 0.3781 0.0654 2145 ILE B CD1 8370 N N . ALA B 499 ? 1.8213 1.2470 1.5076 -0.0859 0.3449 0.0117 2146 ALA B N 8371 C CA . ALA B 499 ? 1.9000 1.2797 1.5205 -0.1038 0.3528 -0.0058 2146 ALA B CA 8372 C C . ALA B 499 ? 1.8993 1.2295 1.5059 -0.0930 0.3813 -0.0042 2146 ALA B C 8373 O O . ALA B 499 ? 1.8413 1.1912 1.4980 -0.0722 0.3880 0.0129 2146 ALA B O 8374 C CB . ALA B 499 ? 1.7454 1.1529 1.3620 -0.1321 0.3257 -0.0211 2146 ALA B CB 8375 N N . ARG B 500 ? 2.0265 1.2924 1.5611 -0.1085 0.3990 -0.0209 2147 ARG B N 8376 C CA . ARG B 500 ? 2.1034 1.3078 1.6124 -0.1017 0.4291 -0.0215 2147 ARG B CA 8377 C C . ARG B 500 ? 2.0752 1.2856 1.5861 -0.1288 0.4116 -0.0345 2147 ARG B C 8378 O O . ARG B 500 ? 1.9128 1.1232 1.4527 -0.1149 0.4195 -0.0221 2147 ARG B O 8379 C CB . ARG B 500 ? 2.2209 1.3325 1.6382 -0.1085 0.4647 -0.0371 2147 ARG B CB 8380 C CG . ARG B 500 ? 2.3645 1.3978 1.7538 -0.0922 0.5068 -0.0325 2147 ARG B CG 8381 C CD . ARG B 500 ? 2.5794 1.5001 1.8629 -0.1060 0.5469 -0.0554 2147 ARG B CD 8382 N NE . ARG B 500 ? 2.7287 1.5666 1.9882 -0.0857 0.5925 -0.0471 2147 ARG B NE 8383 C CZ . ARG B 500 ? 2.8850 1.6499 2.1137 -0.0447 0.6481 -0.0316 2147 ARG B CZ 8384 N NH1 . ARG B 500 ? 2.9794 1.7447 2.1956 -0.0235 0.6643 -0.0256 2147 ARG B NH1 8385 N NH2 . ARG B 500 ? 2.8753 1.5647 2.0844 -0.0223 0.6915 -0.0192 2147 ARG B NH2 8386 N N . TYR B 501 ? 2.1627 1.3851 1.6426 -0.1676 0.3882 -0.0562 2148 TYR B N 8387 C CA . TYR B 501 ? 2.0890 1.3266 1.5691 -0.2012 0.3703 -0.0694 2148 TYR B CA 8388 C C . TYR B 501 ? 2.0120 1.3446 1.5592 -0.2017 0.3330 -0.0619 2148 TYR B C 8389 O O . TYR B 501 ? 2.1757 1.5533 1.7491 -0.1882 0.3183 -0.0534 2148 TYR B O 8390 C CB . TYR B 501 ? 2.2021 1.4092 1.6092 -0.2488 0.3658 -0.0961 2148 TYR B CB 8391 C CG . TYR B 501 ? 2.4639 1.5587 1.7840 -0.2587 0.4064 -0.1124 2148 TYR B CG 8392 C CD1 . TYR B 501 ? 2.4668 1.5136 1.7523 -0.2307 0.4344 -0.1078 2148 TYR B CD1 8393 C CD2 . TYR B 501 ? 2.6766 1.7054 1.9437 -0.2976 0.4218 -0.1329 2148 TYR B CD2 8394 C CE1 . TYR B 501 ? 2.6404 1.5725 1.8381 -0.2368 0.4791 -0.1240 2148 TYR B CE1 8395 C CE2 . TYR B 501 ? 2.7509 1.6582 1.9275 -0.3082 0.4661 -0.1509 2148 TYR B CE2 8396 C CZ . TYR B 501 ? 2.7520 1.6096 1.8926 -0.2759 0.4955 -0.1469 2148 TYR B CZ 8397 O OH . TYR B 501 ? 2.9512 1.6777 1.9954 -0.2835 0.5462 -0.1657 2148 TYR B OH 8398 N N . ILE B 502 ? 1.8121 1.1686 1.3827 -0.2163 0.3226 -0.0642 2149 ILE B N 8399 C CA . ILE B 502 ? 1.6516 1.0907 1.2776 -0.2181 0.2934 -0.0593 2149 ILE B CA 8400 C C . ILE B 502 ? 1.6535 1.1094 1.2738 -0.2533 0.2849 -0.0694 2149 ILE B C 8401 O O . ILE B 502 ? 1.7181 1.1307 1.3222 -0.2614 0.3021 -0.0719 2149 ILE B O 8402 C CB . ILE B 502 ? 1.5596 1.0288 1.2441 -0.1843 0.2917 -0.0436 2149 ILE B CB 8403 C CG1 . ILE B 502 ? 1.4755 1.0140 1.2058 -0.1848 0.2693 -0.0417 2149 ILE B CG1 8404 C CG2 . ILE B 502 ? 1.5068 0.9426 1.1912 -0.1741 0.3096 -0.0369 2149 ILE B CG2 8405 C CD1 . ILE B 502 ? 1.4251 0.9874 1.2003 -0.1577 0.2664 -0.0321 2149 ILE B CD1 8406 N N . ARG B 503 ? 1.7044 1.2270 1.3405 -0.2729 0.2605 -0.0710 2150 ARG B N 8407 C CA . ARG B 503 ? 1.8021 1.3558 1.4381 -0.3120 0.2513 -0.0783 2150 ARG B CA 8408 C C . ARG B 503 ? 1.6955 1.3364 1.3975 -0.2983 0.2348 -0.0644 2150 ARG B C 8409 O O . ARG B 503 ? 1.7338 1.4273 1.4678 -0.2755 0.2213 -0.0524 2150 ARG B O 8410 C CB . ARG B 503 ? 1.8833 1.4478 1.4731 -0.3568 0.2381 -0.0917 2150 ARG B CB 8411 C CG . ARG B 503 ? 1.8299 1.4046 1.4029 -0.4111 0.2347 -0.1042 2150 ARG B CG 8412 C CD . ARG B 503 ? 1.9194 1.4563 1.4161 -0.4622 0.2326 -0.1269 2150 ARG B CD 8413 N NE . ARG B 503 ? 1.9578 1.5692 1.4546 -0.4660 0.2033 -0.1208 2150 ARG B NE 8414 C CZ . ARG B 503 ? 2.2854 1.8850 1.7131 -0.5121 0.1937 -0.1394 2150 ARG B CZ 8415 N NH1 . ARG B 503 ? 2.5373 2.0413 1.8869 -0.5607 0.2145 -0.1696 2150 ARG B NH1 8416 N NH2 . ARG B 503 ? 2.3877 2.0661 1.8175 -0.5106 0.1652 -0.1276 2150 ARG B NH2 8417 N N . LEU B 504 ? 1.5458 1.1961 1.2652 -0.3088 0.2406 -0.0640 2151 LEU B N 8418 C CA . LEU B 504 ? 1.5010 1.2287 1.2771 -0.2940 0.2312 -0.0514 2151 LEU B CA 8419 C C . LEU B 504 ? 1.6117 1.3990 1.4012 -0.3330 0.2234 -0.0503 2151 LEU B C 8420 O O . LEU B 504 ? 1.6749 1.4315 1.4457 -0.3613 0.2355 -0.0573 2151 LEU B O 8421 C CB . LEU B 504 ? 1.3841 1.0921 1.1817 -0.2606 0.2443 -0.0468 2151 LEU B CB 8422 C CG . LEU B 504 ? 1.4338 1.1548 1.2474 -0.2620 0.2542 -0.0438 2151 LEU B CG 8423 C CD1 . LEU B 504 ? 1.4646 1.2654 1.3149 -0.2740 0.2480 -0.0363 2151 LEU B CD1 8424 C CD2 . LEU B 504 ? 1.4006 1.1108 1.2289 -0.2258 0.2599 -0.0407 2151 LEU B CD2 8425 N N . HIS B 505 ? 1.7101 1.5862 1.5339 -0.3335 0.2044 -0.0377 2152 HIS B N 8426 C CA . HIS B 505 ? 1.7614 1.7226 1.6122 -0.3693 0.1932 -0.0300 2152 HIS B CA 8427 C C . HIS B 505 ? 1.7320 1.7586 1.6459 -0.3332 0.2005 -0.0101 2152 HIS B C 8428 O O . HIS B 505 ? 1.6374 1.6848 1.5786 -0.2874 0.2005 0.0031 2152 HIS B O 8429 C CB . HIS B 505 ? 1.8350 1.8702 1.6855 -0.3911 0.1661 -0.0221 2152 HIS B CB 8430 C CG . HIS B 505 ? 1.9935 1.9604 1.7742 -0.4152 0.1608 -0.0418 2152 HIS B CG 8431 N ND1 . HIS B 505 ? 2.1431 2.1432 1.8878 -0.4707 0.1405 -0.0507 2152 HIS B ND1 8432 C CD2 . HIS B 505 ? 1.9687 1.8381 1.7065 -0.3923 0.1751 -0.0541 2152 HIS B CD2 8433 C CE1 . HIS B 505 ? 2.1783 2.0933 1.8531 -0.4795 0.1454 -0.0704 2152 HIS B CE1 8434 N NE2 . HIS B 505 ? 2.0516 1.8888 1.7253 -0.4298 0.1677 -0.0706 2152 HIS B NE2 8435 N N . PRO B 506 ? 1.7401 1.7885 1.6719 -0.3524 0.2119 -0.0082 2153 PRO B N 8436 C CA . PRO B 506 ? 1.6927 1.8144 1.6822 -0.3254 0.2229 0.0117 2153 PRO B CA 8437 C C . PRO B 506 ? 1.5712 1.8232 1.6182 -0.3260 0.2078 0.0388 2153 PRO B C 8438 O O . PRO B 506 ? 1.5664 1.8678 1.6088 -0.3731 0.1863 0.0397 2153 PRO B O 8439 C CB . PRO B 506 ? 1.6636 1.7641 1.6431 -0.3578 0.2396 0.0054 2153 PRO B CB 8440 C CG . PRO B 506 ? 1.5790 1.6192 1.5052 -0.4113 0.2336 -0.0135 2153 PRO B CG 8441 C CD . PRO B 506 ? 1.6380 1.6136 1.5261 -0.3918 0.2251 -0.0254 2153 PRO B CD 8442 N N . THR B 507 ? 1.4917 1.7984 1.5891 -0.2752 0.2205 0.0616 2154 THR B N 8443 C CA . THR B 507 ? 1.6639 2.1068 1.8262 -0.2656 0.2118 0.0973 2154 THR B CA 8444 C C . THR B 507 ? 1.7559 2.2688 1.9715 -0.2538 0.2353 0.1168 2154 THR B C 8445 O O . THR B 507 ? 1.7731 2.4142 2.0474 -0.2611 0.2278 0.1481 2154 THR B O 8446 C CB . THR B 507 ? 1.7680 2.2331 1.9548 -0.2045 0.2142 0.1204 2154 THR B CB 8447 O OG1 . THR B 507 ? 1.8746 2.2302 2.0091 -0.1903 0.2129 0.0979 2154 THR B OG1 8448 C CG2 . THR B 507 ? 1.6666 2.2696 1.8983 -0.2102 0.1875 0.1575 2154 THR B CG2 8449 N N . HIS B 508 ? 1.8846 2.3208 2.0809 -0.2316 0.2644 0.1017 2155 HIS B N 8450 C CA . HIS B 508 ? 2.0522 2.5308 2.2808 -0.2269 0.2918 0.1134 2155 HIS B CA 8451 C C . HIS B 508 ? 1.9950 2.3651 2.1673 -0.2412 0.3078 0.0843 2155 HIS B C 8452 O O . HIS B 508 ? 1.9049 2.1736 2.0234 -0.2381 0.3021 0.0598 2155 HIS B O 8453 C CB . HIS B 508 ? 2.2621 2.7775 2.5325 -0.1584 0.3222 0.1372 2155 HIS B CB 8454 C CG . HIS B 508 ? 2.2652 2.8894 2.5951 -0.1300 0.3128 0.1754 2155 HIS B CG 8455 N ND1 . HIS B 508 ? 2.1284 2.7288 2.4456 -0.1061 0.2969 0.1783 2155 HIS B ND1 8456 C CD2 . HIS B 508 ? 2.2671 3.0292 2.6722 -0.1153 0.3206 0.2177 2155 HIS B CD2 8457 C CE1 . HIS B 508 ? 2.0623 2.7793 2.4406 -0.0779 0.2937 0.2215 2155 HIS B CE1 8458 N NE2 . HIS B 508 ? 2.1498 2.9708 2.5851 -0.0819 0.3073 0.2471 2155 HIS B NE2 8459 N N . TYR B 509 ? 1.9457 2.3435 2.1323 -0.2555 0.3288 0.0912 2156 TYR B N 8460 C CA . TYR B 509 ? 1.8930 2.1984 2.0260 -0.2690 0.3438 0.0706 2156 TYR B CA 8461 C C . TYR B 509 ? 1.8995 2.2422 2.0533 -0.2584 0.3769 0.0847 2156 TYR B C 8462 O O . TYR B 509 ? 1.7847 2.2256 1.9985 -0.2386 0.3905 0.1105 2156 TYR B O 8463 C CB . TYR B 509 ? 1.8780 2.1416 1.9759 -0.3304 0.3273 0.0571 2156 TYR B CB 8464 C CG . TYR B 509 ? 1.9151 2.2713 2.0524 -0.3854 0.3139 0.0711 2156 TYR B CG 8465 C CD1 . TYR B 509 ? 1.9001 2.3843 2.1056 -0.3764 0.3036 0.0973 2156 TYR B CD1 8466 C CD2 . TYR B 509 ? 1.8920 2.2094 1.9976 -0.4481 0.3130 0.0601 2156 TYR B CD2 8467 C CE1 . TYR B 509 ? 1.8644 2.4483 2.1078 -0.4337 0.2866 0.1112 2156 TYR B CE1 8468 C CE2 . TYR B 509 ? 1.9011 2.2998 2.0367 -0.5095 0.2994 0.0684 2156 TYR B CE2 8469 C CZ . TYR B 509 ? 1.8980 2.4365 2.1038 -0.5045 0.2833 0.0936 2156 TYR B CZ 8470 O OH . TYR B 509 ? 2.0279 2.6613 2.2655 -0.5719 0.2658 0.1031 2156 TYR B OH 8471 N N . SER B 510 ? 1.8601 2.1273 1.9642 -0.2685 0.3917 0.0713 2157 SER B N 8472 C CA . SER B 510 ? 1.9472 2.2287 2.0521 -0.2560 0.4264 0.0814 2157 SER B CA 8473 C C . SER B 510 ? 1.9912 2.3480 2.1364 -0.3031 0.4337 0.1020 2157 SER B C 8474 O O . SER B 510 ? 2.2573 2.7125 2.4614 -0.2921 0.4515 0.1264 2157 SER B O 8475 C CB . SER B 510 ? 1.9309 2.1103 1.9636 -0.2511 0.4363 0.0638 2157 SER B CB 8476 O OG . SER B 510 ? 1.9914 2.1310 1.9979 -0.2978 0.4294 0.0627 2157 SER B OG 8477 N N . ILE B 511 ? 1.8650 2.1727 1.9779 -0.3553 0.4237 0.0934 2158 ILE B N 8478 C CA . ILE B 511 ? 1.7680 2.1326 1.9115 -0.4155 0.4279 0.1080 2158 ILE B CA 8479 C C . ILE B 511 ? 1.8825 2.1783 1.9849 -0.4723 0.4067 0.0899 2158 ILE B C 8480 O O . ILE B 511 ? 2.0413 2.3775 2.1630 -0.5352 0.4009 0.0943 2158 ILE B O 8481 C CB . ILE B 511 ? 1.6630 2.0303 1.8031 -0.4176 0.4665 0.1234 2158 ILE B CB 8482 C CG1 . ILE B 511 ? 1.6496 1.9361 1.7332 -0.3619 0.4854 0.1134 2158 ILE B CG1 8483 C CG2 . ILE B 511 ? 1.7158 2.2227 1.9387 -0.4158 0.4827 0.1534 2158 ILE B CG2 8484 C CD1 . ILE B 511 ? 1.8079 2.1336 1.9017 -0.3320 0.5255 0.1308 2158 ILE B CD1 8485 N N . ARG B 512 ? 1.8932 2.0839 1.9369 -0.4502 0.3972 0.0691 2159 ARG B N 8486 C CA . ARG B 512 ? 1.7993 1.9201 1.8020 -0.4862 0.3774 0.0500 2159 ARG B CA 8487 C C . ARG B 512 ? 1.7270 1.7964 1.7040 -0.4382 0.3607 0.0355 2159 ARG B C 8488 O O . ARG B 512 ? 1.5866 1.6221 1.5469 -0.3898 0.3708 0.0348 2159 ARG B O 8489 C CB . ARG B 512 ? 1.8643 1.8831 1.8103 -0.5183 0.3993 0.0458 2159 ARG B CB 8490 C CG . ARG B 512 ? 2.0345 2.0937 2.0026 -0.5699 0.4211 0.0611 2159 ARG B CG 8491 C CD . ARG B 512 ? 2.2552 2.2058 2.1648 -0.6208 0.4389 0.0531 2159 ARG B CD 8492 N NE . ARG B 512 ? 2.3045 2.1392 2.1528 -0.5801 0.4577 0.0536 2159 ARG B NE 8493 C CZ . ARG B 512 ? 2.4091 2.1942 2.2302 -0.5771 0.4914 0.0713 2159 ARG B CZ 8494 N NH1 . ARG B 512 ? 2.5252 2.3592 2.3744 -0.6146 0.5132 0.0877 2159 ARG B NH1 8495 N NH2 . ARG B 512 ? 2.4013 2.0947 2.1695 -0.5361 0.5039 0.0765 2159 ARG B NH2 8496 N N . SER B 513 ? 1.8043 1.8733 1.7771 -0.4554 0.3348 0.0239 2160 SER B N 8497 C CA . SER B 513 ? 1.8737 1.8866 1.8190 -0.4186 0.3206 0.0104 2160 SER B CA 8498 C C . SER B 513 ? 1.8919 1.7878 1.7757 -0.4124 0.3357 0.0012 2160 SER B C 8499 O O . SER B 513 ? 2.0799 1.9085 1.9231 -0.4479 0.3392 -0.0081 2160 SER B O 8500 C CB . SER B 513 ? 2.0012 2.0339 1.9456 -0.4451 0.2930 0.0014 2160 SER B CB 8501 O OG . SER B 513 ? 1.9775 2.1329 1.9807 -0.4584 0.2778 0.0171 2160 SER B OG 8502 N N . THR B 514 ? 1.7075 1.5813 1.5828 -0.3674 0.3467 0.0054 2161 THR B N 8503 C CA . THR B 514 ? 1.6589 1.4455 1.4846 -0.3539 0.3607 0.0061 2161 THR B CA 8504 C C . THR B 514 ? 1.7534 1.5102 1.5655 -0.3108 0.3484 -0.0008 2161 THR B C 8505 O O . THR B 514 ? 1.9026 1.7017 1.7394 -0.2830 0.3391 -0.0047 2161 THR B O 8506 C CB . THR B 514 ? 1.5826 1.3794 1.4044 -0.3463 0.3842 0.0210 2161 THR B CB 8507 O OG1 . THR B 514 ? 1.5665 1.4120 1.4155 -0.3864 0.3955 0.0293 2161 THR B OG1 8508 C CG2 . THR B 514 ? 1.5846 1.2987 1.3546 -0.3379 0.4006 0.0304 2161 THR B CG2 8509 N N . LEU B 515 ? 1.8347 1.5182 1.6083 -0.3049 0.3516 -0.0005 2162 LEU B N 8510 C CA . LEU B 515 ? 1.8513 1.5161 1.6197 -0.2722 0.3374 -0.0061 2162 LEU B CA 8511 C C . LEU B 515 ? 1.8927 1.4983 1.6267 -0.2523 0.3463 0.0055 2162 LEU B C 8512 O O . LEU B 515 ? 1.9541 1.4988 1.6597 -0.2640 0.3615 0.0117 2162 LEU B O 8513 C CB . LEU B 515 ? 1.8026 1.4681 1.5806 -0.2822 0.3212 -0.0188 2162 LEU B CB 8514 C CG . LEU B 515 ? 1.6785 1.3291 1.4572 -0.2549 0.3075 -0.0245 2162 LEU B CG 8515 C CD1 . LEU B 515 ? 1.5661 1.2620 1.3732 -0.2274 0.2969 -0.0277 2162 LEU B CD1 8516 C CD2 . LEU B 515 ? 1.6240 1.2648 1.3977 -0.2737 0.2982 -0.0340 2162 LEU B CD2 8517 N N . ARG B 516 ? 1.9447 1.5704 1.6804 -0.2227 0.3384 0.0092 2163 ARG B N 8518 C CA . ARG B 516 ? 1.9987 1.5980 1.7182 -0.1978 0.3357 0.0209 2163 ARG B CA 8519 C C . ARG B 516 ? 1.9104 1.5315 1.6523 -0.1850 0.3146 0.0067 2163 ARG B C 8520 O O . ARG B 516 ? 1.9338 1.5904 1.6966 -0.1874 0.3052 -0.0090 2163 ARG B O 8521 C CB . ARG B 516 ? 2.0679 1.6847 1.7696 -0.1811 0.3390 0.0376 2163 ARG B CB 8522 C CG . ARG B 516 ? 2.1452 1.7265 1.8183 -0.1845 0.3641 0.0620 2163 ARG B CG 8523 C CD . ARG B 516 ? 2.0884 1.6992 1.7408 -0.1677 0.3649 0.0800 2163 ARG B CD 8524 N NE . ARG B 516 ? 2.1041 1.7585 1.7610 -0.1774 0.3620 0.0633 2163 ARG B NE 8525 C CZ . ARG B 516 ? 2.3112 1.9959 1.9438 -0.1674 0.3612 0.0693 2163 ARG B CZ 8526 N NH1 . ARG B 516 ? 2.4513 2.1393 2.0562 -0.1490 0.3575 0.0944 2163 ARG B NH1 8527 N NH2 . ARG B 516 ? 2.4587 2.1735 2.0925 -0.1741 0.3654 0.0521 2163 ARG B NH2 8528 N N . MET B 517 ? 1.8245 1.4233 1.5634 -0.1697 0.3116 0.0149 2164 MET B N 8529 C CA . MET B 517 ? 1.7842 1.3968 1.5450 -0.1618 0.2956 0.0032 2164 MET B CA 8530 C C . MET B 517 ? 1.7860 1.3839 1.5479 -0.1425 0.2956 0.0186 2164 MET B C 8531 O O . MET B 517 ? 1.9001 1.4597 1.6444 -0.1337 0.3131 0.0369 2164 MET B O 8532 C CB . MET B 517 ? 1.7326 1.3382 1.5035 -0.1774 0.2935 -0.0123 2164 MET B CB 8533 C CG . MET B 517 ? 1.8435 1.4015 1.5895 -0.1949 0.3091 -0.0095 2164 MET B CG 8534 S SD . MET B 517 ? 1.7668 1.2944 1.5046 -0.2019 0.3070 -0.0201 2164 MET B SD 8535 C CE . MET B 517 ? 1.8538 1.3849 1.6079 -0.1677 0.3018 -0.0102 2164 MET B CE 8536 N N . GLU B 518 ? 1.7099 1.3364 1.4934 -0.1357 0.2798 0.0123 2165 GLU B N 8537 C CA . GLU B 518 ? 1.7194 1.3473 1.5153 -0.1194 0.2788 0.0276 2165 GLU B CA 8538 C C . GLU B 518 ? 1.7481 1.3746 1.5634 -0.1234 0.2716 0.0116 2165 GLU B C 8539 O O . GLU B 518 ? 1.6926 1.3326 1.5164 -0.1341 0.2623 -0.0079 2165 GLU B O 8540 C CB . GLU B 518 ? 1.8860 1.5645 1.6905 -0.1133 0.2642 0.0394 2165 GLU B CB 8541 C CG . GLU B 518 ? 2.0894 1.7984 1.9217 -0.1035 0.2553 0.0525 2165 GLU B CG 8542 C CD . GLU B 518 ? 2.2190 1.9285 2.0544 -0.0769 0.2699 0.0901 2165 GLU B CD 8543 O OE1 . GLU B 518 ? 2.1203 1.7719 1.9401 -0.0653 0.2947 0.0967 2165 GLU B OE1 8544 O OE2 . GLU B 518 ? 2.3660 2.1344 2.2167 -0.0684 0.2576 0.1135 2165 GLU B OE2 8545 N N . LEU B 519 ? 1.7651 1.3722 1.5855 -0.1113 0.2805 0.0229 2166 LEU B N 8546 C CA . LEU B 519 ? 1.6657 1.2720 1.5028 -0.1123 0.2761 0.0133 2166 LEU B CA 8547 C C . LEU B 519 ? 1.7123 1.3571 1.5808 -0.1066 0.2662 0.0220 2166 LEU B C 8548 O O . LEU B 519 ? 1.7895 1.4564 1.6693 -0.0933 0.2691 0.0454 2166 LEU B O 8549 C CB . LEU B 519 ? 1.5521 1.1111 1.3694 -0.1060 0.2944 0.0174 2166 LEU B CB 8550 C CG . LEU B 519 ? 1.5916 1.1274 1.3845 -0.1259 0.2941 -0.0015 2166 LEU B CG 8551 C CD1 . LEU B 519 ? 1.7313 1.2078 1.4825 -0.1303 0.3160 0.0000 2166 LEU B CD1 8552 C CD2 . LEU B 519 ? 1.6520 1.2014 1.4573 -0.1300 0.2836 -0.0126 2166 LEU B CD2 8553 N N . MET B 520 ? 1.6480 1.3032 1.5320 -0.1174 0.2561 0.0059 2167 MET B N 8554 C CA . MET B 520 ? 1.7198 1.4051 1.6332 -0.1206 0.2488 0.0115 2167 MET B CA 8555 C C . MET B 520 ? 1.7699 1.4365 1.6963 -0.1126 0.2598 0.0175 2167 MET B C 8556 O O . MET B 520 ? 1.8657 1.5038 1.7821 -0.1138 0.2638 0.0056 2167 MET B O 8557 C CB . MET B 520 ? 1.6256 1.3255 1.5417 -0.1412 0.2354 -0.0100 2167 MET B CB 8558 C CG . MET B 520 ? 1.6941 1.4139 1.5901 -0.1487 0.2264 -0.0152 2167 MET B CG 8559 S SD . MET B 520 ? 1.9051 1.6851 1.8113 -0.1474 0.2139 0.0119 2167 MET B SD 8560 C CE . MET B 520 ? 1.9162 1.7323 1.8267 -0.1833 0.1931 -0.0093 2167 MET B CE 8561 N N . GLY B 521 ? 1.7253 1.4144 1.6746 -0.1020 0.2660 0.0403 2168 GLY B N 8562 C CA . GLY B 521 ? 1.6958 1.3680 1.6547 -0.0908 0.2818 0.0505 2168 GLY B CA 8563 C C . GLY B 521 ? 1.8172 1.5370 1.8158 -0.0820 0.2863 0.0784 2168 GLY B C 8564 O O . GLY B 521 ? 1.8561 1.6318 1.8797 -0.0932 0.2699 0.0860 2168 GLY B O 8565 N N . CYS B 522 ? 1.9073 1.6100 1.9099 -0.0623 0.3093 0.0953 2169 CYS B N 8566 C CA . CYS B 522 ? 1.9588 1.7106 2.0081 -0.0532 0.3187 0.1242 2169 CYS B CA 8567 C C . CYS B 522 ? 1.9504 1.6508 1.9769 -0.0279 0.3512 0.1333 2169 CYS B C 8568 O O . CYS B 522 ? 1.8620 1.5035 1.8450 -0.0321 0.3552 0.1111 2169 CYS B O 8569 C CB . CYS B 522 ? 2.2475 2.0307 2.3304 -0.0846 0.3027 0.1138 2169 CYS B CB 8570 S SG . CYS B 522 ? 2.7295 2.5897 2.8815 -0.0898 0.3088 0.1467 2169 CYS B SG 8571 N N . ASP B 523 ? 1.9711 1.6960 2.0236 -0.0010 0.3756 0.1667 2170 ASP B N 8572 C CA . ASP B 523 ? 2.1564 1.8229 2.1760 0.0255 0.4130 0.1741 2170 ASP B CA 8573 C C . ASP B 523 ? 2.3077 1.9594 2.3260 0.0108 0.4141 0.1625 2170 ASP B C 8574 O O . ASP B 523 ? 2.5466 2.2215 2.5860 -0.0181 0.3885 0.1477 2170 ASP B O 8575 C CB . ASP B 523 ? 2.1666 1.8671 2.2204 0.0629 0.4449 0.2170 2170 ASP B CB 8576 C CG . ASP B 523 ? 2.3097 2.0766 2.4259 0.0592 0.4486 0.2397 2170 ASP B CG 8577 O OD1 . ASP B 523 ? 2.2058 2.0455 2.3730 0.0281 0.4165 0.2395 2170 ASP B OD1 8578 O OD2 . ASP B 523 ? 2.5286 2.2705 2.6379 0.0837 0.4853 0.2555 2170 ASP B OD2 8579 N N . LEU B 524 ? 2.2850 1.8926 2.2736 0.0323 0.4477 0.1706 2171 LEU B N 8580 C CA . LEU B 524 ? 1.9692 1.5603 1.9498 0.0232 0.4530 0.1653 2171 LEU B CA 8581 C C . LEU B 524 ? 1.9325 1.5907 1.9848 0.0120 0.4499 0.1862 2171 LEU B C 8582 O O . LEU B 524 ? 1.7787 1.4438 1.8454 -0.0156 0.4305 0.1731 2171 LEU B O 8583 C CB . LEU B 524 ? 1.8017 1.3319 1.7271 0.0493 0.4927 0.1708 2171 LEU B CB 8584 C CG . LEU B 524 ? 1.7528 1.2177 1.6012 0.0345 0.4823 0.1379 2171 LEU B CG 8585 C CD1 . LEU B 524 ? 1.8307 1.2568 1.6340 0.0437 0.5079 0.1409 2171 LEU B CD1 8586 C CD2 . LEU B 524 ? 1.6020 1.0940 1.4704 0.0046 0.4409 0.1191 2171 LEU B CD2 8587 N N . ASN B 525 ? 1.9444 1.6508 2.0417 0.0338 0.4722 0.2206 2172 ASN B N 8588 C CA . ASN B 525 ? 1.9871 1.7706 2.1598 0.0222 0.4738 0.2472 2172 ASN B CA 8589 C C . ASN B 525 ? 1.9311 1.7901 2.1603 -0.0157 0.4348 0.2437 2172 ASN B C 8590 O O . ASN B 525 ? 2.0220 1.9621 2.3198 -0.0297 0.4335 0.2690 2172 ASN B O 8591 C CB . ASN B 525 ? 2.0829 1.9043 2.2887 0.0621 0.5127 0.2902 2172 ASN B CB 8592 C CG . ASN B 525 ? 2.2958 2.0672 2.4704 0.0846 0.5550 0.2995 2172 ASN B CG 8593 O OD1 . ASN B 525 ? 2.2992 1.9831 2.3955 0.0873 0.5623 0.2728 2172 ASN B OD1 8594 N ND2 . ASN B 525 ? 2.5340 2.3681 2.7700 0.0984 0.5824 0.3388 2172 ASN B ND2 8595 N N . SER B 526 ? 2.4122 1.6507 2.1117 -0.0758 0.1537 0.2973 2173 SER B N 8596 C CA . SER B 526 ? 2.2871 1.5844 2.0960 -0.0564 0.1732 0.2898 2173 SER B CA 8597 C C . SER B 526 ? 2.3471 1.6690 2.1864 -0.0530 0.2211 0.2596 2173 SER B C 8598 O O . SER B 526 ? 2.2863 1.6326 2.1893 -0.0415 0.2391 0.2528 2173 SER B O 8599 C CB . SER B 526 ? 2.1770 1.4541 2.0008 -0.0461 0.1716 0.3128 2173 SER B CB 8600 O OG . SER B 526 ? 2.0828 1.3431 1.8881 -0.0475 0.1234 0.3447 2173 SER B OG 8601 N N . CYS B 527 ? 2.4489 1.7586 2.2401 -0.0629 0.2382 0.2432 2174 CYS B N 8602 C CA . CYS B 527 ? 2.4576 1.7913 2.2794 -0.0596 0.2814 0.2212 2174 CYS B CA 8603 C C . CYS B 527 ? 2.3944 1.7643 2.2420 -0.0587 0.2806 0.1991 2174 CYS B C 8604 O O . CYS B 527 ? 2.3627 1.7172 2.1727 -0.0618 0.3060 0.1870 2174 CYS B O 8605 C CB . CYS B 527 ? 2.4731 1.7619 2.2312 -0.0648 0.3234 0.2262 2174 CYS B CB 8606 S SG . CYS B 527 ? 2.5901 1.9209 2.4160 -0.0607 0.3735 0.2132 2174 CYS B SG 8607 N N . SER B 528 ? 2.2976 1.7132 2.2103 -0.0516 0.2560 0.1966 2175 SER B N 8608 C CA . SER B 528 ? 2.2981 1.7530 2.2477 -0.0492 0.2591 0.1783 2175 SER B CA 8609 C C . SER B 528 ? 2.1734 1.6752 2.2046 -0.0326 0.2640 0.1719 2175 SER B C 8610 O O . SER B 528 ? 2.0982 1.6312 2.1728 -0.0239 0.2454 0.1788 2175 SER B O 8611 C CB . SER B 528 ? 2.5214 1.9733 2.4475 -0.0610 0.2234 0.1840 2175 SER B CB 8612 O OG . SER B 528 ? 2.5623 2.0244 2.5126 -0.0613 0.1841 0.2092 2175 SER B OG 8613 N N . MET B 529 ? 2.1367 1.6384 2.1860 -0.0287 0.2894 0.1614 2176 MET B N 8614 C CA . MET B 529 ? 2.0829 1.6038 2.1829 -0.0143 0.2927 0.1530 2176 MET B CA 8615 C C . MET B 529 ? 1.9649 1.5016 2.0824 -0.0165 0.3106 0.1333 2176 MET B C 8616 O O . MET B 529 ? 1.9360 1.4690 2.0413 -0.0281 0.3261 0.1316 2176 MET B O 8617 C CB . MET B 529 ? 2.2419 1.7312 2.3431 -0.0103 0.2920 0.1633 2176 MET B CB 8618 C CG . MET B 529 ? 2.3074 1.7954 2.4401 0.0124 0.2864 0.1636 2176 MET B CG 8619 S SD . MET B 529 ? 2.2893 1.8054 2.4528 0.0321 0.2672 0.1863 2176 MET B SD 8620 C CE . MET B 529 ? 2.3256 1.8781 2.5302 0.0537 0.2825 0.1725 2176 MET B CE 8621 N N . PRO B 530 ? 1.9484 1.5011 2.0935 -0.0035 0.3098 0.1217 2177 PRO B N 8622 C CA . PRO B 530 ? 1.9757 1.5333 2.1327 -0.0052 0.3178 0.1051 2177 PRO B CA 8623 C C . PRO B 530 ? 2.0051 1.5411 2.1644 -0.0204 0.3205 0.1073 2177 PRO B C 8624 O O . PRO B 530 ? 2.1518 1.6557 2.3056 -0.0210 0.3146 0.1138 2177 PRO B O 8625 C CB . PRO B 530 ? 2.1395 1.6868 2.3025 0.0154 0.3156 0.0978 2177 PRO B CB 8626 C CG . PRO B 530 ? 2.1952 1.7535 2.3699 0.0311 0.3115 0.1140 2177 PRO B CG 8627 C CD . PRO B 530 ? 2.1009 1.6712 2.2667 0.0146 0.3017 0.1275 2177 PRO B CD 8628 N N . LEU B 531 ? 2.0427 1.5972 2.2174 -0.0327 0.3289 0.1057 2178 LEU B N 8629 C CA . LEU B 531 ? 1.9478 1.4947 2.1445 -0.0505 0.3319 0.1170 2178 LEU B CA 8630 C C . LEU B 531 ? 1.9733 1.5099 2.1909 -0.0607 0.3127 0.1097 2178 LEU B C 8631 O O . LEU B 531 ? 2.0020 1.5357 2.2498 -0.0809 0.3079 0.1236 2178 LEU B O 8632 C CB . LEU B 531 ? 1.8143 1.3871 2.0257 -0.0570 0.3562 0.1295 2178 LEU B CB 8633 C CG . LEU B 531 ? 1.7844 1.3361 1.9608 -0.0570 0.3739 0.1448 2178 LEU B CG 8634 C CD1 . LEU B 531 ? 1.9479 1.5103 2.1134 -0.0535 0.4050 0.1515 2178 LEU B CD1 8635 C CD2 . LEU B 531 ? 1.6995 1.2302 1.8900 -0.0703 0.3751 0.1637 2178 LEU B CD2 8636 N N . GLY B 532 ? 2.0242 1.5514 2.2230 -0.0486 0.3006 0.0908 2179 GLY B N 8637 C CA . GLY B 532 ? 2.0365 1.5296 2.2269 -0.0579 0.2766 0.0809 2179 GLY B CA 8638 C C . GLY B 532 ? 1.9719 1.4779 2.1588 -0.0563 0.2664 0.0687 2179 GLY B C 8639 O O . GLY B 532 ? 2.1194 1.5787 2.2687 -0.0568 0.2458 0.0549 2179 GLY B O 8640 N N . MET B 533 ? 1.8208 1.3788 2.0360 -0.0537 0.2803 0.0737 2180 MET B N 8641 C CA . MET B 533 ? 1.8008 1.3731 2.0172 -0.0532 0.2696 0.0667 2180 MET B CA 8642 C C . MET B 533 ? 1.9200 1.4468 2.0762 -0.0380 0.2599 0.0463 2180 MET B C 8643 O O . MET B 533 ? 1.8795 1.3713 2.0094 -0.0478 0.2332 0.0392 2180 MET B O 8644 C CB . MET B 533 ? 1.7142 1.3356 1.9528 -0.0432 0.2926 0.0714 2180 MET B CB 8645 C CG . MET B 533 ? 1.8695 1.5255 2.1576 -0.0527 0.3092 0.0920 2180 MET B CG 8646 S SD . MET B 533 ? 1.8421 1.5285 2.1984 -0.0720 0.2907 0.1127 2180 MET B SD 8647 C CE . MET B 533 ? 1.8241 1.5415 2.1859 -0.0554 0.3005 0.1095 2180 MET B CE 8648 N N . GLU B 534 ? 2.0362 1.5598 2.1693 -0.0142 0.2815 0.0403 2181 GLU B N 8649 C CA . GLU B 534 ? 2.0071 1.4922 2.0878 0.0090 0.2878 0.0266 2181 GLU B CA 8650 C C . GLU B 534 ? 2.1504 1.5628 2.1855 0.0127 0.2786 0.0183 2181 GLU B C 8651 O O . GLU B 534 ? 2.2969 1.6480 2.2685 0.0220 0.2723 0.0036 2181 GLU B O 8652 C CB . GLU B 534 ? 1.9207 1.4392 2.0149 0.0324 0.3152 0.0325 2181 GLU B CB 8653 C CG . GLU B 534 ? 2.1681 1.6606 2.2234 0.0609 0.3332 0.0261 2181 GLU B CG 8654 C CD . GLU B 534 ? 2.3354 1.8511 2.4179 0.0844 0.3570 0.0404 2181 GLU B CD 8655 O OE1 . GLU B 534 ? 2.2789 1.8414 2.4082 0.0742 0.3538 0.0543 2181 GLU B OE1 8656 O OE2 . GLU B 534 ? 2.2631 1.7466 2.3183 0.1139 0.3786 0.0402 2181 GLU B OE2 8657 N N . SER B 535 ? 2.1725 1.5817 2.2298 0.0060 0.2785 0.0277 2182 SER B N 8658 C CA . SER B 535 ? 2.3090 1.6432 2.3270 0.0058 0.2677 0.0224 2182 SER B CA 8659 C C . SER B 535 ? 2.3377 1.6093 2.3161 -0.0200 0.2314 0.0118 2182 SER B C 8660 O O . SER B 535 ? 2.4134 1.6015 2.3389 -0.0208 0.2186 0.0029 2182 SER B O 8661 C CB . SER B 535 ? 2.2691 1.6176 2.3261 -0.0054 0.2691 0.0397 2182 SER B CB 8662 O OG . SER B 535 ? 2.2483 1.6307 2.3251 0.0172 0.2923 0.0505 2182 SER B OG 8663 N N . LYS B 536 ? 2.3570 1.6637 2.3594 -0.0415 0.2116 0.0146 2183 LYS B N 8664 C CA . LYS B 536 ? 2.3164 1.5887 2.3154 -0.0784 0.1658 0.0170 2183 LYS B CA 8665 C C . LYS B 536 ? 2.2291 1.4961 2.2707 -0.1042 0.1537 0.0338 2183 LYS B C 8666 O O . LYS B 536 ? 2.2567 1.4918 2.3059 -0.1398 0.1125 0.0414 2183 LYS B O 8667 C CB . LYS B 536 ? 2.6472 1.8125 2.5405 -0.0767 0.1394 -0.0060 2183 LYS B CB 8668 C CG . LYS B 536 ? 2.7501 1.9148 2.6136 -0.0821 0.1176 -0.0120 2183 LYS B CG 8669 C CD . LYS B 536 ? 2.9147 1.9535 2.6633 -0.0951 0.0752 -0.0314 2183 LYS B CD 8670 C CE . LYS B 536 ? 2.9237 1.9147 2.5748 -0.0657 0.0895 -0.0505 2183 LYS B CE 8671 N NZ . LYS B 536 ? 2.8097 1.9023 2.5266 -0.0599 0.1037 -0.0371 2183 LYS B NZ 8672 N N . ALA B 537 ? 2.0950 1.3913 2.1637 -0.0881 0.1869 0.0425 2184 ALA B N 8673 C CA . ALA B 537 ? 2.0634 1.3638 2.1744 -0.1081 0.1857 0.0629 2184 ALA B CA 8674 C C . ALA B 537 ? 1.9952 1.3612 2.1910 -0.1410 0.1755 0.0898 2184 ALA B C 8675 O O . ALA B 537 ? 2.0637 1.4149 2.2929 -0.1724 0.1543 0.1084 2184 ALA B O 8676 C CB . ALA B 537 ? 1.8965 1.2212 2.0142 -0.0823 0.2223 0.0693 2184 ALA B CB 8677 N N . ILE B 538 ? 1.9536 1.3906 2.1881 -0.1326 0.1925 0.0949 2185 ILE B N 8678 C CA . ILE B 538 ? 1.8663 1.3649 2.1824 -0.1558 0.1856 0.1212 2185 ILE B CA 8679 C C . ILE B 538 ? 2.0978 1.5725 2.4118 -0.1802 0.1345 0.1191 2185 ILE B C 8680 O O . ILE B 538 ? 2.2862 1.7351 2.5422 -0.1660 0.1233 0.0961 2185 ILE B O 8681 C CB . ILE B 538 ? 1.6291 1.1957 1.9722 -0.1327 0.2232 0.1246 2185 ILE B CB 8682 C CG1 . ILE B 538 ? 1.4876 1.0775 1.8472 -0.1234 0.2645 0.1395 2185 ILE B CG1 8683 C CG2 . ILE B 538 ? 1.6247 1.2438 2.0338 -0.1450 0.2111 0.1431 2185 ILE B CG2 8684 C CD1 . ILE B 538 ? 1.3624 0.9826 1.7047 -0.0970 0.2988 0.1320 2185 ILE B CD1 8685 N N . SER B 539 ? 2.2655 1.7468 2.6415 -0.2185 0.1015 0.1464 2186 SER B N 8686 C CA . SER B 539 ? 2.3688 1.8167 2.7408 -0.2512 0.0382 0.1490 2186 SER B CA 8687 C C . SER B 539 ? 2.3136 1.8059 2.7008 -0.2425 0.0284 0.1494 2186 SER B C 8688 O O . SER B 539 ? 2.0348 1.6021 2.4708 -0.2180 0.0716 0.1585 2186 SER B O 8689 C CB . SER B 539 ? 2.4864 1.9545 2.9524 -0.2984 0.0043 0.1898 2186 SER B CB 8690 O OG . SER B 539 ? 2.5942 2.0827 3.1091 -0.3297 -0.0512 0.2100 2186 SER B OG 8691 N N . ASP B 540 ? 2.4966 1.9313 2.8309 -0.2626 -0.0296 0.1391 2187 ASP B N 8692 C CA . ASP B 540 ? 2.5135 1.9772 2.8473 -0.2548 -0.0453 0.1394 2187 ASP B CA 8693 C C . ASP B 540 ? 2.2932 1.8684 2.7697 -0.2651 -0.0417 0.1845 2187 ASP B C 8694 O O . ASP B 540 ? 2.3279 1.9694 2.8429 -0.2329 0.0115 0.1887 2187 ASP B O 8695 C CB . ASP B 540 ? 2.6793 2.0462 2.9131 -0.2766 -0.1132 0.1217 2187 ASP B CB 8696 C CG . ASP B 540 ? 2.6587 1.9703 2.7679 -0.2377 -0.0906 0.0831 2187 ASP B CG 8697 O OD1 . ASP B 540 ? 2.3587 1.7376 2.4963 -0.2056 -0.0454 0.0833 2187 ASP B OD1 8698 O OD2 . ASP B 540 ? 2.7704 1.9654 2.7501 -0.2389 -0.1159 0.0543 2187 ASP B OD2 8699 N N . ALA B 541 ? 2.0883 1.6818 2.6453 -0.3089 -0.0965 0.2209 2188 ALA B N 8700 C CA . ALA B 541 ? 1.8570 1.5648 2.5699 -0.3146 -0.0843 0.2726 2188 ALA B CA 8701 C C . ALA B 541 ? 1.7463 1.5098 2.5413 -0.3062 -0.0219 0.2964 2188 ALA B C 8702 O O . ALA B 541 ? 1.7945 1.6170 2.7130 -0.3321 -0.0286 0.3451 2188 ALA B O 8703 C CB . ALA B 541 ? 1.8585 1.5793 2.6468 -0.3647 -0.1674 0.3121 2188 ALA B CB 8704 N N . GLN B 542 ? 1.7179 1.4592 2.4409 -0.2703 0.0379 0.2644 2189 GLN B N 8705 C CA . GLN B 542 ? 1.7127 1.5003 2.4868 -0.2519 0.1059 0.2824 2189 GLN B CA 8706 C C . GLN B 542 ? 1.6919 1.5336 2.4788 -0.2092 0.1629 0.2810 2189 GLN B C 8707 O O . GLN B 542 ? 1.4910 1.3648 2.3042 -0.1870 0.2246 0.2939 2189 GLN B O 8708 C CB . GLN B 542 ? 1.7749 1.4913 2.4506 -0.2429 0.1245 0.2489 2189 GLN B CB 8709 C CG . GLN B 542 ? 1.8760 1.6134 2.5892 -0.2390 0.1743 0.2708 2189 GLN B CG 8710 C CD . GLN B 542 ? 2.0789 1.7385 2.7013 -0.2378 0.1748 0.2436 2189 GLN B CD 8711 O OE1 . GLN B 542 ? 2.2612 1.8572 2.8496 -0.2642 0.1273 0.2346 2189 GLN B OE1 8712 N NE2 . GLN B 542 ? 2.0521 1.7102 2.6319 -0.2074 0.2264 0.2325 2189 GLN B NE2 8713 N N . ILE B 543 ? 1.8080 1.6465 2.5638 -0.1993 0.1389 0.2649 2190 ILE B N 8714 C CA . ILE B 543 ? 1.7209 1.5949 2.4764 -0.1630 0.1781 0.2602 2190 ILE B CA 8715 C C . ILE B 543 ? 1.8251 1.7374 2.6433 -0.1725 0.1367 0.2845 2190 ILE B C 8716 O O . ILE B 543 ? 1.9619 1.8300 2.7258 -0.1910 0.0775 0.2685 2190 ILE B O 8717 C CB . ILE B 543 ? 1.6377 1.4543 2.2685 -0.1404 0.1825 0.2109 2190 ILE B CB 8718 C CG1 . ILE B 543 ? 1.5967 1.3709 2.1565 -0.1293 0.2138 0.1848 2190 ILE B CG1 8719 C CG2 . ILE B 543 ? 1.5435 1.3904 2.1758 -0.1100 0.2123 0.2086 2190 ILE B CG2 8720 C CD1 . ILE B 543 ? 1.5495 1.2586 2.0028 -0.1217 0.1958 0.1453 2190 ILE B CD1 8721 N N . THR B 544 ? 1.8706 1.8582 2.7966 -0.1582 0.1673 0.3245 2191 THR B N 8722 C CA . THR B 544 ? 2.0753 2.0949 3.0361 -0.1486 0.1454 0.3387 2191 THR B CA 8723 C C . THR B 544 ? 1.9383 1.9932 2.9207 -0.1030 0.2172 0.3449 2191 THR B C 8724 O O . THR B 544 ? 1.8770 1.9316 2.8515 -0.0826 0.2802 0.3424 2191 THR B O 8725 C CB . THR B 544 ? 2.1484 2.2151 3.2216 -0.1840 0.0770 0.3874 2191 THR B CB 8726 O OG1 . THR B 544 ? 2.1341 2.2767 3.3534 -0.1923 0.1010 0.4428 2191 THR B OG1 8727 C CG2 . THR B 544 ? 2.0196 2.0135 3.0174 -0.2296 -0.0108 0.3671 2191 THR B CG2 8728 N N . ALA B 545 ? 1.7668 1.8383 2.7605 -0.0874 0.2053 0.3510 2192 ALA B N 8729 C CA . ALA B 545 ? 1.5788 1.6597 2.5647 -0.0442 0.2663 0.3484 2192 ALA B CA 8730 C C . ALA B 545 ? 1.5124 1.6645 2.6259 -0.0288 0.2720 0.4011 2192 ALA B C 8731 O O . ALA B 545 ? 1.4361 1.6382 2.6522 -0.0549 0.2228 0.4425 2192 ALA B O 8732 C CB . ALA B 545 ? 1.6109 1.6338 2.4757 -0.0330 0.2564 0.3028 2192 ALA B CB 8733 N N . SER B 546 ? 1.5256 1.6773 2.6310 0.0135 0.3303 0.4008 2193 SER B N 8734 C CA . SER B 546 ? 1.5334 1.7467 2.7568 0.0427 0.3587 0.4515 2193 SER B CA 8735 C C . SER B 546 ? 1.6332 1.8766 2.9069 0.0317 0.2917 0.4748 2193 SER B C 8736 O O . SER B 546 ? 1.8584 2.1469 3.2199 0.0604 0.3102 0.5145 2193 SER B O 8737 C CB . SER B 546 ? 1.4926 1.6667 2.6550 0.0913 0.4359 0.4336 2193 SER B CB 8738 O OG . SER B 546 ? 1.4727 1.5727 2.4928 0.0895 0.4232 0.3776 2193 SER B OG 8739 N N . SER B 547 ? 1.6367 1.8491 2.8504 -0.0085 0.2147 0.4523 2194 SER B N 8740 C CA . SER B 547 ? 1.7252 1.9322 2.9274 -0.0221 0.1445 0.4587 2194 SER B CA 8741 C C . SER B 547 ? 1.7836 1.9028 2.8172 -0.0245 0.1351 0.3963 2194 SER B C 8742 O O . SER B 547 ? 1.7308 1.8087 2.6830 -0.0125 0.1835 0.3567 2194 SER B O 8743 C CB . SER B 547 ? 1.6852 1.9330 2.9600 0.0153 0.1665 0.4943 2194 SER B CB 8744 O OG . SER B 547 ? 1.5773 1.7648 2.7375 0.0456 0.2056 0.4525 2194 SER B OG 8745 N N . TYR B 548 ? 1.8775 1.9687 2.8611 -0.0395 0.0726 0.3921 2195 TYR B N 8746 C CA . TYR B 548 ? 1.9466 1.9567 2.7772 -0.0429 0.0611 0.3408 2195 TYR B CA 8747 C C . TYR B 548 ? 2.1437 2.1318 2.9365 -0.0487 0.0042 0.3502 2195 TYR B C 8748 O O . TYR B 548 ? 2.3835 2.4100 3.2583 -0.0651 -0.0514 0.3936 2195 TYR B O 8749 C CB . TYR B 548 ? 1.8961 1.8575 2.6550 -0.0743 0.0346 0.3103 2195 TYR B CB 8750 C CG . TYR B 548 ? 1.9932 1.9540 2.7855 -0.1173 -0.0463 0.3343 2195 TYR B CG 8751 C CD1 . TYR B 548 ? 1.9764 2.0097 2.9140 -0.1352 -0.0609 0.3829 2195 TYR B CD1 8752 C CD2 . TYR B 548 ? 2.1344 2.0155 2.8087 -0.1413 -0.1081 0.3104 2195 TYR B CD2 8753 C CE1 . TYR B 548 ? 2.0304 2.0603 3.0026 -0.1817 -0.1440 0.4080 2195 TYR B CE1 8754 C CE2 . TYR B 548 ? 2.2480 2.1102 2.9353 -0.1856 -0.1901 0.3301 2195 TYR B CE2 8755 C CZ . TYR B 548 ? 2.1609 2.0995 3.0010 -0.2086 -0.2122 0.3794 2195 TYR B CZ 8756 O OH . TYR B 548 ? 2.3178 2.2345 3.1733 -0.2592 -0.3022 0.4017 2195 TYR B OH 8757 N N . PHE B 549 ? 2.2116 2.1385 2.8823 -0.0353 0.0183 0.3133 2196 PHE B N 8758 C CA . PHE B 549 ? 2.1136 2.0003 2.7152 -0.0406 -0.0311 0.3159 2196 PHE B CA 8759 C C . PHE B 549 ? 1.9886 1.8149 2.5073 -0.0783 -0.0989 0.3017 2196 PHE B C 8760 O O . PHE B 549 ? 1.8094 1.5952 2.2662 -0.0893 -0.0878 0.2686 2196 PHE B O 8761 C CB . PHE B 549 ? 2.1911 2.0314 2.6916 -0.0142 0.0135 0.2847 2196 PHE B CB 8762 C CG . PHE B 549 ? 2.3070 2.0992 2.7243 -0.0167 -0.0290 0.2883 2196 PHE B CG 8763 C CD1 . PHE B 549 ? 2.4268 2.2511 2.9080 -0.0113 -0.0625 0.3306 2196 PHE B CD1 8764 C CD2 . PHE B 549 ? 2.3543 2.0670 2.6287 -0.0218 -0.0333 0.2532 2196 PHE B CD2 8765 C CE1 . PHE B 549 ? 2.5361 2.3094 2.9308 -0.0144 -0.1045 0.3361 2196 PHE B CE1 8766 C CE2 . PHE B 549 ? 2.5005 2.1596 2.6844 -0.0225 -0.0679 0.2581 2196 PHE B CE2 8767 C CZ . PHE B 549 ? 2.6589 2.3463 2.8987 -0.0204 -0.1061 0.2988 2196 PHE B CZ 8768 N N . THR B 550 ? 1.9192 1.7345 2.4367 -0.0980 -0.1720 0.3294 2197 THR B N 8769 C CA . THR B 550 ? 2.0631 1.7916 2.4624 -0.1319 -0.2423 0.3132 2197 THR B CA 8770 C C . THR B 550 ? 2.1663 1.8802 2.5528 -0.1445 -0.3156 0.3466 2197 THR B C 8771 O O . THR B 550 ? 2.1827 1.9779 2.7057 -0.1415 -0.3334 0.3960 2197 THR B O 8772 C CB . THR B 550 ? 2.0828 1.8106 2.5211 -0.1704 -0.2825 0.3170 2197 THR B CB 8773 O OG1 . THR B 550 ? 2.1931 1.8187 2.5023 -0.2050 -0.3611 0.3035 2197 THR B OG1 8774 C CG2 . THR B 550 ? 2.0850 1.9208 2.7174 -0.1849 -0.3069 0.3762 2197 THR B CG2 8775 N N . ASN B 551 ? 2.3757 1.9822 2.5940 -0.1550 -0.3539 0.3215 2198 ASN B N 8776 C CA . ASN B 551 ? 2.5821 2.1512 2.7532 -0.1707 -0.4326 0.3501 2198 ASN B CA 8777 C C . ASN B 551 ? 2.7220 2.1560 2.7108 -0.2038 -0.5009 0.3238 2198 ASN B C 8778 O O . ASN B 551 ? 2.4967 1.8698 2.4063 -0.2124 -0.4841 0.2844 2198 ASN B O 8779 C CB . ASN B 551 ? 2.6378 2.2109 2.7790 -0.1325 -0.3929 0.3559 2198 ASN B CB 8780 C CG . ASN B 551 ? 2.7658 2.2506 2.7384 -0.1084 -0.3340 0.3062 2198 ASN B CG 8781 O OD1 . ASN B 551 ? 2.9586 2.3447 2.7866 -0.1217 -0.3484 0.2721 2198 ASN B OD1 8782 N ND2 . ASN B 551 ? 2.7617 2.2787 2.7540 -0.0719 -0.2662 0.3052 2198 ASN B ND2 8783 N N . MET B 552 ? 2.9416 2.3205 2.8557 -0.2200 -0.5769 0.3462 2199 MET B N 8784 C CA . MET B 552 ? 3.0641 2.2967 2.7875 -0.2541 -0.6543 0.3262 2199 MET B CA 8785 C C . MET B 552 ? 3.0425 2.1614 2.5804 -0.2324 -0.5897 0.2634 2199 MET B C 8786 O O . MET B 552 ? 3.2943 2.2907 2.6867 -0.2579 -0.6330 0.2364 2199 MET B O 8787 C CB . MET B 552 ? 3.1473 2.3263 2.7879 -0.2627 -0.7268 0.3555 2199 MET B CB 8788 C CG . MET B 552 ? 3.3383 2.3861 2.8335 -0.3155 -0.8441 0.3555 2199 MET B CG 8789 S SD . MET B 552 ? 3.6574 2.5606 2.9256 -0.3173 -0.9073 0.3600 2199 MET B SD 8790 C CE . MET B 552 ? 3.5751 2.3671 2.6303 -0.2630 -0.7857 0.2936 2199 MET B CE 8791 N N . PHE B 553 ? 2.7940 1.9517 2.3416 -0.1854 -0.4866 0.2431 2200 PHE B N 8792 C CA . PHE B 553 ? 2.8868 1.9605 2.2945 -0.1606 -0.4172 0.1926 2200 PHE B CA 8793 C C . PHE B 553 ? 2.9290 2.0684 2.4358 -0.1508 -0.3528 0.1718 2200 PHE B C 8794 O O . PHE B 553 ? 3.2476 2.3270 2.7023 -0.1696 -0.3698 0.1486 2200 PHE B O 8795 C CB . PHE B 553 ? 2.8276 1.8697 2.1402 -0.1203 -0.3558 0.1844 2200 PHE B CB 8796 C CG . PHE B 553 ? 3.0954 2.0155 2.2313 -0.1295 -0.4143 0.1901 2200 PHE B CG 8797 C CD1 . PHE B 553 ? 3.3730 2.1398 2.3155 -0.1470 -0.4552 0.1621 2200 PHE B CD1 8798 C CD2 . PHE B 553 ? 3.1327 2.0783 2.2820 -0.1199 -0.4292 0.2236 2200 PHE B CD2 8799 C CE1 . PHE B 553 ? 3.5938 2.2316 2.3513 -0.1556 -0.5103 0.1664 2200 PHE B CE1 8800 C CE2 . PHE B 553 ? 3.3062 2.1324 2.2818 -0.1290 -0.4856 0.2309 2200 PHE B CE2 8801 C CZ . PHE B 553 ? 3.5341 2.2041 2.3084 -0.1470 -0.5261 0.2018 2200 PHE B CZ 8802 N N . ALA B 554 ? 2.8219 2.0746 2.4641 -0.1236 -0.2843 0.1810 2201 ALA B N 8803 C CA . ALA B 554 ? 2.6582 1.9672 2.3809 -0.1117 -0.2201 0.1618 2201 ALA B CA 8804 C C . ALA B 554 ? 2.5349 1.9058 2.3883 -0.1422 -0.2542 0.1785 2201 ALA B C 8805 O O . ALA B 554 ? 2.4665 1.8553 2.3778 -0.1744 -0.3293 0.2116 2201 ALA B O 8806 C CB . ALA B 554 ? 2.5558 1.9476 2.3600 -0.0759 -0.1415 0.1657 2201 ALA B CB 8807 N N . THR B 555 ? 2.4264 1.8276 2.3248 -0.1329 -0.2002 0.1591 2202 THR B N 8808 C CA . THR B 555 ? 2.3974 1.8725 2.4343 -0.1530 -0.2074 0.1770 2202 THR B CA 8809 C C . THR B 555 ? 2.2475 1.7686 2.3303 -0.1265 -0.1245 0.1578 2202 THR B C 8810 O O . THR B 555 ? 2.1882 1.6645 2.2190 -0.1286 -0.1077 0.1307 2202 THR B O 8811 C CB . THR B 555 ? 2.5843 1.9916 2.5782 -0.1950 -0.2748 0.1725 2202 THR B CB 8812 O OG1 . THR B 555 ? 2.8060 2.1693 2.7607 -0.2260 -0.3636 0.1948 2202 THR B OG1 8813 C CG2 . THR B 555 ? 2.4042 1.8931 2.5500 -0.2160 -0.2752 0.1960 2202 THR B CG2 8814 N N . TRP B 556 ? 2.1354 1.7375 2.3087 -0.1017 -0.0759 0.1729 2203 TRP B N 8815 C CA . TRP B 556 ? 2.0586 1.6989 2.2683 -0.0784 -0.0031 0.1574 2203 TRP B CA 8816 C C . TRP B 556 ? 2.0506 1.7457 2.3680 -0.0928 0.0013 0.1733 2203 TRP B C 8817 O O . TRP B 556 ? 2.0955 1.8564 2.5027 -0.0771 0.0445 0.1883 2203 TRP B O 8818 C CB . TRP B 556 ? 1.9816 1.6657 2.2251 -0.0489 0.0438 0.1651 2203 TRP B CB 8819 C CG . TRP B 556 ? 2.1941 1.8256 2.3350 -0.0355 0.0449 0.1529 2203 TRP B CG 8820 C CD1 . TRP B 556 ? 2.3115 1.9272 2.4277 -0.0378 0.0062 0.1715 2203 TRP B CD1 8821 C CD2 . TRP B 556 ? 2.2777 1.8653 2.3281 -0.0177 0.0870 0.1243 2203 TRP B CD2 8822 N NE1 . TRP B 556 ? 2.4290 1.9890 2.4370 -0.0220 0.0257 0.1548 2203 TRP B NE1 8823 C CE2 . TRP B 556 ? 2.3671 1.9128 2.3393 -0.0090 0.0772 0.1273 2203 TRP B CE2 8824 C CE3 . TRP B 556 ? 2.3186 1.9015 2.3532 -0.0078 0.1317 0.1014 2203 TRP B CE3 8825 C CZ2 . TRP B 556 ? 2.3714 1.8741 2.2555 0.0101 0.1167 0.1097 2203 TRP B CZ2 8826 C CZ3 . TRP B 556 ? 2.3347 1.8805 2.2914 0.0107 0.1662 0.0856 2203 TRP B CZ3 8827 C CH2 . TRP B 556 ? 2.3768 1.8845 2.2617 0.0199 0.1614 0.0906 2203 TRP B CH2 8828 N N . SER B 557 ? 2.1075 1.7647 2.4054 -0.1226 -0.0425 0.1704 2204 SER B N 8829 C CA . SER B 557 ? 1.9971 1.6979 2.3928 -0.1427 -0.0457 0.1894 2204 SER B CA 8830 C C . SER B 557 ? 1.7952 1.5264 2.2171 -0.1199 0.0261 0.1763 2204 SER B C 8831 O O . SER B 557 ? 1.8355 1.5242 2.1730 -0.1024 0.0586 0.1432 2204 SER B O 8832 C CB . SER B 557 ? 2.1545 1.7835 2.4932 -0.1794 -0.1043 0.1802 2204 SER B CB 8833 O OG . SER B 557 ? 2.3085 1.8341 2.4904 -0.1717 -0.1101 0.1404 2204 SER B OG 8834 N N . PRO B 558 ? 1.6858 1.4899 2.2249 -0.1188 0.0519 0.2060 2205 PRO B N 8835 C CA . PRO B 558 ? 1.7316 1.5556 2.2904 -0.1027 0.1126 0.1982 2205 PRO B CA 8836 C C . PRO B 558 ? 1.7997 1.5649 2.2818 -0.1117 0.1134 0.1678 2205 PRO B C 8837 O O . PRO B 558 ? 1.7153 1.4713 2.1628 -0.0928 0.1588 0.1481 2205 PRO B O 8838 C CB . PRO B 558 ? 1.7176 1.6109 2.4089 -0.1138 0.1176 0.2428 2205 PRO B CB 8839 C CG . PRO B 558 ? 1.7337 1.6435 2.4799 -0.1427 0.0482 0.2738 2205 PRO B CG 8840 C CD . PRO B 558 ? 1.7030 1.5747 2.3665 -0.1319 0.0250 0.2545 2205 PRO B CD 8841 N N . SER B 559 ? 1.9189 1.6386 2.3722 -0.1412 0.0589 0.1661 2206 SER B N 8842 C CA . SER B 559 ? 2.0134 1.6640 2.3899 -0.1501 0.0526 0.1396 2206 SER B CA 8843 C C . SER B 559 ? 1.9780 1.5623 2.2317 -0.1253 0.0702 0.1006 2206 SER B C 8844 O O . SER B 559 ? 1.9442 1.4571 2.1211 -0.1284 0.0618 0.0787 2206 SER B O 8845 C CB . SER B 559 ? 2.2811 1.8897 2.6560 -0.1914 -0.0174 0.1512 2206 SER B CB 8846 O OG . SER B 559 ? 2.4211 2.0735 2.8657 -0.2086 -0.0601 0.1840 2206 SER B OG 8847 N N . LYS B 560 ? 1.8883 1.4960 2.1290 -0.0998 0.0974 0.0959 2207 LYS B N 8848 C CA . LYS B 560 ? 1.8405 1.4029 1.9857 -0.0739 0.1221 0.0683 2207 LYS B CA 8849 C C . LYS B 560 ? 1.6654 1.2714 1.8365 -0.0491 0.1784 0.0647 2207 LYS B C 8850 O O . LYS B 560 ? 1.5413 1.1283 1.6595 -0.0284 0.2032 0.0500 2207 LYS B O 8851 C CB . LYS B 560 ? 1.8742 1.4142 1.9686 -0.0691 0.1002 0.0683 2207 LYS B CB 8852 C CG . LYS B 560 ? 1.9688 1.4354 1.9922 -0.0922 0.0387 0.0656 2207 LYS B CG 8853 C CD . LYS B 560 ? 1.9699 1.3436 1.8528 -0.0745 0.0444 0.0387 2207 LYS B CD 8854 C CE . LYS B 560 ? 2.1719 1.4623 1.9683 -0.0987 -0.0225 0.0379 2207 LYS B CE 8855 N NZ . LYS B 560 ? 2.2922 1.4843 1.9369 -0.0764 -0.0110 0.0150 2207 LYS B NZ 8856 N N . ALA B 561 ? 1.6975 1.3576 1.9472 -0.0519 0.1980 0.0808 2208 ALA B N 8857 C CA . ALA B 561 ? 1.7957 1.4844 2.0582 -0.0330 0.2437 0.0781 2208 ALA B CA 8858 C C . ALA B 561 ? 1.6679 1.3317 1.8941 -0.0264 0.2624 0.0629 2208 ALA B C 8859 O O . ALA B 561 ? 1.5312 1.2110 1.7821 -0.0265 0.2829 0.0678 2208 ALA B O 8860 C CB . ALA B 561 ? 1.8148 1.5528 2.1536 -0.0341 0.2629 0.1001 2208 ALA B CB 8861 N N . ARG B 562 ? 1.5790 1.1999 1.7429 -0.0180 0.2571 0.0469 2209 ARG B N 8862 C CA . ARG B 562 ? 1.6498 1.2417 1.7869 -0.0120 0.2670 0.0376 2209 ARG B CA 8863 C C . ARG B 562 ? 1.6388 1.2311 1.7512 0.0108 0.2949 0.0317 2209 ARG B C 8864 O O . ARG B 562 ? 1.5993 1.1607 1.6632 0.0256 0.2996 0.0239 2209 ARG B O 8865 C CB . ARG B 562 ? 1.9321 1.4613 2.0210 -0.0210 0.2383 0.0281 2209 ARG B CB 8866 C CG . ARG B 562 ? 1.9489 1.4831 2.0803 -0.0506 0.2058 0.0409 2209 ARG B CG 8867 C CD . ARG B 562 ? 2.0351 1.4924 2.1087 -0.0660 0.1683 0.0309 2209 ARG B CD 8868 N NE . ARG B 562 ? 2.0038 1.4772 2.1370 -0.1000 0.1327 0.0505 2209 ARG B NE 8869 C CZ . ARG B 562 ? 2.0592 1.5370 2.2325 -0.1150 0.1334 0.0613 2209 ARG B CZ 8870 N NH1 . ARG B 562 ? 1.9242 1.3847 2.0748 -0.0982 0.1638 0.0517 2209 ARG B NH1 8871 N NH2 . ARG B 562 ? 2.1358 1.6376 2.3777 -0.1474 0.1027 0.0862 2209 ARG B NH2 8872 N N . LEU B 563 ? 1.6338 1.2579 1.7790 0.0126 0.3128 0.0387 2210 LEU B N 8873 C CA . LEU B 563 ? 1.5936 1.2340 1.7403 0.0271 0.3331 0.0422 2210 LEU B CA 8874 C C . LEU B 563 ? 1.5902 1.2112 1.7045 0.0475 0.3453 0.0391 2210 LEU B C 8875 O O . LEU B 563 ? 1.6118 1.2557 1.7352 0.0553 0.3596 0.0463 2210 LEU B O 8876 C CB . LEU B 563 ? 1.5918 1.2374 1.7550 0.0262 0.3375 0.0488 2210 LEU B CB 8877 C CG . LEU B 563 ? 1.6269 1.3013 1.8095 0.0295 0.3465 0.0598 2210 LEU B CG 8878 C CD1 . LEU B 563 ? 1.5193 1.2091 1.7095 0.0152 0.3455 0.0618 2210 LEU B CD1 8879 C CD2 . LEU B 563 ? 1.7833 1.4572 1.9773 0.0326 0.3446 0.0701 2210 LEU B CD2 8880 N N . HIS B 564 ? 1.5602 1.1329 1.6326 0.0576 0.3435 0.0301 2211 HIS B N 8881 C CA . HIS B 564 ? 1.6960 1.2460 1.7302 0.0822 0.3653 0.0294 2211 HIS B CA 8882 C C . HIS B 564 ? 1.8289 1.3264 1.7930 0.0848 0.3560 0.0173 2211 HIS B C 8883 O O . HIS B 564 ? 1.8585 1.3534 1.7975 0.1000 0.3753 0.0212 2211 HIS B O 8884 C CB . HIS B 564 ? 1.8541 1.3991 1.8964 0.1069 0.3908 0.0378 2211 HIS B CB 8885 C CG . HIS B 564 ? 1.8805 1.4921 1.9935 0.1065 0.4016 0.0592 2211 HIS B CG 8886 N ND1 . HIS B 564 ? 1.9451 1.5849 2.0831 0.1258 0.4289 0.0776 2211 HIS B ND1 8887 C CD2 . HIS B 564 ? 1.8490 1.4989 2.0082 0.0861 0.3854 0.0671 2211 HIS B CD2 8888 C CE1 . HIS B 564 ? 1.8735 1.5683 2.0763 0.1130 0.4217 0.0966 2211 HIS B CE1 8889 N NE2 . HIS B 564 ? 1.7604 1.4554 1.9670 0.0895 0.3949 0.0883 2211 HIS B NE2 8890 N N . LEU B 565 ? 1.9253 1.3808 1.8591 0.0666 0.3232 0.0059 2212 LEU B N 8891 C CA . LEU B 565 ? 2.0359 1.4302 1.8943 0.0614 0.2992 -0.0048 2212 LEU B CA 8892 C C . LEU B 565 ? 2.0712 1.4547 1.8830 0.0797 0.3187 -0.0027 2212 LEU B C 8893 O O . LEU B 565 ? 1.9379 1.3730 1.7897 0.0731 0.3182 0.0082 2212 LEU B O 8894 C CB . LEU B 565 ? 1.9661 1.3794 1.8597 0.0273 0.2542 -0.0006 2212 LEU B CB 8895 C CG . LEU B 565 ? 2.0843 1.4684 1.9322 0.0160 0.2213 -0.0006 2212 LEU B CG 8896 C CD1 . LEU B 565 ? 2.2511 1.5275 1.9849 0.0131 0.1928 -0.0168 2212 LEU B CD1 8897 C CD2 . LEU B 565 ? 2.1088 1.5481 2.0369 -0.0124 0.1876 0.0158 2212 LEU B CD2 8898 N N . GLN B 566 ? 2.2260 1.5341 1.9468 0.1050 0.3395 -0.0122 2213 GLN B N 8899 C CA . GLN B 566 ? 2.3995 1.6676 2.0438 0.1192 0.3507 -0.0123 2213 GLN B CA 8900 C C . GLN B 566 ? 2.5928 1.7738 2.1442 0.0986 0.2994 -0.0281 2213 GLN B C 8901 O O . GLN B 566 ? 3.0866 2.1958 2.5841 0.0947 0.2823 -0.0433 2213 GLN B O 8902 C CB . GLN B 566 ? 2.5416 1.7644 2.1274 0.1616 0.4075 -0.0112 2213 GLN B CB 8903 C CG . GLN B 566 ? 2.6286 1.8654 2.1954 0.1809 0.4429 0.0038 2213 GLN B CG 8904 C CD . GLN B 566 ? 2.6656 2.0101 2.3538 0.1861 0.4757 0.0297 2213 GLN B CD 8905 O OE1 . GLN B 566 ? 2.5746 1.9945 2.3547 0.1592 0.4507 0.0361 2213 GLN B OE1 8906 N NE2 . GLN B 566 ? 2.6372 1.9842 2.3236 0.2210 0.5328 0.0472 2213 GLN B NE2 8907 N N . GLY B 567 ? 2.4934 1.6767 2.0268 0.0830 0.2696 -0.0224 2214 GLY B N 8908 C CA . GLY B 567 ? 2.5993 1.7103 2.0606 0.0550 0.2060 -0.0308 2214 GLY B CA 8909 C C . GLY B 567 ? 2.7055 1.7942 2.1080 0.0533 0.1880 -0.0229 2214 GLY B C 8910 O O . GLY B 567 ? 2.4721 1.5856 1.8708 0.0786 0.2337 -0.0138 2214 GLY B O 8911 N N . ARG B 568 ? 2.8622 1.9050 2.2233 0.0214 0.1187 -0.0225 2215 ARG B N 8912 C CA . ARG B 568 ? 3.0273 2.0405 2.3251 0.0162 0.0893 -0.0121 2215 ARG B CA 8913 C C . ARG B 568 ? 2.8165 1.9544 2.2514 0.0131 0.0976 0.0138 2215 ARG B C 8914 O O . ARG B 568 ? 2.9257 2.0908 2.3616 0.0374 0.1436 0.0216 2215 ARG B O 8915 C CB . ARG B 568 ? 3.2218 2.1476 2.4384 -0.0211 0.0023 -0.0146 2215 ARG B CB 8916 C CG . ARG B 568 ? 3.2016 1.9980 2.2347 -0.0148 -0.0195 -0.0224 2215 ARG B CG 8917 C CD . ARG B 568 ? 3.4386 2.1050 2.3074 0.0193 0.0298 -0.0514 2215 ARG B CD 8918 N NE . ARG B 568 ? 3.8859 2.4597 2.6908 0.0028 -0.0017 -0.0745 2215 ARG B NE 8919 C CZ . ARG B 568 ? 3.8061 2.4046 2.6715 0.0139 0.0351 -0.0854 2215 ARG B CZ 8920 N NH1 . ARG B 568 ? 3.5432 2.2599 2.5383 0.0402 0.1023 -0.0755 2215 ARG B NH1 8921 N NH2 . ARG B 568 ? 3.8430 2.3402 2.6344 -0.0038 -0.0005 -0.1052 2215 ARG B NH2 8922 N N . SER B 569 ? 2.4969 1.7065 2.0477 -0.0151 0.0578 0.0289 2216 SER B N 8923 C CA . SER B 569 ? 2.1978 1.5201 1.8828 -0.0125 0.0782 0.0500 2216 SER B CA 8924 C C . SER B 569 ? 2.0746 1.4525 1.8512 -0.0148 0.1034 0.0452 2216 SER B C 8925 O O . SER B 569 ? 2.1126 1.4937 1.9279 -0.0387 0.0686 0.0475 2216 SER B O 8926 C CB . SER B 569 ? 2.2693 1.6260 2.0133 -0.0366 0.0201 0.0764 2216 SER B CB 8927 O OG . SER B 569 ? 2.5882 1.9097 2.3253 -0.0691 -0.0428 0.0782 2216 SER B OG 8928 N N . ASN B 570 ? 1.9782 1.3956 1.7862 0.0079 0.1614 0.0409 2217 ASN B N 8929 C CA . ASN B 570 ? 1.9823 1.4206 1.8328 0.0099 0.1862 0.0315 2217 ASN B CA 8930 C C . ASN B 570 ? 1.7684 1.2910 1.7276 0.0092 0.2104 0.0426 2217 ASN B C 8931 O O . ASN B 570 ? 1.6968 1.2428 1.6719 0.0246 0.2508 0.0398 2217 ASN B O 8932 C CB . ASN B 570 ? 2.2584 1.6473 2.0358 0.0356 0.2273 0.0151 2217 ASN B CB 8933 C CG . ASN B 570 ? 2.2246 1.6318 1.9914 0.0604 0.2724 0.0222 2217 ASN B CG 8934 O OD1 . ASN B 570 ? 2.2331 1.6926 2.0520 0.0575 0.2760 0.0364 2217 ASN B OD1 8935 N ND2 . ASN B 570 ? 2.2322 1.5931 1.9329 0.0863 0.3096 0.0151 2217 ASN B ND2 8936 N N . ALA B 571 ? 1.7020 1.2653 1.7337 -0.0092 0.1845 0.0576 2218 ALA B N 8937 C CA . ALA B 571 ? 1.6862 1.3151 1.8078 -0.0083 0.2087 0.0690 2218 ALA B CA 8938 C C . ALA B 571 ? 1.8220 1.4867 2.0132 -0.0230 0.1795 0.0922 2218 ALA B C 8939 O O . ALA B 571 ? 1.8899 1.5351 2.0641 -0.0349 0.1366 0.1013 2218 ALA B O 8940 C CB . ALA B 571 ? 1.6535 1.3060 1.7810 0.0095 0.2447 0.0707 2218 ALA B CB 8941 N N . TRP B 572 ? 1.8882 1.6029 2.1570 -0.0211 0.2033 0.1048 2219 TRP B N 8942 C CA . TRP B 572 ? 1.7630 1.5240 2.1156 -0.0255 0.1915 0.1340 2219 TRP B CA 8943 C C . TRP B 572 ? 1.6728 1.4489 2.0319 -0.0055 0.2111 0.1421 2219 TRP B C 8944 O O . TRP B 572 ? 1.5539 1.3167 1.8746 0.0090 0.2444 0.1268 2219 TRP B O 8945 C CB . TRP B 572 ? 1.6057 1.4050 2.0326 -0.0281 0.2161 0.1476 2219 TRP B CB 8946 C CG . TRP B 572 ? 1.5457 1.3973 2.0652 -0.0216 0.2232 0.1814 2219 TRP B CG 8947 C CD1 . TRP B 572 ? 1.5815 1.4639 2.1676 -0.0347 0.1822 0.2126 2219 TRP B CD1 8948 C CD2 . TRP B 572 ? 1.5357 1.4112 2.0914 0.0021 0.2748 0.1910 2219 TRP B CD2 8949 N NE1 . TRP B 572 ? 1.5367 1.4714 2.2133 -0.0165 0.2107 0.2447 2219 TRP B NE1 8950 C CE2 . TRP B 572 ? 1.5349 1.4595 2.1863 0.0081 0.2711 0.2298 2219 TRP B CE2 8951 C CE3 . TRP B 572 ? 1.5614 1.4148 2.0735 0.0184 0.3219 0.1721 2219 TRP B CE3 8952 C CZ2 . TRP B 572 ? 1.5407 1.4881 2.2406 0.0361 0.3226 0.2485 2219 TRP B CZ2 8953 C CZ3 . TRP B 572 ? 1.6426 1.5076 2.1876 0.0411 0.3662 0.1869 2219 TRP B CZ3 8954 C CH2 . TRP B 572 ? 1.6292 1.5386 2.2651 0.0528 0.3711 0.2240 2219 TRP B CH2 8955 N N . ARG B 573 ? 1.7395 1.5406 2.1483 -0.0074 0.1843 0.1689 2220 ARG B N 8956 C CA . ARG B 573 ? 1.8306 1.6509 2.2668 0.0129 0.2020 0.1850 2220 ARG B CA 8957 C C . ARG B 573 ? 1.8622 1.7367 2.4076 0.0114 0.1855 0.2251 2220 ARG B C 8958 O O . ARG B 573 ? 2.0053 1.8894 2.5786 -0.0118 0.1346 0.2413 2220 ARG B O 8959 C CB . ARG B 573 ? 1.9432 1.7274 2.3088 0.0146 0.1768 0.1803 2220 ARG B CB 8960 C CG . ARG B 573 ? 1.9977 1.7341 2.2656 0.0188 0.1966 0.1491 2220 ARG B CG 8961 C CD . ARG B 573 ? 1.9622 1.6642 2.1646 0.0240 0.1800 0.1518 2220 ARG B CD 8962 N NE . ARG B 573 ? 1.9820 1.7105 2.2371 0.0335 0.1724 0.1797 2220 ARG B NE 8963 C CZ . ARG B 573 ? 2.1296 1.8352 2.3453 0.0374 0.1502 0.1923 2220 ARG B CZ 8964 N NH1 . ARG B 573 ? 2.1191 1.7701 2.2329 0.0333 0.1370 0.1786 2220 ARG B NH1 8965 N NH2 . ARG B 573 ? 2.3178 2.0512 2.5935 0.0487 0.1449 0.2209 2220 ARG B NH2 8966 N N . PRO B 574 ? 1.8744 1.7808 2.4831 0.0360 0.2281 0.2441 2221 PRO B N 8967 C CA . PRO B 574 ? 2.0693 2.0341 2.7952 0.0424 0.2183 0.2909 2221 PRO B CA 8968 C C . PRO B 574 ? 2.2673 2.2338 2.9977 0.0454 0.1768 0.3117 2221 PRO B C 8969 O O . PRO B 574 ? 2.4447 2.3628 3.0812 0.0486 0.1719 0.2878 2221 PRO B O 8970 C CB . PRO B 574 ? 1.9638 1.9407 2.7275 0.0760 0.2894 0.2986 2221 PRO B CB 8971 C CG . PRO B 574 ? 1.8256 1.7419 2.4806 0.0856 0.3191 0.2581 2221 PRO B CG 8972 C CD . PRO B 574 ? 1.8060 1.6912 2.3816 0.0586 0.2878 0.2255 2221 PRO B CD 8973 N N . GLN B 575 ? 2.1352 2.1579 2.9761 0.0438 0.1465 0.3597 2222 GLN B N 8974 C CA . GLN B 575 ? 2.1215 2.1452 2.9678 0.0449 0.0988 0.3846 2222 GLN B CA 8975 C C . GLN B 575 ? 2.1680 2.1855 3.0164 0.0846 0.1443 0.3921 2222 GLN B C 8976 O O . GLN B 575 ? 2.4336 2.4004 3.1885 0.0879 0.1364 0.3722 2222 GLN B O 8977 C CB . GLN B 575 ? 2.0472 2.1300 3.0083 0.0234 0.0345 0.4371 2222 GLN B CB 8978 C CG . GLN B 575 ? 2.1430 2.3025 3.2498 0.0285 0.0645 0.4747 2222 GLN B CG 8979 C CD . GLN B 575 ? 2.2405 2.4782 3.4992 0.0229 0.0167 0.5439 2222 GLN B CD 8980 O OE1 . GLN B 575 ? 2.1716 2.4697 3.5451 0.0021 -0.0013 0.5803 2222 GLN B OE1 8981 N NE2 . GLN B 575 ? 2.1991 2.4396 3.4679 0.0408 -0.0054 0.5675 2222 GLN B NE2 8982 N N . VAL B 576 ? 2.0563 2.1169 3.0037 0.1161 0.1953 0.4213 2223 VAL B N 8983 C CA . VAL B 576 ? 2.2357 2.2662 3.1594 0.1557 0.2495 0.4183 2223 VAL B CA 8984 C C . VAL B 576 ? 2.0019 1.9821 2.8425 0.1625 0.3106 0.3719 2223 VAL B C 8985 O O . VAL B 576 ? 1.8417 1.8297 2.6775 0.1441 0.3156 0.3557 2223 VAL B O 8986 C CB . VAL B 576 ? 2.6202 2.7062 3.6792 0.1941 0.2798 0.4742 2223 VAL B CB 8987 C CG1 . VAL B 576 ? 2.6485 2.6884 3.6708 0.2330 0.3193 0.4738 2223 VAL B CG1 8988 C CG2 . VAL B 576 ? 2.7544 2.9114 3.9279 0.1781 0.2096 0.5293 2223 VAL B CG2 8989 N N . ASN B 577 ? 1.8819 1.8064 2.6548 0.1852 0.3505 0.3525 2224 ASN B N 8990 C CA . ASN B 577 ? 1.7867 1.6573 2.4811 0.1898 0.4020 0.3134 2224 ASN B CA 8991 C C . ASN B 577 ? 1.7294 1.5876 2.4573 0.2274 0.4708 0.3263 2224 ASN B C 8992 O O . ASN B 577 ? 1.7794 1.6052 2.5044 0.2588 0.5004 0.3378 2224 ASN B O 8993 C CB . ASN B 577 ? 1.8359 1.6407 2.4211 0.1827 0.3992 0.2808 2224 ASN B CB 8994 C CG . ASN B 577 ? 1.8787 1.6870 2.4222 0.1538 0.3432 0.2716 2224 ASN B CG 8995 O OD1 . ASN B 577 ? 2.0325 1.8628 2.6074 0.1535 0.3047 0.2978 2224 ASN B OD1 8996 N ND2 . ASN B 577 ? 1.7347 1.5171 2.2040 0.1313 0.3392 0.2370 2224 ASN B ND2 8997 N N . ASN B 578 ? 1.6608 1.5350 2.4102 0.2255 0.4988 0.3243 2225 ASN B N 8998 C CA . ASN B 578 ? 1.6753 1.5375 2.4554 0.2634 0.5696 0.3411 2225 ASN B CA 8999 C C . ASN B 578 ? 1.6925 1.4829 2.3677 0.2621 0.6109 0.3027 2225 ASN B C 9000 O O . ASN B 578 ? 1.7017 1.4942 2.3385 0.2300 0.5880 0.2782 2225 ASN B O 9001 C CB . ASN B 578 ? 1.8614 1.8079 2.7695 0.2655 0.5749 0.3838 2225 ASN B CB 9002 C CG . ASN B 578 ? 2.1009 2.1151 3.1408 0.2883 0.5654 0.4403 2225 ASN B CG 9003 O OD1 . ASN B 578 ? 2.1984 2.1971 3.2288 0.2996 0.5453 0.4459 2225 ASN B OD1 9004 N ND2 . ASN B 578 ? 2.3042 2.3973 3.4763 0.2948 0.5784 0.4879 2225 ASN B ND2 9005 N N . PRO B 579 ? 1.8236 1.5428 2.4476 0.2982 0.6714 0.2988 2226 PRO B N 9006 C CA . PRO B 579 ? 2.0550 1.6951 2.5715 0.2981 0.7110 0.2665 2226 PRO B CA 9007 C C . PRO B 579 ? 2.1884 1.8694 2.7483 0.2956 0.7356 0.2800 2226 PRO B C 9008 O O . PRO B 579 ? 2.2104 1.8570 2.6926 0.2713 0.7300 0.2504 2226 PRO B O 9009 C CB . PRO B 579 ? 2.3103 1.8623 2.7732 0.3444 0.7739 0.2693 2226 PRO B CB 9010 C CG . PRO B 579 ? 2.2025 1.7661 2.7016 0.3533 0.7470 0.2832 2226 PRO B CG 9011 C CD . PRO B 579 ? 1.9844 1.6696 2.6151 0.3354 0.6956 0.3158 2226 PRO B CD 9012 N N . LYS B 580 ? 2.3209 2.0772 3.0099 0.3192 0.7608 0.3285 2227 LYS B N 9013 C CA . LYS B 580 ? 2.4031 2.2051 3.1486 0.3156 0.7860 0.3493 2227 LYS B CA 9014 C C . LYS B 580 ? 2.0814 1.9847 2.9329 0.2752 0.7176 0.3683 2227 LYS B C 9015 O O . LYS B 580 ? 2.0019 1.9913 2.9933 0.2807 0.7195 0.4187 2227 LYS B O 9016 C CB . LYS B 580 ? 2.7173 2.5280 3.5326 0.3693 0.8716 0.3948 2227 LYS B CB 9017 C CG . LYS B 580 ? 2.8381 2.5226 3.5155 0.4086 0.9507 0.3716 2227 LYS B CG 9018 C CD . LYS B 580 ? 2.8851 2.4848 3.4081 0.3777 0.9408 0.3203 2227 LYS B CD 9019 C CE . LYS B 580 ? 2.6636 2.3043 3.2195 0.3632 0.9566 0.3350 2227 LYS B CE 9020 N NZ . LYS B 580 ? 2.7206 2.3369 3.2905 0.4149 1.0548 0.3699 2227 LYS B NZ 9021 N N . GLU B 581 ? 1.8109 1.6966 2.5906 0.2344 0.6566 0.3288 2228 GLU B N 9022 C CA . GLU B 581 ? 1.6717 1.6198 2.5061 0.1931 0.5892 0.3336 2228 GLU B CA 9023 C C . GLU B 581 ? 1.7048 1.6256 2.4725 0.1679 0.5888 0.3050 2228 GLU B C 9024 O O . GLU B 581 ? 1.7957 1.6498 2.4716 0.1810 0.6323 0.2815 2228 GLU B O 9025 C CB . GLU B 581 ? 1.5497 1.4885 2.3443 0.1734 0.5273 0.3126 2228 GLU B CB 9026 C CG . GLU B 581 ? 1.5387 1.5411 2.4102 0.1434 0.4584 0.3342 2228 GLU B CG 9027 C CD . GLU B 581 ? 1.5597 1.6330 2.5686 0.1595 0.4523 0.3913 2228 GLU B CD 9028 O OE1 . GLU B 581 ? 1.6403 1.7328 2.7154 0.1960 0.5133 0.4229 2228 GLU B OE1 9029 O OE2 . GLU B 581 ? 1.5102 1.6176 2.5601 0.1363 0.3853 0.4074 2228 GLU B OE2 9030 N N . TRP B 582 ? 1.7081 1.6712 2.5151 0.1320 0.5383 0.3082 2229 TRP B N 9031 C CA . TRP B 582 ? 1.7808 1.7231 2.5388 0.1087 0.5362 0.2876 2229 TRP B CA 9032 C C . TRP B 582 ? 1.6930 1.6575 2.4631 0.0680 0.4687 0.2797 2229 TRP B C 9033 O O . TRP B 582 ? 1.7807 1.7827 2.6087 0.0538 0.4202 0.2965 2229 TRP B O 9034 C CB . TRP B 582 ? 1.8820 1.8424 2.6923 0.1233 0.5935 0.3187 2229 TRP B CB 9035 C CG . TRP B 582 ? 1.8674 1.9145 2.8344 0.1268 0.5956 0.3770 2229 TRP B CG 9036 C CD1 . TRP B 582 ? 1.9453 2.0242 2.9943 0.1655 0.6481 0.4184 2229 TRP B CD1 9037 C CD2 . TRP B 582 ? 1.8136 1.9245 2.8783 0.0897 0.5416 0.4043 2229 TRP B CD2 9038 N NE1 . TRP B 582 ? 2.0200 2.1915 3.2267 0.1542 0.6290 0.4744 2229 TRP B NE1 9039 C CE2 . TRP B 582 ? 1.8182 2.0077 3.0340 0.1043 0.5597 0.4659 2229 TRP B CE2 9040 C CE3 . TRP B 582 ? 1.7893 1.8927 2.8271 0.0458 0.4790 0.3843 2229 TRP B CE3 9041 C CZ2 . TRP B 582 ? 1.7659 2.0302 3.1108 0.0698 0.5092 0.5096 2229 TRP B CZ2 9042 C CZ3 . TRP B 582 ? 1.6867 1.8500 2.8359 0.0131 0.4314 0.4225 2229 TRP B CZ3 9043 C CH2 . TRP B 582 ? 1.6200 1.8644 2.9227 0.0220 0.4427 0.4850 2229 TRP B CH2 9044 N N . LEU B 583 ? 1.5254 1.4577 2.2332 0.0503 0.4650 0.2549 2230 LEU B N 9045 C CA . LEU B 583 ? 1.4231 1.3625 2.1353 0.0157 0.4110 0.2483 2230 LEU B CA 9046 C C . LEU B 583 ? 1.4368 1.3713 2.1528 0.0071 0.4350 0.2547 2230 LEU B C 9047 O O . LEU B 583 ? 1.3352 1.2350 1.9946 0.0241 0.4819 0.2436 2230 LEU B O 9048 C CB . LEU B 583 ? 1.4720 1.3632 2.0838 0.0062 0.3797 0.2059 2230 LEU B CB 9049 C CG . LEU B 583 ? 1.4423 1.3157 2.0280 -0.0221 0.3357 0.1915 2230 LEU B CG 9050 C CD1 . LEU B 583 ? 1.5171 1.3925 2.1080 -0.0372 0.2804 0.1926 2230 LEU B CD1 9051 C CD2 . LEU B 583 ? 1.4797 1.3042 1.9701 -0.0194 0.3426 0.1557 2230 LEU B CD2 9052 N N . GLN B 584 ? 1.5846 1.5446 2.3575 -0.0218 0.3987 0.2724 2231 GLN B N 9053 C CA . GLN B 584 ? 1.7748 1.7430 2.5808 -0.0315 0.4234 0.2926 2231 GLN B CA 9054 C C . GLN B 584 ? 1.7547 1.6988 2.5383 -0.0656 0.3785 0.2808 2231 GLN B C 9055 O O . GLN B 584 ? 1.5618 1.5169 2.3838 -0.0941 0.3214 0.2892 2231 GLN B O 9056 C CB . GLN B 584 ? 1.9101 1.9480 2.8517 -0.0278 0.4472 0.3493 2231 GLN B CB 9057 C CG . GLN B 584 ? 1.8105 1.8588 2.7893 -0.0300 0.4922 0.3776 2231 GLN B CG 9058 C CD . GLN B 584 ? 1.8550 1.9823 2.9917 -0.0479 0.4830 0.4386 2231 GLN B CD 9059 O OE1 . GLN B 584 ? 1.8008 1.9623 3.0035 -0.0748 0.4179 0.4526 2231 GLN B OE1 9060 N NE2 . GLN B 584 ? 1.9976 2.1522 3.1950 -0.0345 0.5467 0.4787 2231 GLN B NE2 9061 N N . VAL B 585 ? 1.8729 1.7768 2.5899 -0.0616 0.4062 0.2640 2232 VAL B N 9062 C CA . VAL B 585 ? 2.0590 1.9277 2.7402 -0.0857 0.3788 0.2516 2232 VAL B CA 9063 C C . VAL B 585 ? 2.1387 2.0244 2.8755 -0.0950 0.4098 0.2873 2232 VAL B C 9064 O O . VAL B 585 ? 2.1945 2.0746 2.9122 -0.0734 0.4675 0.2963 2232 VAL B O 9065 C CB . VAL B 585 ? 2.0520 1.8632 2.6175 -0.0726 0.3839 0.2096 2232 VAL B CB 9066 C CG1 . VAL B 585 ? 2.0385 1.8397 2.5619 -0.0442 0.4359 0.2050 2232 VAL B CG1 9067 C CG2 . VAL B 585 ? 2.1329 1.9055 2.6614 -0.0879 0.3724 0.2025 2232 VAL B CG2 9068 N N . ASP B 586 ? 2.1266 2.0262 2.9270 -0.1287 0.3708 0.3093 2233 ASP B N 9069 C CA . ASP B 586 ? 2.2213 2.1311 3.0719 -0.1438 0.3938 0.3437 2233 ASP B CA 9070 C C . ASP B 586 ? 2.3088 2.1503 3.0681 -0.1544 0.3791 0.3155 2233 ASP B C 9071 O O . ASP B 586 ? 2.4757 2.2846 3.2198 -0.1810 0.3239 0.3022 2233 ASP B O 9072 C CB . ASP B 586 ? 2.3142 2.2743 3.2916 -0.1807 0.3534 0.3882 2233 ASP B CB 9073 C CG . ASP B 586 ? 2.3969 2.3530 3.4174 -0.2084 0.3584 0.4198 2233 ASP B CG 9074 O OD1 . ASP B 586 ? 2.3790 2.3481 3.4125 -0.1902 0.4248 0.4438 2233 ASP B OD1 9075 O OD2 . ASP B 586 ? 2.3401 2.2701 3.3713 -0.2487 0.2963 0.4203 2233 ASP B OD2 9076 N N . PHE B 587 ? 2.2079 2.0190 2.8985 -0.1327 0.4259 0.3063 2234 PHE B N 9077 C CA . PHE B 587 ? 2.1608 1.9164 2.7884 -0.1437 0.4151 0.2941 2234 PHE B CA 9078 C C . PHE B 587 ? 2.3091 2.0824 3.0214 -0.1757 0.4071 0.3355 2234 PHE B C 9079 O O . PHE B 587 ? 2.3485 2.1731 3.1463 -0.1758 0.4453 0.3790 2234 PHE B O 9080 C CB . PHE B 587 ? 2.0547 1.7764 2.6013 -0.1190 0.4637 0.2876 2234 PHE B CB 9081 C CG . PHE B 587 ? 2.0017 1.7021 2.4670 -0.0934 0.4672 0.2513 2234 PHE B CG 9082 C CD1 . PHE B 587 ? 1.9054 1.5966 2.3448 -0.0940 0.4239 0.2187 2234 PHE B CD1 9083 C CD2 . PHE B 587 ? 2.1450 1.8263 2.5527 -0.0696 0.5144 0.2515 2234 PHE B CD2 9084 C CE1 . PHE B 587 ? 1.8996 1.5767 2.2763 -0.0736 0.4275 0.1913 2234 PHE B CE1 9085 C CE2 . PHE B 587 ? 2.0710 1.7278 2.4054 -0.0522 0.5111 0.2206 2234 PHE B CE2 9086 C CZ . PHE B 587 ? 1.9811 1.6424 2.3093 -0.0554 0.4672 0.1927 2234 PHE B CZ 9087 N N . GLN B 588 ? 2.4167 2.1458 3.1094 -0.2025 0.3588 0.3250 2235 GLN B N 9088 C CA . GLN B 588 ? 2.4678 2.2027 3.2356 -0.2389 0.3448 0.3646 2235 GLN B CA 9089 C C . GLN B 588 ? 2.3177 2.0665 3.1030 -0.2289 0.4105 0.4009 2235 GLN B C 9090 O O . GLN B 588 ? 2.0914 1.8993 2.9807 -0.2371 0.4411 0.4502 2235 GLN B O 9091 C CB . GLN B 588 ? 2.7334 2.3917 3.4449 -0.2638 0.2886 0.3412 2235 GLN B CB 9092 C CG . GLN B 588 ? 2.7849 2.4180 3.4800 -0.2797 0.2233 0.3142 2235 GLN B CG 9093 C CD . GLN B 588 ? 2.7310 2.4104 3.5385 -0.3192 0.1827 0.3517 2235 GLN B CD 9094 O OE1 . GLN B 588 ? 2.7979 2.4351 3.6193 -0.3605 0.1287 0.3611 2235 GLN B OE1 9095 N NE2 . GLN B 588 ? 2.4071 2.1696 3.2956 -0.3074 0.2052 0.3754 2235 GLN B NE2 9096 N N . LYS B 589 ? 2.3337 2.0281 3.0159 -0.2085 0.4340 0.3793 2236 LYS B N 9097 C CA . LYS B 589 ? 2.2165 1.9001 2.8815 -0.1991 0.4917 0.4092 2236 LYS B CA 9098 C C . LYS B 589 ? 1.9861 1.6770 2.5977 -0.1586 0.5525 0.4037 2236 LYS B C 9099 O O . LYS B 589 ? 1.7493 1.4784 2.3870 -0.1427 0.5596 0.3951 2236 LYS B O 9100 C CB . LYS B 589 ? 2.4566 2.0650 3.0354 -0.2050 0.4736 0.3945 2236 LYS B CB 9101 C CG . LYS B 589 ? 2.4402 2.0033 3.0022 -0.2271 0.4053 0.3677 2236 LYS B CG 9102 C CD . LYS B 589 ? 2.4736 2.0446 3.1266 -0.2715 0.3665 0.3955 2236 LYS B CD 9103 C CE . LYS B 589 ? 2.5540 2.1286 3.2615 -0.2942 0.3949 0.4477 2236 LYS B CE 9104 N NZ . LYS B 589 ? 2.6271 2.1213 3.2692 -0.3043 0.3775 0.4429 2236 LYS B NZ 9105 N N . THR B 590 ? 1.9784 1.6230 2.5072 -0.1429 0.5940 0.4094 2237 THR B N 9106 C CA . THR B 590 ? 1.9895 1.6076 2.4263 -0.1075 0.6391 0.3941 2237 THR B CA 9107 C C . THR B 590 ? 2.1466 1.7072 2.4695 -0.1000 0.6005 0.3488 2237 THR B C 9108 O O . THR B 590 ? 2.1823 1.7005 2.4613 -0.1109 0.5762 0.3462 2237 THR B O 9109 C CB . THR B 590 ? 1.9814 1.5701 2.3768 -0.0931 0.7104 0.4301 2237 THR B CB 9110 O OG1 . THR B 590 ? 2.0018 1.6496 2.5227 -0.1044 0.7462 0.4832 2237 THR B OG1 9111 C CG2 . THR B 590 ? 1.9446 1.4983 2.2446 -0.0561 0.7594 0.4153 2237 THR B CG2 9112 N N . MET B 591 ? 2.1648 1.7262 2.4477 -0.0812 0.5949 0.3176 2238 MET B N 9113 C CA . MET B 591 ? 2.1293 1.6504 2.3256 -0.0755 0.5561 0.2800 2238 MET B CA 9114 C C . MET B 591 ? 2.0429 1.5183 2.1340 -0.0538 0.5829 0.2676 2238 MET B C 9115 O O . MET B 591 ? 1.8932 1.3741 1.9818 -0.0375 0.6256 0.2735 2238 MET B O 9116 C CB . MET B 591 ? 2.1003 1.6549 2.3394 -0.0796 0.5090 0.2513 2238 MET B CB 9117 C CG . MET B 591 ? 2.0809 1.6637 2.4048 -0.1026 0.4755 0.2584 2238 MET B CG 9118 S SD . MET B 591 ? 2.3110 1.8459 2.6138 -0.1200 0.4402 0.2593 2238 MET B SD 9119 C CE . MET B 591 ? 2.2065 1.7532 2.5689 -0.1400 0.3882 0.2451 2238 MET B CE 9120 N N . LYS B 592 ? 2.1052 1.5298 2.1085 -0.0543 0.5556 0.2532 2239 LYS B N 9121 C CA . LYS B 592 ? 2.1398 1.5111 2.0343 -0.0422 0.5583 0.2370 2239 LYS B CA 9122 C C . LYS B 592 ? 2.1864 1.5842 2.0979 -0.0414 0.5168 0.2061 2239 LYS B C 9123 O O . LYS B 592 ? 2.2172 1.6367 2.1630 -0.0493 0.4732 0.1962 2239 LYS B O 9124 C CB . LYS B 592 ? 2.1208 1.4277 1.9214 -0.0480 0.5395 0.2441 2239 LYS B CB 9125 C CG . LYS B 592 ? 2.1537 1.3859 1.8222 -0.0419 0.5377 0.2337 2239 LYS B CG 9126 C CD . LYS B 592 ? 2.2613 1.4446 1.8578 -0.0528 0.4937 0.2400 2239 LYS B CD 9127 C CE . LYS B 592 ? 2.4345 1.5440 1.9041 -0.0550 0.4695 0.2278 2239 LYS B CE 9128 N NZ . LYS B 592 ? 2.4569 1.5426 1.8886 -0.0690 0.4048 0.2334 2239 LYS B NZ 9129 N N . VAL B 593 ? 2.1808 1.5727 2.0675 -0.0298 0.5349 0.1933 2240 VAL B N 9130 C CA . VAL B 593 ? 2.0068 1.4242 1.9125 -0.0293 0.5023 0.1681 2240 VAL B CA 9131 C C . VAL B 593 ? 2.0603 1.4191 1.8644 -0.0327 0.4755 0.1543 2240 VAL B C 9132 O O . VAL B 593 ? 2.0261 1.3158 1.7320 -0.0283 0.4987 0.1573 2240 VAL B O 9133 C CB . VAL B 593 ? 1.8791 1.3339 1.8406 -0.0170 0.5327 0.1660 2240 VAL B CB 9134 C CG1 . VAL B 593 ? 1.7690 1.2523 1.7559 -0.0174 0.5002 0.1432 2240 VAL B CG1 9135 C CG2 . VAL B 593 ? 1.6400 1.1519 1.7061 -0.0200 0.5501 0.1878 2240 VAL B CG2 9136 N N . THR B 594 ? 2.1475 1.5289 1.9733 -0.0413 0.4265 0.1432 2241 THR B N 9137 C CA . THR B 594 ? 2.3809 1.7259 2.1418 -0.0500 0.3902 0.1337 2241 THR B CA 9138 C C . THR B 594 ? 2.3087 1.6613 2.0752 -0.0459 0.3966 0.1169 2241 THR B C 9139 O O . THR B 594 ? 2.3594 1.6502 2.0407 -0.0493 0.3960 0.1096 2241 THR B O 9140 C CB . THR B 594 ? 2.4925 1.8706 2.2961 -0.0588 0.3384 0.1381 2241 THR B CB 9141 O OG1 . THR B 594 ? 2.6400 1.9842 2.4026 -0.0648 0.3223 0.1557 2241 THR B OG1 9142 C CG2 . THR B 594 ? 2.1389 1.5177 1.9326 -0.0696 0.2986 0.1316 2241 THR B CG2 9143 N N . GLY B 595 ? 2.1124 1.5316 1.9709 -0.0394 0.4001 0.1110 2242 GLY B N 9144 C CA . GLY B 595 ? 2.0347 1.4674 1.9093 -0.0341 0.4067 0.0981 2242 GLY B CA 9145 C C . GLY B 595 ? 1.8557 1.3588 1.8259 -0.0290 0.4022 0.0947 2242 GLY B C 9146 O O . GLY B 595 ? 1.7310 1.2650 1.7502 -0.0289 0.3989 0.1010 2242 GLY B O 9147 N N . VAL B 596 ? 1.6957 1.2132 1.6812 -0.0258 0.3998 0.0849 2243 VAL B N 9148 C CA . VAL B 596 ? 1.5821 1.1534 1.6393 -0.0200 0.3969 0.0813 2243 VAL B CA 9149 C C . VAL B 596 ? 1.6606 1.2473 1.7271 -0.0237 0.3722 0.0746 2243 VAL B C 9150 O O . VAL B 596 ? 1.7298 1.2873 1.7560 -0.0303 0.3648 0.0718 2243 VAL B O 9151 C CB . VAL B 596 ? 1.5379 1.1173 1.6162 -0.0084 0.4272 0.0831 2243 VAL B CB 9152 C CG1 . VAL B 596 ? 1.5488 1.1584 1.6822 -0.0063 0.4412 0.0963 2243 VAL B CG1 9153 C CG2 . VAL B 596 ? 1.5686 1.0907 1.5776 -0.0022 0.4541 0.0826 2243 VAL B CG2 9154 N N . THR B 597 ? 1.6464 1.2717 1.7608 -0.0199 0.3605 0.0737 2244 THR B N 9155 C CA . THR B 597 ? 1.6048 1.2518 1.7384 -0.0186 0.3473 0.0721 2244 THR B CA 9156 C C . THR B 597 ? 1.6121 1.2760 1.7675 -0.0104 0.3587 0.0662 2244 THR B C 9157 O O . THR B 597 ? 1.5520 1.2267 1.7287 -0.0063 0.3621 0.0654 2244 THR B O 9158 C CB . THR B 597 ? 1.5682 1.2366 1.7301 -0.0126 0.3357 0.0769 2244 THR B CB 9159 O OG1 . THR B 597 ? 1.6400 1.2949 1.7961 -0.0131 0.3341 0.0803 2244 THR B OG1 9160 C CG2 . THR B 597 ? 1.4705 1.1525 1.6453 -0.0162 0.3200 0.0889 2244 THR B CG2 9161 N N . THR B 598 ? 1.5926 1.2545 1.7416 -0.0107 0.3605 0.0647 2245 THR B N 9162 C CA . THR B 598 ? 1.5636 1.2403 1.7320 -0.0022 0.3679 0.0626 2245 THR B CA 9163 C C . THR B 598 ? 1.5271 1.2215 1.7066 0.0012 0.3605 0.0638 2245 THR B C 9164 O O . THR B 598 ? 1.4104 1.1117 1.5933 -0.0024 0.3536 0.0691 2245 THR B O 9165 C CB . THR B 598 ? 1.4845 1.1412 1.6399 0.0019 0.3851 0.0631 2245 THR B CB 9166 O OG1 . THR B 598 ? 1.5040 1.1296 1.6234 -0.0054 0.3824 0.0612 2245 THR B OG1 9167 C CG2 . THR B 598 ? 1.4146 1.0573 1.5649 0.0053 0.4041 0.0670 2245 THR B CG2 9168 N N . GLN B 599 ? 1.6009 1.3036 1.7888 0.0087 0.3628 0.0632 2246 GLN B N 9169 C CA . GLN B 599 ? 1.5564 1.2684 1.7433 0.0153 0.3610 0.0653 2246 GLN B CA 9170 C C . GLN B 599 ? 1.6316 1.3423 1.8160 0.0204 0.3618 0.0679 2246 GLN B C 9171 O O . GLN B 599 ? 1.6885 1.3973 1.8833 0.0213 0.3628 0.0695 2246 GLN B O 9172 C CB . GLN B 599 ? 1.4678 1.1778 1.6482 0.0226 0.3566 0.0609 2246 GLN B CB 9173 C CG . GLN B 599 ? 1.5909 1.2995 1.7572 0.0349 0.3650 0.0644 2246 GLN B CG 9174 C CD . GLN B 599 ? 1.6863 1.3893 1.8499 0.0447 0.3706 0.0643 2246 GLN B CD 9175 O OE1 . GLN B 599 ? 1.7837 1.4909 1.9632 0.0388 0.3653 0.0648 2246 GLN B OE1 9176 N NE2 . GLN B 599 ? 1.7215 1.4087 1.8594 0.0627 0.3845 0.0652 2246 GLN B NE2 9177 N N . GLY B 600 ? 1.5152 1.2271 1.6883 0.0261 0.3646 0.0725 2247 GLY B N 9178 C CA . GLY B 600 ? 1.5317 1.2378 1.6938 0.0319 0.3622 0.0771 2247 GLY B CA 9179 C C . GLY B 600 ? 1.6227 1.3154 1.7524 0.0408 0.3561 0.0746 2247 GLY B C 9180 O O . GLY B 600 ? 1.7034 1.3869 1.8219 0.0419 0.3506 0.0661 2247 GLY B O 9181 N N . VAL B 601 ? 1.6301 1.3110 1.7342 0.0471 0.3567 0.0819 2248 VAL B N 9182 C CA . VAL B 601 ? 1.6205 1.2698 1.6674 0.0572 0.3531 0.0798 2248 VAL B CA 9183 C C . VAL B 601 ? 1.7159 1.3552 1.7356 0.0653 0.3677 0.0932 2248 VAL B C 9184 O O . VAL B 601 ? 1.8210 1.4758 1.8689 0.0603 0.3699 0.1036 2248 VAL B O 9185 C CB . VAL B 601 ? 1.5591 1.1869 1.5842 0.0518 0.3185 0.0758 2248 VAL B CB 9186 C CG1 . VAL B 601 ? 1.6959 1.3025 1.7028 0.0480 0.3058 0.0621 2248 VAL B CG1 9187 C CG2 . VAL B 601 ? 1.4455 1.1027 1.5272 0.0432 0.3030 0.0850 2248 VAL B CG2 9188 N N . LYS B 602 ? 1.7589 1.3644 1.7171 0.0794 0.3808 0.0938 2249 LYS B N 9189 C CA . LYS B 602 ? 2.0338 1.6190 1.9507 0.0876 0.3922 0.1084 2249 LYS B CA 9190 C C . LYS B 602 ? 2.2358 1.7664 2.0723 0.0904 0.3633 0.1019 2249 LYS B C 9191 O O . LYS B 602 ? 2.4147 1.9081 2.2044 0.0925 0.3509 0.0864 2249 LYS B O 9192 C CB . LYS B 602 ? 2.3212 1.9077 2.2279 0.1033 0.4374 0.1222 2249 LYS B CB 9193 C CG . LYS B 602 ? 2.7717 2.3250 2.6169 0.1155 0.4559 0.1390 2249 LYS B CG 9194 C CD . LYS B 602 ? 2.7275 2.3177 2.6249 0.1134 0.4878 0.1666 2249 LYS B CD 9195 C CE . LYS B 602 ? 2.7193 2.2734 2.5546 0.1215 0.4989 0.1843 2249 LYS B CE 9196 N NZ . LYS B 602 ? 2.5168 2.0963 2.4034 0.1048 0.4930 0.2030 2249 LYS B NZ 9197 N N . SER B 603 ? 2.3251 1.8445 2.1422 0.0883 0.3478 0.1150 2250 SER B N 9198 C CA . SER B 603 ? 2.5024 1.9692 2.2448 0.0858 0.3076 0.1132 2250 SER B CA 9199 C C . SER B 603 ? 2.4930 1.9041 2.1386 0.0989 0.3188 0.1255 2250 SER B C 9200 O O . SER B 603 ? 2.2001 1.5724 1.7908 0.0936 0.2790 0.1325 2250 SER B O 9201 C CB . SER B 603 ? 2.6175 2.1167 2.4231 0.0704 0.2647 0.1218 2250 SER B CB 9202 O OG . SER B 603 ? 2.8603 2.3237 2.6251 0.0589 0.2149 0.1168 2250 SER B OG 9203 N N . LEU B 604 ? 2.6214 2.0295 2.2488 0.1160 0.3728 0.1320 2251 LEU B N 9204 C CA . LEU B 604 ? 2.7969 2.1618 2.3455 0.1316 0.4008 0.1503 2251 LEU B CA 9205 C C . LEU B 604 ? 2.6415 2.0365 2.2371 0.1212 0.3859 0.1724 2251 LEU B C 9206 O O . LEU B 604 ? 2.1620 1.5601 1.7559 0.1281 0.4202 0.1953 2251 LEU B O 9207 C CB . LEU B 604 ? 2.9120 2.1758 2.3108 0.1417 0.3833 0.1396 2251 LEU B CB 9208 C CG . LEU B 604 ? 2.7190 1.9092 2.0156 0.1622 0.4105 0.1207 2251 LEU B CG 9209 C CD1 . LEU B 604 ? 2.5524 1.7018 1.7737 0.1946 0.4817 0.1377 2251 LEU B CD1 9210 C CD2 . LEU B 604 ? 2.5265 1.7532 1.8931 0.1598 0.4154 0.1014 2251 LEU B CD2 9211 N N . LEU B 605 ? 2.5472 1.9644 2.1909 0.1056 0.3367 0.1684 2252 LEU B N 9212 C CA . LEU B 605 ? 2.5960 2.0552 2.3177 0.0981 0.3283 0.1846 2252 LEU B CA 9213 C C . LEU B 605 ? 2.5511 2.0553 2.3451 0.0964 0.3715 0.1879 2252 LEU B C 9214 O O . LEU B 605 ? 2.2903 1.7882 2.0653 0.1032 0.4110 0.2020 2252 LEU B O 9215 C CB . LEU B 605 ? 2.5980 2.0900 2.3881 0.0864 0.2853 0.1779 2252 LEU B CB 9216 C CG . LEU B 605 ? 2.7731 2.2495 2.5506 0.0821 0.2320 0.1925 2252 LEU B CG 9217 C CD1 . LEU B 605 ? 2.6241 2.1544 2.5066 0.0744 0.2076 0.1946 2252 LEU B CD1 9218 C CD2 . LEU B 605 ? 2.8598 2.3168 2.6122 0.0902 0.2340 0.2187 2252 LEU B CD2 9219 N N . THR B 606 ? 2.4711 2.0179 2.3470 0.0860 0.3622 0.1778 2253 THR B N 9220 C CA . THR B 606 ? 2.4790 2.0603 2.4191 0.0782 0.3889 0.1787 2253 THR B CA 9221 C C . THR B 606 ? 2.1766 1.7836 2.1551 0.0724 0.3834 0.1576 2253 THR B C 9222 O O . THR B 606 ? 1.9671 1.5676 1.9309 0.0735 0.3596 0.1444 2253 THR B O 9223 C CB . THR B 606 ? 2.6627 2.2509 2.6495 0.0713 0.3835 0.1892 2253 THR B CB 9224 O OG1 . THR B 606 ? 2.7717 2.3364 2.7313 0.0792 0.3632 0.2031 2253 THR B OG1 9225 C CG2 . THR B 606 ? 2.5347 2.1277 2.5457 0.0610 0.4111 0.2039 2253 THR B CG2 9226 N N . SER B 607 ? 1.9723 1.6051 1.9983 0.0634 0.4019 0.1579 2254 SER B N 9227 C CA . SER B 607 ? 1.7639 1.4195 1.8314 0.0549 0.3965 0.1420 2254 SER B CA 9228 C C . SER B 607 ? 1.7606 1.4163 1.8526 0.0516 0.3773 0.1348 2254 SER B C 9229 O O . SER B 607 ? 1.8922 1.5369 1.9939 0.0507 0.3778 0.1440 2254 SER B O 9230 C CB . SER B 607 ? 1.6424 1.3162 1.7504 0.0413 0.4112 0.1505 2254 SER B CB 9231 O OG . SER B 607 ? 1.6696 1.3565 1.7786 0.0457 0.4344 0.1650 2254 SER B OG 9232 N N . MET B 608 ? 1.6034 1.2693 1.7076 0.0514 0.3646 0.1210 2255 MET B N 9233 C CA . MET B 608 ? 1.4837 1.1564 1.6223 0.0512 0.3561 0.1186 2255 MET B CA 9234 C C . MET B 608 ? 1.4797 1.1626 1.6362 0.0434 0.3634 0.1057 2255 MET B C 9235 O O . MET B 608 ? 1.5737 1.2637 1.7215 0.0411 0.3613 0.0978 2255 MET B O 9236 C CB . MET B 608 ? 1.5234 1.2021 1.6667 0.0555 0.3310 0.1215 2255 MET B CB 9237 C CG . MET B 608 ? 1.7937 1.4522 1.8919 0.0600 0.3146 0.1311 2255 MET B CG 9238 S SD . MET B 608 ? 2.1554 1.8113 2.2509 0.0567 0.2687 0.1383 2255 MET B SD 9239 C CE . MET B 608 ? 2.3265 1.9461 2.3580 0.0637 0.2547 0.1549 2255 MET B CE 9240 N N . TYR B 609 ? 1.4554 1.1292 1.6266 0.0407 0.3731 0.1040 2256 TYR B N 9241 C CA . TYR B 609 ? 1.5068 1.1818 1.6845 0.0337 0.3776 0.0930 2256 TYR B CA 9242 C C . TYR B 609 ? 1.5457 1.1997 1.7271 0.0389 0.3906 0.0921 2256 TYR B C 9243 O O . TYR B 609 ? 1.5857 1.2189 1.7643 0.0478 0.3989 0.0994 2256 TYR B O 9244 C CB . TYR B 609 ? 1.4869 1.1587 1.6540 0.0199 0.3785 0.0904 2256 TYR B CB 9245 C CG . TYR B 609 ? 1.5553 1.2065 1.7126 0.0101 0.3808 0.0990 2256 TYR B CG 9246 C CD1 . TYR B 609 ? 1.7048 1.3672 1.8649 0.0100 0.3831 0.1122 2256 TYR B CD1 9247 C CD2 . TYR B 609 ? 1.7068 1.3193 1.8450 -0.0007 0.3807 0.0952 2256 TYR B CD2 9248 C CE1 . TYR B 609 ? 1.8054 1.4509 1.9648 -0.0032 0.3838 0.1247 2256 TYR B CE1 9249 C CE2 . TYR B 609 ? 1.9113 1.4959 2.0377 -0.0157 0.3761 0.1040 2256 TYR B CE2 9250 C CZ . TYR B 609 ? 1.8878 1.4944 2.0328 -0.0182 0.3769 0.1204 2256 TYR B CZ 9251 O OH . TYR B 609 ? 1.9710 1.5523 2.1127 -0.0365 0.3714 0.1336 2256 TYR B OH 9252 N N . VAL B 610 ? 1.5257 1.1785 1.7080 0.0363 0.3964 0.0848 2257 VAL B N 9253 C CA . VAL B 610 ? 1.6194 1.2397 1.7899 0.0452 0.4181 0.0844 2257 VAL B CA 9254 C C . VAL B 610 ? 1.7386 1.3093 1.8561 0.0313 0.4190 0.0744 2257 VAL B C 9255 O O . VAL B 610 ? 1.8040 1.3800 1.9108 0.0149 0.4047 0.0689 2257 VAL B O 9256 C CB . VAL B 610 ? 1.5824 1.2207 1.7789 0.0524 0.4298 0.0873 2257 VAL B CB 9257 C CG1 . VAL B 610 ? 1.4746 1.0699 1.6488 0.0680 0.4638 0.0895 2257 VAL B CG1 9258 C CG2 . VAL B 610 ? 1.6160 1.3024 1.8714 0.0595 0.4183 0.1017 2257 VAL B CG2 9259 N N . LYS B 611 ? 1.8285 1.3460 1.9119 0.0375 0.4327 0.0741 2258 LYS B N 9260 C CA . LYS B 611 ? 2.1603 1.6124 2.1807 0.0196 0.4256 0.0653 2258 LYS B CA 9261 C C . LYS B 611 ? 2.2224 1.6263 2.1907 0.0216 0.4399 0.0554 2258 LYS B C 9262 O O . LYS B 611 ? 2.3268 1.7021 2.2532 -0.0010 0.4196 0.0486 2258 LYS B O 9263 C CB . LYS B 611 ? 2.4976 1.8937 2.4883 0.0260 0.4345 0.0678 2258 LYS B CB 9264 C CG . LYS B 611 ? 2.8192 2.1745 2.7762 -0.0034 0.4085 0.0678 2258 LYS B CG 9265 C CD . LYS B 611 ? 3.1055 2.3979 2.9958 -0.0292 0.3900 0.0569 2258 LYS B CD 9266 C CE . LYS B 611 ? 2.9036 2.2544 2.8312 -0.0540 0.3597 0.0628 2258 LYS B CE 9267 N NZ . LYS B 611 ? 2.5878 1.8888 2.4558 -0.0725 0.3420 0.0541 2258 LYS B NZ 9268 N N . GLU B 612 ? 2.1812 1.5762 2.1538 0.0493 0.4754 0.0586 2259 GLU B N 9269 C CA . GLU B 612 ? 2.2251 1.5571 2.1331 0.0585 0.5026 0.0518 2259 GLU B CA 9270 C C . GLU B 612 ? 2.1178 1.4987 2.0835 0.0834 0.5353 0.0653 2259 GLU B C 9271 O O . GLU B 612 ? 2.1503 1.5822 2.1888 0.1017 0.5459 0.0808 2259 GLU B O 9272 C CB . GLU B 612 ? 2.3720 1.6027 2.2004 0.0732 0.5280 0.0454 2259 GLU B CB 9273 C CG . GLU B 612 ? 2.5412 1.6952 2.2900 0.0423 0.4935 0.0320 2259 GLU B CG 9274 C CD . GLU B 612 ? 2.7675 1.7992 2.4185 0.0575 0.5196 0.0227 2259 GLU B CD 9275 O OE1 . GLU B 612 ? 2.7066 1.7315 2.3769 0.0968 0.5655 0.0309 2259 GLU B OE1 9276 O OE2 . GLU B 612 ? 3.0316 1.9693 2.5856 0.0298 0.4923 0.0092 2259 GLU B OE2 9277 N N . PHE B 613 ? 2.1184 1.4829 2.0540 0.0830 0.5498 0.0636 2260 PHE B N 9278 C CA . PHE B 613 ? 2.1271 1.5444 2.1303 0.1029 0.5806 0.0822 2260 PHE B CA 9279 C C . PHE B 613 ? 2.2602 1.6282 2.2074 0.1142 0.6197 0.0846 2260 PHE B C 9280 O O . PHE B 613 ? 2.3151 1.6051 2.1589 0.1017 0.6139 0.0682 2260 PHE B O 9281 C CB . PHE B 613 ? 2.0113 1.5191 2.0979 0.0850 0.5454 0.0886 2260 PHE B CB 9282 C CG . PHE B 613 ? 1.9104 1.4138 1.9629 0.0598 0.5174 0.0768 2260 PHE B CG 9283 C CD1 . PHE B 613 ? 1.9030 1.3990 1.9291 0.0378 0.4790 0.0638 2260 PHE B CD1 9284 C CD2 . PHE B 613 ? 1.8683 1.3796 1.9248 0.0589 0.5303 0.0837 2260 PHE B CD2 9285 C CE1 . PHE B 613 ? 1.8935 1.3927 1.9022 0.0179 0.4531 0.0589 2260 PHE B CE1 9286 C CE2 . PHE B 613 ? 1.9657 1.4725 1.9941 0.0378 0.5030 0.0758 2260 PHE B CE2 9287 C CZ . PHE B 613 ? 1.9209 1.4232 1.9278 0.0186 0.4639 0.0638 2260 PHE B CZ 9288 N N . LEU B 614 ? 2.2580 1.6736 2.2779 0.1362 0.6573 0.1090 2261 LEU B N 9289 C CA . LEU B 614 ? 2.1846 1.5627 2.1661 0.1527 0.7067 0.1195 2261 LEU B CA 9290 C C . LEU B 614 ? 2.2022 1.6568 2.2670 0.1433 0.7044 0.1397 2261 LEU B C 9291 O O . LEU B 614 ? 2.2079 1.7513 2.3870 0.1381 0.6844 0.1570 2261 LEU B O 9292 C CB . LEU B 614 ? 2.0347 1.3831 2.0222 0.1965 0.7740 0.1388 2261 LEU B CB 9293 C CG . LEU B 614 ? 2.1749 1.3890 1.9985 0.1969 0.7832 0.1102 2261 LEU B CG 9294 C CD1 . LEU B 614 ? 2.1144 1.2847 1.9111 0.2055 0.7752 0.0979 2261 LEU B CD1 9295 C CD2 . LEU B 614 ? 2.4101 1.5476 2.1569 0.2292 0.8564 0.1208 2261 LEU B CD2 9296 N N . ILE B 615 ? 2.2111 1.6239 2.2125 0.1391 0.7223 0.1391 2262 ILE B N 9297 C CA . ILE B 615 ? 2.0918 1.5713 2.1734 0.1304 0.7250 0.1623 2262 ILE B CA 9298 C C . ILE B 615 ? 2.2115 1.6845 2.3136 0.1618 0.7987 0.1942 2262 ILE B C 9299 O O . ILE B 615 ? 2.3319 1.7134 2.3230 0.1813 0.8457 0.1896 2262 ILE B O 9300 C CB . ILE B 615 ? 1.9231 1.3825 1.9490 0.1015 0.6903 0.1484 2262 ILE B CB 9301 C CG1 . ILE B 615 ? 1.8206 1.2776 1.8189 0.0762 0.6270 0.1203 2262 ILE B CG1 9302 C CG2 . ILE B 615 ? 1.7726 1.3078 1.8982 0.0886 0.6832 0.1724 2262 ILE B CG2 9303 C CD1 . ILE B 615 ? 1.9459 1.3621 1.8685 0.0539 0.5969 0.1076 2262 ILE B CD1 9304 N N . SER B 616 ? 2.2103 1.7782 2.4548 0.1664 0.8076 0.2293 2263 SER B N 9305 C CA . SER B 616 ? 2.3145 1.9070 2.6164 0.1855 0.8688 0.2702 2263 SER B CA 9306 C C . SER B 616 ? 2.2518 1.8904 2.5991 0.1503 0.8335 0.2790 2263 SER B C 9307 O O . SER B 616 ? 2.0291 1.7112 2.4165 0.1179 0.7648 0.2646 2263 SER B O 9308 C CB . SER B 616 ? 2.3913 2.0654 2.8391 0.2102 0.8977 0.3126 2263 SER B CB 9309 O OG . SER B 616 ? 2.4341 2.1927 2.9871 0.1821 0.8279 0.3151 2263 SER B OG 9310 N N . SER B 617 ? 2.3314 1.9476 2.6580 0.1588 0.8842 0.3020 2264 SER B N 9311 C CA . SER B 617 ? 2.2390 1.9007 2.6255 0.1298 0.8643 0.3219 2264 SER B CA 9312 C C . SER B 617 ? 2.2698 1.9841 2.7651 0.1493 0.9313 0.3797 2264 SER B C 9313 O O . SER B 617 ? 2.3799 2.0696 2.8632 0.1913 1.0056 0.3990 2264 SER B O 9314 C CB . SER B 617 ? 2.2210 1.8014 2.4721 0.1153 0.8548 0.2975 2264 SER B CB 9315 O OG . SER B 617 ? 2.2773 1.7678 2.4113 0.1455 0.9239 0.3008 2264 SER B OG 9316 N N . SER B 618 ? 2.2318 2.0175 2.8379 0.1193 0.9057 0.4097 2265 SER B N 9317 C CA . SER B 618 ? 2.2824 2.1264 3.0066 0.1293 0.9648 0.4723 2265 SER B CA 9318 C C . SER B 618 ? 2.1716 2.0015 2.8774 0.1010 0.9597 0.4838 2265 SER B C 9319 O O . SER B 618 ? 2.2079 1.9616 2.7798 0.0889 0.9360 0.4451 2265 SER B O 9320 C CB . SER B 618 ? 2.2377 2.1994 3.1556 0.1159 0.9338 0.5135 2265 SER B CB 9321 O OG . SER B 618 ? 2.1944 2.2251 3.2488 0.1180 0.9828 0.5816 2265 SER B OG 9322 N N . GLN B 619 ? 2.0049 1.9116 2.8544 0.0889 0.9792 0.5415 2266 GLN B N 9323 C CA . GLN B 619 ? 2.0670 1.9632 2.9131 0.0626 0.9805 0.5609 2266 GLN B CA 9324 C C . GLN B 619 ? 2.1759 2.1803 3.2213 0.0341 0.9667 0.6227 2266 GLN B C 9325 O O . GLN B 619 ? 2.3846 2.4000 3.4648 -0.0083 0.9222 0.6325 2266 GLN B O 9326 C CB . GLN B 619 ? 2.1486 1.9684 2.8838 0.0995 1.0761 0.5749 2266 GLN B CB 9327 C CG . GLN B 619 ? 2.3155 2.0754 2.9598 0.0762 1.0687 0.5701 2266 GLN B CG 9328 C CD . GLN B 619 ? 2.2799 1.9901 2.8234 0.0451 0.9783 0.5101 2266 GLN B CD 9329 O OE1 . GLN B 619 ? 2.2978 1.9371 2.7289 0.0361 0.9731 0.4963 2266 GLN B OE1 9330 N NE2 . GLN B 619 ? 2.1963 1.9435 2.7814 0.0304 0.9088 0.4782 2266 GLN B NE2 9331 N N . ASP B 620 ? 2.2484 2.3307 3.4273 0.0561 0.9996 0.6655 2267 ASP B N 9332 C CA . ASP B 620 ? 2.2378 2.4326 3.6269 0.0336 0.9980 0.7395 2267 ASP B CA 9333 C C . ASP B 620 ? 2.0334 2.3049 3.5449 0.0030 0.9083 0.7420 2267 ASP B C 9334 O O . ASP B 620 ? 1.8839 2.2263 3.5371 -0.0425 0.8555 0.7836 2267 ASP B O 9335 C CB . ASP B 620 ? 2.4878 2.7236 3.9609 0.0850 1.1133 0.8042 2267 ASP B CB 9336 C CG . ASP B 620 ? 2.6023 2.7911 3.9868 0.1456 1.1685 0.7764 2267 ASP B CG 9337 O OD1 . ASP B 620 ? 2.4253 2.5895 3.7475 0.1420 1.1065 0.7223 2267 ASP B OD1 9338 O OD2 . ASP B 620 ? 2.7499 2.9190 4.1216 0.1984 1.2781 0.8103 2267 ASP B OD2 9339 N N . GLY B 621 ? 1.9726 2.2222 3.4224 0.0261 0.8888 0.6992 2268 GLY B N 9340 C CA . GLY B 621 ? 1.9347 2.2414 3.4723 0.0012 0.8044 0.6969 2268 GLY B CA 9341 C C . GLY B 621 ? 1.9939 2.3318 3.5733 0.0481 0.8424 0.7093 2268 GLY B C 9342 O O . GLY B 621 ? 1.9342 2.2614 3.4774 0.0462 0.7871 0.6724 2268 GLY B O 9343 N N . HIS B 622 ? 2.1686 2.5391 3.8190 0.0935 0.9419 0.7626 2269 HIS B N 9344 C CA . HIS B 622 ? 2.3235 2.7260 4.0315 0.1458 0.9914 0.7857 2269 HIS B CA 9345 C C . HIS B 622 ? 2.4274 2.7342 3.9872 0.2117 1.0975 0.7609 2269 HIS B C 9346 O O . HIS B 622 ? 2.3224 2.6215 3.8784 0.2548 1.1267 0.7582 2269 HIS B O 9347 C CB . HIS B 622 ? 2.2619 2.7987 4.2159 0.1495 1.0139 0.8819 2269 HIS B CB 9348 C CG . HIS B 622 ? 2.2901 2.8941 4.3697 0.0915 0.9706 0.9285 2269 HIS B CG 9349 N ND1 . HIS B 622 ? 2.4733 3.1117 4.6339 0.1014 1.0514 0.9900 2269 HIS B ND1 9350 C CD2 . HIS B 622 ? 2.2085 2.8400 4.3358 0.0223 0.8557 0.9224 2269 HIS B CD2 9351 C CE1 . HIS B 622 ? 2.4245 3.1151 4.6881 0.0376 0.9850 1.0216 2269 HIS B CE1 9352 N NE2 . HIS B 622 ? 2.3780 3.0599 4.6179 -0.0114 0.8643 0.9795 2269 HIS B NE2 9353 N N . GLN B 623 ? 2.4617 2.6871 3.8928 0.2188 1.1512 0.7436 2270 GLN B N 9354 C CA . GLN B 623 ? 2.4274 2.5367 3.6861 0.2769 1.2463 0.7164 2270 GLN B CA 9355 C C . GLN B 623 ? 2.3164 2.2955 3.3442 0.2663 1.2089 0.6312 2270 GLN B C 9356 O O . GLN B 623 ? 2.0620 1.9795 2.9817 0.2452 1.2042 0.6091 2270 GLN B O 9357 C CB . GLN B 623 ? 2.6087 2.7028 3.8734 0.3127 1.3621 0.7687 2270 GLN B CB 9358 C CG . GLN B 623 ? 2.8627 2.9054 4.0839 0.3908 1.4769 0.7860 2270 GLN B CG 9359 C CD . GLN B 623 ? 2.9798 2.8707 3.9788 0.4284 1.5644 0.7582 2270 GLN B CD 9360 O OE1 . GLN B 623 ? 2.9761 2.8452 3.9384 0.4149 1.5939 0.7750 2270 GLN B OE1 9361 N NE2 . GLN B 623 ? 3.0189 2.7950 3.8610 0.4749 1.6047 0.7168 2270 GLN B NE2 9362 N N . TRP B 624 ? 2.4144 2.3549 3.3776 0.2836 1.1865 0.5906 2271 TRP B N 9363 C CA . TRP B 624 ? 2.4356 2.2728 3.2144 0.2710 1.1373 0.5150 2271 TRP B CA 9364 C C . TRP B 624 ? 2.6952 2.4010 3.2973 0.3183 1.2145 0.4904 2271 TRP B C 9365 O O . TRP B 624 ? 2.9194 2.6094 3.5347 0.3686 1.2812 0.5095 2271 TRP B O 9366 C CB . TRP B 624 ? 2.2576 2.1325 3.0806 0.2596 1.0657 0.4915 2271 TRP B CB 9367 C CG . TRP B 624 ? 2.0828 2.0700 3.0623 0.2154 0.9881 0.5150 2271 TRP B CG 9368 C CD1 . TRP B 624 ? 2.0433 2.1426 3.2154 0.2163 0.9898 0.5773 2271 TRP B CD1 9369 C CD2 . TRP B 624 ? 1.9504 1.9413 2.9031 0.1629 0.8955 0.4792 2271 TRP B CD2 9370 N NE1 . TRP B 624 ? 1.9114 2.0742 3.1652 0.1625 0.8965 0.5791 2271 TRP B NE1 9371 C CE2 . TRP B 624 ? 1.8889 1.9821 3.0047 0.1319 0.8419 0.5176 2271 TRP B CE2 9372 C CE3 . TRP B 624 ? 1.9352 1.8503 2.7429 0.1399 0.8522 0.4212 2271 TRP B CE3 9373 C CZ2 . TRP B 624 ? 1.8658 1.9717 2.9836 0.0813 0.7512 0.4944 2271 TRP B CZ2 9374 C CZ3 . TRP B 624 ? 1.9482 1.8887 2.7746 0.0944 0.7687 0.4023 2271 TRP B CZ3 9375 C CH2 . TRP B 624 ? 1.8971 1.9246 2.8676 0.0666 0.7207 0.4360 2271 TRP B CH2 9376 N N . THR B 625 ? 2.7495 2.3532 3.1801 0.3026 1.2031 0.4487 2272 THR B N 9377 C CA . THR B 625 ? 2.8961 2.3533 3.1282 0.3367 1.2528 0.4148 2272 THR B CA 9378 C C . THR B 625 ? 2.7931 2.1813 2.8945 0.3034 1.1666 0.3488 2272 THR B C 9379 O O . THR B 625 ? 2.6009 1.9637 2.6326 0.2652 1.1131 0.3238 2272 THR B O 9380 C CB . THR B 625 ? 3.0353 2.4105 3.1628 0.3604 1.3373 0.4349 2272 THR B CB 9381 O OG1 . THR B 625 ? 2.7296 2.1744 2.9354 0.3228 1.3115 0.4598 2272 THR B OG1 9382 C CG2 . THR B 625 ? 2.9599 2.3364 3.1419 0.4262 1.4595 0.4881 2272 THR B CG2 9383 N N . LEU B 626 ? 2.7706 2.1365 2.8553 0.3194 1.1554 0.3274 2273 LEU B N 9384 C CA . LEU B 626 ? 2.6963 2.0188 2.6968 0.2901 1.0760 0.2747 2273 LEU B CA 9385 C C . LEU B 626 ? 2.8256 2.0200 2.6284 0.2708 1.0537 0.2332 2273 LEU B C 9386 O O . LEU B 626 ? 2.9908 2.0826 2.6680 0.2948 1.1147 0.2360 2273 LEU B O 9387 C CB . LEU B 626 ? 2.6173 1.9164 2.6195 0.3212 1.0918 0.2674 2273 LEU B CB 9388 C CG . LEU B 626 ? 2.3577 1.7772 2.5356 0.3232 1.0642 0.2903 2273 LEU B CG 9389 C CD1 . LEU B 626 ? 2.3046 1.8327 2.6588 0.3476 1.1140 0.3526 2273 LEU B CD1 9390 C CD2 . LEU B 626 ? 2.1273 1.4893 2.2566 0.3478 1.0688 0.2714 2273 LEU B CD2 9391 N N . PHE B 627 ? 2.7782 1.9773 2.5540 0.2283 0.9668 0.1987 2274 PHE B N 9392 C CA . PHE B 627 ? 2.7866 1.8811 2.3988 0.2035 0.9303 0.1658 2274 PHE B CA 9393 C C . PHE B 627 ? 2.9094 1.8663 2.3608 0.2180 0.9425 0.1370 2274 PHE B C 9394 O O . PHE B 627 ? 2.8772 1.8303 2.3288 0.2061 0.8987 0.1147 2274 PHE B O 9395 C CB . PHE B 627 ? 2.6492 1.7998 2.2997 0.1565 0.8368 0.1451 2274 PHE B CB 9396 C CG . PHE B 627 ? 2.7657 1.8495 2.3012 0.1287 0.7996 0.1301 2274 PHE B CG 9397 C CD1 . PHE B 627 ? 2.9232 1.9589 2.3925 0.1370 0.8412 0.1471 2274 PHE B CD1 9398 C CD2 . PHE B 627 ? 2.6845 1.7601 2.1878 0.0941 0.7224 0.1047 2274 PHE B CD2 9399 C CE1 . PHE B 627 ? 2.9628 1.9370 2.3268 0.1108 0.8010 0.1368 2274 PHE B CE1 9400 C CE2 . PHE B 627 ? 2.6593 1.6830 2.0728 0.0684 0.6825 0.0976 2274 PHE B CE2 9401 C CZ . PHE B 627 ? 2.7130 1.6840 2.0535 0.0762 0.7187 0.1127 2274 PHE B CZ 9402 N N . PHE B 628 ? 3.1343 1.9699 2.4409 0.2430 1.0029 0.1386 2275 PHE B N 9403 C CA . PHE B 628 ? 3.4369 2.1061 2.5450 0.2487 1.0051 0.1067 2275 PHE B CA 9404 C C . PHE B 628 ? 3.5328 2.1474 2.5345 0.1968 0.9177 0.0797 2275 PHE B C 9405 O O . PHE B 628 ? 3.5190 2.2266 2.6060 0.1660 0.8699 0.0882 2275 PHE B O 9406 C CB . PHE B 628 ? 3.6691 2.2160 2.6479 0.2988 1.1077 0.1198 2275 PHE B CB 9407 C CG . PHE B 628 ? 3.7957 2.3820 2.8725 0.3560 1.1969 0.1486 2275 PHE B CG 9408 C CD1 . PHE B 628 ? 3.8849 2.4029 2.9172 0.3814 1.2128 0.1318 2275 PHE B CD1 9409 C CD2 . PHE B 628 ? 3.7391 2.4300 2.9579 0.3845 1.2649 0.1972 2275 PHE B CD2 9410 C CE1 . PHE B 628 ? 3.7356 2.2914 2.8649 0.4378 1.2952 0.1629 2275 PHE B CE1 9411 C CE2 . PHE B 628 ? 3.6592 2.3955 2.9845 0.4378 1.3451 0.2315 2275 PHE B CE2 9412 C CZ . PHE B 628 ? 3.6644 2.3342 2.9457 0.4666 1.3610 0.2145 2275 PHE B CZ 9413 N N . GLN B 629 ? 3.7215 2.1863 2.5438 0.1860 0.8927 0.0498 2276 GLN B N 9414 C CA . GLN B 629 ? 3.7725 2.1803 2.4942 0.1351 0.8047 0.0303 2276 GLN B CA 9415 C C . GLN B 629 ? 4.1095 2.3229 2.5891 0.1391 0.8230 0.0175 2276 GLN B C 9416 O O . GLN B 629 ? 4.1508 2.3333 2.5598 0.1147 0.7899 0.0217 2276 GLN B O 9417 C CB . GLN B 629 ? 3.7256 2.1463 2.4727 0.0996 0.7247 0.0086 2276 GLN B CB 9418 C CG . GLN B 629 ? 3.9134 2.2511 2.5407 0.0488 0.6363 -0.0074 2276 GLN B CG 9419 C CD . GLN B 629 ? 4.0849 2.4117 2.7198 0.0154 0.5672 -0.0245 2276 GLN B CD 9420 O OE1 . GLN B 629 ? 4.2806 2.6919 3.0031 -0.0246 0.4918 -0.0198 2276 GLN B OE1 9421 N NE2 . GLN B 629 ? 4.0342 2.2552 2.5803 0.0334 0.5960 -0.0413 2276 GLN B NE2 9422 N N . ASN B 630 ? 4.2804 2.3547 2.6255 0.1704 0.8736 0.0019 2277 ASN B N 9423 C CA . ASN B 630 ? 4.3893 2.2504 2.4773 0.1848 0.9081 -0.0123 2277 ASN B CA 9424 C C . ASN B 630 ? 4.3586 2.0979 2.3493 0.2387 0.9941 -0.0224 2277 ASN B C 9425 O O . ASN B 630 ? 4.4383 1.9857 2.2174 0.2342 0.9814 -0.0516 2277 ASN B O 9426 C CB . ASN B 630 ? 4.5991 2.3409 2.5243 0.1252 0.8012 -0.0377 2277 ASN B CB 9427 C CG . ASN B 630 ? 4.4967 2.2638 2.4760 0.0847 0.7153 -0.0571 2277 ASN B CG 9428 O OD1 . ASN B 630 ? 4.3648 2.0996 2.3475 0.1068 0.7448 -0.0692 2277 ASN B OD1 9429 N ND2 . ASN B 630 ? 4.4329 2.2561 2.4559 0.0261 0.6099 -0.0563 2277 ASN B ND2 9430 N N . GLY B 631 ? 4.2270 2.0756 2.3744 0.2897 1.0804 0.0045 2278 GLY B N 9431 C CA . GLY B 631 ? 4.4024 2.1799 2.5203 0.3454 1.1611 0.0024 2278 GLY B CA 9432 C C . GLY B 631 ? 4.2207 2.1469 2.5427 0.3364 1.1233 0.0054 2278 GLY B C 9433 O O . GLY B 631 ? 4.0861 2.0806 2.5291 0.3850 1.1931 0.0280 2278 GLY B O 9434 N N . LYS B 632 ? 4.1516 2.1247 2.5087 0.2743 1.0119 -0.0142 2279 LYS B N 9435 C CA . LYS B 632 ? 3.9651 2.0983 2.5222 0.2538 0.9605 -0.0091 2279 LYS B CA 9436 C C . LYS B 632 ? 3.7285 2.0555 2.5044 0.2708 0.9923 0.0280 2279 LYS B C 9437 O O . LYS B 632 ? 3.7080 2.0714 2.4958 0.2662 1.0040 0.0439 2279 LYS B O 9438 C CB . LYS B 632 ? 3.9288 2.0906 2.4877 0.1836 0.8429 -0.0269 2279 LYS B CB 9439 C CG . LYS B 632 ? 3.9680 2.1056 2.5259 0.1544 0.7800 -0.0471 2279 LYS B CG 9440 C CD . LYS B 632 ? 3.6268 1.9554 2.3978 0.1274 0.7254 -0.0343 2279 LYS B CD 9441 C CE . LYS B 632 ? 3.5402 1.8508 2.2922 0.0716 0.6307 -0.0502 2279 LYS B CE 9442 N NZ . LYS B 632 ? 3.7162 1.9020 2.3709 0.0750 0.6315 -0.0684 2279 LYS B NZ 9443 N N . VAL B 633 ? 3.5076 1.9496 2.4492 0.2885 1.0031 0.0431 2280 VAL B N 9444 C CA . VAL B 633 ? 3.1635 1.7991 2.3242 0.2847 0.9961 0.0741 2280 VAL B CA 9445 C C . VAL B 633 ? 3.0737 1.7914 2.3037 0.2287 0.8935 0.0577 2280 VAL B C 9446 O O . VAL B 633 ? 3.1007 1.8588 2.3973 0.2244 0.8663 0.0528 2280 VAL B O 9447 C CB . VAL B 633 ? 2.9212 1.6376 2.2248 0.3294 1.0502 0.1021 2280 VAL B CB 9448 C CG1 . VAL B 633 ? 2.6446 1.5207 2.1349 0.3366 1.0713 0.1439 2280 VAL B CG1 9449 C CG2 . VAL B 633 ? 3.0502 1.6320 2.2410 0.3883 1.1420 0.1048 2280 VAL B CG2 9450 N N . LYS B 634 ? 3.1691 1.9088 2.3833 0.1891 0.8407 0.0521 2281 LYS B N 9451 C CA . LYS B 634 ? 3.0406 1.8202 2.2785 0.1378 0.7466 0.0346 2281 LYS B CA 9452 C C . LYS B 634 ? 2.8495 1.7491 2.2404 0.1312 0.7160 0.0395 2281 LYS B C 9453 O O . LYS B 634 ? 2.6386 1.6624 2.1724 0.1369 0.7217 0.0598 2281 LYS B O 9454 C CB . LYS B 634 ? 3.0219 1.8365 2.2606 0.1045 0.7022 0.0378 2281 LYS B CB 9455 C CG . LYS B 634 ? 2.8725 1.7359 2.1495 0.0577 0.6132 0.0272 2281 LYS B CG 9456 C CD . LYS B 634 ? 3.0417 1.7881 2.1770 0.0245 0.5584 0.0077 2281 LYS B CD 9457 C CE . LYS B 634 ? 3.2111 1.8443 2.2473 0.0331 0.5707 -0.0099 2281 LYS B CE 9458 N NZ . LYS B 634 ? 2.7875 1.4670 1.9026 0.0235 0.5430 -0.0142 2281 LYS B NZ 9459 N N . VAL B 635 ? 2.8206 1.6710 2.1695 0.1172 0.6821 0.0218 2282 VAL B N 9460 C CA . VAL B 635 ? 2.6336 1.5710 2.0969 0.1103 0.6528 0.0248 2282 VAL B CA 9461 C C . VAL B 635 ? 2.5127 1.5120 2.0204 0.0653 0.5783 0.0195 2282 VAL B C 9462 O O . VAL B 635 ? 2.5455 1.4796 1.9779 0.0349 0.5333 0.0059 2282 VAL B O 9463 C CB . VAL B 635 ? 2.6821 1.5274 2.0761 0.1188 0.6581 0.0120 2282 VAL B CB 9464 C CG1 . VAL B 635 ? 2.5576 1.4448 2.0362 0.1633 0.7119 0.0295 2282 VAL B CG1 9465 C CG2 . VAL B 635 ? 2.9079 1.5809 2.1123 0.1173 0.6688 -0.0082 2282 VAL B CG2 9466 N N . PHE B 636 ? 2.3099 1.4317 1.9418 0.0615 0.5658 0.0330 2283 PHE B N 9467 C CA . PHE B 636 ? 2.1653 1.3430 1.8349 0.0270 0.5087 0.0318 2283 PHE B CA 9468 C C . PHE B 636 ? 2.1852 1.3914 1.8932 0.0076 0.4683 0.0288 2283 PHE B C 9469 O O . PHE B 636 ? 2.1725 1.3914 1.9156 0.0226 0.4834 0.0309 2283 PHE B O 9470 C CB . PHE B 636 ? 2.0285 1.3035 1.7943 0.0312 0.5128 0.0454 2283 PHE B CB 9471 C CG . PHE B 636 ? 2.2127 1.4548 1.9311 0.0381 0.5394 0.0508 2283 PHE B CG 9472 C CD1 . PHE B 636 ? 2.2300 1.4374 1.8862 0.0146 0.5072 0.0466 2283 PHE B CD1 9473 C CD2 . PHE B 636 ? 2.4548 1.6968 2.1897 0.0693 0.5988 0.0645 2283 PHE B CD2 9474 C CE1 . PHE B 636 ? 2.4818 1.6496 2.0822 0.0211 0.5329 0.0533 2283 PHE B CE1 9475 C CE2 . PHE B 636 ? 2.6057 1.8126 2.2923 0.0769 0.6305 0.0733 2283 PHE B CE2 9476 C CZ . PHE B 636 ? 2.6425 1.8086 2.2553 0.0523 0.5971 0.0661 2283 PHE B CZ 9477 N N . GLN B 637 ? 2.2192 1.4338 1.9218 -0.0251 0.4183 0.0281 2284 GLN B N 9478 C CA . GLN B 637 ? 2.1848 1.4213 1.9204 -0.0475 0.3802 0.0308 2284 GLN B CA 9479 C C . GLN B 637 ? 2.1402 1.4886 1.9892 -0.0488 0.3664 0.0424 2284 GLN B C 9480 O O . GLN B 637 ? 2.3070 1.6925 2.1844 -0.0662 0.3367 0.0501 2284 GLN B O 9481 C CB . GLN B 637 ? 2.1298 1.2961 1.7893 -0.0838 0.3332 0.0289 2284 GLN B CB 9482 C CG . GLN B 637 ? 2.4914 1.5368 2.0425 -0.0871 0.3382 0.0159 2284 GLN B CG 9483 C CD . GLN B 637 ? 2.5072 1.5561 2.0881 -0.0616 0.3738 0.0138 2284 GLN B CD 9484 O OE1 . GLN B 637 ? 2.2994 1.4290 1.9741 -0.0625 0.3663 0.0243 2284 GLN B OE1 9485 N NE2 . GLN B 637 ? 2.5656 1.5191 2.0596 -0.0364 0.4148 0.0021 2284 GLN B NE2 9486 N N . GLY B 638 ? 2.1004 1.4938 2.0066 -0.0286 0.3883 0.0453 2285 GLY B N 9487 C CA . GLY B 638 ? 2.0026 1.4846 1.9953 -0.0239 0.3821 0.0538 2285 GLY B CA 9488 C C . GLY B 638 ? 2.0174 1.5316 2.0450 -0.0401 0.3570 0.0628 2285 GLY B C 9489 O O . GLY B 638 ? 2.1699 1.6520 2.1722 -0.0630 0.3337 0.0667 2285 GLY B O 9490 N N . ASN B 639 ? 1.8913 1.4646 1.9748 -0.0289 0.3616 0.0688 2286 ASN B N 9491 C CA . ASN B 639 ? 1.9234 1.5357 2.0452 -0.0379 0.3480 0.0815 2286 ASN B CA 9492 C C . ASN B 639 ? 1.9602 1.5547 2.0795 -0.0491 0.3430 0.0908 2286 ASN B C 9493 O O . ASN B 639 ? 1.8485 1.3903 1.9281 -0.0503 0.3473 0.0847 2286 ASN B O 9494 C CB . ASN B 639 ? 1.9711 1.6308 2.1286 -0.0192 0.3590 0.0829 2286 ASN B CB 9495 C CG . ASN B 639 ? 2.0244 1.6915 2.1826 -0.0086 0.3643 0.0734 2286 ASN B CG 9496 O OD1 . ASN B 639 ? 2.1040 1.7927 2.2771 -0.0071 0.3596 0.0743 2286 ASN B OD1 9497 N ND2 . ASN B 639 ? 1.7750 1.4240 1.9223 0.0000 0.3764 0.0679 2286 ASN B ND2 9498 N N . GLN B 640 ? 1.9450 1.5803 2.1068 -0.0552 0.3380 0.1081 2287 GLN B N 9499 C CA . GLN B 640 ? 1.9558 1.5837 2.1263 -0.0652 0.3371 0.1225 2287 GLN B CA 9500 C C . GLN B 640 ? 2.0371 1.7101 2.2429 -0.0498 0.3555 0.1371 2287 GLN B C 9501 O O . GLN B 640 ? 2.2297 1.9038 2.4504 -0.0592 0.3575 0.1554 2287 GLN B O 9502 C CB . GLN B 640 ? 2.0192 1.6325 2.1983 -0.0989 0.3086 0.1381 2287 GLN B CB 9503 C CG . GLN B 640 ? 2.4731 2.0026 2.5831 -0.1159 0.2925 0.1238 2287 GLN B CG 9504 C CD . GLN B 640 ? 2.8834 2.3854 2.9704 -0.1431 0.2580 0.1249 2287 GLN B CD 9505 O OE1 . GLN B 640 ? 3.2254 2.7727 3.3453 -0.1410 0.2513 0.1307 2287 GLN B OE1 9506 N NE2 . GLN B 640 ? 2.9502 2.3677 2.9715 -0.1690 0.2335 0.1197 2287 GLN B NE2 9507 N N . ASP B 641 ? 2.0172 1.7162 2.2256 -0.0269 0.3691 0.1290 2288 ASP B N 9508 C CA . ASP B 641 ? 1.8158 1.5439 2.0369 -0.0098 0.3878 0.1406 2288 ASP B CA 9509 C C . ASP B 641 ? 1.6876 1.4156 1.8849 0.0118 0.3937 0.1245 2288 ASP B C 9510 O O . ASP B 641 ? 1.7950 1.5155 1.9846 0.0121 0.3841 0.1084 2288 ASP B O 9511 C CB . ASP B 641 ? 1.8427 1.6086 2.1085 -0.0131 0.3928 0.1605 2288 ASP B CB 9512 C CG . ASP B 641 ? 1.8888 1.6599 2.1698 -0.0254 0.3730 0.1556 2288 ASP B CG 9513 O OD1 . ASP B 641 ? 1.8910 1.6395 2.1406 -0.0227 0.3647 0.1330 2288 ASP B OD1 9514 O OD2 . ASP B 641 ? 2.0034 1.8025 2.3319 -0.0390 0.3646 0.1788 2288 ASP B OD2 9515 N N . SER B 642 ? 1.6649 1.3957 1.8457 0.0284 0.4091 0.1305 2289 SER B N 9516 C CA . SER B 642 ? 2.0283 1.7476 2.1772 0.0446 0.4086 0.1157 2289 SER B CA 9517 C C . SER B 642 ? 2.1703 1.9019 2.3369 0.0460 0.4079 0.1093 2289 SER B C 9518 O O . SER B 642 ? 2.3782 2.1014 2.5393 0.0425 0.3929 0.0938 2289 SER B O 9519 C CB . SER B 642 ? 2.4867 2.1886 2.5930 0.0630 0.4266 0.1228 2289 SER B CB 9520 O OG . SER B 642 ? 2.8825 2.6027 3.0083 0.0725 0.4554 0.1415 2289 SER B OG 9521 N N . PHE B 643 ? 2.1687 1.9226 2.3637 0.0515 0.4249 0.1258 2290 PHE B N 9522 C CA . PHE B 643 ? 1.9938 1.7608 2.2123 0.0557 0.4246 0.1253 2290 PHE B CA 9523 C C . PHE B 643 ? 2.0546 1.8341 2.3043 0.0328 0.4004 0.1247 2290 PHE B C 9524 O O . PHE B 643 ? 2.4554 2.2175 2.6883 0.0186 0.3849 0.1128 2290 PHE B O 9525 C CB . PHE B 643 ? 2.0022 1.7946 2.2539 0.0735 0.4534 0.1502 2290 PHE B CB 9526 C CG . PHE B 643 ? 2.1377 1.9635 2.4370 0.0645 0.4650 0.1808 2290 PHE B CG 9527 C CD1 . PHE B 643 ? 1.9723 1.8080 2.2984 0.0333 0.4389 0.1868 2290 PHE B CD1 9528 C CD2 . PHE B 643 ? 2.4738 2.3154 2.7890 0.0880 0.5054 0.2067 2290 PHE B CD2 9529 C CE1 . PHE B 643 ? 2.1495 2.0113 2.5214 0.0204 0.4454 0.2176 2290 PHE B CE1 9530 C CE2 . PHE B 643 ? 2.4281 2.3060 2.7985 0.0779 0.5184 0.2415 2290 PHE B CE2 9531 C CZ . PHE B 643 ? 2.3369 2.2262 2.7389 0.0411 0.4845 0.2472 2290 PHE B CZ 9532 N N . THR B 644 ? 1.7706 1.5750 2.0611 0.0316 0.3986 0.1399 2291 THR B N 9533 C CA . THR B 644 ? 1.7985 1.6074 2.1091 0.0074 0.3707 0.1440 2291 THR B CA 9534 C C . THR B 644 ? 1.7687 1.5449 2.0383 0.0007 0.3561 0.1196 2291 THR B C 9535 O O . THR B 644 ? 1.9450 1.6960 2.1838 -0.0073 0.3525 0.1062 2291 THR B O 9536 C CB . THR B 644 ? 1.9356 1.7482 2.2645 -0.0185 0.3553 0.1592 2291 THR B CB 9537 O OG1 . THR B 644 ? 2.0622 1.9183 2.4585 -0.0244 0.3529 0.1935 2291 THR B OG1 9538 C CG2 . THR B 644 ? 1.8868 1.6604 2.1798 -0.0438 0.3260 0.1460 2291 THR B CG2 9539 N N . PRO B 645 ? 1.6035 1.3798 1.8758 0.0070 0.3523 0.1173 2292 PRO B N 9540 C CA . PRO B 645 ? 1.7053 1.4549 1.9474 -0.0014 0.3404 0.1025 2292 PRO B CA 9541 C C . PRO B 645 ? 1.7367 1.4725 1.9699 -0.0249 0.3178 0.1096 2292 PRO B C 9542 O O . PRO B 645 ? 1.7086 1.4618 1.9711 -0.0336 0.3005 0.1292 2292 PRO B O 9543 C CB . PRO B 645 ? 1.7913 1.5440 2.0425 0.0128 0.3433 0.1038 2292 PRO B CB 9544 C CG . PRO B 645 ? 1.8491 1.6130 2.1114 0.0354 0.3645 0.1075 2292 PRO B CG 9545 C CD . PRO B 645 ? 1.6805 1.4720 1.9732 0.0304 0.3689 0.1257 2292 PRO B CD 9546 N N . VAL B 646 ? 1.8291 1.5287 2.0192 -0.0342 0.3174 0.0960 2293 VAL B N 9547 C CA . VAL B 646 ? 1.8375 1.4982 1.9894 -0.0559 0.2971 0.0978 2293 VAL B CA 9548 C C . VAL B 646 ? 1.6918 1.3131 1.7936 -0.0524 0.3070 0.0840 2293 VAL B C 9549 O O . VAL B 646 ? 1.4612 1.0818 1.5604 -0.0379 0.3311 0.0733 2293 VAL B O 9550 C CB . VAL B 646 ? 2.1560 1.7961 2.2946 -0.0696 0.2915 0.0994 2293 VAL B CB 9551 C CG1 . VAL B 646 ? 2.3148 1.9312 2.4260 -0.0561 0.3169 0.0832 2293 VAL B CG1 9552 C CG2 . VAL B 646 ? 2.4351 2.0270 2.5313 -0.0988 0.2583 0.1055 2293 VAL B CG2 9553 N N . VAL B 647 ? 1.7588 1.3505 1.8263 -0.0661 0.2872 0.0893 2294 VAL B N 9554 C CA . VAL B 647 ? 1.6851 1.2495 1.7153 -0.0608 0.2978 0.0841 2294 VAL B CA 9555 C C . VAL B 647 ? 1.9208 1.4083 1.8602 -0.0741 0.2920 0.0798 2294 VAL B C 9556 O O . VAL B 647 ? 2.0383 1.4949 1.9447 -0.0961 0.2570 0.0871 2294 VAL B O 9557 C CB . VAL B 647 ? 1.4246 1.0197 1.4907 -0.0581 0.2839 0.0967 2294 VAL B CB 9558 C CG1 . VAL B 647 ? 1.3287 0.9407 1.4206 -0.0732 0.2476 0.1170 2294 VAL B CG1 9559 C CG2 . VAL B 647 ? 1.3526 0.9113 1.3729 -0.0580 0.2901 0.0958 2294 VAL B CG2 9560 N N . ASN B 648 ? 2.0352 1.4877 1.9321 -0.0612 0.3260 0.0707 2295 ASN B N 9561 C CA . ASN B 648 ? 2.1436 1.5073 1.9348 -0.0670 0.3320 0.0658 2295 ASN B CA 9562 C C . ASN B 648 ? 2.1431 1.4859 1.9002 -0.0641 0.3410 0.0726 2295 ASN B C 9563 O O . ASN B 648 ? 2.0036 1.3842 1.8072 -0.0483 0.3706 0.0762 2295 ASN B O 9564 C CB . ASN B 648 ? 2.1885 1.5125 1.9437 -0.0490 0.3752 0.0549 2295 ASN B CB 9565 C CG . ASN B 648 ? 2.2391 1.5866 2.0343 -0.0478 0.3721 0.0500 2295 ASN B CG 9566 O OD1 . ASN B 648 ? 2.1661 1.5827 2.0440 -0.0352 0.3836 0.0526 2295 ASN B OD1 9567 N ND2 . ASN B 648 ? 2.3539 1.6357 2.0833 -0.0629 0.3534 0.0437 2295 ASN B ND2 9568 N N . SER B 649 ? 2.2437 1.5210 1.9161 -0.0822 0.3118 0.0765 2296 SER B N 9569 C CA . SER B 649 ? 2.4287 1.6671 2.0442 -0.0810 0.3190 0.0848 2296 SER B CA 9570 C C . SER B 649 ? 2.5859 1.7652 2.1322 -0.0607 0.3773 0.0779 2296 SER B C 9571 O O . SER B 649 ? 2.7788 1.9395 2.3138 -0.0494 0.4034 0.0667 2296 SER B O 9572 C CB . SER B 649 ? 2.4644 1.6367 1.9937 -0.1079 0.2659 0.0924 2296 SER B CB 9573 O OG . SER B 649 ? 2.4388 1.6675 2.0340 -0.1168 0.2281 0.1114 2296 SER B OG 9574 N N . LEU B 650 ? 2.6108 1.7615 2.1156 -0.0533 0.4022 0.0881 2297 LEU B N 9575 C CA . LEU B 650 ? 2.6309 1.7185 2.0636 -0.0309 0.4654 0.0876 2297 LEU B CA 9576 C C . LEU B 650 ? 2.9482 1.9097 2.2151 -0.0359 0.4681 0.0882 2297 LEU B C 9577 O O . LEU B 650 ? 2.8115 1.7545 2.0417 -0.0509 0.4379 0.0998 2297 LEU B O 9578 C CB . LEU B 650 ? 2.3433 1.5038 1.8757 -0.0101 0.5156 0.1026 2297 LEU B CB 9579 C CG . LEU B 650 ? 2.0063 1.2694 1.6779 -0.0044 0.5146 0.1012 2297 LEU B CG 9580 C CD1 . LEU B 650 ? 1.9910 1.3091 1.7476 0.0117 0.5607 0.1201 2297 LEU B CD1 9581 C CD2 . LEU B 650 ? 1.9195 1.1703 1.5841 0.0027 0.5182 0.0862 2297 LEU B CD2 9582 N N . ASP B 651 ? 3.2242 2.0922 2.3862 -0.0219 0.5031 0.0753 2298 ASP B N 9583 C CA . ASP B 651 ? 3.3174 2.0335 2.2876 -0.0222 0.5132 0.0691 2298 ASP B CA 9584 C C . ASP B 651 ? 3.2721 1.9688 2.2012 -0.0160 0.5388 0.0894 2298 ASP B C 9585 O O . ASP B 651 ? 3.1918 1.8863 2.1014 -0.0420 0.4820 0.0978 2298 ASP B O 9586 C CB . ASP B 651 ? 3.6267 2.2593 2.5172 0.0098 0.5805 0.0564 2298 ASP B CB 9587 C CG . ASP B 651 ? 3.7272 2.3068 2.5726 -0.0048 0.5420 0.0328 2298 ASP B CG 9588 O OD1 . ASP B 651 ? 3.6146 2.2914 2.5906 -0.0093 0.5226 0.0299 2298 ASP B OD1 9589 O OD2 . ASP B 651 ? 3.7675 2.1953 2.4347 -0.0111 0.5345 0.0175 2298 ASP B OD2 9590 N N . PRO B 652 ? 3.3849 2.0719 2.3096 0.0188 0.6245 0.1023 2299 PRO B N 9591 C CA . PRO B 652 ? 3.5175 2.2400 2.4749 0.0195 0.6412 0.1281 2299 PRO B CA 9592 C C . PRO B 652 ? 3.3319 2.2120 2.4939 0.0140 0.6255 0.1391 2299 PRO B C 9593 O O . PRO B 652 ? 3.4908 2.4425 2.7599 0.0289 0.6521 0.1371 2299 PRO B O 9594 C CB . PRO B 652 ? 3.6525 2.3178 2.5496 0.0583 0.7421 0.1440 2299 PRO B CB 9595 C CG . PRO B 652 ? 3.6021 2.2023 2.4377 0.0825 0.7803 0.1251 2299 PRO B CG 9596 C CD . PRO B 652 ? 3.4570 2.1045 2.3554 0.0582 0.7084 0.1009 2299 PRO B CD 9597 N N . PRO B 653 ? 3.0201 1.9455 2.2290 -0.0074 0.5785 0.1502 2300 PRO B N 9598 C CA . PRO B 653 ? 2.6957 1.7465 2.0747 -0.0101 0.5709 0.1607 2300 PRO B CA 9599 C C . PRO B 653 ? 2.5473 1.6405 2.0003 0.0118 0.6431 0.1819 2300 PRO B C 9600 O O . PRO B 653 ? 2.6155 1.6532 1.9998 0.0246 0.6947 0.2009 2300 PRO B O 9601 C CB . PRO B 653 ? 2.7510 1.8025 2.1228 -0.0294 0.5256 0.1735 2300 PRO B CB 9602 C CG . PRO B 653 ? 2.9400 1.9095 2.1897 -0.0464 0.4727 0.1618 2300 PRO B CG 9603 C CD . PRO B 653 ? 3.0329 1.8970 2.1462 -0.0325 0.5167 0.1513 2300 PRO B CD 9604 N N . LEU B 654 ? 2.4050 1.5945 1.9970 0.0152 0.6456 0.1821 2301 LEU B N 9605 C CA . LEU B 654 ? 2.5946 1.8306 2.2708 0.0354 0.7089 0.2047 2301 LEU B CA 9606 C C . LEU B 654 ? 2.8028 2.1088 2.5895 0.0245 0.7129 0.2331 2301 LEU B C 9607 O O . LEU B 654 ? 3.1228 2.5028 3.0147 0.0089 0.6709 0.2288 2301 LEU B O 9608 C CB . LEU B 654 ? 2.4731 1.7693 2.2360 0.0430 0.7027 0.1921 2301 LEU B CB 9609 C CG . LEU B 654 ? 2.5714 1.9008 2.4033 0.0706 0.7665 0.2125 2301 LEU B CG 9610 C CD1 . LEU B 654 ? 2.3938 1.8070 2.3415 0.0656 0.7326 0.2041 2301 LEU B CD1 9611 C CD2 . LEU B 654 ? 2.5295 1.8950 2.4322 0.0785 0.8200 0.2546 2301 LEU B CD2 9612 N N . LEU B 655 ? 2.7891 2.0656 2.5480 0.0321 0.7640 0.2631 2302 LEU B N 9613 C CA . LEU B 655 ? 2.5577 1.8970 2.4267 0.0184 0.7707 0.2960 2302 LEU B CA 9614 C C . LEU B 655 ? 2.4370 1.8628 2.4498 0.0270 0.8031 0.3191 2302 LEU B C 9615 O O . LEU B 655 ? 2.4264 1.8418 2.4302 0.0553 0.8617 0.3295 2302 LEU B O 9616 C CB . LEU B 655 ? 2.5432 1.8232 2.3386 0.0219 0.8158 0.3260 2302 LEU B CB 9617 C CG . LEU B 655 ? 2.5204 1.7030 2.1609 0.0146 0.7900 0.3142 2302 LEU B CG 9618 C CD1 . LEU B 655 ? 2.6240 1.7475 2.1934 0.0235 0.8504 0.3501 2302 LEU B CD1 9619 C CD2 . LEU B 655 ? 2.3994 1.6077 2.0728 -0.0126 0.7114 0.3012 2302 LEU B CD2 9620 N N . THR B 656 ? 2.3125 1.8164 2.4525 0.0032 0.7625 0.3279 2303 THR B N 9621 C CA . THR B 656 ? 2.1219 1.7130 2.4059 0.0037 0.7700 0.3483 2303 THR B CA 9622 C C . THR B 656 ? 2.0552 1.7144 2.4619 -0.0300 0.7134 0.3578 2303 THR B C 9623 O O . THR B 656 ? 1.9080 1.5479 2.2939 -0.0532 0.6670 0.3453 2303 THR B O 9624 C CB . THR B 656 ? 1.9783 1.5770 2.2546 0.0240 0.7679 0.3230 2303 THR B CB 9625 O OG1 . THR B 656 ? 1.8051 1.4868 2.2215 0.0271 0.7785 0.3509 2303 THR B OG1 9626 C CG2 . THR B 656 ? 1.8946 1.4814 2.1276 0.0093 0.6962 0.2773 2303 THR B CG2 9627 N N . ARG B 657 ? 2.0573 1.7894 2.5870 -0.0309 0.7175 0.3813 2304 ARG B N 9628 C CA . ARG B 657 ? 2.1346 1.9272 2.7836 -0.0641 0.6653 0.3969 2304 ARG B CA 9629 C C . ARG B 657 ? 2.0054 1.8415 2.7050 -0.0576 0.6388 0.3837 2304 ARG B C 9630 O O . ARG B 657 ? 1.9394 1.8016 2.6893 -0.0827 0.5765 0.3748 2304 ARG B O 9631 C CB . ARG B 657 ? 2.3441 2.1902 3.1129 -0.0733 0.7054 0.4589 2304 ARG B CB 9632 C CG . ARG B 657 ? 2.3709 2.2586 3.2489 -0.1188 0.6481 0.4827 2304 ARG B CG 9633 C CD . ARG B 657 ? 2.2114 2.1779 3.2220 -0.1305 0.6172 0.5050 2304 ARG B CD 9634 N NE . ARG B 657 ? 2.2170 2.2439 3.3733 -0.1648 0.6077 0.5645 2304 ARG B NE 9635 C CZ . ARG B 657 ? 2.1794 2.2116 3.3885 -0.2126 0.5303 0.5681 2304 ARG B CZ 9636 N NH1 . ARG B 657 ? 2.1470 2.1237 3.2675 -0.2262 0.4623 0.5138 2304 ARG B NH1 9637 N NH2 . ARG B 657 ? 2.1061 2.1939 3.4549 -0.2471 0.5218 0.6286 2304 ARG B NH2 9638 N N . TYR B 658 ? 1.9646 1.7973 2.6390 -0.0226 0.6876 0.3825 2305 TYR B N 9639 C CA . TYR B 658 ? 1.9921 1.8642 2.7154 -0.0115 0.6718 0.3762 2305 TYR B CA 9640 C C . TYR B 658 ? 2.0845 1.8998 2.6900 0.0139 0.6794 0.3326 2305 TYR B C 9641 O O . TYR B 658 ? 2.2260 1.9906 2.7520 0.0416 0.7358 0.3306 2305 TYR B O 9642 C CB . TYR B 658 ? 2.0442 1.9820 2.8903 0.0067 0.7240 0.4303 2305 TYR B CB 9643 C CG . TYR B 658 ? 2.0069 2.0225 3.0039 -0.0280 0.6860 0.4735 2305 TYR B CG 9644 C CD1 . TYR B 658 ? 2.0288 2.0848 3.0897 -0.0507 0.6151 0.4679 2305 TYR B CD1 9645 C CD2 . TYR B 658 ? 1.9796 2.0218 3.0496 -0.0414 0.7168 0.5214 2305 TYR B CD2 9646 C CE1 . TYR B 658 ? 2.0240 2.1405 3.2143 -0.0887 0.5683 0.5075 2305 TYR B CE1 9647 C CE2 . TYR B 658 ? 2.0250 2.1365 3.2390 -0.0803 0.6730 0.5641 2305 TYR B CE2 9648 C CZ . TYR B 658 ? 2.0252 2.1708 3.2961 -0.1054 0.5947 0.5558 2305 TYR B CZ 9649 O OH . TYR B 658 ? 2.0952 2.2984 3.4986 -0.1498 0.5389 0.5974 2305 TYR B OH 9650 N N . LEU B 659 ? 2.0428 1.8593 2.6313 0.0028 0.6217 0.2991 2306 LEU B N 9651 C CA . LEU B 659 ? 1.9233 1.6947 2.4174 0.0202 0.6187 0.2611 2306 LEU B CA 9652 C C . LEU B 659 ? 1.9012 1.7145 2.4551 0.0271 0.5994 0.2612 2306 LEU B C 9653 O O . LEU B 659 ? 1.8381 1.7073 2.4865 0.0095 0.5637 0.2792 2306 LEU B O 9654 C CB . LEU B 659 ? 1.8510 1.5806 2.2616 0.0026 0.5712 0.2234 2306 LEU B CB 9655 C CG . LEU B 659 ? 1.9756 1.6469 2.2769 0.0156 0.5737 0.1913 2306 LEU B CG 9656 C CD1 . LEU B 659 ? 2.2520 1.8616 2.4681 0.0294 0.6207 0.1962 2306 LEU B CD1 9657 C CD2 . LEU B 659 ? 1.9904 1.6456 2.2487 -0.0012 0.5220 0.1631 2306 LEU B CD2 9658 N N . ARG B 660 ? 1.9295 1.7086 2.4223 0.0505 0.6188 0.2423 2307 ARG B N 9659 C CA . ARG B 660 ? 1.8925 1.7051 2.4369 0.0619 0.6085 0.2464 2307 ARG B CA 9660 C C . ARG B 660 ? 1.9787 1.7341 2.4285 0.0794 0.6173 0.2158 2307 ARG B C 9661 O O . ARG B 660 ? 2.1086 1.8147 2.5024 0.1048 0.6693 0.2170 2307 ARG B O 9662 C CB . ARG B 660 ? 1.8807 1.7382 2.5220 0.0850 0.6582 0.2918 2307 ARG B CB 9663 C CG . ARG B 660 ? 1.9287 1.8651 2.6970 0.0742 0.6205 0.3202 2307 ARG B CG 9664 C CD . ARG B 660 ? 1.9671 1.9535 2.8429 0.1027 0.6766 0.3722 2307 ARG B CD 9665 N NE . ARG B 660 ? 1.7902 1.8634 2.8132 0.0782 0.6400 0.4165 2307 ARG B NE 9666 C CZ . ARG B 660 ? 1.7585 1.9021 2.9167 0.0961 0.6689 0.4721 2307 ARG B CZ 9667 N NH1 . ARG B 660 ? 1.9120 2.0438 3.0702 0.1452 0.7441 0.4880 2307 ARG B NH1 9668 N NH2 . ARG B 660 ? 1.7634 1.9850 3.0568 0.0648 0.6214 0.5140 2307 ARG B NH2 9669 N N . ILE B 661 ? 1.9569 1.7105 2.3823 0.0657 0.5685 0.1897 2308 ILE B N 9670 C CA . ILE B 661 ? 1.8958 1.6008 2.2459 0.0778 0.5720 0.1657 2308 ILE B CA 9671 C C . ILE B 661 ? 1.7812 1.5132 2.1902 0.0994 0.5861 0.1836 2308 ILE B C 9672 O O . ILE B 661 ? 1.5211 1.3177 2.0285 0.0954 0.5683 0.2083 2308 ILE B O 9673 C CB . ILE B 661 ? 1.8837 1.5729 2.1815 0.0569 0.5231 0.1352 2308 ILE B CB 9674 C CG1 . ILE B 661 ? 1.8650 1.6049 2.2227 0.0428 0.4788 0.1372 2308 ILE B CG1 9675 C CG2 . ILE B 661 ? 1.8379 1.4952 2.0767 0.0416 0.5141 0.1219 2308 ILE B CG2 9676 C CD1 . ILE B 661 ? 1.9336 1.6836 2.3059 0.0525 0.4689 0.1374 2308 ILE B CD1 9677 N N . HIS B 662 ? 1.8804 1.5561 2.2254 0.1207 0.6150 0.1728 2309 HIS B N 9678 C CA . HIS B 662 ? 2.0041 1.6868 2.3904 0.1499 0.6420 0.1911 2309 HIS B CA 9679 C C . HIS B 662 ? 1.9035 1.5429 2.2285 0.1499 0.6213 0.1672 2309 HIS B C 9680 O O . HIS B 662 ? 2.0381 1.5966 2.2718 0.1624 0.6484 0.1511 2309 HIS B O 9681 C CB . HIS B 662 ? 2.1727 1.8097 2.5337 0.1857 0.7159 0.2071 2309 HIS B CB 9682 C CG . HIS B 662 ? 2.3679 2.0754 2.8486 0.2022 0.7505 0.2529 2309 HIS B CG 9683 N ND1 . HIS B 662 ? 2.3421 2.0669 2.8420 0.1934 0.7689 0.2678 2309 HIS B ND1 9684 C CD2 . HIS B 662 ? 2.4687 2.2376 3.0657 0.2263 0.7693 0.2928 2309 HIS B CD2 9685 C CE1 . HIS B 662 ? 2.4191 2.2160 3.0467 0.2092 0.7984 0.3159 2309 HIS B CE1 9686 N NE2 . HIS B 662 ? 2.5107 2.3385 3.2034 0.2295 0.7977 0.3330 2309 HIS B NE2 9687 N N . PRO B 663 ? 1.6728 1.3567 2.0400 0.1348 0.5735 0.1661 2310 PRO B N 9688 C CA . PRO B 663 ? 1.6600 1.3037 1.9710 0.1327 0.5566 0.1473 2310 PRO B CA 9689 C C . PRO B 663 ? 1.7550 1.3503 2.0467 0.1652 0.5983 0.1555 2310 PRO B C 9690 O O . PRO B 663 ? 1.8446 1.4781 2.2142 0.1893 0.6158 0.1845 2310 PRO B O 9691 C CB . PRO B 663 ? 1.4835 1.1855 1.8516 0.1188 0.5091 0.1545 2310 PRO B CB 9692 C CG . PRO B 663 ? 1.4222 1.1898 1.8841 0.1188 0.5030 0.1822 2310 PRO B CG 9693 C CD . PRO B 663 ? 1.5326 1.2919 1.9865 0.1178 0.5326 0.1824 2310 PRO B CD 9694 N N . GLN B 664 ? 1.8183 1.3255 2.0068 0.1658 0.6125 0.1325 2311 GLN B N 9695 C CA . GLN B 664 ? 1.9956 1.4367 2.1464 0.1953 0.6482 0.1355 2311 GLN B CA 9696 C C . GLN B 664 ? 2.1547 1.5887 2.3014 0.1870 0.6159 0.1309 2311 GLN B C 9697 O O . GLN B 664 ? 2.3387 1.8105 2.5538 0.2068 0.6188 0.1537 2311 GLN B O 9698 C CB . GLN B 664 ? 2.1582 1.4878 2.1874 0.2031 0.6839 0.1160 2311 GLN B CB 9699 C CG . GLN B 664 ? 2.3256 1.6560 2.3581 0.2214 0.7304 0.1281 2311 GLN B CG 9700 C CD . GLN B 664 ? 2.3417 1.7225 2.4753 0.2641 0.7821 0.1666 2311 GLN B CD 9701 O OE1 . GLN B 664 ? 2.2811 1.6410 2.4301 0.2944 0.8062 0.1788 2311 GLN B OE1 9702 N NE2 . GLN B 664 ? 2.2929 1.7419 2.5028 0.2665 0.7993 0.1903 2311 GLN B NE2 9703 N N . SER B 665 ? 2.2520 1.6424 2.3273 0.1575 0.5842 0.1069 2312 SER B N 9704 C CA . SER B 665 ? 2.1886 1.5786 2.2668 0.1472 0.5556 0.1073 2312 SER B CA 9705 C C . SER B 665 ? 2.0441 1.4864 2.1386 0.1126 0.5095 0.1000 2312 SER B C 9706 O O . SER B 665 ? 2.0089 1.4458 2.0719 0.0903 0.4958 0.0857 2312 SER B O 9707 C CB . SER B 665 ? 2.4696 1.7518 2.4524 0.1445 0.5635 0.0924 2312 SER B CB 9708 O OG . SER B 665 ? 2.6618 1.9029 2.5746 0.1119 0.5417 0.0713 2312 SER B OG 9709 N N . TRP B 666 ? 1.9776 1.4650 2.1167 0.1108 0.4877 0.1120 2313 TRP B N 9710 C CA . TRP B 666 ? 1.8949 1.4333 2.0518 0.0871 0.4534 0.1090 2313 TRP B CA 9711 C C . TRP B 666 ? 1.8604 1.3783 1.9913 0.0725 0.4374 0.1094 2313 TRP B C 9712 O O . TRP B 666 ? 2.2016 1.6606 2.2838 0.0612 0.4403 0.1016 2313 TRP B O 9713 C CB . TRP B 666 ? 1.8439 1.4475 2.0649 0.0960 0.4399 0.1249 2313 TRP B CB 9714 C CG . TRP B 666 ? 1.8307 1.4354 2.0866 0.1207 0.4500 0.1463 2313 TRP B CG 9715 C CD1 . TRP B 666 ? 1.8152 1.4150 2.0709 0.1247 0.4371 0.1583 2313 TRP B CD1 9716 C CD2 . TRP B 666 ? 1.8157 1.4269 2.1161 0.1477 0.4786 0.1631 2313 TRP B CD2 9717 N NE1 . TRP B 666 ? 1.8030 1.4070 2.1027 0.1524 0.4508 0.1816 2313 TRP B NE1 9718 C CE2 . TRP B 666 ? 1.7626 1.3768 2.0958 0.1683 0.4786 0.1863 2313 TRP B CE2 9719 C CE3 . TRP B 666 ? 1.8401 1.4565 2.1593 0.1583 0.5074 0.1650 2313 TRP B CE3 9720 C CZ2 . TRP B 666 ? 1.8075 1.4353 2.2017 0.2010 0.5064 0.2130 2313 TRP B CZ2 9721 C CZ3 . TRP B 666 ? 1.9282 1.5579 2.3054 0.1904 0.5394 0.1915 2313 TRP B CZ3 9722 C CH2 . TRP B 666 ? 1.9594 1.5973 2.3787 0.2126 0.5390 0.2162 2313 TRP B CH2 9723 N N . VAL B 667 ? 1.5847 1.1437 1.7422 0.0712 0.4197 0.1204 2314 VAL B N 9724 C CA . VAL B 667 ? 1.5585 1.1042 1.6957 0.0580 0.4096 0.1260 2314 VAL B CA 9725 C C . VAL B 667 ? 1.6998 1.2569 1.8503 0.0711 0.4030 0.1448 2314 VAL B C 9726 O O . VAL B 667 ? 1.8648 1.3838 2.0017 0.0767 0.4094 0.1552 2314 VAL B O 9727 C CB . VAL B 667 ? 1.4564 1.0315 1.5919 0.0375 0.3972 0.1208 2314 VAL B CB 9728 C CG1 . VAL B 667 ? 1.4000 1.0214 1.5543 0.0448 0.3873 0.1224 2314 VAL B CG1 9729 C CG2 . VAL B 667 ? 1.3463 0.9066 1.4692 0.0213 0.3942 0.1315 2314 VAL B CG2 9730 N N . HIS B 668 ? 1.6738 1.2742 1.8425 0.0744 0.3873 0.1494 2315 HIS B N 9731 C CA . HIS B 668 ? 1.7508 1.3603 1.9217 0.0843 0.3718 0.1676 2315 HIS B CA 9732 C C . HIS B 668 ? 1.7137 1.3574 1.9266 0.0953 0.3550 0.1755 2315 HIS B C 9733 O O . HIS B 668 ? 1.6825 1.3326 1.9191 0.1085 0.3416 0.1968 2315 HIS B O 9734 C CB . HIS B 668 ? 1.9233 1.5396 2.0588 0.0735 0.3622 0.1674 2315 HIS B CB 9735 C CG . HIS B 668 ? 2.0130 1.6073 2.1236 0.0631 0.3769 0.1731 2315 HIS B CG 9736 N ND1 . HIS B 668 ? 2.1365 1.7059 2.2302 0.0673 0.3787 0.1922 2315 HIS B ND1 9737 C CD2 . HIS B 668 ? 2.0173 1.6158 2.1247 0.0473 0.3880 0.1678 2315 HIS B CD2 9738 C CE1 . HIS B 668 ? 2.1648 1.7233 2.2474 0.0526 0.3923 0.1983 2315 HIS B CE1 9739 N NE2 . HIS B 668 ? 2.1416 1.7211 2.2372 0.0402 0.3970 0.1852 2315 HIS B NE2 9740 N N . GLN B 669 ? 1.7776 1.4448 2.0050 0.0875 0.3524 0.1621 2316 GLN B N 9741 C CA . GLN B 669 ? 1.8850 1.5877 2.1615 0.0909 0.3351 0.1714 2316 GLN B CA 9742 C C . GLN B 669 ? 1.9201 1.6323 2.2125 0.0860 0.3530 0.1567 2316 GLN B C 9743 O O . GLN B 669 ? 2.0070 1.6992 2.2621 0.0766 0.3672 0.1377 2316 GLN B O 9744 C CB . GLN B 669 ? 1.8595 1.5701 2.1115 0.0783 0.2988 0.1705 2316 GLN B CB 9745 C CG . GLN B 669 ? 1.8918 1.5859 2.1131 0.0818 0.2753 0.1867 2316 GLN B CG 9746 C CD . GLN B 669 ? 1.9864 1.7053 2.2670 0.0902 0.2495 0.2156 2316 GLN B CD 9747 O OE1 . GLN B 669 ? 1.9756 1.7288 2.3292 0.0956 0.2560 0.2256 2316 GLN B OE1 9748 N NE2 . GLN B 669 ? 2.1694 1.8724 2.4224 0.0922 0.2205 0.2337 2316 GLN B NE2 9749 N N . ILE B 670 ? 1.7191 1.4632 2.0701 0.0910 0.3511 0.1691 2317 ILE B N 9750 C CA . ILE B 670 ? 1.5412 1.2943 1.8988 0.0820 0.3621 0.1562 2317 ILE B CA 9751 C C . ILE B 670 ? 1.4497 1.2096 1.7838 0.0628 0.3286 0.1459 2317 ILE B C 9752 O O . ILE B 670 ? 1.4169 1.1869 1.7591 0.0578 0.2944 0.1577 2317 ILE B O 9753 C CB . ILE B 670 ? 1.5070 1.2907 1.9359 0.0930 0.3795 0.1756 2317 ILE B CB 9754 C CG1 . ILE B 670 ? 1.5285 1.2903 1.9670 0.1198 0.4224 0.1856 2317 ILE B CG1 9755 C CG2 . ILE B 670 ? 1.4262 1.2091 1.8460 0.0824 0.3933 0.1615 2317 ILE B CG2 9756 C CD1 . ILE B 670 ? 1.5308 1.3094 2.0195 0.1395 0.4175 0.2148 2317 ILE B CD1 9757 N N . ALA B 671 ? 1.4096 1.1547 1.7055 0.0532 0.3376 0.1245 2318 ALA B N 9758 C CA . ALA B 671 ? 1.4473 1.1878 1.7140 0.0402 0.3164 0.1122 2318 ALA B CA 9759 C C . ALA B 671 ? 1.4809 1.2176 1.7391 0.0343 0.3327 0.0977 2318 ALA B C 9760 O O . ALA B 671 ? 1.3645 1.0884 1.6040 0.0357 0.3537 0.0903 2318 ALA B O 9761 C CB . ALA B 671 ? 1.4946 1.2113 1.7048 0.0411 0.3093 0.1060 2318 ALA B CB 9762 N N . LEU B 672 ? 1.6082 1.3515 1.8787 0.0248 0.3172 0.0961 2319 LEU B N 9763 C CA . LEU B 672 ? 1.6261 1.3661 1.8933 0.0191 0.3284 0.0866 2319 LEU B CA 9764 C C . LEU B 672 ? 1.5780 1.3019 1.8193 0.0105 0.3082 0.0765 2319 LEU B C 9765 O O . LEU B 672 ? 1.6252 1.3464 1.8764 0.0010 0.2815 0.0814 2319 LEU B O 9766 C CB . LEU B 672 ? 1.5186 1.2775 1.8347 0.0187 0.3428 0.0993 2319 LEU B CB 9767 C CG . LEU B 672 ? 1.4795 1.2241 1.7809 0.0264 0.3767 0.0961 2319 LEU B CG 9768 C CD1 . LEU B 672 ? 1.4594 1.2030 1.7672 0.0198 0.3863 0.0971 2319 LEU B CD1 9769 C CD2 . LEU B 672 ? 1.5117 1.2310 1.7618 0.0255 0.3794 0.0815 2319 LEU B CD2 9770 N N . ARG B 673 ? 1.5241 1.2328 1.7316 0.0140 0.3194 0.0646 2320 ARG B N 9771 C CA . ARG B 673 ? 1.6206 1.3132 1.8142 0.0097 0.3135 0.0568 2320 ARG B CA 9772 C C . ARG B 673 ? 1.6358 1.3405 1.8501 0.0070 0.3310 0.0593 2320 ARG B C 9773 O O . ARG B 673 ? 1.6876 1.4017 1.9108 0.0093 0.3459 0.0637 2320 ARG B O 9774 C CB . ARG B 673 ? 1.6973 1.3671 1.8467 0.0209 0.3196 0.0480 2320 ARG B CB 9775 C CG . ARG B 673 ? 1.7472 1.3772 1.8486 0.0230 0.3010 0.0408 2320 ARG B CG 9776 C CD . ARG B 673 ? 1.6215 1.2265 1.6761 0.0422 0.3215 0.0358 2320 ARG B CD 9777 N NE . ARG B 673 ? 1.5378 1.1685 1.6034 0.0493 0.3397 0.0451 2320 ARG B NE 9778 C CZ . ARG B 673 ? 1.8424 1.4573 1.8723 0.0657 0.3592 0.0482 2320 ARG B CZ 9779 N NH1 . ARG B 673 ? 2.1659 1.7328 2.1375 0.0812 0.3671 0.0404 2320 ARG B NH1 9780 N NH2 . ARG B 673 ? 2.0618 1.7021 2.1099 0.0678 0.3740 0.0606 2320 ARG B NH2 9781 N N . MET B 674 ? 1.6195 1.3135 1.8311 0.0024 0.3287 0.0567 2321 MET B N 9782 C CA . MET B 674 ? 1.6025 1.2991 1.8210 -0.0009 0.3426 0.0607 2321 MET B CA 9783 C C . MET B 674 ? 1.5946 1.2769 1.8127 -0.0070 0.3361 0.0612 2321 MET B C 9784 O O . MET B 674 ? 1.6685 1.3411 1.8935 -0.0137 0.3202 0.0610 2321 MET B O 9785 C CB . MET B 674 ? 1.6729 1.3819 1.9153 -0.0024 0.3572 0.0707 2321 MET B CB 9786 C CG . MET B 674 ? 1.7794 1.4834 2.0296 -0.0071 0.3717 0.0794 2321 MET B CG 9787 S SD . MET B 674 ? 1.8687 1.6007 2.1831 -0.0117 0.3733 0.0992 2321 MET B SD 9788 C CE . MET B 674 ? 2.1028 1.8275 2.4157 -0.0025 0.4174 0.1130 2321 MET B CE 9789 N N . GLU B 675 ? 1.5288 1.2038 1.7352 -0.0070 0.3436 0.0634 2322 GLU B N 9790 C CA . GLU B 675 ? 1.5021 1.1623 1.7101 -0.0138 0.3415 0.0688 2322 GLU B CA 9791 C C . GLU B 675 ? 1.5972 1.2532 1.7977 -0.0185 0.3572 0.0784 2322 GLU B C 9792 O O . GLU B 675 ? 1.6819 1.3367 1.8646 -0.0160 0.3679 0.0780 2322 GLU B O 9793 C CB . GLU B 675 ? 1.4470 1.0891 1.6382 -0.0068 0.3336 0.0659 2322 GLU B CB 9794 C CG . GLU B 675 ? 1.4875 1.1074 1.6789 -0.0142 0.3294 0.0722 2322 GLU B CG 9795 C CD . GLU B 675 ? 1.7830 1.3722 1.9590 -0.0049 0.3194 0.0660 2322 GLU B CD 9796 O OE1 . GLU B 675 ? 1.9205 1.5105 2.0870 0.0128 0.3237 0.0631 2322 GLU B OE1 9797 O OE2 . GLU B 675 ? 1.8225 1.3833 1.9965 -0.0147 0.3092 0.0664 2322 GLU B OE2 9798 N N . VAL B 676 ? 1.5911 1.2343 1.7952 -0.0256 0.3587 0.0873 2323 VAL B N 9799 C CA . VAL B 676 ? 1.6227 1.2504 1.8064 -0.0289 0.3775 0.0989 2323 VAL B CA 9800 C C . VAL B 676 ? 1.7593 1.3611 1.9107 -0.0304 0.3671 0.1025 2323 VAL B C 9801 O O . VAL B 676 ? 1.9274 1.5245 2.0892 -0.0293 0.3511 0.1011 2323 VAL B O 9802 C CB . VAL B 676 ? 1.4294 1.0668 1.6501 -0.0359 0.3942 0.1153 2323 VAL B CB 9803 C CG1 . VAL B 676 ? 1.4267 1.0419 1.6149 -0.0334 0.4259 0.1287 2323 VAL B CG1 9804 C CG2 . VAL B 676 ? 1.3092 0.9795 1.5761 -0.0339 0.3967 0.1170 2323 VAL B CG2 9805 N N . LEU B 677 ? 1.7572 1.3343 1.8624 -0.0317 0.3752 0.1081 2324 LEU B N 9806 C CA . LEU B 677 ? 1.9053 1.4569 1.9775 -0.0346 0.3593 0.1161 2324 LEU B CA 9807 C C . LEU B 677 ? 2.1040 1.6220 2.1422 -0.0401 0.3775 0.1313 2324 LEU B C 9808 O O . LEU B 677 ? 2.3226 1.8274 2.3390 -0.0391 0.4071 0.1351 2324 LEU B O 9809 C CB . LEU B 677 ? 1.8725 1.4139 1.9090 -0.0365 0.3409 0.1136 2324 LEU B CB 9810 C CG . LEU B 677 ? 1.8595 1.4293 1.9317 -0.0317 0.3147 0.1142 2324 LEU B CG 9811 C CD1 . LEU B 677 ? 1.7317 1.3361 1.8457 -0.0232 0.3216 0.1016 2324 LEU B CD1 9812 C CD2 . LEU B 677 ? 1.8641 1.4220 1.9082 -0.0414 0.2875 0.1239 2324 LEU B CD2 9813 N N . GLY B 678 ? 2.0734 1.5752 2.1072 -0.0429 0.3645 0.1425 2325 GLY B N 9814 C CA . GLY B 678 ? 2.0376 1.5023 2.0325 -0.0486 0.3809 0.1608 2325 GLY B CA 9815 C C . GLY B 678 ? 2.1621 1.6199 2.1843 -0.0528 0.3745 0.1739 2325 GLY B C 9816 O O . GLY B 678 ? 2.2275 1.6915 2.2749 -0.0481 0.3492 0.1695 2325 GLY B O 9817 N N . CYS B 679 ? 2.1986 1.6386 2.2144 -0.0600 0.4013 0.1924 2326 CYS B N 9818 C CA . CYS B 679 ? 2.1951 1.6176 2.2296 -0.0681 0.3962 0.2093 2326 CYS B CA 9819 C C . CYS B 679 ? 2.0617 1.4762 2.1093 -0.0791 0.4324 0.2356 2326 CYS B C 9820 O O . CYS B 679 ? 1.8904 1.3306 1.9661 -0.0795 0.4637 0.2412 2326 CYS B O 9821 C CB . CYS B 679 ? 2.3921 1.7778 2.3771 -0.0637 0.3712 0.2170 2326 CYS B CB 9822 S SG . CYS B 679 ? 2.7127 2.0455 2.5965 -0.0659 0.3881 0.2355 2326 CYS B SG 9823 N N . GLU B 680 ? 2.1302 1.5110 2.1638 -0.0867 0.4299 0.2559 2327 GLU B N 9824 C CA . GLU B 680 ? 2.3185 1.6963 2.3838 -0.1009 0.4602 0.2859 2327 GLU B CA 9825 C C . GLU B 680 ? 2.3596 1.6985 2.3516 -0.0961 0.5006 0.3101 2327 GLU B C 9826 O O . GLU B 680 ? 2.5248 1.8148 2.4415 -0.0925 0.4861 0.3145 2327 GLU B O 9827 C CB . GLU B 680 ? 2.5797 1.9318 2.6676 -0.1135 0.4326 0.2952 2327 GLU B CB 9828 C CG . GLU B 680 ? 2.6321 1.9974 2.7681 -0.1164 0.3948 0.2710 2327 GLU B CG 9829 C CD . GLU B 680 ? 2.7555 2.1415 2.9686 -0.1407 0.3935 0.2821 2327 GLU B CD 9830 O OE1 . GLU B 680 ? 2.8165 2.1755 3.0484 -0.1599 0.3928 0.3067 2327 GLU B OE1 9831 O OE2 . GLU B 680 ? 2.7484 2.1761 3.0050 -0.1431 0.3894 0.2693 2327 GLU B OE2 9832 N N . ALA B 681 ? 2.2125 1.5680 2.2228 -0.0942 0.5520 0.3292 2328 ALA B N 9833 C CA . ALA B 681 ? 2.3233 1.6274 2.2468 -0.0851 0.6008 0.3536 2328 ALA B CA 9834 C C . ALA B 681 ? 2.4088 1.7121 2.3735 -0.0970 0.6406 0.3980 2328 ALA B C 9835 O O . ALA B 681 ? 2.3072 1.6195 2.3305 -0.1169 0.6117 0.4087 2328 ALA B O 9836 C CB . ALA B 681 ? 2.3282 1.6265 2.2054 -0.0647 0.6424 0.3447 2328 ALA B CB 9837 N N . GLN B 682 ? 2.5623 1.8472 2.4912 -0.0839 0.7085 0.4253 2329 GLN B N 9838 C CA . GLN B 682 ? 2.7785 2.0733 2.7624 -0.0939 0.7580 0.4759 2329 GLN B CA 9839 C C . GLN B 682 ? 2.8684 2.2547 3.0179 -0.1085 0.7650 0.4952 2329 GLN B C 9840 O O . GLN B 682 ? 2.8266 2.2529 3.0238 -0.0927 0.8179 0.5122 2329 GLN B O 9841 C CB . GLN B 682 ? 2.8897 2.1283 2.7739 -0.0702 0.8373 0.5030 2329 GLN B CB 9842 C CG . GLN B 682 ? 3.0836 2.2220 2.8121 -0.0677 0.8302 0.5054 2329 GLN B CG 9843 C CD . GLN B 682 ? 3.0276 2.1353 2.7473 -0.0755 0.8769 0.5580 2329 GLN B CD 9844 O OE1 . GLN B 682 ? 2.9608 2.0519 2.6887 -0.0967 0.8372 0.5692 2329 GLN B OE1 9845 N NE2 . GLN B 682 ? 2.8928 1.9859 2.5890 -0.0554 0.9655 0.5925 2329 GLN B NE2 9846 N N . ASP B 683 ? 3.0138 2.4253 3.2453 -0.1385 0.7098 0.4947 2330 ASP B N 9847 C CA . ASP B 683 ? 2.9183 2.4053 3.2936 -0.1606 0.6830 0.5006 2330 ASP B CA 9848 C C . ASP B 683 ? 2.7758 2.3132 3.2733 -0.1804 0.7236 0.5612 2330 ASP B C 9849 O O . ASP B 683 ? 2.6535 2.1736 3.1816 -0.2081 0.7122 0.5900 2330 ASP B O 9850 C CB . ASP B 683 ? 2.9569 2.4286 3.3445 -0.1835 0.6031 0.4699 2330 ASP B CB 9851 C CG . ASP B 683 ? 2.9932 2.4421 3.3000 -0.1628 0.5643 0.4147 2330 ASP B CG 9852 O OD1 . ASP B 683 ? 2.9102 2.3558 3.1547 -0.1367 0.5891 0.3981 2330 ASP B OD1 9853 O OD2 . ASP B 683 ? 2.9956 2.4255 3.3007 -0.1726 0.5096 0.3895 2330 ASP B OD2 9854 N N . LEU B 684 ? 2.7382 2.3405 3.3139 -0.1664 0.7668 0.5813 2331 LEU B N 9855 C CA . LEU B 684 ? 2.7870 2.4475 3.4756 -0.1674 0.8355 0.6479 2331 LEU B CA 9856 C C . LEU B 684 ? 2.8663 2.4966 3.4645 -0.1187 0.9300 0.6588 2331 LEU B C 9857 O O . LEU B 684 ? 2.7724 2.3567 3.2525 -0.0900 0.9281 0.6116 2331 LEU B O 9858 C CB . LEU B 684 ? 2.8045 2.4669 3.5660 -0.2063 0.8325 0.6990 2331 LEU B CB 9859 C CG . LEU B 684 ? 2.5902 2.3101 3.5090 -0.2585 0.7701 0.7251 2331 LEU B CG 9860 C CD1 . LEU B 684 ? 2.4033 2.0700 3.3118 -0.2969 0.7358 0.7410 2331 LEU B CD1 9861 C CD2 . LEU B 684 ? 2.5103 2.3328 3.6054 -0.2664 0.8132 0.7916 2331 LEU B CD2 9862 N N . TYR B 685 ? 2.8787 2.5302 3.5310 -0.1098 1.0117 0.7216 2332 TYR B N 9863 C CA . TYR B 685 ? 2.8401 2.4421 3.3907 -0.0619 1.1149 0.7405 2332 TYR B CA 9864 C C . TYR B 685 ? 2.9762 2.4559 3.3023 -0.0396 1.1115 0.6908 2332 TYR B C 9865 O O . TYR B 685 ? 2.9996 2.4495 3.2423 -0.0236 1.0792 0.6365 2332 TYR B O 9866 C CB . TYR B 685 ? 2.6491 2.2663 3.2644 -0.0670 1.1895 0.8165 2332 TYR B CB 9867 C CG . TYR B 685 ? 2.6653 2.2991 3.3574 -0.1218 1.1225 0.8335 2332 TYR B CG 9868 C CD1 . TYR B 685 ? 2.6598 2.2050 3.2193 -0.1372 1.0693 0.7973 2332 TYR B CD1 9869 C CD2 . TYR B 685 ? 2.6719 2.4060 3.5698 -0.1604 1.1018 0.8835 2332 TYR B CD2 9870 C CE1 . TYR B 685 ? 2.6082 2.1552 3.2280 -0.1843 1.0071 0.8091 2332 TYR B CE1 9871 C CE2 . TYR B 685 ? 2.6620 2.3936 3.6157 -0.2137 1.0334 0.8945 2332 TYR B CE2 9872 C CZ . TYR B 685 ? 2.6082 2.2415 3.4169 -0.2231 0.9893 0.8552 2332 TYR B CZ 9873 O OH . TYR B 685 ? 2.5444 2.1601 3.3945 -0.2712 0.9246 0.8636 2332 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A1755 WRONG CHIRALITY AT ATOM C1' # 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 ALA 1 1 1 ALA ALA A . n A 1 2 THR 2 2 2 THR THR A . n A 1 3 ARG 3 3 3 ARG ARG A . n A 1 4 ARG 4 4 4 ARG ARG A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 TYR 6 6 6 TYR TYR A . n A 1 7 LEU 7 7 7 LEU LEU A . n A 1 8 GLY 8 8 8 GLY GLY A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 VAL 10 10 10 VAL VAL A . n A 1 11 GLU 11 11 11 GLU GLU A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 SER 13 13 13 SER SER A . n A 1 14 TRP 14 14 14 TRP TRP A . n A 1 15 ASP 15 15 15 ASP ASP A . n A 1 16 TYR 16 16 16 TYR TYR A . n A 1 17 MET 17 17 ? ? ? A . n A 1 18 GLN 18 18 ? ? ? A . n A 1 19 SER 19 19 ? ? ? A . n A 1 20 ASP 20 20 ? ? ? A . n A 1 21 LEU 21 21 ? ? ? A . n A 1 22 GLY 22 22 ? ? ? A . n A 1 23 GLU 23 23 ? ? ? A . n A 1 24 LEU 24 24 ? ? ? A . n A 1 25 PRO 25 25 ? ? ? A . n A 1 26 VAL 26 26 ? ? ? A . n A 1 27 ASP 27 27 ? ? ? A . n A 1 28 ALA 28 28 ? ? ? A . n A 1 29 ARG 29 29 ? ? ? A . n A 1 30 PHE 30 30 ? ? ? A . n A 1 31 PRO 31 31 ? ? ? A . n A 1 32 PRO 32 32 ? ? ? A . n A 1 33 ARG 33 33 ? ? ? A . n A 1 34 VAL 34 34 ? ? ? A . n A 1 35 PRO 35 35 ? ? ? A . n A 1 36 LYS 36 36 ? ? ? A . n A 1 37 SER 37 37 ? ? ? A . n A 1 38 PHE 38 38 ? ? ? A . n A 1 39 PRO 39 39 ? ? ? A . n A 1 40 PHE 40 40 ? ? ? A . n A 1 41 ASN 41 41 ? ? ? A . n A 1 42 THR 42 42 ? ? ? A . n A 1 43 SER 43 43 ? ? ? A . n A 1 44 VAL 44 44 44 VAL VAL A . n A 1 45 VAL 45 45 45 VAL VAL A . n A 1 46 TYR 46 46 46 TYR TYR A . n A 1 47 LYS 47 47 47 LYS LYS A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 THR 49 49 49 THR THR A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 VAL 52 52 52 VAL VAL A . n A 1 53 GLU 53 53 53 GLU GLU A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 THR 55 55 55 THR THR A . n A 1 56 ASP 56 56 56 ASP ASP A . n A 1 57 HIS 57 57 57 HIS HIS A . n A 1 58 LEU 58 58 58 LEU LEU A . n A 1 59 PHE 59 59 59 PHE PHE A . n A 1 60 ASN 60 60 60 ASN ASN A . n A 1 61 ILE 61 61 61 ILE ILE A . n A 1 62 ALA 62 62 62 ALA ALA A . n A 1 63 LYS 63 63 63 LYS LYS A . n A 1 64 PRO 64 64 64 PRO PRO A . n A 1 65 ARG 65 65 65 ARG ARG A . n A 1 66 PRO 66 66 66 PRO PRO A . n A 1 67 PRO 67 67 67 PRO PRO A . n A 1 68 TRP 68 68 68 TRP TRP A . n A 1 69 MET 69 69 69 MET MET A . n A 1 70 GLY 70 70 70 GLY GLY A . n A 1 71 LEU 71 71 71 LEU LEU A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 THR 75 75 75 THR THR A . n A 1 76 ILE 76 76 76 ILE ILE A . n A 1 77 GLN 77 77 77 GLN GLN A . n A 1 78 ALA 78 78 78 ALA ALA A . n A 1 79 GLU 79 79 79 GLU GLU A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 TYR 81 81 81 TYR TYR A . n A 1 82 ASP 82 82 82 ASP ASP A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 ILE 86 86 86 ILE ILE A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 LEU 88 88 88 LEU LEU A . n A 1 89 LYS 89 89 89 LYS LYS A . n A 1 90 ASN 90 90 90 ASN ASN A . n A 1 91 MET 91 91 91 MET MET A . n A 1 92 ALA 92 92 92 ALA ALA A . n A 1 93 SER 93 93 93 SER SER A . n A 1 94 HIS 94 94 94 HIS HIS A . n A 1 95 PRO 95 95 95 PRO PRO A . n A 1 96 VAL 96 96 96 VAL VAL A . n A 1 97 SER 97 97 97 SER SER A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 HIS 99 99 99 HIS HIS A . n A 1 100 ALA 100 100 100 ALA ALA A . n A 1 101 VAL 101 101 101 VAL VAL A . n A 1 102 GLY 102 102 102 GLY GLY A . n A 1 103 VAL 103 103 103 VAL VAL A . n A 1 104 SER 104 104 104 SER SER A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 TRP 106 106 106 TRP TRP A . n A 1 107 LYS 107 107 107 LYS LYS A . n A 1 108 ALA 108 108 108 ALA ALA A . n A 1 109 SER 109 109 109 SER SER A . n A 1 110 GLU 110 110 110 GLU GLU A . n A 1 111 GLY 111 111 111 GLY GLY A . n A 1 112 ALA 112 112 112 ALA ALA A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 ASP 116 116 116 ASP ASP A . n A 1 117 GLN 117 117 117 GLN GLN A . n A 1 118 THR 118 118 118 THR THR A . n A 1 119 SER 119 119 119 SER SER A . n A 1 120 GLN 120 120 120 GLN GLN A . n A 1 121 ARG 121 121 121 ARG ARG A . n A 1 122 GLU 122 122 122 GLU GLU A . n A 1 123 LYS 123 123 123 LYS LYS A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 ASP 125 125 125 ASP ASP A . n A 1 126 ASP 126 126 126 ASP ASP A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 PHE 129 129 129 PHE PHE A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 GLY 132 132 132 GLY GLY A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 HIS 134 134 134 HIS HIS A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 TYR 136 136 136 TYR TYR A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 TRP 138 138 138 TRP TRP A . n A 1 139 GLN 139 139 139 GLN GLN A . n A 1 140 VAL 140 140 140 VAL VAL A . n A 1 141 LEU 141 141 141 LEU LEU A . n A 1 142 LYS 142 142 142 LYS LYS A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 ASN 144 144 144 ASN ASN A . n A 1 145 GLY 145 145 145 GLY GLY A . n A 1 146 PRO 146 146 146 PRO PRO A . n A 1 147 MET 147 147 147 MET MET A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 ASP 150 150 150 ASP ASP A . n A 1 151 PRO 151 151 151 PRO PRO A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 CYS 153 153 153 CYS CYS A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 THR 155 155 155 THR THR A . n A 1 156 TYR 156 156 156 TYR TYR A . n A 1 157 SER 157 157 157 SER SER A . n A 1 158 TYR 158 158 158 TYR TYR A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 SER 160 160 160 SER SER A . n A 1 161 HIS 161 161 161 HIS HIS A . n A 1 162 VAL 162 162 162 VAL VAL A . n A 1 163 ASP 163 163 163 ASP ASP A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 LYS 166 166 166 LYS LYS A . n A 1 167 ASP 167 167 167 ASP ASP A . n A 1 168 LEU 168 168 168 LEU LEU A . n A 1 169 ASN 169 169 169 ASN ASN A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 GLY 171 171 171 GLY GLY A . n A 1 172 LEU 172 172 172 LEU LEU 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 ALA 175 175 175 ALA ALA A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 VAL 178 178 178 VAL VAL A . n A 1 179 CYS 179 179 179 CYS CYS A . n A 1 180 ARG 180 180 180 ARG ARG A . n A 1 181 GLU 181 181 181 GLU GLU A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 SER 183 183 183 SER SER A . n A 1 184 LEU 184 184 184 LEU LEU A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 LYS 186 186 186 LYS LYS A . n A 1 187 GLU 187 187 187 GLU GLU A . n A 1 188 LYS 188 188 188 LYS LYS A . n A 1 189 THR 189 189 189 THR THR A . n A 1 190 GLN 190 190 190 GLN GLN A . n A 1 191 THR 191 191 191 THR THR A . n A 1 192 LEU 192 192 192 LEU LEU A . n A 1 193 HIS 193 193 193 HIS HIS A . n A 1 194 LYS 194 194 194 LYS LYS A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 LEU 197 197 197 LEU LEU A . n A 1 198 LEU 198 198 198 LEU LEU A . n A 1 199 PHE 199 199 199 PHE PHE A . n A 1 200 ALA 200 200 200 ALA ALA A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 PHE 202 202 202 PHE PHE A . n A 1 203 ASP 203 203 203 ASP ASP A . n A 1 204 GLU 204 204 204 GLU GLU A . n A 1 205 GLY 205 205 205 GLY GLY A . n A 1 206 LYS 206 206 206 LYS LYS A . n A 1 207 SER 207 207 207 SER SER A . n A 1 208 TRP 208 208 208 TRP TRP 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 GLU 211 211 ? ? ? A . n A 1 212 THR 212 212 ? ? ? A . n A 1 213 LYS 213 213 ? ? ? A . n A 1 214 ASN 214 214 ? ? ? A . n A 1 215 SER 215 215 ? ? ? A . n A 1 216 LEU 216 216 ? ? ? A . n A 1 217 MET 217 217 ? ? ? A . n A 1 218 GLN 218 218 ? ? ? A . n A 1 219 ASP 219 219 ? ? ? A . n A 1 220 ARG 220 220 ? ? ? A . n A 1 221 ASP 221 221 ? ? ? A . n A 1 222 ALA 222 222 ? ? ? A . n A 1 223 ALA 223 223 ? ? ? A . n A 1 224 SER 224 224 ? ? ? A . n A 1 225 ALA 225 225 ? ? ? A . n A 1 226 ARG 226 226 ? ? ? A . n A 1 227 ALA 227 227 ? ? ? A . n A 1 228 TRP 228 228 ? ? ? A . n A 1 229 PRO 229 229 229 PRO PRO A . n A 1 230 LYS 230 230 230 LYS LYS A . n A 1 231 MET 231 231 231 MET MET A . n A 1 232 HIS 232 232 232 HIS HIS A . n A 1 233 THR 233 233 233 THR THR A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 ASN 235 235 235 ASN ASN A . n A 1 236 GLY 236 236 236 GLY GLY A . n A 1 237 TYR 237 237 237 TYR TYR A . n A 1 238 VAL 238 238 238 VAL VAL A . n A 1 239 ASN 239 239 239 ASN ASN A . n A 1 240 ARG 240 240 240 ARG ARG A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 PRO 243 243 243 PRO PRO A . n A 1 244 GLY 244 244 244 GLY GLY A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ILE 246 246 246 ILE ILE A . n A 1 247 GLY 247 247 247 GLY GLY A . n A 1 248 CYS 248 248 248 CYS CYS A . n A 1 249 HIS 249 249 249 HIS HIS A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 LYS 251 251 251 LYS LYS A . n A 1 252 SER 252 252 252 SER SER A . n A 1 253 VAL 253 253 253 VAL VAL A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 TRP 255 255 255 TRP TRP A . n A 1 256 HIS 256 256 256 HIS HIS A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 GLY 259 259 259 GLY GLY A . n A 1 260 MET 260 260 260 MET MET A . n A 1 261 GLY 261 261 261 GLY GLY A . n A 1 262 THR 262 262 262 THR THR A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 PRO 264 264 264 PRO PRO A . n A 1 265 GLU 265 265 265 GLU GLU A . n A 1 266 VAL 266 266 266 VAL VAL A . n A 1 267 HIS 267 267 267 HIS HIS A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 ILE 269 269 269 ILE ILE A . n A 1 270 PHE 270 270 270 PHE PHE A . n A 1 271 LEU 271 271 271 LEU LEU A . n A 1 272 GLU 272 272 272 GLU GLU A . n A 1 273 GLY 273 273 273 GLY GLY A . n A 1 274 HIS 274 274 274 HIS HIS A . n A 1 275 THR 275 275 275 THR THR A . n A 1 276 PHE 276 276 276 PHE PHE A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 VAL 278 278 278 VAL VAL A . n A 1 279 ARG 279 279 279 ARG ARG A . n A 1 280 ASN 280 280 280 ASN ASN A . n A 1 281 HIS 281 281 281 HIS HIS A . n A 1 282 ARG 282 282 282 ARG ARG A . n A 1 283 GLN 283 283 283 GLN GLN A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 SER 285 285 285 SER SER A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 GLU 287 287 287 GLU GLU A . n A 1 288 ILE 288 288 288 ILE ILE A . n A 1 289 SER 289 289 289 SER SER A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 ILE 291 291 291 ILE ILE A . n A 1 292 THR 292 292 292 THR THR A . n A 1 293 PHE 293 293 293 PHE PHE A . n A 1 294 LEU 294 294 294 LEU LEU A . n A 1 295 THR 295 295 295 THR THR A . n A 1 296 ALA 296 296 296 ALA ALA A . n A 1 297 GLN 297 297 297 GLN GLN A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 LEU 300 300 300 LEU LEU A . n A 1 301 MET 301 301 301 MET MET A . n A 1 302 ASP 302 302 302 ASP ASP A . n A 1 303 LEU 303 303 303 LEU LEU A . n A 1 304 GLY 304 304 304 GLY GLY A . n A 1 305 GLN 305 305 305 GLN GLN A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 LEU 308 308 308 LEU LEU A . n A 1 309 PHE 309 309 309 PHE PHE A . n A 1 310 CYS 310 310 310 CYS CYS A . n A 1 311 HIS 311 311 311 HIS HIS A . n A 1 312 ILE 312 312 312 ILE ILE A . n A 1 313 SER 313 313 313 SER SER A . n A 1 314 SER 314 314 314 SER SER A . n A 1 315 HIS 315 315 315 HIS HIS A . n A 1 316 GLN 316 316 316 GLN GLN A . n A 1 317 HIS 317 317 317 HIS HIS A . n A 1 318 ASP 318 318 318 ASP ASP A . n A 1 319 GLY 319 319 319 GLY GLY 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 ALA 322 322 322 ALA ALA A . n A 1 323 TYR 323 323 323 TYR TYR A . n A 1 324 VAL 324 324 324 VAL VAL A . n A 1 325 LYS 325 325 325 LYS LYS A . n A 1 326 VAL 326 326 326 VAL VAL A . n A 1 327 ASP 327 327 327 ASP ASP A . n A 1 328 SER 328 328 328 SER SER A . n A 1 329 CYS 329 329 329 CYS CYS A . n A 1 330 PRO 330 330 330 PRO PRO A . n A 1 331 GLU 331 331 331 GLU GLU A . n A 1 332 GLU 332 332 332 GLU GLU A . n A 1 333 PRO 333 333 333 PRO PRO A . n A 1 334 GLN 334 334 ? ? ? A . n A 1 335 LEU 335 335 ? ? ? A . n A 1 336 ARG 336 336 ? ? ? A . n A 1 337 MET 337 337 ? ? ? A . n A 1 338 LYS 338 338 ? ? ? A . n A 1 339 ASN 339 339 ? ? ? A . n A 1 340 ASN 340 340 ? ? ? A . n A 1 341 GLU 341 341 ? ? ? A . n A 1 342 GLU 342 342 ? ? ? A . n A 1 343 ALA 343 343 ? ? ? A . n A 1 344 GLU 344 344 ? ? ? A . n A 1 345 ASP 345 345 ? ? ? A . n A 1 346 TYR 346 346 ? ? ? A . n A 1 347 ASP 347 347 ? ? ? A . n A 1 348 ASP 348 348 ? ? ? A . n A 1 349 ASP 349 349 ? ? ? A . n A 1 350 LEU 350 350 ? ? ? A . n A 1 351 THR 351 351 ? ? ? A . n A 1 352 ASP 352 352 ? ? ? A . n A 1 353 SER 353 353 ? ? ? A . n A 1 354 GLU 354 354 ? ? ? A . n A 1 355 MET 355 355 ? ? ? A . n A 1 356 ASP 356 356 ? ? ? A . n A 1 357 VAL 357 357 ? ? ? A . n A 1 358 VAL 358 358 ? ? ? A . n A 1 359 ARG 359 359 ? ? ? A . n A 1 360 PHE 360 360 ? ? ? A . n A 1 361 ASP 361 361 ? ? ? A . n A 1 362 ASP 362 362 ? ? ? A . n A 1 363 ASP 363 363 ? ? ? A . n A 1 364 ASN 364 364 ? ? ? A . n A 1 365 SER 365 365 ? ? ? A . n A 1 366 PRO 366 366 ? ? ? A . n A 1 367 SER 367 367 ? ? ? A . n A 1 368 PHE 368 368 ? ? ? A . n A 1 369 ILE 369 369 ? ? ? A . n A 1 370 GLN 370 370 ? ? ? A . n A 1 371 ILE 371 371 ? ? ? A . n A 1 372 ARG 372 372 ? ? ? A . n A 1 373 SER 373 373 ? ? ? A . n A 1 374 VAL 374 374 ? ? ? A . n A 1 375 ALA 375 375 ? ? ? A . n A 1 376 LYS 376 376 ? ? ? A . n A 1 377 LYS 377 377 377 LYS LYS A . n A 1 378 HIS 378 378 378 HIS HIS A . n A 1 379 PRO 379 379 379 PRO PRO A . n A 1 380 LYS 380 380 380 LYS LYS A . n A 1 381 THR 381 381 381 THR THR A . n A 1 382 TRP 382 382 382 TRP TRP A . n A 1 383 VAL 383 383 383 VAL VAL A . n A 1 384 HIS 384 384 384 HIS HIS A . n A 1 385 TYR 385 385 385 TYR TYR A . n A 1 386 ILE 386 386 386 ILE ILE A . n A 1 387 ALA 387 387 387 ALA ALA A . n A 1 388 ALA 388 388 388 ALA ALA A . n A 1 389 GLU 389 389 389 GLU GLU A . n A 1 390 GLU 390 390 390 GLU GLU A . n A 1 391 GLU 391 391 391 GLU GLU A . n A 1 392 ASP 392 392 392 ASP ASP A . n A 1 393 TRP 393 393 393 TRP TRP A . n A 1 394 ASP 394 394 394 ASP ASP A . n A 1 395 TYR 395 395 395 TYR TYR A . n A 1 396 ALA 396 396 396 ALA ALA A . n A 1 397 PRO 397 397 397 PRO PRO A . n A 1 398 LEU 398 398 398 LEU LEU A . n A 1 399 VAL 399 399 399 VAL VAL A . n A 1 400 LEU 400 400 400 LEU LEU A . n A 1 401 ALA 401 401 401 ALA ALA A . n A 1 402 PRO 402 402 402 PRO PRO A . n A 1 403 ASP 403 403 403 ASP ASP A . n A 1 404 ASP 404 404 404 ASP ASP A . n A 1 405 ARG 405 405 405 ARG ARG A . n A 1 406 SER 406 406 406 SER SER A . n A 1 407 TYR 407 407 407 TYR TYR A . n A 1 408 LYS 408 408 408 LYS LYS A . n A 1 409 SER 409 409 409 SER SER A . n A 1 410 GLN 410 410 410 GLN GLN A . n A 1 411 TYR 411 411 411 TYR TYR A . n A 1 412 LEU 412 412 412 LEU LEU A . n A 1 413 ASN 413 413 413 ASN ASN A . n A 1 414 ASN 414 414 414 ASN ASN A . n A 1 415 GLY 415 415 415 GLY GLY A . n A 1 416 PRO 416 416 416 PRO PRO A . n A 1 417 GLN 417 417 417 GLN GLN A . n A 1 418 ARG 418 418 418 ARG ARG A . n A 1 419 ILE 419 419 419 ILE ILE A . n A 1 420 GLY 420 420 420 GLY GLY A . n A 1 421 ARG 421 421 421 ARG ARG A . n A 1 422 LYS 422 422 422 LYS LYS A . n A 1 423 TYR 423 423 423 TYR TYR A . n A 1 424 LYS 424 424 424 LYS LYS A . n A 1 425 LYS 425 425 425 LYS LYS A . n A 1 426 VAL 426 426 426 VAL VAL A . n A 1 427 ARG 427 427 427 ARG ARG A . n A 1 428 PHE 428 428 428 PHE PHE A . n A 1 429 MET 429 429 429 MET MET A . n A 1 430 ALA 430 430 430 ALA ALA A . n A 1 431 TYR 431 431 431 TYR TYR A . n A 1 432 THR 432 432 432 THR THR A . n A 1 433 ASP 433 433 433 ASP ASP A . n A 1 434 GLU 434 434 434 GLU GLU A . n A 1 435 THR 435 435 435 THR THR A . n A 1 436 PHE 436 436 436 PHE PHE A . n A 1 437 LYS 437 437 437 LYS LYS A . n A 1 438 THR 438 438 438 THR THR A . n A 1 439 ARG 439 439 439 ARG ARG A . n A 1 440 GLU 440 440 440 GLU GLU A . n A 1 441 ALA 441 441 441 ALA ALA A . n A 1 442 ILE 442 442 442 ILE ILE A . n A 1 443 GLN 443 443 443 GLN GLN A . n A 1 444 HIS 444 444 444 HIS HIS A . n A 1 445 GLU 445 445 445 GLU GLU A . n A 1 446 SER 446 446 446 SER SER A . n A 1 447 GLY 447 447 447 GLY GLY A . n A 1 448 ILE 448 448 448 ILE ILE A . n A 1 449 LEU 449 449 449 LEU LEU A . n A 1 450 GLY 450 450 450 GLY GLY A . n A 1 451 PRO 451 451 451 PRO PRO A . n A 1 452 LEU 452 452 452 LEU LEU A . n A 1 453 LEU 453 453 453 LEU LEU A . n A 1 454 TYR 454 454 454 TYR TYR A . n A 1 455 GLY 455 455 455 GLY GLY A . n A 1 456 GLU 456 456 456 GLU GLU A . n A 1 457 VAL 457 457 457 VAL VAL A . n A 1 458 GLY 458 458 458 GLY GLY A . n A 1 459 ASP 459 459 459 ASP ASP A . n A 1 460 THR 460 460 460 THR THR A . n A 1 461 LEU 461 461 461 LEU LEU A . n A 1 462 LEU 462 462 462 LEU LEU A . n A 1 463 ILE 463 463 463 ILE ILE A . n A 1 464 ILE 464 464 464 ILE ILE A . n A 1 465 PHE 465 465 465 PHE PHE A . n A 1 466 LYS 466 466 466 LYS LYS A . n A 1 467 ASN 467 467 467 ASN ASN A . n A 1 468 GLN 468 468 468 GLN GLN A . n A 1 469 ALA 469 469 469 ALA ALA A . n A 1 470 SER 470 470 470 SER SER A . n A 1 471 ARG 471 471 471 ARG ARG A . n A 1 472 PRO 472 472 472 PRO PRO A . n A 1 473 TYR 473 473 473 TYR TYR A . n A 1 474 ASN 474 474 474 ASN ASN A . n A 1 475 ILE 475 475 475 ILE ILE A . n A 1 476 TYR 476 476 476 TYR TYR A . n A 1 477 PRO 477 477 477 PRO PRO A . n A 1 478 HIS 478 478 478 HIS HIS A . n A 1 479 GLY 479 479 479 GLY GLY A . n A 1 480 ILE 480 480 480 ILE ILE A . n A 1 481 THR 481 481 481 THR THR A . n A 1 482 ASP 482 482 482 ASP ASP A . n A 1 483 VAL 483 483 483 VAL VAL A . n A 1 484 ARG 484 484 484 ARG ARG A . n A 1 485 PRO 485 485 485 PRO PRO A . n A 1 486 LEU 486 486 486 LEU LEU A . n A 1 487 TYR 487 487 487 TYR TYR A . n A 1 488 SER 488 488 488 SER SER A . n A 1 489 ARG 489 489 489 ARG ARG A . n A 1 490 ARG 490 490 490 ARG ARG A . n A 1 491 LEU 491 491 491 LEU LEU A . n A 1 492 PRO 492 492 492 PRO PRO A . n A 1 493 LYS 493 493 493 LYS LYS A . n A 1 494 GLY 494 494 494 GLY GLY A . n A 1 495 VAL 495 495 495 VAL VAL A . n A 1 496 LYS 496 496 496 LYS LYS A . n A 1 497 HIS 497 497 497 HIS HIS A . n A 1 498 LEU 498 498 498 LEU LEU A . n A 1 499 LYS 499 499 499 LYS LYS A . n A 1 500 ASP 500 500 500 ASP ASP A . n A 1 501 PHE 501 501 501 PHE PHE A . n A 1 502 PRO 502 502 502 PRO PRO A . n A 1 503 ILE 503 503 503 ILE ILE A . n A 1 504 LEU 504 504 504 LEU LEU A . n A 1 505 PRO 505 505 505 PRO PRO A . n A 1 506 GLY 506 506 506 GLY GLY A . n A 1 507 GLU 507 507 507 GLU GLU A . n A 1 508 ILE 508 508 508 ILE ILE A . n A 1 509 PHE 509 509 509 PHE PHE A . n A 1 510 LYS 510 510 510 LYS LYS A . n A 1 511 TYR 511 511 511 TYR TYR A . n A 1 512 LYS 512 512 512 LYS LYS A . n A 1 513 TRP 513 513 513 TRP TRP A . n A 1 514 THR 514 514 514 THR THR A . n A 1 515 VAL 515 515 515 VAL VAL A . n A 1 516 THR 516 516 516 THR THR A . n A 1 517 VAL 517 517 517 VAL VAL A . n A 1 518 GLU 518 518 518 GLU GLU A . n A 1 519 ASP 519 519 519 ASP ASP A . n A 1 520 GLY 520 520 520 GLY GLY A . n A 1 521 PRO 521 521 521 PRO PRO A . n A 1 522 THR 522 522 522 THR THR A . n A 1 523 LYS 523 523 523 LYS LYS A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 ASP 525 525 525 ASP ASP A . n A 1 526 PRO 526 526 526 PRO PRO A . n A 1 527 ARG 527 527 527 ARG ARG A . n A 1 528 CYS 528 528 528 CYS CYS A . n A 1 529 LEU 529 529 529 LEU LEU A . n A 1 530 THR 530 530 530 THR THR A . n A 1 531 ARG 531 531 531 ARG ARG A . n A 1 532 TYR 532 532 532 TYR TYR A . n A 1 533 TYR 533 533 533 TYR TYR A . n A 1 534 SER 534 534 534 SER SER A . n A 1 535 SER 535 535 535 SER SER A . n A 1 536 PHE 536 536 536 PHE PHE A . n A 1 537 VAL 537 537 537 VAL VAL A . n A 1 538 ASN 538 538 538 ASN ASN A . n A 1 539 MET 539 539 539 MET MET A . n A 1 540 GLU 540 540 540 GLU GLU A . n A 1 541 ARG 541 541 541 ARG ARG A . n A 1 542 ASP 542 542 542 ASP ASP A . n A 1 543 LEU 543 543 543 LEU LEU A . n A 1 544 ALA 544 544 544 ALA ALA A . n A 1 545 SER 545 545 545 SER SER A . n A 1 546 GLY 546 546 546 GLY GLY A . n A 1 547 LEU 547 547 547 LEU LEU A . n A 1 548 ILE 548 548 548 ILE ILE A . n A 1 549 GLY 549 549 549 GLY GLY A . n A 1 550 PRO 550 550 550 PRO PRO A . n A 1 551 LEU 551 551 551 LEU LEU A . n A 1 552 LEU 552 552 552 LEU LEU A . n A 1 553 ILE 553 553 553 ILE ILE A . n A 1 554 CYS 554 554 554 CYS CYS A . n A 1 555 TYR 555 555 555 TYR TYR A . n A 1 556 LYS 556 556 556 LYS LYS A . n A 1 557 GLU 557 557 557 GLU GLU A . n A 1 558 SER 558 558 ? ? ? A . n A 1 559 VAL 559 559 ? ? ? A . n A 1 560 ASP 560 560 ? ? ? A . n A 1 561 GLN 561 561 ? ? ? A . n A 1 562 ARG 562 562 ? ? ? A . n A 1 563 GLY 563 563 ? ? ? A . n A 1 564 ASN 564 564 ? ? ? A . n A 1 565 GLN 565 565 ? ? ? A . n A 1 566 ILE 566 566 ? ? ? A . n A 1 567 MET 567 567 ? ? ? A . n A 1 568 SER 568 568 ? ? ? A . n A 1 569 ASP 569 569 ? ? ? A . n A 1 570 LYS 570 570 ? ? ? A . n A 1 571 ARG 571 571 571 ARG ARG A . n A 1 572 ASN 572 572 572 ASN ASN A . n A 1 573 VAL 573 573 573 VAL VAL A . n A 1 574 ILE 574 574 574 ILE ILE A . n A 1 575 LEU 575 575 575 LEU LEU A . n A 1 576 PHE 576 576 576 PHE PHE A . n A 1 577 SER 577 577 577 SER SER A . n A 1 578 VAL 578 578 578 VAL VAL A . n A 1 579 PHE 579 579 579 PHE PHE A . n A 1 580 ASP 580 580 580 ASP ASP A . n A 1 581 GLU 581 581 581 GLU GLU A . n A 1 582 ASN 582 582 582 ASN ASN A . n A 1 583 ARG 583 583 583 ARG ARG A . n A 1 584 SER 584 584 584 SER SER A . n A 1 585 TRP 585 585 585 TRP TRP A . n A 1 586 TYR 586 586 586 TYR TYR A . n A 1 587 LEU 587 587 587 LEU LEU A . n A 1 588 THR 588 588 588 THR THR A . n A 1 589 GLU 589 589 589 GLU GLU A . n A 1 590 ASN 590 590 590 ASN ASN A . n A 1 591 ILE 591 591 591 ILE ILE A . n A 1 592 GLN 592 592 592 GLN GLN A . n A 1 593 ARG 593 593 593 ARG ARG A . n A 1 594 PHE 594 594 594 PHE PHE A . n A 1 595 LEU 595 595 595 LEU LEU A . n A 1 596 PRO 596 596 596 PRO PRO A . n A 1 597 ASN 597 597 597 ASN ASN A . n A 1 598 PRO 598 598 598 PRO PRO A . n A 1 599 ALA 599 599 599 ALA ALA A . n A 1 600 GLY 600 600 600 GLY GLY A . n A 1 601 VAL 601 601 601 VAL VAL A . n A 1 602 GLN 602 602 602 GLN GLN A . n A 1 603 LEU 603 603 603 LEU LEU A . n A 1 604 GLU 604 604 604 GLU GLU A . n A 1 605 ASP 605 605 605 ASP ASP A . n A 1 606 PRO 606 606 606 PRO PRO A . n A 1 607 GLU 607 607 607 GLU GLU A . n A 1 608 PHE 608 608 608 PHE PHE A . n A 1 609 GLN 609 609 609 GLN GLN A . n A 1 610 ALA 610 610 610 ALA ALA A . n A 1 611 SER 611 611 611 SER SER A . n A 1 612 ASN 612 612 612 ASN ASN A . n A 1 613 ILE 613 613 613 ILE ILE A . n A 1 614 MET 614 614 614 MET MET A . n A 1 615 HIS 615 615 615 HIS HIS A . n A 1 616 SER 616 616 616 SER SER A . n A 1 617 ILE 617 617 617 ILE ILE A . n A 1 618 ASN 618 618 618 ASN ASN A . n A 1 619 GLY 619 619 619 GLY GLY A . n A 1 620 TYR 620 620 620 TYR TYR A . n A 1 621 VAL 621 621 621 VAL VAL A . n A 1 622 PHE 622 622 622 PHE PHE A . n A 1 623 ASP 623 623 623 ASP ASP A . n A 1 624 SER 624 624 624 SER SER A . n A 1 625 LEU 625 625 625 LEU LEU A . n A 1 626 GLN 626 626 626 GLN GLN A . n A 1 627 LEU 627 627 627 LEU LEU A . n A 1 628 SER 628 628 628 SER SER A . n A 1 629 VAL 629 629 629 VAL VAL A . n A 1 630 CYS 630 630 630 CYS CYS A . n A 1 631 LEU 631 631 631 LEU LEU A . n A 1 632 HIS 632 632 632 HIS HIS A . n A 1 633 GLU 633 633 633 GLU GLU A . n A 1 634 VAL 634 634 634 VAL VAL A . n A 1 635 ALA 635 635 635 ALA ALA A . n A 1 636 TYR 636 636 636 TYR TYR A . n A 1 637 TRP 637 637 637 TRP TRP A . n A 1 638 TYR 638 638 638 TYR TYR A . n A 1 639 ILE 639 639 639 ILE ILE A . n A 1 640 LEU 640 640 640 LEU LEU A . n A 1 641 SER 641 641 641 SER SER A . n A 1 642 ILE 642 642 642 ILE ILE A . n A 1 643 GLY 643 643 643 GLY GLY A . n A 1 644 ALA 644 644 644 ALA ALA A . n A 1 645 GLN 645 645 645 GLN GLN A . n A 1 646 THR 646 646 646 THR THR A . n A 1 647 ASP 647 647 647 ASP ASP A . n A 1 648 PHE 648 648 648 PHE PHE A . n A 1 649 LEU 649 649 649 LEU LEU A . n A 1 650 SER 650 650 650 SER SER A . n A 1 651 VAL 651 651 651 VAL VAL A . n A 1 652 PHE 652 652 652 PHE PHE A . n A 1 653 PHE 653 653 653 PHE PHE A . n A 1 654 SER 654 654 654 SER SER A . n A 1 655 GLY 655 655 655 GLY GLY A . n A 1 656 TYR 656 656 656 TYR TYR A . n A 1 657 THR 657 657 657 THR THR A . n A 1 658 PHE 658 658 658 PHE PHE A . n A 1 659 LYS 659 659 659 LYS LYS A . n A 1 660 HIS 660 660 660 HIS HIS A . n A 1 661 LYS 661 661 661 LYS LYS A . n A 1 662 MET 662 662 662 MET MET A . n A 1 663 VAL 663 663 663 VAL VAL A . n A 1 664 TYR 664 664 664 TYR TYR A . n A 1 665 GLU 665 665 665 GLU GLU A . n A 1 666 ASP 666 666 666 ASP ASP A . n A 1 667 THR 667 667 667 THR THR A . n A 1 668 LEU 668 668 668 LEU LEU A . n A 1 669 THR 669 669 669 THR THR A . n A 1 670 LEU 670 670 670 LEU LEU A . n A 1 671 PHE 671 671 671 PHE PHE A . n A 1 672 PRO 672 672 672 PRO PRO A . n A 1 673 PHE 673 673 673 PHE PHE A . n A 1 674 SER 674 674 674 SER SER A . n A 1 675 GLY 675 675 675 GLY GLY A . n A 1 676 GLU 676 676 676 GLU GLU A . n A 1 677 THR 677 677 677 THR THR A . n A 1 678 VAL 678 678 678 VAL VAL A . n A 1 679 PHE 679 679 679 PHE PHE A . n A 1 680 MET 680 680 680 MET MET A . n A 1 681 SER 681 681 681 SER SER A . n A 1 682 MET 682 682 682 MET MET A . n A 1 683 GLU 683 683 683 GLU GLU A . n A 1 684 ASN 684 684 684 ASN ASN A . n A 1 685 PRO 685 685 685 PRO PRO A . n A 1 686 GLY 686 686 686 GLY GLY A . n A 1 687 LEU 687 687 687 LEU LEU A . n A 1 688 TRP 688 688 688 TRP TRP A . n A 1 689 ILE 689 689 689 ILE ILE A . n A 1 690 LEU 690 690 690 LEU LEU A . n A 1 691 GLY 691 691 691 GLY GLY A . n A 1 692 CYS 692 692 692 CYS CYS A . n A 1 693 HIS 693 693 693 HIS HIS A . n A 1 694 ASN 694 694 694 ASN ASN A . n A 1 695 SER 695 695 695 SER SER A . n A 1 696 ASP 696 696 696 ASP ASP A . n A 1 697 PHE 697 697 697 PHE PHE A . n A 1 698 ARG 698 698 698 ARG ARG A . n A 1 699 ASN 699 699 699 ASN ASN A . n A 1 700 ARG 700 700 700 ARG ARG A . n A 1 701 GLY 701 701 701 GLY GLY A . n A 1 702 MET 702 702 702 MET MET A . n A 1 703 THR 703 703 703 THR THR A . n A 1 704 ALA 704 704 704 ALA ALA A . n A 1 705 LEU 705 705 705 LEU LEU A . n A 1 706 LEU 706 706 706 LEU LEU A . n A 1 707 LYS 707 707 707 LYS LYS A . n A 1 708 VAL 708 708 708 VAL VAL A . n A 1 709 SER 709 709 709 SER SER A . n A 1 710 SER 710 710 710 SER SER A . n A 1 711 CYS 711 711 711 CYS CYS A . n A 1 712 ASP 712 712 712 ASP ASP A . n A 1 713 LYS 713 713 713 LYS LYS A . n A 1 714 ASN 714 714 ? ? ? A . n A 1 715 THR 715 715 ? ? ? A . n A 1 716 GLY 716 716 ? ? ? A . n A 1 717 ASP 717 717 ? ? ? A . n A 1 718 TYR 718 718 ? ? ? A . n A 1 719 TYR 719 719 ? ? ? A . n A 1 720 GLU 720 720 ? ? ? A . n A 1 721 ASP 721 721 ? ? ? A . n A 1 722 SER 722 722 ? ? ? A . n A 1 723 TYR 723 723 ? ? ? A . n A 1 724 GLU 724 724 ? ? ? A . n A 1 725 ASP 725 725 ? ? ? A . n A 1 726 ILE 726 726 ? ? ? A . n A 1 727 SER 727 727 ? ? ? A . n A 1 728 ALA 728 728 ? ? ? A . n A 1 729 TYR 729 729 ? ? ? A . n A 1 730 LEU 730 730 ? ? ? A . n A 1 731 LEU 731 731 ? ? ? A . n A 1 732 SER 732 732 ? ? ? A . n A 1 733 LYS 733 733 ? ? ? A . n A 1 734 ASN 734 734 ? ? ? A . n A 1 735 ASN 735 735 ? ? ? A . n A 1 736 ALA 736 736 ? ? ? A . n A 1 737 ILE 737 737 ? ? ? A . n A 1 738 GLU 738 738 ? ? ? A . n A 1 739 PRO 739 739 ? ? ? A . n A 1 740 ARG 740 740 ? ? ? A . n A 1 741 SER 741 741 ? ? ? A . n A 1 742 PHE 742 742 ? ? ? A . n A 1 743 SER 743 743 ? ? ? A . n A 1 744 GLN 744 744 ? ? ? A . n A 1 745 ASN 745 745 ? ? ? A . n A 1 746 SER 746 746 ? ? ? A . n A 1 747 ARG 747 747 ? ? ? A . n A 1 748 HIS 748 748 ? ? ? A . n A 1 749 PRO 749 749 ? ? ? A . n A 1 750 SER 750 750 ? ? ? A . n A 1 751 GLN 751 751 ? ? ? A . n A 1 752 ASN 752 752 ? ? ? A . n A 1 753 PRO 753 753 ? ? ? A . n A 1 754 PRO 754 754 ? ? ? A . n A 1 755 VAL 755 755 ? ? ? A . n A 1 756 LEU 756 756 ? ? ? A . n A 1 757 LYS 757 757 ? ? ? A . n A 1 758 ARG 758 758 ? ? ? A . n A 1 759 HIS 759 759 ? ? ? A . n A 1 760 GLN 760 760 ? ? ? A . n B 2 1 ARG 1 1648 ? ? ? B . n B 2 2 GLU 2 1649 ? ? ? B . n B 2 3 ILE 3 1650 ? ? ? B . n B 2 4 THR 4 1651 ? ? ? B . n B 2 5 ARG 5 1652 ? ? ? B . n B 2 6 THR 6 1653 ? ? ? B . n B 2 7 THR 7 1654 ? ? ? B . n B 2 8 LEU 8 1655 ? ? ? B . n B 2 9 GLN 9 1656 ? ? ? B . n B 2 10 SER 10 1657 ? ? ? B . n B 2 11 ASP 11 1658 ? ? ? B . n B 2 12 GLN 12 1659 ? ? ? B . n B 2 13 GLU 13 1660 ? ? ? B . n B 2 14 GLU 14 1661 ? ? ? B . n B 2 15 ILE 15 1662 ? ? ? B . n B 2 16 ASP 16 1663 ? ? ? B . n B 2 17 TYR 17 1664 ? ? ? B . n B 2 18 ASP 18 1665 ? ? ? B . n B 2 19 ASP 19 1666 ? ? ? B . n B 2 20 THR 20 1667 ? ? ? B . n B 2 21 ILE 21 1668 ? ? ? B . n B 2 22 SER 22 1669 ? ? ? B . n B 2 23 VAL 23 1670 ? ? ? B . n B 2 24 GLU 24 1671 ? ? ? B . n B 2 25 MET 25 1672 ? ? ? B . n B 2 26 LYS 26 1673 ? ? ? B . n B 2 27 LYS 27 1674 ? ? ? B . n B 2 28 GLU 28 1675 ? ? ? B . n B 2 29 ASP 29 1676 ? ? ? B . n B 2 30 PHE 30 1677 ? ? ? B . n B 2 31 ASP 31 1678 ? ? ? B . n B 2 32 ILE 32 1679 ? ? ? B . n B 2 33 TYR 33 1680 ? ? ? B . n B 2 34 ASP 34 1681 ? ? ? B . n B 2 35 GLU 35 1682 ? ? ? B . n B 2 36 ASP 36 1683 ? ? ? B . n B 2 37 GLU 37 1684 ? ? ? B . n B 2 38 ASN 38 1685 ? ? ? B . n B 2 39 GLN 39 1686 ? ? ? B . n B 2 40 SER 40 1687 ? ? ? B . n B 2 41 PRO 41 1688 ? ? ? B . n B 2 42 ARG 42 1689 ? ? ? B . n B 2 43 SER 43 1690 ? ? ? B . n B 2 44 PHE 44 1691 ? ? ? B . n B 2 45 GLN 45 1692 ? ? ? B . n B 2 46 LYS 46 1693 1693 LYS LYS B . n B 2 47 LYS 47 1694 1694 LYS LYS B . n B 2 48 THR 48 1695 1695 THR THR B . n B 2 49 ARG 49 1696 1696 ARG ARG B . n B 2 50 HIS 50 1697 1697 HIS HIS B . n B 2 51 TYR 51 1698 1698 TYR TYR B . n B 2 52 PHE 52 1699 1699 PHE PHE B . n B 2 53 ILE 53 1700 1700 ILE ILE B . n B 2 54 ALA 54 1701 1701 ALA ALA B . n B 2 55 ALA 55 1702 1702 ALA ALA B . n B 2 56 VAL 56 1703 1703 VAL VAL B . n B 2 57 GLU 57 1704 1704 GLU GLU B . n B 2 58 ARG 58 1705 1705 ARG ARG B . n B 2 59 LEU 59 1706 1706 LEU LEU B . n B 2 60 TRP 60 1707 1707 TRP TRP B . n B 2 61 ASP 61 1708 1708 ASP ASP B . n B 2 62 TYR 62 1709 1709 TYR TYR B . n B 2 63 GLY 63 1710 1710 GLY GLY B . n B 2 64 MET 64 1711 1711 MET MET B . n B 2 65 SER 65 1712 1712 SER SER B . n B 2 66 SER 66 1713 1713 SER SER B . n B 2 67 SER 67 1714 ? ? ? B . n B 2 68 PRO 68 1715 ? ? ? B . n B 2 69 HIS 69 1716 ? ? ? B . n B 2 70 VAL 70 1717 ? ? ? B . n B 2 71 LEU 71 1718 ? ? ? B . n B 2 72 ARG 72 1719 ? ? ? B . n B 2 73 ASN 73 1720 ? ? ? B . n B 2 74 ARG 74 1721 ? ? ? B . n B 2 75 ALA 75 1722 ? ? ? B . n B 2 76 GLN 76 1723 ? ? ? B . n B 2 77 SER 77 1724 ? ? ? B . n B 2 78 GLY 78 1725 ? ? ? B . n B 2 79 SER 79 1726 1726 SER SER B . n B 2 80 VAL 80 1727 1727 VAL VAL B . n B 2 81 PRO 81 1728 1728 PRO PRO B . n B 2 82 GLN 82 1729 1729 GLN GLN B . n B 2 83 PHE 83 1730 1730 PHE PHE B . n B 2 84 LYS 84 1731 1731 LYS LYS B . n B 2 85 LYS 85 1732 1732 LYS LYS B . n B 2 86 VAL 86 1733 1733 VAL VAL B . n B 2 87 VAL 87 1734 1734 VAL VAL B . n B 2 88 PHE 88 1735 1735 PHE PHE B . n B 2 89 GLN 89 1736 1736 GLN GLN B . n B 2 90 GLU 90 1737 1737 GLU GLU B . n B 2 91 PHE 91 1738 1738 PHE PHE B . n B 2 92 THR 92 1739 1739 THR THR B . n B 2 93 ASP 93 1740 1740 ASP ASP B . n B 2 94 GLY 94 1741 1741 GLY GLY B . n B 2 95 SER 95 1742 1742 SER SER B . n B 2 96 PHE 96 1743 1743 PHE PHE B . n B 2 97 THR 97 1744 1744 THR THR B . n B 2 98 GLN 98 1745 1745 GLN GLN B . n B 2 99 PRO 99 1746 1746 PRO PRO B . n B 2 100 LEU 100 1747 1747 LEU LEU B . n B 2 101 TYR 101 1748 1748 TYR TYR B . n B 2 102 ARG 102 1749 1749 ARG ARG B . n B 2 103 GLY 103 1750 1750 GLY GLY B . n B 2 104 GLU 104 1751 1751 GLU GLU B . n B 2 105 LEU 105 1752 1752 LEU LEU B . n B 2 106 ASN 106 1753 1753 ASN ASN B . n B 2 107 GLU 107 1754 1754 GLU GLU B . n B 2 108 HIS 108 1755 1755 HIS HIS B . n B 2 109 LEU 109 1756 1756 LEU LEU B . n B 2 110 GLY 110 1757 1757 GLY GLY B . n B 2 111 LEU 111 1758 1758 LEU LEU B . n B 2 112 LEU 112 1759 1759 LEU LEU B . n B 2 113 GLY 113 1760 1760 GLY GLY B . n B 2 114 PRO 114 1761 1761 PRO PRO B . n B 2 115 TYR 115 1762 1762 TYR TYR B . n B 2 116 ILE 116 1763 1763 ILE ILE B . n B 2 117 ARG 117 1764 1764 ARG ARG B . n B 2 118 ALA 118 1765 1765 ALA ALA B . n B 2 119 GLU 119 1766 1766 GLU GLU B . n B 2 120 VAL 120 1767 1767 VAL VAL B . n B 2 121 GLU 121 1768 1768 GLU GLU B . n B 2 122 ASP 122 1769 1769 ASP ASP B . n B 2 123 ASN 123 1770 1770 ASN ASN B . n B 2 124 ILE 124 1771 1771 ILE ILE B . n B 2 125 MET 125 1772 1772 MET MET B . n B 2 126 VAL 126 1773 1773 VAL VAL B . n B 2 127 THR 127 1774 1774 THR THR B . n B 2 128 PHE 128 1775 1775 PHE PHE B . n B 2 129 ARG 129 1776 1776 ARG ARG B . n B 2 130 ASN 130 1777 1777 ASN ASN B . n B 2 131 GLN 131 1778 1778 GLN GLN B . n B 2 132 ALA 132 1779 1779 ALA ALA B . n B 2 133 SER 133 1780 1780 SER SER B . n B 2 134 ARG 134 1781 1781 ARG ARG B . n B 2 135 PRO 135 1782 1782 PRO PRO B . n B 2 136 TYR 136 1783 1783 TYR TYR B . n B 2 137 SER 137 1784 1784 SER SER B . n B 2 138 PHE 138 1785 1785 PHE PHE B . n B 2 139 TYR 139 1786 1786 TYR TYR B . n B 2 140 SER 140 1787 1787 SER SER B . n B 2 141 SER 141 1788 1788 SER SER B . n B 2 142 LEU 142 1789 1789 LEU LEU B . n B 2 143 ILE 143 1790 1790 ILE ILE B . n B 2 144 SER 144 1791 1791 SER SER B . n B 2 145 TYR 145 1792 1792 TYR TYR B . n B 2 146 GLU 146 1793 1793 GLU GLU B . n B 2 147 GLU 147 1794 1794 GLU GLU B . n B 2 148 ASP 148 1795 1795 ASP ASP B . n B 2 149 GLN 149 1796 ? ? ? B . n B 2 150 ARG 150 1797 ? ? ? B . n B 2 151 GLN 151 1798 ? ? ? B . n B 2 152 GLY 152 1799 ? ? ? B . n B 2 153 ALA 153 1800 ? ? ? B . n B 2 154 GLU 154 1801 ? ? ? B . n B 2 155 PRO 155 1802 1802 PRO PRO B . n B 2 156 ARG 156 1803 1803 ARG ARG B . n B 2 157 LYS 157 1804 1804 LYS LYS B . n B 2 158 ASN 158 1805 1805 ASN ASN B . n B 2 159 PHE 159 1806 1806 PHE PHE B . n B 2 160 VAL 160 1807 1807 VAL VAL B . n B 2 161 LYS 161 1808 1808 LYS LYS B . n B 2 162 PRO 162 1809 1809 PRO PRO B . n B 2 163 ASN 163 1810 1810 ASN ASN B . n B 2 164 GLU 164 1811 1811 GLU GLU B . n B 2 165 THR 165 1812 1812 THR THR B . n B 2 166 LYS 166 1813 1813 LYS LYS B . n B 2 167 THR 167 1814 1814 THR THR B . n B 2 168 TYR 168 1815 1815 TYR TYR B . n B 2 169 PHE 169 1816 1816 PHE PHE B . n B 2 170 TRP 170 1817 1817 TRP TRP B . n B 2 171 LYS 171 1818 1818 LYS LYS B . n B 2 172 VAL 172 1819 1819 VAL VAL B . n B 2 173 GLN 173 1820 1820 GLN GLN B . n B 2 174 HIS 174 1821 1821 HIS HIS B . n B 2 175 HIS 175 1822 1822 HIS HIS B . n B 2 176 MET 176 1823 1823 MET MET B . n B 2 177 ALA 177 1824 1824 ALA ALA B . n B 2 178 PRO 178 1825 1825 PRO PRO B . n B 2 179 THR 179 1826 1826 THR THR B . n B 2 180 LYS 180 1827 1827 LYS LYS B . n B 2 181 ASP 181 1828 1828 ASP ASP B . n B 2 182 GLU 182 1829 1829 GLU GLU B . n B 2 183 PHE 183 1830 1830 PHE PHE B . n B 2 184 ASP 184 1831 1831 ASP ASP B . n B 2 185 CYS 185 1832 1832 CYS CYS B . n B 2 186 LYS 186 1833 1833 LYS LYS B . n B 2 187 ALA 187 1834 1834 ALA ALA B . n B 2 188 TRP 188 1835 1835 TRP TRP B . n B 2 189 ALA 189 1836 1836 ALA ALA B . n B 2 190 TYR 190 1837 1837 TYR TYR B . n B 2 191 PHE 191 1838 1838 PHE PHE B . n B 2 192 SER 192 1839 1839 SER SER B . n B 2 193 ASP 193 1840 1840 ASP ASP B . n B 2 194 VAL 194 1841 1841 VAL VAL B . n B 2 195 ASP 195 1842 1842 ASP ASP B . n B 2 196 LEU 196 1843 1843 LEU LEU B . n B 2 197 GLU 197 1844 1844 GLU GLU B . n B 2 198 LYS 198 1845 1845 LYS LYS B . n B 2 199 ASP 199 1846 1846 ASP ASP B . n B 2 200 VAL 200 1847 1847 VAL VAL B . n B 2 201 HIS 201 1848 1848 HIS HIS B . n B 2 202 SER 202 1849 1849 SER SER B . n B 2 203 GLY 203 1850 1850 GLY GLY B . n B 2 204 LEU 204 1851 1851 LEU LEU B . n B 2 205 ILE 205 1852 1852 ILE ILE B . n B 2 206 GLY 206 1853 1853 GLY GLY B . n B 2 207 PRO 207 1854 1854 PRO PRO B . n B 2 208 LEU 208 1855 1855 LEU LEU B . n B 2 209 LEU 209 1856 1856 LEU LEU B . n B 2 210 VAL 210 1857 1857 VAL VAL B . n B 2 211 CYS 211 1858 1858 CYS CYS B . n B 2 212 HIS 212 1859 1859 HIS HIS B . n B 2 213 THR 213 1860 1860 THR THR B . n B 2 214 ASN 214 1861 1861 ASN ASN B . n B 2 215 THR 215 1862 1862 THR THR B . n B 2 216 LEU 216 1863 1863 LEU LEU B . n B 2 217 ASN 217 1864 1864 ASN ASN B . n B 2 218 PRO 218 1865 1865 PRO PRO B . n B 2 219 ALA 219 1866 1866 ALA ALA B . n B 2 220 HIS 220 1867 1867 HIS HIS B . n B 2 221 GLY 221 1868 1868 GLY GLY B . n B 2 222 ARG 222 1869 1869 ARG ARG B . n B 2 223 GLN 223 1870 1870 GLN GLN B . n B 2 224 VAL 224 1871 1871 VAL VAL B . n B 2 225 THR 225 1872 1872 THR THR B . n B 2 226 VAL 226 1873 1873 VAL VAL B . n B 2 227 GLN 227 1874 1874 GLN GLN B . n B 2 228 GLU 228 1875 1875 GLU GLU B . n B 2 229 PHE 229 1876 1876 PHE PHE B . n B 2 230 ALA 230 1877 1877 ALA ALA B . n B 2 231 LEU 231 1878 1878 LEU LEU B . n B 2 232 PHE 232 1879 1879 PHE PHE B . n B 2 233 PHE 233 1880 1880 PHE PHE B . n B 2 234 THR 234 1881 1881 THR THR B . n B 2 235 ILE 235 1882 1882 ILE ILE B . n B 2 236 PHE 236 1883 1883 PHE PHE B . n B 2 237 ASP 237 1884 1884 ASP ASP B . n B 2 238 GLU 238 1885 1885 GLU GLU B . n B 2 239 THR 239 1886 1886 THR THR B . n B 2 240 LYS 240 1887 1887 LYS LYS B . n B 2 241 SER 241 1888 1888 SER SER B . n B 2 242 TRP 242 1889 1889 TRP TRP B . n B 2 243 TYR 243 1890 1890 TYR TYR B . n B 2 244 PHE 244 1891 1891 PHE PHE B . n B 2 245 THR 245 1892 1892 THR THR B . n B 2 246 GLU 246 1893 1893 GLU GLU B . n B 2 247 ASN 247 1894 1894 ASN ASN B . n B 2 248 MET 248 1895 ? ? ? B . n B 2 249 GLU 249 1896 ? ? ? B . n B 2 250 ARG 250 1897 ? ? ? B . n B 2 251 ASN 251 1898 ? ? ? B . n B 2 252 CYS 252 1899 ? ? ? B . n B 2 253 ARG 253 1900 ? ? ? B . n B 2 254 ALA 254 1901 ? ? ? B . n B 2 255 PRO 255 1902 ? ? ? B . n B 2 256 CYS 256 1903 ? ? ? B . n B 2 257 ASN 257 1904 ? ? ? B . n B 2 258 ILE 258 1905 ? ? ? B . n B 2 259 GLN 259 1906 ? ? ? B . n B 2 260 MET 260 1907 ? ? ? B . n B 2 261 GLU 261 1908 ? ? ? B . n B 2 262 ASP 262 1909 ? ? ? B . n B 2 263 PRO 263 1910 ? ? ? B . n B 2 264 THR 264 1911 1911 THR THR B . n B 2 265 PHE 265 1912 1912 PHE PHE B . n B 2 266 LYS 266 1913 1913 LYS LYS B . n B 2 267 GLU 267 1914 1914 GLU GLU B . n B 2 268 ASN 268 1915 1915 ASN ASN B . n B 2 269 TYR 269 1916 1916 TYR TYR B . n B 2 270 ARG 270 1917 1917 ARG ARG B . n B 2 271 PHE 271 1918 1918 PHE PHE B . n B 2 272 HIS 272 1919 1919 HIS HIS B . n B 2 273 ALA 273 1920 1920 ALA ALA B . n B 2 274 ILE 274 1921 1921 ILE ILE B . n B 2 275 ASN 275 1922 1922 ASN ASN B . n B 2 276 GLY 276 1923 1923 GLY GLY B . n B 2 277 TYR 277 1924 1924 TYR TYR B . n B 2 278 ILE 278 1925 1925 ILE ILE B . n B 2 279 MET 279 1926 1926 MET MET B . n B 2 280 ASP 280 1927 1927 ASP ASP B . n B 2 281 THR 281 1928 1928 THR THR B . n B 2 282 LEU 282 1929 1929 LEU LEU B . n B 2 283 PRO 283 1930 1930 PRO PRO B . n B 2 284 GLY 284 1931 1931 GLY GLY B . n B 2 285 LEU 285 1932 1932 LEU LEU B . n B 2 286 VAL 286 1933 1933 VAL VAL B . n B 2 287 MET 287 1934 1934 MET MET B . n B 2 288 ALA 288 1935 1935 ALA ALA B . n B 2 289 GLN 289 1936 1936 GLN GLN B . n B 2 290 ASP 290 1937 1937 ASP ASP B . n B 2 291 GLN 291 1938 1938 GLN GLN B . n B 2 292 ARG 292 1939 1939 ARG ARG B . n B 2 293 ILE 293 1940 1940 ILE ILE B . n B 2 294 ARG 294 1941 1941 ARG ARG B . n B 2 295 TRP 295 1942 1942 TRP TRP B . n B 2 296 TYR 296 1943 1943 TYR TYR B . n B 2 297 LEU 297 1944 1944 LEU LEU B . n B 2 298 LEU 298 1945 1945 LEU LEU B . n B 2 299 SER 299 1946 1946 SER SER B . n B 2 300 MET 300 1947 1947 MET MET B . n B 2 301 GLY 301 1948 1948 GLY GLY B . n B 2 302 SER 302 1949 1949 SER SER B . n B 2 303 ASN 303 1950 1950 ASN ASN B . n B 2 304 GLU 304 1951 1951 GLU GLU B . n B 2 305 ASN 305 1952 1952 ASN ASN B . n B 2 306 ILE 306 1953 1953 ILE ILE B . n B 2 307 HIS 307 1954 1954 HIS HIS B . n B 2 308 SER 308 1955 1955 SER SER B . n B 2 309 ILE 309 1956 1956 ILE ILE B . n B 2 310 HIS 310 1957 1957 HIS HIS B . n B 2 311 PHE 311 1958 1958 PHE PHE B . n B 2 312 SER 312 1959 1959 SER SER B . n B 2 313 GLY 313 1960 1960 GLY GLY B . n B 2 314 HIS 314 1961 1961 HIS HIS B . n B 2 315 VAL 315 1962 1962 VAL VAL B . n B 2 316 PHE 316 1963 1963 PHE PHE B . n B 2 317 THR 317 1964 1964 THR THR B . n B 2 318 VAL 318 1965 1965 VAL VAL B . n B 2 319 ARG 319 1966 1966 ARG ARG B . n B 2 320 LYS 320 1967 1967 LYS LYS B . n B 2 321 LYS 321 1968 1968 LYS LYS B . n B 2 322 GLU 322 1969 1969 GLU GLU B . n B 2 323 GLU 323 1970 1970 GLU GLU B . n B 2 324 TYR 324 1971 1971 TYR TYR B . n B 2 325 LYS 325 1972 1972 LYS LYS B . n B 2 326 MET 326 1973 1973 MET MET B . n B 2 327 ALA 327 1974 1974 ALA ALA B . n B 2 328 LEU 328 1975 1975 LEU LEU B . n B 2 329 TYR 329 1976 1976 TYR TYR B . n B 2 330 ASN 330 1977 1977 ASN ASN B . n B 2 331 LEU 331 1978 1978 LEU LEU B . n B 2 332 TYR 332 1979 1979 TYR TYR B . n B 2 333 PRO 333 1980 1980 PRO PRO B . n B 2 334 GLY 334 1981 1981 GLY GLY B . n B 2 335 VAL 335 1982 1982 VAL VAL B . n B 2 336 PHE 336 1983 1983 PHE PHE B . n B 2 337 GLU 337 1984 1984 GLU GLU B . n B 2 338 THR 338 1985 1985 THR THR B . n B 2 339 VAL 339 1986 1986 VAL VAL B . n B 2 340 GLU 340 1987 1987 GLU GLU B . n B 2 341 MET 341 1988 1988 MET MET B . n B 2 342 LEU 342 1989 1989 LEU LEU B . n B 2 343 PRO 343 1990 1990 PRO PRO B . n B 2 344 SER 344 1991 1991 SER SER B . n B 2 345 LYS 345 1992 1992 LYS LYS B . n B 2 346 ALA 346 1993 1993 ALA ALA B . n B 2 347 GLY 347 1994 1994 GLY GLY B . n B 2 348 ILE 348 1995 1995 ILE ILE B . n B 2 349 TRP 349 1996 1996 TRP TRP B . n B 2 350 ARG 350 1997 1997 ARG ARG B . n B 2 351 VAL 351 1998 1998 VAL VAL B . n B 2 352 GLU 352 1999 1999 GLU GLU B . n B 2 353 CYS 353 2000 2000 CYS CYS B . n B 2 354 LEU 354 2001 2001 LEU LEU B . n B 2 355 ILE 355 2002 2002 ILE ILE B . n B 2 356 GLY 356 2003 2003 GLY GLY B . n B 2 357 GLU 357 2004 2004 GLU GLU B . n B 2 358 HIS 358 2005 2005 HIS HIS B . n B 2 359 LEU 359 2006 2006 LEU LEU B . n B 2 360 HIS 360 2007 2007 HIS HIS B . n B 2 361 ALA 361 2008 2008 ALA ALA B . n B 2 362 GLY 362 2009 2009 GLY GLY B . n B 2 363 MET 363 2010 2010 MET MET B . n B 2 364 SER 364 2011 2011 SER SER B . n B 2 365 THR 365 2012 2012 THR THR B . n B 2 366 LEU 366 2013 2013 LEU LEU B . n B 2 367 PHE 367 2014 2014 PHE PHE B . n B 2 368 LEU 368 2015 2015 LEU LEU B . n B 2 369 VAL 369 2016 2016 VAL VAL B . n B 2 370 TYR 370 2017 2017 TYR TYR B . n B 2 371 SER 371 2018 2018 SER SER B . n B 2 372 ASN 372 2019 2019 ASN ASN B . n B 2 373 LYS 373 2020 2020 LYS LYS B . n B 2 374 CYS 374 2021 2021 CYS CYS B . n B 2 375 GLN 375 2022 2022 GLN GLN B . n B 2 376 THR 376 2023 2023 THR THR B . n B 2 377 PRO 377 2024 2024 PRO PRO B . n B 2 378 LEU 378 2025 2025 LEU LEU B . n B 2 379 GLY 379 2026 2026 GLY GLY B . n B 2 380 MET 380 2027 2027 MET MET B . n B 2 381 ALA 381 2028 2028 ALA ALA B . n B 2 382 SER 382 2029 2029 SER SER B . n B 2 383 GLY 383 2030 2030 GLY GLY B . n B 2 384 HIS 384 2031 2031 HIS HIS B . n B 2 385 ILE 385 2032 2032 ILE ILE B . n B 2 386 ARG 386 2033 2033 ARG ARG B . n B 2 387 ASP 387 2034 2034 ASP ASP B . n B 2 388 PHE 388 2035 2035 PHE PHE B . n B 2 389 GLN 389 2036 2036 GLN GLN B . n B 2 390 ILE 390 2037 2037 ILE ILE B . n B 2 391 THR 391 2038 2038 THR THR B . n B 2 392 ALA 392 2039 2039 ALA ALA B . n B 2 393 SER 393 2040 2040 SER SER B . n B 2 394 GLY 394 2041 2041 GLY GLY B . n B 2 395 GLN 395 2042 2042 GLN GLN B . n B 2 396 TYR 396 2043 2043 TYR TYR B . n B 2 397 GLY 397 2044 2044 GLY GLY B . n B 2 398 GLN 398 2045 2045 GLN GLN B . n B 2 399 TRP 399 2046 2046 TRP TRP B . n B 2 400 ALA 400 2047 2047 ALA ALA B . n B 2 401 PRO 401 2048 2048 PRO PRO B . n B 2 402 LYS 402 2049 2049 LYS LYS B . n B 2 403 LEU 403 2050 2050 LEU LEU B . n B 2 404 ALA 404 2051 2051 ALA ALA B . n B 2 405 ARG 405 2052 2052 ARG ARG B . n B 2 406 LEU 406 2053 2053 LEU LEU B . n B 2 407 HIS 407 2054 2054 HIS HIS B . n B 2 408 TYR 408 2055 2055 TYR TYR B . n B 2 409 SER 409 2056 2056 SER SER B . n B 2 410 GLY 410 2057 2057 GLY GLY B . n B 2 411 SER 411 2058 2058 SER SER B . n B 2 412 ILE 412 2059 2059 ILE ILE B . n B 2 413 ASN 413 2060 2060 ASN ASN B . n B 2 414 ALA 414 2061 2061 ALA ALA B . n B 2 415 TRP 415 2062 2062 TRP TRP B . n B 2 416 SER 416 2063 2063 SER SER B . n B 2 417 THR 417 2064 2064 THR THR B . n B 2 418 LYS 418 2065 2065 LYS LYS B . n B 2 419 GLU 419 2066 2066 GLU GLU B . n B 2 420 PRO 420 2067 2067 PRO PRO B . n B 2 421 PHE 421 2068 2068 PHE PHE B . n B 2 422 SER 422 2069 2069 SER SER B . n B 2 423 TRP 423 2070 2070 TRP TRP B . n B 2 424 ILE 424 2071 2071 ILE ILE B . n B 2 425 LYS 425 2072 2072 LYS LYS B . n B 2 426 VAL 426 2073 2073 VAL VAL B . n B 2 427 ASP 427 2074 2074 ASP ASP B . n B 2 428 LEU 428 2075 2075 LEU LEU B . n B 2 429 LEU 429 2076 2076 LEU LEU B . n B 2 430 ALA 430 2077 2077 ALA ALA B . n B 2 431 PRO 431 2078 2078 PRO PRO B . n B 2 432 MET 432 2079 2079 MET MET B . n B 2 433 ILE 433 2080 2080 ILE ILE B . n B 2 434 ILE 434 2081 2081 ILE ILE B . n B 2 435 HIS 435 2082 2082 HIS HIS B . n B 2 436 GLY 436 2083 2083 GLY GLY B . n B 2 437 ILE 437 2084 2084 ILE ILE B . n B 2 438 LYS 438 2085 2085 LYS LYS B . n B 2 439 THR 439 2086 2086 THR THR B . n B 2 440 GLN 440 2087 2087 GLN GLN B . n B 2 441 GLY 441 2088 2088 GLY GLY B . n B 2 442 ALA 442 2089 2089 ALA ALA B . n B 2 443 ARG 443 2090 2090 ARG ARG B . n B 2 444 GLN 444 2091 2091 GLN GLN B . n B 2 445 LYS 445 2092 2092 LYS LYS B . n B 2 446 PHE 446 2093 2093 PHE PHE B . n B 2 447 SER 447 2094 2094 SER SER B . n B 2 448 SER 448 2095 2095 SER SER B . n B 2 449 LEU 449 2096 2096 LEU LEU B . n B 2 450 TYR 450 2097 2097 TYR TYR B . n B 2 451 ILE 451 2098 2098 ILE ILE B . n B 2 452 SER 452 2099 2099 SER SER B . n B 2 453 GLN 453 2100 2100 GLN GLN B . n B 2 454 PHE 454 2101 2101 PHE PHE B . n B 2 455 ILE 455 2102 2102 ILE ILE B . n B 2 456 ILE 456 2103 2103 ILE ILE B . n B 2 457 MET 457 2104 2104 MET MET B . n B 2 458 TYR 458 2105 2105 TYR TYR B . n B 2 459 SER 459 2106 2106 SER SER B . n B 2 460 LEU 460 2107 2107 LEU LEU B . n B 2 461 ASP 461 2108 2108 ASP ASP B . n B 2 462 GLY 462 2109 2109 GLY GLY B . n B 2 463 LYS 463 2110 2110 LYS LYS B . n B 2 464 LYS 464 2111 2111 LYS LYS B . n B 2 465 TRP 465 2112 2112 TRP TRP B . n B 2 466 GLN 466 2113 2113 GLN GLN B . n B 2 467 THR 467 2114 2114 THR THR B . n B 2 468 TYR 468 2115 2115 TYR TYR B . n B 2 469 ARG 469 2116 2116 ARG ARG B . n B 2 470 GLY 470 2117 2117 GLY GLY B . n B 2 471 ASN 471 2118 2118 ASN ASN B . n B 2 472 SER 472 2119 2119 SER SER B . n B 2 473 THR 473 2120 2120 THR THR B . n B 2 474 GLY 474 2121 2121 GLY GLY B . n B 2 475 THR 475 2122 2122 THR THR B . n B 2 476 LEU 476 2123 2123 LEU LEU B . n B 2 477 MET 477 2124 2124 MET MET B . n B 2 478 VAL 478 2125 2125 VAL VAL B . n B 2 479 PHE 479 2126 2126 PHE PHE B . n B 2 480 PHE 480 2127 2127 PHE PHE B . n B 2 481 GLY 481 2128 2128 GLY GLY B . n B 2 482 ASN 482 2129 2129 ASN ASN B . n B 2 483 VAL 483 2130 2130 VAL VAL B . n B 2 484 ASP 484 2131 2131 ASP ASP B . n B 2 485 SER 485 2132 2132 SER SER B . n B 2 486 SER 486 2133 2133 SER SER B . n B 2 487 GLY 487 2134 2134 GLY GLY B . n B 2 488 ILE 488 2135 2135 ILE ILE B . n B 2 489 LYS 489 2136 2136 LYS LYS B . n B 2 490 HIS 490 2137 2137 HIS HIS B . n B 2 491 ASN 491 2138 2138 ASN ASN B . n B 2 492 ILE 492 2139 2139 ILE ILE B . n B 2 493 PHE 493 2140 2140 PHE PHE B . n B 2 494 ASN 494 2141 2141 ASN ASN B . n B 2 495 PRO 495 2142 2142 PRO PRO B . n B 2 496 PRO 496 2143 2143 PRO PRO B . n B 2 497 ILE 497 2144 2144 ILE ILE B . n B 2 498 ILE 498 2145 2145 ILE ILE B . n B 2 499 ALA 499 2146 2146 ALA ALA B . n B 2 500 ARG 500 2147 2147 ARG ARG B . n B 2 501 TYR 501 2148 2148 TYR TYR B . n B 2 502 ILE 502 2149 2149 ILE ILE B . n B 2 503 ARG 503 2150 2150 ARG ARG B . n B 2 504 LEU 504 2151 2151 LEU LEU B . n B 2 505 HIS 505 2152 2152 HIS HIS B . n B 2 506 PRO 506 2153 2153 PRO PRO B . n B 2 507 THR 507 2154 2154 THR THR B . n B 2 508 HIS 508 2155 2155 HIS HIS B . n B 2 509 TYR 509 2156 2156 TYR TYR B . n B 2 510 SER 510 2157 2157 SER SER B . n B 2 511 ILE 511 2158 2158 ILE ILE B . n B 2 512 ARG 512 2159 2159 ARG ARG B . n B 2 513 SER 513 2160 2160 SER SER B . n B 2 514 THR 514 2161 2161 THR THR B . n B 2 515 LEU 515 2162 2162 LEU LEU B . n B 2 516 ARG 516 2163 2163 ARG ARG B . n B 2 517 MET 517 2164 2164 MET MET B . n B 2 518 GLU 518 2165 2165 GLU GLU B . n B 2 519 LEU 519 2166 2166 LEU LEU B . n B 2 520 MET 520 2167 2167 MET MET B . n B 2 521 GLY 521 2168 2168 GLY GLY B . n B 2 522 CYS 522 2169 2169 CYS CYS B . n B 2 523 ASP 523 2170 2170 ASP ASP B . n B 2 524 LEU 524 2171 2171 LEU LEU B . n B 2 525 ASN 525 2172 2172 ASN ASN B . n B 2 526 SER 526 2173 2173 SER SER B . n B 2 527 CYS 527 2174 2174 CYS CYS B . n B 2 528 SER 528 2175 2175 SER SER B . n B 2 529 MET 529 2176 2176 MET MET B . n B 2 530 PRO 530 2177 2177 PRO PRO B . n B 2 531 LEU 531 2178 2178 LEU LEU B . n B 2 532 GLY 532 2179 2179 GLY GLY B . n B 2 533 MET 533 2180 2180 MET MET B . n B 2 534 GLU 534 2181 2181 GLU GLU B . n B 2 535 SER 535 2182 2182 SER SER B . n B 2 536 LYS 536 2183 2183 LYS LYS B . n B 2 537 ALA 537 2184 2184 ALA ALA B . n B 2 538 ILE 538 2185 2185 ILE ILE B . n B 2 539 SER 539 2186 2186 SER SER B . n B 2 540 ASP 540 2187 2187 ASP ASP B . n B 2 541 ALA 541 2188 2188 ALA ALA B . n B 2 542 GLN 542 2189 2189 GLN GLN B . n B 2 543 ILE 543 2190 2190 ILE ILE B . n B 2 544 THR 544 2191 2191 THR THR B . n B 2 545 ALA 545 2192 2192 ALA ALA B . n B 2 546 SER 546 2193 2193 SER SER B . n B 2 547 SER 547 2194 2194 SER SER B . n B 2 548 TYR 548 2195 2195 TYR TYR B . n B 2 549 PHE 549 2196 2196 PHE PHE B . n B 2 550 THR 550 2197 2197 THR THR B . n B 2 551 ASN 551 2198 2198 ASN ASN B . n B 2 552 MET 552 2199 2199 MET MET B . n B 2 553 PHE 553 2200 2200 PHE PHE B . n B 2 554 ALA 554 2201 2201 ALA ALA B . n B 2 555 THR 555 2202 2202 THR THR B . n B 2 556 TRP 556 2203 2203 TRP TRP B . n B 2 557 SER 557 2204 2204 SER SER B . n B 2 558 PRO 558 2205 2205 PRO PRO B . n B 2 559 SER 559 2206 2206 SER SER B . n B 2 560 LYS 560 2207 2207 LYS LYS B . n B 2 561 ALA 561 2208 2208 ALA ALA B . n B 2 562 ARG 562 2209 2209 ARG ARG B . n B 2 563 LEU 563 2210 2210 LEU LEU B . n B 2 564 HIS 564 2211 2211 HIS HIS B . n B 2 565 LEU 565 2212 2212 LEU LEU B . n B 2 566 GLN 566 2213 2213 GLN GLN B . n B 2 567 GLY 567 2214 2214 GLY GLY B . n B 2 568 ARG 568 2215 2215 ARG ARG B . n B 2 569 SER 569 2216 2216 SER SER B . n B 2 570 ASN 570 2217 2217 ASN ASN B . n B 2 571 ALA 571 2218 2218 ALA ALA B . n B 2 572 TRP 572 2219 2219 TRP TRP B . n B 2 573 ARG 573 2220 2220 ARG ARG B . n B 2 574 PRO 574 2221 2221 PRO PRO B . n B 2 575 GLN 575 2222 2222 GLN GLN B . n B 2 576 VAL 576 2223 2223 VAL VAL B . n B 2 577 ASN 577 2224 2224 ASN ASN B . n B 2 578 ASN 578 2225 2225 ASN ASN B . n B 2 579 PRO 579 2226 2226 PRO PRO B . n B 2 580 LYS 580 2227 2227 LYS LYS B . n B 2 581 GLU 581 2228 2228 GLU GLU B . n B 2 582 TRP 582 2229 2229 TRP TRP B . n B 2 583 LEU 583 2230 2230 LEU LEU B . n B 2 584 GLN 584 2231 2231 GLN GLN B . n B 2 585 VAL 585 2232 2232 VAL VAL B . n B 2 586 ASP 586 2233 2233 ASP ASP B . n B 2 587 PHE 587 2234 2234 PHE PHE B . n B 2 588 GLN 588 2235 2235 GLN GLN B . n B 2 589 LYS 589 2236 2236 LYS LYS B . n B 2 590 THR 590 2237 2237 THR THR B . n B 2 591 MET 591 2238 2238 MET MET B . n B 2 592 LYS 592 2239 2239 LYS LYS B . n B 2 593 VAL 593 2240 2240 VAL VAL B . n B 2 594 THR 594 2241 2241 THR THR B . n B 2 595 GLY 595 2242 2242 GLY GLY B . n B 2 596 VAL 596 2243 2243 VAL VAL B . n B 2 597 THR 597 2244 2244 THR THR B . n B 2 598 THR 598 2245 2245 THR THR B . n B 2 599 GLN 599 2246 2246 GLN GLN B . n B 2 600 GLY 600 2247 2247 GLY GLY B . n B 2 601 VAL 601 2248 2248 VAL VAL B . n B 2 602 LYS 602 2249 2249 LYS LYS B . n B 2 603 SER 603 2250 2250 SER SER B . n B 2 604 LEU 604 2251 2251 LEU LEU B . n B 2 605 LEU 605 2252 2252 LEU LEU B . n B 2 606 THR 606 2253 2253 THR THR B . n B 2 607 SER 607 2254 2254 SER SER B . n B 2 608 MET 608 2255 2255 MET MET B . n B 2 609 TYR 609 2256 2256 TYR TYR B . n B 2 610 VAL 610 2257 2257 VAL VAL B . n B 2 611 LYS 611 2258 2258 LYS LYS B . n B 2 612 GLU 612 2259 2259 GLU GLU B . n B 2 613 PHE 613 2260 2260 PHE PHE B . n B 2 614 LEU 614 2261 2261 LEU LEU B . n B 2 615 ILE 615 2262 2262 ILE ILE B . n B 2 616 SER 616 2263 2263 SER SER B . n B 2 617 SER 617 2264 2264 SER SER B . n B 2 618 SER 618 2265 2265 SER SER B . n B 2 619 GLN 619 2266 2266 GLN GLN B . n B 2 620 ASP 620 2267 2267 ASP ASP B . n B 2 621 GLY 621 2268 2268 GLY GLY B . n B 2 622 HIS 622 2269 2269 HIS HIS B . n B 2 623 GLN 623 2270 2270 GLN GLN B . n B 2 624 TRP 624 2271 2271 TRP TRP B . n B 2 625 THR 625 2272 2272 THR THR B . n B 2 626 LEU 626 2273 2273 LEU LEU B . n B 2 627 PHE 627 2274 2274 PHE PHE B . n B 2 628 PHE 628 2275 2275 PHE PHE B . n B 2 629 GLN 629 2276 2276 GLN GLN B . n B 2 630 ASN 630 2277 2277 ASN ASN B . n B 2 631 GLY 631 2278 2278 GLY GLY B . n B 2 632 LYS 632 2279 2279 LYS LYS B . n B 2 633 VAL 633 2280 2280 VAL VAL B . n B 2 634 LYS 634 2281 2281 LYS LYS B . n B 2 635 VAL 635 2282 2282 VAL VAL B . n B 2 636 PHE 636 2283 2283 PHE PHE B . n B 2 637 GLN 637 2284 2284 GLN GLN B . n B 2 638 GLY 638 2285 2285 GLY GLY B . n B 2 639 ASN 639 2286 2286 ASN ASN B . n B 2 640 GLN 640 2287 2287 GLN GLN B . n B 2 641 ASP 641 2288 2288 ASP ASP B . n B 2 642 SER 642 2289 2289 SER SER B . n B 2 643 PHE 643 2290 2290 PHE PHE B . n B 2 644 THR 644 2291 2291 THR THR B . n B 2 645 PRO 645 2292 2292 PRO PRO B . n B 2 646 VAL 646 2293 2293 VAL VAL B . n B 2 647 VAL 647 2294 2294 VAL VAL B . n B 2 648 ASN 648 2295 2295 ASN ASN B . n B 2 649 SER 649 2296 2296 SER SER B . n B 2 650 LEU 650 2297 2297 LEU LEU B . n B 2 651 ASP 651 2298 2298 ASP ASP B . n B 2 652 PRO 652 2299 2299 PRO PRO B . n B 2 653 PRO 653 2300 2300 PRO PRO B . n B 2 654 LEU 654 2301 2301 LEU LEU B . n B 2 655 LEU 655 2302 2302 LEU LEU B . n B 2 656 THR 656 2303 2303 THR THR B . n B 2 657 ARG 657 2304 2304 ARG ARG B . n B 2 658 TYR 658 2305 2305 TYR TYR B . n B 2 659 LEU 659 2306 2306 LEU LEU B . n B 2 660 ARG 660 2307 2307 ARG ARG B . n B 2 661 ILE 661 2308 2308 ILE ILE B . n B 2 662 HIS 662 2309 2309 HIS HIS B . n B 2 663 PRO 663 2310 2310 PRO PRO B . n B 2 664 GLN 664 2311 2311 GLN GLN B . n B 2 665 SER 665 2312 2312 SER SER B . n B 2 666 TRP 666 2313 2313 TRP TRP B . n B 2 667 VAL 667 2314 2314 VAL VAL B . n B 2 668 HIS 668 2315 2315 HIS HIS B . n B 2 669 GLN 669 2316 2316 GLN GLN B . n B 2 670 ILE 670 2317 2317 ILE ILE B . n B 2 671 ALA 671 2318 2318 ALA ALA B . n B 2 672 LEU 672 2319 2319 LEU LEU B . n B 2 673 ARG 673 2320 2320 ARG ARG B . n B 2 674 MET 674 2321 2321 MET MET B . n B 2 675 GLU 675 2322 2322 GLU GLU B . n B 2 676 VAL 676 2323 2323 VAL VAL B . n B 2 677 LEU 677 2324 2324 LEU LEU B . n B 2 678 GLY 678 2325 2325 GLY GLY B . n B 2 679 CYS 679 2326 2326 CYS CYS B . n B 2 680 GLU 680 2327 2327 GLU GLU B . n B 2 681 ALA 681 2328 2328 ALA ALA B . n B 2 682 GLN 682 2329 2329 GLN GLN B . n B 2 683 ASP 683 2330 2330 ASP ASP B . n B 2 684 LEU 684 2331 2331 LEU LEU B . n B 2 685 TYR 685 2332 2332 TYR TYR B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 ZN 1 800 800 ZN ZN A . D 4 CA 1 801 801 CA CA A . E 5 NAG 1 1755 1755 NAG NAG A . F 5 NAG 2 1756 1756 NAG NAG A . G 6 EDO 1 3333 3333 EDO EDO A . H 7 CU1 1 1 1 CU1 CU1 B . I 5 NAG 1 2334 2334 NAG NAG B . J 5 NAG 2 2335 2335 NAG NAG B . K 8 BMA 3 2336 2336 BMA BMA B . L 8 BMA 4 2337 2337 BMA BMA B . M 8 BMA 5 2338 2338 BMA BMA B . N 6 EDO 1 3333 3333 EDO EDO B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 239 A ASN 239 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 471 B ASN 2118 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 9310 ? 1 MORE -6.4 ? 1 'SSA (A^2)' 50530 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 ND1 ? A HIS 267 ? A HIS 267 ? 1_555 ZN ? C ZN . ? A ZN 800 ? 1_555 SG ? A CYS 310 ? A CYS 310 ? 1_555 84.8 ? 2 ND1 ? A HIS 267 ? A HIS 267 ? 1_555 ZN ? C ZN . ? A ZN 800 ? 1_555 ND1 ? A HIS 315 ? A HIS 315 ? 1_555 114.1 ? 3 SG ? A CYS 310 ? A CYS 310 ? 1_555 ZN ? C ZN . ? A ZN 800 ? 1_555 ND1 ? A HIS 315 ? A HIS 315 ? 1_555 126.8 ? 4 OD1 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD2 ? A ASP 125 ? A ASP 125 ? 1_555 48.0 ? 5 OD1 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 O ? A LYS 107 ? A LYS 107 ? 1_555 74.9 ? 6 OD2 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 O ? A LYS 107 ? A LYS 107 ? 1_555 95.1 ? 7 OD1 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD2 ? A ASP 116 ? A ASP 116 ? 1_555 135.6 ? 8 OD2 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD2 ? A ASP 116 ? A ASP 116 ? 1_555 169.1 ? 9 O ? A LYS 107 ? A LYS 107 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD2 ? A ASP 116 ? A ASP 116 ? 1_555 95.7 ? 10 OD1 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD1 ? A ASP 126 ? A ASP 126 ? 1_555 67.6 ? 11 OD2 ? A ASP 125 ? A ASP 125 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD1 ? A ASP 126 ? A ASP 126 ? 1_555 81.0 ? 12 O ? A LYS 107 ? A LYS 107 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD1 ? A ASP 126 ? A ASP 126 ? 1_555 132.5 ? 13 OD2 ? A ASP 116 ? A ASP 116 ? 1_555 CA ? D CA . ? A CA 801 ? 1_555 OD1 ? A ASP 126 ? A ASP 126 ? 1_555 91.5 ? 14 SG ? B CYS 353 ? B CYS 2000 ? 1_555 CU ? H CU1 . ? B CU1 1 ? 1_555 ND1 ? B HIS 358 ? B HIS 2005 ? 1_555 124.7 ? 15 SG ? B CYS 353 ? B CYS 2000 ? 1_555 CU ? H CU1 . ? B CU1 1 ? 1_555 ND1 ? B HIS 307 ? B HIS 1954 ? 1_555 135.3 ? 16 ND1 ? B HIS 358 ? B HIS 2005 ? 1_555 CU ? H CU1 . ? B CU1 1 ? 1_555 ND1 ? B HIS 307 ? B HIS 1954 ? 1_555 98.3 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-05-15 2 'Structure model' 1 1 2017-01-25 3 'Structure model' 1 2 2018-01-17 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Data collection' 2 3 'Structure model' 'Data collection' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category diffrn_source # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_diffrn_source.pdbx_synchrotron_site' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -54.1300 -42.2810 77.0890 0.4808 0.1463 0.4543 0.2107 0.4414 0.1872 2.9429 5.7848 3.4262 0.2063 -0.3214 -2.6296 0.2147 -0.0358 0.4771 0.5019 0.4016 0.7729 -0.6167 -0.4882 -0.6163 'X-RAY DIFFRACTION' 2 ? refined -31.7160 -66.3760 96.4940 0.2379 0.1286 0.2494 -0.0010 0.0430 0.1027 3.5323 3.6266 3.3934 0.6840 -0.8583 -2.0051 0.0985 -0.4139 -0.3489 0.4442 -0.1859 -0.5456 -0.4502 0.4095 0.0874 'X-RAY DIFFRACTION' 3 ? refined -20.1210 -41.2390 73.5660 0.5416 0.1653 0.3221 -0.1824 0.1504 0.0201 4.1561 3.2585 3.2277 -0.2772 -0.0668 -1.0614 0.0666 -0.3199 0.0425 0.6491 -0.1552 -0.5146 -0.6929 0.4928 0.0887 'X-RAY DIFFRACTION' 4 ? refined -15.7690 -18.6710 45.3520 0.4678 0.1533 0.2347 -0.1877 0.2662 -0.0681 5.1695 4.6833 8.3583 0.5355 -3.6043 -2.7040 0.3206 -0.0084 0.2452 0.2368 -0.0815 -0.2292 -0.9537 0.8289 -0.2391 'X-RAY DIFFRACTION' 5 ? refined -47.6990 -13.2270 37.3060 0.2985 0.0849 0.6612 0.0328 0.4005 0.1012 2.7980 10.1925 5.7005 -0.2512 0.1892 -4.4220 0.1783 -0.0436 -0.1361 0.4387 0.4287 1.4042 -0.0980 -0.6658 -0.6069 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 333 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 377 ? ? A 713 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 B 1691 ? ? B 2017 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 B 2018 ? ? B 2172 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 2173 ? ? B 2332 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0032 ? 1 XDS 'data reduction' . ? 2 XSCALE 'data scaling' . ? 3 REFMAC phasing . ? 4 # _pdbx_entry_details.entry_id 4BDV _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE SEQUENCE IS DESCRIBED IN THIM, L. ET AL. (2010), HAEMOPHILIA. 16, 349-359. ; # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 ND2 _pdbx_validate_close_contact.auth_asym_id_1 B _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 2118 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 C2 _pdbx_validate_close_contact.auth_asym_id_2 B _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 2334 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 1.96 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 N A ASP 15 ? ? CA A ASP 15 ? ? C A ASP 15 ? ? 130.16 111.00 19.16 2.70 N 2 1 N A TYR 46 ? ? CA A TYR 46 ? ? C A TYR 46 ? ? 131.93 111.00 20.93 2.70 N 3 1 C A PRO 66 ? ? N A PRO 67 ? ? CA A PRO 67 ? ? 129.28 119.30 9.98 1.50 Y 4 1 C A ASP 150 ? ? N A PRO 151 ? ? CA A PRO 151 ? ? 129.46 119.30 10.16 1.50 Y 5 1 CA A LEU 184 ? ? CB A LEU 184 ? ? CG A LEU 184 ? ? 131.73 115.30 16.43 2.30 N 6 1 C A SER 289 ? ? N A PRO 290 ? ? CA A PRO 290 ? ? 128.40 119.30 9.10 1.50 Y 7 1 NE A ARG 489 ? ? CZ A ARG 489 ? ? NH1 A ARG 489 ? ? 124.78 120.30 4.48 0.50 N 8 1 NE A ARG 489 ? ? CZ A ARG 489 ? ? NH2 A ARG 489 ? ? 116.80 120.30 -3.50 0.50 N 9 1 C A PHE 501 ? ? N A PRO 502 ? ? CA A PRO 502 ? ? 129.05 119.30 9.75 1.50 Y 10 1 C A ASN 597 ? ? N A PRO 598 ? ? CA A PRO 598 ? ? 130.28 119.30 10.98 1.50 Y 11 1 C B VAL 1727 ? ? N B PRO 1728 ? ? CA B PRO 1728 ? ? 133.06 119.30 13.76 1.50 Y 12 1 C B ALA 1824 ? ? N B PRO 1825 ? ? CA B PRO 1825 ? ? 128.34 119.30 9.04 1.50 Y 13 1 CA B LEU 1989 ? ? CB B LEU 1989 ? ? CG B LEU 1989 ? ? 130.79 115.30 15.49 2.30 N 14 1 CA B LEU 2025 ? ? CB B LEU 2025 ? ? CG B LEU 2025 ? ? 100.15 115.30 -15.15 2.30 N 15 1 CA B LEU 2261 ? ? CB B LEU 2261 ? ? CG B LEU 2261 ? ? 93.89 115.30 -21.41 2.30 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 THR A 2 ? ? 164.91 124.68 2 1 LEU A 7 ? ? -38.64 147.65 3 1 ALA A 9 ? ? -111.70 71.45 4 1 LEU A 12 ? ? -117.03 -151.53 5 1 ASP A 15 ? ? 164.90 -81.77 6 1 TYR A 46 ? ? 33.45 145.15 7 1 LYS A 47 ? ? -165.08 110.38 8 1 PHE A 54 ? ? 40.79 151.36 9 1 ASP A 56 ? ? -36.70 170.21 10 1 PHE A 59 ? ? -145.52 -20.78 11 1 ALA A 62 ? ? 162.10 96.63 12 1 LYS A 63 ? ? -178.23 47.47 13 1 PRO A 64 ? ? -57.05 103.87 14 1 PRO A 67 ? ? -12.34 -64.73 15 1 MET A 69 ? ? -57.86 47.75 16 1 VAL A 80 ? ? -96.21 54.23 17 1 TYR A 81 ? ? -175.18 -8.93 18 1 ASN A 90 ? ? 28.87 86.42 19 1 SER A 97 ? ? -118.43 -153.98 20 1 LEU A 98 ? ? -159.87 81.53 21 1 TYR A 105 ? ? -170.96 -179.88 22 1 SER A 109 ? ? -129.28 -159.10 23 1 GLU A 110 ? ? 84.32 -54.21 24 1 TYR A 114 ? ? -141.52 -98.08 25 1 GLN A 117 ? ? 76.16 -7.25 26 1 LYS A 127 ? ? -178.83 90.93 27 1 ALA A 148 ? ? -24.79 -70.70 28 1 PRO A 151 ? ? -14.09 162.79 29 1 TYR A 156 ? ? -132.37 -152.66 30 1 SER A 157 ? ? 172.58 170.63 31 1 HIS A 161 ? ? -115.52 61.73 32 1 ASP A 163 ? ? -150.27 11.09 33 1 LEU A 164 ? ? 31.95 -78.24 34 1 ARG A 180 ? ? -59.73 -180.00 35 1 LYS A 186 ? ? -169.33 100.31 36 1 GLU A 187 ? ? 99.62 72.10 37 1 LYS A 206 ? ? -158.27 57.61 38 1 SER A 207 ? ? -135.03 -102.29 39 1 TRP A 208 ? ? -144.27 19.92 40 1 LYS A 230 ? ? 160.22 96.70 41 1 HIS A 232 ? ? 179.20 62.58 42 1 THR A 233 ? ? -106.33 -166.14 43 1 ASN A 235 ? ? 88.00 7.68 44 1 ASN A 239 ? ? 57.65 -62.34 45 1 ARG A 240 ? ? 169.50 53.45 46 1 SER A 241 ? ? -81.76 -156.83 47 1 LEU A 242 ? ? 90.12 103.47 48 1 PRO A 243 ? ? -80.91 -76.00 49 1 LEU A 245 ? ? 24.75 91.03 50 1 PRO A 264 ? ? -56.78 3.80 51 1 GLU A 272 ? ? -26.83 123.39 52 1 ARG A 279 ? ? 39.98 -93.97 53 1 ASN A 280 ? ? -150.56 22.84 54 1 PRO A 290 ? ? -14.09 -77.36 55 1 LEU A 299 ? ? 55.61 98.17 56 1 ASP A 302 ? ? 71.67 122.49 57 1 PHE A 309 ? ? -178.40 -169.45 58 1 ASP A 318 ? ? -48.39 -7.85 59 1 GLU A 321 ? ? 176.12 146.73 60 1 VAL A 326 ? ? -156.18 78.87 61 1 PRO A 397 ? ? -46.85 -118.45 62 1 PRO A 402 ? ? -35.44 169.43 63 1 ASP A 403 ? ? 65.37 134.54 64 1 SER A 406 ? ? -69.99 -161.41 65 1 SER A 409 ? ? -66.08 95.73 66 1 GLN A 410 ? ? 151.87 -32.68 67 1 LEU A 412 ? ? -97.35 -98.47 68 1 ASN A 413 ? ? -24.62 93.15 69 1 GLN A 417 ? ? -156.57 51.73 70 1 ARG A 421 ? ? 60.03 -50.44 71 1 PHE A 436 ? ? -117.89 76.53 72 1 THR A 438 ? ? 83.56 133.43 73 1 GLU A 445 ? ? -55.59 -72.97 74 1 ALA A 469 ? ? 156.11 162.02 75 1 PRO A 472 ? ? -42.47 108.08 76 1 ARG A 489 ? ? -94.32 -102.38 77 1 ARG A 490 ? ? 21.47 86.18 78 1 LYS A 493 ? ? 53.76 -119.04 79 1 PRO A 526 ? ? -58.40 100.22 80 1 ARG A 527 ? ? -63.06 75.27 81 1 CYS A 528 ? ? 152.37 63.23 82 1 PHE A 536 ? ? -98.17 38.63 83 1 ASN A 538 ? ? -157.02 81.02 84 1 MET A 539 ? ? -20.04 -45.45 85 1 LYS A 556 ? ? -76.76 36.44 86 1 GLN A 592 ? ? -77.65 39.57 87 1 ARG A 593 ? ? -165.33 -14.06 88 1 ASN A 597 ? ? -16.44 97.89 89 1 PRO A 598 ? ? -54.05 45.96 90 1 ALA A 599 ? ? -64.72 -81.45 91 1 VAL A 601 ? ? -69.67 -89.30 92 1 GLN A 602 ? ? 59.80 86.93 93 1 ASP A 605 ? ? 178.29 115.55 94 1 PRO A 606 ? ? -27.85 -90.87 95 1 SER A 611 ? ? -48.53 -15.19 96 1 PHE A 622 ? ? 45.51 80.12 97 1 ASP A 623 ? ? 32.62 37.44 98 1 LEU A 625 ? ? 84.64 113.90 99 1 HIS A 632 ? ? 94.05 -37.76 100 1 GLN A 645 ? ? -33.66 146.29 101 1 THR A 646 ? ? 58.59 -56.75 102 1 PHE A 652 ? ? -107.14 -85.96 103 1 PHE A 653 ? ? 68.34 86.09 104 1 LYS A 661 ? ? 46.67 74.06 105 1 MET A 662 ? ? 30.80 44.63 106 1 THR A 667 ? ? -166.43 117.54 107 1 PRO A 672 ? ? 3.77 -102.43 108 1 HIS A 693 ? ? -81.29 39.06 109 1 ASP A 696 ? ? -50.18 -85.91 110 1 ARG A 698 ? ? -57.00 13.87 111 1 MET A 702 ? ? 90.09 40.28 112 1 CYS A 711 ? ? -111.33 -155.40 113 1 ASP A 712 ? ? -154.30 31.41 114 1 TYR B 1709 ? ? -157.96 49.68 115 1 MET B 1711 ? ? -46.17 -116.71 116 1 SER B 1712 ? ? -160.32 1.12 117 1 GLN B 1729 ? ? -77.05 -123.82 118 1 PHE B 1730 ? ? 105.21 96.37 119 1 THR B 1739 ? ? -126.42 -86.01 120 1 THR B 1744 ? ? -95.31 -74.04 121 1 TYR B 1748 ? ? -24.29 119.78 122 1 LEU B 1752 ? ? -27.25 -78.54 123 1 ASN B 1753 ? ? -102.36 55.37 124 1 GLU B 1768 ? ? -58.58 -8.89 125 1 ALA B 1779 ? ? -103.16 -166.24 126 1 PHE B 1785 ? ? -99.54 -87.30 127 1 TYR B 1786 ? ? 59.32 117.95 128 1 ILE B 1790 ? ? -52.98 73.40 129 1 TYR B 1792 ? ? -95.86 -158.79 130 1 GLU B 1793 ? ? -109.77 -79.97 131 1 GLU B 1794 ? ? 145.16 150.22 132 1 LYS B 1804 ? ? 139.15 -149.58 133 1 PRO B 1809 ? ? -45.98 163.63 134 1 ASN B 1810 ? ? 44.96 28.08 135 1 LYS B 1827 ? ? -32.21 -19.76 136 1 GLU B 1829 ? ? -79.08 -135.26 137 1 ASP B 1846 ? ? -72.28 28.94 138 1 VAL B 1847 ? ? -122.12 -53.52 139 1 ALA B 1866 ? ? 52.01 -43.84 140 1 HIS B 1867 ? ? -67.06 33.33 141 1 GLN B 1870 ? ? 49.13 -145.35 142 1 VAL B 1871 ? ? 161.06 -34.56 143 1 GLU B 1885 ? ? -79.55 37.84 144 1 LYS B 1887 ? ? -76.41 -156.71 145 1 SER B 1888 ? ? 74.07 104.96 146 1 TRP B 1889 ? ? -38.61 -17.07 147 1 PHE B 1891 ? ? -106.74 66.31 148 1 THR B 1892 ? ? -65.10 -142.27 149 1 GLU B 1893 ? ? 133.29 149.87 150 1 PHE B 1912 ? ? -100.14 -88.43 151 1 LYS B 1913 ? ? -176.63 84.13 152 1 GLU B 1914 ? ? 78.83 143.77 153 1 ASN B 1915 ? ? -174.79 -58.05 154 1 MET B 1926 ? ? 45.03 -136.49 155 1 LEU B 1932 ? ? -116.55 66.79 156 1 ASP B 1937 ? ? -106.64 -81.36 157 1 GLN B 1938 ? ? -33.18 123.62 158 1 MET B 1947 ? ? -166.98 107.29 159 1 SER B 1949 ? ? -38.18 132.01 160 1 ASN B 1950 ? ? -64.00 5.17 161 1 ASN B 1952 ? ? -54.38 32.62 162 1 HIS B 1954 ? ? -56.36 105.19 163 1 ARG B 1966 ? ? -53.79 -91.62 164 1 LYS B 1967 ? ? 30.87 -138.97 165 1 LYS B 1968 ? ? -56.64 -76.10 166 1 SER B 1991 ? ? 25.99 -123.59 167 1 LEU B 2001 ? ? -66.86 4.18 168 1 HIS B 2007 ? ? -80.22 42.67 169 1 ALA B 2008 ? ? -143.38 -3.39 170 1 SER B 2011 ? ? -36.40 136.80 171 1 CYS B 2021 ? ? -119.16 77.47 172 1 ALA B 2028 ? ? -65.10 -77.41 173 1 PHE B 2035 ? ? -71.63 -154.84 174 1 GLN B 2036 ? ? 49.27 14.14 175 1 TRP B 2046 ? ? 125.12 42.42 176 1 LYS B 2049 ? ? 104.80 -70.54 177 1 LEU B 2050 ? ? -58.95 1.57 178 1 ALA B 2061 ? ? 66.12 143.76 179 1 SER B 2063 ? ? -171.80 135.62 180 1 PRO B 2067 ? ? -50.50 -81.05 181 1 ALA B 2077 ? ? 137.56 131.59 182 1 GLN B 2091 ? ? -109.37 -101.63 183 1 LYS B 2092 ? ? -95.22 -82.79 184 1 ASP B 2108 ? ? -110.92 -76.27 185 1 LYS B 2110 ? ? -84.82 -74.46 186 1 ASN B 2118 ? ? -33.78 159.29 187 1 SER B 2119 ? ? -16.49 106.53 188 1 THR B 2120 ? ? -133.46 -67.36 189 1 SER B 2132 ? ? -67.20 17.13 190 1 SER B 2133 ? ? -178.60 -17.79 191 1 ILE B 2158 ? ? -151.80 -16.49 192 1 SER B 2160 ? ? -62.52 99.46 193 1 MET B 2164 ? ? -173.43 149.97 194 1 CYS B 2169 ? ? 179.47 149.53 195 1 ASP B 2170 ? ? -65.91 -172.69 196 1 SER B 2173 ? ? 55.02 19.65 197 1 CYS B 2174 ? ? -119.94 58.55 198 1 LYS B 2183 ? ? 50.78 6.36 199 1 ASP B 2187 ? ? -59.48 -76.67 200 1 ALA B 2188 ? ? -76.69 47.27 201 1 SER B 2193 ? ? -66.75 14.12 202 1 SER B 2194 ? ? 120.33 172.31 203 1 PHE B 2200 ? ? -101.29 -70.97 204 1 THR B 2202 ? ? -156.96 84.08 205 1 LEU B 2210 ? ? -13.37 -47.43 206 1 LEU B 2212 ? ? -7.01 106.10 207 1 ARG B 2215 ? ? -70.93 -71.36 208 1 ASN B 2217 ? ? -116.73 69.69 209 1 ALA B 2218 ? ? 167.88 169.90 210 1 LYS B 2227 ? ? -101.62 62.04 211 1 LYS B 2236 ? ? -97.65 -153.16 212 1 LEU B 2251 ? ? 62.48 -34.77 213 1 LEU B 2252 ? ? -47.54 -111.81 214 1 SER B 2265 ? ? -128.30 -155.51 215 1 GLN B 2266 ? ? -161.44 -29.80 216 1 ASN B 2277 ? ? -165.94 48.33 217 1 ASN B 2286 ? ? -69.75 -178.55 218 1 PHE B 2290 ? ? -72.25 -146.06 219 1 THR B 2291 ? ? 56.89 97.23 220 1 ASP B 2298 ? ? -43.63 -90.96 221 1 ARG B 2307 ? ? -165.26 108.48 222 1 GLN B 2311 ? ? -88.79 -72.32 223 1 TRP B 2313 ? ? -117.61 -130.35 224 1 VAL B 2314 ? ? -138.13 -65.48 225 1 MET B 2321 ? ? 170.17 150.07 226 1 CYS B 2326 ? ? -170.54 -153.07 227 1 ALA B 2328 ? ? -107.76 -145.09 228 1 LEU B 2331 ? ? 108.61 -158.90 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 ALA A 108 ? ? SER A 109 ? ? 146.82 2 1 PHE A 436 ? ? LYS A 437 ? ? 143.67 3 1 LEU A 547 ? ? ILE A 548 ? ? 144.70 4 1 ARG A 583 ? ? SER A 584 ? ? 148.80 5 1 HIS A 693 ? ? ASN A 694 ? ? 145.88 6 1 GLY B 1710 ? ? MET B 1711 ? ? -147.44 7 1 ASN B 2141 ? ? PRO B 2142 ? ? 143.36 8 1 LEU B 2319 ? ? ARG B 2320 ? ? 147.67 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1755 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # 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 17 ? A MET 17 2 1 Y 1 A GLN 18 ? A GLN 18 3 1 Y 1 A SER 19 ? A SER 19 4 1 Y 1 A ASP 20 ? A ASP 20 5 1 Y 1 A LEU 21 ? A LEU 21 6 1 Y 1 A GLY 22 ? A GLY 22 7 1 Y 1 A GLU 23 ? A GLU 23 8 1 Y 1 A LEU 24 ? A LEU 24 9 1 Y 1 A PRO 25 ? A PRO 25 10 1 Y 1 A VAL 26 ? A VAL 26 11 1 Y 1 A ASP 27 ? A ASP 27 12 1 Y 1 A ALA 28 ? A ALA 28 13 1 Y 1 A ARG 29 ? A ARG 29 14 1 Y 1 A PHE 30 ? A PHE 30 15 1 Y 1 A PRO 31 ? A PRO 31 16 1 Y 1 A PRO 32 ? A PRO 32 17 1 Y 1 A ARG 33 ? A ARG 33 18 1 Y 1 A VAL 34 ? A VAL 34 19 1 Y 1 A PRO 35 ? A PRO 35 20 1 Y 1 A LYS 36 ? A LYS 36 21 1 Y 1 A SER 37 ? A SER 37 22 1 Y 1 A PHE 38 ? A PHE 38 23 1 Y 1 A PRO 39 ? A PRO 39 24 1 Y 1 A PHE 40 ? A PHE 40 25 1 Y 1 A ASN 41 ? A ASN 41 26 1 Y 1 A THR 42 ? A THR 42 27 1 Y 1 A SER 43 ? A SER 43 28 1 Y 1 A GLU 211 ? A GLU 211 29 1 Y 1 A THR 212 ? A THR 212 30 1 Y 1 A LYS 213 ? A LYS 213 31 1 Y 1 A ASN 214 ? A ASN 214 32 1 Y 1 A SER 215 ? A SER 215 33 1 Y 1 A LEU 216 ? A LEU 216 34 1 Y 1 A MET 217 ? A MET 217 35 1 Y 1 A GLN 218 ? A GLN 218 36 1 Y 1 A ASP 219 ? A ASP 219 37 1 Y 1 A ARG 220 ? A ARG 220 38 1 Y 1 A ASP 221 ? A ASP 221 39 1 Y 1 A ALA 222 ? A ALA 222 40 1 Y 1 A ALA 223 ? A ALA 223 41 1 Y 1 A SER 224 ? A SER 224 42 1 Y 1 A ALA 225 ? A ALA 225 43 1 Y 1 A ARG 226 ? A ARG 226 44 1 Y 1 A ALA 227 ? A ALA 227 45 1 Y 1 A TRP 228 ? A TRP 228 46 1 Y 1 A GLN 334 ? A GLN 334 47 1 Y 1 A LEU 335 ? A LEU 335 48 1 Y 1 A ARG 336 ? A ARG 336 49 1 Y 1 A MET 337 ? A MET 337 50 1 Y 1 A LYS 338 ? A LYS 338 51 1 Y 1 A ASN 339 ? A ASN 339 52 1 Y 1 A ASN 340 ? A ASN 340 53 1 Y 1 A GLU 341 ? A GLU 341 54 1 Y 1 A GLU 342 ? A GLU 342 55 1 Y 1 A ALA 343 ? A ALA 343 56 1 Y 1 A GLU 344 ? A GLU 344 57 1 Y 1 A ASP 345 ? A ASP 345 58 1 Y 1 A TYR 346 ? A TYR 346 59 1 Y 1 A ASP 347 ? A ASP 347 60 1 Y 1 A ASP 348 ? A ASP 348 61 1 Y 1 A ASP 349 ? A ASP 349 62 1 Y 1 A LEU 350 ? A LEU 350 63 1 Y 1 A THR 351 ? A THR 351 64 1 Y 1 A ASP 352 ? A ASP 352 65 1 Y 1 A SER 353 ? A SER 353 66 1 Y 1 A GLU 354 ? A GLU 354 67 1 Y 1 A MET 355 ? A MET 355 68 1 Y 1 A ASP 356 ? A ASP 356 69 1 Y 1 A VAL 357 ? A VAL 357 70 1 Y 1 A VAL 358 ? A VAL 358 71 1 Y 1 A ARG 359 ? A ARG 359 72 1 Y 1 A PHE 360 ? A PHE 360 73 1 Y 1 A ASP 361 ? A ASP 361 74 1 Y 1 A ASP 362 ? A ASP 362 75 1 Y 1 A ASP 363 ? A ASP 363 76 1 Y 1 A ASN 364 ? A ASN 364 77 1 Y 1 A SER 365 ? A SER 365 78 1 Y 1 A PRO 366 ? A PRO 366 79 1 Y 1 A SER 367 ? A SER 367 80 1 Y 1 A PHE 368 ? A PHE 368 81 1 Y 1 A ILE 369 ? A ILE 369 82 1 Y 1 A GLN 370 ? A GLN 370 83 1 Y 1 A ILE 371 ? A ILE 371 84 1 Y 1 A ARG 372 ? A ARG 372 85 1 Y 1 A SER 373 ? A SER 373 86 1 Y 1 A VAL 374 ? A VAL 374 87 1 Y 1 A ALA 375 ? A ALA 375 88 1 Y 1 A LYS 376 ? A LYS 376 89 1 Y 1 A SER 558 ? A SER 558 90 1 Y 1 A VAL 559 ? A VAL 559 91 1 Y 1 A ASP 560 ? A ASP 560 92 1 Y 1 A GLN 561 ? A GLN 561 93 1 Y 1 A ARG 562 ? A ARG 562 94 1 Y 1 A GLY 563 ? A GLY 563 95 1 Y 1 A ASN 564 ? A ASN 564 96 1 Y 1 A GLN 565 ? A GLN 565 97 1 Y 1 A ILE 566 ? A ILE 566 98 1 Y 1 A MET 567 ? A MET 567 99 1 Y 1 A SER 568 ? A SER 568 100 1 Y 1 A ASP 569 ? A ASP 569 101 1 Y 1 A LYS 570 ? A LYS 570 102 1 Y 1 A ASN 714 ? A ASN 714 103 1 Y 1 A THR 715 ? A THR 715 104 1 Y 1 A GLY 716 ? A GLY 716 105 1 Y 1 A ASP 717 ? A ASP 717 106 1 Y 1 A TYR 718 ? A TYR 718 107 1 Y 1 A TYR 719 ? A TYR 719 108 1 Y 1 A GLU 720 ? A GLU 720 109 1 Y 1 A ASP 721 ? A ASP 721 110 1 Y 1 A SER 722 ? A SER 722 111 1 Y 1 A TYR 723 ? A TYR 723 112 1 Y 1 A GLU 724 ? A GLU 724 113 1 Y 1 A ASP 725 ? A ASP 725 114 1 Y 1 A ILE 726 ? A ILE 726 115 1 Y 1 A SER 727 ? A SER 727 116 1 Y 1 A ALA 728 ? A ALA 728 117 1 Y 1 A TYR 729 ? A TYR 729 118 1 Y 1 A LEU 730 ? A LEU 730 119 1 Y 1 A LEU 731 ? A LEU 731 120 1 Y 1 A SER 732 ? A SER 732 121 1 Y 1 A LYS 733 ? A LYS 733 122 1 Y 1 A ASN 734 ? A ASN 734 123 1 Y 1 A ASN 735 ? A ASN 735 124 1 Y 1 A ALA 736 ? A ALA 736 125 1 Y 1 A ILE 737 ? A ILE 737 126 1 Y 1 A GLU 738 ? A GLU 738 127 1 Y 1 A PRO 739 ? A PRO 739 128 1 Y 1 A ARG 740 ? A ARG 740 129 1 Y 1 A SER 741 ? A SER 741 130 1 Y 1 A PHE 742 ? A PHE 742 131 1 Y 1 A SER 743 ? A SER 743 132 1 Y 1 A GLN 744 ? A GLN 744 133 1 Y 1 A ASN 745 ? A ASN 745 134 1 Y 1 A SER 746 ? A SER 746 135 1 Y 1 A ARG 747 ? A ARG 747 136 1 Y 1 A HIS 748 ? A HIS 748 137 1 Y 1 A PRO 749 ? A PRO 749 138 1 Y 1 A SER 750 ? A SER 750 139 1 Y 1 A GLN 751 ? A GLN 751 140 1 Y 1 A ASN 752 ? A ASN 752 141 1 Y 1 A PRO 753 ? A PRO 753 142 1 Y 1 A PRO 754 ? A PRO 754 143 1 Y 1 A VAL 755 ? A VAL 755 144 1 Y 1 A LEU 756 ? A LEU 756 145 1 Y 1 A LYS 757 ? A LYS 757 146 1 Y 1 A ARG 758 ? A ARG 758 147 1 Y 1 A HIS 759 ? A HIS 759 148 1 Y 1 A GLN 760 ? A GLN 760 149 1 Y 1 B ARG 1648 ? B ARG 1 150 1 Y 1 B GLU 1649 ? B GLU 2 151 1 Y 1 B ILE 1650 ? B ILE 3 152 1 Y 1 B THR 1651 ? B THR 4 153 1 Y 1 B ARG 1652 ? B ARG 5 154 1 Y 1 B THR 1653 ? B THR 6 155 1 Y 1 B THR 1654 ? B THR 7 156 1 Y 1 B LEU 1655 ? B LEU 8 157 1 Y 1 B GLN 1656 ? B GLN 9 158 1 Y 1 B SER 1657 ? B SER 10 159 1 Y 1 B ASP 1658 ? B ASP 11 160 1 Y 1 B GLN 1659 ? B GLN 12 161 1 Y 1 B GLU 1660 ? B GLU 13 162 1 Y 1 B GLU 1661 ? B GLU 14 163 1 Y 1 B ILE 1662 ? B ILE 15 164 1 Y 1 B ASP 1663 ? B ASP 16 165 1 Y 1 B TYR 1664 ? B TYR 17 166 1 Y 1 B ASP 1665 ? B ASP 18 167 1 Y 1 B ASP 1666 ? B ASP 19 168 1 Y 1 B THR 1667 ? B THR 20 169 1 Y 1 B ILE 1668 ? B ILE 21 170 1 Y 1 B SER 1669 ? B SER 22 171 1 Y 1 B VAL 1670 ? B VAL 23 172 1 Y 1 B GLU 1671 ? B GLU 24 173 1 Y 1 B MET 1672 ? B MET 25 174 1 Y 1 B LYS 1673 ? B LYS 26 175 1 Y 1 B LYS 1674 ? B LYS 27 176 1 Y 1 B GLU 1675 ? B GLU 28 177 1 Y 1 B ASP 1676 ? B ASP 29 178 1 Y 1 B PHE 1677 ? B PHE 30 179 1 Y 1 B ASP 1678 ? B ASP 31 180 1 Y 1 B ILE 1679 ? B ILE 32 181 1 Y 1 B TYR 1680 ? B TYR 33 182 1 Y 1 B ASP 1681 ? B ASP 34 183 1 Y 1 B GLU 1682 ? B GLU 35 184 1 Y 1 B ASP 1683 ? B ASP 36 185 1 Y 1 B GLU 1684 ? B GLU 37 186 1 Y 1 B ASN 1685 ? B ASN 38 187 1 Y 1 B GLN 1686 ? B GLN 39 188 1 Y 1 B SER 1687 ? B SER 40 189 1 Y 1 B PRO 1688 ? B PRO 41 190 1 Y 1 B ARG 1689 ? B ARG 42 191 1 Y 1 B SER 1690 ? B SER 43 192 1 Y 1 B PHE 1691 ? B PHE 44 193 1 Y 1 B GLN 1692 ? B GLN 45 194 1 Y 1 B SER 1714 ? B SER 67 195 1 Y 1 B PRO 1715 ? B PRO 68 196 1 Y 1 B HIS 1716 ? B HIS 69 197 1 Y 1 B VAL 1717 ? B VAL 70 198 1 Y 1 B LEU 1718 ? B LEU 71 199 1 Y 1 B ARG 1719 ? B ARG 72 200 1 Y 1 B ASN 1720 ? B ASN 73 201 1 Y 1 B ARG 1721 ? B ARG 74 202 1 Y 1 B ALA 1722 ? B ALA 75 203 1 Y 1 B GLN 1723 ? B GLN 76 204 1 Y 1 B SER 1724 ? B SER 77 205 1 Y 1 B GLY 1725 ? B GLY 78 206 1 Y 1 B GLN 1796 ? B GLN 149 207 1 Y 1 B ARG 1797 ? B ARG 150 208 1 Y 1 B GLN 1798 ? B GLN 151 209 1 Y 1 B GLY 1799 ? B GLY 152 210 1 Y 1 B ALA 1800 ? B ALA 153 211 1 Y 1 B GLU 1801 ? B GLU 154 212 1 Y 1 B MET 1895 ? B MET 248 213 1 Y 1 B GLU 1896 ? B GLU 249 214 1 Y 1 B ARG 1897 ? B ARG 250 215 1 Y 1 B ASN 1898 ? B ASN 251 216 1 Y 1 B CYS 1899 ? B CYS 252 217 1 Y 1 B ARG 1900 ? B ARG 253 218 1 Y 1 B ALA 1901 ? B ALA 254 219 1 Y 1 B PRO 1902 ? B PRO 255 220 1 Y 1 B CYS 1903 ? B CYS 256 221 1 Y 1 B ASN 1904 ? B ASN 257 222 1 Y 1 B ILE 1905 ? B ILE 258 223 1 Y 1 B GLN 1906 ? B GLN 259 224 1 Y 1 B MET 1907 ? B MET 260 225 1 Y 1 B GLU 1908 ? B GLU 261 226 1 Y 1 B ASP 1909 ? B ASP 262 227 1 Y 1 B PRO 1910 ? B PRO 263 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'ZINC ION' ZN 4 'CALCIUM ION' CA 5 N-ACETYL-D-GLUCOSAMINE NAG 6 1,2-ETHANEDIOL EDO 7 'COPPER (I) ION' CU1 8 BETA-D-MANNOSE BMA #