data_4MMY # _entry.id 4MMY # _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 4MMY RCSB RCSB082112 WWPDB D_1000082112 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1JV2 'Integrin alpha-V complexed with a high affinity variant of FN10' unspecified PDB 1L5G 'Integrin alpha-V complexed with a high affinity variant of FN10' unspecified PDB 3IJE 'Integrin alpha-V complexed with a high affinity variant of FN10' unspecified PDB 4G1M 'Integrin alpha-V complexed with a high affinity variant of FN10' unspecified PDB 4G1E 'Integrin alpha-V complexed with a high affinity variant of FN10' unspecified PDB 4MMX . unspecified PDB 4MMZ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MMY _pdbx_database_status.recvd_initial_deposition_date 2013-09-09 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'van Agthoven, J.' 1 'Xiong, J.' 2 'Arnaout, M.A.' 3 # _citation.id primary _citation.title 'Structural basis for pure antagonism of integrin alpha V beta 3 by a high-affinity form of fibronectin.' _citation.journal_abbrev Nat.Struct.Mol.Biol. _citation.journal_volume 21 _citation.page_first 383 _citation.page_last 388 _citation.year 2014 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1545-9993 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24658351 _citation.pdbx_database_id_DOI 10.1038/nsmb.2797 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Van Agthoven, J.F.' 1 primary 'Xiong, J.P.' 2 primary 'Alonso, J.L.' 3 primary 'Rui, X.' 4 primary 'Adair, B.D.' 5 primary 'Goodman, S.L.' 6 primary 'Arnaout, M.A.' 7 # _cell.entry_id 4MMY _cell.length_a 130.018 _cell.length_b 130.018 _cell.length_c 308.203 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4MMY _symmetry.space_group_name_H-M 'P 32 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 154 _symmetry.space_group_name_Hall ? # 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 'Integrin alpha-V' 106048.359 1 ? ? 'Extracellular domain (UNP residues 31-989)' ? 2 polymer man 'Integrin beta-3' 76523.125 1 ? ? 'Extracellular domain (UNP residues 27-718)' ? 3 polymer man Fibronectin 10505.757 1 ? 'TGRGDSPASS to IARGDWNDG' 'Fibronectin type-III domain 10 (UNP residues 1448-1540)' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 23 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 6 ? ? ? ? 6 non-polymer man ALPHA-D-MANNOSE 180.156 4 ? ? ? ? 7 non-polymer syn 'MANGANESE (II) ION' 54.938 8 ? ? ? ? 8 water nat water 18.015 5 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Vitronectin receptor subunit alpha, Integrin alpha-V heavy chain, Integrin alpha-V light chain' 2 'Platelet membrane glycoprotein IIIa, GPIIIa' 3 'FN, Cold-insoluble globulin, CIG' # 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 ;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYE AELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSS NLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWP YKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCL KIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAP ; ;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYE AELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSS NLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWP YKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCL KIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAP ; A ? 2 'polypeptide(L)' no no ;GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPD ; ;GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPD ; B ? 3 'polypeptide(L)' no no ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVIARGDW NDGSKPISINYRTGKKGK ; ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVIARGDW NDGSKPISINYRTGKKGK ; C ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 PHE n 1 2 ASN n 1 3 LEU n 1 4 ASP n 1 5 VAL n 1 6 ASP n 1 7 SER n 1 8 PRO n 1 9 ALA n 1 10 GLU n 1 11 TYR n 1 12 SER n 1 13 GLY n 1 14 PRO n 1 15 GLU n 1 16 GLY n 1 17 SER n 1 18 TYR n 1 19 PHE n 1 20 GLY n 1 21 PHE n 1 22 ALA n 1 23 VAL n 1 24 ASP n 1 25 PHE n 1 26 PHE n 1 27 VAL n 1 28 PRO n 1 29 SER n 1 30 ALA n 1 31 SER n 1 32 SER n 1 33 ARG n 1 34 MET n 1 35 PHE n 1 36 LEU n 1 37 LEU n 1 38 VAL n 1 39 GLY n 1 40 ALA n 1 41 PRO n 1 42 LYS n 1 43 ALA n 1 44 ASN n 1 45 THR n 1 46 THR n 1 47 GLN n 1 48 PRO n 1 49 GLY n 1 50 ILE n 1 51 VAL n 1 52 GLU n 1 53 GLY n 1 54 GLY n 1 55 GLN n 1 56 VAL n 1 57 LEU n 1 58 LYS n 1 59 CYS n 1 60 ASP n 1 61 TRP n 1 62 SER n 1 63 SER n 1 64 THR n 1 65 ARG n 1 66 ARG n 1 67 CYS n 1 68 GLN n 1 69 PRO n 1 70 ILE n 1 71 GLU n 1 72 PHE n 1 73 ASP n 1 74 ALA n 1 75 THR n 1 76 GLY n 1 77 ASN n 1 78 ARG n 1 79 ASP n 1 80 TYR n 1 81 ALA n 1 82 LYS n 1 83 ASP n 1 84 ASP n 1 85 PRO n 1 86 LEU n 1 87 GLU n 1 88 PHE n 1 89 LYS n 1 90 SER n 1 91 HIS n 1 92 GLN n 1 93 TRP n 1 94 PHE n 1 95 GLY n 1 96 ALA n 1 97 SER n 1 98 VAL n 1 99 ARG n 1 100 SER n 1 101 LYS n 1 102 GLN n 1 103 ASP n 1 104 LYS n 1 105 ILE n 1 106 LEU n 1 107 ALA n 1 108 CYS n 1 109 ALA n 1 110 PRO n 1 111 LEU n 1 112 TYR n 1 113 HIS n 1 114 TRP n 1 115 ARG n 1 116 THR n 1 117 GLU n 1 118 MET n 1 119 LYS n 1 120 GLN n 1 121 GLU n 1 122 ARG n 1 123 GLU n 1 124 PRO n 1 125 VAL n 1 126 GLY n 1 127 THR n 1 128 CYS n 1 129 PHE n 1 130 LEU n 1 131 GLN n 1 132 ASP n 1 133 GLY n 1 134 THR n 1 135 LYS n 1 136 THR n 1 137 VAL n 1 138 GLU n 1 139 TYR n 1 140 ALA n 1 141 PRO n 1 142 CYS n 1 143 ARG n 1 144 SER n 1 145 GLN n 1 146 ASP n 1 147 ILE n 1 148 ASP n 1 149 ALA n 1 150 ASP n 1 151 GLY n 1 152 GLN n 1 153 GLY n 1 154 PHE n 1 155 CYS n 1 156 GLN n 1 157 GLY n 1 158 GLY n 1 159 PHE n 1 160 SER n 1 161 ILE n 1 162 ASP n 1 163 PHE n 1 164 THR n 1 165 LYS n 1 166 ALA n 1 167 ASP n 1 168 ARG n 1 169 VAL n 1 170 LEU n 1 171 LEU n 1 172 GLY n 1 173 GLY n 1 174 PRO n 1 175 GLY n 1 176 SER n 1 177 PHE n 1 178 TYR n 1 179 TRP n 1 180 GLN n 1 181 GLY n 1 182 GLN n 1 183 LEU n 1 184 ILE n 1 185 SER n 1 186 ASP n 1 187 GLN n 1 188 VAL n 1 189 ALA n 1 190 GLU n 1 191 ILE n 1 192 VAL n 1 193 SER n 1 194 LYS n 1 195 TYR n 1 196 ASP n 1 197 PRO n 1 198 ASN n 1 199 VAL n 1 200 TYR n 1 201 SER n 1 202 ILE n 1 203 LYS n 1 204 TYR n 1 205 ASN n 1 206 ASN n 1 207 GLN n 1 208 LEU n 1 209 ALA n 1 210 THR n 1 211 ARG n 1 212 THR n 1 213 ALA n 1 214 GLN n 1 215 ALA n 1 216 ILE n 1 217 PHE n 1 218 ASP n 1 219 ASP n 1 220 SER n 1 221 TYR n 1 222 LEU n 1 223 GLY n 1 224 TYR n 1 225 SER n 1 226 VAL n 1 227 ALA n 1 228 VAL n 1 229 GLY n 1 230 ASP n 1 231 PHE n 1 232 ASN n 1 233 GLY n 1 234 ASP n 1 235 GLY n 1 236 ILE n 1 237 ASP n 1 238 ASP n 1 239 PHE n 1 240 VAL n 1 241 SER n 1 242 GLY n 1 243 VAL n 1 244 PRO n 1 245 ARG n 1 246 ALA n 1 247 ALA n 1 248 ARG n 1 249 THR n 1 250 LEU n 1 251 GLY n 1 252 MET n 1 253 VAL n 1 254 TYR n 1 255 ILE n 1 256 TYR n 1 257 ASP n 1 258 GLY n 1 259 LYS n 1 260 ASN n 1 261 MET n 1 262 SER n 1 263 SER n 1 264 LEU n 1 265 TYR n 1 266 ASN n 1 267 PHE n 1 268 THR n 1 269 GLY n 1 270 GLU n 1 271 GLN n 1 272 MET n 1 273 ALA n 1 274 ALA n 1 275 TYR n 1 276 PHE n 1 277 GLY n 1 278 PHE n 1 279 SER n 1 280 VAL n 1 281 ALA n 1 282 ALA n 1 283 THR n 1 284 ASP n 1 285 ILE n 1 286 ASN n 1 287 GLY n 1 288 ASP n 1 289 ASP n 1 290 TYR n 1 291 ALA n 1 292 ASP n 1 293 VAL n 1 294 PHE n 1 295 ILE n 1 296 GLY n 1 297 ALA n 1 298 PRO n 1 299 LEU n 1 300 PHE n 1 301 MET n 1 302 ASP n 1 303 ARG n 1 304 GLY n 1 305 SER n 1 306 ASP n 1 307 GLY n 1 308 LYS n 1 309 LEU n 1 310 GLN n 1 311 GLU n 1 312 VAL n 1 313 GLY n 1 314 GLN n 1 315 VAL n 1 316 SER n 1 317 VAL n 1 318 SER n 1 319 LEU n 1 320 GLN n 1 321 ARG n 1 322 ALA n 1 323 SER n 1 324 GLY n 1 325 ASP n 1 326 PHE n 1 327 GLN n 1 328 THR n 1 329 THR n 1 330 LYS n 1 331 LEU n 1 332 ASN n 1 333 GLY n 1 334 PHE n 1 335 GLU n 1 336 VAL n 1 337 PHE n 1 338 ALA n 1 339 ARG n 1 340 PHE n 1 341 GLY n 1 342 SER n 1 343 ALA n 1 344 ILE n 1 345 ALA n 1 346 PRO n 1 347 LEU n 1 348 GLY n 1 349 ASP n 1 350 LEU n 1 351 ASP n 1 352 GLN n 1 353 ASP n 1 354 GLY n 1 355 PHE n 1 356 ASN n 1 357 ASP n 1 358 ILE n 1 359 ALA n 1 360 ILE n 1 361 ALA n 1 362 ALA n 1 363 PRO n 1 364 TYR n 1 365 GLY n 1 366 GLY n 1 367 GLU n 1 368 ASP n 1 369 LYS n 1 370 LYS n 1 371 GLY n 1 372 ILE n 1 373 VAL n 1 374 TYR n 1 375 ILE n 1 376 PHE n 1 377 ASN n 1 378 GLY n 1 379 ARG n 1 380 SER n 1 381 THR n 1 382 GLY n 1 383 LEU n 1 384 ASN n 1 385 ALA n 1 386 VAL n 1 387 PRO n 1 388 SER n 1 389 GLN n 1 390 ILE n 1 391 LEU n 1 392 GLU n 1 393 GLY n 1 394 GLN n 1 395 TRP n 1 396 ALA n 1 397 ALA n 1 398 ARG n 1 399 SER n 1 400 MET n 1 401 PRO n 1 402 PRO n 1 403 SER n 1 404 PHE n 1 405 GLY n 1 406 TYR n 1 407 SER n 1 408 MET n 1 409 LYS n 1 410 GLY n 1 411 ALA n 1 412 THR n 1 413 ASP n 1 414 ILE n 1 415 ASP n 1 416 LYS n 1 417 ASN n 1 418 GLY n 1 419 TYR n 1 420 PRO n 1 421 ASP n 1 422 LEU n 1 423 ILE n 1 424 VAL n 1 425 GLY n 1 426 ALA n 1 427 PHE n 1 428 GLY n 1 429 VAL n 1 430 ASP n 1 431 ARG n 1 432 ALA n 1 433 ILE n 1 434 LEU n 1 435 TYR n 1 436 ARG n 1 437 ALA n 1 438 ARG n 1 439 PRO n 1 440 VAL n 1 441 ILE n 1 442 THR n 1 443 VAL n 1 444 ASN n 1 445 ALA n 1 446 GLY n 1 447 LEU n 1 448 GLU n 1 449 VAL n 1 450 TYR n 1 451 PRO n 1 452 SER n 1 453 ILE n 1 454 LEU n 1 455 ASN n 1 456 GLN n 1 457 ASP n 1 458 ASN n 1 459 LYS n 1 460 THR n 1 461 CYS n 1 462 SER n 1 463 LEU n 1 464 PRO n 1 465 GLY n 1 466 THR n 1 467 ALA n 1 468 LEU n 1 469 LYS n 1 470 VAL n 1 471 SER n 1 472 CYS n 1 473 PHE n 1 474 ASN n 1 475 VAL n 1 476 ARG n 1 477 PHE n 1 478 CYS n 1 479 LEU n 1 480 LYS n 1 481 ALA n 1 482 ASP n 1 483 GLY n 1 484 LYS n 1 485 GLY n 1 486 VAL n 1 487 LEU n 1 488 PRO n 1 489 ARG n 1 490 LYS n 1 491 LEU n 1 492 ASN n 1 493 PHE n 1 494 GLN n 1 495 VAL n 1 496 GLU n 1 497 LEU n 1 498 LEU n 1 499 LEU n 1 500 ASP n 1 501 LYS n 1 502 LEU n 1 503 LYS n 1 504 GLN n 1 505 LYS n 1 506 GLY n 1 507 ALA n 1 508 ILE n 1 509 ARG n 1 510 ARG n 1 511 ALA n 1 512 LEU n 1 513 PHE n 1 514 LEU n 1 515 TYR n 1 516 SER n 1 517 ARG n 1 518 SER n 1 519 PRO n 1 520 SER n 1 521 HIS n 1 522 SER n 1 523 LYS n 1 524 ASN n 1 525 MET n 1 526 THR n 1 527 ILE n 1 528 SER n 1 529 ARG n 1 530 GLY n 1 531 GLY n 1 532 LEU n 1 533 MET n 1 534 GLN n 1 535 CYS n 1 536 GLU n 1 537 GLU n 1 538 LEU n 1 539 ILE n 1 540 ALA n 1 541 TYR n 1 542 LEU n 1 543 ARG n 1 544 ASP n 1 545 GLU n 1 546 SER n 1 547 GLU n 1 548 PHE n 1 549 ARG n 1 550 ASP n 1 551 LYS n 1 552 LEU n 1 553 THR n 1 554 PRO n 1 555 ILE n 1 556 THR n 1 557 ILE n 1 558 PHE n 1 559 MET n 1 560 GLU n 1 561 TYR n 1 562 ARG n 1 563 LEU n 1 564 ASP n 1 565 TYR n 1 566 ARG n 1 567 THR n 1 568 ALA n 1 569 ALA n 1 570 ASP n 1 571 THR n 1 572 THR n 1 573 GLY n 1 574 LEU n 1 575 GLN n 1 576 PRO n 1 577 ILE n 1 578 LEU n 1 579 ASN n 1 580 GLN n 1 581 PHE n 1 582 THR n 1 583 PRO n 1 584 ALA n 1 585 ASN n 1 586 ILE n 1 587 SER n 1 588 ARG n 1 589 GLN n 1 590 ALA n 1 591 HIS n 1 592 ILE n 1 593 LEU n 1 594 LEU n 1 595 ASP n 1 596 CYS n 1 597 GLY n 1 598 GLU n 1 599 ASP n 1 600 ASN n 1 601 VAL n 1 602 CYS n 1 603 LYS n 1 604 PRO n 1 605 LYS n 1 606 LEU n 1 607 GLU n 1 608 VAL n 1 609 SER n 1 610 VAL n 1 611 ASP n 1 612 SER n 1 613 ASP n 1 614 GLN n 1 615 LYS n 1 616 LYS n 1 617 ILE n 1 618 TYR n 1 619 ILE n 1 620 GLY n 1 621 ASP n 1 622 ASP n 1 623 ASN n 1 624 PRO n 1 625 LEU n 1 626 THR n 1 627 LEU n 1 628 ILE n 1 629 VAL n 1 630 LYS n 1 631 ALA n 1 632 GLN n 1 633 ASN n 1 634 GLN n 1 635 GLY n 1 636 GLU n 1 637 GLY n 1 638 ALA n 1 639 TYR n 1 640 GLU n 1 641 ALA n 1 642 GLU n 1 643 LEU n 1 644 ILE n 1 645 VAL n 1 646 SER n 1 647 ILE n 1 648 PRO n 1 649 LEU n 1 650 GLN n 1 651 ALA n 1 652 ASP n 1 653 PHE n 1 654 ILE n 1 655 GLY n 1 656 VAL n 1 657 VAL n 1 658 ARG n 1 659 ASN n 1 660 ASN n 1 661 GLU n 1 662 ALA n 1 663 LEU n 1 664 ALA n 1 665 ARG n 1 666 LEU n 1 667 SER n 1 668 CYS n 1 669 ALA n 1 670 PHE n 1 671 LYS n 1 672 THR n 1 673 GLU n 1 674 ASN n 1 675 GLN n 1 676 THR n 1 677 ARG n 1 678 GLN n 1 679 VAL n 1 680 VAL n 1 681 CYS n 1 682 ASP n 1 683 LEU n 1 684 GLY n 1 685 ASN n 1 686 PRO n 1 687 MET n 1 688 LYS n 1 689 ALA n 1 690 GLY n 1 691 THR n 1 692 GLN n 1 693 LEU n 1 694 LEU n 1 695 ALA n 1 696 GLY n 1 697 LEU n 1 698 ARG n 1 699 PHE n 1 700 SER n 1 701 VAL n 1 702 HIS n 1 703 GLN n 1 704 GLN n 1 705 SER n 1 706 GLU n 1 707 MET n 1 708 ASP n 1 709 THR n 1 710 SER n 1 711 VAL n 1 712 LYS n 1 713 PHE n 1 714 ASP n 1 715 LEU n 1 716 GLN n 1 717 ILE n 1 718 GLN n 1 719 SER n 1 720 SER n 1 721 ASN n 1 722 LEU n 1 723 PHE n 1 724 ASP n 1 725 LYS n 1 726 VAL n 1 727 SER n 1 728 PRO n 1 729 VAL n 1 730 VAL n 1 731 SER n 1 732 HIS n 1 733 LYS n 1 734 VAL n 1 735 ASP n 1 736 LEU n 1 737 ALA n 1 738 VAL n 1 739 LEU n 1 740 ALA n 1 741 ALA n 1 742 VAL n 1 743 GLU n 1 744 ILE n 1 745 ARG n 1 746 GLY n 1 747 VAL n 1 748 SER n 1 749 SER n 1 750 PRO n 1 751 ASP n 1 752 HIS n 1 753 VAL n 1 754 PHE n 1 755 LEU n 1 756 PRO n 1 757 ILE n 1 758 PRO n 1 759 ASN n 1 760 TRP n 1 761 GLU n 1 762 HIS n 1 763 LYS n 1 764 GLU n 1 765 ASN n 1 766 PRO n 1 767 GLU n 1 768 THR n 1 769 GLU n 1 770 GLU n 1 771 ASP n 1 772 VAL n 1 773 GLY n 1 774 PRO n 1 775 VAL n 1 776 VAL n 1 777 GLN n 1 778 HIS n 1 779 ILE n 1 780 TYR n 1 781 GLU n 1 782 LEU n 1 783 ARG n 1 784 ASN n 1 785 ASN n 1 786 GLY n 1 787 PRO n 1 788 SER n 1 789 SER n 1 790 PHE n 1 791 SER n 1 792 LYS n 1 793 ALA n 1 794 MET n 1 795 LEU n 1 796 HIS n 1 797 LEU n 1 798 GLN n 1 799 TRP n 1 800 PRO n 1 801 TYR n 1 802 LYS n 1 803 TYR n 1 804 ASN n 1 805 ASN n 1 806 ASN n 1 807 THR n 1 808 LEU n 1 809 LEU n 1 810 TYR n 1 811 ILE n 1 812 LEU n 1 813 HIS n 1 814 TYR n 1 815 ASP n 1 816 ILE n 1 817 ASP n 1 818 GLY n 1 819 PRO n 1 820 MET n 1 821 ASN n 1 822 CYS n 1 823 THR n 1 824 SER n 1 825 ASP n 1 826 MET n 1 827 GLU n 1 828 ILE n 1 829 ASN n 1 830 PRO n 1 831 LEU n 1 832 ARG n 1 833 ILE n 1 834 LYS n 1 835 ILE n 1 836 SER n 1 837 SER n 1 838 LEU n 1 839 GLN n 1 840 THR n 1 841 THR n 1 842 GLU n 1 843 LYS n 1 844 ASN n 1 845 ASP n 1 846 THR n 1 847 VAL n 1 848 ALA n 1 849 GLY n 1 850 GLN n 1 851 GLY n 1 852 GLU n 1 853 ARG n 1 854 ASP n 1 855 HIS n 1 856 LEU n 1 857 ILE n 1 858 THR n 1 859 LYS n 1 860 ARG n 1 861 ASP n 1 862 LEU n 1 863 ALA n 1 864 LEU n 1 865 SER n 1 866 GLU n 1 867 GLY n 1 868 ASP n 1 869 ILE n 1 870 HIS n 1 871 THR n 1 872 LEU n 1 873 GLY n 1 874 CYS n 1 875 GLY n 1 876 VAL n 1 877 ALA n 1 878 GLN n 1 879 CYS n 1 880 LEU n 1 881 LYS n 1 882 ILE n 1 883 VAL n 1 884 CYS n 1 885 GLN n 1 886 VAL n 1 887 GLY n 1 888 ARG n 1 889 LEU n 1 890 ASP n 1 891 ARG n 1 892 GLY n 1 893 LYS n 1 894 SER n 1 895 ALA n 1 896 ILE n 1 897 LEU n 1 898 TYR n 1 899 VAL n 1 900 LYS n 1 901 SER n 1 902 LEU n 1 903 LEU n 1 904 TRP n 1 905 THR n 1 906 GLU n 1 907 THR n 1 908 PHE n 1 909 MET n 1 910 ASN n 1 911 LYS n 1 912 GLU n 1 913 ASN n 1 914 GLN n 1 915 ASN n 1 916 HIS n 1 917 SER n 1 918 TYR n 1 919 SER n 1 920 LEU n 1 921 LYS n 1 922 SER n 1 923 SER n 1 924 ALA n 1 925 SER n 1 926 PHE n 1 927 ASN n 1 928 VAL n 1 929 ILE n 1 930 GLU n 1 931 PHE n 1 932 PRO n 1 933 TYR n 1 934 LYS n 1 935 ASN n 1 936 LEU n 1 937 PRO n 1 938 ILE n 1 939 GLU n 1 940 ASP n 1 941 ILE n 1 942 THR n 1 943 ASN n 1 944 SER n 1 945 THR n 1 946 LEU n 1 947 VAL n 1 948 THR n 1 949 THR n 1 950 ASN n 1 951 VAL n 1 952 THR n 1 953 TRP n 1 954 GLY n 1 955 ILE n 1 956 GLN n 1 957 PRO n 1 958 ALA n 1 959 PRO n 2 1 GLY n 2 2 PRO n 2 3 ASN n 2 4 ILE n 2 5 CYS n 2 6 THR n 2 7 THR n 2 8 ARG n 2 9 GLY n 2 10 VAL n 2 11 SER n 2 12 SER n 2 13 CYS n 2 14 GLN n 2 15 GLN n 2 16 CYS n 2 17 LEU n 2 18 ALA n 2 19 VAL n 2 20 SER n 2 21 PRO n 2 22 MET n 2 23 CYS n 2 24 ALA n 2 25 TRP n 2 26 CYS n 2 27 SER n 2 28 ASP n 2 29 GLU n 2 30 ALA n 2 31 LEU n 2 32 PRO n 2 33 LEU n 2 34 GLY n 2 35 SER n 2 36 PRO n 2 37 ARG n 2 38 CYS n 2 39 ASP n 2 40 LEU n 2 41 LYS n 2 42 GLU n 2 43 ASN n 2 44 LEU n 2 45 LEU n 2 46 LYS n 2 47 ASP n 2 48 ASN n 2 49 CYS n 2 50 ALA n 2 51 PRO n 2 52 GLU n 2 53 SER n 2 54 ILE n 2 55 GLU n 2 56 PHE n 2 57 PRO n 2 58 VAL n 2 59 SER n 2 60 GLU n 2 61 ALA n 2 62 ARG n 2 63 VAL n 2 64 LEU n 2 65 GLU n 2 66 ASP n 2 67 ARG n 2 68 PRO n 2 69 LEU n 2 70 SER n 2 71 ASP n 2 72 LYS n 2 73 GLY n 2 74 SER n 2 75 GLY n 2 76 ASP n 2 77 SER n 2 78 SER n 2 79 GLN n 2 80 VAL n 2 81 THR n 2 82 GLN n 2 83 VAL n 2 84 SER n 2 85 PRO n 2 86 GLN n 2 87 ARG n 2 88 ILE n 2 89 ALA n 2 90 LEU n 2 91 ARG n 2 92 LEU n 2 93 ARG n 2 94 PRO n 2 95 ASP n 2 96 ASP n 2 97 SER n 2 98 LYS n 2 99 ASN n 2 100 PHE n 2 101 SER n 2 102 ILE n 2 103 GLN n 2 104 VAL n 2 105 ARG n 2 106 GLN n 2 107 VAL n 2 108 GLU n 2 109 ASP n 2 110 TYR n 2 111 PRO n 2 112 VAL n 2 113 ASP n 2 114 ILE n 2 115 TYR n 2 116 TYR n 2 117 LEU n 2 118 MET n 2 119 ASP n 2 120 LEU n 2 121 SER n 2 122 TYR n 2 123 SER n 2 124 MET n 2 125 LYS n 2 126 ASP n 2 127 ASP n 2 128 LEU n 2 129 TRP n 2 130 SER n 2 131 ILE n 2 132 GLN n 2 133 ASN n 2 134 LEU n 2 135 GLY n 2 136 THR n 2 137 LYS n 2 138 LEU n 2 139 ALA n 2 140 THR n 2 141 GLN n 2 142 MET n 2 143 ARG n 2 144 LYS n 2 145 LEU n 2 146 THR n 2 147 SER n 2 148 ASN n 2 149 LEU n 2 150 ARG n 2 151 ILE n 2 152 GLY n 2 153 PHE n 2 154 GLY n 2 155 ALA n 2 156 PHE n 2 157 VAL n 2 158 ASP n 2 159 LYS n 2 160 PRO n 2 161 VAL n 2 162 SER n 2 163 PRO n 2 164 TYR n 2 165 MET n 2 166 TYR n 2 167 ILE n 2 168 SER n 2 169 PRO n 2 170 PRO n 2 171 GLU n 2 172 ALA n 2 173 LEU n 2 174 GLU n 2 175 ASN n 2 176 PRO n 2 177 CYS n 2 178 TYR n 2 179 ASP n 2 180 MET n 2 181 LYS n 2 182 THR n 2 183 THR n 2 184 CYS n 2 185 LEU n 2 186 PRO n 2 187 MET n 2 188 PHE n 2 189 GLY n 2 190 TYR n 2 191 LYS n 2 192 HIS n 2 193 VAL n 2 194 LEU n 2 195 THR n 2 196 LEU n 2 197 THR n 2 198 ASP n 2 199 GLN n 2 200 VAL n 2 201 THR n 2 202 ARG n 2 203 PHE n 2 204 ASN n 2 205 GLU n 2 206 GLU n 2 207 VAL n 2 208 LYS n 2 209 LYS n 2 210 GLN n 2 211 SER n 2 212 VAL n 2 213 SER n 2 214 ARG n 2 215 ASN n 2 216 ARG n 2 217 ASP n 2 218 ALA n 2 219 PRO n 2 220 GLU n 2 221 GLY n 2 222 GLY n 2 223 PHE n 2 224 ASP n 2 225 ALA n 2 226 ILE n 2 227 MET n 2 228 GLN n 2 229 ALA n 2 230 THR n 2 231 VAL n 2 232 CYS n 2 233 ASP n 2 234 GLU n 2 235 LYS n 2 236 ILE n 2 237 GLY n 2 238 TRP n 2 239 ARG n 2 240 ASN n 2 241 ASP n 2 242 ALA n 2 243 SER n 2 244 HIS n 2 245 LEU n 2 246 LEU n 2 247 VAL n 2 248 PHE n 2 249 THR n 2 250 THR n 2 251 ASP n 2 252 ALA n 2 253 LYS n 2 254 THR n 2 255 HIS n 2 256 ILE n 2 257 ALA n 2 258 LEU n 2 259 ASP n 2 260 GLY n 2 261 ARG n 2 262 LEU n 2 263 ALA n 2 264 GLY n 2 265 ILE n 2 266 VAL n 2 267 GLN n 2 268 PRO n 2 269 ASN n 2 270 ASP n 2 271 GLY n 2 272 GLN n 2 273 CYS n 2 274 HIS n 2 275 VAL n 2 276 GLY n 2 277 SER n 2 278 ASP n 2 279 ASN n 2 280 HIS n 2 281 TYR n 2 282 SER n 2 283 ALA n 2 284 SER n 2 285 THR n 2 286 THR n 2 287 MET n 2 288 ASP n 2 289 TYR n 2 290 PRO n 2 291 SER n 2 292 LEU n 2 293 GLY n 2 294 LEU n 2 295 MET n 2 296 THR n 2 297 GLU n 2 298 LYS n 2 299 LEU n 2 300 SER n 2 301 GLN n 2 302 LYS n 2 303 ASN n 2 304 ILE n 2 305 ASN n 2 306 LEU n 2 307 ILE n 2 308 PHE n 2 309 ALA n 2 310 VAL n 2 311 THR n 2 312 GLU n 2 313 ASN n 2 314 VAL n 2 315 VAL n 2 316 ASN n 2 317 LEU n 2 318 TYR n 2 319 GLN n 2 320 ASN n 2 321 TYR n 2 322 SER n 2 323 GLU n 2 324 LEU n 2 325 ILE n 2 326 PRO n 2 327 GLY n 2 328 THR n 2 329 THR n 2 330 VAL n 2 331 GLY n 2 332 VAL n 2 333 LEU n 2 334 SER n 2 335 MET n 2 336 ASP n 2 337 SER n 2 338 SER n 2 339 ASN n 2 340 VAL n 2 341 LEU n 2 342 GLN n 2 343 LEU n 2 344 ILE n 2 345 VAL n 2 346 ASP n 2 347 ALA n 2 348 TYR n 2 349 GLY n 2 350 LYS n 2 351 ILE n 2 352 ARG n 2 353 SER n 2 354 LYS n 2 355 VAL n 2 356 GLU n 2 357 LEU n 2 358 GLU n 2 359 VAL n 2 360 ARG n 2 361 ASP n 2 362 LEU n 2 363 PRO n 2 364 GLU n 2 365 GLU n 2 366 LEU n 2 367 SER n 2 368 LEU n 2 369 SER n 2 370 PHE n 2 371 ASN n 2 372 ALA n 2 373 THR n 2 374 CYS n 2 375 LEU n 2 376 ASN n 2 377 ASN n 2 378 GLU n 2 379 VAL n 2 380 ILE n 2 381 PRO n 2 382 GLY n 2 383 LEU n 2 384 LYS n 2 385 SER n 2 386 CYS n 2 387 MET n 2 388 GLY n 2 389 LEU n 2 390 LYS n 2 391 ILE n 2 392 GLY n 2 393 ASP n 2 394 THR n 2 395 VAL n 2 396 SER n 2 397 PHE n 2 398 SER n 2 399 ILE n 2 400 GLU n 2 401 ALA n 2 402 LYS n 2 403 VAL n 2 404 ARG n 2 405 GLY n 2 406 CYS n 2 407 PRO n 2 408 GLN n 2 409 GLU n 2 410 LYS n 2 411 GLU n 2 412 LYS n 2 413 SER n 2 414 PHE n 2 415 THR n 2 416 ILE n 2 417 LYS n 2 418 PRO n 2 419 VAL n 2 420 GLY n 2 421 PHE n 2 422 LYS n 2 423 ASP n 2 424 SER n 2 425 LEU n 2 426 ILE n 2 427 VAL n 2 428 GLN n 2 429 VAL n 2 430 THR n 2 431 PHE n 2 432 ASP n 2 433 CYS n 2 434 ASP n 2 435 CYS n 2 436 ALA n 2 437 CYS n 2 438 GLN n 2 439 ALA n 2 440 GLN n 2 441 ALA n 2 442 GLU n 2 443 PRO n 2 444 ASN n 2 445 SER n 2 446 HIS n 2 447 ARG n 2 448 CYS n 2 449 ASN n 2 450 ASN n 2 451 GLY n 2 452 ASN n 2 453 GLY n 2 454 THR n 2 455 PHE n 2 456 GLU n 2 457 CYS n 2 458 GLY n 2 459 VAL n 2 460 CYS n 2 461 ARG n 2 462 CYS n 2 463 GLY n 2 464 PRO n 2 465 GLY n 2 466 TRP n 2 467 LEU n 2 468 GLY n 2 469 SER n 2 470 GLN n 2 471 CYS n 2 472 GLU n 2 473 CYS n 2 474 SER n 2 475 GLU n 2 476 GLU n 2 477 ASP n 2 478 TYR n 2 479 ARG n 2 480 PRO n 2 481 SER n 2 482 GLN n 2 483 GLN n 2 484 ASP n 2 485 GLU n 2 486 CYS n 2 487 SER n 2 488 PRO n 2 489 ARG n 2 490 GLU n 2 491 GLY n 2 492 GLN n 2 493 PRO n 2 494 VAL n 2 495 CYS n 2 496 SER n 2 497 GLN n 2 498 ARG n 2 499 GLY n 2 500 GLU n 2 501 CYS n 2 502 LEU n 2 503 CYS n 2 504 GLY n 2 505 GLN n 2 506 CYS n 2 507 VAL n 2 508 CYS n 2 509 HIS n 2 510 SER n 2 511 SER n 2 512 ASP n 2 513 PHE n 2 514 GLY n 2 515 LYS n 2 516 ILE n 2 517 THR n 2 518 GLY n 2 519 LYS n 2 520 TYR n 2 521 CYS n 2 522 GLU n 2 523 CYS n 2 524 ASP n 2 525 ASP n 2 526 PHE n 2 527 SER n 2 528 CYS n 2 529 VAL n 2 530 ARG n 2 531 TYR n 2 532 LYS n 2 533 GLY n 2 534 GLU n 2 535 MET n 2 536 CYS n 2 537 SER n 2 538 GLY n 2 539 HIS n 2 540 GLY n 2 541 GLN n 2 542 CYS n 2 543 SER n 2 544 CYS n 2 545 GLY n 2 546 ASP n 2 547 CYS n 2 548 LEU n 2 549 CYS n 2 550 ASP n 2 551 SER n 2 552 ASP n 2 553 TRP n 2 554 THR n 2 555 GLY n 2 556 TYR n 2 557 TYR n 2 558 CYS n 2 559 ASN n 2 560 CYS n 2 561 THR n 2 562 THR n 2 563 ARG n 2 564 THR n 2 565 ASP n 2 566 THR n 2 567 CYS n 2 568 MET n 2 569 SER n 2 570 SER n 2 571 ASN n 2 572 GLY n 2 573 LEU n 2 574 LEU n 2 575 CYS n 2 576 SER n 2 577 GLY n 2 578 ARG n 2 579 GLY n 2 580 LYS n 2 581 CYS n 2 582 GLU n 2 583 CYS n 2 584 GLY n 2 585 SER n 2 586 CYS n 2 587 VAL n 2 588 CYS n 2 589 ILE n 2 590 GLN n 2 591 PRO n 2 592 GLY n 2 593 SER n 2 594 TYR n 2 595 GLY n 2 596 ASP n 2 597 THR n 2 598 CYS n 2 599 GLU n 2 600 LYS n 2 601 CYS n 2 602 PRO n 2 603 THR n 2 604 CYS n 2 605 PRO n 2 606 ASP n 2 607 ALA n 2 608 CYS n 2 609 THR n 2 610 PHE n 2 611 LYS n 2 612 LYS n 2 613 GLU n 2 614 CYS n 2 615 VAL n 2 616 GLU n 2 617 CYS n 2 618 LYS n 2 619 LYS n 2 620 PHE n 2 621 ASP n 2 622 ARG n 2 623 GLY n 2 624 ALA n 2 625 LEU n 2 626 HIS n 2 627 ASP n 2 628 GLU n 2 629 ASN n 2 630 THR n 2 631 CYS n 2 632 ASN n 2 633 ARG n 2 634 TYR n 2 635 CYS n 2 636 ARG n 2 637 ASP n 2 638 GLU n 2 639 ILE n 2 640 GLU n 2 641 SER n 2 642 VAL n 2 643 LYS n 2 644 GLU n 2 645 LEU n 2 646 LYS n 2 647 ASP n 2 648 THR n 2 649 GLY n 2 650 LYS n 2 651 ASP n 2 652 ALA n 2 653 VAL n 2 654 ASN n 2 655 CYS n 2 656 THR n 2 657 TYR n 2 658 LYS n 2 659 ASN n 2 660 GLU n 2 661 ASP n 2 662 ASP n 2 663 CYS n 2 664 VAL n 2 665 VAL n 2 666 ARG n 2 667 PHE n 2 668 GLN n 2 669 TYR n 2 670 TYR n 2 671 GLU n 2 672 ASP n 2 673 SER n 2 674 SER n 2 675 GLY n 2 676 LYS n 2 677 SER n 2 678 ILE n 2 679 LEU n 2 680 TYR n 2 681 VAL n 2 682 VAL n 2 683 GLU n 2 684 GLU n 2 685 PRO n 2 686 GLU n 2 687 CYS n 2 688 PRO n 2 689 LYS n 2 690 GLY n 2 691 PRO n 2 692 ASP n 3 1 SER n 3 2 ASP n 3 3 VAL n 3 4 PRO n 3 5 ARG n 3 6 ASP n 3 7 LEU n 3 8 GLU n 3 9 VAL n 3 10 VAL n 3 11 ALA n 3 12 ALA n 3 13 THR n 3 14 PRO n 3 15 THR n 3 16 SER n 3 17 LEU n 3 18 LEU n 3 19 ILE n 3 20 SER n 3 21 TRP n 3 22 ASP n 3 23 ALA n 3 24 PRO n 3 25 ALA n 3 26 VAL n 3 27 THR n 3 28 VAL n 3 29 ARG n 3 30 TYR n 3 31 TYR n 3 32 ARG n 3 33 ILE n 3 34 THR n 3 35 TYR n 3 36 GLY n 3 37 GLU n 3 38 THR n 3 39 GLY n 3 40 GLY n 3 41 ASN n 3 42 SER n 3 43 PRO n 3 44 VAL n 3 45 GLN n 3 46 GLU n 3 47 PHE n 3 48 THR n 3 49 VAL n 3 50 PRO n 3 51 GLY n 3 52 SER n 3 53 LYS n 3 54 SER n 3 55 THR n 3 56 ALA n 3 57 THR n 3 58 ILE n 3 59 SER n 3 60 GLY n 3 61 LEU n 3 62 LYS n 3 63 PRO n 3 64 GLY n 3 65 VAL n 3 66 ASP n 3 67 TYR n 3 68 THR n 3 69 ILE n 3 70 THR n 3 71 VAL n 3 72 TYR n 3 73 ALA n 3 74 VAL n 3 75 ILE n 3 76 ALA n 3 77 ARG n 3 78 GLY n 3 79 ASP n 3 80 TRP n 3 81 ASN n 3 82 ASP n 3 83 GLY n 3 84 SER n 3 85 LYS n 3 86 PRO n 3 87 ILE n 3 88 SER n 3 89 ILE n 3 90 ASN n 3 91 TYR n 3 92 ARG n 3 93 THR n 3 94 GLY n 3 95 LYS n 3 96 LYS n 3 97 GLY n 3 98 LYS 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 ? 'ITGAV, MSK8, VNRA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 2 1 sample ? ? ? human ? 'ITGB3, GP3A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 3 1 sample ? ? ? human ? 'FN1, FN' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? plasmid ? ? ? pET ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP ITAV_HUMAN P06756 1 ;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYE AELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSS NLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWP YKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCL KIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAP ; 31 ? 2 UNP ITB3_HUMAN P05106 2 ;GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPD ; 27 ? 3 UNP FINC_HUMAN P02751 3 ;SDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDS PASSKPISINYRT ; 1448 ? # 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 4MMY A 1 ? 959 ? P06756 31 ? 989 ? 1 959 2 2 4MMY B 1 ? 692 ? P05106 27 ? 718 ? 1 692 3 3 4MMY C 1 ? 93 ? P02751 1448 ? 1540 ? 1417 1509 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 3 4MMY ILE C 75 ? UNP P02751 THR 1522 'ENGINEERED MUTATION' 1491 1 3 4MMY ALA C 76 ? UNP P02751 GLY 1523 'ENGINEERED MUTATION' 1492 2 3 4MMY TRP C 80 ? UNP P02751 SER 1527 'ENGINEERED MUTATION' 1496 3 3 4MMY ASN C 81 ? UNP P02751 PRO 1528 'ENGINEERED MUTATION' 1497 4 3 4MMY ASP C 82 ? UNP P02751 ALA 1529 'ENGINEERED MUTATION' 1498 5 3 4MMY GLY C 83 ? UNP P02751 SER 1530 'ENGINEERED MUTATION' 1499 6 3 4MMY GLY C 94 ? UNP P02751 ? ? 'EXPRESSION TAG' 1510 7 3 4MMY LYS C 95 ? UNP P02751 ? ? 'EXPRESSION TAG' 1511 8 3 4MMY LYS C 96 ? UNP P02751 ? ? 'EXPRESSION TAG' 1512 9 3 4MMY GLY C 97 ? UNP P02751 ? ? 'EXPRESSION TAG' 1513 10 3 4MMY LYS C 98 ? UNP P02751 ? ? 'EXPRESSION TAG' 1514 11 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MN non-polymer . 'MANGANESE (II) ION' ? 'Mn 2' 54.938 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 # _exptl.entry_id 4MMY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.84 _exptl_crystal.density_percent_sol 68.01 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 277.15 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '12% PEG3350, 0.8 M sodium chloride, 0.1 M sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K' # _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 'ADSC QUANTUM 315r' _diffrn_detector.pdbx_collection_date 2013-07-19 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'sagitally focused Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97921 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 19-ID' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 19-ID _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.97921 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MMY _reflns.observed_criterion_sigma_I 14.3 _reflns.observed_criterion_sigma_F 14.3 _reflns.d_resolution_low 50 _reflns.d_resolution_high 3.18 _reflns.number_obs 51260 _reflns.number_all 51260 _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.104 _reflns.pdbx_netI_over_sigmaI 12.6 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.3 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 3.18 _reflns_shell.d_res_low 3.28 _reflns_shell.percent_possible_all 99.7 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.894 _reflns_shell.meanI_over_sigI_obs 2.2 _reflns_shell.pdbx_redundancy 5.1 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MMY _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 51144 _refine.ls_number_reflns_all 49336 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.36 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 41.021 _refine.ls_d_res_high 3.183 _refine.ls_percent_reflns_obs 99.39 _refine.ls_R_factor_obs 0.2130 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2111 _refine.ls_R_factor_R_free 0.2520 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.96 _refine.ls_number_reflns_R_free 2535 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.39 _refine.pdbx_overall_phase_error 25.09 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 12555 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 440 _refine_hist.number_atoms_solvent 5 _refine_hist.number_atoms_total 13000 _refine_hist.d_res_high 3.183 _refine_hist.d_res_low 41.021 # 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 f_bond_d 0.007 ? ? 13359 'X-RAY DIFFRACTION' ? f_angle_d 0.996 ? ? 18031 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.730 ? ? 4942 'X-RAY DIFFRACTION' ? f_chiral_restr 0.039 ? ? 2064 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 2332 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 3.1829 3.2441 2527 0.3069 95.00 0.3341 . . 155 . . . . 'X-RAY DIFFRACTION' . 3.2441 3.3103 2651 0.2819 100.00 0.3479 . . 148 . . . . 'X-RAY DIFFRACTION' . 3.3103 3.3822 2649 0.2703 100.00 0.2941 . . 133 . . . . 'X-RAY DIFFRACTION' . 3.3822 3.4609 2678 0.2614 100.00 0.3027 . . 123 . . . . 'X-RAY DIFFRACTION' . 3.4609 3.5474 2696 0.2460 100.00 0.3198 . . 154 . . . . 'X-RAY DIFFRACTION' . 3.5474 3.6432 2660 0.2346 100.00 0.2928 . . 133 . . . . 'X-RAY DIFFRACTION' . 3.6432 3.7504 2684 0.2199 100.00 0.2581 . . 133 . . . . 'X-RAY DIFFRACTION' . 3.7504 3.8713 2695 0.2241 100.00 0.2529 . . 115 . . . . 'X-RAY DIFFRACTION' . 3.8713 4.0096 2682 0.2160 100.00 0.2802 . . 141 . . . . 'X-RAY DIFFRACTION' . 4.0096 4.1700 2707 0.2021 100.00 0.2270 . . 137 . . . . 'X-RAY DIFFRACTION' . 4.1700 4.3596 2711 0.1927 100.00 0.2236 . . 130 . . . . 'X-RAY DIFFRACTION' . 4.3596 4.5891 2701 0.1799 100.00 0.2033 . . 149 . . . . 'X-RAY DIFFRACTION' . 4.5891 4.8762 2704 0.1713 100.00 0.2200 . . 149 . . . . 'X-RAY DIFFRACTION' . 4.8762 5.2520 2700 0.1808 100.00 0.2326 . . 165 . . . . 'X-RAY DIFFRACTION' . 5.2520 5.7792 2742 0.2084 100.00 0.2319 . . 148 . . . . 'X-RAY DIFFRACTION' . 5.7792 6.6125 2753 0.2282 100.00 0.2903 . . 147 . . . . 'X-RAY DIFFRACTION' . 6.6125 8.3196 2774 0.2242 100.00 0.2601 . . 155 . . . . 'X-RAY DIFFRACTION' . 8.3196 41.0246 2895 0.1984 97.00 0.2336 . . 120 . . . . # _struct.entry_id 4MMY _struct.title 'Integrin AlphaVBeta3 ectodomain bound to the tenth domain of Fibronectin with the IAKGDWND motif' _struct.pdbx_descriptor 'Integrin alpha-V, Integrin beta-3, Fibronectin' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MMY _struct_keywords.pdbx_keywords 'CELL ADHESION' _struct_keywords.text ;integrin, A domain, hybrid domain, PSI, EGF repeats, beta TA thigh, beta propeller, RGD motif, fibronectin, vitronectin, CELL ADHESION ; # 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 4 ? F N N 5 ? G N N 6 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 5 ? M N N 6 ? N N N 5 ? O N N 6 ? P N N 4 ? Q N N 4 ? R N N 5 ? S N N 6 ? T N N 4 ? U N N 4 ? V N N 4 ? W N N 4 ? X N N 4 ? Y N N 4 ? Z N N 4 ? AA N N 4 ? BA N N 4 ? CA N N 5 ? DA N N 7 ? EA N N 7 ? FA N N 7 ? GA N N 7 ? HA N N 7 ? IA N N 4 ? JA N N 4 ? KA N N 4 ? LA N N 4 ? MA N N 4 ? NA N N 4 ? OA N N 5 ? PA N N 7 ? QA N N 7 ? RA N N 7 ? SA N N 8 ? TA N N 8 ? # _struct_biol.id 1 _struct_biol.details ? # 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 GLY A 175 ? GLN A 180 ? GLY A 175 GLN A 180 1 ? 6 HELX_P HELX_P2 2 VAL A 188 ? LYS A 194 ? VAL A 188 LYS A 194 1 ? 7 HELX_P HELX_P3 3 GLN A 214 ? ASP A 218 ? GLN A 214 ASP A 218 5 ? 5 HELX_P HELX_P4 4 GLY A 366 ? LYS A 370 ? GLY A 366 LYS A 370 5 ? 5 HELX_P HELX_P5 5 THR A 768 ? VAL A 772 ? THR A 768 VAL A 772 5 ? 5 HELX_P HELX_P6 6 ASN B 3 ? GLY B 9 ? ASN B 3 GLY B 9 1 ? 7 HELX_P HELX_P7 7 SER B 12 ? ALA B 18 ? SER B 12 ALA B 18 1 ? 7 HELX_P HELX_P8 8 LEU B 40 ? LYS B 46 ? LEU B 40 LYS B 46 5 ? 7 HELX_P HELX_P9 9 SER B 121 ? LYS B 125 ? SER B 121 LYS B 125 5 ? 5 HELX_P HELX_P10 10 ASP B 127 ? GLN B 132 ? ASP B 127 GLN B 132 5 ? 6 HELX_P HELX_P11 11 LEU B 134 ? ARG B 143 ? LEU B 134 ARG B 143 1 ? 10 HELX_P HELX_P12 12 PRO B 169 ? LEU B 173 ? PRO B 169 LEU B 173 5 ? 5 HELX_P HELX_P13 13 GLN B 199 ? LYS B 208 ? GLN B 199 LYS B 208 1 ? 10 HELX_P HELX_P14 14 GLY B 222 ? CYS B 232 ? GLY B 222 CYS B 232 1 ? 11 HELX_P HELX_P15 15 CYS B 232 ? GLY B 237 ? CYS B 232 GLY B 237 1 ? 6 HELX_P HELX_P16 16 LEU B 258 ? GLY B 264 ? LEU B 258 GLY B 264 5 ? 7 HELX_P HELX_P17 17 SER B 291 ? LYS B 302 ? SER B 291 LYS B 302 1 ? 12 HELX_P HELX_P18 18 VAL B 314 ? GLU B 323 ? VAL B 314 GLU B 323 1 ? 10 HELX_P HELX_P19 19 SER B 338 ? ARG B 352 ? SER B 338 ARG B 352 1 ? 15 HELX_P HELX_P20 20 GLU B 534 ? GLY B 538 ? GLU B 534 GLY B 538 5 ? 5 HELX_P HELX_P21 21 THR B 564 ? MET B 568 ? THR B 564 MET B 568 5 ? 5 HELX_P HELX_P22 22 LEU B 573 ? GLY B 577 ? LEU B 573 GLY B 577 5 ? 5 HELX_P HELX_P23 23 ALA B 607 ? LYS B 619 ? ALA B 607 LYS B 619 1 ? 13 HELX_P HELX_P24 24 THR B 630 ? CYS B 635 ? THR B 630 CYS B 635 1 ? 6 # _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 59 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 59 A CYS 67 1_555 ? ? ? ? ? ? ? 2.032 ? disulf2 disulf ? ? A CYS 108 SG ? ? ? 1_555 A CYS 128 SG ? ? A CYS 108 A CYS 128 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? A CYS 142 SG ? ? ? 1_555 A CYS 155 SG ? ? A CYS 142 A CYS 155 1_555 ? ? ? ? ? ? ? 2.033 ? disulf4 disulf ? ? A CYS 461 SG ? ? ? 1_555 A CYS 472 SG ? ? A CYS 461 A CYS 472 1_555 ? ? ? ? ? ? ? 2.033 ? disulf5 disulf ? ? A CYS 478 SG ? ? ? 1_555 A CYS 535 SG ? ? A CYS 478 A CYS 535 1_555 ? ? ? ? ? ? ? 2.031 ? disulf6 disulf ? ? A CYS 596 SG ? ? ? 1_555 A CYS 602 SG ? ? A CYS 596 A CYS 602 1_555 ? ? ? ? ? ? ? 2.032 ? disulf7 disulf ? ? A CYS 668 SG ? ? ? 1_555 A CYS 681 SG ? ? A CYS 668 A CYS 681 1_555 ? ? ? ? ? ? ? 2.031 ? disulf8 disulf ? ? A CYS 822 SG ? ? ? 1_555 A CYS 884 SG ? ? A CYS 822 A CYS 884 1_555 ? ? ? ? ? ? ? 2.030 ? disulf9 disulf ? ? A CYS 874 SG ? ? ? 1_555 A CYS 879 SG ? ? A CYS 874 A CYS 879 1_555 ? ? ? ? ? ? ? 2.031 ? disulf10 disulf ? ? B CYS 5 SG ? ? ? 1_555 B CYS 23 SG ? ? B CYS 5 B CYS 23 1_555 ? ? ? ? ? ? ? 2.031 ? disulf11 disulf ? ? B CYS 13 SG ? ? ? 1_555 B CYS 435 SG ? ? B CYS 13 B CYS 435 1_555 ? ? ? ? ? ? ? 2.028 ? disulf12 disulf ? ? B CYS 16 SG ? ? ? 1_555 B CYS 38 SG ? ? B CYS 16 B CYS 38 1_555 ? ? ? ? ? ? ? 2.032 ? disulf13 disulf ? ? B CYS 26 SG ? ? ? 1_555 B CYS 49 SG ? ? B CYS 26 B CYS 49 1_555 ? ? ? ? ? ? ? 2.035 ? disulf14 disulf ? ? B CYS 177 SG ? ? ? 1_555 B CYS 184 SG ? ? B CYS 177 B CYS 184 1_555 ? ? ? ? ? ? ? 2.030 ? disulf15 disulf ? ? B CYS 232 SG ? ? ? 1_555 B CYS 273 SG ? ? B CYS 232 B CYS 273 1_555 ? ? ? ? ? ? ? 2.031 ? disulf16 disulf ? ? B CYS 374 SG ? ? ? 1_555 B CYS 386 SG ? ? B CYS 374 B CYS 386 1_555 ? ? ? ? ? ? ? 2.033 ? disulf17 disulf ? ? B CYS 406 SG ? ? ? 1_555 B CYS 433 SG ? ? B CYS 406 B CYS 433 1_555 ? ? ? ? ? ? ? 2.031 ? disulf18 disulf ? ? B CYS 437 SG ? ? ? 1_555 B CYS 457 SG ? ? B CYS 437 B CYS 457 1_555 ? ? ? ? ? ? ? 2.033 ? disulf19 disulf ? ? B CYS 448 SG ? ? ? 1_555 B CYS 460 SG ? ? B CYS 448 B CYS 460 1_555 ? ? ? ? ? ? ? 2.028 ? disulf20 disulf ? ? B CYS 462 SG ? ? ? 1_555 B CYS 471 SG ? ? B CYS 462 B CYS 471 1_555 ? ? ? ? ? ? ? 2.033 ? disulf21 disulf ? ? B CYS 473 SG ? ? ? 1_555 B CYS 503 SG ? ? B CYS 473 B CYS 503 1_555 ? ? ? ? ? ? ? 2.032 ? disulf22 disulf ? ? B CYS 486 SG ? ? ? 1_555 B CYS 501 SG ? ? B CYS 486 B CYS 501 1_555 ? ? ? ? ? ? ? 2.036 ? disulf23 disulf ? ? B CYS 495 SG ? ? ? 1_555 B CYS 506 SG ? ? B CYS 495 B CYS 506 1_555 ? ? ? ? ? ? ? 2.036 ? disulf24 disulf ? ? B CYS 508 SG ? ? ? 1_555 B CYS 521 SG ? ? B CYS 508 B CYS 521 1_555 ? ? ? ? ? ? ? 2.031 ? disulf25 disulf ? ? B CYS 523 SG ? ? ? 1_555 B CYS 544 SG ? ? B CYS 523 B CYS 544 1_555 ? ? ? ? ? ? ? 2.031 ? disulf26 disulf ? ? B CYS 528 SG ? ? ? 1_555 B CYS 542 SG ? ? B CYS 528 B CYS 542 1_555 ? ? ? ? ? ? ? 2.030 ? disulf27 disulf ? ? B CYS 536 SG ? ? ? 1_555 B CYS 547 SG ? ? B CYS 536 B CYS 547 1_555 ? ? ? ? ? ? ? 2.032 ? disulf28 disulf ? ? B CYS 549 SG ? ? ? 1_555 B CYS 558 SG ? ? B CYS 549 B CYS 558 1_555 ? ? ? ? ? ? ? 2.032 ? disulf29 disulf ? ? B CYS 560 SG ? ? ? 1_555 B CYS 583 SG ? ? B CYS 560 B CYS 583 1_555 ? ? ? ? ? ? ? 2.031 ? disulf30 disulf ? ? B CYS 567 SG ? ? ? 1_555 B CYS 581 SG ? ? B CYS 567 B CYS 581 1_555 ? ? ? ? ? ? ? 2.032 ? disulf31 disulf ? ? B CYS 575 SG ? ? ? 1_555 B CYS 586 SG ? ? B CYS 575 B CYS 586 1_555 ? ? ? ? ? ? ? 2.032 ? disulf32 disulf ? ? B CYS 588 SG ? ? ? 1_555 B CYS 598 SG ? ? B CYS 588 B CYS 598 1_555 ? ? ? ? ? ? ? 2.031 ? disulf33 disulf ? ? B CYS 601 SG ? ? ? 1_555 B CYS 604 SG ? ? B CYS 601 B CYS 604 1_555 ? ? ? ? ? ? ? 2.031 ? disulf34 disulf ? ? B CYS 608 SG ? ? ? 1_555 B CYS 655 SG ? ? B CYS 608 B CYS 655 1_555 ? ? ? ? ? ? ? 2.031 ? disulf35 disulf ? ? B CYS 614 SG ? ? ? 1_555 B CYS 635 SG ? ? B CYS 614 B CYS 635 1_555 ? ? ? ? ? ? ? 2.032 ? disulf36 disulf ? ? B CYS 617 SG ? ? ? 1_555 B CYS 631 SG ? ? B CYS 617 B CYS 631 1_555 ? ? ? ? ? ? ? 2.031 ? disulf37 disulf ? ? B CYS 663 SG ? ? ? 1_555 B CYS 687 SG ? ? B CYS 663 B CYS 687 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? A ASN 821 ND2 ? ? ? 1_555 X NAG . C1 ? ? A ASN 821 A NAG 1021 1_555 ? ? ? ? ? ? ? 1.436 ? covale2 covale ? ? A ASN 524 ND2 ? ? ? 1_555 T NAG . C1 ? ? A ASN 524 A NAG 1017 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? A ASN 458 ND2 ? ? ? 1_555 P NAG . C1 ? ? A ASN 458 A NAG 1013 1_555 ? ? ? ? ? ? ? 1.436 ? covale4 covale ? ? B ASN 559 ND2 ? ? ? 1_555 MA NAG . C1 ? ? B ASN 559 B NAG 705 1_555 ? ? ? ? ? ? ? 1.436 ? covale5 covale ? ? A ASN 44 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 44 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.436 ? covale6 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 1007 A NAG 1008 1_555 ? ? ? ? ? ? ? 1.437 ? covale7 covale ? ? P NAG . O4 ? ? ? 1_555 Q NAG . C1 ? ? A NAG 1013 A NAG 1014 1_555 ? ? ? ? ? ? ? 1.437 ? covale8 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 1005 A NAG 1006 1_555 ? ? ? ? ? ? ? 1.438 ? covale9 covale ? ? B ASN 99 ND2 ? ? ? 1_555 IA NAG . C1 ? ? B ASN 99 B NAG 701 1_555 ? ? ? ? ? ? ? 1.438 ? covale10 covale ? ? A ASN 585 ND2 ? ? ? 1_555 U NAG . C1 ? ? A ASN 585 A NAG 1018 1_555 ? ? ? ? ? ? ? 1.438 ? covale11 covale ? ? B ASN 320 ND2 ? ? ? 1_555 JA NAG . C1 ? ? B ASN 320 B NAG 702 1_555 ? ? ? ? ? ? ? 1.439 ? covale12 covale ? ? A ASN 266 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 266 A NAG 1007 1_555 ? ? ? ? ? ? ? 1.439 ? covale13 covale ? ? A ASN 950 ND2 ? ? ? 1_555 AA NAG . C1 ? ? A ASN 950 A NAG 1024 1_555 ? ? ? ? ? ? ? 1.439 ? covale14 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1001 A NAG 1002 1_555 ? ? ? ? ? ? ? 1.439 ? covale15 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 1002 A BMA 1003 1_555 ? ? ? ? ? ? ? 1.440 ? covale16 covale ? ? A ASN 943 ND2 ? ? ? 1_555 Y NAG . C1 ? ? A ASN 943 A NAG 1022 1_555 ? ? ? ? ? ? ? 1.440 ? covale17 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 1003 A MAN 1004 1_555 ? ? ? ? ? ? ? 1.440 ? covale18 covale ? ? N BMA . O4 ? ? ? 1_555 O MAN . C1 ? ? A BMA 1011 A MAN 1012 1_555 ? ? ? ? ? ? ? 1.441 ? covale19 covale ? ? L BMA . O6 ? ? ? 1_555 N BMA . C1 ? ? A BMA 1009 A BMA 1011 1_555 ? ? ? ? ? ? ? 1.441 ? covale20 covale ? ? L BMA . O3 ? ? ? 1_555 M MAN . C1 ? ? A BMA 1009 A MAN 1010 1_555 ? ? ? ? ? ? ? 1.442 ? covale21 covale ? ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? A NAG 1008 A BMA 1009 1_555 ? ? ? ? ? ? ? 1.442 ? covale22 covale ? ? BA NAG . O4 ? ? ? 1_555 CA BMA . C1 ? ? A NAG 1025 A BMA 1026 1_555 ? ? ? ? ? ? ? 1.442 ? covale23 covale ? ? B ASN 371 ND2 ? ? ? 1_555 KA NAG . C1 ? ? B ASN 371 B NAG 703 1_555 ? ? ? ? ? ? ? 1.442 ? covale24 covale ? ? A ASN 674 ND2 ? ? ? 1_555 W NAG . C1 ? ? A ASN 674 A NAG 1020 1_555 ? ? ? ? ? ? ? 1.442 ? covale25 covale ? ? A ASN 260 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 260 A NAG 1005 1_555 ? ? ? ? ? ? ? 1.443 ? covale26 covale ? ? U NAG . O4 ? ? ? 1_555 V NAG . C1 ? ? A NAG 1018 A NAG 1019 1_555 ? ? ? ? ? ? ? 1.443 ? covale27 covale ? ? R BMA . O3 ? ? ? 1_555 S MAN . C1 ? ? A BMA 1015 A MAN 1016 1_555 ? ? ? ? ? ? ? 1.443 ? covale28 covale ? ? NA NAG . O4 ? ? ? 1_555 OA BMA . C1 ? ? B NAG 706 B BMA 707 1_555 ? ? ? ? ? ? ? 1.443 ? covale29 covale ? ? Q NAG . O4 ? ? ? 1_555 R BMA . C1 ? ? A NAG 1014 A BMA 1015 1_555 ? ? ? ? ? ? ? 1.443 ? covale30 covale ? ? Y NAG . O4 ? ? ? 1_555 Z NAG . C1 ? ? A NAG 1022 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.444 ? covale31 covale ? ? AA NAG . O4 ? ? ? 1_555 BA NAG . C1 ? ? A NAG 1024 A NAG 1025 1_555 ? ? ? ? ? ? ? 1.446 ? covale32 covale ? ? KA NAG . O4 ? ? ? 1_555 LA NAG . C1 ? ? B NAG 703 B NAG 704 1_555 ? ? ? ? ? ? ? 1.447 ? covale33 covale ? ? MA NAG . O4 ? ? ? 1_555 NA NAG . C1 ? ? B NAG 705 B NAG 706 1_555 ? ? ? ? ? ? ? 1.449 ? metalc1 metalc ? ? B ASP 251 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 251 B MN 709 1_555 ? ? ? ? ? ? ? 2.050 ? metalc2 metalc ? ? A TYR 290 O ? ? ? 1_555 EA MN . MN ? ? A TYR 290 A MN 1028 1_555 ? ? ? ? ? ? ? 2.065 ? metalc3 metalc ? ? A TYR 419 O ? ? ? 1_555 GA MN . MN ? ? A TYR 419 A MN 1030 1_555 ? ? ? ? ? ? ? 2.068 ? metalc4 metalc ? ? A ASP 230 OD2 ? ? ? 1_555 DA MN . MN ? ? A ASP 230 A MN 1027 1_555 ? ? ? ? ? ? ? 2.136 ? metalc5 metalc ? ? A ASP 413 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASP 413 A MN 1030 1_555 ? ? ? ? ? ? ? 2.146 ? metalc6 metalc ? ? B ASP 217 OD1 ? ? ? 1_555 RA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.148 ? metalc7 metalc ? ? B GLU 220 OE1 ? ? ? 1_555 PA MN . MN ? ? B GLU 220 B MN 708 1_555 ? ? ? ? ? ? ? 2.148 ? metalc8 metalc ? ? A GLU 636 OE2 ? ? ? 1_555 HA MN . MN ? ? A GLU 636 A MN 1031 1_555 ? ? ? ? ? ? ? 2.150 ? metalc9 metalc ? ? A ASP 238 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASP 238 A MN 1027 1_555 ? ? ? ? ? ? ? 2.151 ? metalc10 metalc ? ? A ASP 284 OD2 ? ? ? 1_555 EA MN . MN ? ? A ASP 284 A MN 1028 1_555 ? ? ? ? ? ? ? 2.152 ? metalc11 metalc ? ? A ASP 599 OD1 ? ? ? 1_555 HA MN . MN ? ? A ASP 599 A MN 1031 1_555 ? ? ? ? ? ? ? 2.152 ? metalc12 metalc ? ? B ASP 127 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 127 B MN 709 1_555 ? ? ? ? ? ? ? 2.154 ? metalc13 metalc ? ? A ASP 599 OD2 ? ? ? 1_555 HA MN . MN ? ? A ASP 599 A MN 1031 1_555 ? ? ? ? ? ? ? 2.156 ? metalc14 metalc ? ? A ASP 353 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 353 A MN 1029 1_555 ? ? ? ? ? ? ? 2.156 ? metalc15 metalc ? ? B ASP 126 OD2 ? ? ? 1_555 QA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.157 ? metalc16 metalc ? ? A ASP 353 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 353 A MN 1029 1_555 ? ? ? ? ? ? ? 2.160 ? metalc17 metalc ? ? A GLU 636 OE1 ? ? ? 1_555 HA MN . MN ? ? A GLU 636 A MN 1031 1_555 ? ? ? ? ? ? ? 2.160 ? metalc18 metalc ? ? B ASP 126 OD1 ? ? ? 1_555 QA MN . MN ? ? B ASP 126 B MN 709 1_555 ? ? ? ? ? ? ? 2.160 ? metalc19 metalc ? ? B GLU 220 OE2 ? ? ? 1_555 RA MN . MN ? ? B GLU 220 B MN 710 1_555 ? ? ? ? ? ? ? 2.161 ? metalc20 metalc ? ? A ASP 357 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 357 A MN 1029 1_555 ? ? ? ? ? ? ? 2.161 ? metalc21 metalc ? ? B ASP 217 O ? ? ? 1_555 RA MN . MN ? ? B ASP 217 B MN 710 1_555 ? ? ? ? ? ? ? 2.163 ? metalc22 metalc ? ? B ASP 158 OD2 ? ? ? 1_555 RA MN . MN ? ? B ASP 158 B MN 710 1_555 ? ? ? ? ? ? ? 2.163 ? metalc23 metalc ? ? A ASP 292 OD2 ? ? ? 1_555 EA MN . MN ? ? A ASP 292 A MN 1028 1_555 ? ? ? ? ? ? ? 2.166 ? metalc24 metalc ? ? B SER 123 OG ? ? ? 1_555 PA MN . MN ? ? B SER 123 B MN 708 1_555 ? ? ? ? ? ? ? 2.166 ? metalc25 metalc ? ? A ASP 351 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 351 A MN 1029 1_555 ? ? ? ? ? ? ? 2.169 ? metalc26 metalc ? ? A ASP 288 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASP 288 A MN 1028 1_555 ? ? ? ? ? ? ? 2.169 ? metalc27 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 FA MN . MN ? ? A ASP 357 A MN 1029 1_555 ? ? ? ? ? ? ? 2.170 ? metalc28 metalc ? ? B SER 123 O ? ? ? 1_555 QA MN . MN ? ? B SER 123 B MN 709 1_555 ? ? ? ? ? ? ? 2.170 ? metalc29 metalc ? ? A ASP 292 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASP 292 A MN 1028 1_555 ? ? ? ? ? ? ? 2.171 ? metalc30 metalc ? ? B SER 121 OG ? ? ? 1_555 PA MN . MN ? ? B SER 121 B MN 708 1_555 ? ? ? ? ? ? ? 2.171 ? metalc31 metalc ? ? A ASP 421 OD2 ? ? ? 1_555 GA MN . MN ? ? A ASP 421 A MN 1030 1_555 ? ? ? ? ? ? ? 2.173 ? metalc32 metalc ? ? A ASP 234 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASP 234 A MN 1027 1_555 ? ? ? ? ? ? ? 2.176 ? metalc33 metalc ? ? A ASP 421 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASP 421 A MN 1030 1_555 ? ? ? ? ? ? ? 2.176 ? metalc34 metalc ? ? B ASN 215 OD1 ? ? ? 1_555 RA MN . MN ? ? B ASN 215 B MN 710 1_555 ? ? ? ? ? ? ? 2.178 ? metalc35 metalc ? ? A ASN 286 OD1 ? ? ? 1_555 EA MN . MN ? ? A ASN 286 A MN 1028 1_555 ? ? ? ? ? ? ? 2.184 ? metalc36 metalc ? ? A ASP 238 OD2 ? ? ? 1_555 DA MN . MN ? ? A ASP 238 A MN 1027 1_555 ? ? ? ? ? ? ? 2.186 ? metalc37 metalc ? ? A ASN 417 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASN 417 A MN 1030 1_555 ? ? ? ? ? ? ? 2.188 ? metalc38 metalc ? ? A CYS 596 O ? ? ? 1_555 HA MN . MN ? ? A CYS 596 A MN 1031 1_555 ? ? ? ? ? ? ? 2.191 ? metalc39 metalc ? ? B ASP 251 OD2 ? ? ? 1_555 QA MN . MN ? ? B ASP 251 B MN 709 1_555 ? ? ? ? ? ? ? 2.199 ? metalc40 metalc ? ? B PRO 219 O ? ? ? 1_555 RA MN . MN ? ? B PRO 219 B MN 710 1_555 ? ? ? ? ? ? ? 2.219 ? metalc41 metalc ? ? A ASP 415 OD1 ? ? ? 1_555 GA MN . MN ? ? A ASP 415 A MN 1030 1_555 ? ? ? ? ? ? ? 2.240 ? metalc42 metalc ? ? A ASN 232 OD1 ? ? ? 1_555 DA MN . MN ? ? A ASN 232 A MN 1027 1_555 ? ? ? ? ? ? ? 2.270 ? metalc43 metalc ? ? A VAL 601 O ? ? ? 1_555 HA MN . MN ? ? A VAL 601 A MN 1031 1_555 ? ? ? ? ? ? ? 2.292 ? metalc44 metalc ? ? A ILE 236 O ? ? ? 1_555 DA MN . MN ? ? A ILE 236 A MN 1027 1_555 ? ? ? ? ? ? ? 2.365 ? metalc45 metalc ? ? A ASP 349 OD1 ? ? ? 1_555 FA MN . MN ? ? A ASP 349 A MN 1029 1_555 ? ? ? ? ? ? ? 2.371 ? metalc46 metalc ? ? A PHE 355 O ? ? ? 1_555 FA MN . MN ? ? A PHE 355 A MN 1029 1_555 ? ? ? ? ? ? ? 2.420 ? metalc47 metalc ? ? A ASP 415 OD2 ? ? ? 1_555 GA MN . MN ? ? A ASP 415 A MN 1030 1_555 ? ? ? ? ? ? ? 2.427 ? metalc48 metalc ? ? PA MN . MN ? ? ? 1_555 TA HOH . O ? ? B MN 708 B HOH 802 1_555 ? ? ? ? ? ? ? 2.187 ? metalc49 metalc ? ? PA MN . MN ? ? ? 1_555 TA HOH . O ? ? B MN 708 B HOH 801 1_555 ? ? ? ? ? ? ? 2.195 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 TYR 450 A . ? TYR 450 A PRO 451 A ? PRO 451 A 1 -16.75 2 ASN 685 A . ? ASN 685 A PRO 686 A ? PRO 686 A 1 1.50 3 SER 749 A . ? SER 749 A PRO 750 A ? PRO 750 A 1 -5.52 4 LEU 755 A . ? LEU 755 A PRO 756 A ? PRO 756 A 1 -2.24 5 SER 84 B . ? SER 84 B PRO 85 B ? PRO 85 B 1 -4.33 6 SER 162 B . ? SER 162 B PRO 163 B ? PRO 163 B 1 -11.22 7 SER 510 B . ? SER 510 B SER 511 B ? SER 511 B 1 -9.56 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 4 ? C ? 2 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? H ? 2 ? I ? 4 ? J ? 2 ? K ? 5 ? L ? 5 ? M ? 4 ? N ? 6 ? O ? 4 ? P ? 6 ? Q ? 4 ? R ? 2 ? S ? 6 ? T ? 4 ? U ? 6 ? V ? 2 ? W ? 2 ? X ? 2 ? Y ? 4 ? # 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 A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel H 1 2 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel J 1 2 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel K 4 5 ? parallel L 1 2 ? parallel L 2 3 ? anti-parallel L 3 4 ? anti-parallel L 4 5 ? anti-parallel M 1 2 ? anti-parallel M 2 3 ? anti-parallel M 3 4 ? anti-parallel N 1 2 ? parallel N 2 3 ? anti-parallel N 3 4 ? anti-parallel N 4 5 ? anti-parallel N 5 6 ? anti-parallel O 1 2 ? anti-parallel O 2 3 ? anti-parallel O 3 4 ? anti-parallel P 1 2 ? parallel P 2 3 ? anti-parallel P 3 4 ? anti-parallel P 4 5 ? anti-parallel P 5 6 ? anti-parallel Q 1 2 ? anti-parallel Q 2 3 ? anti-parallel Q 3 4 ? parallel R 1 2 ? anti-parallel S 1 2 ? anti-parallel S 2 3 ? parallel S 3 4 ? anti-parallel S 4 5 ? anti-parallel S 5 6 ? anti-parallel T 1 2 ? anti-parallel T 2 3 ? anti-parallel T 3 4 ? anti-parallel U 1 2 ? anti-parallel U 2 3 ? parallel U 3 4 ? parallel U 4 5 ? parallel U 5 6 ? parallel V 1 2 ? anti-parallel W 1 2 ? anti-parallel X 1 2 ? anti-parallel Y 1 2 ? parallel Y 2 3 ? anti-parallel Y 3 4 ? 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 A 1 LEU A 3 ? SER A 12 ? LEU A 3 SER A 12 A 2 ARG A 431 ? ALA A 437 ? ARG A 431 ALA A 437 A 3 ASP A 421 ? ALA A 426 ? ASP A 421 ALA A 426 A 4 PHE A 404 ? THR A 412 ? PHE A 404 THR A 412 B 1 VAL A 23 ? PHE A 26 ? VAL A 23 PHE A 26 B 2 PHE A 35 ? ALA A 40 ? PHE A 35 ALA A 40 B 3 GLN A 55 ? ASP A 60 ? GLN A 55 ASP A 60 B 4 CYS A 67 ? PRO A 69 ? CYS A 67 PRO A 69 C 1 ASP A 79 ? ALA A 81 ? ASP A 79 ALA A 81 C 2 ASP A 84 ? PRO A 85 ? ASP A 84 PRO A 85 D 1 VAL A 98 ? LYS A 101 ? VAL A 98 LYS A 101 D 2 LYS A 104 ? ALA A 109 ? LYS A 104 ALA A 109 D 3 THR A 127 ? ASP A 132 ? THR A 127 ASP A 132 D 4 LYS A 135 ? TYR A 139 ? LYS A 135 TYR A 139 E 1 SER A 160 ? PHE A 163 ? SER A 160 PHE A 163 E 2 ARG A 168 ? GLY A 173 ? ARG A 168 GLY A 173 E 3 GLN A 182 ? GLN A 187 ? GLN A 182 GLN A 187 E 4 LEU A 208 ? ALA A 209 ? LEU A 208 ALA A 209 F 1 VAL A 226 ? GLY A 229 ? VAL A 226 GLY A 229 F 2 ASP A 238 ? VAL A 243 ? ASP A 238 VAL A 243 F 3 MET A 252 ? TYR A 256 ? MET A 252 TYR A 256 F 4 SER A 263 ? THR A 268 ? SER A 263 THR A 268 G 1 VAL A 280 ? THR A 283 ? VAL A 280 THR A 283 G 2 ASP A 292 ? ALA A 297 ? ASP A 292 ALA A 297 G 3 GLN A 314 ? GLN A 320 ? GLN A 314 GLN A 320 G 4 PHE A 326 ? ASN A 332 ? PHE A 326 ASN A 332 H 1 MET A 301 ? ARG A 303 ? MET A 301 ARG A 303 H 2 LEU A 309 ? GLU A 311 ? LEU A 309 GLU A 311 I 1 ALA A 343 ? GLY A 348 ? ALA A 343 GLY A 348 I 2 ASP A 357 ? ALA A 362 ? ASP A 357 ALA A 362 I 3 ILE A 372 ? PHE A 376 ? ILE A 372 PHE A 376 I 4 GLN A 389 ? LEU A 391 ? GLN A 389 LEU A 391 J 1 GLY A 378 ? ARG A 379 ? GLY A 378 ARG A 379 J 2 GLY A 382 ? LEU A 383 ? GLY A 382 LEU A 383 K 1 ALA A 511 ? PHE A 513 ? ALA A 511 PHE A 513 K 2 GLN A 534 ? LEU A 542 ? GLN A 534 LEU A 542 K 3 SER A 471 ? GLY A 483 ? SER A 471 GLY A 483 K 4 VAL A 440 ? TYR A 450 ? VAL A 440 TYR A 450 K 5 ILE A 577 ? LEU A 578 ? ILE A 577 LEU A 578 L 1 ILE A 453 ? LEU A 454 ? ILE A 453 LEU A 454 L 2 ASN A 585 ? ILE A 592 ? ASN A 585 ILE A 592 L 3 ILE A 555 ? TYR A 561 ? ILE A 555 TYR A 561 L 4 GLN A 494 ? LEU A 498 ? GLN A 494 LEU A 498 L 5 SER A 520 ? ASN A 524 ? SER A 520 ASN A 524 M 1 LEU A 606 ? VAL A 610 ? LEU A 606 VAL A 610 M 2 ASN A 623 ? ASN A 633 ? ASN A 623 ASN A 633 M 3 GLN A 692 ? VAL A 701 ? GLN A 692 VAL A 701 M 4 ASP A 652 ? VAL A 656 ? ASP A 652 VAL A 656 N 1 LYS A 616 ? TYR A 618 ? LYS A 616 TYR A 618 N 2 VAL A 730 ? ALA A 737 ? VAL A 730 ALA A 737 N 3 SER A 710 ? GLN A 718 ? SER A 710 GLN A 718 N 4 ALA A 641 ? SER A 646 ? ALA A 641 SER A 646 N 5 THR A 676 ? GLY A 684 ? THR A 676 GLY A 684 N 6 CYS A 668 ? GLU A 673 ? CYS A 668 GLU A 673 O 1 VAL A 742 ? SER A 749 ? VAL A 742 SER A 749 O 2 VAL A 775 ? ASN A 784 ? VAL A 775 ASN A 784 O 3 SER A 894 ? LEU A 903 ? SER A 894 LEU A 903 O 4 LEU A 809 ? ASP A 817 ? LEU A 809 ASP A 817 P 1 HIS A 752 ? LEU A 755 ? HIS A 752 LEU A 755 P 2 ILE A 941 ? TRP A 953 ? ILE A 941 TRP A 953 P 3 SER A 917 ? GLU A 930 ? SER A 917 GLU A 930 P 4 PHE A 790 ? TYR A 803 ? PHE A 790 TYR A 803 P 5 GLN A 878 ? LEU A 889 ? GLN A 878 LEU A 889 P 6 MET A 820 ? SER A 824 ? MET A 820 SER A 824 Q 1 ASN A 806 ? THR A 807 ? ASN A 806 THR A 807 Q 2 PHE A 790 ? TYR A 803 ? PHE A 790 TYR A 803 Q 3 SER A 917 ? GLU A 930 ? SER A 917 GLU A 930 Q 4 ILE A 869 ? LEU A 872 ? ILE A 869 LEU A 872 R 1 TRP B 25 ? CYS B 26 ? TRP B 25 CYS B 26 R 2 ILE B 54 ? GLU B 55 ? ILE B 54 GLU B 55 S 1 GLU B 60 ? GLU B 65 ? GLU B 60 GLU B 65 S 2 ARG B 87 ? LEU B 92 ? ARG B 87 LEU B 92 S 3 LEU B 425 ? PHE B 431 ? LEU B 425 PHE B 431 S 4 GLU B 411 ? PRO B 418 ? GLU B 411 PRO B 418 S 5 VAL B 355 ? ARG B 360 ? VAL B 355 ARG B 360 S 6 SER B 385 ? CYS B 386 ? SER B 385 CYS B 386 T 1 VAL B 83 ? SER B 84 ? VAL B 83 SER B 84 T 2 SER B 97 ? ARG B 105 ? SER B 97 ARG B 105 T 3 THR B 394 ? VAL B 403 ? THR B 394 VAL B 403 T 4 LEU B 366 ? THR B 373 ? LEU B 366 THR B 373 U 1 TYR B 190 ? THR B 197 ? TYR B 190 THR B 197 U 2 ARG B 150 ? PHE B 156 ? ARG B 150 PHE B 156 U 3 VAL B 112 ? ASP B 119 ? VAL B 112 ASP B 119 U 4 SER B 243 ? THR B 250 ? SER B 243 THR B 250 U 5 ILE B 304 ? THR B 311 ? ILE B 304 THR B 311 U 6 THR B 329 ? LEU B 333 ? THR B 329 LEU B 333 V 1 GLY B 540 ? SER B 543 ? GLY B 540 SER B 543 V 2 ASP B 546 ? CYS B 549 ? ASP B 546 CYS B 549 W 1 TRP B 553 ? THR B 554 ? TRP B 553 THR B 554 W 2 CYS B 560 ? THR B 561 ? CYS B 560 THR B 561 X 1 GLY B 579 ? GLU B 582 ? GLY B 579 GLU B 582 X 2 SER B 585 ? CYS B 588 ? SER B 585 CYS B 588 Y 1 ILE B 639 ? VAL B 642 ? ILE B 639 VAL B 642 Y 2 LEU B 679 ? VAL B 682 ? LEU B 679 VAL B 682 Y 3 VAL B 664 ? TYR B 670 ? VAL B 664 TYR B 670 Y 4 ALA B 652 ? LYS B 658 ? ALA B 652 LYS B 658 # 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 A 1 2 N TYR A 11 ? N TYR A 11 O ALA A 432 ? O ALA A 432 A 2 3 O ARG A 431 ? O ARG A 431 N ALA A 426 ? N ALA A 426 A 3 4 O ASP A 421 ? O ASP A 421 N THR A 412 ? N THR A 412 B 1 2 N ASP A 24 ? N ASP A 24 O LEU A 37 ? O LEU A 37 B 2 3 N ALA A 40 ? N ALA A 40 O GLN A 55 ? O GLN A 55 B 3 4 N LYS A 58 ? N LYS A 58 O GLN A 68 ? O GLN A 68 C 1 2 N TYR A 80 ? N TYR A 80 O ASP A 84 ? O ASP A 84 D 1 2 N ARG A 99 ? N ARG A 99 O LEU A 106 ? O LEU A 106 D 2 3 N ALA A 109 ? N ALA A 109 O THR A 127 ? O THR A 127 D 3 4 N LEU A 130 ? N LEU A 130 O VAL A 137 ? O VAL A 137 E 1 2 N ASP A 162 ? N ASP A 162 O LEU A 170 ? O LEU A 170 E 2 3 N VAL A 169 ? N VAL A 169 O ASP A 186 ? O ASP A 186 E 3 4 N SER A 185 ? N SER A 185 O LEU A 208 ? O LEU A 208 F 1 2 N ALA A 227 ? N ALA A 227 O VAL A 240 ? O VAL A 240 F 2 3 N PHE A 239 ? N PHE A 239 O TYR A 256 ? O TYR A 256 F 3 4 N ILE A 255 ? N ILE A 255 O LEU A 264 ? O LEU A 264 G 1 2 N THR A 283 ? N THR A 283 O ASP A 292 ? O ASP A 292 G 2 3 N VAL A 293 ? N VAL A 293 O SER A 318 ? O SER A 318 G 3 4 N LEU A 319 ? N LEU A 319 O GLN A 327 ? O GLN A 327 H 1 2 N ASP A 302 ? N ASP A 302 O GLN A 310 ? O GLN A 310 I 1 2 N ALA A 345 ? N ALA A 345 O ALA A 359 ? O ALA A 359 I 2 3 N ILE A 360 ? N ILE A 360 O TYR A 374 ? O TYR A 374 I 3 4 N VAL A 373 ? N VAL A 373 O LEU A 391 ? O LEU A 391 J 1 2 N ARG A 379 ? N ARG A 379 O GLY A 382 ? O GLY A 382 K 1 2 N LEU A 512 ? N LEU A 512 O TYR A 541 ? O TYR A 541 K 2 3 O LEU A 538 ? O LEU A 538 N VAL A 475 ? N VAL A 475 K 3 4 O ASP A 482 ? O ASP A 482 N THR A 442 ? N THR A 442 K 4 5 N ILE A 441 ? N ILE A 441 O ILE A 577 ? O ILE A 577 L 1 2 N LEU A 454 ? N LEU A 454 O HIS A 591 ? O HIS A 591 L 2 3 O ALA A 590 ? O ALA A 590 N ILE A 555 ? N ILE A 555 L 3 4 O GLU A 560 ? O GLU A 560 N GLU A 496 ? N GLU A 496 L 4 5 N LEU A 497 ? N LEU A 497 O HIS A 521 ? O HIS A 521 M 1 2 N SER A 609 ? N SER A 609 O LYS A 630 ? O LYS A 630 M 2 3 N LEU A 625 ? N LEU A 625 O PHE A 699 ? O PHE A 699 M 3 4 O ARG A 698 ? O ARG A 698 N ILE A 654 ? N ILE A 654 N 1 2 N ILE A 617 ? N ILE A 617 O ALA A 737 ? O ALA A 737 N 2 3 O VAL A 730 ? O VAL A 730 N LEU A 715 ? N LEU A 715 N 3 4 O GLN A 716 ? O GLN A 716 N ILE A 644 ? N ILE A 644 N 4 5 N LEU A 643 ? N LEU A 643 O CYS A 681 ? O CYS A 681 N 5 6 O GLN A 678 ? O GLN A 678 N LYS A 671 ? N LYS A 671 O 1 2 N SER A 749 ? N SER A 749 O GLN A 777 ? O GLN A 777 O 2 3 N TYR A 780 ? N TYR A 780 O LEU A 897 ? O LEU A 897 O 3 4 O ILE A 896 ? O ILE A 896 N ASP A 817 ? N ASP A 817 P 1 2 N LEU A 755 ? N LEU A 755 O THR A 952 ? O THR A 952 P 2 3 O VAL A 947 ? O VAL A 947 N SER A 922 ? N SER A 922 P 3 4 O SER A 923 ? O SER A 923 N GLN A 798 ? N GLN A 798 P 4 5 N ALA A 793 ? N ALA A 793 O VAL A 886 ? O VAL A 886 P 5 6 O GLN A 885 ? O GLN A 885 N ASN A 821 ? N ASN A 821 Q 1 2 O ASN A 806 ? O ASN A 806 N TYR A 803 ? N TYR A 803 Q 2 3 N GLN A 798 ? N GLN A 798 O SER A 923 ? O SER A 923 Q 3 4 O SER A 917 ? O SER A 917 N HIS A 870 ? N HIS A 870 R 1 2 N TRP B 25 ? N TRP B 25 O GLU B 55 ? O GLU B 55 S 1 2 N GLU B 60 ? N GLU B 60 O ARG B 91 ? O ARG B 91 S 2 3 N LEU B 90 ? N LEU B 90 O GLN B 428 ? O GLN B 428 S 3 4 O LEU B 425 ? O LEU B 425 N ILE B 416 ? N ILE B 416 S 4 5 O LYS B 417 ? O LYS B 417 N GLU B 358 ? N GLU B 358 S 5 6 N VAL B 355 ? N VAL B 355 O CYS B 386 ? O CYS B 386 T 1 2 N SER B 84 ? N SER B 84 O GLN B 103 ? O GLN B 103 T 2 3 N PHE B 100 ? N PHE B 100 O ILE B 399 ? O ILE B 399 T 3 4 O LYS B 402 ? O LYS B 402 N SER B 367 ? N SER B 367 U 1 2 O LYS B 191 ? O LYS B 191 N ALA B 155 ? N ALA B 155 U 2 3 O ARG B 150 ? O ARG B 150 N ILE B 114 ? N ILE B 114 U 3 4 N ASP B 113 ? N ASP B 113 O SER B 243 ? O SER B 243 U 4 5 N PHE B 248 ? N PHE B 248 O ILE B 307 ? O ILE B 307 U 5 6 N VAL B 310 ? N VAL B 310 O LEU B 333 ? O LEU B 333 V 1 2 N GLN B 541 ? N GLN B 541 O LEU B 548 ? O LEU B 548 W 1 2 N THR B 554 ? N THR B 554 O CYS B 560 ? O CYS B 560 X 1 2 N LYS B 580 ? N LYS B 580 O VAL B 587 ? O VAL B 587 Y 1 2 N VAL B 642 ? N VAL B 642 O VAL B 681 ? O VAL B 681 Y 2 3 O TYR B 680 ? O TYR B 680 N GLN B 668 ? N GLN B 668 Y 3 4 O PHE B 667 ? O PHE B 667 N CYS B 655 ? N CYS B 655 # 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 MN A 1027' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1028' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1029' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN A 1030' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MN A 1031' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN B 708' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN B 709' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MN B 710' AC9 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 44 RESIDUES 1001 TO 1004' BC1 Software ? ? ? ? 3 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 260 RESIDUES 1005 TO 1006' BC2 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 266 RESIDUES 1007 TO 1012' BC3 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 458 RESIDUES 1013 TO 1016' BC4 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND TO ASN A 524' BC5 Software ? ? ? ? 2 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 585 RESIDUES 1018 TO 1019' BC6 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A1020 BOUND TO ASN A 674' BC7 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1021 BOUND TO ASN A 821' BC8 Software ? ? ? ? 1 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 943 RESIDUES 1022 TO 1023' BC9 Software ? ? ? ? 3 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 950 RESIDUES 1024 TO 1026' CC1 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND TO ASN B 99' CC2 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND TO ASN B 320' CC3 Software ? ? ? ? 3 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 371 RESIDUES 703 TO 704' CC4 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 559 RESIDUES 705 TO 707' # 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 ASP A 230 ? ASP A 230 . ? 1_555 ? 2 AC1 5 ASN A 232 ? ASN A 232 . ? 1_555 ? 3 AC1 5 ASP A 234 ? ASP A 234 . ? 1_555 ? 4 AC1 5 ILE A 236 ? ILE A 236 . ? 1_555 ? 5 AC1 5 ASP A 238 ? ASP A 238 . ? 1_555 ? 6 AC2 5 ASP A 284 ? ASP A 284 . ? 1_555 ? 7 AC2 5 ASN A 286 ? ASN A 286 . ? 1_555 ? 8 AC2 5 ASP A 288 ? ASP A 288 . ? 1_555 ? 9 AC2 5 TYR A 290 ? TYR A 290 . ? 1_555 ? 10 AC2 5 ASP A 292 ? ASP A 292 . ? 1_555 ? 11 AC3 5 ASP A 349 ? ASP A 349 . ? 1_555 ? 12 AC3 5 ASP A 351 ? ASP A 351 . ? 1_555 ? 13 AC3 5 ASP A 353 ? ASP A 353 . ? 1_555 ? 14 AC3 5 PHE A 355 ? PHE A 355 . ? 1_555 ? 15 AC3 5 ASP A 357 ? ASP A 357 . ? 1_555 ? 16 AC4 5 ASP A 413 ? ASP A 413 . ? 1_555 ? 17 AC4 5 ASP A 415 ? ASP A 415 . ? 1_555 ? 18 AC4 5 ASN A 417 ? ASN A 417 . ? 1_555 ? 19 AC4 5 TYR A 419 ? TYR A 419 . ? 1_555 ? 20 AC4 5 ASP A 421 ? ASP A 421 . ? 1_555 ? 21 AC5 4 CYS A 596 ? CYS A 596 . ? 1_555 ? 22 AC5 4 ASP A 599 ? ASP A 599 . ? 1_555 ? 23 AC5 4 VAL A 601 ? VAL A 601 . ? 1_555 ? 24 AC5 4 GLU A 636 ? GLU A 636 . ? 1_555 ? 25 AC6 6 SER B 121 ? SER B 121 . ? 1_555 ? 26 AC6 6 SER B 123 ? SER B 123 . ? 1_555 ? 27 AC6 6 GLU B 220 ? GLU B 220 . ? 1_555 ? 28 AC6 6 HOH TA . ? HOH B 801 . ? 1_555 ? 29 AC6 6 HOH TA . ? HOH B 802 . ? 1_555 ? 30 AC6 6 ASP C 79 ? ASP C 1495 . ? 1_555 ? 31 AC7 5 SER B 123 ? SER B 123 . ? 1_555 ? 32 AC7 5 ASP B 126 ? ASP B 126 . ? 1_555 ? 33 AC7 5 ASP B 127 ? ASP B 127 . ? 1_555 ? 34 AC7 5 ASP B 251 ? ASP B 251 . ? 1_555 ? 35 AC7 5 ASN C 81 ? ASN C 1497 . ? 1_555 ? 36 AC8 5 ASP B 158 ? ASP B 158 . ? 1_555 ? 37 AC8 5 ASN B 215 ? ASN B 215 . ? 1_555 ? 38 AC8 5 ASP B 217 ? ASP B 217 . ? 1_555 ? 39 AC8 5 PRO B 219 ? PRO B 219 . ? 1_555 ? 40 AC8 5 GLU B 220 ? GLU B 220 . ? 1_555 ? 41 AC9 5 GLU A 15 ? GLU A 15 . ? 1_555 ? 42 AC9 5 GLY A 16 ? GLY A 16 . ? 1_555 ? 43 AC9 5 LYS A 42 ? LYS A 42 . ? 1_555 ? 44 AC9 5 ASN A 44 ? ASN A 44 . ? 1_555 ? 45 AC9 5 GLU A 52 ? GLU A 52 . ? 1_555 ? 46 BC1 3 ASP A 257 ? ASP A 257 . ? 1_555 ? 47 BC1 3 ASN A 260 ? ASN A 260 . ? 1_555 ? 48 BC1 3 SER A 262 ? SER A 262 . ? 1_555 ? 49 BC2 6 GLN A 214 ? GLN A 214 . ? 1_555 ? 50 BC2 6 PHE A 217 ? PHE A 217 . ? 1_555 ? 51 BC2 6 TYR A 254 ? TYR A 254 . ? 1_555 ? 52 BC2 6 SER A 263 ? SER A 263 . ? 1_555 ? 53 BC2 6 LEU A 264 ? LEU A 264 . ? 1_555 ? 54 BC2 6 ASN A 266 ? ASN A 266 . ? 1_555 ? 55 BC3 5 TYR A 450 ? TYR A 450 . ? 1_555 ? 56 BC3 5 ASN A 458 ? ASN A 458 . ? 1_555 ? 57 BC3 5 THR A 460 ? THR A 460 . ? 1_555 ? 58 BC3 5 CYS A 472 ? CYS A 472 . ? 1_555 ? 59 BC3 5 ASN B 48 ? ASN B 48 . ? 4_565 ? 60 BC4 1 ASN A 524 ? ASN A 524 . ? 1_555 ? 61 BC5 2 PHE A 558 ? PHE A 558 . ? 1_555 ? 62 BC5 2 ASN A 585 ? ASN A 585 . ? 1_555 ? 63 BC6 1 ASN A 674 ? ASN A 674 . ? 1_555 ? 64 BC7 2 ASN A 821 ? ASN A 821 . ? 1_555 ? 65 BC7 2 GLN A 885 ? GLN A 885 . ? 1_555 ? 66 BC8 1 ASN A 943 ? ASN A 943 . ? 1_555 ? 67 BC9 3 ASP A 751 ? ASP A 751 . ? 1_555 ? 68 BC9 3 ILE A 869 ? ILE A 869 . ? 1_555 ? 69 BC9 3 ASN A 950 ? ASN A 950 . ? 1_555 ? 70 CC1 2 LYS B 98 ? LYS B 98 . ? 1_555 ? 71 CC1 2 ASN B 99 ? ASN B 99 . ? 1_555 ? 72 CC2 2 ARG A 248 ? ARG A 248 . ? 1_555 ? 73 CC2 2 ASN B 320 ? ASN B 320 . ? 1_555 ? 74 CC3 3 ASN B 371 ? ASN B 371 . ? 1_555 ? 75 CC3 3 SER B 398 ? SER B 398 . ? 1_555 ? 76 CC3 3 GLU B 400 ? GLU B 400 . ? 1_555 ? 77 CC4 5 ASP A 621 ? ASP A 621 . ? 1_555 ? 78 CC4 5 PRO A 624 ? PRO A 624 . ? 1_555 ? 79 CC4 5 TYR B 531 ? TYR B 531 . ? 1_555 ? 80 CC4 5 TYR B 557 ? TYR B 557 . ? 1_555 ? 81 CC4 5 ASN B 559 ? ASN B 559 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MMY _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 4MMY _atom_sites.fract_transf_matrix[1][1] 0.007691 _atom_sites.fract_transf_matrix[1][2] 0.004441 _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] 0.008881 _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] 0.003245 _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 MN N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PHE A 1 1 ? -17.434 49.434 8.596 1.00 82.55 ? 1 PHE A N 1 ATOM 2 C CA . PHE A 1 1 ? -18.038 48.692 7.496 1.00 84.91 ? 1 PHE A CA 1 ATOM 3 C C . PHE A 1 1 ? -17.790 49.394 6.165 1.00 98.50 ? 1 PHE A C 1 ATOM 4 O O . PHE A 1 1 ? -17.961 48.804 5.097 1.00 106.69 ? 1 PHE A O 1 ATOM 5 C CB . PHE A 1 1 ? -19.540 48.513 7.729 1.00 89.58 ? 1 PHE A CB 1 ATOM 6 C CG . PHE A 1 1 ? -20.311 49.803 7.753 1.00 94.07 ? 1 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 1 ? -20.938 50.273 6.611 1.00 91.43 ? 1 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? -20.413 50.545 8.920 1.00 96.83 ? 1 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? -21.646 51.456 6.628 1.00 92.97 ? 1 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? -21.121 51.732 8.943 1.00 103.93 ? 1 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 1 ? -21.737 52.186 7.797 1.00 92.88 ? 1 PHE A CZ 1 ATOM 12 N N . ASN A 1 2 ? -17.384 50.657 6.238 1.00 90.70 ? 2 ASN A N 1 ATOM 13 C CA . ASN A 1 2 ? -17.196 51.476 5.047 1.00 99.36 ? 2 ASN A CA 1 ATOM 14 C C . ASN A 1 2 ? -15.760 51.503 4.524 1.00 100.98 ? 2 ASN A C 1 ATOM 15 O O . ASN A 1 2 ? -15.469 52.193 3.550 1.00 91.66 ? 2 ASN A O 1 ATOM 16 C CB . ASN A 1 2 ? -17.667 52.906 5.322 1.00 99.64 ? 2 ASN A CB 1 ATOM 17 C CG . ASN A 1 2 ? -17.259 53.399 6.695 1.00 93.66 ? 2 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 2 ? -17.322 52.659 7.678 1.00 93.89 ? 2 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 2 ? -16.836 54.655 6.771 1.00 90.04 ? 2 ASN A ND2 1 ATOM 20 N N . LEU A 1 3 ? -14.863 50.764 5.168 1.00 87.47 ? 3 LEU A N 1 ATOM 21 C CA . LEU A 1 3 ? -13.482 50.680 4.697 1.00 86.01 ? 3 LEU A CA 1 ATOM 22 C C . LEU A 1 3 ? -13.404 49.859 3.411 1.00 90.35 ? 3 LEU A C 1 ATOM 23 O O . LEU A 1 3 ? -14.095 48.851 3.268 1.00 90.16 ? 3 LEU A O 1 ATOM 24 C CB . LEU A 1 3 ? -12.576 50.073 5.773 1.00 82.78 ? 3 LEU A CB 1 ATOM 25 C CG . LEU A 1 3 ? -12.283 50.946 6.996 1.00 80.79 ? 3 LEU A CG 1 ATOM 26 C CD1 . LEU A 1 3 ? -11.431 50.198 8.012 1.00 77.25 ? 3 LEU A CD1 1 ATOM 27 C CD2 . LEU A 1 3 ? -11.602 52.238 6.575 1.00 82.37 ? 3 LEU A CD2 1 ATOM 28 N N . ASP A 1 4 ? -12.562 50.295 2.478 1.00 90.84 ? 4 ASP A N 1 ATOM 29 C CA . ASP A 1 4 ? -12.430 49.614 1.192 1.00 96.24 ? 4 ASP A CA 1 ATOM 30 C C . ASP A 1 4 ? -11.305 48.587 1.216 1.00 107.10 ? 4 ASP A C 1 ATOM 31 O O . ASP A 1 4 ? -10.130 48.942 1.317 1.00 91.99 ? 4 ASP A O 1 ATOM 32 C CB . ASP A 1 4 ? -12.188 50.628 0.069 1.00 97.54 ? 4 ASP A CB 1 ATOM 33 C CG . ASP A 1 4 ? -11.886 49.966 -1.265 1.00 125.59 ? 4 ASP A CG 1 ATOM 34 O OD1 . ASP A 1 4 ? -10.695 49.729 -1.559 1.00 110.11 ? 4 ASP A OD1 1 ATOM 35 O OD2 . ASP A 1 4 ? -12.839 49.684 -2.023 1.00 137.27 ? 4 ASP A OD2 1 ATOM 36 N N . VAL A 1 5 ? -11.672 47.313 1.125 1.00 102.69 ? 5 VAL A N 1 ATOM 37 C CA . VAL A 1 5 ? -10.690 46.236 1.077 1.00 93.72 ? 5 VAL A CA 1 ATOM 38 C C . VAL A 1 5 ? -10.406 45.817 -0.362 1.00 100.78 ? 5 VAL A C 1 ATOM 39 O O . VAL A 1 5 ? -9.557 44.961 -0.612 1.00 105.93 ? 5 VAL A O 1 ATOM 40 C CB . VAL A 1 5 ? -11.161 45.006 1.875 1.00 94.67 ? 5 VAL A CB 1 ATOM 41 C CG1 . VAL A 1 5 ? -11.570 45.416 3.277 1.00 95.37 ? 5 VAL A CG1 1 ATOM 42 C CG2 . VAL A 1 5 ? -12.313 44.317 1.160 1.00 110.78 ? 5 VAL A CG2 1 ATOM 43 N N . ASP A 1 6 ? -11.122 46.426 -1.303 1.00 101.44 ? 6 ASP A N 1 ATOM 44 C CA . ASP A 1 6 ? -10.968 46.103 -2.717 1.00 125.11 ? 6 ASP A CA 1 ATOM 45 C C . ASP A 1 6 ? -9.601 46.519 -3.251 1.00 121.56 ? 6 ASP A C 1 ATOM 46 O O . ASP A 1 6 ? -8.867 45.699 -3.803 1.00 123.70 ? 6 ASP A O 1 ATOM 47 C CB . ASP A 1 6 ? -12.071 46.772 -3.542 1.00 149.78 ? 6 ASP A CB 1 ATOM 48 C CG . ASP A 1 6 ? -13.451 46.236 -3.216 1.00 167.85 ? 6 ASP A CG 1 ATOM 49 O OD1 . ASP A 1 6 ? -13.549 45.079 -2.758 1.00 166.60 ? 6 ASP A OD1 1 ATOM 50 O OD2 . ASP A 1 6 ? -14.440 46.972 -3.423 1.00 175.47 ? 6 ASP A OD2 1 ATOM 51 N N . SER A 1 7 ? -9.265 47.793 -3.083 1.00 123.58 ? 7 SER A N 1 ATOM 52 C CA . SER A 1 7 ? -8.002 48.317 -3.592 1.00 122.61 ? 7 SER A CA 1 ATOM 53 C C . SER A 1 7 ? -7.334 49.271 -2.606 1.00 116.75 ? 7 SER A C 1 ATOM 54 O O . SER A 1 7 ? -7.392 50.488 -2.780 1.00 128.27 ? 7 SER A O 1 ATOM 55 C CB . SER A 1 7 ? -8.222 49.027 -4.929 1.00 132.04 ? 7 SER A CB 1 ATOM 56 O OG . SER A 1 7 ? -8.796 48.152 -5.885 1.00 157.55 ? 7 SER A OG 1 ATOM 57 N N . PRO A 1 8 ? -6.696 48.719 -1.564 1.00 103.64 ? 8 PRO A N 1 ATOM 58 C CA . PRO A 1 8 ? -5.947 49.540 -0.609 1.00 105.71 ? 8 PRO A CA 1 ATOM 59 C C . PRO A 1 8 ? -4.568 49.911 -1.148 1.00 107.45 ? 8 PRO A C 1 ATOM 60 O O . PRO A 1 8 ? -4.224 49.521 -2.264 1.00 128.50 ? 8 PRO A O 1 ATOM 61 C CB . PRO A 1 8 ? -5.832 48.629 0.613 1.00 91.50 ? 8 PRO A CB 1 ATOM 62 C CG . PRO A 1 8 ? -5.800 47.258 0.032 1.00 93.63 ? 8 PRO A CG 1 ATOM 63 C CD . PRO A 1 8 ? -6.691 47.294 -1.186 1.00 100.46 ? 8 PRO A CD 1 ATOM 64 N N . ALA A 1 9 ? -3.793 50.652 -0.364 1.00 95.30 ? 9 ALA A N 1 ATOM 65 C CA . ALA A 1 9 ? -2.451 51.048 -0.775 1.00 103.05 ? 9 ALA A CA 1 ATOM 66 C C . ALA A 1 9 ? -1.392 50.228 -0.046 1.00 96.74 ? 9 ALA A C 1 ATOM 67 O O . ALA A 1 9 ? -1.254 50.324 1.173 1.00 89.53 ? 9 ALA A O 1 ATOM 68 C CB . ALA A 1 9 ? -2.236 52.533 -0.526 1.00 115.05 ? 9 ALA A CB 1 ATOM 69 N N . GLU A 1 10 ? -0.646 49.425 -0.797 1.00 102.29 ? 10 GLU A N 1 ATOM 70 C CA . GLU A 1 10 ? 0.373 48.560 -0.211 1.00 100.05 ? 10 GLU A CA 1 ATOM 71 C C . GLU A 1 10 ? 1.769 49.162 -0.338 1.00 92.93 ? 10 GLU A C 1 ATOM 72 O O . GLU A 1 10 ? 2.246 49.426 -1.441 1.00 96.64 ? 10 GLU A O 1 ATOM 73 C CB . GLU A 1 10 ? 0.341 47.178 -0.866 1.00 107.30 ? 10 GLU A CB 1 ATOM 74 C CG . GLU A 1 10 ? -0.952 46.411 -0.634 1.00 121.01 ? 10 GLU A CG 1 ATOM 75 C CD . GLU A 1 10 ? -0.962 45.061 -1.324 1.00 144.58 ? 10 GLU A CD 1 ATOM 76 O OE1 . GLU A 1 10 ? 0.013 44.747 -2.039 1.00 159.92 ? 10 GLU A OE1 1 ATOM 77 O OE2 . GLU A 1 10 ? -1.947 44.311 -1.152 1.00 146.56 ? 10 GLU A OE2 1 ATOM 78 N N . TYR A 1 11 ? 2.418 49.376 0.801 1.00 89.24 ? 11 TYR A N 1 ATOM 79 C CA . TYR A 1 11 ? 3.788 49.874 0.824 1.00 89.28 ? 11 TYR A CA 1 ATOM 80 C C . TYR A 1 11 ? 4.724 48.801 1.367 1.00 88.80 ? 11 TYR A C 1 ATOM 81 O O . TYR A 1 11 ? 4.381 48.091 2.312 1.00 85.16 ? 11 TYR A O 1 ATOM 82 C CB . TYR A 1 11 ? 3.889 51.147 1.665 1.00 98.42 ? 11 TYR A CB 1 ATOM 83 C CG . TYR A 1 11 ? 3.066 52.301 1.138 1.00 96.16 ? 11 TYR A CG 1 ATOM 84 C CD1 . TYR A 1 11 ? 1.754 52.492 1.554 1.00 86.93 ? 11 TYR A CD1 1 ATOM 85 C CD2 . TYR A 1 11 ? 3.602 53.203 0.228 1.00 117.31 ? 11 TYR A CD2 1 ATOM 86 C CE1 . TYR A 1 11 ? 0.999 53.547 1.076 1.00 88.70 ? 11 TYR A CE1 1 ATOM 87 C CE2 . TYR A 1 11 ? 2.854 54.261 -0.255 1.00 123.71 ? 11 TYR A CE2 1 ATOM 88 C CZ . TYR A 1 11 ? 1.554 54.428 0.172 1.00 120.90 ? 11 TYR A CZ 1 ATOM 89 O OH . TYR A 1 11 ? 0.805 55.479 -0.306 1.00 118.79 ? 11 TYR A OH 1 ATOM 90 N N . SER A 1 12 ? 5.905 48.683 0.770 1.00 103.69 ? 12 SER A N 1 ATOM 91 C CA . SER A 1 12 ? 6.846 47.642 1.165 1.00 102.73 ? 12 SER A CA 1 ATOM 92 C C . SER A 1 12 ? 8.258 48.180 1.341 1.00 89.56 ? 12 SER A C 1 ATOM 93 O O . SER A 1 12 ? 8.823 48.781 0.427 1.00 92.63 ? 12 SER A O 1 ATOM 94 C CB . SER A 1 12 ? 6.849 46.510 0.136 1.00 116.83 ? 12 SER A CB 1 ATOM 95 O OG . SER A 1 12 ? 7.350 46.958 -1.112 1.00 128.51 ? 12 SER A OG 1 ATOM 96 N N . GLY A 1 13 ? 8.822 47.958 2.523 1.00 86.21 ? 13 GLY A N 1 ATOM 97 C CA . GLY A 1 13 ? 10.189 48.350 2.806 1.00 86.20 ? 13 GLY A CA 1 ATOM 98 C C . GLY A 1 13 ? 11.147 47.196 2.595 1.00 97.83 ? 13 GLY A C 1 ATOM 99 O O . GLY A 1 13 ? 10.735 46.118 2.165 1.00 101.00 ? 13 GLY A O 1 ATOM 100 N N . PRO A 1 14 ? 12.436 47.414 2.895 1.00 100.21 ? 14 PRO A N 1 ATOM 101 C CA . PRO A 1 14 ? 13.460 46.377 2.735 1.00 96.90 ? 14 PRO A CA 1 ATOM 102 C C . PRO A 1 14 ? 13.222 45.191 3.665 1.00 90.67 ? 14 PRO A C 1 ATOM 103 O O . PRO A 1 14 ? 12.646 45.359 4.739 1.00 94.95 ? 14 PRO A O 1 ATOM 104 C CB . PRO A 1 14 ? 14.759 47.106 3.091 1.00 89.18 ? 14 PRO A CB 1 ATOM 105 C CG . PRO A 1 14 ? 14.331 48.235 3.963 1.00 86.25 ? 14 PRO A CG 1 ATOM 106 C CD . PRO A 1 14 ? 12.997 48.665 3.434 1.00 88.87 ? 14 PRO A CD 1 ATOM 107 N N . GLU A 1 15 ? 13.663 44.009 3.247 1.00 89.95 ? 15 GLU A N 1 ATOM 108 C CA . GLU A 1 15 ? 13.406 42.780 3.990 1.00 98.69 ? 15 GLU A CA 1 ATOM 109 C C . GLU A 1 15 ? 14.160 42.734 5.318 1.00 90.68 ? 15 GLU A C 1 ATOM 110 O O . GLU A 1 15 ? 15.328 43.114 5.395 1.00 89.21 ? 15 GLU A O 1 ATOM 111 C CB . GLU A 1 15 ? 13.779 41.563 3.137 1.00 107.91 ? 15 GLU A CB 1 ATOM 112 C CG . GLU A 1 15 ? 13.394 40.227 3.752 1.00 111.03 ? 15 GLU A CG 1 ATOM 113 C CD . GLU A 1 15 ? 13.714 39.052 2.847 1.00 138.60 ? 15 GLU A CD 1 ATOM 114 O OE1 . GLU A 1 15 ? 14.495 39.230 1.888 1.00 140.09 ? 15 GLU A OE1 1 ATOM 115 O OE2 . GLU A 1 15 ? 13.182 37.949 3.094 1.00 154.54 ? 15 GLU A OE2 1 ATOM 116 N N . GLY A 1 16 ? 13.478 42.268 6.360 1.00 86.52 ? 16 GLY A N 1 ATOM 117 C CA . GLY A 1 16 ? 14.087 42.099 7.668 1.00 85.48 ? 16 GLY A CA 1 ATOM 118 C C . GLY A 1 16 ? 14.261 43.393 8.437 1.00 84.57 ? 16 GLY A C 1 ATOM 119 O O . GLY A 1 16 ? 14.858 43.406 9.513 1.00 84.64 ? 16 GLY A O 1 ATOM 120 N N . SER A 1 17 ? 13.727 44.481 7.893 1.00 84.07 ? 17 SER A N 1 ATOM 121 C CA . SER A 1 17 ? 13.899 45.802 8.488 1.00 83.95 ? 17 SER A CA 1 ATOM 122 C C . SER A 1 17 ? 12.779 46.147 9.461 1.00 81.10 ? 17 SER A C 1 ATOM 123 O O . SER A 1 17 ? 12.787 47.219 10.069 1.00 80.43 ? 17 SER A O 1 ATOM 124 C CB . SER A 1 17 ? 13.973 46.867 7.392 1.00 84.30 ? 17 SER A CB 1 ATOM 125 O OG . SER A 1 17 ? 12.773 46.905 6.639 1.00 83.39 ? 17 SER A OG 1 ATOM 126 N N . TYR A 1 18 ? 11.827 45.229 9.605 1.00 78.99 ? 18 TYR A N 1 ATOM 127 C CA . TYR A 1 18 ? 10.629 45.451 10.413 1.00 78.68 ? 18 TYR A CA 1 ATOM 128 C C . TYR A 1 18 ? 9.895 46.707 9.958 1.00 76.03 ? 18 TYR A C 1 ATOM 129 O O . TYR A 1 18 ? 9.402 47.486 10.773 1.00 73.18 ? 18 TYR A O 1 ATOM 130 C CB . TYR A 1 18 ? 10.972 45.545 11.904 1.00 73.24 ? 18 TYR A CB 1 ATOM 131 C CG . TYR A 1 18 ? 11.322 44.222 12.552 1.00 72.05 ? 18 TYR A CG 1 ATOM 132 C CD1 . TYR A 1 18 ? 11.498 44.126 13.925 1.00 69.70 ? 18 TYR A CD1 1 ATOM 133 C CD2 . TYR A 1 18 ? 11.482 43.071 11.790 1.00 74.10 ? 18 TYR A CD2 1 ATOM 134 C CE1 . TYR A 1 18 ? 11.817 42.922 14.522 1.00 68.88 ? 18 TYR A CE1 1 ATOM 135 C CE2 . TYR A 1 18 ? 11.803 41.864 12.378 1.00 74.50 ? 18 TYR A CE2 1 ATOM 136 C CZ . TYR A 1 18 ? 11.970 41.795 13.744 1.00 72.95 ? 18 TYR A CZ 1 ATOM 137 O OH . TYR A 1 18 ? 12.289 40.594 14.334 1.00 98.37 ? 18 TYR A OH 1 ATOM 138 N N . PHE A 1 19 ? 9.831 46.889 8.643 1.00 78.28 ? 19 PHE A N 1 ATOM 139 C CA . PHE A 1 19 ? 9.074 47.977 8.043 1.00 78.77 ? 19 PHE A CA 1 ATOM 140 C C . PHE A 1 19 ? 7.605 47.829 8.423 1.00 77.05 ? 19 PHE A C 1 ATOM 141 O O . PHE A 1 19 ? 7.000 46.782 8.194 1.00 76.41 ? 19 PHE A O 1 ATOM 142 C CB . PHE A 1 19 ? 9.260 47.970 6.522 1.00 81.20 ? 19 PHE A CB 1 ATOM 143 C CG . PHE A 1 19 ? 8.456 49.011 5.790 1.00 82.32 ? 19 PHE A CG 1 ATOM 144 C CD1 . PHE A 1 19 ? 7.192 48.714 5.305 1.00 99.81 ? 19 PHE A CD1 1 ATOM 145 C CD2 . PHE A 1 19 ? 8.978 50.273 5.556 1.00 82.89 ? 19 PHE A CD2 1 ATOM 146 C CE1 . PHE A 1 19 ? 6.455 49.662 4.621 1.00 93.13 ? 19 PHE A CE1 1 ATOM 147 C CE2 . PHE A 1 19 ? 8.246 51.227 4.870 1.00 87.47 ? 19 PHE A CE2 1 ATOM 148 C CZ . PHE A 1 19 ? 6.983 50.920 4.403 1.00 82.59 ? 19 PHE A CZ 1 ATOM 149 N N . GLY A 1 20 ? 7.036 48.873 9.013 1.00 77.03 ? 20 GLY A N 1 ATOM 150 C CA . GLY A 1 20 ? 5.652 48.838 9.446 1.00 72.96 ? 20 GLY A CA 1 ATOM 151 C C . GLY A 1 20 ? 5.472 48.607 10.935 1.00 67.87 ? 20 GLY A C 1 ATOM 152 O O . GLY A 1 20 ? 4.344 48.470 11.409 1.00 81.65 ? 20 GLY A O 1 ATOM 153 N N . PHE A 1 21 ? 6.578 48.560 11.675 1.00 67.23 ? 21 PHE A N 1 ATOM 154 C CA . PHE A 1 21 ? 6.519 48.346 13.121 1.00 71.71 ? 21 PHE A CA 1 ATOM 155 C C . PHE A 1 21 ? 5.824 49.516 13.812 1.00 67.60 ? 21 PHE A C 1 ATOM 156 O O . PHE A 1 21 ? 5.235 49.359 14.881 1.00 56.28 ? 21 PHE A O 1 ATOM 157 C CB . PHE A 1 21 ? 7.924 48.153 13.698 1.00 63.08 ? 21 PHE A CB 1 ATOM 158 C CG . PHE A 1 21 ? 7.938 47.696 15.134 1.00 58.29 ? 21 PHE A CG 1 ATOM 159 C CD1 . PHE A 1 21 ? 7.887 46.347 15.445 1.00 58.30 ? 21 PHE A CD1 1 ATOM 160 C CD2 . PHE A 1 21 ? 8.011 48.613 16.172 1.00 55.34 ? 21 PHE A CD2 1 ATOM 161 C CE1 . PHE A 1 21 ? 7.903 45.922 16.760 1.00 62.23 ? 21 PHE A CE1 1 ATOM 162 C CE2 . PHE A 1 21 ? 8.027 48.191 17.490 1.00 53.13 ? 21 PHE A CE2 1 ATOM 163 C CZ . PHE A 1 21 ? 7.973 46.843 17.784 1.00 53.23 ? 21 PHE A CZ 1 ATOM 164 N N . ALA A 1 22 ? 5.905 50.690 13.195 1.00 74.06 ? 22 ALA A N 1 ATOM 165 C CA . ALA A 1 22 ? 5.213 51.874 13.690 1.00 58.66 ? 22 ALA A CA 1 ATOM 166 C C . ALA A 1 22 ? 4.715 52.718 12.522 1.00 68.17 ? 22 ALA A C 1 ATOM 167 O O . ALA A 1 22 ? 5.413 52.877 11.520 1.00 88.16 ? 22 ALA A O 1 ATOM 168 C CB . ALA A 1 22 ? 6.124 52.689 14.590 1.00 60.48 ? 22 ALA A CB 1 ATOM 169 N N . VAL A 1 23 ? 3.505 53.255 12.653 1.00 73.64 ? 23 VAL A N 1 ATOM 170 C CA . VAL A 1 23 ? 2.896 54.037 11.579 1.00 75.28 ? 23 VAL A CA 1 ATOM 171 C C . VAL A 1 23 ? 2.169 55.274 12.093 1.00 82.88 ? 23 VAL A C 1 ATOM 172 O O . VAL A 1 23 ? 1.601 55.268 13.186 1.00 97.46 ? 23 VAL A O 1 ATOM 173 C CB . VAL A 1 23 ? 1.891 53.196 10.763 1.00 73.74 ? 23 VAL A CB 1 ATOM 174 C CG1 . VAL A 1 23 ? 2.612 52.157 9.921 1.00 81.71 ? 23 VAL A CG1 1 ATOM 175 C CG2 . VAL A 1 23 ? 0.870 52.541 11.681 1.00 62.37 ? 23 VAL A CG2 1 ATOM 176 N N . ASP A 1 24 ? 2.197 56.337 11.295 1.00 69.98 ? 24 ASP A N 1 ATOM 177 C CA . ASP A 1 24 ? 1.431 57.540 11.592 1.00 80.76 ? 24 ASP A CA 1 ATOM 178 C C . ASP A 1 24 ? 1.219 58.380 10.333 1.00 69.19 ? 24 ASP A C 1 ATOM 179 O O . ASP A 1 24 ? 1.919 58.208 9.336 1.00 87.17 ? 24 ASP A O 1 ATOM 180 C CB . ASP A 1 24 ? 2.129 58.369 12.672 1.00 101.54 ? 24 ASP A CB 1 ATOM 181 C CG . ASP A 1 24 ? 1.178 59.304 13.395 1.00 117.36 ? 24 ASP A CG 1 ATOM 182 O OD1 . ASP A 1 24 ? 0.154 59.696 12.798 1.00 116.85 ? 24 ASP A OD1 1 ATOM 183 O OD2 . ASP A 1 24 ? 1.456 59.646 14.563 1.00 125.31 ? 24 ASP A OD2 1 ATOM 184 N N . PHE A 1 25 ? 0.247 59.285 10.385 1.00 79.40 ? 25 PHE A N 1 ATOM 185 C CA . PHE A 1 25 ? 0.012 60.222 9.290 1.00 84.03 ? 25 PHE A CA 1 ATOM 186 C C . PHE A 1 25 ? 0.892 61.463 9.431 1.00 85.33 ? 25 PHE A C 1 ATOM 187 O O . PHE A 1 25 ? 1.124 61.950 10.539 1.00 80.90 ? 25 PHE A O 1 ATOM 188 C CB . PHE A 1 25 ? -1.458 60.638 9.234 1.00 74.06 ? 25 PHE A CB 1 ATOM 189 C CG . PHE A 1 25 ? -2.386 59.544 8.786 1.00 78.70 ? 25 PHE A CG 1 ATOM 190 C CD1 . PHE A 1 25 ? -3.006 58.719 9.711 1.00 76.61 ? 25 PHE A CD1 1 ATOM 191 C CD2 . PHE A 1 25 ? -2.650 59.349 7.440 1.00 77.05 ? 25 PHE A CD2 1 ATOM 192 C CE1 . PHE A 1 25 ? -3.866 57.719 9.302 1.00 73.34 ? 25 PHE A CE1 1 ATOM 193 C CE2 . PHE A 1 25 ? -3.508 58.349 7.025 1.00 77.21 ? 25 PHE A CE2 1 ATOM 194 C CZ . PHE A 1 25 ? -4.119 57.534 7.956 1.00 74.67 ? 25 PHE A CZ 1 ATOM 195 N N . PHE A 1 26 ? 1.384 61.966 8.303 1.00 81.20 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 2.161 63.200 8.282 1.00 94.68 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 1.417 64.281 7.503 1.00 98.64 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 1.278 64.194 6.284 1.00 104.87 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 3.544 62.955 7.674 1.00 97.71 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 4.431 64.168 7.669 1.00 103.54 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 5.194 64.479 6.556 1.00 102.34 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 4.497 65.000 8.774 1.00 99.04 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 6.013 65.592 6.548 1.00 87.86 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 5.310 66.117 8.773 1.00 93.50 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 6.070 66.414 7.657 1.00 92.57 ? 26 PHE A CZ 1 ATOM 206 N N . VAL A 1 27 ? 0.943 65.299 8.217 1.00 85.97 ? 27 VAL A N 1 ATOM 207 C CA . VAL A 1 27 ? 0.165 66.373 7.605 1.00 101.01 ? 27 VAL A CA 1 ATOM 208 C C . VAL A 1 27 ? 0.832 67.730 7.827 1.00 105.05 ? 27 VAL A C 1 ATOM 209 O O . VAL A 1 27 ? 0.515 68.434 8.787 1.00 91.11 ? 27 VAL A O 1 ATOM 210 C CB . VAL A 1 27 ? -1.274 66.415 8.165 1.00 107.40 ? 27 VAL A CB 1 ATOM 211 C CG1 . VAL A 1 27 ? -2.133 67.383 7.362 1.00 109.35 ? 27 VAL A CG1 1 ATOM 212 C CG2 . VAL A 1 27 ? -1.890 65.024 8.160 1.00 83.12 ? 27 VAL A CG2 1 ATOM 213 N N . PRO A 1 28 ? 1.767 68.098 6.937 1.00 90.27 ? 28 PRO A N 1 ATOM 214 C CA . PRO A 1 28 ? 2.479 69.378 7.021 1.00 92.63 ? 28 PRO A CA 1 ATOM 215 C C . PRO A 1 28 ? 1.544 70.570 6.851 1.00 112.31 ? 28 PRO A C 1 ATOM 216 O O . PRO A 1 28 ? 0.570 70.481 6.104 1.00 111.38 ? 28 PRO A O 1 ATOM 217 C CB . PRO A 1 28 ? 3.477 69.308 5.860 1.00 106.26 ? 28 PRO A CB 1 ATOM 218 C CG . PRO A 1 28 ? 3.581 67.861 5.518 1.00 99.89 ? 28 PRO A CG 1 ATOM 219 C CD . PRO A 1 28 ? 2.236 67.283 5.805 1.00 107.30 ? 28 PRO A CD 1 ATOM 220 N N . SER A 1 29 ? 1.838 71.670 7.536 1.00 124.88 ? 29 SER A N 1 ATOM 221 C CA . SER A 1 29 ? 1.038 72.883 7.414 1.00 115.47 ? 29 SER A CA 1 ATOM 222 C C . SER A 1 29 ? 1.435 73.684 6.177 1.00 105.42 ? 29 SER A C 1 ATOM 223 O O . SER A 1 29 ? 0.671 74.519 5.692 1.00 109.13 ? 29 SER A O 1 ATOM 224 C CB . SER A 1 29 ? 1.181 73.746 8.668 1.00 107.86 ? 29 SER A CB 1 ATOM 225 O OG . SER A 1 29 ? 2.539 74.075 8.907 1.00 103.84 ? 29 SER A OG 1 ATOM 226 N N . ALA A 1 30 ? 2.633 73.417 5.668 1.00 105.54 ? 30 ALA A N 1 ATOM 227 C CA . ALA A 1 30 ? 3.178 74.174 4.547 1.00 137.60 ? 30 ALA A CA 1 ATOM 228 C C . ALA A 1 30 ? 2.839 73.542 3.199 1.00 112.06 ? 30 ALA A C 1 ATOM 229 O O . ALA A 1 30 ? 3.266 74.034 2.154 1.00 116.15 ? 30 ALA A O 1 ATOM 230 C CB . ALA A 1 30 ? 4.685 74.314 4.697 1.00 144.68 ? 30 ALA A CB 1 ATOM 231 N N . SER A 1 31 ? 2.076 72.454 3.223 1.00 133.30 ? 31 SER A N 1 ATOM 232 C CA . SER A 1 31 ? 1.713 71.758 1.992 1.00 124.43 ? 31 SER A CA 1 ATOM 233 C C . SER A 1 31 ? 0.306 71.174 2.060 1.00 123.74 ? 31 SER A C 1 ATOM 234 O O . SER A 1 31 ? -0.168 70.792 3.130 1.00 106.26 ? 31 SER A O 1 ATOM 235 C CB . SER A 1 31 ? 2.723 70.648 1.691 1.00 123.35 ? 31 SER A CB 1 ATOM 236 O OG . SER A 1 31 ? 2.414 69.994 0.473 1.00 131.53 ? 31 SER A OG 1 ATOM 237 N N . SER A 1 32 ? -0.356 71.110 0.908 1.00 113.28 ? 32 SER A N 1 ATOM 238 C CA . SER A 1 32 ? -1.695 70.540 0.821 1.00 112.74 ? 32 SER A CA 1 ATOM 239 C C . SER A 1 32 ? -1.634 69.019 0.733 1.00 113.18 ? 32 SER A C 1 ATOM 240 O O . SER A 1 32 ? -2.631 68.331 0.951 1.00 123.33 ? 32 SER A O 1 ATOM 241 C CB . SER A 1 32 ? -2.441 71.109 -0.387 1.00 119.87 ? 32 SER A CB 1 ATOM 242 O OG . SER A 1 32 ? -1.707 70.905 -1.582 1.00 125.38 ? 32 SER A OG 1 ATOM 243 N N . ARG A 1 33 ? -0.454 68.501 0.407 1.00 109.00 ? 33 ARG A N 1 ATOM 244 C CA . ARG A 1 33 ? -0.234 67.063 0.320 1.00 106.34 ? 33 ARG A CA 1 ATOM 245 C C . ARG A 1 33 ? -0.137 66.423 1.701 1.00 110.52 ? 33 ARG A C 1 ATOM 246 O O . ARG A 1 33 ? 0.155 67.097 2.690 1.00 99.43 ? 33 ARG A O 1 ATOM 247 C CB . ARG A 1 33 ? 1.037 66.766 -0.477 1.00 107.93 ? 33 ARG A CB 1 ATOM 248 C CG . ARG A 1 33 ? 0.990 67.229 -1.922 1.00 127.84 ? 33 ARG A CG 1 ATOM 249 C CD . ARG A 1 33 ? 2.362 67.132 -2.568 1.00 148.60 ? 33 ARG A CD 1 ATOM 250 N NE . ARG A 1 33 ? 2.890 65.772 -2.536 1.00 154.87 ? 33 ARG A NE 1 ATOM 251 C CZ . ARG A 1 33 ? 4.127 65.443 -2.896 1.00 161.55 ? 33 ARG A CZ 1 ATOM 252 N NH1 . ARG A 1 33 ? 4.968 66.379 -3.313 1.00 159.72 ? 33 ARG A NH1 1 ATOM 253 N NH2 . ARG A 1 33 ? 4.524 64.179 -2.836 1.00 157.30 ? 33 ARG A NH2 1 ATOM 254 N N . MET A 1 34 ? -0.385 65.120 1.758 1.00 129.04 ? 34 MET A N 1 ATOM 255 C CA . MET A 1 34 ? -0.225 64.362 2.992 1.00 116.91 ? 34 MET A CA 1 ATOM 256 C C . MET A 1 34 ? 0.586 63.098 2.735 1.00 92.43 ? 34 MET A C 1 ATOM 257 O O . MET A 1 34 ? 0.613 62.584 1.617 1.00 94.89 ? 34 MET A O 1 ATOM 258 C CB . MET A 1 34 ? -1.587 64.018 3.593 1.00 92.17 ? 34 MET A CB 1 ATOM 259 C CG . MET A 1 34 ? -2.171 65.134 4.442 1.00 117.85 ? 34 MET A CG 1 ATOM 260 S SD . MET A 1 34 ? -3.916 64.903 4.825 1.00 96.82 ? 34 MET A SD 1 ATOM 261 C CE . MET A 1 34 ? -4.653 65.225 3.224 1.00 96.75 ? 34 MET A CE 1 ATOM 262 N N . PHE A 1 35 ? 1.251 62.604 3.773 1.00 88.73 ? 35 PHE A N 1 ATOM 263 C CA . PHE A 1 35 ? 2.167 61.480 3.624 1.00 87.50 ? 35 PHE A CA 1 ATOM 264 C C . PHE A 1 35 ? 1.979 60.426 4.708 1.00 95.02 ? 35 PHE A C 1 ATOM 265 O O . PHE A 1 35 ? 1.308 60.660 5.713 1.00 102.17 ? 35 PHE A O 1 ATOM 266 C CB . PHE A 1 35 ? 3.617 61.971 3.639 1.00 87.99 ? 35 PHE A CB 1 ATOM 267 C CG . PHE A 1 35 ? 3.946 62.937 2.537 1.00 103.32 ? 35 PHE A CG 1 ATOM 268 C CD1 . PHE A 1 35 ? 3.727 64.296 2.700 1.00 93.93 ? 35 PHE A CD1 1 ATOM 269 C CD2 . PHE A 1 35 ? 4.486 62.490 1.344 1.00 111.24 ? 35 PHE A CD2 1 ATOM 270 C CE1 . PHE A 1 35 ? 4.032 65.188 1.691 1.00 102.54 ? 35 PHE A CE1 1 ATOM 271 C CE2 . PHE A 1 35 ? 4.794 63.378 0.331 1.00 108.83 ? 35 PHE A CE2 1 ATOM 272 C CZ . PHE A 1 35 ? 4.566 64.730 0.505 1.00 109.84 ? 35 PHE A CZ 1 ATOM 273 N N . LEU A 1 36 ? 2.580 59.261 4.489 1.00 82.62 ? 36 LEU A N 1 ATOM 274 C CA . LEU A 1 36 ? 2.606 58.204 5.489 1.00 88.07 ? 36 LEU A CA 1 ATOM 275 C C . LEU A 1 36 ? 3.975 58.151 6.157 1.00 85.63 ? 36 LEU A C 1 ATOM 276 O O . LEU A 1 36 ? 5.002 58.294 5.494 1.00 90.04 ? 36 LEU A O 1 ATOM 277 C CB . LEU A 1 36 ? 2.277 56.842 4.865 1.00 83.41 ? 36 LEU A CB 1 ATOM 278 C CG . LEU A 1 36 ? 0.844 56.548 4.414 1.00 88.73 ? 36 LEU A CG 1 ATOM 279 C CD1 . LEU A 1 36 ? 0.536 57.178 3.065 1.00 115.43 ? 36 LEU A CD1 1 ATOM 280 C CD2 . LEU A 1 36 ? 0.601 55.047 4.372 1.00 83.10 ? 36 LEU A CD2 1 ATOM 281 N N . LEU A 1 37 ? 3.986 57.955 7.471 1.00 77.46 ? 37 LEU A N 1 ATOM 282 C CA . LEU A 1 37 ? 5.232 57.756 8.201 1.00 72.08 ? 37 LEU A CA 1 ATOM 283 C C . LEU A 1 37 ? 5.322 56.315 8.683 1.00 87.75 ? 37 LEU A C 1 ATOM 284 O O . LEU A 1 37 ? 4.454 55.839 9.414 1.00 72.92 ? 37 LEU A O 1 ATOM 285 C CB . LEU A 1 37 ? 5.337 58.726 9.379 1.00 70.37 ? 37 LEU A CB 1 ATOM 286 C CG . LEU A 1 37 ? 5.463 60.204 9.003 1.00 84.35 ? 37 LEU A CG 1 ATOM 287 C CD1 . LEU A 1 37 ? 5.642 61.068 10.241 1.00 97.51 ? 37 LEU A CD1 1 ATOM 288 C CD2 . LEU A 1 37 ? 6.611 60.413 8.028 1.00 75.24 ? 37 LEU A CD2 1 ATOM 289 N N . VAL A 1 38 ? 6.368 55.616 8.257 1.00 82.86 ? 38 VAL A N 1 ATOM 290 C CA . VAL A 1 38 ? 6.526 54.208 8.595 1.00 79.43 ? 38 VAL A CA 1 ATOM 291 C C . VAL A 1 38 ? 7.879 53.938 9.241 1.00 83.17 ? 38 VAL A C 1 ATOM 292 O O . VAL A 1 38 ? 8.923 54.278 8.684 1.00 74.72 ? 38 VAL A O 1 ATOM 293 C CB . VAL A 1 38 ? 6.380 53.312 7.353 1.00 74.07 ? 38 VAL A CB 1 ATOM 294 C CG1 . VAL A 1 38 ? 6.396 51.856 7.761 1.00 75.02 ? 38 VAL A CG1 1 ATOM 295 C CG2 . VAL A 1 38 ? 5.101 53.643 6.601 1.00 74.90 ? 38 VAL A CG2 1 ATOM 296 N N . GLY A 1 39 ? 7.856 53.330 10.423 1.00 72.03 ? 39 GLY A N 1 ATOM 297 C CA . GLY A 1 39 ? 9.082 52.983 11.113 1.00 65.70 ? 39 GLY A CA 1 ATOM 298 C C . GLY A 1 39 ? 9.676 51.676 10.626 1.00 70.07 ? 39 GLY A C 1 ATOM 299 O O . GLY A 1 39 ? 8.953 50.733 10.302 1.00 91.22 ? 39 GLY A O 1 ATOM 300 N N . ALA A 1 40 ? 11.003 51.622 10.578 1.00 70.79 ? 40 ALA A N 1 ATOM 301 C CA . ALA A 1 40 ? 11.721 50.407 10.211 1.00 74.47 ? 40 ALA A CA 1 ATOM 302 C C . ALA A 1 40 ? 12.957 50.266 11.090 1.00 73.68 ? 40 ALA A C 1 ATOM 303 O O . ALA A 1 40 ? 14.069 50.559 10.655 1.00 75.23 ? 40 ALA A O 1 ATOM 304 C CB . ALA A 1 40 ? 12.103 50.427 8.742 1.00 77.35 ? 40 ALA A CB 1 ATOM 305 N N . PRO A 1 41 ? 12.759 49.809 12.335 1.00 70.88 ? 41 PRO A N 1 ATOM 306 C CA . PRO A 1 41 ? 13.787 49.819 13.383 1.00 69.83 ? 41 PRO A CA 1 ATOM 307 C C . PRO A 1 41 ? 15.028 48.982 13.074 1.00 73.76 ? 41 PRO A C 1 ATOM 308 O O . PRO A 1 41 ? 16.108 49.303 13.570 1.00 95.40 ? 41 PRO A O 1 ATOM 309 C CB . PRO A 1 41 ? 13.047 49.250 14.600 1.00 67.35 ? 41 PRO A CB 1 ATOM 310 C CG . PRO A 1 41 ? 11.923 48.459 14.031 1.00 82.79 ? 41 PRO A CG 1 ATOM 311 C CD . PRO A 1 41 ? 11.502 49.198 12.802 1.00 70.06 ? 41 PRO A CD 1 ATOM 312 N N . LYS A 1 42 ? 14.880 47.919 12.291 1.00 78.51 ? 42 LYS A N 1 ATOM 313 C CA . LYS A 1 42 ? 16.015 47.057 11.968 1.00 83.11 ? 42 LYS A CA 1 ATOM 314 C C . LYS A 1 42 ? 16.657 47.379 10.618 1.00 85.23 ? 42 LYS A C 1 ATOM 315 O O . LYS A 1 42 ? 17.560 46.671 10.174 1.00 87.59 ? 42 LYS A O 1 ATOM 316 C CB . LYS A 1 42 ? 15.593 45.588 12.014 1.00 82.37 ? 42 LYS A CB 1 ATOM 317 C CG . LYS A 1 42 ? 15.428 45.065 13.433 1.00 79.09 ? 42 LYS A CG 1 ATOM 318 C CD . LYS A 1 42 ? 15.248 43.559 13.486 1.00 88.26 ? 42 LYS A CD 1 ATOM 319 C CE . LYS A 1 42 ? 15.275 43.075 14.929 1.00 85.55 ? 42 LYS A CE 1 ATOM 320 N NZ . LYS A 1 42 ? 15.022 41.614 15.050 1.00 106.86 ? 42 LYS A NZ 1 ATOM 321 N N . ALA A 1 43 ? 16.181 48.435 9.963 1.00 90.00 ? 43 ALA A N 1 ATOM 322 C CA . ALA A 1 43 ? 16.717 48.840 8.663 1.00 88.85 ? 43 ALA A CA 1 ATOM 323 C C . ALA A 1 43 ? 18.183 49.259 8.748 1.00 84.69 ? 43 ALA A C 1 ATOM 324 O O . ALA A 1 43 ? 18.629 49.790 9.763 1.00 82.60 ? 43 ALA A O 1 ATOM 325 C CB . ALA A 1 43 ? 15.883 49.970 8.079 1.00 81.88 ? 43 ALA A CB 1 ATOM 326 N N . ASN A 1 44 ? 18.924 49.017 7.671 1.00 91.56 ? 44 ASN A N 1 ATOM 327 C CA . ASN A 1 44 ? 20.332 49.396 7.593 1.00 88.90 ? 44 ASN A CA 1 ATOM 328 C C . ASN A 1 44 ? 20.505 50.830 7.099 1.00 97.79 ? 44 ASN A C 1 ATOM 329 O O . ASN A 1 44 ? 19.765 51.287 6.230 1.00 102.28 ? 44 ASN A O 1 ATOM 330 C CB . ASN A 1 44 ? 21.094 48.425 6.689 1.00 89.87 ? 44 ASN A CB 1 ATOM 331 C CG . ASN A 1 44 ? 21.654 47.242 7.453 1.00 91.72 ? 44 ASN A CG 1 ATOM 332 O OD1 . ASN A 1 44 ? 22.172 47.401 8.558 1.00 90.92 ? 44 ASN A OD1 1 ATOM 333 N ND2 . ASN A 1 44 ? 21.550 46.050 6.877 1.00 128.59 ? 44 ASN A ND2 1 ATOM 334 N N . THR A 1 45 ? 21.488 51.534 7.653 1.00 108.61 ? 45 THR A N 1 ATOM 335 C CA . THR A 1 45 ? 21.643 52.962 7.393 1.00 99.64 ? 45 THR A CA 1 ATOM 336 C C . THR A 1 45 ? 23.006 53.328 6.810 1.00 96.84 ? 45 THR A C 1 ATOM 337 O O . THR A 1 45 ? 23.958 52.550 6.878 1.00 87.50 ? 45 THR A O 1 ATOM 338 C CB . THR A 1 45 ? 21.427 53.787 8.678 1.00 107.53 ? 45 THR A CB 1 ATOM 339 O OG1 . THR A 1 45 ? 22.371 53.379 9.676 1.00 110.87 ? 45 THR A OG1 1 ATOM 340 C CG2 . THR A 1 45 ? 20.018 53.588 9.210 1.00 113.88 ? 45 THR A CG2 1 ATOM 341 N N . THR A 1 46 ? 23.082 54.526 6.237 1.00 113.29 ? 46 THR A N 1 ATOM 342 C CA . THR A 1 46 ? 24.316 55.041 5.652 1.00 105.03 ? 46 THR A CA 1 ATOM 343 C C . THR A 1 46 ? 25.290 55.531 6.720 1.00 100.67 ? 46 THR A C 1 ATOM 344 O O . THR A 1 46 ? 26.423 55.905 6.414 1.00 103.97 ? 46 THR A O 1 ATOM 345 C CB . THR A 1 46 ? 24.031 56.194 4.670 1.00 94.63 ? 46 THR A CB 1 ATOM 346 O OG1 . THR A 1 46 ? 25.269 56.749 4.208 1.00 147.64 ? 46 THR A OG1 1 ATOM 347 C CG2 . THR A 1 46 ? 23.216 57.284 5.352 1.00 92.01 ? 46 THR A CG2 1 ATOM 348 N N . GLN A 1 47 ? 24.835 55.538 7.970 1.00 98.95 ? 47 GLN A N 1 ATOM 349 C CA . GLN A 1 47 ? 25.660 55.965 9.095 1.00 91.47 ? 47 GLN A CA 1 ATOM 350 C C . GLN A 1 47 ? 26.900 55.084 9.233 1.00 94.35 ? 47 GLN A C 1 ATOM 351 O O . GLN A 1 47 ? 26.797 53.856 9.235 1.00 90.82 ? 47 GLN A O 1 ATOM 352 C CB . GLN A 1 47 ? 24.845 55.937 10.389 1.00 80.58 ? 47 GLN A CB 1 ATOM 353 C CG . GLN A 1 47 ? 23.493 56.629 10.285 1.00 79.29 ? 47 GLN A CG 1 ATOM 354 C CD . GLN A 1 47 ? 22.662 56.485 11.547 1.00 99.84 ? 47 GLN A CD 1 ATOM 355 O OE1 . GLN A 1 47 ? 21.559 55.938 11.519 1.00 110.69 ? 47 GLN A OE1 1 ATOM 356 N NE2 . GLN A 1 47 ? 23.189 56.979 12.661 1.00 101.66 ? 47 GLN A NE2 1 ATOM 357 N N . PRO A 1 48 ? 28.080 55.714 9.345 1.00 99.28 ? 48 PRO A N 1 ATOM 358 C CA . PRO A 1 48 ? 29.364 55.006 9.422 1.00 91.70 ? 48 PRO A CA 1 ATOM 359 C C . PRO A 1 48 ? 29.474 54.078 10.629 1.00 88.42 ? 48 PRO A C 1 ATOM 360 O O . PRO A 1 48 ? 29.199 54.493 11.755 1.00 83.85 ? 48 PRO A O 1 ATOM 361 C CB . PRO A 1 48 ? 30.386 56.144 9.527 1.00 91.66 ? 48 PRO A CB 1 ATOM 362 C CG . PRO A 1 48 ? 29.695 57.333 8.952 1.00 92.39 ? 48 PRO A CG 1 ATOM 363 C CD . PRO A 1 48 ? 28.258 57.175 9.337 1.00 96.45 ? 48 PRO A CD 1 ATOM 364 N N . GLY A 1 49 ? 29.880 52.835 10.385 1.00 98.82 ? 49 GLY A N 1 ATOM 365 C CA . GLY A 1 49 ? 30.091 51.866 11.446 1.00 91.89 ? 49 GLY A CA 1 ATOM 366 C C . GLY A 1 49 ? 28.846 51.509 12.235 1.00 89.88 ? 49 GLY A C 1 ATOM 367 O O . GLY A 1 49 ? 28.939 50.993 13.349 1.00 90.15 ? 49 GLY A O 1 ATOM 368 N N . ILE A 1 50 ? 27.677 51.781 11.662 1.00 85.89 ? 50 ILE A N 1 ATOM 369 C CA . ILE A 1 50 ? 26.416 51.509 12.341 1.00 87.37 ? 50 ILE A CA 1 ATOM 370 C C . ILE A 1 50 ? 25.628 50.403 11.644 1.00 95.88 ? 50 ILE A C 1 ATOM 371 O O . ILE A 1 50 ? 25.223 50.548 10.490 1.00 100.42 ? 50 ILE A O 1 ATOM 372 C CB . ILE A 1 50 ? 25.539 52.773 12.428 1.00 85.91 ? 50 ILE A CB 1 ATOM 373 C CG1 . ILE A 1 50 ? 26.282 53.888 13.168 1.00 84.89 ? 50 ILE A CG1 1 ATOM 374 C CG2 . ILE A 1 50 ? 24.218 52.462 13.116 1.00 77.84 ? 50 ILE A CG2 1 ATOM 375 C CD1 . ILE A 1 50 ? 26.724 53.507 14.565 1.00 82.64 ? 50 ILE A CD1 1 ATOM 376 N N . VAL A 1 51 ? 25.414 49.300 12.356 1.00 89.09 ? 51 VAL A N 1 ATOM 377 C CA . VAL A 1 51 ? 24.665 48.170 11.817 1.00 89.20 ? 51 VAL A CA 1 ATOM 378 C C . VAL A 1 51 ? 23.220 48.182 12.306 1.00 86.90 ? 51 VAL A C 1 ATOM 379 O O . VAL A 1 51 ? 22.967 48.173 13.512 1.00 85.27 ? 51 VAL A O 1 ATOM 380 C CB . VAL A 1 51 ? 25.314 46.828 12.202 1.00 94.39 ? 51 VAL A CB 1 ATOM 381 C CG1 . VAL A 1 51 ? 24.537 45.670 11.596 1.00 96.62 ? 51 VAL A CG1 1 ATOM 382 C CG2 . VAL A 1 51 ? 26.765 46.793 11.753 1.00 110.85 ? 51 VAL A CG2 1 ATOM 383 N N . GLU A 1 52 ? 22.285 48.195 11.358 1.00 89.93 ? 52 GLU A N 1 ATOM 384 C CA . GLU A 1 52 ? 20.853 48.239 11.649 1.00 85.24 ? 52 GLU A CA 1 ATOM 385 C C . GLU A 1 52 ? 20.496 49.368 12.610 1.00 80.68 ? 52 GLU A C 1 ATOM 386 O O . GLU A 1 52 ? 20.024 49.126 13.720 1.00 78.48 ? 52 GLU A O 1 ATOM 387 C CB . GLU A 1 52 ? 20.377 46.901 12.222 1.00 87.40 ? 52 GLU A CB 1 ATOM 388 C CG . GLU A 1 52 ? 20.513 45.729 11.266 1.00 98.73 ? 52 GLU A CG 1 ATOM 389 C CD . GLU A 1 52 ? 19.850 44.471 11.791 1.00 111.84 ? 52 GLU A CD 1 ATOM 390 O OE1 . GLU A 1 52 ? 19.329 44.500 12.927 1.00 115.31 ? 52 GLU A OE1 1 ATOM 391 O OE2 . GLU A 1 52 ? 19.846 43.452 11.067 1.00 109.77 ? 52 GLU A OE2 1 ATOM 392 N N . GLY A 1 53 ? 20.718 50.603 12.174 1.00 93.60 ? 53 GLY A N 1 ATOM 393 C CA . GLY A 1 53 ? 20.418 51.760 12.992 1.00 89.19 ? 53 GLY A CA 1 ATOM 394 C C . GLY A 1 53 ? 18.927 52.011 13.087 1.00 87.49 ? 53 GLY A C 1 ATOM 395 O O . GLY A 1 53 ? 18.429 52.470 14.112 1.00 90.02 ? 53 GLY A O 1 ATOM 396 N N . GLY A 1 54 ? 18.212 51.702 12.011 1.00 89.61 ? 54 GLY A N 1 ATOM 397 C CA . GLY A 1 54 ? 16.781 51.930 11.960 1.00 73.16 ? 54 GLY A CA 1 ATOM 398 C C . GLY A 1 54 ? 16.434 53.143 11.122 1.00 72.90 ? 54 GLY A C 1 ATOM 399 O O . GLY A 1 54 ? 17.241 54.061 10.982 1.00 100.01 ? 54 GLY A O 1 ATOM 400 N N . GLN A 1 55 ? 15.228 53.150 10.565 1.00 72.43 ? 55 GLN A N 1 ATOM 401 C CA . GLN A 1 55 ? 14.803 54.239 9.697 1.00 77.64 ? 55 GLN A CA 1 ATOM 402 C C . GLN A 1 55 ? 13.356 54.651 9.929 1.00 84.66 ? 55 GLN A C 1 ATOM 403 O O . GLN A 1 55 ? 12.546 53.880 10.446 1.00 87.72 ? 55 GLN A O 1 ATOM 404 C CB . GLN A 1 55 ? 14.979 53.853 8.226 1.00 76.31 ? 55 GLN A CB 1 ATOM 405 C CG . GLN A 1 55 ? 16.403 53.933 7.710 1.00 87.55 ? 55 GLN A CG 1 ATOM 406 C CD . GLN A 1 55 ? 16.478 53.758 6.206 1.00 96.81 ? 55 GLN A CD 1 ATOM 407 O OE1 . GLN A 1 55 ? 15.473 53.480 5.551 1.00 91.38 ? 55 GLN A OE1 1 ATOM 408 N NE2 . GLN A 1 55 ? 17.672 53.924 5.650 1.00 117.72 ? 55 GLN A NE2 1 ATOM 409 N N . VAL A 1 56 ? 13.049 55.884 9.543 1.00 95.44 ? 56 VAL A N 1 ATOM 410 C CA . VAL A 1 56 ? 11.675 56.355 9.444 1.00 79.01 ? 56 VAL A CA 1 ATOM 411 C C . VAL A 1 56 ? 11.464 56.885 8.035 1.00 90.80 ? 56 VAL A C 1 ATOM 412 O O . VAL A 1 56 ? 12.077 57.876 7.639 1.00 85.95 ? 56 VAL A O 1 ATOM 413 C CB . VAL A 1 56 ? 11.359 57.457 10.470 1.00 71.45 ? 56 VAL A CB 1 ATOM 414 C CG1 . VAL A 1 56 ? 9.932 57.954 10.289 1.00 68.73 ? 56 VAL A CG1 1 ATOM 415 C CG2 . VAL A 1 56 ? 11.573 56.943 11.880 1.00 80.22 ? 56 VAL A CG2 1 ATOM 416 N N . LEU A 1 57 ? 10.600 56.222 7.275 1.00 100.61 ? 57 LEU A N 1 ATOM 417 C CA . LEU A 1 57 ? 10.433 56.555 5.867 1.00 109.97 ? 57 LEU A CA 1 ATOM 418 C C . LEU A 1 57 ? 9.181 57.385 5.615 1.00 97.42 ? 57 LEU A C 1 ATOM 419 O O . LEU A 1 57 ? 8.151 57.193 6.258 1.00 80.42 ? 57 LEU A O 1 ATOM 420 C CB . LEU A 1 57 ? 10.393 55.282 5.016 1.00 107.13 ? 57 LEU A CB 1 ATOM 421 C CG . LEU A 1 57 ? 11.655 54.416 4.998 1.00 92.05 ? 57 LEU A CG 1 ATOM 422 C CD1 . LEU A 1 57 ? 11.614 53.350 6.085 1.00 86.31 ? 57 LEU A CD1 1 ATOM 423 C CD2 . LEU A 1 57 ? 11.859 53.786 3.629 1.00 93.70 ? 57 LEU A CD2 1 ATOM 424 N N . LYS A 1 58 ? 9.289 58.315 4.672 1.00 82.37 ? 58 LYS A N 1 ATOM 425 C CA . LYS A 1 58 ? 8.160 59.138 4.264 1.00 83.80 ? 58 LYS A CA 1 ATOM 426 C C . LYS A 1 58 ? 7.565 58.593 2.972 1.00 86.80 ? 58 LYS A C 1 ATOM 427 O O . LYS A 1 58 ? 8.209 58.621 1.924 1.00 96.20 ? 58 LYS A O 1 ATOM 428 C CB . LYS A 1 58 ? 8.595 60.594 4.085 1.00 105.06 ? 58 LYS A CB 1 ATOM 429 C CG . LYS A 1 58 ? 7.504 61.520 3.580 1.00 108.71 ? 58 LYS A CG 1 ATOM 430 C CD . LYS A 1 58 ? 7.925 62.973 3.716 1.00 94.91 ? 58 LYS A CD 1 ATOM 431 C CE . LYS A 1 58 ? 9.214 63.248 2.960 1.00 104.48 ? 58 LYS A CE 1 ATOM 432 N NZ . LYS A 1 58 ? 9.036 63.071 1.493 1.00 97.80 ? 58 LYS A NZ 1 ATOM 433 N N . CYS A 1 59 ? 6.338 58.090 3.051 1.00 85.83 ? 59 CYS A N 1 ATOM 434 C CA . CYS A 1 59 ? 5.701 57.458 1.900 1.00 105.72 ? 59 CYS A CA 1 ATOM 435 C C . CYS A 1 59 ? 4.663 58.363 1.242 1.00 91.16 ? 59 CYS A C 1 ATOM 436 O O . CYS A 1 59 ? 3.724 58.826 1.889 1.00 89.52 ? 59 CYS A O 1 ATOM 437 C CB . CYS A 1 59 ? 5.055 56.133 2.315 1.00 114.36 ? 59 CYS A CB 1 ATOM 438 S SG . CYS A 1 59 ? 6.231 54.883 2.887 1.00 106.54 ? 59 CYS A SG 1 ATOM 439 N N . ASP A 1 60 ? 4.841 58.604 -0.053 1.00 95.47 ? 60 ASP A N 1 ATOM 440 C CA . ASP A 1 60 ? 3.935 59.461 -0.813 1.00 113.22 ? 60 ASP A CA 1 ATOM 441 C C . ASP A 1 60 ? 2.719 58.686 -1.310 1.00 116.67 ? 60 ASP A C 1 ATOM 442 O O . ASP A 1 60 ? 2.857 57.669 -1.987 1.00 153.90 ? 60 ASP A O 1 ATOM 443 C CB . ASP A 1 60 ? 4.667 60.098 -1.997 1.00 122.85 ? 60 ASP A CB 1 ATOM 444 C CG . ASP A 1 60 ? 3.792 61.064 -2.771 1.00 138.54 ? 60 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 60 ? 3.994 61.208 -3.996 1.00 149.08 ? 60 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 60 ? 2.899 61.684 -2.153 1.00 134.43 ? 60 ASP A OD2 1 ATOM 447 N N . TRP A 1 61 ? 1.531 59.175 -0.969 1.00 98.81 ? 61 TRP A N 1 ATOM 448 C CA . TRP A 1 61 ? 0.286 58.533 -1.376 1.00 101.26 ? 61 TRP A CA 1 ATOM 449 C C . TRP A 1 61 ? -0.105 58.866 -2.812 1.00 109.78 ? 61 TRP A C 1 ATOM 450 O O . TRP A 1 61 ? -0.678 58.035 -3.518 1.00 106.77 ? 61 TRP A O 1 ATOM 451 C CB . TRP A 1 61 ? -0.852 58.932 -0.434 1.00 97.20 ? 61 TRP A CB 1 ATOM 452 C CG . TRP A 1 61 ? -2.188 58.392 -0.851 1.00 104.66 ? 61 TRP A CG 1 ATOM 453 C CD1 . TRP A 1 61 ? -2.622 57.104 -0.737 1.00 104.54 ? 61 TRP A CD1 1 ATOM 454 C CD2 . TRP A 1 61 ? -3.264 59.127 -1.447 1.00 115.68 ? 61 TRP A CD2 1 ATOM 455 N NE1 . TRP A 1 61 ? -3.900 56.989 -1.227 1.00 109.16 ? 61 TRP A NE1 1 ATOM 456 C CE2 . TRP A 1 61 ? -4.318 58.218 -1.669 1.00 123.96 ? 61 TRP A CE2 1 ATOM 457 C CE3 . TRP A 1 61 ? -3.440 60.464 -1.815 1.00 119.79 ? 61 TRP A CE3 1 ATOM 458 C CZ2 . TRP A 1 61 ? -5.529 58.602 -2.240 1.00 127.57 ? 61 TRP A CZ2 1 ATOM 459 C CZ3 . TRP A 1 61 ? -4.643 60.843 -2.384 1.00 127.77 ? 61 TRP A CZ3 1 ATOM 460 C CH2 . TRP A 1 61 ? -5.671 59.915 -2.591 1.00 131.38 ? 61 TRP A CH2 1 ATOM 461 N N . SER A 1 62 ? 0.207 60.086 -3.236 1.00 107.57 ? 62 SER A N 1 ATOM 462 C CA . SER A 1 62 ? -0.255 60.602 -4.521 1.00 135.72 ? 62 SER A CA 1 ATOM 463 C C . SER A 1 62 ? 0.249 59.798 -5.717 1.00 158.40 ? 62 SER A C 1 ATOM 464 O O . SER A 1 62 ? -0.545 59.310 -6.522 1.00 163.16 ? 62 SER A O 1 ATOM 465 C CB . SER A 1 62 ? 0.162 62.065 -4.678 1.00 147.68 ? 62 SER A CB 1 ATOM 466 O OG . SER A 1 62 ? 1.573 62.195 -4.678 1.00 155.30 ? 62 SER A OG 1 ATOM 467 N N . SER A 1 63 ? 1.566 59.657 -5.832 1.00 168.75 ? 63 SER A N 1 ATOM 468 C CA . SER A 1 63 ? 2.155 59.057 -7.024 1.00 165.50 ? 63 SER A CA 1 ATOM 469 C C . SER A 1 63 ? 3.143 57.934 -6.720 1.00 172.89 ? 63 SER A C 1 ATOM 470 O O . SER A 1 63 ? 3.981 58.051 -5.825 1.00 167.79 ? 63 SER A O 1 ATOM 471 C CB . SER A 1 63 ? 2.851 60.134 -7.859 1.00 142.94 ? 63 SER A CB 1 ATOM 472 O OG . SER A 1 63 ? 3.881 60.764 -7.118 1.00 122.96 ? 63 SER A OG 1 ATOM 473 N N . THR A 1 64 ? 3.013 56.840 -7.469 1.00 170.72 ? 64 THR A N 1 ATOM 474 C CA . THR A 1 64 ? 3.982 55.738 -7.502 1.00 153.99 ? 64 THR A CA 1 ATOM 475 C C . THR A 1 64 ? 4.123 54.968 -6.188 1.00 130.90 ? 64 THR A C 1 ATOM 476 O O . THR A 1 64 ? 4.792 53.934 -6.149 1.00 124.64 ? 64 THR A O 1 ATOM 477 C CB . THR A 1 64 ? 5.391 56.232 -7.923 1.00 137.68 ? 64 THR A CB 1 ATOM 478 O OG1 . THR A 1 64 ? 5.940 57.076 -6.903 1.00 141.55 ? 64 THR A OG1 1 ATOM 479 C CG2 . THR A 1 64 ? 5.322 56.996 -9.238 1.00 142.45 ? 64 THR A CG2 1 ATOM 480 N N . ARG A 1 65 ? 3.491 55.467 -5.128 1.00 111.07 ? 65 ARG A N 1 ATOM 481 C CA . ARG A 1 65 ? 3.554 54.852 -3.802 1.00 123.83 ? 65 ARG A CA 1 ATOM 482 C C . ARG A 1 65 ? 4.996 54.662 -3.336 1.00 121.05 ? 65 ARG A C 1 ATOM 483 O O . ARG A 1 65 ? 5.309 53.705 -2.626 1.00 126.02 ? 65 ARG A O 1 ATOM 484 C CB . ARG A 1 65 ? 2.817 53.509 -3.798 1.00 129.02 ? 65 ARG A CB 1 ATOM 485 C CG . ARG A 1 65 ? 1.444 53.556 -4.447 1.00 148.87 ? 65 ARG A CG 1 ATOM 486 C CD . ARG A 1 65 ? 0.498 54.484 -3.701 1.00 145.64 ? 65 ARG A CD 1 ATOM 487 N NE . ARG A 1 65 ? -0.712 54.753 -4.475 1.00 153.52 ? 65 ARG A NE 1 ATOM 488 C CZ . ARG A 1 65 ? -1.767 53.947 -4.521 1.00 136.39 ? 65 ARG A CZ 1 ATOM 489 N NH1 . ARG A 1 65 ? -1.769 52.811 -3.838 1.00 110.16 ? 65 ARG A NH1 1 ATOM 490 N NH2 . ARG A 1 65 ? -2.821 54.276 -5.256 1.00 135.00 ? 65 ARG A NH2 1 ATOM 491 N N . ARG A 1 66 ? 5.868 55.578 -3.746 1.00 112.31 ? 66 ARG A N 1 ATOM 492 C CA . ARG A 1 66 ? 7.279 55.515 -3.386 1.00 107.46 ? 66 ARG A CA 1 ATOM 493 C C . ARG A 1 66 ? 7.508 55.950 -1.946 1.00 108.33 ? 66 ARG A C 1 ATOM 494 O O . ARG A 1 66 ? 6.723 56.715 -1.385 1.00 103.52 ? 66 ARG A O 1 ATOM 495 C CB . ARG A 1 66 ? 8.112 56.381 -4.333 1.00 123.89 ? 66 ARG A CB 1 ATOM 496 C CG . ARG A 1 66 ? 8.534 55.678 -5.613 1.00 150.38 ? 66 ARG A CG 1 ATOM 497 C CD . ARG A 1 66 ? 10.033 55.400 -5.632 1.00 159.90 ? 66 ARG A CD 1 ATOM 498 N NE . ARG A 1 66 ? 10.821 56.623 -5.759 1.00 163.14 ? 66 ARG A NE 1 ATOM 499 C CZ . ARG A 1 66 ? 11.398 57.255 -4.742 1.00 152.83 ? 66 ARG A CZ 1 ATOM 500 N NH1 . ARG A 1 66 ? 11.280 56.781 -3.509 1.00 130.81 ? 66 ARG A NH1 1 ATOM 501 N NH2 . ARG A 1 66 ? 12.095 58.362 -4.958 1.00 138.76 ? 66 ARG A NH2 1 ATOM 502 N N . CYS A 1 67 ? 8.592 55.459 -1.355 1.00 119.64 ? 67 CYS A N 1 ATOM 503 C CA . CYS A 1 67 ? 8.945 55.810 0.014 1.00 113.17 ? 67 CYS A CA 1 ATOM 504 C C . CYS A 1 67 ? 10.405 56.233 0.108 1.00 124.75 ? 67 CYS A C 1 ATOM 505 O O . CYS A 1 67 ? 11.289 55.570 -0.432 1.00 138.07 ? 67 CYS A O 1 ATOM 506 C CB . CYS A 1 67 ? 8.677 54.635 0.957 1.00 90.96 ? 67 CYS A CB 1 ATOM 507 S SG . CYS A 1 67 ? 6.934 54.183 1.114 1.00 184.10 ? 67 CYS A SG 1 ATOM 508 N N . GLN A 1 68 ? 10.651 57.342 0.797 1.00 122.01 ? 68 GLN A N 1 ATOM 509 C CA . GLN A 1 68 ? 12.011 57.816 1.011 1.00 115.45 ? 68 GLN A CA 1 ATOM 510 C C . GLN A 1 68 ? 12.284 57.968 2.499 1.00 103.02 ? 68 GLN A C 1 ATOM 511 O O . GLN A 1 68 ? 11.418 58.413 3.252 1.00 104.10 ? 68 GLN A O 1 ATOM 512 C CB . GLN A 1 68 ? 12.237 59.150 0.297 1.00 97.79 ? 68 GLN A CB 1 ATOM 513 C CG . GLN A 1 68 ? 11.981 59.113 -1.199 1.00 106.33 ? 68 GLN A CG 1 ATOM 514 C CD . GLN A 1 68 ? 12.069 60.486 -1.835 1.00 141.49 ? 68 GLN A CD 1 ATOM 515 O OE1 . GLN A 1 68 ? 11.926 60.632 -3.049 1.00 154.27 ? 68 GLN A OE1 1 ATOM 516 N NE2 . GLN A 1 68 ? 12.305 61.504 -1.015 1.00 148.39 ? 68 GLN A NE2 1 ATOM 517 N N . PRO A 1 69 ? 13.495 57.591 2.931 1.00 93.37 ? 69 PRO A N 1 ATOM 518 C CA . PRO A 1 69 ? 13.877 57.729 4.339 1.00 85.44 ? 69 PRO A CA 1 ATOM 519 C C . PRO A 1 69 ? 14.074 59.186 4.744 1.00 91.22 ? 69 PRO A C 1 ATOM 520 O O . PRO A 1 69 ? 14.701 59.946 4.007 1.00 96.56 ? 69 PRO A O 1 ATOM 521 C CB . PRO A 1 69 ? 15.201 56.957 4.424 1.00 85.73 ? 69 PRO A CB 1 ATOM 522 C CG . PRO A 1 69 ? 15.221 56.077 3.208 1.00 88.86 ? 69 PRO A CG 1 ATOM 523 C CD . PRO A 1 69 ? 14.511 56.864 2.155 1.00 100.74 ? 69 PRO A CD 1 ATOM 524 N N . ILE A 1 70 ? 13.539 59.568 5.897 1.00 83.98 ? 70 ILE A N 1 ATOM 525 C CA . ILE A 1 70 ? 13.833 60.874 6.467 1.00 86.99 ? 70 ILE A CA 1 ATOM 526 C C . ILE A 1 70 ? 15.178 60.779 7.174 1.00 95.65 ? 70 ILE A C 1 ATOM 527 O O . ILE A 1 70 ? 15.422 59.824 7.911 1.00 113.21 ? 70 ILE A O 1 ATOM 528 C CB . ILE A 1 70 ? 12.744 61.336 7.457 1.00 79.80 ? 70 ILE A CB 1 ATOM 529 C CG1 . ILE A 1 70 ? 11.365 61.285 6.800 1.00 80.65 ? 70 ILE A CG1 1 ATOM 530 C CG2 . ILE A 1 70 ? 13.039 62.741 7.963 1.00 90.20 ? 70 ILE A CG2 1 ATOM 531 C CD1 . ILE A 1 70 ? 10.235 61.687 7.723 1.00 78.40 ? 70 ILE A CD1 1 ATOM 532 N N . GLU A 1 71 ? 16.054 61.755 6.957 1.00 86.28 ? 71 GLU A N 1 ATOM 533 C CA . GLU A 1 71 ? 17.378 61.684 7.561 1.00 97.46 ? 71 GLU A CA 1 ATOM 534 C C . GLU A 1 71 ? 17.445 62.579 8.790 1.00 91.32 ? 71 GLU A C 1 ATOM 535 O O . GLU A 1 71 ? 17.523 63.804 8.688 1.00 90.42 ? 71 GLU A O 1 ATOM 536 C CB . GLU A 1 71 ? 18.448 62.084 6.541 1.00 107.28 ? 71 GLU A CB 1 ATOM 537 C CG . GLU A 1 71 ? 19.846 61.581 6.858 1.00 115.19 ? 71 GLU A CG 1 ATOM 538 C CD . GLU A 1 71 ? 20.819 61.824 5.719 1.00 146.36 ? 71 GLU A CD 1 ATOM 539 O OE1 . GLU A 1 71 ? 21.777 61.036 5.574 1.00 160.01 ? 71 GLU A OE1 1 ATOM 540 O OE2 . GLU A 1 71 ? 20.624 62.801 4.965 1.00 145.05 ? 71 GLU A OE2 1 ATOM 541 N N . PHE A 1 72 ? 17.408 61.945 9.957 1.00 84.62 ? 72 PHE A N 1 ATOM 542 C CA . PHE A 1 72 ? 17.467 62.649 11.230 1.00 80.98 ? 72 PHE A CA 1 ATOM 543 C C . PHE A 1 72 ? 18.894 62.942 11.684 1.00 101.38 ? 72 PHE A C 1 ATOM 544 O O . PHE A 1 72 ? 19.191 64.038 12.157 1.00 129.72 ? 72 PHE A O 1 ATOM 545 C CB . PHE A 1 72 ? 16.730 61.844 12.304 1.00 82.45 ? 72 PHE A CB 1 ATOM 546 C CG . PHE A 1 72 ? 15.235 61.821 12.127 1.00 88.33 ? 72 PHE A CG 1 ATOM 547 C CD1 . PHE A 1 72 ? 14.638 60.945 11.234 1.00 102.91 ? 72 PHE A CD1 1 ATOM 548 C CD2 . PHE A 1 72 ? 14.426 62.672 12.862 1.00 70.95 ? 72 PHE A CD2 1 ATOM 549 C CE1 . PHE A 1 72 ? 13.264 60.922 11.074 1.00 88.50 ? 72 PHE A CE1 1 ATOM 550 C CE2 . PHE A 1 72 ? 13.052 62.654 12.708 1.00 74.17 ? 72 PHE A CE2 1 ATOM 551 C CZ . PHE A 1 72 ? 12.471 61.779 11.813 1.00 72.64 ? 72 PHE A CZ 1 ATOM 552 N N . ASP A 1 73 ? 19.774 61.957 11.528 1.00 76.81 ? 73 ASP A N 1 ATOM 553 C CA . ASP A 1 73 ? 21.104 62.017 12.127 1.00 99.85 ? 73 ASP A CA 1 ATOM 554 C C . ASP A 1 73 ? 22.233 61.869 11.111 1.00 114.62 ? 73 ASP A C 1 ATOM 555 O O . ASP A 1 73 ? 23.023 62.796 10.916 1.00 115.92 ? 73 ASP A O 1 ATOM 556 C CB . ASP A 1 73 ? 21.238 60.935 13.201 1.00 73.87 ? 73 ASP A CB 1 ATOM 557 C CG . ASP A 1 73 ? 22.550 61.018 13.953 1.00 110.56 ? 73 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 73 ? 23.080 59.957 14.344 1.00 133.19 ? 73 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 73 ? 23.048 62.144 14.160 1.00 119.65 ? 73 ASP A OD2 1 ATOM 560 N N . ALA A 1 74 ? 22.320 60.684 10.506 1.00 99.53 ? 74 ALA A N 1 ATOM 561 C CA . ALA A 1 74 ? 23.353 60.341 9.522 1.00 122.80 ? 74 ALA A CA 1 ATOM 562 C C . ALA A 1 74 ? 24.751 60.269 10.138 1.00 100.71 ? 74 ALA A C 1 ATOM 563 O O . ALA A 1 74 ? 25.718 59.940 9.453 1.00 86.57 ? 74 ALA A O 1 ATOM 564 C CB . ALA A 1 74 ? 23.342 61.328 8.357 1.00 87.32 ? 74 ALA A CB 1 ATOM 565 N N . THR A 1 75 ? 24.853 60.582 11.425 1.00 94.07 ? 75 THR A N 1 ATOM 566 C CA . THR A 1 75 ? 26.135 60.590 12.117 1.00 101.00 ? 75 THR A CA 1 ATOM 567 C C . THR A 1 75 ? 26.396 59.258 12.814 1.00 79.56 ? 75 THR A C 1 ATOM 568 O O . THR A 1 75 ? 25.478 58.639 13.351 1.00 81.58 ? 75 THR A O 1 ATOM 569 C CB . THR A 1 75 ? 26.201 61.731 13.154 1.00 99.42 ? 75 THR A CB 1 ATOM 570 O OG1 . THR A 1 75 ? 25.807 62.963 12.538 1.00 111.24 ? 75 THR A OG1 1 ATOM 571 C CG2 . THR A 1 75 ? 27.608 61.880 13.717 1.00 100.23 ? 75 THR A CG2 1 ATOM 572 N N . GLY A 1 76 ? 27.651 58.820 12.797 1.00 85.10 ? 76 GLY A N 1 ATOM 573 C CA . GLY A 1 76 ? 28.048 57.614 13.499 1.00 79.53 ? 76 GLY A CA 1 ATOM 574 C C . GLY A 1 76 ? 28.186 57.859 14.989 1.00 77.25 ? 76 GLY A C 1 ATOM 575 O O . GLY A 1 76 ? 27.652 58.831 15.522 1.00 79.90 ? 76 GLY A O 1 ATOM 576 N N . ASN A 1 77 ? 28.906 56.972 15.668 1.00 76.50 ? 77 ASN A N 1 ATOM 577 C CA . ASN A 1 77 ? 29.083 57.076 17.112 1.00 78.10 ? 77 ASN A CA 1 ATOM 578 C C . ASN A 1 77 ? 30.065 58.172 17.521 1.00 95.67 ? 77 ASN A C 1 ATOM 579 O O . ASN A 1 77 ? 31.165 58.270 16.977 1.00 91.81 ? 77 ASN A O 1 ATOM 580 C CB . ASN A 1 77 ? 29.545 55.732 17.680 1.00 75.34 ? 77 ASN A CB 1 ATOM 581 C CG . ASN A 1 77 ? 28.494 54.650 17.542 1.00 90.67 ? 77 ASN A CG 1 ATOM 582 O OD1 . ASN A 1 77 ? 27.298 54.910 17.672 1.00 72.27 ? 77 ASN A OD1 1 ATOM 583 N ND2 . ASN A 1 77 ? 28.936 53.425 17.282 1.00 139.04 ? 77 ASN A ND2 1 ATOM 584 N N . ARG A 1 78 ? 29.654 58.995 18.481 1.00 81.83 ? 78 ARG A N 1 ATOM 585 C CA . ARG A 1 78 ? 30.525 60.019 19.051 1.00 85.61 ? 78 ARG A CA 1 ATOM 586 C C . ARG A 1 78 ? 31.521 59.390 20.026 1.00 88.47 ? 78 ARG A C 1 ATOM 587 O O . ARG A 1 78 ? 31.284 58.299 20.544 1.00 78.82 ? 78 ARG A O 1 ATOM 588 C CB . ARG A 1 78 ? 29.694 61.105 19.740 1.00 75.11 ? 78 ARG A CB 1 ATOM 589 C CG . ARG A 1 78 ? 28.970 62.025 18.764 1.00 76.07 ? 78 ARG A CG 1 ATOM 590 C CD . ARG A 1 78 ? 28.043 63.008 19.469 1.00 75.00 ? 78 ARG A CD 1 ATOM 591 N NE . ARG A 1 78 ? 26.834 62.361 19.976 1.00 71.92 ? 78 ARG A NE 1 ATOM 592 C CZ . ARG A 1 78 ? 25.797 63.015 20.490 1.00 78.44 ? 78 ARG A CZ 1 ATOM 593 N NH1 . ARG A 1 78 ? 25.815 64.338 20.567 1.00 77.46 ? 78 ARG A NH1 1 ATOM 594 N NH2 . ARG A 1 78 ? 24.739 62.344 20.927 1.00 87.46 ? 78 ARG A NH2 1 ATOM 595 N N . ASP A 1 79 ? 32.638 60.072 20.265 1.00 78.16 ? 79 ASP A N 1 ATOM 596 C CA . ASP A 1 79 ? 33.722 59.501 21.065 1.00 87.74 ? 79 ASP A CA 1 ATOM 597 C C . ASP A 1 79 ? 33.953 60.206 22.401 1.00 87.55 ? 79 ASP A C 1 ATOM 598 O O . ASP A 1 79 ? 33.996 61.433 22.473 1.00 112.45 ? 79 ASP A O 1 ATOM 599 C CB . ASP A 1 79 ? 35.027 59.509 20.265 1.00 111.42 ? 79 ASP A CB 1 ATOM 600 C CG . ASP A 1 79 ? 34.991 58.565 19.081 1.00 132.79 ? 79 ASP A CG 1 ATOM 601 O OD1 . ASP A 1 79 ? 36.021 57.911 18.808 1.00 129.09 ? 79 ASP A OD1 1 ATOM 602 O OD2 . ASP A 1 79 ? 33.937 58.478 18.418 1.00 154.57 ? 79 ASP A OD2 1 ATOM 603 N N . TYR A 1 80 ? 34.098 59.406 23.453 1.00 76.84 ? 80 TYR A N 1 ATOM 604 C CA . TYR A 1 80 ? 34.472 59.895 24.776 1.00 76.87 ? 80 TYR A CA 1 ATOM 605 C C . TYR A 1 80 ? 35.988 60.106 24.894 1.00 84.08 ? 80 TYR A C 1 ATOM 606 O O . TYR A 1 80 ? 36.451 60.943 25.668 1.00 80.97 ? 80 TYR A O 1 ATOM 607 C CB . TYR A 1 80 ? 33.979 58.917 25.848 1.00 75.32 ? 80 TYR A CB 1 ATOM 608 C CG . TYR A 1 80 ? 34.376 59.261 27.263 1.00 86.59 ? 80 TYR A CG 1 ATOM 609 C CD1 . TYR A 1 80 ? 33.652 60.183 28.006 1.00 75.32 ? 80 TYR A CD1 1 ATOM 610 C CD2 . TYR A 1 80 ? 35.466 58.645 27.867 1.00 101.80 ? 80 TYR A CD2 1 ATOM 611 C CE1 . TYR A 1 80 ? 34.009 60.492 29.305 1.00 74.99 ? 80 TYR A CE1 1 ATOM 612 C CE2 . TYR A 1 80 ? 35.831 58.947 29.164 1.00 100.48 ? 80 TYR A CE2 1 ATOM 613 C CZ . TYR A 1 80 ? 35.098 59.871 29.879 1.00 79.97 ? 80 TYR A CZ 1 ATOM 614 O OH . TYR A 1 80 ? 35.459 60.174 31.172 1.00 91.38 ? 80 TYR A OH 1 ATOM 615 N N . ALA A 1 81 ? 36.750 59.343 24.112 1.00 81.97 ? 81 ALA A N 1 ATOM 616 C CA . ALA A 1 81 ? 38.214 59.399 24.128 1.00 85.24 ? 81 ALA A CA 1 ATOM 617 C C . ALA A 1 81 ? 38.767 58.951 22.776 1.00 102.25 ? 81 ALA A C 1 ATOM 618 O O . ALA A 1 81 ? 38.015 58.868 21.804 1.00 105.99 ? 81 ALA A O 1 ATOM 619 C CB . ALA A 1 81 ? 38.778 58.544 25.251 1.00 84.78 ? 81 ALA A CB 1 ATOM 620 N N . LYS A 1 82 ? 40.076 58.695 22.714 1.00 118.95 ? 82 LYS A N 1 ATOM 621 C CA . LYS A 1 82 ? 40.751 58.342 21.459 1.00 127.15 ? 82 LYS A CA 1 ATOM 622 C C . LYS A 1 82 ? 40.009 57.241 20.703 1.00 139.55 ? 82 LYS A C 1 ATOM 623 O O . LYS A 1 82 ? 39.397 57.510 19.669 1.00 170.49 ? 82 LYS A O 1 ATOM 624 C CB . LYS A 1 82 ? 42.194 57.912 21.728 1.00 120.22 ? 82 LYS A CB 1 ATOM 625 C CG . LYS A 1 82 ? 43.079 57.945 20.493 1.00 114.11 ? 82 LYS A CG 1 ATOM 626 C CD . LYS A 1 82 ? 42.966 59.287 19.788 1.00 120.72 ? 82 LYS A CD 1 ATOM 627 C CE . LYS A 1 82 ? 43.868 59.359 18.567 1.00 127.87 ? 82 LYS A CE 1 ATOM 628 N NZ . LYS A 1 82 ? 45.311 59.308 18.932 1.00 121.20 ? 82 LYS A NZ 1 ATOM 629 N N . ASP A 1 83 ? 40.056 56.006 21.197 1.00 97.94 ? 83 ASP A N 1 ATOM 630 C CA . ASP A 1 83 ? 38.994 55.080 20.842 1.00 95.95 ? 83 ASP A CA 1 ATOM 631 C C . ASP A 1 83 ? 38.247 54.720 22.117 1.00 109.73 ? 83 ASP A C 1 ATOM 632 O O . ASP A 1 83 ? 38.652 53.823 22.858 1.00 118.71 ? 83 ASP A O 1 ATOM 633 C CB . ASP A 1 83 ? 39.554 53.824 20.167 1.00 116.78 ? 83 ASP A CB 1 ATOM 634 C CG . ASP A 1 83 ? 40.540 54.144 19.057 1.00 146.33 ? 83 ASP A CG 1 ATOM 635 O OD1 . ASP A 1 83 ? 40.096 54.401 17.918 1.00 165.13 ? 83 ASP A OD1 1 ATOM 636 O OD2 . ASP A 1 83 ? 41.762 54.130 19.322 1.00 128.88 ? 83 ASP A OD2 1 ATOM 637 N N . ASP A 1 84 ? 37.149 55.426 22.356 1.00 101.13 ? 84 ASP A N 1 ATOM 638 C CA . ASP A 1 84 ? 36.236 55.126 23.448 1.00 85.37 ? 84 ASP A CA 1 ATOM 639 C C . ASP A 1 84 ? 34.837 55.613 23.098 1.00 84.96 ? 84 ASP A C 1 ATOM 640 O O . ASP A 1 84 ? 34.452 56.697 23.536 1.00 87.36 ? 84 ASP A O 1 ATOM 641 C CB . ASP A 1 84 ? 36.712 55.760 24.752 1.00 85.50 ? 84 ASP A CB 1 ATOM 642 C CG . ASP A 1 84 ? 36.126 55.087 25.973 1.00 113.20 ? 84 ASP A CG 1 ATOM 643 O OD1 . ASP A 1 84 ? 36.848 54.303 26.626 1.00 114.79 ? 84 ASP A OD1 1 ATOM 644 O OD2 . ASP A 1 84 ? 34.940 55.333 26.275 1.00 144.58 ? 84 ASP A OD2 1 ATOM 645 N N . PRO A 1 85 ? 34.088 54.849 22.290 1.00 87.28 ? 85 PRO A N 1 ATOM 646 C CA . PRO A 1 85 ? 32.784 55.330 21.814 1.00 78.48 ? 85 PRO A CA 1 ATOM 647 C C . PRO A 1 85 ? 31.878 55.850 22.934 1.00 83.34 ? 85 PRO A C 1 ATOM 648 O O . PRO A 1 85 ? 31.694 55.184 23.952 1.00 77.60 ? 85 PRO A O 1 ATOM 649 C CB . PRO A 1 85 ? 32.174 54.085 21.165 1.00 79.70 ? 85 PRO A CB 1 ATOM 650 C CG . PRO A 1 85 ? 33.349 53.283 20.727 1.00 94.58 ? 85 PRO A CG 1 ATOM 651 C CD . PRO A 1 85 ? 34.416 53.514 21.761 1.00 102.17 ? 85 PRO A CD 1 ATOM 652 N N . LEU A 1 86 ? 31.332 57.046 22.732 1.00 73.59 ? 86 LEU A N 1 ATOM 653 C CA . LEU A 1 86 ? 30.462 57.688 23.712 1.00 70.19 ? 86 LEU A CA 1 ATOM 654 C C . LEU A 1 86 ? 29.042 57.154 23.606 1.00 68.54 ? 86 LEU A C 1 ATOM 655 O O . LEU A 1 86 ? 28.242 57.280 24.531 1.00 85.39 ? 86 LEU A O 1 ATOM 656 C CB . LEU A 1 86 ? 30.470 59.207 23.519 1.00 89.32 ? 86 LEU A CB 1 ATOM 657 C CG . LEU A 1 86 ? 29.377 60.022 24.219 1.00 69.17 ? 86 LEU A CG 1 ATOM 658 C CD1 . LEU A 1 86 ? 29.667 60.190 25.706 1.00 68.61 ? 86 LEU A CD1 1 ATOM 659 C CD2 . LEU A 1 86 ? 29.175 61.358 23.535 1.00 89.14 ? 86 LEU A CD2 1 ATOM 660 N N . GLU A 1 87 ? 28.733 56.554 22.464 1.00 74.25 ? 87 GLU A N 1 ATOM 661 C CA . GLU A 1 87 ? 27.399 56.032 22.218 1.00 67.34 ? 87 GLU A CA 1 ATOM 662 C C . GLU A 1 87 ? 27.461 54.858 21.258 1.00 87.77 ? 87 GLU A C 1 ATOM 663 O O . GLU A 1 87 ? 28.430 54.705 20.519 1.00 71.82 ? 87 GLU A O 1 ATOM 664 C CB . GLU A 1 87 ? 26.491 57.128 21.662 1.00 69.92 ? 87 GLU A CB 1 ATOM 665 C CG . GLU A 1 87 ? 27.054 57.831 20.437 1.00 93.96 ? 87 GLU A CG 1 ATOM 666 C CD . GLU A 1 87 ? 26.236 59.044 20.039 1.00 87.88 ? 87 GLU A CD 1 ATOM 667 O OE1 . GLU A 1 87 ? 26.633 59.745 19.085 1.00 84.35 ? 87 GLU A OE1 1 ATOM 668 O OE2 . GLU A 1 87 ? 25.197 59.299 20.682 1.00 75.95 ? 87 GLU A OE2 1 ATOM 669 N N . PHE A 1 88 ? 26.433 54.018 21.283 1.00 101.65 ? 88 PHE A N 1 ATOM 670 C CA . PHE A 1 88 ? 26.363 52.896 20.359 1.00 73.58 ? 88 PHE A CA 1 ATOM 671 C C . PHE A 1 88 ? 25.005 52.875 19.663 1.00 69.61 ? 88 PHE A C 1 ATOM 672 O O . PHE A 1 88 ? 23.979 52.613 20.291 1.00 70.31 ? 88 PHE A O 1 ATOM 673 C CB . PHE A 1 88 ? 26.624 51.586 21.103 1.00 72.14 ? 88 PHE A CB 1 ATOM 674 C CG . PHE A 1 88 ? 27.794 51.651 22.051 1.00 73.54 ? 88 PHE A CG 1 ATOM 675 C CD1 . PHE A 1 88 ? 29.079 51.382 21.609 1.00 76.86 ? 88 PHE A CD1 1 ATOM 676 C CD2 . PHE A 1 88 ? 27.608 51.984 23.385 1.00 71.71 ? 88 PHE A CD2 1 ATOM 677 C CE1 . PHE A 1 88 ? 30.155 51.442 22.477 1.00 78.43 ? 88 PHE A CE1 1 ATOM 678 C CE2 . PHE A 1 88 ? 28.679 52.049 24.256 1.00 73.06 ? 88 PHE A CE2 1 ATOM 679 C CZ . PHE A 1 88 ? 29.955 51.776 23.800 1.00 76.56 ? 88 PHE A CZ 1 ATOM 680 N N . LYS A 1 89 ? 25.007 53.150 18.363 1.00 70.14 ? 89 LYS A N 1 ATOM 681 C CA . LYS A 1 89 ? 23.768 53.264 17.599 1.00 68.90 ? 89 LYS A CA 1 ATOM 682 C C . LYS A 1 89 ? 23.425 51.990 16.834 1.00 81.68 ? 89 LYS A C 1 ATOM 683 O O . LYS A 1 89 ? 22.391 51.918 16.170 1.00 97.68 ? 89 LYS A O 1 ATOM 684 C CB . LYS A 1 89 ? 23.854 54.443 16.629 1.00 75.72 ? 89 LYS A CB 1 ATOM 685 C CG . LYS A 1 89 ? 24.079 55.779 17.313 1.00 81.99 ? 89 LYS A CG 1 ATOM 686 C CD . LYS A 1 89 ? 24.315 56.886 16.302 1.00 87.97 ? 89 LYS A CD 1 ATOM 687 C CE . LYS A 1 89 ? 24.587 58.206 17.000 1.00 77.34 ? 89 LYS A CE 1 ATOM 688 N NZ . LYS A 1 89 ? 24.924 59.282 16.031 1.00 79.91 ? 89 LYS A NZ 1 ATOM 689 N N . SER A 1 90 ? 24.296 50.991 16.920 1.00 97.85 ? 90 SER A N 1 ATOM 690 C CA . SER A 1 90 ? 24.045 49.718 16.260 1.00 83.83 ? 90 SER A CA 1 ATOM 691 C C . SER A 1 90 ? 22.900 48.979 16.943 1.00 76.75 ? 90 SER A C 1 ATOM 692 O O . SER A 1 90 ? 22.914 48.795 18.160 1.00 75.09 ? 90 SER A O 1 ATOM 693 C CB . SER A 1 90 ? 25.307 48.855 16.250 1.00 88.57 ? 90 SER A CB 1 ATOM 694 O OG . SER A 1 90 ? 26.318 49.438 15.446 1.00 110.44 ? 90 SER A OG 1 ATOM 695 N N . HIS A 1 91 ? 21.914 48.570 16.148 1.00 78.07 ? 91 HIS A N 1 ATOM 696 C CA . HIS A 1 91 ? 20.727 47.876 16.644 1.00 76.64 ? 91 HIS A CA 1 ATOM 697 C C . HIS A 1 91 ? 19.994 48.704 17.698 1.00 73.54 ? 91 HIS A C 1 ATOM 698 O O . HIS A 1 91 ? 19.502 48.166 18.690 1.00 69.03 ? 91 HIS A O 1 ATOM 699 C CB . HIS A 1 91 ? 21.101 46.506 17.217 1.00 78.85 ? 91 HIS A CB 1 ATOM 700 C CG . HIS A 1 91 ? 21.966 45.684 16.311 1.00 84.47 ? 91 HIS A CG 1 ATOM 701 N ND1 . HIS A 1 91 ? 21.455 44.921 15.282 1.00 88.81 ? 91 HIS A ND1 1 ATOM 702 C CD2 . HIS A 1 91 ? 23.307 45.502 16.283 1.00 91.88 ? 91 HIS A CD2 1 ATOM 703 C CE1 . HIS A 1 91 ? 22.444 44.308 14.658 1.00 93.55 ? 91 HIS A CE1 1 ATOM 704 N NE2 . HIS A 1 91 ? 23.579 44.643 15.245 1.00 94.14 ? 91 HIS A NE2 1 ATOM 705 N N . GLN A 1 92 ? 19.921 50.013 17.474 1.00 89.58 ? 92 GLN A N 1 ATOM 706 C CA . GLN A 1 92 ? 19.310 50.926 18.435 1.00 85.89 ? 92 GLN A CA 1 ATOM 707 C C . GLN A 1 92 ? 17.794 50.997 18.269 1.00 62.85 ? 92 GLN A C 1 ATOM 708 O O . GLN A 1 92 ? 17.108 51.639 19.067 1.00 63.66 ? 92 GLN A O 1 ATOM 709 C CB . GLN A 1 92 ? 19.911 52.327 18.298 1.00 67.01 ? 92 GLN A CB 1 ATOM 710 C CG . GLN A 1 92 ? 19.526 53.038 17.013 1.00 63.83 ? 92 GLN A CG 1 ATOM 711 C CD . GLN A 1 92 ? 20.187 54.393 16.871 1.00 70.50 ? 92 GLN A CD 1 ATOM 712 O OE1 . GLN A 1 92 ? 20.805 54.897 17.808 1.00 89.54 ? 92 GLN A OE1 1 ATOM 713 N NE2 . GLN A 1 92 ? 20.064 54.989 15.691 1.00 80.33 ? 92 GLN A NE2 1 ATOM 714 N N . TRP A 1 93 ? 17.284 50.334 17.232 1.00 63.54 ? 93 TRP A N 1 ATOM 715 C CA . TRP A 1 93 ? 15.850 50.292 16.942 1.00 75.46 ? 93 TRP A CA 1 ATOM 716 C C . TRP A 1 93 ? 15.244 51.679 16.744 1.00 67.74 ? 93 TRP A C 1 ATOM 717 O O . TRP A 1 93 ? 14.226 52.007 17.351 1.00 76.07 ? 93 TRP A O 1 ATOM 718 C CB . TRP A 1 93 ? 15.097 49.560 18.059 1.00 77.71 ? 93 TRP A CB 1 ATOM 719 C CG . TRP A 1 93 ? 15.039 48.075 17.892 1.00 62.06 ? 93 TRP A CG 1 ATOM 720 C CD1 . TRP A 1 93 ? 16.092 47.209 17.877 1.00 80.35 ? 93 TRP A CD1 1 ATOM 721 C CD2 . TRP A 1 93 ? 13.860 47.276 17.731 1.00 61.44 ? 93 TRP A CD2 1 ATOM 722 N NE1 . TRP A 1 93 ? 15.644 45.920 17.710 1.00 78.92 ? 93 TRP A NE1 1 ATOM 723 C CE2 . TRP A 1 93 ? 14.277 45.935 17.619 1.00 67.43 ? 93 TRP A CE2 1 ATOM 724 C CE3 . TRP A 1 93 ? 12.493 47.565 17.670 1.00 59.07 ? 93 TRP A CE3 1 ATOM 725 C CZ2 . TRP A 1 93 ? 13.376 44.885 17.446 1.00 74.05 ? 93 TRP A CZ2 1 ATOM 726 C CZ3 . TRP A 1 93 ? 11.601 46.522 17.498 1.00 58.71 ? 93 TRP A CZ3 1 ATOM 727 C CH2 . TRP A 1 93 ? 12.045 45.199 17.389 1.00 66.59 ? 93 TRP A CH2 1 ATOM 728 N N . PHE A 1 94 ? 15.864 52.491 15.895 1.00 61.54 ? 94 PHE A N 1 ATOM 729 C CA . PHE A 1 94 ? 15.327 53.818 15.609 1.00 76.08 ? 94 PHE A CA 1 ATOM 730 C C . PHE A 1 94 ? 14.125 53.725 14.675 1.00 76.69 ? 94 PHE A C 1 ATOM 731 O O . PHE A 1 94 ? 14.205 53.138 13.597 1.00 78.47 ? 94 PHE A O 1 ATOM 732 C CB . PHE A 1 94 ? 16.398 54.725 15.001 1.00 85.84 ? 94 PHE A CB 1 ATOM 733 C CG . PHE A 1 94 ? 15.875 56.061 14.549 1.00 83.00 ? 94 PHE A CG 1 ATOM 734 C CD1 . PHE A 1 94 ? 15.569 57.049 15.470 1.00 81.22 ? 94 PHE A CD1 1 ATOM 735 C CD2 . PHE A 1 94 ? 15.695 56.329 13.202 1.00 82.03 ? 94 PHE A CD2 1 ATOM 736 C CE1 . PHE A 1 94 ? 15.089 58.279 15.057 1.00 72.91 ? 94 PHE A CE1 1 ATOM 737 C CE2 . PHE A 1 94 ? 15.216 57.556 12.782 1.00 74.34 ? 94 PHE A CE2 1 ATOM 738 C CZ . PHE A 1 94 ? 14.914 58.531 13.710 1.00 65.18 ? 94 PHE A CZ 1 ATOM 739 N N . GLY A 1 95 ? 13.012 54.314 15.099 1.00 76.51 ? 95 GLY A N 1 ATOM 740 C CA . GLY A 1 95 ? 11.779 54.251 14.337 1.00 78.63 ? 95 GLY A CA 1 ATOM 741 C C . GLY A 1 95 ? 10.797 53.257 14.925 1.00 80.80 ? 95 GLY A C 1 ATOM 742 O O . GLY A 1 95 ? 9.761 52.968 14.327 1.00 76.20 ? 95 GLY A O 1 ATOM 743 N N . ALA A 1 96 ? 11.124 52.731 16.101 1.00 78.19 ? 96 ALA A N 1 ATOM 744 C CA . ALA A 1 96 ? 10.240 51.798 16.790 1.00 61.85 ? 96 ALA A CA 1 ATOM 745 C C . ALA A 1 96 ? 8.965 52.505 17.243 1.00 58.83 ? 96 ALA A C 1 ATOM 746 O O . ALA A 1 96 ? 7.931 51.868 17.452 1.00 84.12 ? 96 ALA A O 1 ATOM 747 C CB . ALA A 1 96 ? 10.952 51.166 17.975 1.00 61.96 ? 96 ALA A CB 1 ATOM 748 N N . SER A 1 97 ? 9.051 53.822 17.402 1.00 69.65 ? 97 SER A N 1 ATOM 749 C CA . SER A 1 97 ? 7.889 54.647 17.713 1.00 59.42 ? 97 SER A CA 1 ATOM 750 C C . SER A 1 97 ? 7.934 55.951 16.920 1.00 55.39 ? 97 SER A C 1 ATOM 751 O O . SER A 1 97 ? 8.949 56.647 16.917 1.00 56.09 ? 97 SER A O 1 ATOM 752 C CB . SER A 1 97 ? 7.814 54.936 19.214 1.00 61.31 ? 97 SER A CB 1 ATOM 753 O OG . SER A 1 97 ? 9.015 55.522 19.682 1.00 79.12 ? 97 SER A OG 1 ATOM 754 N N . VAL A 1 98 ? 6.840 56.269 16.235 1.00 56.39 ? 98 VAL A N 1 ATOM 755 C CA . VAL A 1 98 ? 6.763 57.483 15.426 1.00 58.49 ? 98 VAL A CA 1 ATOM 756 C C . VAL A 1 98 ? 5.451 58.233 15.648 1.00 81.82 ? 98 VAL A C 1 ATOM 757 O O . VAL A 1 98 ? 4.370 57.672 15.476 1.00 94.95 ? 98 VAL A O 1 ATOM 758 C CB . VAL A 1 98 ? 6.906 57.171 13.922 1.00 80.30 ? 98 VAL A CB 1 ATOM 759 C CG1 . VAL A 1 98 ? 6.632 58.413 13.089 1.00 89.00 ? 98 VAL A CG1 1 ATOM 760 C CG2 . VAL A 1 98 ? 8.288 56.618 13.617 1.00 112.75 ? 98 VAL A CG2 1 ATOM 761 N N . ARG A 1 99 ? 5.556 59.503 16.027 1.00 60.28 ? 99 ARG A N 1 ATOM 762 C CA . ARG A 1 99 ? 4.386 60.356 16.210 1.00 60.44 ? 99 ARG A CA 1 ATOM 763 C C . ARG A 1 99 ? 4.560 61.685 15.484 1.00 80.04 ? 99 ARG A C 1 ATOM 764 O O . ARG A 1 99 ? 5.650 62.257 15.469 1.00 114.30 ? 99 ARG A O 1 ATOM 765 C CB . ARG A 1 99 ? 4.121 60.600 17.697 1.00 67.04 ? 99 ARG A CB 1 ATOM 766 C CG . ARG A 1 99 ? 3.343 59.489 18.380 1.00 76.77 ? 99 ARG A CG 1 ATOM 767 C CD . ARG A 1 99 ? 1.927 59.396 17.836 1.00 83.50 ? 99 ARG A CD 1 ATOM 768 N NE . ARG A 1 99 ? 1.659 58.108 17.204 1.00 106.46 ? 99 ARG A NE 1 ATOM 769 C CZ . ARG A 1 99 ? 1.146 57.057 17.834 1.00 122.77 ? 99 ARG A CZ 1 ATOM 770 N NH1 . ARG A 1 99 ? 0.842 57.137 19.122 1.00 120.32 ? 99 ARG A NH1 1 ATOM 771 N NH2 . ARG A 1 99 ? 0.935 55.925 17.177 1.00 121.92 ? 99 ARG A NH2 1 ATOM 772 N N . SER A 1 100 ? 3.479 62.172 14.882 1.00 70.77 ? 100 SER A N 1 ATOM 773 C CA . SER A 1 100 ? 3.527 63.414 14.121 1.00 76.67 ? 100 SER A CA 1 ATOM 774 C C . SER A 1 100 ? 2.353 64.334 14.437 1.00 80.72 ? 100 SER A C 1 ATOM 775 O O . SER A 1 100 ? 1.195 63.973 14.231 1.00 113.80 ? 100 SER A O 1 ATOM 776 C CB . SER A 1 100 ? 3.556 63.116 12.621 1.00 91.84 ? 100 SER A CB 1 ATOM 777 O OG . SER A 1 100 ? 3.463 64.310 11.863 1.00 105.32 ? 100 SER A OG 1 ATOM 778 N N . LYS A 1 101 ? 2.662 65.526 14.937 1.00 70.41 ? 101 LYS A N 1 ATOM 779 C CA . LYS A 1 101 ? 1.655 66.561 15.117 1.00 85.18 ? 101 LYS A CA 1 ATOM 780 C C . LYS A 1 101 ? 1.964 67.739 14.203 1.00 87.45 ? 101 LYS A C 1 ATOM 781 O O . LYS A 1 101 ? 3.010 68.375 14.337 1.00 77.17 ? 101 LYS A O 1 ATOM 782 C CB . LYS A 1 101 ? 1.585 67.024 16.572 1.00 101.42 ? 101 LYS A CB 1 ATOM 783 C CG . LYS A 1 101 ? 0.674 68.224 16.776 1.00 111.49 ? 101 LYS A CG 1 ATOM 784 C CD . LYS A 1 101 ? 0.524 68.583 18.242 1.00 96.75 ? 101 LYS A CD 1 ATOM 785 C CE . LYS A 1 101 ? -0.369 69.801 18.408 1.00 109.31 ? 101 LYS A CE 1 ATOM 786 N NZ . LYS A 1 101 ? -1.705 69.602 17.780 1.00 120.83 ? 101 LYS A NZ 1 ATOM 787 N N . GLN A 1 102 ? 1.048 68.016 13.278 1.00 88.68 ? 102 GLN A N 1 ATOM 788 C CA . GLN A 1 102 ? 1.223 69.077 12.289 1.00 84.30 ? 102 GLN A CA 1 ATOM 789 C C . GLN A 1 102 ? 2.524 68.899 11.505 1.00 82.59 ? 102 GLN A C 1 ATOM 790 O O . GLN A 1 102 ? 2.706 67.898 10.812 1.00 133.04 ? 102 GLN A O 1 ATOM 791 C CB . GLN A 1 102 ? 1.182 70.452 12.962 1.00 84.24 ? 102 GLN A CB 1 ATOM 792 C CG . GLN A 1 102 ? -0.175 70.804 13.556 1.00 98.38 ? 102 GLN A CG 1 ATOM 793 C CD . GLN A 1 102 ? -0.184 72.152 14.251 1.00 137.28 ? 102 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 102 ? 0.784 72.532 14.909 1.00 145.65 ? 102 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 102 ? -1.282 72.886 14.103 1.00 144.55 ? 102 GLN A NE2 1 ATOM 796 N N . ASP A 1 103 ? 3.421 69.872 11.617 1.00 90.76 ? 103 ASP A N 1 ATOM 797 C CA . ASP A 1 103 ? 4.681 69.843 10.880 1.00 97.73 ? 103 ASP A CA 1 ATOM 798 C C . ASP A 1 103 ? 5.810 69.220 11.704 1.00 97.00 ? 103 ASP A C 1 ATOM 799 O O . ASP A 1 103 ? 6.951 69.146 11.249 1.00 82.98 ? 103 ASP A O 1 ATOM 800 C CB . ASP A 1 103 ? 5.068 71.258 10.443 1.00 89.97 ? 103 ASP A CB 1 ATOM 801 C CG . ASP A 1 103 ? 5.667 71.298 9.049 1.00 115.55 ? 103 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 103 ? 6.518 70.439 8.734 1.00 129.71 ? 103 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 103 ? 5.278 72.188 8.263 1.00 112.69 ? 103 ASP A OD2 1 ATOM 804 N N . LYS A 1 104 ? 5.486 68.773 12.914 1.00 93.17 ? 104 LYS A N 1 ATOM 805 C CA . LYS A 1 104 ? 6.480 68.180 13.804 1.00 76.63 ? 104 LYS A CA 1 ATOM 806 C C . LYS A 1 104 ? 6.525 66.660 13.660 1.00 111.23 ? 104 LYS A C 1 ATOM 807 O O . LYS A 1 104 ? 5.488 66.011 13.528 1.00 122.63 ? 104 LYS A O 1 ATOM 808 C CB . LYS A 1 104 ? 6.187 68.555 15.260 1.00 80.48 ? 104 LYS A CB 1 ATOM 809 C CG . LYS A 1 104 ? 6.180 70.051 15.547 1.00 80.92 ? 104 LYS A CG 1 ATOM 810 C CD . LYS A 1 104 ? 7.586 70.625 15.546 1.00 99.57 ? 104 LYS A CD 1 ATOM 811 C CE . LYS A 1 104 ? 7.593 72.086 15.973 1.00 114.76 ? 104 LYS A CE 1 ATOM 812 N NZ . LYS A 1 104 ? 6.775 72.941 15.069 1.00 134.10 ? 104 LYS A NZ 1 ATOM 813 N N . ILE A 1 105 ? 7.730 66.098 13.684 1.00 95.96 ? 105 ILE A N 1 ATOM 814 C CA . ILE A 1 105 ? 7.906 64.648 13.625 1.00 70.36 ? 105 ILE A CA 1 ATOM 815 C C . ILE A 1 105 ? 8.818 64.162 14.750 1.00 79.77 ? 105 ILE A C 1 ATOM 816 O O . ILE A 1 105 ? 9.931 64.662 14.917 1.00 99.97 ? 105 ILE A O 1 ATOM 817 C CB . ILE A 1 105 ? 8.490 64.197 12.269 1.00 72.01 ? 105 ILE A CB 1 ATOM 818 C CG1 . ILE A 1 105 ? 7.527 64.534 11.130 1.00 74.52 ? 105 ILE A CG1 1 ATOM 819 C CG2 . ILE A 1 105 ? 8.781 62.704 12.282 1.00 69.81 ? 105 ILE A CG2 1 ATOM 820 C CD1 . ILE A 1 105 ? 8.005 64.065 9.773 1.00 76.53 ? 105 ILE A CD1 1 ATOM 821 N N . LEU A 1 106 ? 8.340 63.186 15.517 1.00 65.66 ? 106 LEU A N 1 ATOM 822 C CA . LEU A 1 106 ? 9.105 62.641 16.634 1.00 78.57 ? 106 LEU A CA 1 ATOM 823 C C . LEU A 1 106 ? 9.356 61.143 16.467 1.00 74.16 ? 106 LEU A C 1 ATOM 824 O O . LEU A 1 106 ? 8.415 60.351 16.405 1.00 81.13 ? 106 LEU A O 1 ATOM 825 C CB . LEU A 1 106 ? 8.379 62.903 17.954 1.00 71.27 ? 106 LEU A CB 1 ATOM 826 C CG . LEU A 1 106 ? 9.107 62.480 19.231 1.00 72.21 ? 106 LEU A CG 1 ATOM 827 C CD1 . LEU A 1 106 ? 10.406 63.256 19.387 1.00 80.03 ? 106 LEU A CD1 1 ATOM 828 C CD2 . LEU A 1 106 ? 8.211 62.671 20.444 1.00 65.29 ? 106 LEU A CD2 1 ATOM 829 N N . ALA A 1 107 ? 10.629 60.763 16.395 1.00 66.55 ? 107 ALA A N 1 ATOM 830 C CA . ALA A 1 107 ? 11.009 59.363 16.232 1.00 75.22 ? 107 ALA A CA 1 ATOM 831 C C . ALA A 1 107 ? 12.072 58.975 17.254 1.00 58.65 ? 107 ALA A C 1 ATOM 832 O O . ALA A 1 107 ? 12.998 59.742 17.514 1.00 61.20 ? 107 ALA A O 1 ATOM 833 C CB . ALA A 1 107 ? 11.512 59.110 14.823 1.00 92.63 ? 107 ALA A CB 1 ATOM 834 N N . CYS A 1 108 ? 11.946 57.778 17.820 1.00 71.34 ? 108 CYS A N 1 ATOM 835 C CA . CYS A 1 108 ? 12.809 57.367 18.925 1.00 58.91 ? 108 CYS A CA 1 ATOM 836 C C . CYS A 1 108 ? 13.571 56.067 18.668 1.00 77.55 ? 108 CYS A C 1 ATOM 837 O O . CYS A 1 108 ? 13.179 55.254 17.831 1.00 77.90 ? 108 CYS A O 1 ATOM 838 C CB . CYS A 1 108 ? 11.978 57.223 20.200 1.00 53.68 ? 108 CYS A CB 1 ATOM 839 S SG . CYS A 1 108 ? 11.062 58.710 20.660 1.00 91.04 ? 108 CYS A SG 1 ATOM 840 N N . ALA A 1 109 ? 14.663 55.887 19.406 1.00 83.32 ? 109 ALA A N 1 ATOM 841 C CA . ALA A 1 109 ? 15.464 54.668 19.346 1.00 66.23 ? 109 ALA A CA 1 ATOM 842 C C . ALA A 1 109 ? 15.657 54.102 20.751 1.00 59.45 ? 109 ALA A C 1 ATOM 843 O O . ALA A 1 109 ? 16.643 54.412 21.422 1.00 66.89 ? 109 ALA A O 1 ATOM 844 C CB . ALA A 1 109 ? 16.808 54.941 18.692 1.00 56.64 ? 109 ALA A CB 1 ATOM 845 N N . PRO A 1 110 ? 14.708 53.266 21.201 1.00 59.82 ? 110 PRO A N 1 ATOM 846 C CA . PRO A 1 110 ? 14.665 52.757 22.577 1.00 50.45 ? 110 PRO A CA 1 ATOM 847 C C . PRO A 1 110 ? 15.862 51.887 22.966 1.00 53.93 ? 110 PRO A C 1 ATOM 848 O O . PRO A 1 110 ? 16.139 51.753 24.157 1.00 77.73 ? 110 PRO A O 1 ATOM 849 C CB . PRO A 1 110 ? 13.373 51.928 22.601 1.00 49.51 ? 110 PRO A CB 1 ATOM 850 C CG . PRO A 1 110 ? 12.557 52.448 21.466 1.00 56.30 ? 110 PRO A CG 1 ATOM 851 C CD . PRO A 1 110 ? 13.553 52.807 20.412 1.00 54.26 ? 110 PRO A CD 1 ATOM 852 N N . LEU A 1 111 ? 16.550 51.300 21.991 1.00 57.71 ? 111 LEU A N 1 ATOM 853 C CA . LEU A 1 111 ? 17.676 50.416 22.290 1.00 65.48 ? 111 LEU A CA 1 ATOM 854 C C . LEU A 1 111 ? 19.034 51.122 22.225 1.00 58.21 ? 111 LEU A C 1 ATOM 855 O O . LEU A 1 111 ? 20.077 50.481 22.341 1.00 62.02 ? 111 LEU A O 1 ATOM 856 C CB . LEU A 1 111 ? 17.664 49.205 21.356 1.00 81.21 ? 111 LEU A CB 1 ATOM 857 C CG . LEU A 1 111 ? 17.161 47.927 22.040 1.00 71.27 ? 111 LEU A CG 1 ATOM 858 C CD1 . LEU A 1 111 ? 15.779 48.140 22.632 1.00 54.69 ? 111 LEU A CD1 1 ATOM 859 C CD2 . LEU A 1 111 ? 17.156 46.745 21.085 1.00 91.73 ? 111 LEU A CD2 1 ATOM 860 N N . TYR A 1 112 ? 19.013 52.436 22.025 1.00 56.79 ? 112 TYR A N 1 ATOM 861 C CA . TYR A 1 112 ? 20.225 53.258 22.020 1.00 60.28 ? 112 TYR A CA 1 ATOM 862 C C . TYR A 1 112 ? 21.009 53.134 23.333 1.00 67.39 ? 112 TYR A C 1 ATOM 863 O O . TYR A 1 112 ? 20.423 53.169 24.412 1.00 57.26 ? 112 TYR A O 1 ATOM 864 C CB . TYR A 1 112 ? 19.841 54.715 21.749 1.00 58.85 ? 112 TYR A CB 1 ATOM 865 C CG . TYR A 1 112 ? 20.925 55.743 21.985 1.00 60.14 ? 112 TYR A CG 1 ATOM 866 C CD1 . TYR A 1 112 ? 21.867 56.028 21.007 1.00 59.30 ? 112 TYR A CD1 1 ATOM 867 C CD2 . TYR A 1 112 ? 20.978 56.458 23.175 1.00 60.79 ? 112 TYR A CD2 1 ATOM 868 C CE1 . TYR A 1 112 ? 22.848 56.981 21.216 1.00 67.60 ? 112 TYR A CE1 1 ATOM 869 C CE2 . TYR A 1 112 ? 21.955 57.410 23.393 1.00 67.97 ? 112 TYR A CE2 1 ATOM 870 C CZ . TYR A 1 112 ? 22.887 57.669 22.412 1.00 60.01 ? 112 TYR A CZ 1 ATOM 871 O OH . TYR A 1 112 ? 23.857 58.618 22.631 1.00 61.68 ? 112 TYR A OH 1 ATOM 872 N N . HIS A 1 113 ? 22.333 53.010 23.234 1.00 75.61 ? 113 HIS A N 1 ATOM 873 C CA . HIS A 1 113 ? 23.190 52.746 24.397 1.00 94.99 ? 113 HIS A CA 1 ATOM 874 C C . HIS A 1 113 ? 24.199 53.871 24.652 1.00 94.20 ? 113 HIS A C 1 ATOM 875 O O . HIS A 1 113 ? 24.474 54.674 23.761 1.00 85.14 ? 113 HIS A O 1 ATOM 876 C CB . HIS A 1 113 ? 23.931 51.416 24.223 1.00 99.83 ? 113 HIS A CB 1 ATOM 877 C CG . HIS A 1 113 ? 23.054 50.210 24.365 1.00 92.80 ? 113 HIS A CG 1 ATOM 878 N ND1 . HIS A 1 113 ? 22.547 49.798 25.579 1.00 77.00 ? 113 HIS A ND1 1 ATOM 879 C CD2 . HIS A 1 113 ? 22.602 49.323 23.448 1.00 98.07 ? 113 HIS A CD2 1 ATOM 880 C CE1 . HIS A 1 113 ? 21.816 48.712 25.402 1.00 69.72 ? 113 HIS A CE1 1 ATOM 881 N NE2 . HIS A 1 113 ? 21.832 48.403 24.119 1.00 89.62 ? 113 HIS A NE2 1 ATOM 882 N N . TRP A 1 114 ? 24.747 53.927 25.868 1.00 77.96 ? 114 TRP A N 1 ATOM 883 C CA . TRP A 1 114 ? 25.534 55.091 26.286 1.00 77.21 ? 114 TRP A CA 1 ATOM 884 C C . TRP A 1 114 ? 27.002 54.827 26.688 1.00 84.97 ? 114 TRP A C 1 ATOM 885 O O . TRP A 1 114 ? 27.888 55.078 25.880 1.00 104.36 ? 114 TRP A O 1 ATOM 886 C CB . TRP A 1 114 ? 24.817 55.788 27.443 1.00 63.28 ? 114 TRP A CB 1 ATOM 887 C CG . TRP A 1 114 ? 25.214 57.218 27.610 1.00 68.32 ? 114 TRP A CG 1 ATOM 888 C CD1 . TRP A 1 114 ? 26.045 57.938 26.801 1.00 100.41 ? 114 TRP A CD1 1 ATOM 889 C CD2 . TRP A 1 114 ? 24.797 58.109 28.650 1.00 74.69 ? 114 TRP A CD2 1 ATOM 890 N NE1 . TRP A 1 114 ? 26.175 59.220 27.277 1.00 96.74 ? 114 TRP A NE1 1 ATOM 891 C CE2 . TRP A 1 114 ? 25.420 59.351 28.411 1.00 94.91 ? 114 TRP A CE2 1 ATOM 892 C CE3 . TRP A 1 114 ? 23.966 57.974 29.766 1.00 86.05 ? 114 TRP A CE3 1 ATOM 893 C CZ2 . TRP A 1 114 ? 25.236 60.451 29.246 1.00 113.21 ? 114 TRP A CZ2 1 ATOM 894 C CZ3 . TRP A 1 114 ? 23.783 59.066 30.589 1.00 122.86 ? 114 TRP A CZ3 1 ATOM 895 C CH2 . TRP A 1 114 ? 24.415 60.289 30.326 1.00 121.44 ? 114 TRP A CH2 1 ATOM 896 N N . ARG A 1 115 ? 27.214 54.250 27.882 1.00 77.40 ? 115 ARG A N 1 ATOM 897 C CA . ARG A 1 115 ? 28.472 54.228 28.691 1.00 90.37 ? 115 ARG A CA 1 ATOM 898 C C . ARG A 1 115 ? 28.565 55.413 29.658 1.00 78.63 ? 115 ARG A C 1 ATOM 899 O O . ARG A 1 115 ? 29.439 55.453 30.524 1.00 88.02 ? 115 ARG A O 1 ATOM 900 C CB . ARG A 1 115 ? 29.758 54.184 27.826 1.00 82.00 ? 115 ARG A CB 1 ATOM 901 C CG . ARG A 1 115 ? 30.374 55.538 27.409 1.00 72.57 ? 115 ARG A CG 1 ATOM 902 C CD . ARG A 1 115 ? 31.472 56.050 28.349 1.00 86.73 ? 115 ARG A CD 1 ATOM 903 N NE . ARG A 1 115 ? 32.742 55.339 28.243 1.00 88.03 ? 115 ARG A NE 1 ATOM 904 C CZ . ARG A 1 115 ? 33.798 55.599 29.009 1.00 79.75 ? 115 ARG A CZ 1 ATOM 905 N NH1 . ARG A 1 115 ? 33.731 56.548 29.933 1.00 77.04 ? 115 ARG A NH1 1 ATOM 906 N NH2 . ARG A 1 115 ? 34.923 54.914 28.854 1.00 85.25 ? 115 ARG A NH2 1 ATOM 907 N N . THR A 1 116 ? 27.628 56.343 29.528 1.00 67.96 ? 116 THR A N 1 ATOM 908 C CA . THR A 1 116 ? 27.591 57.596 30.288 1.00 103.80 ? 116 THR A CA 1 ATOM 909 C C . THR A 1 116 ? 28.881 58.413 30.181 1.00 105.68 ? 116 THR A C 1 ATOM 910 O O . THR A 1 116 ? 29.550 58.387 29.150 1.00 127.23 ? 116 THR A O 1 ATOM 911 C CB . THR A 1 116 ? 27.300 57.331 31.784 1.00 96.25 ? 116 THR A CB 1 ATOM 912 O OG1 . THR A 1 116 ? 28.470 56.800 32.419 1.00 78.38 ? 116 THR A OG1 1 ATOM 913 C CG2 . THR A 1 116 ? 26.153 56.343 31.940 1.00 84.26 ? 116 THR A CG2 1 ATOM 914 N N . GLU A 1 117 ? 29.212 59.159 31.232 1.00 70.87 ? 117 GLU A N 1 ATOM 915 C CA . GLU A 1 117 ? 30.482 59.881 31.288 1.00 75.97 ? 117 GLU A CA 1 ATOM 916 C C . GLU A 1 117 ? 31.511 59.329 32.278 1.00 99.91 ? 117 GLU A C 1 ATOM 917 O O . GLU A 1 117 ? 32.641 59.817 32.333 1.00 105.75 ? 117 GLU A O 1 ATOM 918 C CB . GLU A 1 117 ? 30.224 61.356 31.595 1.00 91.71 ? 117 GLU A CB 1 ATOM 919 C CG . GLU A 1 117 ? 30.656 62.284 30.471 1.00 80.97 ? 117 GLU A CG 1 ATOM 920 C CD . GLU A 1 117 ? 29.530 63.158 29.964 1.00 99.90 ? 117 GLU A CD 1 ATOM 921 O OE1 . GLU A 1 117 ? 28.404 63.050 30.494 1.00 105.79 ? 117 GLU A OE1 1 ATOM 922 O OE2 . GLU A 1 117 ? 29.772 63.959 29.036 1.00 106.62 ? 117 GLU A OE2 1 ATOM 923 N N . MET A 1 118 ? 31.130 58.322 33.055 1.00 110.00 ? 118 MET A N 1 ATOM 924 C CA . MET A 1 118 ? 31.910 57.967 34.239 1.00 94.31 ? 118 MET A CA 1 ATOM 925 C C . MET A 1 118 ? 32.667 56.654 34.083 1.00 96.46 ? 118 MET A C 1 ATOM 926 O O . MET A 1 118 ? 33.885 56.648 33.903 1.00 100.26 ? 118 MET A O 1 ATOM 927 C CB . MET A 1 118 ? 30.988 57.900 35.459 1.00 77.49 ? 118 MET A CB 1 ATOM 928 C CG . MET A 1 118 ? 30.019 59.072 35.539 1.00 75.43 ? 118 MET A CG 1 ATOM 929 S SD . MET A 1 118 ? 28.860 58.984 36.916 1.00 141.29 ? 118 MET A SD 1 ATOM 930 C CE . MET A 1 118 ? 27.775 60.356 36.526 1.00 72.75 ? 118 MET A CE 1 ATOM 931 N N . LYS A 1 119 ? 31.943 55.544 34.155 1.00 81.17 ? 119 LYS A N 1 ATOM 932 C CA . LYS A 1 119 ? 32.540 54.238 33.930 1.00 81.30 ? 119 LYS A CA 1 ATOM 933 C C . LYS A 1 119 ? 32.424 53.897 32.453 1.00 90.72 ? 119 LYS A C 1 ATOM 934 O O . LYS A 1 119 ? 31.872 54.674 31.677 1.00 114.81 ? 119 LYS A O 1 ATOM 935 C CB . LYS A 1 119 ? 31.854 53.171 34.784 1.00 83.67 ? 119 LYS A CB 1 ATOM 936 C CG . LYS A 1 119 ? 31.765 53.521 36.259 1.00 99.23 ? 119 LYS A CG 1 ATOM 937 C CD . LYS A 1 119 ? 30.858 52.550 37.001 1.00 123.46 ? 119 LYS A CD 1 ATOM 938 C CE . LYS A 1 119 ? 29.443 52.578 36.440 1.00 110.76 ? 119 LYS A CE 1 ATOM 939 N NZ . LYS A 1 119 ? 28.540 51.631 37.154 1.00 84.80 ? 119 LYS A NZ 1 ATOM 940 N N . GLN A 1 120 ? 32.946 52.742 32.059 1.00 82.15 ? 120 GLN A N 1 ATOM 941 C CA . GLN A 1 120 ? 32.723 52.256 30.705 1.00 82.33 ? 120 GLN A CA 1 ATOM 942 C C . GLN A 1 120 ? 31.578 51.254 30.721 1.00 99.04 ? 120 GLN A C 1 ATOM 943 O O . GLN A 1 120 ? 31.701 50.164 31.279 1.00 113.45 ? 120 GLN A O 1 ATOM 944 C CB . GLN A 1 120 ? 33.987 51.626 30.123 1.00 85.50 ? 120 GLN A CB 1 ATOM 945 C CG . GLN A 1 120 ? 33.790 51.054 28.728 1.00 100.03 ? 120 GLN A CG 1 ATOM 946 C CD . GLN A 1 120 ? 35.094 50.656 28.067 1.00 129.31 ? 120 GLN A CD 1 ATOM 947 O OE1 . GLN A 1 120 ? 36.150 51.214 28.365 1.00 124.92 ? 120 GLN A OE1 1 ATOM 948 N NE2 . GLN A 1 120 ? 35.026 49.686 27.162 1.00 131.66 ? 120 GLN A NE2 1 ATOM 949 N N . GLU A 1 121 ? 30.461 51.635 30.111 1.00 90.62 ? 121 GLU A N 1 ATOM 950 C CA . GLU A 1 121 ? 29.249 50.827 30.158 1.00 89.94 ? 121 GLU A CA 1 ATOM 951 C C . GLU A 1 121 ? 28.584 50.719 28.792 1.00 90.89 ? 121 GLU A C 1 ATOM 952 O O . GLU A 1 121 ? 29.087 51.244 27.803 1.00 113.39 ? 121 GLU A O 1 ATOM 953 C CB . GLU A 1 121 ? 28.254 51.422 31.162 1.00 91.20 ? 121 GLU A CB 1 ATOM 954 C CG . GLU A 1 121 ? 28.781 51.563 32.583 1.00 108.86 ? 121 GLU A CG 1 ATOM 955 C CD . GLU A 1 121 ? 28.546 50.323 33.421 1.00 136.78 ? 121 GLU A CD 1 ATOM 956 O OE1 . GLU A 1 121 ? 27.516 49.647 33.213 1.00 136.86 ? 121 GLU A OE1 1 ATOM 957 O OE2 . GLU A 1 121 ? 29.392 50.026 34.292 1.00 138.92 ? 121 GLU A OE2 1 ATOM 958 N N . ARG A 1 122 ? 27.477 49.988 28.734 1.00 73.98 ? 122 ARG A N 1 ATOM 959 C CA . ARG A 1 122 ? 26.491 50.196 27.684 1.00 71.34 ? 122 ARG A CA 1 ATOM 960 C C . ARG A 1 122 ? 25.124 50.229 28.351 1.00 76.21 ? 122 ARG A C 1 ATOM 961 O O . ARG A 1 122 ? 24.640 49.208 28.837 1.00 110.72 ? 122 ARG A O 1 ATOM 962 C CB . ARG A 1 122 ? 26.562 49.095 26.621 1.00 72.85 ? 122 ARG A CB 1 ATOM 963 C CG . ARG A 1 122 ? 27.878 49.046 25.855 1.00 75.94 ? 122 ARG A CG 1 ATOM 964 C CD . ARG A 1 122 ? 27.934 47.854 24.912 1.00 79.07 ? 122 ARG A CD 1 ATOM 965 N NE . ARG A 1 122 ? 26.982 47.971 23.811 1.00 95.46 ? 122 ARG A NE 1 ATOM 966 C CZ . ARG A 1 122 ? 27.326 48.139 22.538 1.00 88.19 ? 122 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 122 ? 28.607 48.203 22.201 1.00 81.71 ? 122 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 122 ? 26.391 48.235 21.602 1.00 87.77 ? 122 ARG A NH2 1 ATOM 969 N N . GLU A 1 123 ? 24.504 51.404 28.374 1.00 70.29 ? 123 GLU A N 1 ATOM 970 C CA . GLU A 1 123 ? 23.220 51.567 29.045 1.00 81.98 ? 123 GLU A CA 1 ATOM 971 C C . GLU A 1 123 ? 22.119 52.044 28.104 1.00 80.41 ? 123 GLU A C 1 ATOM 972 O O . GLU A 1 123 ? 22.194 53.146 27.557 1.00 78.83 ? 123 GLU A O 1 ATOM 973 C CB . GLU A 1 123 ? 23.365 52.519 30.232 1.00 84.64 ? 123 GLU A CB 1 ATOM 974 C CG . GLU A 1 123 ? 24.289 51.967 31.307 1.00 87.27 ? 123 GLU A CG 1 ATOM 975 C CD . GLU A 1 123 ? 24.229 52.741 32.605 1.00 93.18 ? 123 GLU A CD 1 ATOM 976 O OE1 . GLU A 1 123 ? 24.924 52.338 33.559 1.00 71.10 ? 123 GLU A OE1 1 ATOM 977 O OE2 . GLU A 1 123 ? 23.492 53.747 32.673 1.00 114.43 ? 123 GLU A OE2 1 ATOM 978 N N . PRO A 1 124 ? 21.087 51.210 27.917 1.00 66.23 ? 124 PRO A N 1 ATOM 979 C CA . PRO A 1 124 ? 19.952 51.541 27.051 1.00 70.43 ? 124 PRO A CA 1 ATOM 980 C C . PRO A 1 124 ? 19.091 52.664 27.620 1.00 75.46 ? 124 PRO A C 1 ATOM 981 O O . PRO A 1 124 ? 17.997 52.404 28.120 1.00 58.71 ? 124 PRO A O 1 ATOM 982 C CB . PRO A 1 124 ? 19.166 50.229 26.988 1.00 72.83 ? 124 PRO A CB 1 ATOM 983 C CG . PRO A 1 124 ? 19.514 49.525 28.250 1.00 75.12 ? 124 PRO A CG 1 ATOM 984 C CD . PRO A 1 124 ? 20.943 49.881 28.534 1.00 71.53 ? 124 PRO A CD 1 ATOM 985 N N . VAL A 1 125 ? 19.589 53.895 27.551 1.00 59.47 ? 125 VAL A N 1 ATOM 986 C CA . VAL A 1 125 ? 18.814 55.051 27.985 1.00 54.01 ? 125 VAL A CA 1 ATOM 987 C C . VAL A 1 125 ? 17.732 55.366 26.959 1.00 54.82 ? 125 VAL A C 1 ATOM 988 O O . VAL A 1 125 ? 16.656 55.855 27.304 1.00 51.45 ? 125 VAL A O 1 ATOM 989 C CB . VAL A 1 125 ? 19.699 56.303 28.192 1.00 55.20 ? 125 VAL A CB 1 ATOM 990 C CG1 . VAL A 1 125 ? 20.556 56.161 29.437 1.00 57.08 ? 125 VAL A CG1 1 ATOM 991 C CG2 . VAL A 1 125 ? 20.566 56.562 26.966 1.00 76.38 ? 125 VAL A CG2 1 ATOM 992 N N . GLY A 1 126 ? 18.029 55.079 25.696 1.00 64.47 ? 126 GLY A N 1 ATOM 993 C CA . GLY A 1 126 ? 17.135 55.415 24.606 1.00 63.70 ? 126 GLY A CA 1 ATOM 994 C C . GLY A 1 126 ? 17.323 56.864 24.203 1.00 69.15 ? 126 GLY A C 1 ATOM 995 O O . GLY A 1 126 ? 17.769 57.684 25.004 1.00 69.35 ? 126 GLY A O 1 ATOM 996 N N . THR A 1 127 ? 16.987 57.182 22.959 1.00 66.11 ? 127 THR A N 1 ATOM 997 C CA . THR A 1 127 ? 17.062 58.558 22.487 1.00 55.54 ? 127 THR A CA 1 ATOM 998 C C . THR A 1 127 ? 16.026 58.794 21.399 1.00 55.99 ? 127 THR A C 1 ATOM 999 O O . THR A 1 127 ? 15.610 57.861 20.711 1.00 78.28 ? 127 THR A O 1 ATOM 1000 C CB . THR A 1 127 ? 18.466 58.907 21.946 1.00 75.52 ? 127 THR A CB 1 ATOM 1001 O OG1 . THR A 1 127 ? 18.535 60.307 21.651 1.00 83.65 ? 127 THR A OG1 1 ATOM 1002 C CG2 . THR A 1 127 ? 18.772 58.114 20.685 1.00 74.52 ? 127 THR A CG2 1 ATOM 1003 N N . CYS A 1 128 ? 15.597 60.042 21.252 1.00 61.65 ? 128 CYS A N 1 ATOM 1004 C CA . CYS A 1 128 ? 14.672 60.386 20.186 1.00 58.01 ? 128 CYS A CA 1 ATOM 1005 C C . CYS A 1 128 ? 15.224 61.519 19.336 1.00 82.57 ? 128 CYS A C 1 ATOM 1006 O O . CYS A 1 128 ? 16.282 62.076 19.631 1.00 81.35 ? 128 CYS A O 1 ATOM 1007 C CB . CYS A 1 128 ? 13.309 60.774 20.759 1.00 57.28 ? 128 CYS A CB 1 ATOM 1008 S SG . CYS A 1 128 ? 12.554 59.501 21.788 1.00 122.70 ? 128 CYS A SG 1 ATOM 1009 N N . PHE A 1 129 ? 14.498 61.852 18.276 1.00 72.88 ? 129 PHE A N 1 ATOM 1010 C CA . PHE A 1 129 ? 14.869 62.958 17.408 1.00 64.55 ? 129 PHE A CA 1 ATOM 1011 C C . PHE A 1 129 ? 13.637 63.752 16.994 1.00 79.52 ? 129 PHE A C 1 ATOM 1012 O O . PHE A 1 129 ? 12.694 63.198 16.428 1.00 85.68 ? 129 PHE A O 1 ATOM 1013 C CB . PHE A 1 129 ? 15.612 62.447 16.172 1.00 65.97 ? 129 PHE A CB 1 ATOM 1014 C CG . PHE A 1 129 ? 17.025 62.015 16.449 1.00 86.52 ? 129 PHE A CG 1 ATOM 1015 C CD1 . PHE A 1 129 ? 17.304 60.720 16.855 1.00 81.92 ? 129 PHE A CD1 1 ATOM 1016 C CD2 . PHE A 1 129 ? 18.074 62.905 16.301 1.00 68.13 ? 129 PHE A CD2 1 ATOM 1017 C CE1 . PHE A 1 129 ? 18.603 60.324 17.110 1.00 93.68 ? 129 PHE A CE1 1 ATOM 1018 C CE2 . PHE A 1 129 ? 19.375 62.514 16.554 1.00 68.32 ? 129 PHE A CE2 1 ATOM 1019 C CZ . PHE A 1 129 ? 19.640 61.221 16.960 1.00 98.16 ? 129 PHE A CZ 1 ATOM 1020 N N . LEU A 1 130 ? 13.648 65.049 17.278 1.00 88.02 ? 130 LEU A N 1 ATOM 1021 C CA . LEU A 1 130 ? 12.562 65.925 16.860 1.00 69.81 ? 130 LEU A CA 1 ATOM 1022 C C . LEU A 1 130 ? 13.040 66.779 15.693 1.00 90.85 ? 130 LEU A C 1 ATOM 1023 O O . LEU A 1 130 ? 14.043 67.484 15.795 1.00 118.56 ? 130 LEU A O 1 ATOM 1024 C CB . LEU A 1 130 ? 12.086 66.804 18.022 1.00 68.98 ? 130 LEU A CB 1 ATOM 1025 C CG . LEU A 1 130 ? 10.633 67.297 18.016 1.00 69.58 ? 130 LEU A CG 1 ATOM 1026 C CD1 . LEU A 1 130 ? 10.256 67.861 19.377 1.00 95.37 ? 130 LEU A CD1 1 ATOM 1027 C CD2 . LEU A 1 130 ? 10.389 68.337 16.932 1.00 102.42 ? 130 LEU A CD2 1 ATOM 1028 N N . GLN A 1 131 ? 12.317 66.705 14.582 1.00 85.72 ? 131 GLN A N 1 ATOM 1029 C CA . GLN A 1 131 ? 12.675 67.447 13.380 1.00 99.80 ? 131 GLN A CA 1 ATOM 1030 C C . GLN A 1 131 ? 11.490 68.242 12.856 1.00 94.76 ? 131 GLN A C 1 ATOM 1031 O O . GLN A 1 131 ? 10.453 67.664 12.529 1.00 85.99 ? 131 GLN A O 1 ATOM 1032 C CB . GLN A 1 131 ? 13.183 66.494 12.294 1.00 96.75 ? 131 GLN A CB 1 ATOM 1033 C CG . GLN A 1 131 ? 13.209 67.095 10.896 1.00 119.46 ? 131 GLN A CG 1 ATOM 1034 C CD . GLN A 1 131 ? 13.641 66.099 9.836 1.00 107.76 ? 131 GLN A CD 1 ATOM 1035 O OE1 . GLN A 1 131 ? 14.577 65.326 10.038 1.00 108.74 ? 131 GLN A OE1 1 ATOM 1036 N NE2 . GLN A 1 131 ? 12.954 66.110 8.699 1.00 107.38 ? 131 GLN A NE2 1 ATOM 1037 N N . ASP A 1 132 ? 11.624 69.563 12.789 1.00 81.91 ? 132 ASP A N 1 ATOM 1038 C CA . ASP A 1 132 ? 10.585 70.347 12.139 1.00 92.37 ? 132 ASP A CA 1 ATOM 1039 C C . ASP A 1 132 ? 11.091 71.025 10.867 1.00 88.52 ? 132 ASP A C 1 ATOM 1040 O O . ASP A 1 132 ? 11.725 72.078 10.910 1.00 91.14 ? 132 ASP A O 1 ATOM 1041 C CB . ASP A 1 132 ? 10.051 71.398 13.114 1.00 93.09 ? 132 ASP A CB 1 ATOM 1042 C CG . ASP A 1 132 ? 8.970 72.266 12.509 1.00 125.02 ? 132 ASP A CG 1 ATOM 1043 O OD1 . ASP A 1 132 ? 8.252 71.786 11.607 1.00 165.61 ? 132 ASP A OD1 1 ATOM 1044 O OD2 . ASP A 1 132 ? 8.836 73.429 12.944 1.00 118.97 ? 132 ASP A OD2 1 ATOM 1045 N N . GLY A 1 133 ? 10.805 70.387 9.738 1.00 123.60 ? 133 GLY A N 1 ATOM 1046 C CA . GLY A 1 133 ? 10.824 70.978 8.411 1.00 120.61 ? 133 GLY A CA 1 ATOM 1047 C C . GLY A 1 133 ? 12.195 71.293 7.842 1.00 135.01 ? 133 GLY A C 1 ATOM 1048 O O . GLY A 1 133 ? 12.405 71.219 6.632 1.00 173.05 ? 133 GLY A O 1 ATOM 1049 N N . THR A 1 134 ? 13.132 71.636 8.722 1.00 125.49 ? 134 THR A N 1 ATOM 1050 C CA . THR A 1 134 ? 14.534 71.831 8.361 1.00 132.94 ? 134 THR A CA 1 ATOM 1051 C C . THR A 1 134 ? 15.458 71.251 9.423 1.00 132.11 ? 134 THR A C 1 ATOM 1052 O O . THR A 1 134 ? 16.170 70.271 9.204 1.00 148.03 ? 134 THR A O 1 ATOM 1053 C CB . THR A 1 134 ? 14.877 73.322 8.164 1.00 122.53 ? 134 THR A CB 1 ATOM 1054 O OG1 . THR A 1 134 ? 14.337 74.088 9.249 1.00 130.22 ? 134 THR A OG1 1 ATOM 1055 C CG2 . THR A 1 134 ? 14.309 73.840 6.850 1.00 105.40 ? 134 THR A CG2 1 ATOM 1056 N N . LYS A 1 135 ? 15.422 71.898 10.585 1.00 102.29 ? 135 LYS A N 1 ATOM 1057 C CA . LYS A 1 135 ? 16.319 71.613 11.696 1.00 100.24 ? 135 LYS A CA 1 ATOM 1058 C C . LYS A 1 135 ? 15.938 70.324 12.415 1.00 94.73 ? 135 LYS A C 1 ATOM 1059 O O . LYS A 1 135 ? 14.761 69.974 12.506 1.00 85.48 ? 135 LYS A O 1 ATOM 1060 C CB . LYS A 1 135 ? 16.314 72.791 12.678 1.00 107.53 ? 135 LYS A CB 1 ATOM 1061 C CG . LYS A 1 135 ? 17.310 72.688 13.821 1.00 121.01 ? 135 LYS A CG 1 ATOM 1062 C CD . LYS A 1 135 ? 17.148 73.850 14.792 1.00 113.90 ? 135 LYS A CD 1 ATOM 1063 C CE . LYS A 1 135 ? 18.133 73.753 15.945 1.00 106.86 ? 135 LYS A CE 1 ATOM 1064 N NZ . LYS A 1 135 ? 17.943 74.855 16.928 1.00 103.16 ? 135 LYS A NZ 1 ATOM 1065 N N . THR A 1 136 ? 16.944 69.622 12.925 1.00 91.34 ? 136 THR A N 1 ATOM 1066 C CA . THR A 1 136 ? 16.722 68.387 13.660 1.00 87.87 ? 136 THR A CA 1 ATOM 1067 C C . THR A 1 136 ? 17.438 68.421 15.004 1.00 104.04 ? 136 THR A C 1 ATOM 1068 O O . THR A 1 136 ? 18.655 68.593 15.064 1.00 126.71 ? 136 THR A O 1 ATOM 1069 C CB . THR A 1 136 ? 17.205 67.163 12.862 1.00 89.91 ? 136 THR A CB 1 ATOM 1070 O OG1 . THR A 1 136 ? 16.639 67.195 11.546 1.00 95.42 ? 136 THR A OG1 1 ATOM 1071 C CG2 . THR A 1 136 ? 16.798 65.873 13.561 1.00 76.08 ? 136 THR A CG2 1 ATOM 1072 N N . VAL A 1 137 ? 16.679 68.257 16.082 1.00 76.41 ? 137 VAL A N 1 ATOM 1073 C CA . VAL A 1 137 ? 17.254 68.241 17.422 1.00 74.95 ? 137 VAL A CA 1 ATOM 1074 C C . VAL A 1 137 ? 17.128 66.862 18.058 1.00 79.05 ? 137 VAL A C 1 ATOM 1075 O O . VAL A 1 137 ? 16.204 66.108 17.755 1.00 82.92 ? 137 VAL A O 1 ATOM 1076 C CB . VAL A 1 137 ? 16.588 69.286 18.340 1.00 75.59 ? 137 VAL A CB 1 ATOM 1077 C CG1 . VAL A 1 137 ? 16.787 70.685 17.778 1.00 83.56 ? 137 VAL A CG1 1 ATOM 1078 C CG2 . VAL A 1 137 ? 15.108 68.981 18.518 1.00 73.96 ? 137 VAL A CG2 1 ATOM 1079 N N . GLU A 1 138 ? 18.069 66.530 18.935 1.00 80.64 ? 138 GLU A N 1 ATOM 1080 C CA . GLU A 1 138 ? 18.021 65.265 19.653 1.00 77.70 ? 138 GLU A CA 1 ATOM 1081 C C . GLU A 1 138 ? 17.377 65.458 21.021 1.00 66.03 ? 138 GLU A C 1 ATOM 1082 O O . GLU A 1 138 ? 17.699 66.403 21.738 1.00 84.83 ? 138 GLU A O 1 ATOM 1083 C CB . GLU A 1 138 ? 19.424 64.674 19.806 1.00 92.13 ? 138 GLU A CB 1 ATOM 1084 C CG . GLU A 1 138 ? 19.446 63.291 20.433 1.00 102.05 ? 138 GLU A CG 1 ATOM 1085 C CD . GLU A 1 138 ? 20.854 62.762 20.622 1.00 102.29 ? 138 GLU A CD 1 ATOM 1086 O OE1 . GLU A 1 138 ? 21.787 63.585 20.737 1.00 105.86 ? 138 GLU A OE1 1 ATOM 1087 O OE2 . GLU A 1 138 ? 21.030 61.526 20.649 1.00 87.43 ? 138 GLU A OE2 1 ATOM 1088 N N . TYR A 1 139 ? 16.460 64.563 21.373 1.00 92.69 ? 139 TYR A N 1 ATOM 1089 C CA . TYR A 1 139 ? 15.797 64.616 22.670 1.00 84.08 ? 139 TYR A CA 1 ATOM 1090 C C . TYR A 1 139 ? 15.986 63.300 23.415 1.00 65.29 ? 139 TYR A C 1 ATOM 1091 O O . TYR A 1 139 ? 15.472 62.263 22.996 1.00 77.50 ? 139 TYR A O 1 ATOM 1092 C CB . TYR A 1 139 ? 14.309 64.930 22.497 1.00 62.38 ? 139 TYR A CB 1 ATOM 1093 C CG . TYR A 1 139 ? 13.532 65.000 23.793 1.00 61.45 ? 139 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 139 ? 13.855 65.933 24.768 1.00 93.32 ? 139 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 139 ? 12.463 64.145 24.033 1.00 59.57 ? 139 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 139 ? 13.145 66.005 25.952 1.00 77.89 ? 139 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 139 ? 11.746 64.211 25.213 1.00 59.04 ? 139 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 139 ? 12.092 65.142 26.169 1.00 74.36 ? 139 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 139 ? 11.381 65.210 27.345 1.00 85.02 ? 139 TYR A OH 1 ATOM 1100 N N . ALA A 1 140 ? 16.723 63.349 24.519 1.00 59.89 ? 140 ALA A N 1 ATOM 1101 C CA . ALA A 1 140 ? 17.015 62.156 25.304 1.00 58.00 ? 140 ALA A CA 1 ATOM 1102 C C . ALA A 1 140 ? 16.972 62.455 26.799 1.00 57.92 ? 140 ALA A C 1 ATOM 1103 O O . ALA A 1 140 ? 18.015 62.537 27.446 1.00 62.18 ? 140 ALA A O 1 ATOM 1104 C CB . ALA A 1 140 ? 18.370 61.587 24.918 1.00 58.29 ? 140 ALA A CB 1 ATOM 1105 N N . PRO A 1 141 ? 15.760 62.608 27.353 1.00 57.41 ? 141 PRO A N 1 ATOM 1106 C CA . PRO A 1 141 ? 15.578 62.961 28.766 1.00 69.35 ? 141 PRO A CA 1 ATOM 1107 C C . PRO A 1 141 ? 16.096 61.891 29.727 1.00 64.16 ? 141 PRO A C 1 ATOM 1108 O O . PRO A 1 141 ? 16.487 62.217 30.848 1.00 78.64 ? 141 PRO A O 1 ATOM 1109 C CB . PRO A 1 141 ? 14.058 63.119 28.894 1.00 77.94 ? 141 PRO A CB 1 ATOM 1110 C CG . PRO A 1 141 ? 13.496 62.303 27.782 1.00 63.18 ? 141 PRO A CG 1 ATOM 1111 C CD . PRO A 1 141 ? 14.475 62.429 26.657 1.00 61.63 ? 141 PRO A CD 1 ATOM 1112 N N . CYS A 1 142 ? 16.102 60.635 29.290 1.00 71.40 ? 142 CYS A N 1 ATOM 1113 C CA . CYS A 1 142 ? 16.597 59.536 30.114 1.00 78.58 ? 142 CYS A CA 1 ATOM 1114 C C . CYS A 1 142 ? 18.122 59.485 30.134 1.00 76.89 ? 142 CYS A C 1 ATOM 1115 O O . CYS A 1 142 ? 18.717 58.733 30.906 1.00 72.75 ? 142 CYS A O 1 ATOM 1116 C CB . CYS A 1 142 ? 16.040 58.198 29.618 1.00 93.94 ? 142 CYS A CB 1 ATOM 1117 S SG . CYS A 1 142 ? 14.644 57.556 30.576 1.00 72.55 ? 142 CYS A SG 1 ATOM 1118 N N . ARG A 1 143 ? 18.752 60.287 29.282 1.00 75.76 ? 143 ARG A N 1 ATOM 1119 C CA . ARG A 1 143 ? 20.206 60.359 29.251 1.00 58.44 ? 143 ARG A CA 1 ATOM 1120 C C . ARG A 1 143 ? 20.661 61.497 30.155 1.00 65.33 ? 143 ARG A C 1 ATOM 1121 O O . ARG A 1 143 ? 20.455 62.669 29.840 1.00 98.72 ? 143 ARG A O 1 ATOM 1122 C CB . ARG A 1 143 ? 20.703 60.561 27.816 1.00 57.88 ? 143 ARG A CB 1 ATOM 1123 C CG . ARG A 1 143 ? 22.210 60.491 27.657 1.00 59.16 ? 143 ARG A CG 1 ATOM 1124 C CD . ARG A 1 143 ? 22.623 60.479 26.191 1.00 59.99 ? 143 ARG A CD 1 ATOM 1125 N NE . ARG A 1 143 ? 22.331 61.741 25.518 1.00 68.30 ? 143 ARG A NE 1 ATOM 1126 C CZ . ARG A 1 143 ? 22.459 61.936 24.209 1.00 74.34 ? 143 ARG A CZ 1 ATOM 1127 N NH1 . ARG A 1 143 ? 22.868 60.948 23.426 1.00 80.94 ? 143 ARG A NH1 1 ATOM 1128 N NH2 . ARG A 1 143 ? 22.172 63.118 23.680 1.00 64.19 ? 143 ARG A NH2 1 ATOM 1129 N N . SER A 1 144 ? 21.285 61.147 31.277 1.00 70.47 ? 144 SER A N 1 ATOM 1130 C CA . SER A 1 144 ? 21.598 62.129 32.310 1.00 87.04 ? 144 SER A CA 1 ATOM 1131 C C . SER A 1 144 ? 22.658 61.639 33.293 1.00 76.59 ? 144 SER A C 1 ATOM 1132 O O . SER A 1 144 ? 23.222 60.559 33.135 1.00 67.11 ? 144 SER A O 1 ATOM 1133 C CB . SER A 1 144 ? 20.328 62.506 33.078 1.00 95.07 ? 144 SER A CB 1 ATOM 1134 O OG . SER A 1 144 ? 19.740 61.365 33.679 1.00 62.08 ? 144 SER A OG 1 ATOM 1135 N N . GLN A 1 145 ? 22.911 62.440 34.322 1.00 67.95 ? 145 GLN A N 1 ATOM 1136 C CA . GLN A 1 145 ? 23.937 62.122 35.307 1.00 76.52 ? 145 GLN A CA 1 ATOM 1137 C C . GLN A 1 145 ? 23.445 61.092 36.324 1.00 88.97 ? 145 GLN A C 1 ATOM 1138 O O . GLN A 1 145 ? 24.224 60.583 37.129 1.00 113.72 ? 145 GLN A O 1 ATOM 1139 C CB . GLN A 1 145 ? 24.393 63.396 36.021 1.00 106.88 ? 145 GLN A CB 1 ATOM 1140 C CG . GLN A 1 145 ? 24.595 64.601 35.105 1.00 119.56 ? 145 GLN A CG 1 ATOM 1141 C CD . GLN A 1 145 ? 25.887 64.549 34.303 1.00 112.51 ? 145 GLN A CD 1 ATOM 1142 O OE1 . GLN A 1 145 ? 26.345 63.481 33.895 1.00 115.17 ? 145 GLN A OE1 1 ATOM 1143 N NE2 . GLN A 1 145 ? 26.482 65.714 34.076 1.00 95.79 ? 145 GLN A NE2 1 ATOM 1144 N N . ASP A 1 146 ? 22.151 60.793 36.281 1.00 75.42 ? 146 ASP A N 1 ATOM 1145 C CA . ASP A 1 146 ? 21.571 59.747 37.118 1.00 88.57 ? 146 ASP A CA 1 ATOM 1146 C C . ASP A 1 146 ? 21.563 58.437 36.334 1.00 84.02 ? 146 ASP A C 1 ATOM 1147 O O . ASP A 1 146 ? 20.827 58.298 35.357 1.00 92.31 ? 146 ASP A O 1 ATOM 1148 C CB . ASP A 1 146 ? 20.157 60.136 37.557 1.00 97.25 ? 146 ASP A CB 1 ATOM 1149 C CG . ASP A 1 146 ? 19.522 59.107 38.470 1.00 102.55 ? 146 ASP A CG 1 ATOM 1150 O OD1 . ASP A 1 146 ? 20.266 58.367 39.149 1.00 131.81 ? 146 ASP A OD1 1 ATOM 1151 O OD2 . ASP A 1 146 ? 18.276 59.044 38.515 1.00 78.78 ? 146 ASP A OD2 1 ATOM 1152 N N . ILE A 1 147 ? 22.374 57.476 36.770 1.00 75.33 ? 147 ILE A N 1 ATOM 1153 C CA . ILE A 1 147 ? 22.717 56.337 35.919 1.00 88.53 ? 147 ILE A CA 1 ATOM 1154 C C . ILE A 1 147 ? 22.497 54.942 36.512 1.00 98.12 ? 147 ILE A C 1 ATOM 1155 O O . ILE A 1 147 ? 21.931 54.775 37.594 1.00 111.00 ? 147 ILE A O 1 ATOM 1156 C CB . ILE A 1 147 ? 24.194 56.418 35.477 1.00 70.21 ? 147 ILE A CB 1 ATOM 1157 C CG1 . ILE A 1 147 ? 25.123 56.290 36.686 1.00 73.34 ? 147 ILE A CG1 1 ATOM 1158 C CG2 . ILE A 1 147 ? 24.462 57.718 34.733 1.00 68.36 ? 147 ILE A CG2 1 ATOM 1159 C CD1 . ILE A 1 147 ? 26.588 56.239 36.319 1.00 73.94 ? 147 ILE A CD1 1 ATOM 1160 N N . ASP A 1 148 ? 22.977 53.955 35.758 1.00 76.40 ? 148 ASP A N 1 ATOM 1161 C CA . ASP A 1 148 ? 22.818 52.521 36.005 1.00 76.03 ? 148 ASP A CA 1 ATOM 1162 C C . ASP A 1 148 ? 21.367 52.057 36.113 1.00 84.70 ? 148 ASP A C 1 ATOM 1163 O O . ASP A 1 148 ? 20.483 52.574 35.431 1.00 106.59 ? 148 ASP A O 1 ATOM 1164 C CB . ASP A 1 148 ? 23.564 52.121 37.285 1.00 95.87 ? 148 ASP A CB 1 ATOM 1165 C CG . ASP A 1 148 ? 25.016 52.559 37.281 1.00 93.07 ? 148 ASP A CG 1 ATOM 1166 O OD1 . ASP A 1 148 ? 25.615 52.649 36.190 1.00 88.57 ? 148 ASP A OD1 1 ATOM 1167 O OD2 . ASP A 1 148 ? 25.561 52.812 38.376 1.00 92.67 ? 148 ASP A OD2 1 ATOM 1168 N N . ALA A 1 149 ? 21.133 51.082 36.988 1.00 84.87 ? 149 ALA A N 1 ATOM 1169 C CA . ALA A 1 149 ? 19.800 50.525 37.197 1.00 81.43 ? 149 ALA A CA 1 ATOM 1170 C C . ALA A 1 149 ? 19.004 51.373 38.174 1.00 76.19 ? 149 ALA A C 1 ATOM 1171 O O . ALA A 1 149 ? 17.803 51.582 38.005 1.00 74.19 ? 149 ALA A O 1 ATOM 1172 C CB . ALA A 1 149 ? 19.893 49.088 37.687 1.00 102.18 ? 149 ALA A CB 1 ATOM 1173 N N . ASP A 1 150 ? 19.695 51.849 39.203 1.00 78.88 ? 150 ASP A N 1 ATOM 1174 C CA . ASP A 1 150 ? 19.097 52.693 40.228 1.00 80.77 ? 150 ASP A CA 1 ATOM 1175 C C . ASP A 1 150 ? 18.560 53.990 39.626 1.00 77.68 ? 150 ASP A C 1 ATOM 1176 O O . ASP A 1 150 ? 17.573 54.548 40.105 1.00 78.65 ? 150 ASP A O 1 ATOM 1177 C CB . ASP A 1 150 ? 20.125 52.996 41.324 1.00 86.96 ? 150 ASP A CB 1 ATOM 1178 C CG . ASP A 1 150 ? 19.545 53.804 42.466 1.00 124.78 ? 150 ASP A CG 1 ATOM 1179 O OD1 . ASP A 1 150 ? 18.355 53.611 42.791 1.00 135.53 ? 150 ASP A OD1 1 ATOM 1180 O OD2 . ASP A 1 150 ? 20.282 54.634 43.042 1.00 137.08 ? 150 ASP A OD2 1 ATOM 1181 N N . GLY A 1 151 ? 19.220 54.458 38.570 1.00 74.49 ? 151 GLY A N 1 ATOM 1182 C CA . GLY A 1 151 ? 18.830 55.682 37.892 1.00 71.82 ? 151 GLY A CA 1 ATOM 1183 C C . GLY A 1 151 ? 18.051 55.455 36.609 1.00 69.47 ? 151 GLY A C 1 ATOM 1184 O O . GLY A 1 151 ? 17.303 54.487 36.484 1.00 90.68 ? 151 GLY A O 1 ATOM 1185 N N . GLN A 1 152 ? 18.229 56.365 35.656 1.00 68.82 ? 152 GLN A N 1 ATOM 1186 C CA . GLN A 1 152 ? 17.524 56.316 34.378 1.00 74.36 ? 152 GLN A CA 1 ATOM 1187 C C . GLN A 1 152 ? 18.321 55.603 33.286 1.00 63.75 ? 152 GLN A C 1 ATOM 1188 O O . GLN A 1 152 ? 17.920 55.605 32.124 1.00 58.59 ? 152 GLN A O 1 ATOM 1189 C CB . GLN A 1 152 ? 17.179 57.732 33.913 1.00 73.26 ? 152 GLN A CB 1 ATOM 1190 C CG . GLN A 1 152 ? 16.298 58.511 34.873 1.00 63.39 ? 152 GLN A CG 1 ATOM 1191 C CD . GLN A 1 152 ? 16.174 59.971 34.486 1.00 97.30 ? 152 GLN A CD 1 ATOM 1192 O OE1 . GLN A 1 152 ? 17.095 60.553 33.913 1.00 116.18 ? 152 GLN A OE1 1 ATOM 1193 N NE2 . GLN A 1 152 ? 15.031 60.571 34.795 1.00 115.44 ? 152 GLN A NE2 1 ATOM 1194 N N . GLY A 1 153 ? 19.459 55.024 33.654 1.00 62.51 ? 153 GLY A N 1 ATOM 1195 C CA . GLY A 1 153 ? 20.350 54.397 32.691 1.00 62.89 ? 153 GLY A CA 1 ATOM 1196 C C . GLY A 1 153 ? 19.722 53.362 31.773 1.00 60.36 ? 153 GLY A C 1 ATOM 1197 O O . GLY A 1 153 ? 20.028 53.306 30.583 1.00 64.41 ? 153 GLY A O 1 ATOM 1198 N N . PHE A 1 154 ? 18.864 52.519 32.331 1.00 65.56 ? 154 PHE A N 1 ATOM 1199 C CA . PHE A 1 154 ? 18.220 51.458 31.561 1.00 59.00 ? 154 PHE A CA 1 ATOM 1200 C C . PHE A 1 154 ? 16.807 51.810 31.095 1.00 59.94 ? 154 PHE A C 1 ATOM 1201 O O . PHE A 1 154 ? 16.092 50.955 30.573 1.00 87.73 ? 154 PHE A O 1 ATOM 1202 C CB . PHE A 1 154 ? 18.237 50.164 32.368 1.00 61.15 ? 154 PHE A CB 1 ATOM 1203 C CG . PHE A 1 154 ? 19.601 49.554 32.450 1.00 63.53 ? 154 PHE A CG 1 ATOM 1204 C CD1 . PHE A 1 154 ? 20.532 50.028 33.357 1.00 78.31 ? 154 PHE A CD1 1 ATOM 1205 C CD2 . PHE A 1 154 ? 19.971 48.544 31.583 1.00 63.76 ? 154 PHE A CD2 1 ATOM 1206 C CE1 . PHE A 1 154 ? 21.798 49.486 33.415 1.00 85.98 ? 154 PHE A CE1 1 ATOM 1207 C CE2 . PHE A 1 154 ? 21.234 47.999 31.636 1.00 66.82 ? 154 PHE A CE2 1 ATOM 1208 C CZ . PHE A 1 154 ? 22.149 48.476 32.549 1.00 77.64 ? 154 PHE A CZ 1 ATOM 1209 N N . CYS A 1 155 ? 16.418 53.066 31.304 1.00 68.83 ? 155 CYS A N 1 ATOM 1210 C CA . CYS A 1 155 ? 15.071 53.557 31.002 1.00 76.60 ? 155 CYS A CA 1 ATOM 1211 C C . CYS A 1 155 ? 14.520 53.157 29.632 1.00 73.45 ? 155 CYS A C 1 ATOM 1212 O O . CYS A 1 155 ? 13.346 52.798 29.520 1.00 60.21 ? 155 CYS A O 1 ATOM 1213 C CB . CYS A 1 155 ? 15.044 55.083 31.111 1.00 55.86 ? 155 CYS A CB 1 ATOM 1214 S SG . CYS A 1 155 ? 13.530 55.857 30.501 1.00 156.49 ? 155 CYS A SG 1 ATOM 1215 N N . GLN A 1 156 ? 15.366 53.221 28.606 1.00 73.49 ? 156 GLN A N 1 ATOM 1216 C CA . GLN A 1 156 ? 14.937 53.017 27.222 1.00 64.66 ? 156 GLN A CA 1 ATOM 1217 C C . GLN A 1 156 ? 13.814 53.989 26.870 1.00 81.33 ? 156 GLN A C 1 ATOM 1218 O O . GLN A 1 156 ? 12.796 53.595 26.299 1.00 72.61 ? 156 GLN A O 1 ATOM 1219 C CB . GLN A 1 156 ? 14.483 51.571 26.983 1.00 50.07 ? 156 GLN A CB 1 ATOM 1220 C CG . GLN A 1 156 ? 15.536 50.516 27.278 1.00 69.63 ? 156 GLN A CG 1 ATOM 1221 C CD . GLN A 1 156 ? 15.050 49.109 26.978 1.00 74.35 ? 156 GLN A CD 1 ATOM 1222 O OE1 . GLN A 1 156 ? 15.219 48.196 27.786 1.00 55.77 ? 156 GLN A OE1 1 ATOM 1223 N NE2 . GLN A 1 156 ? 14.449 48.927 25.806 1.00 62.17 ? 156 GLN A NE2 1 ATOM 1224 N N . GLY A 1 157 ? 14.005 55.256 27.230 1.00 80.21 ? 157 GLY A N 1 ATOM 1225 C CA . GLY A 1 157 ? 13.031 56.293 26.940 1.00 60.67 ? 157 GLY A CA 1 ATOM 1226 C C . GLY A 1 157 ? 12.788 56.422 25.451 1.00 65.07 ? 157 GLY A C 1 ATOM 1227 O O . GLY A 1 157 ? 13.724 56.357 24.655 1.00 74.55 ? 157 GLY A O 1 ATOM 1228 N N . GLY A 1 158 ? 11.527 56.600 25.074 1.00 49.66 ? 158 GLY A N 1 ATOM 1229 C CA . GLY A 1 158 ? 11.154 56.637 23.674 1.00 58.48 ? 158 GLY A CA 1 ATOM 1230 C C . GLY A 1 158 ? 10.498 55.338 23.256 1.00 61.92 ? 158 GLY A C 1 ATOM 1231 O O . GLY A 1 158 ? 10.164 55.145 22.087 1.00 53.76 ? 158 GLY A O 1 ATOM 1232 N N . PHE A 1 159 ? 10.322 54.443 24.223 1.00 80.30 ? 159 PHE A N 1 ATOM 1233 C CA . PHE A 1 159 ? 9.635 53.176 24.001 1.00 79.38 ? 159 PHE A CA 1 ATOM 1234 C C . PHE A 1 159 ? 8.207 53.436 23.528 1.00 76.14 ? 159 PHE A C 1 ATOM 1235 O O . PHE A 1 159 ? 7.652 52.676 22.735 1.00 53.07 ? 159 PHE A O 1 ATOM 1236 C CB . PHE A 1 159 ? 9.636 52.339 25.282 1.00 71.41 ? 159 PHE A CB 1 ATOM 1237 C CG . PHE A 1 159 ? 9.263 50.900 25.073 1.00 50.45 ? 159 PHE A CG 1 ATOM 1238 C CD1 . PHE A 1 159 ? 10.213 49.979 24.668 1.00 48.86 ? 159 PHE A CD1 1 ATOM 1239 C CD2 . PHE A 1 159 ? 7.967 50.465 25.298 1.00 77.64 ? 159 PHE A CD2 1 ATOM 1240 C CE1 . PHE A 1 159 ? 9.878 48.650 24.479 1.00 60.21 ? 159 PHE A CE1 1 ATOM 1241 C CE2 . PHE A 1 159 ? 7.624 49.137 25.112 1.00 51.74 ? 159 PHE A CE2 1 ATOM 1242 C CZ . PHE A 1 159 ? 8.582 48.230 24.703 1.00 54.08 ? 159 PHE A CZ 1 ATOM 1243 N N . SER A 1 160 ? 7.626 54.522 24.029 1.00 48.02 ? 160 SER A N 1 ATOM 1244 C CA . SER A 1 160 ? 6.309 54.975 23.600 1.00 67.95 ? 160 SER A CA 1 ATOM 1245 C C . SER A 1 160 ? 6.229 56.497 23.684 1.00 75.22 ? 160 SER A C 1 ATOM 1246 O O . SER A 1 160 ? 6.768 57.099 24.613 1.00 97.12 ? 160 SER A O 1 ATOM 1247 C CB . SER A 1 160 ? 5.215 54.334 24.452 1.00 69.35 ? 160 SER A CB 1 ATOM 1248 O OG . SER A 1 160 ? 5.390 54.650 25.822 1.00 54.84 ? 160 SER A OG 1 ATOM 1249 N N . ILE A 1 161 ? 5.555 57.117 22.718 1.00 69.13 ? 161 ILE A N 1 ATOM 1250 C CA . ILE A 1 161 ? 5.476 58.577 22.651 1.00 52.19 ? 161 ILE A CA 1 ATOM 1251 C C . ILE A 1 161 ? 4.111 59.075 22.185 1.00 54.18 ? 161 ILE A C 1 ATOM 1252 O O . ILE A 1 161 ? 3.380 58.361 21.500 1.00 59.45 ? 161 ILE A O 1 ATOM 1253 C CB . ILE A 1 161 ? 6.543 59.159 21.700 1.00 56.38 ? 161 ILE A CB 1 ATOM 1254 C CG1 . ILE A 1 161 ? 6.533 58.406 20.367 1.00 53.60 ? 161 ILE A CG1 1 ATOM 1255 C CG2 . ILE A 1 161 ? 7.922 59.114 22.338 1.00 52.88 ? 161 ILE A CG2 1 ATOM 1256 C CD1 . ILE A 1 161 ? 7.580 58.886 19.388 1.00 99.76 ? 161 ILE A CD1 1 ATOM 1257 N N . ASP A 1 162 ? 3.776 60.307 22.562 1.00 79.93 ? 162 ASP A N 1 ATOM 1258 C CA . ASP A 1 162 ? 2.546 60.947 22.104 1.00 76.74 ? 162 ASP A CA 1 ATOM 1259 C C . ASP A 1 162 ? 2.627 62.471 22.208 1.00 71.22 ? 162 ASP A C 1 ATOM 1260 O O . ASP A 1 162 ? 3.470 63.011 22.923 1.00 78.72 ? 162 ASP A O 1 ATOM 1261 C CB . ASP A 1 162 ? 1.346 60.433 22.900 1.00 68.12 ? 162 ASP A CB 1 ATOM 1262 C CG . ASP A 1 162 ? 0.146 60.143 22.017 1.00 102.27 ? 162 ASP A CG 1 ATOM 1263 O OD1 . ASP A 1 162 ? 0.055 60.736 20.922 1.00 107.83 ? 162 ASP A OD1 1 ATOM 1264 O OD2 . ASP A 1 162 ? -0.701 59.318 22.417 1.00 107.55 ? 162 ASP A OD2 1 ATOM 1265 N N . PHE A 1 163 ? 1.740 63.156 21.492 1.00 74.44 ? 163 PHE A N 1 ATOM 1266 C CA . PHE A 1 163 ? 1.665 64.615 21.535 1.00 62.59 ? 163 PHE A CA 1 ATOM 1267 C C . PHE A 1 163 ? 0.373 65.077 22.197 1.00 70.29 ? 163 PHE A C 1 ATOM 1268 O O . PHE A 1 163 ? -0.641 64.380 22.152 1.00 64.19 ? 163 PHE A O 1 ATOM 1269 C CB . PHE A 1 163 ? 1.749 65.209 20.128 1.00 64.60 ? 163 PHE A CB 1 ATOM 1270 C CG . PHE A 1 163 ? 3.132 65.225 19.548 1.00 80.21 ? 163 PHE A CG 1 ATOM 1271 C CD1 . PHE A 1 163 ? 3.538 64.242 18.663 1.00 76.64 ? 163 PHE A CD1 1 ATOM 1272 C CD2 . PHE A 1 163 ? 4.023 66.234 19.875 1.00 72.37 ? 163 PHE A CD2 1 ATOM 1273 C CE1 . PHE A 1 163 ? 4.808 64.259 18.121 1.00 76.47 ? 163 PHE A CE1 1 ATOM 1274 C CE2 . PHE A 1 163 ? 5.294 66.258 19.337 1.00 72.72 ? 163 PHE A CE2 1 ATOM 1275 C CZ . PHE A 1 163 ? 5.687 65.268 18.459 1.00 72.45 ? 163 PHE A CZ 1 ATOM 1276 N N . THR A 1 164 ? 0.413 66.254 22.814 1.00 86.26 ? 164 THR A N 1 ATOM 1277 C CA . THR A 1 164 ? -0.795 66.878 23.343 1.00 95.92 ? 164 THR A CA 1 ATOM 1278 C C . THR A 1 164 ? -1.224 68.035 22.446 1.00 100.44 ? 164 THR A C 1 ATOM 1279 O O . THR A 1 164 ? -0.556 68.346 21.461 1.00 118.65 ? 164 THR A O 1 ATOM 1280 C CB . THR A 1 164 ? -0.597 67.396 24.781 1.00 84.24 ? 164 THR A CB 1 ATOM 1281 O OG1 . THR A 1 164 ? 0.362 68.460 24.781 1.00 78.16 ? 164 THR A OG1 1 ATOM 1282 C CG2 . THR A 1 164 ? -0.115 66.278 25.690 1.00 65.34 ? 164 THR A CG2 1 ATOM 1283 N N . LYS A 1 165 ? -2.335 68.674 22.799 1.00 84.42 ? 165 LYS A N 1 ATOM 1284 C CA . LYS A 1 165 ? -2.833 69.825 22.051 1.00 81.88 ? 165 LYS A CA 1 ATOM 1285 C C . LYS A 1 165 ? -1.972 71.054 22.316 1.00 88.06 ? 165 LYS A C 1 ATOM 1286 O O . LYS A 1 165 ? -1.901 71.969 21.497 1.00 101.84 ? 165 LYS A O 1 ATOM 1287 C CB . LYS A 1 165 ? -4.287 70.120 22.421 1.00 78.11 ? 165 LYS A CB 1 ATOM 1288 C CG . LYS A 1 165 ? -5.248 68.970 22.167 1.00 90.36 ? 165 LYS A CG 1 ATOM 1289 C CD . LYS A 1 165 ? -6.642 69.252 22.724 1.00 100.30 ? 165 LYS A CD 1 ATOM 1290 C CE . LYS A 1 165 ? -7.401 70.292 21.903 1.00 120.11 ? 165 LYS A CE 1 ATOM 1291 N NZ . LYS A 1 165 ? -7.036 71.700 22.238 1.00 120.72 ? 165 LYS A NZ 1 ATOM 1292 N N . ALA A 1 166 ? -1.316 71.054 23.472 1.00 92.21 ? 166 ALA A N 1 ATOM 1293 C CA . ALA A 1 166 ? -0.523 72.186 23.935 1.00 108.03 ? 166 ALA A CA 1 ATOM 1294 C C . ALA A 1 166 ? 0.924 72.088 23.465 1.00 105.99 ? 166 ALA A C 1 ATOM 1295 O O . ALA A 1 166 ? 1.774 72.866 23.899 1.00 118.61 ? 166 ALA A O 1 ATOM 1296 C CB . ALA A 1 166 ? -0.579 72.285 25.452 1.00 131.24 ? 166 ALA A CB 1 ATOM 1297 N N . ASP A 1 167 ? 1.192 71.113 22.599 1.00 98.04 ? 167 ASP A N 1 ATOM 1298 C CA . ASP A 1 167 ? 2.542 70.812 22.123 1.00 93.36 ? 167 ASP A CA 1 ATOM 1299 C C . ASP A 1 167 ? 3.449 70.369 23.266 1.00 80.13 ? 167 ASP A C 1 ATOM 1300 O O . ASP A 1 167 ? 4.561 70.872 23.425 1.00 83.05 ? 167 ASP A O 1 ATOM 1301 C CB . ASP A 1 167 ? 3.155 72.013 21.395 1.00 122.62 ? 167 ASP A CB 1 ATOM 1302 C CG . ASP A 1 167 ? 2.591 72.202 20.003 1.00 138.40 ? 167 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 167 ? 2.381 71.190 19.302 1.00 131.55 ? 167 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 167 ? 2.356 73.363 19.606 1.00 157.75 ? 167 ASP A OD2 1 ATOM 1305 N N . ARG A 1 168 ? 2.954 69.432 24.065 1.00 91.08 ? 168 ARG A N 1 ATOM 1306 C CA . ARG A 1 168 ? 3.780 68.738 25.042 1.00 79.39 ? 168 ARG A CA 1 ATOM 1307 C C . ARG A 1 168 ? 4.034 67.312 24.570 1.00 80.31 ? 168 ARG A C 1 ATOM 1308 O O . ARG A 1 168 ? 3.118 66.629 24.109 1.00 79.02 ? 168 ARG A O 1 ATOM 1309 C CB . ARG A 1 168 ? 3.119 68.727 26.424 1.00 68.89 ? 168 ARG A CB 1 ATOM 1310 C CG . ARG A 1 168 ? 3.630 69.796 27.375 1.00 71.74 ? 168 ARG A CG 1 ATOM 1311 C CD . ARG A 1 168 ? 3.169 69.523 28.799 1.00 84.54 ? 168 ARG A CD 1 ATOM 1312 N NE . ARG A 1 168 ? 3.668 70.526 29.735 1.00 103.57 ? 168 ARG A NE 1 ATOM 1313 C CZ . ARG A 1 168 ? 4.851 70.458 30.336 1.00 99.26 ? 168 ARG A CZ 1 ATOM 1314 N NH1 . ARG A 1 168 ? 5.659 69.435 30.096 1.00 75.67 ? 168 ARG A NH1 1 ATOM 1315 N NH2 . ARG A 1 168 ? 5.227 71.414 31.175 1.00 118.27 ? 168 ARG A NH2 1 ATOM 1316 N N . VAL A 1 169 ? 5.280 66.871 24.675 1.00 76.04 ? 169 VAL A N 1 ATOM 1317 C CA . VAL A 1 169 ? 5.632 65.503 24.326 1.00 61.64 ? 169 VAL A CA 1 ATOM 1318 C C . VAL A 1 169 ? 5.496 64.596 25.539 1.00 66.41 ? 169 VAL A C 1 ATOM 1319 O O . VAL A 1 169 ? 6.107 64.845 26.574 1.00 75.35 ? 169 VAL A O 1 ATOM 1320 C CB . VAL A 1 169 ? 7.071 65.407 23.779 1.00 61.43 ? 169 VAL A CB 1 ATOM 1321 C CG1 . VAL A 1 169 ? 7.547 63.961 23.776 1.00 95.01 ? 169 VAL A CG1 1 ATOM 1322 C CG2 . VAL A 1 169 ? 7.157 66.010 22.386 1.00 63.23 ? 169 VAL A CG2 1 ATOM 1323 N N . LEU A 1 170 ? 4.683 63.551 25.416 1.00 72.33 ? 170 LEU A N 1 ATOM 1324 C CA . LEU A 1 170 ? 4.606 62.538 26.461 1.00 70.08 ? 170 LEU A CA 1 ATOM 1325 C C . LEU A 1 170 ? 5.523 61.373 26.114 1.00 70.98 ? 170 LEU A C 1 ATOM 1326 O O . LEU A 1 170 ? 5.275 60.642 25.156 1.00 89.30 ? 170 LEU A O 1 ATOM 1327 C CB . LEU A 1 170 ? 3.169 62.048 26.654 1.00 56.01 ? 170 LEU A CB 1 ATOM 1328 C CG . LEU A 1 170 ? 2.996 61.018 27.772 1.00 56.64 ? 170 LEU A CG 1 ATOM 1329 C CD1 . LEU A 1 170 ? 3.496 61.587 29.088 1.00 58.83 ? 170 LEU A CD1 1 ATOM 1330 C CD2 . LEU A 1 170 ? 1.547 60.570 27.894 1.00 71.25 ? 170 LEU A CD2 1 ATOM 1331 N N . LEU A 1 171 ? 6.586 61.208 26.894 1.00 72.71 ? 171 LEU A N 1 ATOM 1332 C CA . LEU A 1 171 ? 7.572 60.164 26.637 1.00 70.19 ? 171 LEU A CA 1 ATOM 1333 C C . LEU A 1 171 ? 7.822 59.323 27.881 1.00 95.29 ? 171 LEU A C 1 ATOM 1334 O O . LEU A 1 171 ? 8.339 59.820 28.882 1.00 119.09 ? 171 LEU A O 1 ATOM 1335 C CB . LEU A 1 171 ? 8.885 60.787 26.147 1.00 69.18 ? 171 LEU A CB 1 ATOM 1336 C CG . LEU A 1 171 ? 10.036 59.905 25.656 1.00 68.76 ? 171 LEU A CG 1 ATOM 1337 C CD1 . LEU A 1 171 ? 10.873 60.693 24.663 1.00 101.29 ? 171 LEU A CD1 1 ATOM 1338 C CD2 . LEU A 1 171 ? 10.914 59.420 26.802 1.00 54.89 ? 171 LEU A CD2 1 ATOM 1339 N N . GLY A 1 172 ? 7.444 58.052 27.821 1.00 85.52 ? 172 GLY A N 1 ATOM 1340 C CA . GLY A 1 172 ? 7.778 57.120 28.878 1.00 89.27 ? 172 GLY A CA 1 ATOM 1341 C C . GLY A 1 172 ? 8.865 56.135 28.491 1.00 71.75 ? 172 GLY A C 1 ATOM 1342 O O . GLY A 1 172 ? 9.249 56.039 27.325 1.00 57.96 ? 172 GLY A O 1 ATOM 1343 N N . GLY A 1 173 ? 9.367 55.406 29.482 1.00 68.45 ? 173 GLY A N 1 ATOM 1344 C CA . GLY A 1 173 ? 10.111 54.188 29.226 1.00 65.11 ? 173 GLY A CA 1 ATOM 1345 C C . GLY A 1 173 ? 10.009 53.278 30.433 1.00 73.17 ? 173 GLY A C 1 ATOM 1346 O O . GLY A 1 173 ? 9.923 53.752 31.565 1.00 97.83 ? 173 GLY A O 1 ATOM 1347 N N . PRO A 1 174 ? 10.048 51.960 30.194 1.00 56.06 ? 174 PRO A N 1 ATOM 1348 C CA . PRO A 1 174 ? 9.871 50.910 31.205 1.00 56.95 ? 174 PRO A CA 1 ATOM 1349 C C . PRO A 1 174 ? 11.054 50.700 32.151 1.00 65.72 ? 174 PRO A C 1 ATOM 1350 O O . PRO A 1 174 ? 10.848 50.214 33.260 1.00 92.30 ? 174 PRO A O 1 ATOM 1351 C CB . PRO A 1 174 ? 9.634 49.654 30.360 1.00 84.54 ? 174 PRO A CB 1 ATOM 1352 C CG . PRO A 1 174 ? 10.287 49.945 29.061 1.00 63.42 ? 174 PRO A CG 1 ATOM 1353 C CD . PRO A 1 174 ? 10.129 51.409 28.830 1.00 49.31 ? 174 PRO A CD 1 ATOM 1354 N N . GLY A 1 175 ? 12.260 51.066 31.728 1.00 55.58 ? 175 GLY A N 1 ATOM 1355 C CA . GLY A 1 175 ? 13.462 50.657 32.435 1.00 64.19 ? 175 GLY A CA 1 ATOM 1356 C C . GLY A 1 175 ? 14.000 51.553 33.538 1.00 64.78 ? 175 GLY A C 1 ATOM 1357 O O . GLY A 1 175 ? 15.072 51.285 34.082 1.00 100.29 ? 175 GLY A O 1 ATOM 1358 N N . SER A 1 176 ? 13.271 52.611 33.878 1.00 61.07 ? 176 SER A N 1 ATOM 1359 C CA . SER A 1 176 ? 13.728 53.538 34.910 1.00 66.34 ? 176 SER A CA 1 ATOM 1360 C C . SER A 1 176 ? 13.586 52.969 36.319 1.00 87.24 ? 176 SER A C 1 ATOM 1361 O O . SER A 1 176 ? 12.557 52.385 36.662 1.00 104.14 ? 176 SER A O 1 ATOM 1362 C CB . SER A 1 176 ? 12.968 54.862 34.816 1.00 64.02 ? 176 SER A CB 1 ATOM 1363 O OG . SER A 1 176 ? 13.495 55.688 33.794 1.00 61.06 ? 176 SER A OG 1 ATOM 1364 N N . PHE A 1 177 ? 14.633 53.155 37.122 1.00 73.44 ? 177 PHE A N 1 ATOM 1365 C CA . PHE A 1 177 ? 14.648 52.778 38.536 1.00 75.36 ? 177 PHE A CA 1 ATOM 1366 C C . PHE A 1 177 ? 14.325 51.304 38.751 1.00 77.89 ? 177 PHE A C 1 ATOM 1367 O O . PHE A 1 177 ? 13.294 50.963 39.333 1.00 79.09 ? 177 PHE A O 1 ATOM 1368 C CB . PHE A 1 177 ? 13.671 53.651 39.327 1.00 76.82 ? 177 PHE A CB 1 ATOM 1369 C CG . PHE A 1 177 ? 13.584 55.060 38.821 1.00 75.92 ? 177 PHE A CG 1 ATOM 1370 C CD1 . PHE A 1 177 ? 12.406 55.540 38.274 1.00 73.70 ? 177 PHE A CD1 1 ATOM 1371 C CD2 . PHE A 1 177 ? 14.686 55.900 38.870 1.00 73.27 ? 177 PHE A CD2 1 ATOM 1372 C CE1 . PHE A 1 177 ? 12.322 56.833 37.799 1.00 73.63 ? 177 PHE A CE1 1 ATOM 1373 C CE2 . PHE A 1 177 ? 14.609 57.194 38.396 1.00 71.11 ? 177 PHE A CE2 1 ATOM 1374 C CZ . PHE A 1 177 ? 13.426 57.662 37.860 1.00 69.57 ? 177 PHE A CZ 1 ATOM 1375 N N . TYR A 1 178 ? 15.230 50.443 38.291 1.00 81.94 ? 178 TYR A N 1 ATOM 1376 C CA . TYR A 1 178 ? 15.036 48.994 38.311 1.00 73.13 ? 178 TYR A CA 1 ATOM 1377 C C . TYR A 1 178 ? 13.694 48.613 37.698 1.00 75.80 ? 178 TYR A C 1 ATOM 1378 O O . TYR A 1 178 ? 12.927 47.834 38.268 1.00 71.96 ? 178 TYR A O 1 ATOM 1379 C CB . TYR A 1 178 ? 15.163 48.444 39.733 1.00 76.37 ? 178 TYR A CB 1 ATOM 1380 C CG . TYR A 1 178 ? 16.600 48.215 40.148 1.00 78.85 ? 178 TYR A CG 1 ATOM 1381 C CD1 . TYR A 1 178 ? 17.251 47.025 39.843 1.00 80.25 ? 178 TYR A CD1 1 ATOM 1382 C CD2 . TYR A 1 178 ? 17.311 49.190 40.833 1.00 82.02 ? 178 TYR A CD2 1 ATOM 1383 C CE1 . TYR A 1 178 ? 18.566 46.813 40.214 1.00 79.59 ? 178 TYR A CE1 1 ATOM 1384 C CE2 . TYR A 1 178 ? 18.626 48.987 41.209 1.00 83.54 ? 178 TYR A CE2 1 ATOM 1385 C CZ . TYR A 1 178 ? 19.248 47.797 40.898 1.00 82.27 ? 178 TYR A CZ 1 ATOM 1386 O OH . TYR A 1 178 ? 20.557 47.591 41.270 1.00 84.95 ? 178 TYR A OH 1 ATOM 1387 N N . TRP A 1 179 ? 13.429 49.195 36.532 1.00 85.54 ? 179 TRP A N 1 ATOM 1388 C CA . TRP A 1 179 ? 12.277 48.862 35.701 1.00 66.54 ? 179 TRP A CA 1 ATOM 1389 C C . TRP A 1 179 ? 10.928 49.157 36.356 1.00 66.85 ? 179 TRP A C 1 ATOM 1390 O O . TRP A 1 179 ? 9.921 48.531 36.024 1.00 65.43 ? 179 TRP A O 1 ATOM 1391 C CB . TRP A 1 179 ? 12.352 47.396 35.271 1.00 62.65 ? 179 TRP A CB 1 ATOM 1392 C CG . TRP A 1 179 ? 13.478 47.152 34.318 1.00 61.35 ? 179 TRP A CG 1 ATOM 1393 C CD1 . TRP A 1 179 ? 13.439 47.258 32.959 1.00 59.83 ? 179 TRP A CD1 1 ATOM 1394 C CD2 . TRP A 1 179 ? 14.821 46.788 34.655 1.00 63.18 ? 179 TRP A CD2 1 ATOM 1395 N NE1 . TRP A 1 179 ? 14.672 46.974 32.426 1.00 68.87 ? 179 TRP A NE1 1 ATOM 1396 C CE2 . TRP A 1 179 ? 15.539 46.681 33.448 1.00 64.43 ? 179 TRP A CE2 1 ATOM 1397 C CE3 . TRP A 1 179 ? 15.485 46.534 35.857 1.00 66.24 ? 179 TRP A CE3 1 ATOM 1398 C CZ2 . TRP A 1 179 ? 16.884 46.332 33.409 1.00 70.45 ? 179 TRP A CZ2 1 ATOM 1399 C CZ3 . TRP A 1 179 ? 16.821 46.190 35.817 1.00 67.69 ? 179 TRP A CZ3 1 ATOM 1400 C CH2 . TRP A 1 179 ? 17.506 46.092 34.602 1.00 66.31 ? 179 TRP A CH2 1 ATOM 1401 N N . GLN A 1 180 ? 10.907 50.122 37.270 1.00 71.00 ? 180 GLN A N 1 ATOM 1402 C CA . GLN A 1 180 ? 9.646 50.683 37.734 1.00 73.57 ? 180 GLN A CA 1 ATOM 1403 C C . GLN A 1 180 ? 8.994 51.413 36.569 1.00 70.30 ? 180 GLN A C 1 ATOM 1404 O O . GLN A 1 180 ? 7.775 51.398 36.412 1.00 70.59 ? 180 GLN A O 1 ATOM 1405 C CB . GLN A 1 180 ? 9.856 51.643 38.909 1.00 78.73 ? 180 GLN A CB 1 ATOM 1406 C CG . GLN A 1 180 ? 10.272 50.981 40.211 1.00 82.20 ? 180 GLN A CG 1 ATOM 1407 C CD . GLN A 1 180 ? 10.513 51.987 41.320 1.00 83.45 ? 180 GLN A CD 1 ATOM 1408 O OE1 . GLN A 1 180 ? 10.175 53.164 41.191 1.00 82.30 ? 180 GLN A OE1 1 ATOM 1409 N NE2 . GLN A 1 180 ? 11.101 51.528 42.418 1.00 94.04 ? 180 GLN A NE2 1 ATOM 1410 N N . GLY A 1 181 ? 9.832 52.045 35.750 1.00 67.44 ? 181 GLY A N 1 ATOM 1411 C CA . GLY A 1 181 ? 9.368 52.830 34.622 1.00 63.28 ? 181 GLY A CA 1 ATOM 1412 C C . GLY A 1 181 ? 9.056 54.256 35.029 1.00 65.17 ? 181 GLY A C 1 ATOM 1413 O O . GLY A 1 181 ? 8.886 54.546 36.214 1.00 91.77 ? 181 GLY A O 1 ATOM 1414 N N . GLN A 1 182 ? 8.989 55.153 34.051 1.00 64.41 ? 182 GLN A N 1 ATOM 1415 C CA . GLN A 1 182 ? 8.643 56.543 34.323 1.00 74.79 ? 182 GLN A CA 1 ATOM 1416 C C . GLN A 1 182 ? 8.087 57.238 33.087 1.00 68.14 ? 182 GLN A C 1 ATOM 1417 O O . GLN A 1 182 ? 8.286 56.781 31.964 1.00 57.07 ? 182 GLN A O 1 ATOM 1418 C CB . GLN A 1 182 ? 9.861 57.313 34.841 1.00 78.48 ? 182 GLN A CB 1 ATOM 1419 C CG . GLN A 1 182 ? 10.895 57.647 33.779 1.00 60.64 ? 182 GLN A CG 1 ATOM 1420 C CD . GLN A 1 182 ? 11.916 58.660 34.261 1.00 64.21 ? 182 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 182 ? 13.068 58.653 33.826 1.00 85.04 ? 182 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 182 ? 11.495 59.543 35.159 1.00 72.69 ? 182 GLN A NE2 1 ATOM 1423 N N . LEU A 1 183 ? 7.388 58.346 33.306 1.00 77.65 ? 183 LEU A N 1 ATOM 1424 C CA . LEU A 1 183 ? 6.912 59.189 32.218 1.00 66.46 ? 183 LEU A CA 1 ATOM 1425 C C . LEU A 1 183 ? 7.613 60.540 32.277 1.00 84.13 ? 183 LEU A C 1 ATOM 1426 O O . LEU A 1 183 ? 7.823 61.084 33.357 1.00 70.58 ? 183 LEU A O 1 ATOM 1427 C CB . LEU A 1 183 ? 5.397 59.378 32.293 1.00 62.04 ? 183 LEU A CB 1 ATOM 1428 C CG . LEU A 1 183 ? 4.523 58.128 32.271 1.00 62.31 ? 183 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 183 ? 3.064 58.518 32.412 1.00 65.17 ? 183 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 183 ? 4.753 57.346 30.992 1.00 58.22 ? 183 LEU A CD2 1 ATOM 1431 N N . ILE A 1 184 ? 7.984 61.075 31.118 1.00 74.94 ? 184 ILE A N 1 ATOM 1432 C CA . ILE A 1 184 ? 8.636 62.378 31.062 1.00 60.14 ? 184 ILE A CA 1 ATOM 1433 C C . ILE A 1 184 ? 7.961 63.275 30.029 1.00 66.92 ? 184 ILE A C 1 ATOM 1434 O O . ILE A 1 184 ? 7.905 62.939 28.846 1.00 81.97 ? 184 ILE A O 1 ATOM 1435 C CB . ILE A 1 184 ? 10.139 62.253 30.725 1.00 58.68 ? 184 ILE A CB 1 ATOM 1436 C CG1 . ILE A 1 184 ? 10.823 61.259 31.666 1.00 56.94 ? 184 ILE A CG1 1 ATOM 1437 C CG2 . ILE A 1 184 ? 10.817 63.614 30.799 1.00 67.57 ? 184 ILE A CG2 1 ATOM 1438 C CD1 . ILE A 1 184 ? 12.268 60.978 31.317 1.00 67.87 ? 184 ILE A CD1 1 ATOM 1439 N N . SER A 1 185 ? 7.448 64.415 30.480 1.00 72.29 ? 185 SER A N 1 ATOM 1440 C CA . SER A 1 185 ? 6.767 65.344 29.585 1.00 79.87 ? 185 SER A CA 1 ATOM 1441 C C . SER A 1 185 ? 7.511 66.669 29.452 1.00 89.14 ? 185 SER A C 1 ATOM 1442 O O . SER A 1 185 ? 7.855 67.307 30.449 1.00 94.62 ? 185 SER A O 1 ATOM 1443 C CB . SER A 1 185 ? 5.337 65.600 30.065 1.00 80.81 ? 185 SER A CB 1 ATOM 1444 O OG . SER A 1 185 ? 4.633 66.414 29.142 1.00 91.36 ? 185 SER A OG 1 ATOM 1445 N N . ASP A 1 186 ? 7.752 67.078 28.211 1.00 75.45 ? 186 ASP A N 1 ATOM 1446 C CA . ASP A 1 186 ? 8.412 68.346 27.932 1.00 85.11 ? 186 ASP A CA 1 ATOM 1447 C C . ASP A 1 186 ? 7.720 69.105 26.808 1.00 94.95 ? 186 ASP A C 1 ATOM 1448 O O . ASP A 1 186 ? 7.199 68.507 25.867 1.00 79.56 ? 186 ASP A O 1 ATOM 1449 C CB . ASP A 1 186 ? 9.882 68.122 27.574 1.00 93.96 ? 186 ASP A CB 1 ATOM 1450 C CG . ASP A 1 186 ? 10.752 67.914 28.795 1.00 106.61 ? 186 ASP A CG 1 ATOM 1451 O OD1 . ASP A 1 186 ? 11.021 68.907 29.500 1.00 105.50 ? 186 ASP A OD1 1 ATOM 1452 O OD2 . ASP A 1 186 ? 11.171 66.765 29.043 1.00 113.77 ? 186 ASP A OD2 1 ATOM 1453 N N . GLN A 1 187 ? 7.723 70.428 26.916 1.00 85.27 ? 187 GLN A N 1 ATOM 1454 C CA . GLN A 1 187 ? 7.162 71.282 25.881 1.00 86.04 ? 187 GLN A CA 1 ATOM 1455 C C . GLN A 1 187 ? 8.058 71.261 24.647 1.00 88.37 ? 187 GLN A C 1 ATOM 1456 O O . GLN A 1 187 ? 9.281 71.339 24.763 1.00 73.90 ? 187 GLN A O 1 ATOM 1457 C CB . GLN A 1 187 ? 6.989 72.709 26.405 1.00 92.26 ? 187 GLN A CB 1 ATOM 1458 C CG . GLN A 1 187 ? 6.146 72.794 27.670 1.00 102.31 ? 187 GLN A CG 1 ATOM 1459 C CD . GLN A 1 187 ? 6.276 74.130 28.376 1.00 129.20 ? 187 GLN A CD 1 ATOM 1460 O OE1 . GLN A 1 187 ? 7.062 74.987 27.971 1.00 116.45 ? 187 GLN A OE1 1 ATOM 1461 N NE2 . GLN A 1 187 ? 5.504 74.312 29.441 1.00 144.50 ? 187 GLN A NE2 1 ATOM 1462 N N . VAL A 1 188 ? 7.443 71.145 23.472 1.00 77.30 ? 188 VAL A N 1 ATOM 1463 C CA . VAL A 1 188 ? 8.180 71.086 22.212 1.00 74.37 ? 188 VAL A CA 1 ATOM 1464 C C . VAL A 1 188 ? 9.093 72.297 22.040 1.00 93.71 ? 188 VAL A C 1 ATOM 1465 O O . VAL A 1 188 ? 10.248 72.162 21.633 1.00 77.41 ? 188 VAL A O 1 ATOM 1466 C CB . VAL A 1 188 ? 7.222 70.993 21.006 1.00 74.98 ? 188 VAL A CB 1 ATOM 1467 C CG1 . VAL A 1 188 ? 7.994 71.067 19.698 1.00 76.09 ? 188 VAL A CG1 1 ATOM 1468 C CG2 . VAL A 1 188 ? 6.412 69.708 21.073 1.00 80.57 ? 188 VAL A CG2 1 ATOM 1469 N N . ALA A 1 189 ? 8.572 73.476 22.371 1.00 106.19 ? 189 ALA A N 1 ATOM 1470 C CA . ALA A 1 189 ? 9.340 74.713 22.286 1.00 83.99 ? 189 ALA A CA 1 ATOM 1471 C C . ALA A 1 189 ? 10.598 74.643 23.149 1.00 83.36 ? 189 ALA A C 1 ATOM 1472 O O . ALA A 1 189 ? 11.667 75.101 22.741 1.00 90.50 ? 189 ALA A O 1 ATOM 1473 C CB . ALA A 1 189 ? 8.480 75.896 22.698 1.00 97.62 ? 189 ALA A CB 1 ATOM 1474 N N . GLU A 1 190 ? 10.461 74.067 24.339 1.00 81.28 ? 190 GLU A N 1 ATOM 1475 C CA . GLU A 1 190 ? 11.591 73.865 25.239 1.00 80.75 ? 190 GLU A CA 1 ATOM 1476 C C . GLU A 1 190 ? 12.644 72.953 24.617 1.00 86.33 ? 190 GLU A C 1 ATOM 1477 O O . GLU A 1 190 ? 13.833 73.266 24.632 1.00 87.83 ? 190 GLU A O 1 ATOM 1478 C CB . GLU A 1 190 ? 11.115 73.279 26.571 1.00 93.02 ? 190 GLU A CB 1 ATOM 1479 C CG . GLU A 1 190 ? 10.699 74.318 27.602 1.00 114.73 ? 190 GLU A CG 1 ATOM 1480 C CD . GLU A 1 190 ? 11.887 74.943 28.307 1.00 135.12 ? 190 GLU A CD 1 ATOM 1481 O OE1 . GLU A 1 190 ? 11.742 76.061 28.847 1.00 147.56 ? 190 GLU A OE1 1 ATOM 1482 O OE2 . GLU A 1 190 ? 12.966 74.314 28.327 1.00 128.86 ? 190 GLU A OE2 1 ATOM 1483 N N . ILE A 1 191 ? 12.194 71.829 24.067 1.00 75.54 ? 191 ILE A N 1 ATOM 1484 C CA . ILE A 1 191 ? 13.085 70.838 23.470 1.00 73.53 ? 191 ILE A CA 1 ATOM 1485 C C . ILE A 1 191 ? 13.909 71.424 22.321 1.00 91.78 ? 191 ILE A C 1 ATOM 1486 O O . ILE A 1 191 ? 15.097 71.128 22.184 1.00 116.43 ? 191 ILE A O 1 ATOM 1487 C CB . ILE A 1 191 ? 12.293 69.614 22.959 1.00 73.94 ? 191 ILE A CB 1 ATOM 1488 C CG1 . ILE A 1 191 ? 11.480 68.994 24.098 1.00 76.79 ? 191 ILE A CG1 1 ATOM 1489 C CG2 . ILE A 1 191 ? 13.227 68.580 22.349 1.00 79.80 ? 191 ILE A CG2 1 ATOM 1490 C CD1 . ILE A 1 191 ? 10.707 67.753 23.698 1.00 78.58 ? 191 ILE A CD1 1 ATOM 1491 N N . VAL A 1 192 ? 13.278 72.266 21.508 1.00 78.26 ? 192 VAL A N 1 ATOM 1492 C CA . VAL A 1 192 ? 13.947 72.871 20.361 1.00 80.89 ? 192 VAL A CA 1 ATOM 1493 C C . VAL A 1 192 ? 14.894 73.998 20.777 1.00 100.90 ? 192 VAL A C 1 ATOM 1494 O O . VAL A 1 192 ? 16.035 74.061 20.316 1.00 112.66 ? 192 VAL A O 1 ATOM 1495 C CB . VAL A 1 192 ? 12.927 73.425 19.343 1.00 82.94 ? 192 VAL A CB 1 ATOM 1496 C CG1 . VAL A 1 192 ? 13.643 74.072 18.168 1.00 86.98 ? 192 VAL A CG1 1 ATOM 1497 C CG2 . VAL A 1 192 ? 12.007 72.319 18.857 1.00 96.03 ? 192 VAL A CG2 1 ATOM 1498 N N . SER A 1 193 ? 14.421 74.877 21.656 1.00 93.12 ? 193 SER A N 1 ATOM 1499 C CA . SER A 1 193 ? 15.177 76.068 22.036 1.00 106.19 ? 193 SER A CA 1 ATOM 1500 C C . SER A 1 193 ? 16.364 75.765 22.952 1.00 103.38 ? 193 SER A C 1 ATOM 1501 O O . SER A 1 193 ? 17.360 76.489 22.945 1.00 90.60 ? 193 SER A O 1 ATOM 1502 C CB . SER A 1 193 ? 14.253 77.081 22.716 1.00 98.85 ? 193 SER A CB 1 ATOM 1503 O OG . SER A 1 193 ? 13.712 76.555 23.916 1.00 89.09 ? 193 SER A OG 1 ATOM 1504 N N . LYS A 1 194 ? 16.254 74.699 23.738 1.00 84.51 ? 194 LYS A N 1 ATOM 1505 C CA . LYS A 1 194 ? 17.273 74.372 24.734 1.00 83.65 ? 194 LYS A CA 1 ATOM 1506 C C . LYS A 1 194 ? 18.328 73.387 24.237 1.00 89.62 ? 194 LYS A C 1 ATOM 1507 O O . LYS A 1 194 ? 19.192 72.968 25.007 1.00 99.28 ? 194 LYS A O 1 ATOM 1508 C CB . LYS A 1 194 ? 16.615 73.812 25.998 1.00 82.96 ? 194 LYS A CB 1 ATOM 1509 C CG . LYS A 1 194 ? 15.935 74.860 26.862 1.00 88.14 ? 194 LYS A CG 1 ATOM 1510 C CD . LYS A 1 194 ? 16.957 75.750 27.551 1.00 98.19 ? 194 LYS A CD 1 ATOM 1511 C CE . LYS A 1 194 ? 16.285 76.929 28.235 1.00 128.05 ? 194 LYS A CE 1 ATOM 1512 N NZ . LYS A 1 194 ? 15.200 76.493 29.156 1.00 139.62 ? 194 LYS A NZ 1 ATOM 1513 N N . TYR A 1 195 ? 18.267 73.015 22.962 1.00 81.37 ? 195 TYR A N 1 ATOM 1514 C CA . TYR A 1 195 ? 19.164 71.981 22.453 1.00 93.12 ? 195 TYR A CA 1 ATOM 1515 C C . TYR A 1 195 ? 20.570 72.505 22.171 1.00 82.13 ? 195 TYR A C 1 ATOM 1516 O O . TYR A 1 195 ? 20.764 73.391 21.340 1.00 118.01 ? 195 TYR A O 1 ATOM 1517 C CB . TYR A 1 195 ? 18.592 71.350 21.183 1.00 89.74 ? 195 TYR A CB 1 ATOM 1518 C CG . TYR A 1 195 ? 19.537 70.372 20.520 1.00 79.95 ? 195 TYR A CG 1 ATOM 1519 C CD1 . TYR A 1 195 ? 20.185 70.695 19.334 1.00 85.59 ? 195 TYR A CD1 1 ATOM 1520 C CD2 . TYR A 1 195 ? 19.792 69.131 21.088 1.00 79.91 ? 195 TYR A CD2 1 ATOM 1521 C CE1 . TYR A 1 195 ? 21.054 69.804 18.729 1.00 89.82 ? 195 TYR A CE1 1 ATOM 1522 C CE2 . TYR A 1 195 ? 20.658 68.235 20.491 1.00 90.00 ? 195 TYR A CE2 1 ATOM 1523 C CZ . TYR A 1 195 ? 21.287 68.577 19.312 1.00 103.45 ? 195 TYR A CZ 1 ATOM 1524 O OH . TYR A 1 195 ? 22.150 67.689 18.713 1.00 134.32 ? 195 TYR A OH 1 ATOM 1525 N N . ASP A 1 196 ? 21.543 71.941 22.880 1.00 81.03 ? 196 ASP A N 1 ATOM 1526 C CA . ASP A 1 196 ? 22.955 72.215 22.647 1.00 83.07 ? 196 ASP A CA 1 ATOM 1527 C C . ASP A 1 196 ? 23.658 70.924 22.229 1.00 97.11 ? 196 ASP A C 1 ATOM 1528 O O . ASP A 1 196 ? 23.697 69.963 22.999 1.00 90.71 ? 196 ASP A O 1 ATOM 1529 C CB . ASP A 1 196 ? 23.605 72.811 23.900 1.00 84.37 ? 196 ASP A CB 1 ATOM 1530 C CG . ASP A 1 196 ? 24.948 73.469 23.615 1.00 118.32 ? 196 ASP A CG 1 ATOM 1531 O OD1 . ASP A 1 196 ? 25.699 72.971 22.750 1.00 109.46 ? 196 ASP A OD1 1 ATOM 1532 O OD2 . ASP A 1 196 ? 25.254 74.492 24.263 1.00 130.22 ? 196 ASP A OD2 1 ATOM 1533 N N . PRO A 1 197 ? 24.209 70.895 21.008 1.00 82.78 ? 197 PRO A N 1 ATOM 1534 C CA . PRO A 1 197 ? 24.885 69.698 20.493 1.00 96.04 ? 197 PRO A CA 1 ATOM 1535 C C . PRO A 1 197 ? 26.112 69.297 21.313 1.00 101.77 ? 197 PRO A C 1 ATOM 1536 O O . PRO A 1 197 ? 26.535 68.142 21.255 1.00 88.35 ? 197 PRO A O 1 ATOM 1537 C CB . PRO A 1 197 ? 25.293 70.109 19.074 1.00 96.09 ? 197 PRO A CB 1 ATOM 1538 C CG . PRO A 1 197 ? 25.352 71.598 19.114 1.00 87.34 ? 197 PRO A CG 1 ATOM 1539 C CD . PRO A 1 197 ? 24.256 72.010 20.046 1.00 86.09 ? 197 PRO A CD 1 ATOM 1540 N N . ASN A 1 198 ? 26.669 70.239 22.068 1.00 101.81 ? 198 ASN A N 1 ATOM 1541 C CA . ASN A 1 198 ? 27.852 69.969 22.876 1.00 93.83 ? 198 ASN A CA 1 ATOM 1542 C C . ASN A 1 198 ? 27.515 69.563 24.308 1.00 92.95 ? 198 ASN A C 1 ATOM 1543 O O . ASN A 1 198 ? 28.408 69.286 25.108 1.00 111.10 ? 198 ASN A O 1 ATOM 1544 C CB . ASN A 1 198 ? 28.772 71.190 22.889 1.00 99.95 ? 198 ASN A CB 1 ATOM 1545 C CG . ASN A 1 198 ? 29.352 71.496 21.523 1.00 103.67 ? 198 ASN A CG 1 ATOM 1546 O OD1 . ASN A 1 198 ? 29.538 70.600 20.699 1.00 110.63 ? 198 ASN A OD1 1 ATOM 1547 N ND2 . ASN A 1 198 ? 29.642 72.768 21.276 1.00 93.25 ? 198 ASN A ND2 1 ATOM 1548 N N . VAL A 1 199 ? 26.226 69.533 24.628 1.00 89.95 ? 199 VAL A N 1 ATOM 1549 C CA . VAL A 1 199 ? 25.783 69.136 25.960 1.00 87.75 ? 199 VAL A CA 1 ATOM 1550 C C . VAL A 1 199 ? 24.991 67.832 25.897 1.00 73.75 ? 199 VAL A C 1 ATOM 1551 O O . VAL A 1 199 ? 23.891 67.788 25.347 1.00 84.14 ? 199 VAL A O 1 ATOM 1552 C CB . VAL A 1 199 ? 24.924 70.230 26.617 1.00 97.80 ? 199 VAL A CB 1 ATOM 1553 C CG1 . VAL A 1 199 ? 24.513 69.810 28.014 1.00 110.16 ? 199 VAL A CG1 1 ATOM 1554 C CG2 . VAL A 1 199 ? 25.689 71.542 26.661 1.00 82.21 ? 199 VAL A CG2 1 ATOM 1555 N N . TYR A 1 200 ? 25.561 66.774 26.466 1.00 76.00 ? 200 TYR A N 1 ATOM 1556 C CA . TYR A 1 200 ? 24.970 65.441 26.387 1.00 90.72 ? 200 TYR A CA 1 ATOM 1557 C C . TYR A 1 200 ? 23.790 65.276 27.339 1.00 87.12 ? 200 TYR A C 1 ATOM 1558 O O . TYR A 1 200 ? 22.870 64.503 27.069 1.00 87.64 ? 200 TYR A O 1 ATOM 1559 C CB . TYR A 1 200 ? 26.033 64.379 26.674 1.00 68.65 ? 200 TYR A CB 1 ATOM 1560 C CG . TYR A 1 200 ? 27.228 64.462 25.752 1.00 86.14 ? 200 TYR A CG 1 ATOM 1561 C CD1 . TYR A 1 200 ? 27.069 64.762 24.405 1.00 75.02 ? 200 TYR A CD1 1 ATOM 1562 C CD2 . TYR A 1 200 ? 28.516 64.260 26.230 1.00 94.62 ? 200 TYR A CD2 1 ATOM 1563 C CE1 . TYR A 1 200 ? 28.159 64.846 23.558 1.00 74.06 ? 200 TYR A CE1 1 ATOM 1564 C CE2 . TYR A 1 200 ? 29.612 64.344 25.391 1.00 98.54 ? 200 TYR A CE2 1 ATOM 1565 C CZ . TYR A 1 200 ? 29.428 64.640 24.056 1.00 85.14 ? 200 TYR A CZ 1 ATOM 1566 O OH . TYR A 1 200 ? 30.517 64.720 23.219 1.00 87.79 ? 200 TYR A OH 1 ATOM 1567 N N . SER A 1 201 ? 23.817 66.000 28.454 1.00 89.28 ? 201 SER A N 1 ATOM 1568 C CA . SER A 1 201 ? 22.708 65.974 29.400 1.00 79.18 ? 201 SER A CA 1 ATOM 1569 C C . SER A 1 201 ? 22.095 67.360 29.542 1.00 86.20 ? 201 SER A C 1 ATOM 1570 O O . SER A 1 201 ? 22.707 68.264 30.109 1.00 108.96 ? 201 SER A O 1 ATOM 1571 C CB . SER A 1 201 ? 23.175 65.460 30.763 1.00 89.48 ? 201 SER A CB 1 ATOM 1572 O OG . SER A 1 201 ? 23.741 64.166 30.651 1.00 98.94 ? 201 SER A OG 1 ATOM 1573 N N . ILE A 1 202 ? 20.873 67.517 29.044 1.00 68.86 ? 202 ILE A N 1 ATOM 1574 C CA . ILE A 1 202 ? 20.232 68.826 28.999 1.00 78.76 ? 202 ILE A CA 1 ATOM 1575 C C . ILE A 1 202 ? 19.093 68.947 30.002 1.00 81.77 ? 202 ILE A C 1 ATOM 1576 O O . ILE A 1 202 ? 18.156 68.148 29.995 1.00 106.78 ? 202 ILE A O 1 ATOM 1577 C CB . ILE A 1 202 ? 19.686 69.132 27.589 1.00 84.03 ? 202 ILE A CB 1 ATOM 1578 C CG1 . ILE A 1 202 ? 20.830 69.172 26.573 1.00 78.52 ? 202 ILE A CG1 1 ATOM 1579 C CG2 . ILE A 1 202 ? 18.917 70.446 27.585 1.00 73.90 ? 202 ILE A CG2 1 ATOM 1580 C CD1 . ILE A 1 202 ? 20.382 69.473 25.160 1.00 88.16 ? 202 ILE A CD1 1 ATOM 1581 N N . LYS A 1 203 ? 19.181 69.952 30.867 1.00 97.87 ? 203 LYS A N 1 ATOM 1582 C CA . LYS A 1 203 ? 18.108 70.244 31.806 1.00 102.65 ? 203 LYS A CA 1 ATOM 1583 C C . LYS A 1 203 ? 17.025 71.077 31.130 1.00 96.24 ? 203 LYS A C 1 ATOM 1584 O O . LYS A 1 203 ? 17.283 72.178 30.643 1.00 77.68 ? 203 LYS A O 1 ATOM 1585 C CB . LYS A 1 203 ? 18.648 70.976 33.037 1.00 103.56 ? 203 LYS A CB 1 ATOM 1586 C CG . LYS A 1 203 ? 17.580 71.352 34.054 1.00 108.57 ? 203 LYS A CG 1 ATOM 1587 C CD . LYS A 1 203 ? 18.171 72.115 35.230 1.00 131.62 ? 203 LYS A CD 1 ATOM 1588 C CE . LYS A 1 203 ? 17.100 72.480 36.248 1.00 136.07 ? 203 LYS A CE 1 ATOM 1589 N NZ . LYS A 1 203 ? 16.012 73.298 35.643 1.00 122.59 ? 203 LYS A NZ 1 ATOM 1590 N N . TYR A 1 204 ? 15.810 70.542 31.103 1.00 104.40 ? 204 TYR A N 1 ATOM 1591 C CA . TYR A 1 204 ? 14.681 71.241 30.508 1.00 109.56 ? 204 TYR A CA 1 ATOM 1592 C C . TYR A 1 204 ? 13.786 71.851 31.577 1.00 117.46 ? 204 TYR A C 1 ATOM 1593 O O . TYR A 1 204 ? 13.321 71.156 32.480 1.00 124.38 ? 204 TYR A O 1 ATOM 1594 C CB . TYR A 1 204 ? 13.861 70.292 29.631 1.00 92.30 ? 204 TYR A CB 1 ATOM 1595 C CG . TYR A 1 204 ? 14.583 69.799 28.400 1.00 92.68 ? 204 TYR A CG 1 ATOM 1596 C CD1 . TYR A 1 204 ? 15.228 68.570 28.395 1.00 90.47 ? 204 TYR A CD1 1 ATOM 1597 C CD2 . TYR A 1 204 ? 14.619 70.562 27.241 1.00 96.32 ? 204 TYR A CD2 1 ATOM 1598 C CE1 . TYR A 1 204 ? 15.889 68.115 27.270 1.00 84.12 ? 204 TYR A CE1 1 ATOM 1599 C CE2 . TYR A 1 204 ? 15.277 70.116 26.113 1.00 112.93 ? 204 TYR A CE2 1 ATOM 1600 C CZ . TYR A 1 204 ? 15.910 68.893 26.132 1.00 104.38 ? 204 TYR A CZ 1 ATOM 1601 O OH . TYR A 1 204 ? 16.565 68.449 25.007 1.00 112.16 ? 204 TYR A OH 1 ATOM 1602 N N . ASN A 1 205 ? 13.550 73.154 31.473 1.00 101.75 ? 205 ASN A N 1 ATOM 1603 C CA . ASN A 1 205 ? 12.590 73.814 32.345 1.00 94.51 ? 205 ASN A CA 1 ATOM 1604 C C . ASN A 1 205 ? 11.173 73.397 31.973 1.00 96.49 ? 205 ASN A C 1 ATOM 1605 O O . ASN A 1 205 ? 10.912 73.034 30.826 1.00 93.17 ? 205 ASN A O 1 ATOM 1606 C CB . ASN A 1 205 ? 12.743 75.333 32.269 1.00 99.68 ? 205 ASN A CB 1 ATOM 1607 C CG . ASN A 1 205 ? 14.078 75.812 32.803 1.00 126.43 ? 205 ASN A CG 1 ATOM 1608 O OD1 . ASN A 1 205 ? 14.667 75.187 33.685 1.00 137.81 ? 205 ASN A OD1 1 ATOM 1609 N ND2 . ASN A 1 205 ? 14.561 76.929 32.271 1.00 126.17 ? 205 ASN A ND2 1 ATOM 1610 N N . ASN A 1 206 ? 10.272 73.449 32.951 1.00 111.68 ? 206 ASN A N 1 ATOM 1611 C CA . ASN A 1 206 ? 8.897 72.980 32.786 1.00 109.03 ? 206 ASN A CA 1 ATOM 1612 C C . ASN A 1 206 ? 8.851 71.522 32.337 1.00 93.00 ? 206 ASN A C 1 ATOM 1613 O O . ASN A 1 206 ? 8.109 71.169 31.420 1.00 89.70 ? 206 ASN A O 1 ATOM 1614 C CB . ASN A 1 206 ? 8.137 73.860 31.790 1.00 98.40 ? 206 ASN A CB 1 ATOM 1615 C CG . ASN A 1 206 ? 8.187 75.330 32.153 1.00 114.89 ? 206 ASN A CG 1 ATOM 1616 O OD1 . ASN A 1 206 ? 8.574 76.169 31.339 1.00 130.39 ? 206 ASN A OD1 1 ATOM 1617 N ND2 . ASN A 1 206 ? 7.797 75.651 33.381 1.00 121.82 ? 206 ASN A ND2 1 ATOM 1618 N N . GLN A 1 207 ? 9.653 70.682 32.983 1.00 93.97 ? 207 GLN A N 1 ATOM 1619 C CA . GLN A 1 207 ? 9.665 69.255 32.681 1.00 85.07 ? 207 GLN A CA 1 ATOM 1620 C C . GLN A 1 207 ? 8.827 68.474 33.684 1.00 91.35 ? 207 GLN A C 1 ATOM 1621 O O . GLN A 1 207 ? 9.130 68.449 34.877 1.00 107.93 ? 207 GLN A O 1 ATOM 1622 C CB . GLN A 1 207 ? 11.094 68.708 32.669 1.00 84.62 ? 207 GLN A CB 1 ATOM 1623 C CG . GLN A 1 207 ? 11.172 67.229 32.312 1.00 88.24 ? 207 GLN A CG 1 ATOM 1624 C CD . GLN A 1 207 ? 12.590 66.694 32.312 1.00 98.27 ? 207 GLN A CD 1 ATOM 1625 O OE1 . GLN A 1 207 ? 13.221 66.577 33.362 1.00 123.55 ? 207 GLN A OE1 1 ATOM 1626 N NE2 . GLN A 1 207 ? 13.098 66.363 31.130 1.00 73.52 ? 207 GLN A NE2 1 ATOM 1627 N N . LEU A 1 208 ? 7.772 67.836 33.191 1.00 93.71 ? 208 LEU A N 1 ATOM 1628 C CA . LEU A 1 208 ? 6.923 67.007 34.033 1.00 92.48 ? 208 LEU A CA 1 ATOM 1629 C C . LEU A 1 208 ? 7.361 65.552 33.950 1.00 94.57 ? 208 LEU A C 1 ATOM 1630 O O . LEU A 1 208 ? 7.248 64.919 32.900 1.00 114.62 ? 208 LEU A O 1 ATOM 1631 C CB . LEU A 1 208 ? 5.458 67.147 33.622 1.00 88.17 ? 208 LEU A CB 1 ATOM 1632 C CG . LEU A 1 208 ? 4.896 68.565 33.675 1.00 72.37 ? 208 LEU A CG 1 ATOM 1633 C CD1 . LEU A 1 208 ? 3.520 68.602 33.048 1.00 75.12 ? 208 LEU A CD1 1 ATOM 1634 C CD2 . LEU A 1 208 ? 4.847 69.068 35.107 1.00 75.82 ? 208 LEU A CD2 1 ATOM 1635 N N . ALA A 1 209 ? 7.864 65.028 35.061 1.00 88.07 ? 209 ALA A N 1 ATOM 1636 C CA . ALA A 1 209 ? 8.360 63.661 35.090 1.00 77.16 ? 209 ALA A CA 1 ATOM 1637 C C . ALA A 1 209 ? 8.082 62.980 36.423 1.00 71.65 ? 209 ALA A C 1 ATOM 1638 O O . ALA A 1 209 ? 8.213 63.591 37.484 1.00 78.42 ? 209 ALA A O 1 ATOM 1639 C CB . ALA A 1 209 ? 9.851 63.637 34.790 1.00 65.03 ? 209 ALA A CB 1 ATOM 1640 N N . THR A 1 210 ? 7.695 61.711 36.361 1.00 70.70 ? 210 THR A N 1 ATOM 1641 C CA . THR A 1 210 ? 7.560 60.896 37.560 1.00 73.43 ? 210 THR A CA 1 ATOM 1642 C C . THR A 1 210 ? 8.950 60.533 38.065 1.00 75.59 ? 210 THR A C 1 ATOM 1643 O O . THR A 1 210 ? 9.915 60.553 37.302 1.00 88.43 ? 210 THR A O 1 ATOM 1644 C CB . THR A 1 210 ? 6.750 59.615 37.299 1.00 73.74 ? 210 THR A CB 1 ATOM 1645 O OG1 . THR A 1 210 ? 7.462 58.778 36.381 1.00 74.39 ? 210 THR A OG1 1 ATOM 1646 C CG2 . THR A 1 210 ? 5.391 59.954 36.713 1.00 74.55 ? 210 THR A CG2 1 ATOM 1647 N N . ARG A 1 211 ? 9.054 60.197 39.345 1.00 75.98 ? 211 ARG A N 1 ATOM 1648 C CA . ARG A 1 211 ? 10.350 59.881 39.929 1.00 85.05 ? 211 ARG A CA 1 ATOM 1649 C C . ARG A 1 211 ? 10.293 58.572 40.706 1.00 82.14 ? 211 ARG A C 1 ATOM 1650 O O . ARG A 1 211 ? 9.214 58.022 40.932 1.00 79.45 ? 211 ARG A O 1 ATOM 1651 C CB . ARG A 1 211 ? 10.831 61.020 40.829 1.00 90.77 ? 211 ARG A CB 1 ATOM 1652 C CG . ARG A 1 211 ? 10.058 61.184 42.122 1.00 111.73 ? 211 ARG A CG 1 ATOM 1653 C CD . ARG A 1 211 ? 10.603 62.359 42.915 1.00 136.35 ? 211 ARG A CD 1 ATOM 1654 N NE . ARG A 1 211 ? 10.145 62.359 44.299 1.00 144.64 ? 211 ARG A NE 1 ATOM 1655 C CZ . ARG A 1 211 ? 10.511 63.261 45.203 1.00 146.25 ? 211 ARG A CZ 1 ATOM 1656 N NH1 . ARG A 1 211 ? 11.341 64.239 44.867 1.00 134.50 ? 211 ARG A NH1 1 ATOM 1657 N NH2 . ARG A 1 211 ? 10.047 63.186 46.443 1.00 147.43 ? 211 ARG A NH2 1 ATOM 1658 N N . THR A 1 212 ? 11.464 58.076 41.094 1.00 82.82 ? 212 THR A N 1 ATOM 1659 C CA . THR A 1 212 ? 11.598 56.751 41.692 1.00 79.85 ? 212 THR A CA 1 ATOM 1660 C C . THR A 1 212 ? 10.729 56.557 42.935 1.00 82.35 ? 212 THR A C 1 ATOM 1661 O O . THR A 1 212 ? 10.481 57.493 43.695 1.00 90.20 ? 212 THR A O 1 ATOM 1662 C CB . THR A 1 212 ? 13.066 56.456 42.064 1.00 80.60 ? 212 THR A CB 1 ATOM 1663 O OG1 . THR A 1 212 ? 13.158 55.162 42.671 1.00 91.98 ? 212 THR A OG1 1 ATOM 1664 C CG2 . THR A 1 212 ? 13.600 57.505 43.027 1.00 81.21 ? 212 THR A CG2 1 ATOM 1665 N N . ALA A 1 213 ? 10.264 55.327 43.117 1.00 83.82 ? 213 ALA A N 1 ATOM 1666 C CA . ALA A 1 213 ? 9.394 54.972 44.229 1.00 84.77 ? 213 ALA A CA 1 ATOM 1667 C C . ALA A 1 213 ? 9.986 53.801 44.998 1.00 85.74 ? 213 ALA A C 1 ATOM 1668 O O . ALA A 1 213 ? 11.127 53.406 44.753 1.00 85.12 ? 213 ALA A O 1 ATOM 1669 C CB . ALA A 1 213 ? 7.999 54.634 43.732 1.00 85.39 ? 213 ALA A CB 1 ATOM 1670 N N . GLN A 1 214 ? 9.214 53.261 45.935 1.00 87.23 ? 214 GLN A N 1 ATOM 1671 C CA . GLN A 1 214 ? 9.659 52.120 46.727 1.00 87.47 ? 214 GLN A CA 1 ATOM 1672 C C . GLN A 1 214 ? 9.979 50.929 45.831 1.00 87.19 ? 214 GLN A C 1 ATOM 1673 O O . GLN A 1 214 ? 9.399 50.771 44.756 1.00 87.01 ? 214 GLN A O 1 ATOM 1674 C CB . GLN A 1 214 ? 8.599 51.727 47.759 1.00 88.39 ? 214 GLN A CB 1 ATOM 1675 C CG . GLN A 1 214 ? 8.341 52.770 48.837 1.00 91.45 ? 214 GLN A CG 1 ATOM 1676 C CD . GLN A 1 214 ? 7.336 53.825 48.411 1.00 104.71 ? 214 GLN A CD 1 ATOM 1677 O OE1 . GLN A 1 214 ? 6.974 53.918 47.238 1.00 103.84 ? 214 GLN A OE1 1 ATOM 1678 N NE2 . GLN A 1 214 ? 6.875 54.622 49.368 1.00 109.10 ? 214 GLN A NE2 1 ATOM 1679 N N . ALA A 1 215 ? 10.907 50.091 46.285 1.00 86.29 ? 215 ALA A N 1 ATOM 1680 C CA . ALA A 1 215 ? 11.373 48.945 45.510 1.00 85.00 ? 215 ALA A CA 1 ATOM 1681 C C . ALA A 1 215 ? 10.270 47.917 45.260 1.00 83.52 ? 215 ALA A C 1 ATOM 1682 O O . ALA A 1 215 ? 10.443 46.994 44.464 1.00 81.39 ? 215 ALA A O 1 ATOM 1683 C CB . ALA A 1 215 ? 12.550 48.287 46.210 1.00 88.89 ? 215 ALA A CB 1 ATOM 1684 N N . ILE A 1 216 ? 9.142 48.078 45.943 1.00 89.00 ? 216 ILE A N 1 ATOM 1685 C CA . ILE A 1 216 ? 8.000 47.189 45.769 1.00 82.77 ? 216 ILE A CA 1 ATOM 1686 C C . ILE A 1 216 ? 7.438 47.305 44.353 1.00 81.46 ? 216 ILE A C 1 ATOM 1687 O O . ILE A 1 216 ? 6.816 46.375 43.838 1.00 92.04 ? 216 ILE A O 1 ATOM 1688 C CB . ILE A 1 216 ? 6.882 47.503 46.785 1.00 84.18 ? 216 ILE A CB 1 ATOM 1689 C CG1 . ILE A 1 216 ? 7.477 47.905 48.138 1.00 105.94 ? 216 ILE A CG1 1 ATOM 1690 C CG2 . ILE A 1 216 ? 5.939 46.316 46.930 1.00 82.59 ? 216 ILE A CG2 1 ATOM 1691 C CD1 . ILE A 1 216 ? 8.234 46.793 48.838 1.00 124.83 ? 216 ILE A CD1 1 ATOM 1692 N N . PHE A 1 217 ? 7.673 48.455 43.729 1.00 82.14 ? 217 PHE A N 1 ATOM 1693 C CA . PHE A 1 217 ? 7.144 48.748 42.403 1.00 81.03 ? 217 PHE A CA 1 ATOM 1694 C C . PHE A 1 217 ? 8.118 48.369 41.292 1.00 79.16 ? 217 PHE A C 1 ATOM 1695 O O . PHE A 1 217 ? 7.870 48.653 40.120 1.00 78.11 ? 217 PHE A O 1 ATOM 1696 C CB . PHE A 1 217 ? 6.788 50.232 42.295 1.00 83.19 ? 217 PHE A CB 1 ATOM 1697 C CG . PHE A 1 217 ? 5.758 50.683 43.290 1.00 85.19 ? 217 PHE A CG 1 ATOM 1698 C CD1 . PHE A 1 217 ? 4.407 50.558 43.012 1.00 85.83 ? 217 PHE A CD1 1 ATOM 1699 C CD2 . PHE A 1 217 ? 6.140 51.233 44.504 1.00 86.29 ? 217 PHE A CD2 1 ATOM 1700 C CE1 . PHE A 1 217 ? 3.456 50.971 43.924 1.00 87.70 ? 217 PHE A CE1 1 ATOM 1701 C CE2 . PHE A 1 217 ? 5.193 51.648 45.421 1.00 88.01 ? 217 PHE A CE2 1 ATOM 1702 C CZ . PHE A 1 217 ? 3.850 51.517 45.131 1.00 88.72 ? 217 PHE A CZ 1 ATOM 1703 N N . ASP A 1 218 ? 9.232 47.745 41.665 1.00 79.39 ? 218 ASP A N 1 ATOM 1704 C CA . ASP A 1 218 ? 10.241 47.328 40.697 1.00 76.39 ? 218 ASP A CA 1 ATOM 1705 C C . ASP A 1 218 ? 9.669 46.387 39.640 1.00 72.82 ? 218 ASP A C 1 ATOM 1706 O O . ASP A 1 218 ? 8.768 45.594 39.921 1.00 82.00 ? 218 ASP A O 1 ATOM 1707 C CB . ASP A 1 218 ? 11.418 46.654 41.406 1.00 77.43 ? 218 ASP A CB 1 ATOM 1708 C CG . ASP A 1 218 ? 12.342 47.651 42.080 1.00 91.75 ? 218 ASP A CG 1 ATOM 1709 O OD1 . ASP A 1 218 ? 13.487 47.274 42.407 1.00 98.09 ? 218 ASP A OD1 1 ATOM 1710 O OD2 . ASP A 1 218 ? 11.928 48.812 42.276 1.00 91.09 ? 218 ASP A OD2 1 ATOM 1711 N N . ASP A 1 219 ? 10.196 46.503 38.423 1.00 73.19 ? 219 ASP A N 1 ATOM 1712 C CA . ASP A 1 219 ? 9.811 45.657 37.295 1.00 68.84 ? 219 ASP A CA 1 ATOM 1713 C C . ASP A 1 219 ? 8.329 45.780 36.949 1.00 66.44 ? 219 ASP A C 1 ATOM 1714 O O . ASP A 1 219 ? 7.714 44.819 36.498 1.00 80.43 ? 219 ASP A O 1 ATOM 1715 C CB . ASP A 1 219 ? 10.164 44.197 37.581 1.00 66.05 ? 219 ASP A CB 1 ATOM 1716 C CG . ASP A 1 219 ? 11.600 44.027 38.028 1.00 67.82 ? 219 ASP A CG 1 ATOM 1717 O OD1 . ASP A 1 219 ? 12.498 44.050 37.160 1.00 79.41 ? 219 ASP A OD1 1 ATOM 1718 O OD2 . ASP A 1 219 ? 11.832 43.872 39.244 1.00 71.58 ? 219 ASP A OD2 1 ATOM 1719 N N . SER A 1 220 ? 7.764 46.963 37.174 1.00 68.02 ? 220 SER A N 1 ATOM 1720 C CA . SER A 1 220 ? 6.378 47.243 36.806 1.00 67.20 ? 220 SER A CA 1 ATOM 1721 C C . SER A 1 220 ? 6.237 47.599 35.326 1.00 71.48 ? 220 SER A C 1 ATOM 1722 O O . SER A 1 220 ? 5.190 47.364 34.724 1.00 76.26 ? 220 SER A O 1 ATOM 1723 C CB . SER A 1 220 ? 5.819 48.374 37.668 1.00 71.72 ? 220 SER A CB 1 ATOM 1724 O OG . SER A 1 220 ? 5.847 48.027 39.041 1.00 75.76 ? 220 SER A OG 1 ATOM 1725 N N . TYR A 1 221 ? 7.307 48.153 34.756 1.00 63.35 ? 221 TYR A N 1 ATOM 1726 C CA . TYR A 1 221 ? 7.343 48.613 33.363 1.00 65.69 ? 221 TYR A CA 1 ATOM 1727 C C . TYR A 1 221 ? 6.354 49.740 33.061 1.00 75.13 ? 221 TYR A C 1 ATOM 1728 O O . TYR A 1 221 ? 5.589 49.655 32.101 1.00 74.45 ? 221 TYR A O 1 ATOM 1729 C CB . TYR A 1 221 ? 7.082 47.454 32.394 1.00 55.27 ? 221 TYR A CB 1 ATOM 1730 C CG . TYR A 1 221 ? 8.177 46.412 32.329 1.00 55.22 ? 221 TYR A CG 1 ATOM 1731 C CD1 . TYR A 1 221 ? 8.038 45.290 31.524 1.00 58.23 ? 221 TYR A CD1 1 ATOM 1732 C CD2 . TYR A 1 221 ? 9.344 46.546 33.069 1.00 62.09 ? 221 TYR A CD2 1 ATOM 1733 C CE1 . TYR A 1 221 ? 9.028 44.332 31.455 1.00 58.70 ? 221 TYR A CE1 1 ATOM 1734 C CE2 . TYR A 1 221 ? 10.341 45.589 33.008 1.00 80.24 ? 221 TYR A CE2 1 ATOM 1735 C CZ . TYR A 1 221 ? 10.177 44.485 32.200 1.00 74.87 ? 221 TYR A CZ 1 ATOM 1736 O OH . TYR A 1 221 ? 11.166 43.531 32.134 1.00 95.39 ? 221 TYR A OH 1 ATOM 1737 N N . LEU A 1 222 ? 6.366 50.790 33.878 1.00 63.97 ? 222 LEU A N 1 ATOM 1738 C CA . LEU A 1 222 ? 5.575 51.983 33.587 1.00 62.98 ? 222 LEU A CA 1 ATOM 1739 C C . LEU A 1 222 ? 6.107 52.682 32.342 1.00 64.74 ? 222 LEU A C 1 ATOM 1740 O O . LEU A 1 222 ? 7.309 52.904 32.213 1.00 80.90 ? 222 LEU A O 1 ATOM 1741 C CB . LEU A 1 222 ? 5.583 52.949 34.775 1.00 75.25 ? 222 LEU A CB 1 ATOM 1742 C CG . LEU A 1 222 ? 5.052 54.364 34.519 1.00 67.74 ? 222 LEU A CG 1 ATOM 1743 C CD1 . LEU A 1 222 ? 3.584 54.339 34.129 1.00 68.44 ? 222 LEU A CD1 1 ATOM 1744 C CD2 . LEU A 1 222 ? 5.267 55.246 35.737 1.00 71.52 ? 222 LEU A CD2 1 ATOM 1745 N N . GLY A 1 223 ? 5.210 53.025 31.425 1.00 77.15 ? 223 GLY A N 1 ATOM 1746 C CA . GLY A 1 223 ? 5.605 53.687 30.197 1.00 76.82 ? 223 GLY A CA 1 ATOM 1747 C C . GLY A 1 223 ? 5.749 52.721 29.038 1.00 75.70 ? 223 GLY A C 1 ATOM 1748 O O . GLY A 1 223 ? 6.329 53.060 28.007 1.00 78.12 ? 223 GLY A O 1 ATOM 1749 N N . TYR A 1 224 ? 5.228 51.510 29.215 1.00 67.11 ? 224 TYR A N 1 ATOM 1750 C CA . TYR A 1 224 ? 5.225 50.509 28.153 1.00 48.73 ? 224 TYR A CA 1 ATOM 1751 C C . TYR A 1 224 ? 4.428 51.031 26.965 1.00 55.08 ? 224 TYR A C 1 ATOM 1752 O O . TYR A 1 224 ? 4.831 50.881 25.812 1.00 64.61 ? 224 TYR A O 1 ATOM 1753 C CB . TYR A 1 224 ? 4.634 49.192 28.657 1.00 53.44 ? 224 TYR A CB 1 ATOM 1754 C CG . TYR A 1 224 ? 4.988 47.978 27.824 1.00 59.14 ? 224 TYR A CG 1 ATOM 1755 C CD1 . TYR A 1 224 ? 5.936 47.065 28.267 1.00 48.27 ? 224 TYR A CD1 1 ATOM 1756 C CD2 . TYR A 1 224 ? 4.374 47.743 26.601 1.00 54.61 ? 224 TYR A CD2 1 ATOM 1757 C CE1 . TYR A 1 224 ? 6.263 45.952 27.515 1.00 47.59 ? 224 TYR A CE1 1 ATOM 1758 C CE2 . TYR A 1 224 ? 4.697 46.634 25.842 1.00 55.57 ? 224 TYR A CE2 1 ATOM 1759 C CZ . TYR A 1 224 ? 5.641 45.742 26.304 1.00 58.85 ? 224 TYR A CZ 1 ATOM 1760 O OH . TYR A 1 224 ? 5.964 44.637 25.552 1.00 67.52 ? 224 TYR A OH 1 ATOM 1761 N N . SER A 1 225 ? 3.293 51.652 27.266 1.00 52.77 ? 225 SER A N 1 ATOM 1762 C CA . SER A 1 225 ? 2.459 52.289 26.257 1.00 62.62 ? 225 SER A CA 1 ATOM 1763 C C . SER A 1 225 ? 1.913 53.600 26.811 1.00 75.89 ? 225 SER A C 1 ATOM 1764 O O . SER A 1 225 ? 1.739 53.742 28.021 1.00 66.04 ? 225 SER A O 1 ATOM 1765 C CB . SER A 1 225 ? 1.316 51.365 25.836 1.00 71.14 ? 225 SER A CB 1 ATOM 1766 O OG . SER A 1 225 ? 0.518 51.006 26.950 1.00 78.41 ? 225 SER A OG 1 ATOM 1767 N N . VAL A 1 226 ? 1.656 54.563 25.931 1.00 81.38 ? 226 VAL A N 1 ATOM 1768 C CA . VAL A 1 226 ? 1.148 55.862 26.365 1.00 72.22 ? 226 VAL A CA 1 ATOM 1769 C C . VAL A 1 226 ? -0.010 56.357 25.502 1.00 72.19 ? 226 VAL A C 1 ATOM 1770 O O . VAL A 1 226 ? -0.138 55.988 24.335 1.00 86.47 ? 226 VAL A O 1 ATOM 1771 C CB . VAL A 1 226 ? 2.256 56.937 26.358 1.00 63.44 ? 226 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 226 ? 3.309 56.630 27.413 1.00 54.72 ? 226 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 226 ? 2.881 57.056 24.975 1.00 50.19 ? 226 VAL A CG2 1 ATOM 1774 N N . ALA A 1 227 ? -0.848 57.196 26.101 1.00 57.06 ? 227 ALA A N 1 ATOM 1775 C CA . ALA A 1 227 ? -1.965 57.830 25.410 1.00 59.73 ? 227 ALA A CA 1 ATOM 1776 C C . ALA A 1 227 ? -2.316 59.138 26.115 1.00 70.77 ? 227 ALA A C 1 ATOM 1777 O O . ALA A 1 227 ? -1.938 59.343 27.268 1.00 70.36 ? 227 ALA A O 1 ATOM 1778 C CB . ALA A 1 227 ? -3.169 56.900 25.361 1.00 63.52 ? 227 ALA A CB 1 ATOM 1779 N N . VAL A 1 228 ? -3.028 60.025 25.425 1.00 75.01 ? 228 VAL A N 1 ATOM 1780 C CA . VAL A 1 228 ? -3.367 61.328 25.996 1.00 68.15 ? 228 VAL A CA 1 ATOM 1781 C C . VAL A 1 228 ? -4.850 61.686 25.852 1.00 75.28 ? 228 VAL A C 1 ATOM 1782 O O . VAL A 1 228 ? -5.501 61.323 24.874 1.00 84.08 ? 228 VAL A O 1 ATOM 1783 C CB . VAL A 1 228 ? -2.519 62.453 25.362 1.00 63.64 ? 228 VAL A CB 1 ATOM 1784 C CG1 . VAL A 1 228 ? -1.078 62.363 25.832 1.00 61.87 ? 228 VAL A CG1 1 ATOM 1785 C CG2 . VAL A 1 228 ? -2.594 62.388 23.848 1.00 82.47 ? 228 VAL A CG2 1 ATOM 1786 N N . GLY A 1 229 ? -5.362 62.406 26.846 1.00 73.58 ? 229 GLY A N 1 ATOM 1787 C CA . GLY A 1 229 ? -6.743 62.854 26.880 1.00 77.64 ? 229 GLY A CA 1 ATOM 1788 C C . GLY A 1 229 ? -7.003 63.600 28.173 1.00 82.55 ? 229 GLY A C 1 ATOM 1789 O O . GLY A 1 229 ? -6.247 63.455 29.131 1.00 97.07 ? 229 GLY A O 1 ATOM 1790 N N . ASP A 1 230 ? -8.067 64.395 28.224 1.00 85.66 ? 230 ASP A N 1 ATOM 1791 C CA . ASP A 1 230 ? -8.313 65.201 29.421 1.00 90.27 ? 230 ASP A CA 1 ATOM 1792 C C . ASP A 1 230 ? -9.479 64.681 30.257 1.00 95.69 ? 230 ASP A C 1 ATOM 1793 O O . ASP A 1 230 ? -10.644 64.776 29.866 1.00 99.17 ? 230 ASP A O 1 ATOM 1794 C CB . ASP A 1 230 ? -8.554 66.662 29.036 1.00 99.25 ? 230 ASP A CB 1 ATOM 1795 C CG . ASP A 1 230 ? -8.998 67.513 30.211 1.00 106.32 ? 230 ASP A CG 1 ATOM 1796 O OD1 . ASP A 1 230 ? -10.090 68.112 30.113 1.00 104.53 ? 230 ASP A OD1 1 ATOM 1797 O OD2 . ASP A 1 230 ? -8.267 67.585 31.228 1.00 122.82 ? 230 ASP A OD2 1 ATOM 1798 N N . PHE A 1 231 ? -9.139 64.187 31.438 1.00 98.03 ? 231 PHE A N 1 ATOM 1799 C CA . PHE A 1 231 ? -10.095 63.554 32.325 1.00 104.70 ? 231 PHE A CA 1 ATOM 1800 C C . PHE A 1 231 ? -10.427 64.329 33.578 1.00 108.27 ? 231 PHE A C 1 ATOM 1801 O O . PHE A 1 231 ? -11.034 63.798 34.486 1.00 114.19 ? 231 PHE A O 1 ATOM 1802 C CB . PHE A 1 231 ? -9.589 62.182 32.707 1.00 105.58 ? 231 PHE A CB 1 ATOM 1803 C CG . PHE A 1 231 ? -9.076 61.411 31.551 1.00 100.27 ? 231 PHE A CG 1 ATOM 1804 C CD1 . PHE A 1 231 ? -9.801 60.382 31.021 1.00 102.11 ? 231 PHE A CD1 1 ATOM 1805 C CD2 . PHE A 1 231 ? -7.895 61.754 30.970 1.00 93.30 ? 231 PHE A CD2 1 ATOM 1806 C CE1 . PHE A 1 231 ? -9.343 59.686 29.942 1.00 96.22 ? 231 PHE A CE1 1 ATOM 1807 C CE2 . PHE A 1 231 ? -7.422 61.057 29.896 1.00 93.24 ? 231 PHE A CE2 1 ATOM 1808 C CZ . PHE A 1 231 ? -8.150 60.022 29.378 1.00 94.18 ? 231 PHE A CZ 1 ATOM 1809 N N . ASN A 1 232 ? -10.033 65.586 33.628 1.00 115.93 ? 232 ASN A N 1 ATOM 1810 C CA . ASN A 1 232 ? -10.513 66.510 34.654 1.00 116.38 ? 232 ASN A CA 1 ATOM 1811 C C . ASN A 1 232 ? -11.123 67.764 34.045 1.00 110.41 ? 232 ASN A C 1 ATOM 1812 O O . ASN A 1 232 ? -11.242 67.878 32.824 1.00 110.86 ? 232 ASN A O 1 ATOM 1813 C CB . ASN A 1 232 ? -9.378 66.891 35.612 1.00 107.44 ? 232 ASN A CB 1 ATOM 1814 C CG . ASN A 1 232 ? -8.084 67.158 34.887 1.00 102.79 ? 232 ASN A CG 1 ATOM 1815 O OD1 . ASN A 1 232 ? -8.058 67.165 33.662 1.00 112.43 ? 232 ASN A OD1 1 ATOM 1816 N ND2 . ASN A 1 232 ? -7.002 67.373 35.631 1.00 100.96 ? 232 ASN A ND2 1 ATOM 1817 N N . GLY A 1 233 ? -11.517 68.688 34.914 1.00 113.41 ? 233 GLY A N 1 ATOM 1818 C CA . GLY A 1 233 ? -12.209 69.894 34.508 1.00 127.98 ? 233 GLY A CA 1 ATOM 1819 C C . GLY A 1 233 ? -11.434 70.785 33.560 1.00 143.15 ? 233 GLY A C 1 ATOM 1820 O O . GLY A 1 233 ? -12.032 71.503 32.760 1.00 154.65 ? 233 GLY A O 1 ATOM 1821 N N . ASP A 1 234 ? -10.107 70.754 33.642 1.00 141.11 ? 234 ASP A N 1 ATOM 1822 C CA . ASP A 1 234 ? -9.312 71.640 32.792 1.00 121.95 ? 234 ASP A CA 1 ATOM 1823 C C . ASP A 1 234 ? -9.417 71.267 31.316 1.00 107.17 ? 234 ASP A C 1 ATOM 1824 O O . ASP A 1 234 ? -10.135 70.341 30.952 1.00 100.93 ? 234 ASP A O 1 ATOM 1825 C CB . ASP A 1 234 ? -7.843 71.634 33.232 1.00 104.13 ? 234 ASP A CB 1 ATOM 1826 C CG . ASP A 1 234 ? -7.281 70.229 33.406 1.00 121.01 ? 234 ASP A CG 1 ATOM 1827 O OD1 . ASP A 1 234 ? -7.548 69.348 32.559 1.00 137.35 ? 234 ASP A OD1 1 ATOM 1828 O OD2 . ASP A 1 234 ? -6.564 70.006 34.404 1.00 126.06 ? 234 ASP A OD2 1 ATOM 1829 N N . GLY A 1 235 ? -8.707 72.003 30.467 1.00 102.44 ? 235 GLY A N 1 ATOM 1830 C CA . GLY A 1 235 ? -8.730 71.744 29.039 1.00 102.43 ? 235 GLY A CA 1 ATOM 1831 C C . GLY A 1 235 ? -7.463 71.082 28.537 1.00 107.97 ? 235 GLY A C 1 ATOM 1832 O O . GLY A 1 235 ? -7.339 70.772 27.352 1.00 132.71 ? 235 GLY A O 1 ATOM 1833 N N . ILE A 1 236 ? -6.521 70.861 29.446 1.00 103.32 ? 236 ILE A N 1 ATOM 1834 C CA . ILE A 1 236 ? -5.225 70.304 29.085 1.00 103.99 ? 236 ILE A CA 1 ATOM 1835 C C . ILE A 1 236 ? -5.261 68.779 29.064 1.00 100.24 ? 236 ILE A C 1 ATOM 1836 O O . ILE A 1 236 ? -5.781 68.149 29.987 1.00 86.77 ? 236 ILE A O 1 ATOM 1837 C CB . ILE A 1 236 ? -4.119 70.771 30.056 1.00 107.67 ? 236 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 236 ? -4.115 72.298 30.178 1.00 94.06 ? 236 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 236 ? -2.756 70.269 29.603 1.00 115.33 ? 236 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 236 ? -4.846 72.823 31.400 1.00 98.40 ? 236 ILE A CD1 1 ATOM 1841 N N . ASP A 1 237 ? -4.712 68.198 28.000 1.00 117.12 ? 237 ASP A N 1 ATOM 1842 C CA . ASP A 1 237 ? -4.600 66.749 27.877 1.00 91.57 ? 237 ASP A CA 1 ATOM 1843 C C . ASP A 1 237 ? -3.801 66.167 29.035 1.00 78.77 ? 237 ASP A C 1 ATOM 1844 O O . ASP A 1 237 ? -2.735 66.675 29.385 1.00 80.49 ? 237 ASP A O 1 ATOM 1845 C CB . ASP A 1 237 ? -3.942 66.369 26.547 1.00 85.23 ? 237 ASP A CB 1 ATOM 1846 C CG . ASP A 1 237 ? -4.780 66.760 25.345 1.00 123.80 ? 237 ASP A CG 1 ATOM 1847 O OD1 . ASP A 1 237 ? -4.580 66.170 24.262 1.00 138.12 ? 237 ASP A OD1 1 ATOM 1848 O OD2 . ASP A 1 237 ? -5.641 67.655 25.481 1.00 134.58 ? 237 ASP A OD2 1 ATOM 1849 N N . ASP A 1 238 ? -4.323 65.100 29.629 1.00 80.39 ? 238 ASP A N 1 ATOM 1850 C CA . ASP A 1 238 ? -3.649 64.440 30.737 1.00 80.97 ? 238 ASP A CA 1 ATOM 1851 C C . ASP A 1 238 ? -2.964 63.171 30.240 1.00 89.84 ? 238 ASP A C 1 ATOM 1852 O O . ASP A 1 238 ? -3.085 62.815 29.067 1.00 82.92 ? 238 ASP A O 1 ATOM 1853 C CB . ASP A 1 238 ? -4.647 64.138 31.855 1.00 86.43 ? 238 ASP A CB 1 ATOM 1854 C CG . ASP A 1 238 ? -5.328 65.394 32.376 1.00 105.75 ? 238 ASP A CG 1 ATOM 1855 O OD1 . ASP A 1 238 ? -4.617 66.385 32.640 1.00 122.53 ? 238 ASP A OD1 1 ATOM 1856 O OD2 . ASP A 1 238 ? -6.569 65.402 32.504 1.00 110.67 ? 238 ASP A OD2 1 ATOM 1857 N N . PHE A 1 239 ? -2.254 62.485 31.130 1.00 95.86 ? 239 PHE A N 1 ATOM 1858 C CA . PHE A 1 239 ? -1.374 61.396 30.715 1.00 73.14 ? 239 PHE A CA 1 ATOM 1859 C C . PHE A 1 239 ? -1.908 60.019 31.091 1.00 75.16 ? 239 PHE A C 1 ATOM 1860 O O . PHE A 1 239 ? -2.158 59.741 32.261 1.00 79.36 ? 239 PHE A O 1 ATOM 1861 C CB . PHE A 1 239 ? 0.019 61.591 31.321 1.00 71.38 ? 239 PHE A CB 1 ATOM 1862 C CG . PHE A 1 239 ? 0.656 62.906 30.968 1.00 73.20 ? 239 PHE A CG 1 ATOM 1863 C CD1 . PHE A 1 239 ? 1.451 63.577 31.884 1.00 70.98 ? 239 PHE A CD1 1 ATOM 1864 C CD2 . PHE A 1 239 ? 0.460 63.472 29.719 1.00 67.66 ? 239 PHE A CD2 1 ATOM 1865 C CE1 . PHE A 1 239 ? 2.036 64.786 31.562 1.00 75.07 ? 239 PHE A CE1 1 ATOM 1866 C CE2 . PHE A 1 239 ? 1.044 64.680 29.391 1.00 67.07 ? 239 PHE A CE2 1 ATOM 1867 C CZ . PHE A 1 239 ? 1.831 65.338 30.312 1.00 82.30 ? 239 PHE A CZ 1 ATOM 1868 N N . VAL A 1 240 ? -2.075 59.161 30.089 1.00 72.44 ? 240 VAL A N 1 ATOM 1869 C CA . VAL A 1 240 ? -2.471 57.774 30.309 1.00 71.38 ? 240 VAL A CA 1 ATOM 1870 C C . VAL A 1 240 ? -1.337 56.837 29.912 1.00 79.76 ? 240 VAL A C 1 ATOM 1871 O O . VAL A 1 240 ? -0.846 56.892 28.785 1.00 77.84 ? 240 VAL A O 1 ATOM 1872 C CB . VAL A 1 240 ? -3.734 57.406 29.513 1.00 71.18 ? 240 VAL A CB 1 ATOM 1873 C CG1 . VAL A 1 240 ? -4.130 55.962 29.777 1.00 71.53 ? 240 VAL A CG1 1 ATOM 1874 C CG2 . VAL A 1 240 ? -4.861 58.331 29.875 1.00 76.16 ? 240 VAL A CG2 1 ATOM 1875 N N . SER A 1 241 ? -0.922 55.981 30.839 1.00 68.69 ? 241 SER A N 1 ATOM 1876 C CA . SER A 1 241 ? 0.182 55.068 30.579 1.00 68.90 ? 241 SER A CA 1 ATOM 1877 C C . SER A 1 241 ? -0.114 53.658 31.063 1.00 64.29 ? 241 SER A C 1 ATOM 1878 O O . SER A 1 241 ? -0.557 53.455 32.194 1.00 68.72 ? 241 SER A O 1 ATOM 1879 C CB . SER A 1 241 ? 1.465 55.575 31.238 1.00 70.41 ? 241 SER A CB 1 ATOM 1880 O OG . SER A 1 241 ? 2.542 54.682 31.011 1.00 71.99 ? 241 SER A OG 1 ATOM 1881 N N . GLY A 1 242 ? 0.129 52.685 30.193 1.00 60.15 ? 242 GLY A N 1 ATOM 1882 C CA . GLY A 1 242 ? 0.026 51.291 30.571 1.00 64.19 ? 242 GLY A CA 1 ATOM 1883 C C . GLY A 1 242 ? 1.242 50.863 31.369 1.00 77.01 ? 242 GLY A C 1 ATOM 1884 O O . GLY A 1 242 ? 2.367 51.262 31.066 1.00 93.10 ? 242 GLY A O 1 ATOM 1885 N N . VAL A 1 243 ? 1.011 50.053 32.395 1.00 72.62 ? 243 VAL A N 1 ATOM 1886 C CA . VAL A 1 243 ? 2.090 49.512 33.207 1.00 81.00 ? 243 VAL A CA 1 ATOM 1887 C C . VAL A 1 243 ? 1.749 48.042 33.506 1.00 62.18 ? 243 VAL A C 1 ATOM 1888 O O . VAL A 1 243 ? 1.197 47.703 34.555 1.00 64.94 ? 243 VAL A O 1 ATOM 1889 C CB . VAL A 1 243 ? 2.317 50.377 34.487 1.00 69.05 ? 243 VAL A CB 1 ATOM 1890 C CG1 . VAL A 1 243 ? 1.010 50.672 35.212 1.00 73.83 ? 243 VAL A CG1 1 ATOM 1891 C CG2 . VAL A 1 243 ? 3.349 49.758 35.409 1.00 83.65 ? 243 VAL A CG2 1 ATOM 1892 N N . PRO A 1 244 ? 2.072 47.162 32.545 1.00 58.30 ? 244 PRO A N 1 ATOM 1893 C CA . PRO A 1 244 ? 1.584 45.780 32.424 1.00 61.18 ? 244 PRO A CA 1 ATOM 1894 C C . PRO A 1 244 ? 2.072 44.797 33.488 1.00 59.01 ? 244 PRO A C 1 ATOM 1895 O O . PRO A 1 244 ? 1.371 43.827 33.775 1.00 74.08 ? 244 PRO A O 1 ATOM 1896 C CB . PRO A 1 244 ? 2.100 45.356 31.046 1.00 53.52 ? 244 PRO A CB 1 ATOM 1897 C CG . PRO A 1 244 ? 3.315 46.183 30.833 1.00 53.11 ? 244 PRO A CG 1 ATOM 1898 C CD . PRO A 1 244 ? 3.021 47.505 31.471 1.00 55.43 ? 244 PRO A CD 1 ATOM 1899 N N . ARG A 1 245 ? 3.252 45.028 34.050 1.00 59.29 ? 245 ARG A N 1 ATOM 1900 C CA . ARG A 1 245 ? 3.806 44.103 35.031 1.00 60.79 ? 245 ARG A CA 1 ATOM 1901 C C . ARG A 1 245 ? 3.512 44.517 36.471 1.00 64.71 ? 245 ARG A C 1 ATOM 1902 O O . ARG A 1 245 ? 3.913 43.828 37.409 1.00 87.04 ? 245 ARG A O 1 ATOM 1903 C CB . ARG A 1 245 ? 5.316 43.966 34.840 1.00 60.83 ? 245 ARG A CB 1 ATOM 1904 C CG . ARG A 1 245 ? 5.743 42.923 33.825 1.00 73.05 ? 245 ARG A CG 1 ATOM 1905 C CD . ARG A 1 245 ? 7.227 42.625 33.967 1.00 64.68 ? 245 ARG A CD 1 ATOM 1906 N NE . ARG A 1 245 ? 7.582 42.318 35.351 1.00 81.87 ? 245 ARG A NE 1 ATOM 1907 C CZ . ARG A 1 245 ? 7.585 41.094 35.870 1.00 76.97 ? 245 ARG A CZ 1 ATOM 1908 N NH1 . ARG A 1 245 ? 7.258 40.050 35.120 1.00 59.94 ? 245 ARG A NH1 1 ATOM 1909 N NH2 . ARG A 1 245 ? 7.918 40.913 37.142 1.00 81.42 ? 245 ARG A NH2 1 ATOM 1910 N N . ALA A 1 246 ? 2.815 45.636 36.646 1.00 67.32 ? 246 ALA A N 1 ATOM 1911 C CA . ALA A 1 246 ? 2.550 46.159 37.984 1.00 75.25 ? 246 ALA A CA 1 ATOM 1912 C C . ALA A 1 246 ? 1.497 45.339 38.716 1.00 77.76 ? 246 ALA A C 1 ATOM 1913 O O . ALA A 1 246 ? 0.935 44.398 38.154 1.00 79.94 ? 246 ALA A O 1 ATOM 1914 C CB . ALA A 1 246 ? 2.116 47.609 37.908 1.00 91.36 ? 246 ALA A CB 1 ATOM 1915 N N . ALA A 1 247 ? 1.232 45.721 39.965 1.00 81.24 ? 247 ALA A N 1 ATOM 1916 C CA . ALA A 1 247 ? 0.248 45.046 40.811 1.00 76.58 ? 247 ALA A CA 1 ATOM 1917 C C . ALA A 1 247 ? 0.471 43.539 40.832 1.00 78.15 ? 247 ALA A C 1 ATOM 1918 O O . ALA A 1 247 ? -0.445 42.775 40.537 1.00 79.79 ? 247 ALA A O 1 ATOM 1919 C CB . ALA A 1 247 ? -1.164 45.364 40.344 1.00 78.23 ? 247 ALA A CB 1 ATOM 1920 N N . ARG A 1 248 ? 1.696 43.134 41.170 1.00 85.03 ? 248 ARG A N 1 ATOM 1921 C CA . ARG A 1 248 ? 2.153 41.737 41.123 1.00 90.45 ? 248 ARG A CA 1 ATOM 1922 C C . ARG A 1 248 ? 1.705 41.045 39.833 1.00 72.84 ? 248 ARG A C 1 ATOM 1923 O O . ARG A 1 248 ? 1.080 39.988 39.866 1.00 65.92 ? 248 ARG A O 1 ATOM 1924 C CB . ARG A 1 248 ? 1.721 40.935 42.374 1.00 91.82 ? 248 ARG A CB 1 ATOM 1925 C CG . ARG A 1 248 ? 0.289 41.083 42.886 1.00 101.27 ? 248 ARG A CG 1 ATOM 1926 C CD . ARG A 1 248 ? -0.596 39.935 42.430 1.00 117.51 ? 248 ARG A CD 1 ATOM 1927 N NE . ARG A 1 248 ? -1.966 40.067 42.917 1.00 125.30 ? 248 ARG A NE 1 ATOM 1928 C CZ . ARG A 1 248 ? -2.920 39.165 42.713 1.00 125.79 ? 248 ARG A CZ 1 ATOM 1929 N NH1 . ARG A 1 248 ? -2.656 38.059 42.029 1.00 118.62 ? 248 ARG A NH1 1 ATOM 1930 N NH2 . ARG A 1 248 ? -4.139 39.366 43.191 1.00 118.05 ? 248 ARG A NH2 1 ATOM 1931 N N . THR A 1 249 ? 2.016 41.698 38.712 1.00 71.87 ? 249 THR A N 1 ATOM 1932 C CA . THR A 1 249 ? 1.832 41.195 37.343 1.00 67.32 ? 249 THR A CA 1 ATOM 1933 C C . THR A 1 249 ? 0.366 41.213 36.881 1.00 68.23 ? 249 THR A C 1 ATOM 1934 O O . THR A 1 249 ? 0.072 40.909 35.721 1.00 60.79 ? 249 THR A O 1 ATOM 1935 C CB . THR A 1 249 ? 2.452 39.767 37.164 1.00 63.05 ? 249 THR A CB 1 ATOM 1936 O OG1 . THR A 1 249 ? 3.162 39.703 35.922 1.00 79.43 ? 249 THR A OG1 1 ATOM 1937 C CG2 . THR A 1 249 ? 1.403 38.667 37.194 1.00 68.74 ? 249 THR A CG2 1 ATOM 1938 N N . LEU A 1 250 ? -0.547 41.605 37.769 1.00 76.67 ? 250 LEU A N 1 ATOM 1939 C CA . LEU A 1 250 ? -1.944 41.829 37.381 1.00 79.14 ? 250 LEU A CA 1 ATOM 1940 C C . LEU A 1 250 ? -2.056 42.877 36.277 1.00 69.77 ? 250 LEU A C 1 ATOM 1941 O O . LEU A 1 250 ? -2.943 42.808 35.426 1.00 65.21 ? 250 LEU A O 1 ATOM 1942 C CB . LEU A 1 250 ? -2.786 42.267 38.583 1.00 69.59 ? 250 LEU A CB 1 ATOM 1943 C CG . LEU A 1 250 ? -3.374 41.194 39.502 1.00 78.25 ? 250 LEU A CG 1 ATOM 1944 C CD1 . LEU A 1 250 ? -4.025 41.834 40.719 1.00 73.44 ? 250 LEU A CD1 1 ATOM 1945 C CD2 . LEU A 1 250 ? -4.380 40.338 38.750 1.00 93.51 ? 250 LEU A CD2 1 ATOM 1946 N N . GLY A 1 251 ? -1.149 43.848 36.303 1.00 70.78 ? 251 GLY A N 1 ATOM 1947 C CA . GLY A 1 251 ? -1.135 44.923 35.328 1.00 69.86 ? 251 GLY A CA 1 ATOM 1948 C C . GLY A 1 251 ? -1.978 46.103 35.765 1.00 73.84 ? 251 GLY A C 1 ATOM 1949 O O . GLY A 1 251 ? -2.988 45.938 36.448 1.00 88.58 ? 251 GLY A O 1 ATOM 1950 N N . MET A 1 252 ? -1.564 47.300 35.362 1.00 71.16 ? 252 MET A N 1 ATOM 1951 C CA . MET A 1 252 ? -2.272 48.521 35.730 1.00 76.06 ? 252 MET A CA 1 ATOM 1952 C C . MET A 1 252 ? -2.227 49.574 34.627 1.00 75.24 ? 252 MET A C 1 ATOM 1953 O O . MET A 1 252 ? -1.462 49.459 33.668 1.00 70.40 ? 252 MET A O 1 ATOM 1954 C CB . MET A 1 252 ? -1.697 49.111 37.022 1.00 80.03 ? 252 MET A CB 1 ATOM 1955 C CG . MET A 1 252 ? -2.246 48.500 38.299 1.00 82.53 ? 252 MET A CG 1 ATOM 1956 S SD . MET A 1 252 ? -1.762 49.446 39.755 1.00 88.11 ? 252 MET A SD 1 ATOM 1957 C CE . MET A 1 252 ? -2.720 48.629 41.027 1.00 126.13 ? 252 MET A CE 1 ATOM 1958 N N . VAL A 1 253 ? -3.074 50.588 34.762 1.00 79.97 ? 253 VAL A N 1 ATOM 1959 C CA . VAL A 1 253 ? -3.027 51.757 33.893 1.00 79.05 ? 253 VAL A CA 1 ATOM 1960 C C . VAL A 1 253 ? -3.109 53.029 34.729 1.00 85.54 ? 253 VAL A C 1 ATOM 1961 O O . VAL A 1 253 ? -4.095 53.259 35.428 1.00 92.98 ? 253 VAL A O 1 ATOM 1962 C CB . VAL A 1 253 ? -4.162 51.744 32.853 1.00 77.28 ? 253 VAL A CB 1 ATOM 1963 C CG1 . VAL A 1 253 ? -4.313 53.112 32.210 1.00 77.32 ? 253 VAL A CG1 1 ATOM 1964 C CG2 . VAL A 1 253 ? -3.889 50.692 31.797 1.00 70.61 ? 253 VAL A CG2 1 ATOM 1965 N N . TYR A 1 254 ? -2.066 53.849 34.656 1.00 83.59 ? 254 TYR A N 1 ATOM 1966 C CA . TYR A 1 254 ? -2.004 55.079 35.435 1.00 87.92 ? 254 TYR A CA 1 ATOM 1967 C C . TYR A 1 254 ? -2.502 56.278 34.633 1.00 86.89 ? 254 TYR A C 1 ATOM 1968 O O . TYR A 1 254 ? -2.244 56.385 33.434 1.00 81.78 ? 254 TYR A O 1 ATOM 1969 C CB . TYR A 1 254 ? -0.573 55.343 35.918 1.00 85.66 ? 254 TYR A CB 1 ATOM 1970 C CG . TYR A 1 254 ? -0.009 54.298 36.860 1.00 87.51 ? 254 TYR A CG 1 ATOM 1971 C CD1 . TYR A 1 254 ? -0.834 53.380 37.498 1.00 92.16 ? 254 TYR A CD1 1 ATOM 1972 C CD2 . TYR A 1 254 ? 1.355 54.240 37.118 1.00 85.00 ? 254 TYR A CD2 1 ATOM 1973 C CE1 . TYR A 1 254 ? -0.314 52.429 38.358 1.00 92.03 ? 254 TYR A CE1 1 ATOM 1974 C CE2 . TYR A 1 254 ? 1.883 53.295 37.976 1.00 86.84 ? 254 TYR A CE2 1 ATOM 1975 C CZ . TYR A 1 254 ? 1.044 52.392 38.593 1.00 89.57 ? 254 TYR A CZ 1 ATOM 1976 O OH . TYR A 1 254 ? 1.571 51.452 39.448 1.00 87.58 ? 254 TYR A OH 1 ATOM 1977 N N . ILE A 1 255 ? -3.221 57.175 35.300 1.00 91.70 ? 255 ILE A N 1 ATOM 1978 C CA . ILE A 1 255 ? -3.605 58.442 34.690 1.00 90.90 ? 255 ILE A CA 1 ATOM 1979 C C . ILE A 1 255 ? -3.038 59.603 35.499 1.00 92.14 ? 255 ILE A C 1 ATOM 1980 O O . ILE A 1 255 ? -3.376 59.783 36.669 1.00 99.65 ? 255 ILE A O 1 ATOM 1981 C CB . ILE A 1 255 ? -5.136 58.587 34.569 1.00 94.71 ? 255 ILE A CB 1 ATOM 1982 C CG1 . ILE A 1 255 ? -5.678 57.608 33.527 1.00 91.88 ? 255 ILE A CG1 1 ATOM 1983 C CG2 . ILE A 1 255 ? -5.505 60.008 34.180 1.00 93.84 ? 255 ILE A CG2 1 ATOM 1984 C CD1 . ILE A 1 255 ? -7.140 57.815 33.184 1.00 94.91 ? 255 ILE A CD1 1 ATOM 1985 N N . TYR A 1 256 ? -2.165 60.384 34.868 1.00 87.69 ? 256 TYR A N 1 ATOM 1986 C CA . TYR A 1 256 ? -1.539 61.527 35.522 1.00 88.05 ? 256 TYR A CA 1 ATOM 1987 C C . TYR A 1 256 ? -2.087 62.838 34.971 1.00 92.23 ? 256 TYR A C 1 ATOM 1988 O O . TYR A 1 256 ? -2.459 62.920 33.802 1.00 105.11 ? 256 TYR A O 1 ATOM 1989 C CB . TYR A 1 256 ? -0.019 61.490 35.349 1.00 83.69 ? 256 TYR A CB 1 ATOM 1990 C CG . TYR A 1 256 ? 0.667 60.337 36.045 1.00 83.30 ? 256 TYR A CG 1 ATOM 1991 C CD1 . TYR A 1 256 ? 1.150 59.254 35.325 1.00 79.68 ? 256 TYR A CD1 1 ATOM 1992 C CD2 . TYR A 1 256 ? 0.835 60.333 37.422 1.00 86.62 ? 256 TYR A CD2 1 ATOM 1993 C CE1 . TYR A 1 256 ? 1.781 58.200 35.958 1.00 79.83 ? 256 TYR A CE1 1 ATOM 1994 C CE2 . TYR A 1 256 ? 1.464 59.287 38.064 1.00 86.51 ? 256 TYR A CE2 1 ATOM 1995 C CZ . TYR A 1 256 ? 1.935 58.222 37.327 1.00 83.49 ? 256 TYR A CZ 1 ATOM 1996 O OH . TYR A 1 256 ? 2.561 57.177 37.965 1.00 97.22 ? 256 TYR A OH 1 ATOM 1997 N N . ASP A 1 257 ? -2.134 63.860 35.820 1.00 90.37 ? 257 ASP A N 1 ATOM 1998 C CA . ASP A 1 257 ? -2.622 65.177 35.420 1.00 99.96 ? 257 ASP A CA 1 ATOM 1999 C C . ASP A 1 257 ? -1.671 65.832 34.415 1.00 98.54 ? 257 ASP A C 1 ATOM 2000 O O . ASP A 1 257 ? -0.476 65.538 34.396 1.00 106.99 ? 257 ASP A O 1 ATOM 2001 C CB . ASP A 1 257 ? -2.803 66.071 36.651 1.00 96.29 ? 257 ASP A CB 1 ATOM 2002 C CG . ASP A 1 257 ? -3.448 67.401 36.321 1.00 105.21 ? 257 ASP A CG 1 ATOM 2003 O OD1 . ASP A 1 257 ? -4.687 67.509 36.435 1.00 116.93 ? 257 ASP A OD1 1 ATOM 2004 O OD2 . ASP A 1 257 ? -2.714 68.339 35.948 1.00 116.61 ? 257 ASP A OD2 1 ATOM 2005 N N . GLY A 1 258 ? -2.211 66.712 33.576 1.00 95.25 ? 258 GLY A N 1 ATOM 2006 C CA . GLY A 1 258 ? -1.431 67.354 32.532 1.00 92.97 ? 258 GLY A CA 1 ATOM 2007 C C . GLY A 1 258 ? -0.637 68.561 32.994 1.00 96.68 ? 258 GLY A C 1 ATOM 2008 O O . GLY A 1 258 ? 0.418 68.866 32.439 1.00 83.67 ? 258 GLY A O 1 ATOM 2009 N N . LYS A 1 259 ? -1.145 69.257 34.006 1.00 100.76 ? 259 LYS A N 1 ATOM 2010 C CA . LYS A 1 259 ? -0.467 70.428 34.556 1.00 86.32 ? 259 LYS A CA 1 ATOM 2011 C C . LYS A 1 259 ? 0.706 69.996 35.426 1.00 90.39 ? 259 LYS A C 1 ATOM 2012 O O . LYS A 1 259 ? 1.854 70.344 35.155 1.00 94.71 ? 259 LYS A O 1 ATOM 2013 C CB . LYS A 1 259 ? -1.438 71.297 35.355 1.00 89.39 ? 259 LYS A CB 1 ATOM 2014 C CG . LYS A 1 259 ? -2.592 71.840 34.528 1.00 100.90 ? 259 LYS A CG 1 ATOM 2015 C CD . LYS A 1 259 ? -3.317 72.963 35.248 1.00 115.72 ? 259 LYS A CD 1 ATOM 2016 C CE . LYS A 1 259 ? -2.408 74.165 35.443 1.00 118.26 ? 259 LYS A CE 1 ATOM 2017 N NZ . LYS A 1 259 ? -3.122 75.305 36.081 1.00 129.65 ? 259 LYS A NZ 1 ATOM 2018 N N . ASN A 1 260 ? 0.405 69.251 36.483 1.00 99.32 ? 260 ASN A N 1 ATOM 2019 C CA . ASN A 1 260 ? 1.430 68.673 37.342 1.00 89.29 ? 260 ASN A CA 1 ATOM 2020 C C . ASN A 1 260 ? 1.321 67.152 37.322 1.00 110.76 ? 260 ASN A C 1 ATOM 2021 O O . ASN A 1 260 ? 0.306 66.603 36.899 1.00 119.57 ? 260 ASN A O 1 ATOM 2022 C CB . ASN A 1 260 ? 1.321 69.214 38.769 1.00 91.49 ? 260 ASN A CB 1 ATOM 2023 C CG . ASN A 1 260 ? -0.080 69.108 39.332 1.00 130.44 ? 260 ASN A CG 1 ATOM 2024 O OD1 . ASN A 1 260 ? -1.028 68.790 38.614 1.00 140.05 ? 260 ASN A OD1 1 ATOM 2025 N ND2 . ASN A 1 260 ? -0.218 69.381 40.628 1.00 172.82 ? 260 ASN A ND2 1 ATOM 2026 N N . MET A 1 261 ? 2.367 66.472 37.775 1.00 103.27 ? 261 MET A N 1 ATOM 2027 C CA . MET A 1 261 ? 2.507 65.040 37.532 1.00 92.98 ? 261 MET A CA 1 ATOM 2028 C C . MET A 1 261 ? 1.710 64.189 38.520 1.00 88.08 ? 261 MET A C 1 ATOM 2029 O O . MET A 1 261 ? 1.814 62.964 38.512 1.00 87.79 ? 261 MET A O 1 ATOM 2030 C CB . MET A 1 261 ? 3.985 64.644 37.571 1.00 116.13 ? 261 MET A CB 1 ATOM 2031 C CG . MET A 1 261 ? 4.341 63.496 36.640 1.00 108.93 ? 261 MET A CG 1 ATOM 2032 S SD . MET A 1 261 ? 3.646 63.723 34.991 1.00 115.10 ? 261 MET A SD 1 ATOM 2033 C CE . MET A 1 261 ? 4.405 62.366 34.107 1.00 70.22 ? 261 MET A CE 1 ATOM 2034 N N . SER A 1 262 ? 0.935 64.846 39.379 1.00 107.67 ? 262 SER A N 1 ATOM 2035 C CA . SER A 1 262 ? 0.083 64.157 40.348 1.00 107.83 ? 262 SER A CA 1 ATOM 2036 C C . SER A 1 262 ? -0.844 63.136 39.691 1.00 100.28 ? 262 SER A C 1 ATOM 2037 O O . SER A 1 262 ? -1.352 63.361 38.593 1.00 101.64 ? 262 SER A O 1 ATOM 2038 C CB . SER A 1 262 ? -0.754 65.170 41.128 1.00 101.27 ? 262 SER A CB 1 ATOM 2039 O OG . SER A 1 262 ? -1.666 65.831 40.267 1.00 99.74 ? 262 SER A OG 1 ATOM 2040 N N . SER A 1 263 ? -1.053 62.014 40.373 1.00 97.12 ? 263 SER A N 1 ATOM 2041 C CA . SER A 1 263 ? -1.926 60.953 39.883 1.00 98.54 ? 263 SER A CA 1 ATOM 2042 C C . SER A 1 263 ? -3.394 61.368 39.926 1.00 102.16 ? 263 SER A C 1 ATOM 2043 O O . SER A 1 263 ? -3.783 62.221 40.724 1.00 116.95 ? 263 SER A O 1 ATOM 2044 C CB . SER A 1 263 ? -1.718 59.676 40.702 1.00 99.56 ? 263 SER A CB 1 ATOM 2045 O OG . SER A 1 263 ? -2.654 58.675 40.342 1.00 102.00 ? 263 SER A OG 1 ATOM 2046 N N . LEU A 1 264 ? -4.204 60.759 39.065 1.00 103.23 ? 264 LEU A N 1 ATOM 2047 C CA . LEU A 1 264 ? -5.635 61.045 39.020 1.00 107.06 ? 264 LEU A CA 1 ATOM 2048 C C . LEU A 1 264 ? -6.464 59.784 39.245 1.00 110.93 ? 264 LEU A C 1 ATOM 2049 O O . LEU A 1 264 ? -7.149 59.654 40.259 1.00 118.73 ? 264 LEU A O 1 ATOM 2050 C CB . LEU A 1 264 ? -6.014 61.686 37.684 1.00 105.38 ? 264 LEU A CB 1 ATOM 2051 C CG . LEU A 1 264 ? -5.520 63.115 37.450 1.00 102.78 ? 264 LEU A CG 1 ATOM 2052 C CD1 . LEU A 1 264 ? -5.977 63.630 36.094 1.00 100.59 ? 264 LEU A CD1 1 ATOM 2053 C CD2 . LEU A 1 264 ? -6.001 64.030 38.563 1.00 112.72 ? 264 LEU A CD2 1 ATOM 2054 N N . TYR A 1 265 ? -6.400 58.862 38.290 1.00 110.07 ? 265 TYR A N 1 ATOM 2055 C CA . TYR A 1 265 ? -7.157 57.617 38.371 1.00 113.73 ? 265 TYR A CA 1 ATOM 2056 C C . TYR A 1 265 ? -6.271 56.400 38.132 1.00 111.00 ? 265 TYR A C 1 ATOM 2057 O O . TYR A 1 265 ? -5.179 56.512 37.577 1.00 105.65 ? 265 TYR A O 1 ATOM 2058 C CB . TYR A 1 265 ? -8.306 57.621 37.362 1.00 116.75 ? 265 TYR A CB 1 ATOM 2059 C CG . TYR A 1 265 ? -9.282 58.756 37.551 1.00 126.45 ? 265 TYR A CG 1 ATOM 2060 C CD1 . TYR A 1 265 ? -10.339 58.645 38.443 1.00 133.72 ? 265 TYR A CD1 1 ATOM 2061 C CD2 . TYR A 1 265 ? -9.146 59.939 36.837 1.00 128.83 ? 265 TYR A CD2 1 ATOM 2062 C CE1 . TYR A 1 265 ? -11.235 59.681 38.620 1.00 134.05 ? 265 TYR A CE1 1 ATOM 2063 C CE2 . TYR A 1 265 ? -10.037 60.980 37.007 1.00 131.92 ? 265 TYR A CE2 1 ATOM 2064 C CZ . TYR A 1 265 ? -11.079 60.846 37.899 1.00 134.97 ? 265 TYR A CZ 1 ATOM 2065 O OH . TYR A 1 265 ? -11.969 61.881 38.071 1.00 145.06 ? 265 TYR A OH 1 ATOM 2066 N N . ASN A 1 266 ? -6.756 55.236 38.552 1.00 115.88 ? 266 ASN A N 1 ATOM 2067 C CA . ASN A 1 266 ? -6.048 53.980 38.334 1.00 109.00 ? 266 ASN A CA 1 ATOM 2068 C C . ASN A 1 266 ? -6.938 52.906 37.720 1.00 106.68 ? 266 ASN A C 1 ATOM 2069 O O . ASN A 1 266 ? -8.158 52.928 37.876 1.00 110.05 ? 266 ASN A O 1 ATOM 2070 C CB . ASN A 1 266 ? -5.462 53.457 39.646 1.00 106.29 ? 266 ASN A CB 1 ATOM 2071 C CG . ASN A 1 266 ? -4.118 54.071 39.974 1.00 104.50 ? 266 ASN A CG 1 ATOM 2072 O OD1 . ASN A 1 266 ? -3.453 54.644 39.111 1.00 102.64 ? 266 ASN A OD1 1 ATOM 2073 N ND2 . ASN A 1 266 ? -3.707 53.946 41.230 1.00 108.84 ? 266 ASN A ND2 1 ATOM 2074 N N . PHE A 1 267 ? -6.311 51.969 37.022 1.00 100.08 ? 267 PHE A N 1 ATOM 2075 C CA . PHE A 1 267 ? -6.998 50.799 36.495 1.00 96.20 ? 267 PHE A CA 1 ATOM 2076 C C . PHE A 1 267 ? -6.176 49.562 36.825 1.00 90.68 ? 267 PHE A C 1 ATOM 2077 O O . PHE A 1 267 ? -4.954 49.638 36.924 1.00 88.53 ? 267 PHE A O 1 ATOM 2078 C CB . PHE A 1 267 ? -7.212 50.923 34.985 1.00 96.16 ? 267 PHE A CB 1 ATOM 2079 C CG . PHE A 1 267 ? -8.195 51.991 34.598 1.00 97.17 ? 267 PHE A CG 1 ATOM 2080 C CD1 . PHE A 1 267 ? -7.784 53.303 34.433 1.00 98.85 ? 267 PHE A CD1 1 ATOM 2081 C CD2 . PHE A 1 267 ? -9.530 51.681 34.401 1.00 98.83 ? 267 PHE A CD2 1 ATOM 2082 C CE1 . PHE A 1 267 ? -8.688 54.288 34.080 1.00 102.56 ? 267 PHE A CE1 1 ATOM 2083 C CE2 . PHE A 1 267 ? -10.438 52.661 34.049 1.00 103.26 ? 267 PHE A CE2 1 ATOM 2084 C CZ . PHE A 1 267 ? -10.016 53.966 33.887 1.00 105.09 ? 267 PHE A CZ 1 ATOM 2085 N N . THR A 1 268 ? -6.844 48.429 37.013 1.00 88.73 ? 268 THR A N 1 ATOM 2086 C CA . THR A 1 268 ? -6.147 47.194 37.356 1.00 85.65 ? 268 THR A CA 1 ATOM 2087 C C . THR A 1 268 ? -6.762 45.989 36.650 1.00 90.65 ? 268 THR A C 1 ATOM 2088 O O . THR A 1 268 ? -7.981 45.814 36.649 1.00 98.78 ? 268 THR A O 1 ATOM 2089 C CB . THR A 1 268 ? -6.159 46.948 38.878 1.00 85.56 ? 268 THR A CB 1 ATOM 2090 O OG1 . THR A 1 268 ? -5.667 48.110 39.556 1.00 89.15 ? 268 THR A OG1 1 ATOM 2091 C CG2 . THR A 1 268 ? -5.290 45.754 39.236 1.00 81.32 ? 268 THR A CG2 1 ATOM 2092 N N . GLY A 1 269 ? -5.913 45.162 36.047 1.00 78.62 ? 269 GLY A N 1 ATOM 2093 C CA . GLY A 1 269 ? -6.367 43.939 35.409 1.00 86.66 ? 269 GLY A CA 1 ATOM 2094 C C . GLY A 1 269 ? -6.830 42.926 36.437 1.00 83.04 ? 269 GLY A C 1 ATOM 2095 O O . GLY A 1 269 ? -6.328 42.902 37.561 1.00 88.51 ? 269 GLY A O 1 ATOM 2096 N N . GLU A 1 270 ? -7.794 42.093 36.059 1.00 83.86 ? 270 GLU A N 1 ATOM 2097 C CA . GLU A 1 270 ? -8.335 41.094 36.974 1.00 89.41 ? 270 GLU A CA 1 ATOM 2098 C C . GLU A 1 270 ? -7.614 39.751 36.875 1.00 71.65 ? 270 GLU A C 1 ATOM 2099 O O . GLU A 1 270 ? -7.842 38.859 37.690 1.00 98.08 ? 270 GLU A O 1 ATOM 2100 C CB . GLU A 1 270 ? -9.830 40.894 36.718 1.00 88.58 ? 270 GLU A CB 1 ATOM 2101 C CG . GLU A 1 270 ? -10.687 42.097 37.068 1.00 96.90 ? 270 GLU A CG 1 ATOM 2102 C CD . GLU A 1 270 ? -12.169 41.815 36.918 1.00 146.18 ? 270 GLU A CD 1 ATOM 2103 O OE1 . GLU A 1 270 ? -12.520 40.724 36.423 1.00 161.02 ? 270 GLU A OE1 1 ATOM 2104 O OE2 . GLU A 1 270 ? -12.982 42.684 37.297 1.00 159.94 ? 270 GLU A OE2 1 ATOM 2105 N N . GLN A 1 271 ? -6.744 39.610 35.880 1.00 65.15 ? 271 GLN A N 1 ATOM 2106 C CA . GLN A 1 271 ? -6.022 38.357 35.682 1.00 62.83 ? 271 GLN A CA 1 ATOM 2107 C C . GLN A 1 271 ? -4.523 38.584 35.528 1.00 67.64 ? 271 GLN A C 1 ATOM 2108 O O . GLN A 1 271 ? -4.088 39.457 34.777 1.00 80.97 ? 271 GLN A O 1 ATOM 2109 C CB . GLN A 1 271 ? -6.562 37.613 34.460 1.00 77.88 ? 271 GLN A CB 1 ATOM 2110 C CG . GLN A 1 271 ? -5.817 36.323 34.147 1.00 69.56 ? 271 GLN A CG 1 ATOM 2111 C CD . GLN A 1 271 ? -6.246 35.706 32.832 1.00 84.88 ? 271 GLN A CD 1 ATOM 2112 O OE1 . GLN A 1 271 ? -7.413 35.780 32.450 1.00 90.37 ? 271 GLN A OE1 1 ATOM 2113 N NE2 . GLN A 1 271 ? -5.298 35.101 32.127 1.00 96.37 ? 271 GLN A NE2 1 ATOM 2114 N N . MET A 1 272 ? -3.740 37.779 36.239 1.00 80.63 ? 272 MET A N 1 ATOM 2115 C CA . MET A 1 272 ? -2.287 37.890 36.215 1.00 70.91 ? 272 MET A CA 1 ATOM 2116 C C . MET A 1 272 ? -1.699 37.438 34.879 1.00 65.65 ? 272 MET A C 1 ATOM 2117 O O . MET A 1 272 ? -2.285 36.605 34.185 1.00 76.51 ? 272 MET A O 1 ATOM 2118 C CB . MET A 1 272 ? -1.682 37.073 37.357 1.00 63.36 ? 272 MET A CB 1 ATOM 2119 C CG . MET A 1 272 ? -2.218 37.439 38.733 1.00 74.91 ? 272 MET A CG 1 ATOM 2120 S SD . MET A 1 272 ? -1.046 37.064 40.049 1.00 84.98 ? 272 MET A SD 1 ATOM 2121 C CE . MET A 1 272 ? -0.542 35.417 39.571 1.00 80.29 ? 272 MET A CE 1 ATOM 2122 N N . ALA A 1 273 ? -0.556 38.025 34.521 1.00 76.09 ? 273 ALA A N 1 ATOM 2123 C CA . ALA A 1 273 ? 0.210 37.661 33.326 1.00 73.82 ? 273 ALA A CA 1 ATOM 2124 C C . ALA A 1 273 ? -0.506 37.999 32.014 1.00 79.43 ? 273 ALA A C 1 ATOM 2125 O O . ALA A 1 273 ? 0.048 37.806 30.930 1.00 74.48 ? 273 ALA A O 1 ATOM 2126 C CB . ALA A 1 273 ? 0.577 36.178 33.357 1.00 60.84 ? 273 ALA A CB 1 ATOM 2127 N N . ALA A 1 274 ? -1.731 38.505 32.112 1.00 66.00 ? 274 ALA A N 1 ATOM 2128 C CA . ALA A 1 274 ? -2.522 38.858 30.934 1.00 56.38 ? 274 ALA A CA 1 ATOM 2129 C C . ALA A 1 274 ? -1.945 40.066 30.198 1.00 75.33 ? 274 ALA A C 1 ATOM 2130 O O . ALA A 1 274 ? -2.396 40.409 29.102 1.00 72.75 ? 274 ALA A O 1 ATOM 2131 C CB . ALA A 1 274 ? -3.962 39.127 31.332 1.00 55.25 ? 274 ALA A CB 1 ATOM 2132 N N . TYR A 1 275 ? -0.951 40.699 30.815 1.00 71.62 ? 275 TYR A N 1 ATOM 2133 C CA . TYR A 1 275 ? -0.314 41.903 30.288 1.00 67.20 ? 275 TYR A CA 1 ATOM 2134 C C . TYR A 1 275 ? -1.334 43.009 30.056 1.00 64.48 ? 275 TYR A C 1 ATOM 2135 O O . TYR A 1 275 ? -1.369 43.632 28.994 1.00 52.39 ? 275 TYR A O 1 ATOM 2136 C CB . TYR A 1 275 ? 0.453 41.599 28.999 1.00 65.11 ? 275 TYR A CB 1 ATOM 2137 C CG . TYR A 1 275 ? 1.887 42.069 29.054 1.00 59.62 ? 275 TYR A CG 1 ATOM 2138 C CD1 . TYR A 1 275 ? 2.808 41.437 29.875 1.00 52.05 ? 275 TYR A CD1 1 ATOM 2139 C CD2 . TYR A 1 275 ? 2.318 43.152 28.297 1.00 49.84 ? 275 TYR A CD2 1 ATOM 2140 C CE1 . TYR A 1 275 ? 4.117 41.861 29.940 1.00 51.57 ? 275 TYR A CE1 1 ATOM 2141 C CE2 . TYR A 1 275 ? 3.631 43.584 28.355 1.00 49.53 ? 275 TYR A CE2 1 ATOM 2142 C CZ . TYR A 1 275 ? 4.525 42.932 29.182 1.00 52.76 ? 275 TYR A CZ 1 ATOM 2143 O OH . TYR A 1 275 ? 5.834 43.348 29.252 1.00 59.37 ? 275 TYR A OH 1 ATOM 2144 N N . PHE A 1 276 ? -2.168 43.233 31.065 1.00 70.63 ? 276 PHE A N 1 ATOM 2145 C CA . PHE A 1 276 ? -3.108 44.344 31.069 1.00 62.71 ? 276 PHE A CA 1 ATOM 2146 C C . PHE A 1 276 ? -2.341 45.657 30.956 1.00 68.25 ? 276 PHE A C 1 ATOM 2147 O O . PHE A 1 276 ? -1.470 45.945 31.773 1.00 60.23 ? 276 PHE A O 1 ATOM 2148 C CB . PHE A 1 276 ? -3.947 44.299 32.349 1.00 62.14 ? 276 PHE A CB 1 ATOM 2149 C CG . PHE A 1 276 ? -4.919 45.434 32.498 1.00 65.32 ? 276 PHE A CG 1 ATOM 2150 C CD1 . PHE A 1 276 ? -6.194 45.348 31.967 1.00 71.85 ? 276 PHE A CD1 1 ATOM 2151 C CD2 . PHE A 1 276 ? -4.568 46.572 33.206 1.00 68.62 ? 276 PHE A CD2 1 ATOM 2152 C CE1 . PHE A 1 276 ? -7.094 46.386 32.121 1.00 70.86 ? 276 PHE A CE1 1 ATOM 2153 C CE2 . PHE A 1 276 ? -5.462 47.613 33.362 1.00 73.21 ? 276 PHE A CE2 1 ATOM 2154 C CZ . PHE A 1 276 ? -6.727 47.519 32.820 1.00 74.96 ? 276 PHE A CZ 1 ATOM 2155 N N . GLY A 1 277 ? -2.671 46.456 29.948 1.00 79.14 ? 277 GLY A N 1 ATOM 2156 C CA . GLY A 1 277 ? -1.966 47.704 29.716 1.00 59.44 ? 277 GLY A CA 1 ATOM 2157 C C . GLY A 1 277 ? -0.839 47.590 28.705 1.00 59.54 ? 277 GLY A C 1 ATOM 2158 O O . GLY A 1 277 ? 0.049 48.441 28.661 1.00 61.74 ? 277 GLY A O 1 ATOM 2159 N N . PHE A 1 278 ? -0.867 46.535 27.896 1.00 71.39 ? 278 PHE A N 1 ATOM 2160 C CA . PHE A 1 278 ? 0.095 46.382 26.809 1.00 59.03 ? 278 PHE A CA 1 ATOM 2161 C C . PHE A 1 278 ? -0.080 47.505 25.795 1.00 64.73 ? 278 PHE A C 1 ATOM 2162 O O . PHE A 1 278 ? 0.884 47.965 25.183 1.00 78.43 ? 278 PHE A O 1 ATOM 2163 C CB . PHE A 1 278 ? -0.065 45.022 26.127 1.00 52.04 ? 278 PHE A CB 1 ATOM 2164 C CG . PHE A 1 278 ? 0.791 44.852 24.901 1.00 62.24 ? 278 PHE A CG 1 ATOM 2165 C CD1 . PHE A 1 278 ? 2.138 44.557 25.016 1.00 72.67 ? 278 PHE A CD1 1 ATOM 2166 C CD2 . PHE A 1 278 ? 0.246 44.980 23.633 1.00 51.47 ? 278 PHE A CD2 1 ATOM 2167 C CE1 . PHE A 1 278 ? 2.928 44.398 23.893 1.00 62.60 ? 278 PHE A CE1 1 ATOM 2168 C CE2 . PHE A 1 278 ? 1.031 44.821 22.505 1.00 59.59 ? 278 PHE A CE2 1 ATOM 2169 C CZ . PHE A 1 278 ? 2.374 44.529 22.636 1.00 55.46 ? 278 PHE A CZ 1 ATOM 2170 N N . SER A 1 279 ? -1.325 47.936 25.625 1.00 55.16 ? 279 SER A N 1 ATOM 2171 C CA . SER A 1 279 ? -1.650 49.049 24.747 1.00 63.85 ? 279 SER A CA 1 ATOM 2172 C C . SER A 1 279 ? -2.775 49.873 25.357 1.00 71.38 ? 279 SER A C 1 ATOM 2173 O O . SER A 1 279 ? -3.650 49.336 26.036 1.00 69.22 ? 279 SER A O 1 ATOM 2174 C CB . SER A 1 279 ? -2.050 48.548 23.357 1.00 82.47 ? 279 SER A CB 1 ATOM 2175 O OG . SER A 1 279 ? -3.226 47.761 23.420 1.00 59.33 ? 279 SER A OG 1 ATOM 2176 N N . VAL A 1 280 ? -2.743 51.181 25.124 1.00 75.94 ? 280 VAL A N 1 ATOM 2177 C CA . VAL A 1 280 ? -3.776 52.074 25.638 1.00 56.30 ? 280 VAL A CA 1 ATOM 2178 C C . VAL A 1 280 ? -4.231 53.061 24.569 1.00 59.45 ? 280 VAL A C 1 ATOM 2179 O O . VAL A 1 280 ? -3.476 53.388 23.653 1.00 71.78 ? 280 VAL A O 1 ATOM 2180 C CB . VAL A 1 280 ? -3.286 52.859 26.872 1.00 65.48 ? 280 VAL A CB 1 ATOM 2181 C CG1 . VAL A 1 280 ? -3.177 51.941 28.082 1.00 60.17 ? 280 VAL A CG1 1 ATOM 2182 C CG2 . VAL A 1 280 ? -1.954 53.536 26.581 1.00 72.05 ? 280 VAL A CG2 1 ATOM 2183 N N . ALA A 1 281 ? -5.468 53.531 24.690 1.00 71.10 ? 281 ALA A N 1 ATOM 2184 C CA . ALA A 1 281 ? -6.018 54.495 23.745 1.00 69.52 ? 281 ALA A CA 1 ATOM 2185 C C . ALA A 1 281 ? -7.030 55.411 24.422 1.00 68.06 ? 281 ALA A C 1 ATOM 2186 O O . ALA A 1 281 ? -7.729 55.004 25.351 1.00 67.57 ? 281 ALA A O 1 ATOM 2187 C CB . ALA A 1 281 ? -6.657 53.778 22.566 1.00 67.83 ? 281 ALA A CB 1 ATOM 2188 N N . ALA A 1 282 ? -7.103 56.651 23.950 1.00 75.06 ? 282 ALA A N 1 ATOM 2189 C CA . ALA A 1 282 ? -8.044 57.622 24.493 1.00 69.55 ? 282 ALA A CA 1 ATOM 2190 C C . ALA A 1 282 ? -8.858 58.273 23.380 1.00 70.10 ? 282 ALA A C 1 ATOM 2191 O O . ALA A 1 282 ? -8.309 58.933 22.498 1.00 68.90 ? 282 ALA A O 1 ATOM 2192 C CB . ALA A 1 282 ? -7.311 58.677 25.303 1.00 71.43 ? 282 ALA A CB 1 ATOM 2193 N N . THR A 1 283 ? -10.170 58.074 23.428 1.00 73.10 ? 283 THR A N 1 ATOM 2194 C CA . THR A 1 283 ? -11.085 58.646 22.447 1.00 75.14 ? 283 THR A CA 1 ATOM 2195 C C . THR A 1 283 ? -12.446 58.835 23.101 1.00 90.81 ? 283 THR A C 1 ATOM 2196 O O . THR A 1 283 ? -12.713 58.254 24.152 1.00 106.41 ? 283 THR A O 1 ATOM 2197 C CB . THR A 1 283 ? -11.235 57.747 21.201 1.00 83.94 ? 283 THR A CB 1 ATOM 2198 O OG1 . THR A 1 283 ? -10.081 56.910 21.062 1.00 89.97 ? 283 THR A OG1 1 ATOM 2199 C CG2 . THR A 1 283 ? -11.410 58.589 19.945 1.00 100.21 ? 283 THR A CG2 1 ATOM 2200 N N . ASP A 1 284 ? -13.309 59.641 22.492 1.00 85.21 ? 284 ASP A N 1 ATOM 2201 C CA . ASP A 1 284 ? -14.677 59.740 22.981 1.00 94.96 ? 284 ASP A CA 1 ATOM 2202 C C . ASP A 1 284 ? -15.577 58.905 22.083 1.00 102.29 ? 284 ASP A C 1 ATOM 2203 O O . ASP A 1 284 ? -15.897 59.301 20.964 1.00 86.64 ? 284 ASP A O 1 ATOM 2204 C CB . ASP A 1 284 ? -15.144 61.196 23.013 1.00 90.27 ? 284 ASP A CB 1 ATOM 2205 C CG . ASP A 1 284 ? -16.544 61.347 23.570 1.00 96.66 ? 284 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 284 ? -17.272 62.249 23.109 1.00 117.81 ? 284 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 284 ? -16.915 60.566 24.471 1.00 99.74 ? 284 ASP A OD2 1 ATOM 2208 N N . ILE A 1 285 ? -15.989 57.748 22.589 1.00 101.33 ? 285 ILE A N 1 ATOM 2209 C CA . ILE A 1 285 ? -16.742 56.789 21.791 1.00 88.39 ? 285 ILE A CA 1 ATOM 2210 C C . ILE A 1 285 ? -18.243 57.091 21.761 1.00 92.37 ? 285 ILE A C 1 ATOM 2211 O O . ILE A 1 285 ? -18.920 56.789 20.778 1.00 98.57 ? 285 ILE A O 1 ATOM 2212 C CB . ILE A 1 285 ? -16.494 55.336 22.288 1.00 85.51 ? 285 ILE A CB 1 ATOM 2213 C CG1 . ILE A 1 285 ? -16.432 54.368 21.104 1.00 82.37 ? 285 ILE A CG1 1 ATOM 2214 C CG2 . ILE A 1 285 ? -17.527 54.900 23.322 1.00 89.79 ? 285 ILE A CG2 1 ATOM 2215 C CD1 . ILE A 1 285 ? -15.264 54.620 20.176 1.00 77.29 ? 285 ILE A CD1 1 ATOM 2216 N N . ASN A 1 286 ? -18.759 57.683 22.835 1.00 96.87 ? 286 ASN A N 1 ATOM 2217 C CA . ASN A 1 286 ? -20.197 57.899 22.963 1.00 101.88 ? 286 ASN A CA 1 ATOM 2218 C C . ASN A 1 286 ? -20.649 59.299 22.554 1.00 103.59 ? 286 ASN A C 1 ATOM 2219 O O . ASN A 1 286 ? -21.835 59.622 22.637 1.00 111.40 ? 286 ASN A O 1 ATOM 2220 C CB . ASN A 1 286 ? -20.645 57.604 24.396 1.00 106.62 ? 286 ASN A CB 1 ATOM 2221 C CG . ASN A 1 286 ? -19.801 58.316 25.435 1.00 108.88 ? 286 ASN A CG 1 ATOM 2222 O OD1 . ASN A 1 286 ? -18.688 58.762 25.154 1.00 106.87 ? 286 ASN A OD1 1 ATOM 2223 N ND2 . ASN A 1 286 ? -20.327 58.414 26.650 1.00 114.86 ? 286 ASN A ND2 1 ATOM 2224 N N . GLY A 1 287 ? -19.706 60.125 22.115 1.00 100.23 ? 287 GLY A N 1 ATOM 2225 C CA . GLY A 1 287 ? -20.023 61.465 21.652 1.00 102.92 ? 287 GLY A CA 1 ATOM 2226 C C . GLY A 1 287 ? -20.519 62.379 22.755 1.00 111.14 ? 287 GLY A C 1 ATOM 2227 O O . GLY A 1 287 ? -21.253 63.335 22.501 1.00 106.66 ? 287 GLY A O 1 ATOM 2228 N N . ASP A 1 288 ? -20.113 62.083 23.985 1.00 127.01 ? 288 ASP A N 1 ATOM 2229 C CA . ASP A 1 288 ? -20.523 62.869 25.143 1.00 119.01 ? 288 ASP A CA 1 ATOM 2230 C C . ASP A 1 288 ? -19.502 63.959 25.460 1.00 110.30 ? 288 ASP A C 1 ATOM 2231 O O . ASP A 1 288 ? -19.607 64.633 26.487 1.00 115.27 ? 288 ASP A O 1 ATOM 2232 C CB . ASP A 1 288 ? -20.729 61.965 26.362 1.00 117.05 ? 288 ASP A CB 1 ATOM 2233 C CG . ASP A 1 288 ? -19.435 61.352 26.867 1.00 131.03 ? 288 ASP A CG 1 ATOM 2234 O OD1 . ASP A 1 288 ? -18.551 61.030 26.043 1.00 128.61 ? 288 ASP A OD1 1 ATOM 2235 O OD2 . ASP A 1 288 ? -19.307 61.185 28.097 1.00 145.93 ? 288 ASP A OD2 1 ATOM 2236 N N . ASP A 1 289 ? -18.505 64.087 24.584 1.00 105.27 ? 289 ASP A N 1 ATOM 2237 C CA . ASP A 1 289 ? -17.420 65.068 24.704 1.00 103.38 ? 289 ASP A CA 1 ATOM 2238 C C . ASP A 1 289 ? -16.452 64.736 25.840 1.00 106.46 ? 289 ASP A C 1 ATOM 2239 O O . ASP A 1 289 ? -15.448 65.422 26.026 1.00 101.65 ? 289 ASP A O 1 ATOM 2240 C CB . ASP A 1 289 ? -17.974 66.487 24.881 1.00 121.93 ? 289 ASP A CB 1 ATOM 2241 C CG . ASP A 1 289 ? -18.662 67.002 23.634 1.00 142.41 ? 289 ASP A CG 1 ATOM 2242 O OD1 . ASP A 1 289 ? -19.896 66.840 23.524 1.00 156.32 ? 289 ASP A OD1 1 ATOM 2243 O OD2 . ASP A 1 289 ? -17.970 67.568 22.762 1.00 131.44 ? 289 ASP A OD2 1 ATOM 2244 N N . TYR A 1 290 ? -16.757 63.687 26.599 1.00 115.98 ? 290 TYR A N 1 ATOM 2245 C CA . TYR A 1 290 ? -15.838 63.187 27.613 1.00 107.00 ? 290 TYR A CA 1 ATOM 2246 C C . TYR A 1 290 ? -15.039 62.008 27.063 1.00 103.30 ? 290 TYR A C 1 ATOM 2247 O O . TYR A 1 290 ? -15.610 60.992 26.662 1.00 117.61 ? 290 TYR A O 1 ATOM 2248 C CB . TYR A 1 290 ? -16.592 62.774 28.880 1.00 112.80 ? 290 TYR A CB 1 ATOM 2249 C CG . TYR A 1 290 ? -17.122 63.935 29.692 1.00 116.13 ? 290 TYR A CG 1 ATOM 2250 C CD1 . TYR A 1 290 ? -18.451 64.326 29.597 1.00 118.61 ? 290 TYR A CD1 1 ATOM 2251 C CD2 . TYR A 1 290 ? -16.293 64.635 30.559 1.00 116.48 ? 290 TYR A CD2 1 ATOM 2252 C CE1 . TYR A 1 290 ? -18.939 65.385 30.341 1.00 121.16 ? 290 TYR A CE1 1 ATOM 2253 C CE2 . TYR A 1 290 ? -16.772 65.694 31.306 1.00 121.64 ? 290 TYR A CE2 1 ATOM 2254 C CZ . TYR A 1 290 ? -18.095 66.065 31.194 1.00 122.07 ? 290 TYR A CZ 1 ATOM 2255 O OH . TYR A 1 290 ? -18.576 67.119 31.935 1.00 128.66 ? 290 TYR A OH 1 ATOM 2256 N N . ALA A 1 291 ? -13.717 62.157 27.042 1.00 97.85 ? 291 ALA A N 1 ATOM 2257 C CA . ALA A 1 291 ? -12.828 61.127 26.513 1.00 92.20 ? 291 ALA A CA 1 ATOM 2258 C C . ALA A 1 291 ? -12.924 59.840 27.323 1.00 93.77 ? 291 ALA A C 1 ATOM 2259 O O . ALA A 1 291 ? -13.020 59.874 28.548 1.00 98.93 ? 291 ALA A O 1 ATOM 2260 C CB . ALA A 1 291 ? -11.395 61.630 26.489 1.00 94.93 ? 291 ALA A CB 1 ATOM 2261 N N . ASP A 1 292 ? -12.890 58.706 26.629 1.00 91.43 ? 292 ASP A N 1 ATOM 2262 C CA . ASP A 1 292 ? -13.047 57.405 27.270 1.00 91.21 ? 292 ASP A CA 1 ATOM 2263 C C . ASP A 1 292 ? -11.792 56.548 27.082 1.00 85.64 ? 292 ASP A C 1 ATOM 2264 O O . ASP A 1 292 ? -11.086 56.679 26.082 1.00 79.96 ? 292 ASP A O 1 ATOM 2265 C CB . ASP A 1 292 ? -14.281 56.691 26.713 1.00 92.20 ? 292 ASP A CB 1 ATOM 2266 C CG . ASP A 1 292 ? -15.475 57.625 26.553 1.00 98.26 ? 292 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 292 ? -15.802 57.993 25.406 1.00 96.42 ? 292 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 292 ? -16.086 58.002 27.575 1.00 107.08 ? 292 ASP A OD2 1 ATOM 2269 N N . VAL A 1 293 ? -11.524 55.668 28.044 1.00 86.66 ? 293 VAL A N 1 ATOM 2270 C CA . VAL A 1 293 ? -10.264 54.926 28.084 1.00 81.72 ? 293 VAL A CA 1 ATOM 2271 C C . VAL A 1 293 ? -10.371 53.504 27.535 1.00 77.81 ? 293 VAL A C 1 ATOM 2272 O O . VAL A 1 293 ? -11.267 52.748 27.911 1.00 90.16 ? 293 VAL A O 1 ATOM 2273 C CB . VAL A 1 293 ? -9.716 54.847 29.526 1.00 85.99 ? 293 VAL A CB 1 ATOM 2274 C CG1 . VAL A 1 293 ? -8.396 54.092 29.563 1.00 93.72 ? 293 VAL A CG1 1 ATOM 2275 C CG2 . VAL A 1 293 ? -9.546 56.237 30.106 1.00 93.24 ? 293 VAL A CG2 1 ATOM 2276 N N . PHE A 1 294 ? -9.442 53.147 26.652 1.00 72.35 ? 294 PHE A N 1 ATOM 2277 C CA . PHE A 1 294 ? -9.357 51.794 26.110 1.00 80.84 ? 294 PHE A CA 1 ATOM 2278 C C . PHE A 1 294 ? -8.052 51.127 26.536 1.00 76.77 ? 294 PHE A C 1 ATOM 2279 O O . PHE A 1 294 ? -6.971 51.686 26.350 1.00 90.40 ? 294 PHE A O 1 ATOM 2280 C CB . PHE A 1 294 ? -9.466 51.814 24.584 1.00 71.84 ? 294 PHE A CB 1 ATOM 2281 C CG . PHE A 1 294 ? -10.811 52.248 24.077 1.00 75.34 ? 294 PHE A CG 1 ATOM 2282 C CD1 . PHE A 1 294 ? -11.126 53.593 23.970 1.00 71.03 ? 294 PHE A CD1 1 ATOM 2283 C CD2 . PHE A 1 294 ? -11.760 51.312 23.699 1.00 83.57 ? 294 PHE A CD2 1 ATOM 2284 C CE1 . PHE A 1 294 ? -12.363 53.996 23.504 1.00 80.26 ? 294 PHE A CE1 1 ATOM 2285 C CE2 . PHE A 1 294 ? -12.998 51.710 23.229 1.00 71.93 ? 294 PHE A CE2 1 ATOM 2286 C CZ . PHE A 1 294 ? -13.299 53.053 23.131 1.00 78.85 ? 294 PHE A CZ 1 ATOM 2287 N N . ILE A 1 295 ? -8.154 49.931 27.110 1.00 65.65 ? 295 ILE A N 1 ATOM 2288 C CA . ILE A 1 295 ? -6.980 49.221 27.609 1.00 63.49 ? 295 ILE A CA 1 ATOM 2289 C C . ILE A 1 295 ? -6.897 47.793 27.080 1.00 74.34 ? 295 ILE A C 1 ATOM 2290 O O . ILE A 1 295 ? -7.785 46.977 27.326 1.00 84.84 ? 295 ILE A O 1 ATOM 2291 C CB . ILE A 1 295 ? -6.968 49.164 29.144 1.00 66.55 ? 295 ILE A CB 1 ATOM 2292 C CG1 . ILE A 1 295 ? -7.102 50.569 29.736 1.00 70.81 ? 295 ILE A CG1 1 ATOM 2293 C CG2 . ILE A 1 295 ? -5.701 48.480 29.629 1.00 63.42 ? 295 ILE A CG2 1 ATOM 2294 C CD1 . ILE A 1 295 ? -7.472 50.585 31.204 1.00 76.46 ? 295 ILE A CD1 1 ATOM 2295 N N . GLY A 1 296 ? -5.824 47.495 26.353 1.00 66.84 ? 296 GLY A N 1 ATOM 2296 C CA . GLY A 1 296 ? -5.616 46.160 25.821 1.00 72.03 ? 296 GLY A CA 1 ATOM 2297 C C . GLY A 1 296 ? -4.963 45.196 26.794 1.00 77.97 ? 296 GLY A C 1 ATOM 2298 O O . GLY A 1 296 ? -4.086 45.574 27.571 1.00 75.47 ? 296 GLY A O 1 ATOM 2299 N N . ALA A 1 297 ? -5.399 43.941 26.742 1.00 85.73 ? 297 ALA A N 1 ATOM 2300 C CA . ALA A 1 297 ? -4.785 42.855 27.500 1.00 78.44 ? 297 ALA A CA 1 ATOM 2301 C C . ALA A 1 297 ? -4.805 41.585 26.656 1.00 81.38 ? 297 ALA A C 1 ATOM 2302 O O . ALA A 1 297 ? -5.608 40.685 26.903 1.00 90.89 ? 297 ALA A O 1 ATOM 2303 C CB . ALA A 1 297 ? -5.507 42.639 28.819 1.00 58.54 ? 297 ALA A CB 1 ATOM 2304 N N . PRO A 1 298 ? -3.914 41.511 25.655 1.00 72.99 ? 298 PRO A N 1 ATOM 2305 C CA . PRO A 1 298 ? -3.957 40.488 24.602 1.00 81.00 ? 298 PRO A CA 1 ATOM 2306 C C . PRO A 1 298 ? -3.799 39.051 25.096 1.00 82.69 ? 298 PRO A C 1 ATOM 2307 O O . PRO A 1 298 ? -4.224 38.125 24.407 1.00 96.06 ? 298 PRO A O 1 ATOM 2308 C CB . PRO A 1 298 ? -2.779 40.873 23.699 1.00 82.45 ? 298 PRO A CB 1 ATOM 2309 C CG . PRO A 1 298 ? -1.852 41.624 24.586 1.00 74.70 ? 298 PRO A CG 1 ATOM 2310 C CD . PRO A 1 298 ? -2.740 42.392 25.515 1.00 50.33 ? 298 PRO A CD 1 ATOM 2311 N N . LEU A 1 299 ? -3.189 38.867 26.261 1.00 67.82 ? 299 LEU A N 1 ATOM 2312 C CA . LEU A 1 299 ? -2.942 37.527 26.782 1.00 67.93 ? 299 LEU A CA 1 ATOM 2313 C C . LEU A 1 299 ? -4.009 37.055 27.769 1.00 66.94 ? 299 LEU A C 1 ATOM 2314 O O . LEU A 1 299 ? -3.877 35.982 28.360 1.00 73.56 ? 299 LEU A O 1 ATOM 2315 C CB . LEU A 1 299 ? -1.564 37.466 27.439 1.00 63.92 ? 299 LEU A CB 1 ATOM 2316 C CG . LEU A 1 299 ? -0.408 37.811 26.499 1.00 53.40 ? 299 LEU A CG 1 ATOM 2317 C CD1 . LEU A 1 299 ? 0.922 37.504 27.160 1.00 59.52 ? 299 LEU A CD1 1 ATOM 2318 C CD2 . LEU A 1 299 ? -0.540 37.070 25.179 1.00 54.82 ? 299 LEU A CD2 1 ATOM 2319 N N . PHE A 1 300 ? -5.052 37.860 27.956 1.00 71.73 ? 300 PHE A N 1 ATOM 2320 C CA . PHE A 1 300 ? -6.132 37.516 28.879 1.00 56.63 ? 300 PHE A CA 1 ATOM 2321 C C . PHE A 1 300 ? -6.785 36.190 28.512 1.00 58.73 ? 300 PHE A C 1 ATOM 2322 O O . PHE A 1 300 ? -7.060 35.926 27.342 1.00 75.03 ? 300 PHE A O 1 ATOM 2323 C CB . PHE A 1 300 ? -7.188 38.623 28.906 1.00 82.18 ? 300 PHE A CB 1 ATOM 2324 C CG . PHE A 1 300 ? -8.363 38.322 29.798 1.00 80.57 ? 300 PHE A CG 1 ATOM 2325 C CD1 . PHE A 1 300 ? -8.312 38.612 31.150 1.00 61.40 ? 300 PHE A CD1 1 ATOM 2326 C CD2 . PHE A 1 300 ? -9.518 37.758 29.281 1.00 93.65 ? 300 PHE A CD2 1 ATOM 2327 C CE1 . PHE A 1 300 ? -9.388 38.341 31.973 1.00 61.27 ? 300 PHE A CE1 1 ATOM 2328 C CE2 . PHE A 1 300 ? -10.597 37.482 30.098 1.00 69.17 ? 300 PHE A CE2 1 ATOM 2329 C CZ . PHE A 1 300 ? -10.533 37.775 31.446 1.00 69.48 ? 300 PHE A CZ 1 ATOM 2330 N N . MET A 1 301 ? -7.028 35.360 29.520 1.00 60.15 ? 301 MET A N 1 ATOM 2331 C CA . MET A 1 301 ? -7.657 34.065 29.305 1.00 65.94 ? 301 MET A CA 1 ATOM 2332 C C . MET A 1 301 ? -9.070 34.032 29.872 1.00 84.19 ? 301 MET A C 1 ATOM 2333 O O . MET A 1 301 ? -9.264 34.118 31.085 1.00 102.44 ? 301 MET A O 1 ATOM 2334 C CB . MET A 1 301 ? -6.820 32.948 29.934 1.00 63.76 ? 301 MET A CB 1 ATOM 2335 C CG . MET A 1 301 ? -5.408 32.839 29.387 1.00 62.87 ? 301 MET A CG 1 ATOM 2336 S SD . MET A 1 301 ? -4.530 31.399 30.024 1.00 86.12 ? 301 MET A SD 1 ATOM 2337 C CE . MET A 1 301 ? -4.501 31.759 31.778 1.00 64.75 ? 301 MET A CE 1 ATOM 2338 N N . ASP A 1 302 ? -10.056 33.902 28.989 1.00 78.10 ? 302 ASP A N 1 ATOM 2339 C CA . ASP A 1 302 ? -11.447 33.797 29.411 1.00 88.62 ? 302 ASP A CA 1 ATOM 2340 C C . ASP A 1 302 ? -11.858 32.331 29.508 1.00 94.36 ? 302 ASP A C 1 ATOM 2341 O O . ASP A 1 302 ? -11.056 31.436 29.243 1.00 76.96 ? 302 ASP A O 1 ATOM 2342 C CB . ASP A 1 302 ? -12.370 34.554 28.447 1.00 87.27 ? 302 ASP A CB 1 ATOM 2343 C CG . ASP A 1 302 ? -12.684 33.767 27.183 1.00 98.67 ? 302 ASP A CG 1 ATOM 2344 O OD1 . ASP A 1 302 ? -11.826 32.985 26.722 1.00 105.15 ? 302 ASP A OD1 1 ATOM 2345 O OD2 . ASP A 1 302 ? -13.799 33.937 26.645 1.00 111.33 ? 302 ASP A OD2 1 ATOM 2346 N N . ARG A 1 303 ? -13.109 32.090 29.880 1.00 91.00 ? 303 ARG A N 1 ATOM 2347 C CA . ARG A 1 303 ? -13.613 30.728 29.987 1.00 74.27 ? 303 ARG A CA 1 ATOM 2348 C C . ARG A 1 303 ? -14.315 30.304 28.700 1.00 79.53 ? 303 ARG A C 1 ATOM 2349 O O . ARG A 1 303 ? -15.178 31.017 28.188 1.00 83.88 ? 303 ARG A O 1 ATOM 2350 C CB . ARG A 1 303 ? -14.566 30.600 31.180 1.00 116.04 ? 303 ARG A CB 1 ATOM 2351 C CG . ARG A 1 303 ? -13.903 30.801 32.540 1.00 88.39 ? 303 ARG A CG 1 ATOM 2352 C CD . ARG A 1 303 ? -12.967 29.652 32.883 1.00 76.78 ? 303 ARG A CD 1 ATOM 2353 N NE . ARG A 1 303 ? -12.322 29.830 34.182 1.00 86.94 ? 303 ARG A NE 1 ATOM 2354 C CZ . ARG A 1 303 ? -11.587 28.900 34.783 1.00 99.81 ? 303 ARG A CZ 1 ATOM 2355 N NH1 . ARG A 1 303 ? -11.407 27.721 34.205 1.00 92.64 ? 303 ARG A NH1 1 ATOM 2356 N NH2 . ARG A 1 303 ? -11.033 29.145 35.964 1.00 121.96 ? 303 ARG A NH2 1 ATOM 2357 N N . GLY A 1 304 ? -13.934 29.142 28.177 1.00 88.46 ? 304 GLY A N 1 ATOM 2358 C CA . GLY A 1 304 ? -14.584 28.590 27.004 1.00 93.51 ? 304 GLY A CA 1 ATOM 2359 C C . GLY A 1 304 ? -15.950 28.033 27.353 1.00 98.89 ? 304 GLY A C 1 ATOM 2360 O O . GLY A 1 304 ? -16.363 28.070 28.513 1.00 85.06 ? 304 GLY A O 1 ATOM 2361 N N . SER A 1 305 ? -16.654 27.515 26.352 1.00 113.55 ? 305 SER A N 1 ATOM 2362 C CA . SER A 1 305 ? -17.972 26.929 26.566 1.00 110.66 ? 305 SER A CA 1 ATOM 2363 C C . SER A 1 305 ? -17.890 25.720 27.492 1.00 90.08 ? 305 SER A C 1 ATOM 2364 O O . SER A 1 305 ? -18.826 25.431 28.237 1.00 92.14 ? 305 SER A O 1 ATOM 2365 C CB . SER A 1 305 ? -18.604 26.527 25.232 1.00 112.56 ? 305 SER A CB 1 ATOM 2366 O OG . SER A 1 305 ? -17.795 25.583 24.553 1.00 139.04 ? 305 SER A OG 1 ATOM 2367 N N . ASP A 1 306 ? -16.762 25.019 27.440 1.00 100.59 ? 306 ASP A N 1 ATOM 2368 C CA . ASP A 1 306 ? -16.545 23.843 28.275 1.00 108.47 ? 306 ASP A CA 1 ATOM 2369 C C . ASP A 1 306 ? -16.094 24.228 29.680 1.00 112.11 ? 306 ASP A C 1 ATOM 2370 O O . ASP A 1 306 ? -16.063 23.392 30.583 1.00 112.21 ? 306 ASP A O 1 ATOM 2371 C CB . ASP A 1 306 ? -15.517 22.913 27.626 1.00 107.17 ? 306 ASP A CB 1 ATOM 2372 C CG . ASP A 1 306 ? -14.262 23.643 27.194 1.00 137.85 ? 306 ASP A CG 1 ATOM 2373 O OD1 . ASP A 1 306 ? -14.330 24.874 26.991 1.00 129.20 ? 306 ASP A OD1 1 ATOM 2374 O OD2 . ASP A 1 306 ? -13.208 22.987 27.051 1.00 145.02 ? 306 ASP A OD2 1 ATOM 2375 N N . GLY A 1 307 ? -15.743 25.497 29.857 1.00 100.42 ? 307 GLY A N 1 ATOM 2376 C CA . GLY A 1 307 ? -15.325 25.997 31.153 1.00 86.69 ? 307 GLY A CA 1 ATOM 2377 C C . GLY A 1 307 ? -13.819 26.019 31.325 1.00 100.07 ? 307 GLY A C 1 ATOM 2378 O O . GLY A 1 307 ? -13.311 26.459 32.355 1.00 115.60 ? 307 GLY A O 1 ATOM 2379 N N . LYS A 1 308 ? -13.102 25.537 30.315 1.00 98.49 ? 308 LYS A N 1 ATOM 2380 C CA . LYS A 1 308 ? -11.645 25.522 30.357 1.00 83.41 ? 308 LYS A CA 1 ATOM 2381 C C . LYS A 1 308 ? -11.076 26.854 29.884 1.00 79.56 ? 308 LYS A C 1 ATOM 2382 O O . LYS A 1 308 ? -11.610 27.472 28.963 1.00 105.32 ? 308 LYS A O 1 ATOM 2383 C CB . LYS A 1 308 ? -11.092 24.378 29.503 1.00 85.63 ? 308 LYS A CB 1 ATOM 2384 C CG . LYS A 1 308 ? -9.580 24.227 29.579 1.00 143.82 ? 308 LYS A CG 1 ATOM 2385 C CD . LYS A 1 308 ? -9.077 23.163 28.620 1.00 142.19 ? 308 LYS A CD 1 ATOM 2386 C CE . LYS A 1 308 ? -7.560 23.075 28.642 1.00 147.62 ? 308 LYS A CE 1 ATOM 2387 N NZ . LYS A 1 308 ? -7.050 22.087 27.651 1.00 138.73 ? 308 LYS A NZ 1 ATOM 2388 N N . LEU A 1 309 ? -9.995 27.290 30.526 1.00 77.68 ? 309 LEU A N 1 ATOM 2389 C CA . LEU A 1 309 ? -9.326 28.534 30.161 1.00 85.37 ? 309 LEU A CA 1 ATOM 2390 C C . LEU A 1 309 ? -8.782 28.480 28.739 1.00 86.80 ? 309 LEU A C 1 ATOM 2391 O O . LEU A 1 309 ? -8.340 27.429 28.271 1.00 95.51 ? 309 LEU A O 1 ATOM 2392 C CB . LEU A 1 309 ? -8.187 28.839 31.137 1.00 72.89 ? 309 LEU A CB 1 ATOM 2393 C CG . LEU A 1 309 ? -8.557 29.230 32.569 1.00 72.95 ? 309 LEU A CG 1 ATOM 2394 C CD1 . LEU A 1 309 ? -7.308 29.364 33.424 1.00 72.09 ? 309 LEU A CD1 1 ATOM 2395 C CD2 . LEU A 1 309 ? -9.352 30.524 32.584 1.00 82.60 ? 309 LEU A CD2 1 ATOM 2396 N N . GLN A 1 310 ? -8.824 29.618 28.055 1.00 71.37 ? 310 GLN A N 1 ATOM 2397 C CA . GLN A 1 310 ? -8.262 29.730 26.716 1.00 97.72 ? 310 GLN A CA 1 ATOM 2398 C C . GLN A 1 310 ? -7.752 31.146 26.483 1.00 101.78 ? 310 GLN A C 1 ATOM 2399 O O . GLN A 1 310 ? -8.362 32.114 26.933 1.00 106.95 ? 310 GLN A O 1 ATOM 2400 C CB . GLN A 1 310 ? -9.303 29.350 25.660 1.00 87.41 ? 310 GLN A CB 1 ATOM 2401 C CG . GLN A 1 310 ? -10.578 30.176 25.711 1.00 87.74 ? 310 GLN A CG 1 ATOM 2402 C CD . GLN A 1 310 ? -11.638 29.672 24.753 1.00 104.19 ? 310 GLN A CD 1 ATOM 2403 O OE1 . GLN A 1 310 ? -11.527 28.572 24.212 1.00 91.38 ? 310 GLN A OE1 1 ATOM 2404 N NE2 . GLN A 1 310 ? -12.673 30.477 24.537 1.00 107.96 ? 310 GLN A NE2 1 ATOM 2405 N N . GLU A 1 311 ? -6.638 31.268 25.769 1.00 106.83 ? 311 GLU A N 1 ATOM 2406 C CA . GLU A 1 311 ? -6.045 32.578 25.528 1.00 94.32 ? 311 GLU A CA 1 ATOM 2407 C C . GLU A 1 311 ? -6.707 33.255 24.333 1.00 85.57 ? 311 GLU A C 1 ATOM 2408 O O . GLU A 1 311 ? -6.631 32.775 23.206 1.00 97.90 ? 311 GLU A O 1 ATOM 2409 C CB . GLU A 1 311 ? -4.537 32.455 25.302 1.00 90.52 ? 311 GLU A CB 1 ATOM 2410 C CG . GLU A 1 311 ? -3.843 33.772 24.991 1.00 97.10 ? 311 GLU A CG 1 ATOM 2411 C CD . GLU A 1 311 ? -2.343 33.618 24.827 1.00 114.12 ? 311 GLU A CD 1 ATOM 2412 O OE1 . GLU A 1 311 ? -1.768 34.290 23.944 1.00 119.64 ? 311 GLU A OE1 1 ATOM 2413 O OE2 . GLU A 1 311 ? -1.736 32.829 25.583 1.00 118.20 ? 311 GLU A OE2 1 ATOM 2414 N N . VAL A 1 312 ? -7.347 34.385 24.599 1.00 84.46 ? 312 VAL A N 1 ATOM 2415 C CA . VAL A 1 312 ? -8.110 35.120 23.600 1.00 90.06 ? 312 VAL A CA 1 ATOM 2416 C C . VAL A 1 312 ? -7.634 36.565 23.576 1.00 75.76 ? 312 VAL A C 1 ATOM 2417 O O . VAL A 1 312 ? -7.203 37.078 22.544 1.00 88.12 ? 312 VAL A O 1 ATOM 2418 C CB . VAL A 1 312 ? -9.627 35.055 23.868 1.00 88.11 ? 312 VAL A CB 1 ATOM 2419 C CG1 . VAL A 1 312 ? -10.227 33.824 23.205 1.00 66.34 ? 312 VAL A CG1 1 ATOM 2420 C CG2 . VAL A 1 312 ? -9.910 35.051 25.361 1.00 97.68 ? 312 VAL A CG2 1 ATOM 2421 N N . GLY A 1 313 ? -7.727 37.212 24.732 1.00 64.61 ? 313 GLY A N 1 ATOM 2422 C CA . GLY A 1 313 ? -7.398 38.613 24.885 1.00 79.92 ? 313 GLY A CA 1 ATOM 2423 C C . GLY A 1 313 ? -8.640 39.423 25.176 1.00 94.30 ? 313 GLY A C 1 ATOM 2424 O O . GLY A 1 313 ? -9.752 39.034 24.819 1.00 98.85 ? 313 GLY A O 1 ATOM 2425 N N . GLN A 1 314 ? -8.443 40.558 25.835 1.00 83.71 ? 314 GLN A N 1 ATOM 2426 C CA . GLN A 1 314 ? -9.554 41.353 26.328 1.00 72.36 ? 314 GLN A CA 1 ATOM 2427 C C . GLN A 1 314 ? -9.230 42.840 26.263 1.00 69.31 ? 314 GLN A C 1 ATOM 2428 O O . GLN A 1 314 ? -8.106 43.256 26.542 1.00 72.02 ? 314 GLN A O 1 ATOM 2429 C CB . GLN A 1 314 ? -9.896 40.941 27.763 1.00 77.66 ? 314 GLN A CB 1 ATOM 2430 C CG . GLN A 1 314 ? -11.207 41.495 28.293 1.00 80.15 ? 314 GLN A CG 1 ATOM 2431 C CD . GLN A 1 314 ? -11.560 40.937 29.660 1.00 74.40 ? 314 GLN A CD 1 ATOM 2432 O OE1 . GLN A 1 314 ? -10.876 41.201 30.649 1.00 74.59 ? 314 GLN A OE1 1 ATOM 2433 N NE2 . GLN A 1 314 ? -12.630 40.153 29.718 1.00 92.70 ? 314 GLN A NE2 1 ATOM 2434 N N . VAL A 1 315 ? -10.225 43.635 25.888 1.00 66.62 ? 315 VAL A N 1 ATOM 2435 C CA . VAL A 1 315 ? -10.068 45.081 25.835 1.00 72.44 ? 315 VAL A CA 1 ATOM 2436 C C . VAL A 1 315 ? -11.012 45.743 26.827 1.00 88.57 ? 315 VAL A C 1 ATOM 2437 O O . VAL A 1 315 ? -12.224 45.529 26.783 1.00 87.93 ? 315 VAL A O 1 ATOM 2438 C CB . VAL A 1 315 ? -10.335 45.631 24.424 1.00 69.22 ? 315 VAL A CB 1 ATOM 2439 C CG1 . VAL A 1 315 ? -10.231 47.149 24.417 1.00 70.89 ? 315 VAL A CG1 1 ATOM 2440 C CG2 . VAL A 1 315 ? -9.364 45.020 23.429 1.00 69.09 ? 315 VAL A CG2 1 ATOM 2441 N N . SER A 1 316 ? -10.451 46.546 27.724 1.00 89.66 ? 316 SER A N 1 ATOM 2442 C CA . SER A 1 316 ? -11.246 47.228 28.733 1.00 81.39 ? 316 SER A CA 1 ATOM 2443 C C . SER A 1 316 ? -11.732 48.575 28.210 1.00 84.74 ? 316 SER A C 1 ATOM 2444 O O . SER A 1 316 ? -10.933 49.466 27.920 1.00 90.92 ? 316 SER A O 1 ATOM 2445 C CB . SER A 1 316 ? -10.433 47.414 30.017 1.00 74.30 ? 316 SER A CB 1 ATOM 2446 O OG . SER A 1 316 ? -11.210 48.002 31.045 1.00 80.31 ? 316 SER A OG 1 ATOM 2447 N N . VAL A 1 317 ? -13.047 48.715 28.087 1.00 77.81 ? 317 VAL A N 1 ATOM 2448 C CA . VAL A 1 317 ? -13.643 49.960 27.625 1.00 80.98 ? 317 VAL A CA 1 ATOM 2449 C C . VAL A 1 317 ? -14.199 50.739 28.810 1.00 87.27 ? 317 VAL A C 1 ATOM 2450 O O . VAL A 1 317 ? -15.191 50.336 29.414 1.00 91.02 ? 317 VAL A O 1 ATOM 2451 C CB . VAL A 1 317 ? -14.764 49.704 26.600 1.00 79.74 ? 317 VAL A CB 1 ATOM 2452 C CG1 . VAL A 1 317 ? -15.448 51.008 26.218 1.00 83.10 ? 317 VAL A CG1 1 ATOM 2453 C CG2 . VAL A 1 317 ? -14.206 49.000 25.370 1.00 73.94 ? 317 VAL A CG2 1 ATOM 2454 N N . SER A 1 318 ? -13.555 51.853 29.141 1.00 89.03 ? 318 SER A N 1 ATOM 2455 C CA . SER A 1 318 ? -13.942 52.643 30.302 1.00 96.68 ? 318 SER A CA 1 ATOM 2456 C C . SER A 1 318 ? -14.511 53.995 29.890 1.00 100.62 ? 318 SER A C 1 ATOM 2457 O O . SER A 1 318 ? -13.789 54.855 29.387 1.00 98.25 ? 318 SER A O 1 ATOM 2458 C CB . SER A 1 318 ? -12.745 52.841 31.234 1.00 97.46 ? 318 SER A CB 1 ATOM 2459 O OG . SER A 1 318 ? -12.168 51.597 31.591 1.00 93.45 ? 318 SER A OG 1 ATOM 2460 N N . LEU A 1 319 ? -15.809 54.175 30.110 1.00 106.13 ? 319 LEU A N 1 ATOM 2461 C CA . LEU A 1 319 ? -16.483 55.417 29.752 1.00 109.75 ? 319 LEU A CA 1 ATOM 2462 C C . LEU A 1 319 ? -16.425 56.424 30.895 1.00 116.78 ? 319 LEU A C 1 ATOM 2463 O O . LEU A 1 319 ? -16.848 56.131 32.013 1.00 121.62 ? 319 LEU A O 1 ATOM 2464 C CB . LEU A 1 319 ? -17.938 55.143 29.365 1.00 112.59 ? 319 LEU A CB 1 ATOM 2465 C CG . LEU A 1 319 ? -18.157 54.151 28.220 1.00 105.84 ? 319 LEU A CG 1 ATOM 2466 C CD1 . LEU A 1 319 ? -19.641 53.993 27.915 1.00 109.49 ? 319 LEU A CD1 1 ATOM 2467 C CD2 . LEU A 1 319 ? -17.393 54.588 26.981 1.00 98.74 ? 319 LEU A CD2 1 ATOM 2468 N N . GLN A 1 320 ? -15.896 57.609 30.610 1.00 114.91 ? 320 GLN A N 1 ATOM 2469 C CA . GLN A 1 320 ? -15.800 58.665 31.612 1.00 118.57 ? 320 GLN A CA 1 ATOM 2470 C C . GLN A 1 320 ? -17.123 59.406 31.750 1.00 121.68 ? 320 GLN A C 1 ATOM 2471 O O . GLN A 1 320 ? -17.788 59.697 30.756 1.00 119.88 ? 320 GLN A O 1 ATOM 2472 C CB . GLN A 1 320 ? -14.685 59.649 31.251 1.00 121.35 ? 320 GLN A CB 1 ATOM 2473 C CG . GLN A 1 320 ? -14.526 60.803 32.230 1.00 121.24 ? 320 GLN A CG 1 ATOM 2474 C CD . GLN A 1 320 ? -13.605 61.889 31.710 1.00 111.97 ? 320 GLN A CD 1 ATOM 2475 O OE1 . GLN A 1 320 ? -13.221 62.796 32.446 1.00 113.30 ? 320 GLN A OE1 1 ATOM 2476 N NE2 . GLN A 1 320 ? -13.252 61.805 30.432 1.00 106.56 ? 320 GLN A NE2 1 ATOM 2477 N N . ARG A 1 321 ? -17.503 59.708 32.987 1.00 125.48 ? 321 ARG A N 1 ATOM 2478 C CA . ARG A 1 321 ? -18.711 60.480 33.246 1.00 130.88 ? 321 ARG A CA 1 ATOM 2479 C C . ARG A 1 321 ? -18.363 61.836 33.851 1.00 137.76 ? 321 ARG A C 1 ATOM 2480 O O . ARG A 1 321 ? -17.192 62.146 34.068 1.00 127.76 ? 321 ARG A O 1 ATOM 2481 C CB . ARG A 1 321 ? -19.657 59.708 34.168 1.00 129.97 ? 321 ARG A CB 1 ATOM 2482 C CG . ARG A 1 321 ? -20.271 58.477 33.521 1.00 128.97 ? 321 ARG A CG 1 ATOM 2483 C CD . ARG A 1 321 ? -20.970 58.841 32.221 1.00 132.26 ? 321 ARG A CD 1 ATOM 2484 N NE . ARG A 1 321 ? -21.534 57.674 31.548 1.00 134.82 ? 321 ARG A NE 1 ATOM 2485 C CZ . ARG A 1 321 ? -22.130 57.714 30.360 1.00 132.69 ? 321 ARG A CZ 1 ATOM 2486 N NH1 . ARG A 1 321 ? -22.240 58.865 29.711 1.00 136.76 ? 321 ARG A NH1 1 ATOM 2487 N NH2 . ARG A 1 321 ? -22.615 56.604 29.821 1.00 122.40 ? 321 ARG A NH2 1 ATOM 2488 N N . ALA A 1 322 ? -19.387 62.639 34.120 1.00 148.10 ? 322 ALA A N 1 ATOM 2489 C CA . ALA A 1 322 ? -19.190 63.995 34.622 1.00 139.68 ? 322 ALA A CA 1 ATOM 2490 C C . ALA A 1 322 ? -18.600 64.004 36.029 1.00 139.46 ? 322 ALA A C 1 ATOM 2491 O O . ALA A 1 322 ? -17.871 64.924 36.400 1.00 136.83 ? 322 ALA A O 1 ATOM 2492 C CB . ALA A 1 322 ? -20.505 64.759 34.600 1.00 142.45 ? 322 ALA A CB 1 ATOM 2493 N N . SER A 1 323 ? -18.917 62.975 36.808 1.00 142.40 ? 323 SER A N 1 ATOM 2494 C CA . SER A 1 323 ? -18.447 62.883 38.186 1.00 145.41 ? 323 SER A CA 1 ATOM 2495 C C . SER A 1 323 ? -16.990 62.436 38.259 1.00 149.98 ? 323 SER A C 1 ATOM 2496 O O . SER A 1 323 ? -16.282 62.752 39.214 1.00 152.41 ? 323 SER A O 1 ATOM 2497 C CB . SER A 1 323 ? -19.327 61.921 38.986 1.00 137.29 ? 323 SER A CB 1 ATOM 2498 O OG . SER A 1 323 ? -19.285 60.616 38.435 1.00 133.59 ? 323 SER A OG 1 ATOM 2499 N N . GLY A 1 324 ? -16.548 61.706 37.241 1.00 148.57 ? 324 GLY A N 1 ATOM 2500 C CA . GLY A 1 324 ? -15.199 61.172 37.217 1.00 148.93 ? 324 GLY A CA 1 ATOM 2501 C C . GLY A 1 324 ? -15.181 59.674 37.447 1.00 139.35 ? 324 GLY A C 1 ATOM 2502 O O . GLY A 1 324 ? -14.150 59.022 37.286 1.00 130.24 ? 324 GLY A O 1 ATOM 2503 N N . ASP A 1 325 ? -16.331 59.127 37.830 1.00 145.80 ? 325 ASP A N 1 ATOM 2504 C CA . ASP A 1 325 ? -16.476 57.686 37.991 1.00 140.58 ? 325 ASP A CA 1 ATOM 2505 C C . ASP A 1 325 ? -16.653 57.027 36.629 1.00 135.52 ? 325 ASP A C 1 ATOM 2506 O O . ASP A 1 325 ? -17.457 57.477 35.812 1.00 141.85 ? 325 ASP A O 1 ATOM 2507 C CB . ASP A 1 325 ? -17.659 57.357 38.903 1.00 146.18 ? 325 ASP A CB 1 ATOM 2508 C CG . ASP A 1 325 ? -17.446 57.829 40.329 1.00 157.75 ? 325 ASP A CG 1 ATOM 2509 O OD1 . ASP A 1 325 ? -18.021 57.215 41.251 1.00 157.95 ? 325 ASP A OD1 1 ATOM 2510 O OD2 . ASP A 1 325 ? -16.701 58.812 40.526 1.00 166.75 ? 325 ASP A OD2 1 ATOM 2511 N N . PHE A 1 326 ? -15.899 55.961 36.387 1.00 127.61 ? 326 PHE A N 1 ATOM 2512 C CA . PHE A 1 326 ? -15.896 55.313 35.083 1.00 123.83 ? 326 PHE A CA 1 ATOM 2513 C C . PHE A 1 326 ? -16.904 54.172 34.988 1.00 121.72 ? 326 PHE A C 1 ATOM 2514 O O . PHE A 1 326 ? -17.067 53.389 35.924 1.00 121.10 ? 326 PHE A O 1 ATOM 2515 C CB . PHE A 1 326 ? -14.496 54.788 34.757 1.00 120.61 ? 326 PHE A CB 1 ATOM 2516 C CG . PHE A 1 326 ? -13.506 55.864 34.418 1.00 121.14 ? 326 PHE A CG 1 ATOM 2517 C CD1 . PHE A 1 326 ? -13.241 56.187 33.097 1.00 115.66 ? 326 PHE A CD1 1 ATOM 2518 C CD2 . PHE A 1 326 ? -12.839 56.552 35.419 1.00 123.45 ? 326 PHE A CD2 1 ATOM 2519 C CE1 . PHE A 1 326 ? -12.329 57.176 32.780 1.00 111.81 ? 326 PHE A CE1 1 ATOM 2520 C CE2 . PHE A 1 326 ? -11.926 57.543 35.108 1.00 120.70 ? 326 PHE A CE2 1 ATOM 2521 C CZ . PHE A 1 326 ? -11.671 57.855 33.787 1.00 114.54 ? 326 PHE A CZ 1 ATOM 2522 N N . GLN A 1 327 ? -17.577 54.091 33.845 1.00 120.31 ? 327 GLN A N 1 ATOM 2523 C CA . GLN A 1 327 ? -18.429 52.954 33.526 1.00 117.90 ? 327 GLN A CA 1 ATOM 2524 C C . GLN A 1 327 ? -17.669 52.038 32.578 1.00 112.38 ? 327 GLN A C 1 ATOM 2525 O O . GLN A 1 327 ? -17.439 52.384 31.419 1.00 118.60 ? 327 GLN A O 1 ATOM 2526 C CB . GLN A 1 327 ? -19.746 53.412 32.896 1.00 122.06 ? 327 GLN A CB 1 ATOM 2527 C CG . GLN A 1 327 ? -20.590 52.286 32.322 1.00 125.90 ? 327 GLN A CG 1 ATOM 2528 C CD . GLN A 1 327 ? -21.774 52.797 31.525 1.00 131.77 ? 327 GLN A CD 1 ATOM 2529 O OE1 . GLN A 1 327 ? -22.166 53.957 31.649 1.00 151.50 ? 327 GLN A OE1 1 ATOM 2530 N NE2 . GLN A 1 327 ? -22.346 51.932 30.694 1.00 117.89 ? 327 GLN A NE2 1 ATOM 2531 N N . THR A 1 328 ? -17.277 50.870 33.072 1.00 108.77 ? 328 THR A N 1 ATOM 2532 C CA . THR A 1 328 ? -16.364 50.011 32.333 1.00 102.25 ? 328 THR A CA 1 ATOM 2533 C C . THR A 1 328 ? -17.021 48.729 31.835 1.00 97.99 ? 328 THR A C 1 ATOM 2534 O O . THR A 1 328 ? -17.704 48.033 32.587 1.00 98.44 ? 328 THR A O 1 ATOM 2535 C CB . THR A 1 328 ? -15.138 49.641 33.193 1.00 100.54 ? 328 THR A CB 1 ATOM 2536 O OG1 . THR A 1 328 ? -14.518 50.836 33.683 1.00 104.63 ? 328 THR A OG1 1 ATOM 2537 C CG2 . THR A 1 328 ? -14.127 48.853 32.374 1.00 93.31 ? 328 THR A CG2 1 ATOM 2538 N N . THR A 1 329 ? -16.808 48.427 30.558 1.00 94.30 ? 329 THR A N 1 ATOM 2539 C CA . THR A 1 329 ? -17.248 47.166 29.979 1.00 89.26 ? 329 THR A CA 1 ATOM 2540 C C . THR A 1 329 ? -16.016 46.350 29.604 1.00 83.64 ? 329 THR A C 1 ATOM 2541 O O . THR A 1 329 ? -14.889 46.816 29.771 1.00 97.84 ? 329 THR A O 1 ATOM 2542 C CB . THR A 1 329 ? -18.131 47.385 28.738 1.00 89.11 ? 329 THR A CB 1 ATOM 2543 O OG1 . THR A 1 329 ? -18.701 48.699 28.781 1.00 108.37 ? 329 THR A OG1 1 ATOM 2544 C CG2 . THR A 1 329 ? -19.246 46.351 28.681 1.00 93.03 ? 329 THR A CG2 1 ATOM 2545 N N . LYS A 1 330 ? -16.223 45.138 29.100 1.00 79.98 ? 330 LYS A N 1 ATOM 2546 C CA . LYS A 1 330 ? -15.111 44.286 28.694 1.00 74.86 ? 330 LYS A CA 1 ATOM 2547 C C . LYS A 1 330 ? -15.411 43.563 27.386 1.00 81.67 ? 330 LYS A C 1 ATOM 2548 O O . LYS A 1 330 ? -16.491 42.998 27.209 1.00 90.21 ? 330 LYS A O 1 ATOM 2549 C CB . LYS A 1 330 ? -14.775 43.273 29.792 1.00 73.83 ? 330 LYS A CB 1 ATOM 2550 C CG . LYS A 1 330 ? -14.164 43.899 31.034 1.00 77.55 ? 330 LYS A CG 1 ATOM 2551 C CD . LYS A 1 330 ? -13.523 42.863 31.938 1.00 96.23 ? 330 LYS A CD 1 ATOM 2552 C CE . LYS A 1 330 ? -12.784 43.535 33.083 1.00 93.46 ? 330 LYS A CE 1 ATOM 2553 N NZ . LYS A 1 330 ? -11.976 42.571 33.875 1.00 106.07 ? 330 LYS A NZ 1 ATOM 2554 N N . LEU A 1 331 ? -14.447 43.588 26.472 1.00 84.99 ? 331 LEU A N 1 ATOM 2555 C CA . LEU A 1 331 ? -14.624 42.989 25.155 1.00 78.49 ? 331 LEU A CA 1 ATOM 2556 C C . LEU A 1 331 ? -13.611 41.873 24.915 1.00 77.03 ? 331 LEU A C 1 ATOM 2557 O O . LEU A 1 331 ? -12.413 42.123 24.788 1.00 87.33 ? 331 LEU A O 1 ATOM 2558 C CB . LEU A 1 331 ? -14.502 44.061 24.071 1.00 73.49 ? 331 LEU A CB 1 ATOM 2559 C CG . LEU A 1 331 ? -14.828 43.669 22.631 1.00 94.05 ? 331 LEU A CG 1 ATOM 2560 C CD1 . LEU A 1 331 ? -16.265 43.187 22.511 1.00 112.95 ? 331 LEU A CD1 1 ATOM 2561 C CD2 . LEU A 1 331 ? -14.578 44.848 21.709 1.00 88.42 ? 331 LEU A CD2 1 ATOM 2562 N N . ASN A 1 332 ? -14.107 40.640 24.855 1.00 66.93 ? 332 ASN A N 1 ATOM 2563 C CA . ASN A 1 332 ? -13.263 39.461 24.675 1.00 65.19 ? 332 ASN A CA 1 ATOM 2564 C C . ASN A 1 332 ? -12.904 39.175 23.220 1.00 73.86 ? 332 ASN A C 1 ATOM 2565 O O . ASN A 1 332 ? -13.674 39.472 22.307 1.00 88.33 ? 332 ASN A O 1 ATOM 2566 C CB . ASN A 1 332 ? -13.943 38.233 25.283 1.00 63.80 ? 332 ASN A CB 1 ATOM 2567 C CG . ASN A 1 332 ? -13.928 38.251 26.796 1.00 80.16 ? 332 ASN A CG 1 ATOM 2568 O OD1 . ASN A 1 332 ? -13.597 39.265 27.412 1.00 97.06 ? 332 ASN A OD1 1 ATOM 2569 N ND2 . ASN A 1 332 ? -14.286 37.128 27.406 1.00 85.53 ? 332 ASN A ND2 1 ATOM 2570 N N . GLY A 1 333 ? -11.725 38.596 23.015 1.00 74.61 ? 333 GLY A N 1 ATOM 2571 C CA . GLY A 1 333 ? -11.280 38.200 21.691 1.00 82.02 ? 333 GLY A CA 1 ATOM 2572 C C . GLY A 1 333 ? -12.052 37.008 21.160 1.00 87.13 ? 333 GLY A C 1 ATOM 2573 O O . GLY A 1 333 ? -13.022 36.561 21.771 1.00 99.54 ? 333 GLY A O 1 ATOM 2574 N N . PHE A 1 334 ? -11.619 36.486 20.018 1.00 81.54 ? 334 PHE A N 1 ATOM 2575 C CA . PHE A 1 334 ? -12.358 35.423 19.348 1.00 81.77 ? 334 PHE A CA 1 ATOM 2576 C C . PHE A 1 334 ? -11.500 34.178 19.136 1.00 82.80 ? 334 PHE A C 1 ATOM 2577 O O . PHE A 1 334 ? -11.769 33.124 19.712 1.00 93.97 ? 334 PHE A O 1 ATOM 2578 C CB . PHE A 1 334 ? -12.903 35.931 18.013 1.00 91.04 ? 334 PHE A CB 1 ATOM 2579 C CG . PHE A 1 334 ? -13.575 37.273 18.110 1.00 76.37 ? 334 PHE A CG 1 ATOM 2580 C CD1 . PHE A 1 334 ? -12.867 38.437 17.854 1.00 97.75 ? 334 PHE A CD1 1 ATOM 2581 C CD2 . PHE A 1 334 ? -14.910 37.372 18.466 1.00 72.07 ? 334 PHE A CD2 1 ATOM 2582 C CE1 . PHE A 1 334 ? -13.478 39.674 17.945 1.00 98.33 ? 334 PHE A CE1 1 ATOM 2583 C CE2 . PHE A 1 334 ? -15.528 38.606 18.558 1.00 98.21 ? 334 PHE A CE2 1 ATOM 2584 C CZ . PHE A 1 334 ? -14.811 39.758 18.298 1.00 95.17 ? 334 PHE A CZ 1 ATOM 2585 N N . GLU A 1 335 ? -10.471 34.299 18.303 1.00 91.29 ? 335 GLU A N 1 ATOM 2586 C CA . GLU A 1 335 ? -9.556 33.189 18.056 1.00 80.59 ? 335 GLU A CA 1 ATOM 2587 C C . GLU A 1 335 ? -8.545 33.035 19.190 1.00 71.40 ? 335 GLU A C 1 ATOM 2588 O O . GLU A 1 335 ? -8.246 33.994 19.900 1.00 79.31 ? 335 GLU A O 1 ATOM 2589 C CB . GLU A 1 335 ? -8.825 33.380 16.727 1.00 83.77 ? 335 GLU A CB 1 ATOM 2590 C CG . GLU A 1 335 ? -9.738 33.399 15.513 1.00 102.28 ? 335 GLU A CG 1 ATOM 2591 C CD . GLU A 1 335 ? -8.970 33.468 14.209 1.00 118.13 ? 335 GLU A CD 1 ATOM 2592 O OE1 . GLU A 1 335 ? -9.614 33.536 13.141 1.00 123.87 ? 335 GLU A OE1 1 ATOM 2593 O OE2 . GLU A 1 335 ? -7.722 33.447 14.253 1.00 128.59 ? 335 GLU A OE2 1 ATOM 2594 N N . VAL A 1 336 ? -8.023 31.823 19.356 1.00 80.00 ? 336 VAL A N 1 ATOM 2595 C CA . VAL A 1 336 ? -7.027 31.555 20.388 1.00 91.58 ? 336 VAL A CA 1 ATOM 2596 C C . VAL A 1 336 ? -5.620 31.916 19.919 1.00 86.91 ? 336 VAL A C 1 ATOM 2597 O O . VAL A 1 336 ? -5.283 31.742 18.746 1.00 92.17 ? 336 VAL A O 1 ATOM 2598 C CB . VAL A 1 336 ? -7.053 30.081 20.837 1.00 72.53 ? 336 VAL A CB 1 ATOM 2599 C CG1 . VAL A 1 336 ? -8.207 29.839 21.801 1.00 72.98 ? 336 VAL A CG1 1 ATOM 2600 C CG2 . VAL A 1 336 ? -7.141 29.157 19.632 1.00 121.53 ? 336 VAL A CG2 1 ATOM 2601 N N . PHE A 1 337 ? -4.819 32.437 20.848 1.00 84.64 ? 337 PHE A N 1 ATOM 2602 C CA . PHE A 1 337 ? -3.458 32.909 20.578 1.00 81.12 ? 337 PHE A CA 1 ATOM 2603 C C . PHE A 1 337 ? -3.449 34.013 19.522 1.00 81.10 ? 337 PHE A C 1 ATOM 2604 O O . PHE A 1 337 ? -2.440 34.246 18.854 1.00 81.67 ? 337 PHE A O 1 ATOM 2605 C CB . PHE A 1 337 ? -2.557 31.750 20.143 1.00 89.53 ? 337 PHE A CB 1 ATOM 2606 C CG . PHE A 1 337 ? -2.427 30.663 21.173 1.00 81.26 ? 337 PHE A CG 1 ATOM 2607 C CD1 . PHE A 1 337 ? -2.387 30.967 22.525 1.00 72.16 ? 337 PHE A CD1 1 ATOM 2608 C CD2 . PHE A 1 337 ? -2.352 29.335 20.788 1.00 86.80 ? 337 PHE A CD2 1 ATOM 2609 C CE1 . PHE A 1 337 ? -2.269 29.965 23.471 1.00 90.38 ? 337 PHE A CE1 1 ATOM 2610 C CE2 . PHE A 1 337 ? -2.237 28.330 21.729 1.00 73.50 ? 337 PHE A CE2 1 ATOM 2611 C CZ . PHE A 1 337 ? -2.195 28.644 23.072 1.00 84.42 ? 337 PHE A CZ 1 ATOM 2612 N N . ALA A 1 338 ? -4.582 34.695 19.386 1.00 84.83 ? 338 ALA A N 1 ATOM 2613 C CA . ALA A 1 338 ? -4.715 35.797 18.443 1.00 63.53 ? 338 ALA A CA 1 ATOM 2614 C C . ALA A 1 338 ? -4.129 37.081 19.014 1.00 74.29 ? 338 ALA A C 1 ATOM 2615 O O . ALA A 1 338 ? -3.729 37.973 18.264 1.00 86.66 ? 338 ALA A O 1 ATOM 2616 C CB . ALA A 1 338 ? -6.177 36.001 18.075 1.00 84.06 ? 338 ALA A CB 1 ATOM 2617 N N . ARG A 1 339 ? -4.090 37.160 20.343 1.00 86.32 ? 339 ARG A N 1 ATOM 2618 C CA . ARG A 1 339 ? -3.645 38.360 21.050 1.00 89.07 ? 339 ARG A CA 1 ATOM 2619 C C . ARG A 1 339 ? -4.482 39.559 20.609 1.00 71.57 ? 339 ARG A C 1 ATOM 2620 O O . ARG A 1 339 ? -4.002 40.460 19.922 1.00 76.02 ? 339 ARG A O 1 ATOM 2621 C CB . ARG A 1 339 ? -2.151 38.602 20.825 1.00 66.76 ? 339 ARG A CB 1 ATOM 2622 C CG . ARG A 1 339 ? -1.290 37.460 21.341 1.00 66.94 ? 339 ARG A CG 1 ATOM 2623 C CD . ARG A 1 339 ? 0.196 37.743 21.218 1.00 76.49 ? 339 ARG A CD 1 ATOM 2624 N NE . ARG A 1 339 ? 0.983 36.710 21.890 1.00 57.01 ? 339 ARG A NE 1 ATOM 2625 C CZ . ARG A 1 339 ? 2.311 36.700 21.960 1.00 78.24 ? 339 ARG A CZ 1 ATOM 2626 N NH1 . ARG A 1 339 ? 3.017 37.669 21.395 1.00 105.86 ? 339 ARG A NH1 1 ATOM 2627 N NH2 . ARG A 1 339 ? 2.933 35.718 22.595 1.00 99.77 ? 339 ARG A NH2 1 ATOM 2628 N N . PHE A 1 340 ? -5.744 39.543 21.027 1.00 56.93 ? 340 PHE A N 1 ATOM 2629 C CA . PHE A 1 340 ? -6.773 40.457 20.540 1.00 57.79 ? 340 PHE A CA 1 ATOM 2630 C C . PHE A 1 340 ? -6.557 41.931 20.883 1.00 70.48 ? 340 PHE A C 1 ATOM 2631 O O . PHE A 1 340 ? -6.886 42.805 20.085 1.00 92.42 ? 340 PHE A O 1 ATOM 2632 C CB . PHE A 1 340 ? -8.134 40.002 21.080 1.00 81.87 ? 340 PHE A CB 1 ATOM 2633 C CG . PHE A 1 340 ? -9.259 40.953 20.794 1.00 58.51 ? 340 PHE A CG 1 ATOM 2634 C CD1 . PHE A 1 340 ? -9.659 41.205 19.493 1.00 59.76 ? 340 PHE A CD1 1 ATOM 2635 C CD2 . PHE A 1 340 ? -9.932 41.578 21.830 1.00 61.62 ? 340 PHE A CD2 1 ATOM 2636 C CE1 . PHE A 1 340 ? -10.701 42.076 19.229 1.00 71.90 ? 340 PHE A CE1 1 ATOM 2637 C CE2 . PHE A 1 340 ? -10.974 42.448 21.573 1.00 75.42 ? 340 PHE A CE2 1 ATOM 2638 C CZ . PHE A 1 340 ? -11.357 42.697 20.271 1.00 73.35 ? 340 PHE A CZ 1 ATOM 2639 N N . GLY A 1 341 ? -6.012 42.210 22.061 1.00 78.04 ? 341 GLY A N 1 ATOM 2640 C CA . GLY A 1 341 ? -5.872 43.583 22.518 1.00 94.06 ? 341 GLY A CA 1 ATOM 2641 C C . GLY A 1 341 ? -4.512 44.204 22.258 1.00 82.93 ? 341 GLY A C 1 ATOM 2642 O O . GLY A 1 341 ? -4.133 45.178 22.909 1.00 78.94 ? 341 GLY A O 1 ATOM 2643 N N . SER A 1 342 ? -3.782 43.643 21.298 1.00 76.02 ? 342 SER A N 1 ATOM 2644 C CA . SER A 1 342 ? -2.412 44.063 21.016 1.00 76.12 ? 342 SER A CA 1 ATOM 2645 C C . SER A 1 342 ? -2.306 45.508 20.531 1.00 74.42 ? 342 SER A C 1 ATOM 2646 O O . SER A 1 342 ? -1.388 46.229 20.921 1.00 82.68 ? 342 SER A O 1 ATOM 2647 C CB . SER A 1 342 ? -1.781 43.126 19.985 1.00 74.40 ? 342 SER A CB 1 ATOM 2648 O OG . SER A 1 342 ? -1.691 41.806 20.488 1.00 89.13 ? 342 SER A OG 1 ATOM 2649 N N . ALA A 1 343 ? -3.236 45.930 19.680 1.00 77.27 ? 343 ALA A N 1 ATOM 2650 C CA . ALA A 1 343 ? -3.218 47.293 19.159 1.00 76.44 ? 343 ALA A CA 1 ATOM 2651 C C . ALA A 1 343 ? -4.610 47.919 19.136 1.00 78.51 ? 343 ALA A C 1 ATOM 2652 O O . ALA A 1 343 ? -5.551 47.345 18.589 1.00 89.34 ? 343 ALA A O 1 ATOM 2653 C CB . ALA A 1 343 ? -2.610 47.313 17.764 1.00 77.61 ? 343 ALA A CB 1 ATOM 2654 N N . ILE A 1 344 ? -4.732 49.100 19.734 1.00 53.55 ? 344 ILE A N 1 ATOM 2655 C CA . ILE A 1 344 ? -5.998 49.827 19.751 1.00 66.17 ? 344 ILE A CA 1 ATOM 2656 C C . ILE A 1 344 ? -5.841 51.193 19.086 1.00 67.08 ? 344 ILE A C 1 ATOM 2657 O O . ILE A 1 344 ? -5.153 52.071 19.608 1.00 98.71 ? 344 ILE A O 1 ATOM 2658 C CB . ILE A 1 344 ? -6.522 50.014 21.190 1.00 61.39 ? 344 ILE A CB 1 ATOM 2659 C CG1 . ILE A 1 344 ? -6.464 48.691 21.958 1.00 56.04 ? 344 ILE A CG1 1 ATOM 2660 C CG2 . ILE A 1 344 ? -7.938 50.560 21.176 1.00 57.05 ? 344 ILE A CG2 1 ATOM 2661 C CD1 . ILE A 1 344 ? -6.983 48.784 23.379 1.00 57.71 ? 344 ILE A CD1 1 ATOM 2662 N N . ALA A 1 345 ? -6.481 51.368 17.933 1.00 60.59 ? 345 ALA A N 1 ATOM 2663 C CA . ALA A 1 345 ? -6.353 52.602 17.160 1.00 81.55 ? 345 ALA A CA 1 ATOM 2664 C C . ALA A 1 345 ? -7.668 53.363 17.039 1.00 67.03 ? 345 ALA A C 1 ATOM 2665 O O . ALA A 1 345 ? -8.628 52.859 16.455 1.00 60.69 ? 345 ALA A O 1 ATOM 2666 C CB . ALA A 1 345 ? -5.807 52.296 15.780 1.00 88.73 ? 345 ALA A CB 1 ATOM 2667 N N . PRO A 1 346 ? -7.719 54.582 17.599 1.00 60.78 ? 346 PRO A N 1 ATOM 2668 C CA . PRO A 1 346 ? -8.872 55.464 17.389 1.00 62.11 ? 346 PRO A CA 1 ATOM 2669 C C . PRO A 1 346 ? -9.016 55.841 15.918 1.00 65.04 ? 346 PRO A C 1 ATOM 2670 O O . PRO A 1 346 ? -8.053 56.311 15.314 1.00 73.75 ? 346 PRO A O 1 ATOM 2671 C CB . PRO A 1 346 ? -8.536 56.696 18.234 1.00 62.46 ? 346 PRO A CB 1 ATOM 2672 C CG . PRO A 1 346 ? -7.518 56.226 19.221 1.00 62.63 ? 346 PRO A CG 1 ATOM 2673 C CD . PRO A 1 346 ? -6.729 55.171 18.517 1.00 58.23 ? 346 PRO A CD 1 ATOM 2674 N N . LEU A 1 347 ? -10.203 55.718 15.330 1.00 80.74 ? 347 LEU A N 1 ATOM 2675 C CA . LEU A 1 347 ? -10.426 56.104 13.923 1.00 81.66 ? 347 LEU A CA 1 ATOM 2676 C C . LEU A 1 347 ? -11.237 57.367 13.873 1.00 76.60 ? 347 LEU A C 1 ATOM 2677 O O . LEU A 1 347 ? -11.731 57.811 12.871 1.00 72.30 ? 347 LEU A O 1 ATOM 2678 C CB . LEU A 1 347 ? -11.185 55.026 13.204 1.00 76.67 ? 347 LEU A CB 1 ATOM 2679 C CG . LEU A 1 347 ? -10.648 53.686 13.600 1.00 70.93 ? 347 LEU A CG 1 ATOM 2680 C CD1 . LEU A 1 347 ? -10.530 52.858 12.352 1.00 77.30 ? 347 LEU A CD1 1 ATOM 2681 C CD2 . LEU A 1 347 ? -9.283 53.946 14.195 1.00 77.61 ? 347 LEU A CD2 1 ATOM 2682 N N . GLY A 1 348 ? -11.368 57.892 15.051 1.00 76.66 ? 348 GLY A N 1 ATOM 2683 C CA . GLY A 1 348 ? -11.963 59.150 15.410 1.00 83.61 ? 348 GLY A CA 1 ATOM 2684 C C . GLY A 1 348 ? -13.403 58.998 15.044 1.00 94.62 ? 348 GLY A C 1 ATOM 2685 O O . GLY A 1 348 ? -14.232 58.596 15.848 1.00 99.94 ? 348 GLY A O 1 ATOM 2686 N N . ASP A 1 349 ? -13.686 59.124 13.750 1.00 84.13 ? 349 ASP A N 1 ATOM 2687 C CA . ASP A 1 349 ? -14.990 58.718 13.223 1.00 94.82 ? 349 ASP A CA 1 ATOM 2688 C C . ASP A 1 349 ? -14.951 58.163 11.788 1.00 107.42 ? 349 ASP A C 1 ATOM 2689 O O . ASP A 1 349 ? -14.821 58.932 10.835 1.00 111.61 ? 349 ASP A O 1 ATOM 2690 C CB . ASP A 1 349 ? -15.982 59.881 13.303 1.00 92.38 ? 349 ASP A CB 1 ATOM 2691 C CG . ASP A 1 349 ? -17.423 59.428 13.178 1.00 107.74 ? 349 ASP A CG 1 ATOM 2692 O OD1 . ASP A 1 349 ? -17.664 58.203 13.177 1.00 123.34 ? 349 ASP A OD1 1 ATOM 2693 O OD2 . ASP A 1 349 ? -18.315 60.297 13.079 1.00 100.20 ? 349 ASP A OD2 1 ATOM 2694 N N . LEU A 1 350 ? -15.078 56.842 11.626 1.00 100.51 ? 350 LEU A N 1 ATOM 2695 C CA . LEU A 1 350 ? -15.245 56.271 10.277 1.00 81.21 ? 350 LEU A CA 1 ATOM 2696 C C . LEU A 1 350 ? -16.461 56.603 9.352 1.00 84.78 ? 350 LEU A C 1 ATOM 2697 O O . LEU A 1 350 ? -16.262 57.067 8.260 1.00 108.43 ? 350 LEU A O 1 ATOM 2698 C CB . LEU A 1 350 ? -15.111 54.766 10.375 1.00 80.77 ? 350 LEU A CB 1 ATOM 2699 C CG . LEU A 1 350 ? -14.355 54.172 9.210 1.00 80.54 ? 350 LEU A CG 1 ATOM 2700 C CD1 . LEU A 1 350 ? -13.191 55.063 8.885 1.00 86.43 ? 350 LEU A CD1 1 ATOM 2701 C CD2 . LEU A 1 350 ? -13.869 52.778 9.519 1.00 78.38 ? 350 LEU A CD2 1 ATOM 2702 N N . ASP A 1 351 ? -17.693 56.313 9.750 1.00 87.56 ? 351 ASP A N 1 ATOM 2703 C CA . ASP A 1 351 ? -18.880 56.340 8.905 1.00 102.72 ? 351 ASP A CA 1 ATOM 2704 C C . ASP A 1 351 ? -19.603 57.681 8.982 1.00 114.43 ? 351 ASP A C 1 ATOM 2705 O O . ASP A 1 351 ? -20.671 57.848 8.390 1.00 114.85 ? 351 ASP A O 1 ATOM 2706 C CB . ASP A 1 351 ? -19.829 55.204 9.293 1.00 104.98 ? 351 ASP A CB 1 ATOM 2707 C CG . ASP A 1 351 ? -20.133 55.178 10.779 1.00 109.94 ? 351 ASP A CG 1 ATOM 2708 O OD1 . ASP A 1 351 ? -21.181 54.613 11.158 1.00 111.85 ? 351 ASP A OD1 1 ATOM 2709 O OD2 . ASP A 1 351 ? -19.330 55.722 11.569 1.00 120.96 ? 351 ASP A OD2 1 ATOM 2710 N N . GLN A 1 352 ? -19.015 58.623 9.717 1.00 111.85 ? 352 GLN A N 1 ATOM 2711 C CA . GLN A 1 352 ? -19.611 59.939 9.947 1.00 96.47 ? 352 GLN A CA 1 ATOM 2712 C C . GLN A 1 352 ? -21.002 59.812 10.560 1.00 101.22 ? 352 GLN A C 1 ATOM 2713 O O . GLN A 1 352 ? -21.902 60.597 10.256 1.00 100.30 ? 352 GLN A O 1 ATOM 2714 C CB . GLN A 1 352 ? -19.673 60.747 8.647 1.00 94.51 ? 352 GLN A CB 1 ATOM 2715 C CG . GLN A 1 352 ? -18.315 61.180 8.116 1.00 126.72 ? 352 GLN A CG 1 ATOM 2716 C CD . GLN A 1 352 ? -17.638 62.218 8.993 1.00 131.49 ? 352 GLN A CD 1 ATOM 2717 O OE1 . GLN A 1 352 ? -18.297 62.960 9.721 1.00 137.45 ? 352 GLN A OE1 1 ATOM 2718 N NE2 . GLN A 1 352 ? -16.314 62.276 8.923 1.00 91.11 ? 352 GLN A NE2 1 ATOM 2719 N N . ASP A 1 353 ? -21.164 58.816 11.427 1.00 113.96 ? 353 ASP A N 1 ATOM 2720 C CA . ASP A 1 353 ? -22.442 58.552 12.078 1.00 100.01 ? 353 ASP A CA 1 ATOM 2721 C C . ASP A 1 353 ? -22.753 59.583 13.156 1.00 105.72 ? 353 ASP A C 1 ATOM 2722 O O . ASP A 1 353 ? -23.887 59.683 13.623 1.00 115.13 ? 353 ASP A O 1 ATOM 2723 C CB . ASP A 1 353 ? -22.450 57.145 12.685 1.00 98.78 ? 353 ASP A CB 1 ATOM 2724 C CG . ASP A 1 353 ? -21.181 56.830 13.462 1.00 124.05 ? 353 ASP A CG 1 ATOM 2725 O OD1 . ASP A 1 353 ? -20.403 57.762 13.754 1.00 140.48 ? 353 ASP A OD1 1 ATOM 2726 O OD2 . ASP A 1 353 ? -20.961 55.644 13.784 1.00 123.21 ? 353 ASP A OD2 1 ATOM 2727 N N . GLY A 1 354 ? -21.740 60.352 13.542 1.00 94.34 ? 354 GLY A N 1 ATOM 2728 C CA . GLY A 1 354 ? -21.883 61.327 14.605 1.00 95.62 ? 354 GLY A CA 1 ATOM 2729 C C . GLY A 1 354 ? -21.191 60.855 15.868 1.00 95.25 ? 354 GLY A C 1 ATOM 2730 O O . GLY A 1 354 ? -21.002 61.621 16.811 1.00 100.91 ? 354 GLY A O 1 ATOM 2731 N N . PHE A 1 355 ? -20.816 59.581 15.880 1.00 94.20 ? 355 PHE A N 1 ATOM 2732 C CA . PHE A 1 355 ? -20.114 58.999 17.014 1.00 93.62 ? 355 PHE A CA 1 ATOM 2733 C C . PHE A 1 355 ? -18.790 58.389 16.567 1.00 91.03 ? 355 PHE A C 1 ATOM 2734 O O . PHE A 1 355 ? -18.732 57.682 15.558 1.00 101.22 ? 355 PHE A O 1 ATOM 2735 C CB . PHE A 1 355 ? -20.981 57.941 17.699 1.00 95.27 ? 355 PHE A CB 1 ATOM 2736 C CG . PHE A 1 355 ? -22.316 58.456 18.158 1.00 99.82 ? 355 PHE A CG 1 ATOM 2737 C CD1 . PHE A 1 355 ? -22.441 59.107 19.374 1.00 102.65 ? 355 PHE A CD1 1 ATOM 2738 C CD2 . PHE A 1 355 ? -23.447 58.284 17.376 1.00 101.82 ? 355 PHE A CD2 1 ATOM 2739 C CE1 . PHE A 1 355 ? -23.669 59.579 19.800 1.00 114.55 ? 355 PHE A CE1 1 ATOM 2740 C CE2 . PHE A 1 355 ? -24.677 58.754 17.797 1.00 126.75 ? 355 PHE A CE2 1 ATOM 2741 C CZ . PHE A 1 355 ? -24.788 59.403 19.010 1.00 129.07 ? 355 PHE A CZ 1 ATOM 2742 N N . ASN A 1 356 ? -17.730 58.669 17.318 1.00 86.89 ? 356 ASN A N 1 ATOM 2743 C CA . ASN A 1 356 ? -16.404 58.168 16.981 1.00 87.36 ? 356 ASN A CA 1 ATOM 2744 C C . ASN A 1 356 ? -16.341 56.645 17.023 1.00 90.83 ? 356 ASN A C 1 ATOM 2745 O O . ASN A 1 356 ? -17.059 56.003 17.790 1.00 98.80 ? 356 ASN A O 1 ATOM 2746 C CB . ASN A 1 356 ? -15.351 58.763 17.919 1.00 81.54 ? 356 ASN A CB 1 ATOM 2747 C CG . ASN A 1 356 ? -15.256 60.271 17.803 1.00 81.50 ? 356 ASN A CG 1 ATOM 2748 O OD1 . ASN A 1 356 ? -15.672 60.854 16.802 1.00 100.25 ? 356 ASN A OD1 1 ATOM 2749 N ND2 . ASN A 1 356 ? -14.701 60.911 18.826 1.00 82.15 ? 356 ASN A ND2 1 ATOM 2750 N N . ASP A 1 357 ? -15.482 56.076 16.186 1.00 83.09 ? 357 ASP A N 1 ATOM 2751 C CA . ASP A 1 357 ? -15.339 54.630 16.099 1.00 76.84 ? 357 ASP A CA 1 ATOM 2752 C C . ASP A 1 357 ? -13.906 54.239 16.458 1.00 71.78 ? 357 ASP A C 1 ATOM 2753 O O . ASP A 1 357 ? -13.074 55.107 16.723 1.00 84.20 ? 357 ASP A O 1 ATOM 2754 C CB . ASP A 1 357 ? -15.713 54.147 14.696 1.00 81.19 ? 357 ASP A CB 1 ATOM 2755 C CG . ASP A 1 357 ? -17.023 54.751 14.203 1.00 101.79 ? 357 ASP A CG 1 ATOM 2756 O OD1 . ASP A 1 357 ? -17.993 54.801 14.988 1.00 109.05 ? 357 ASP A OD1 1 ATOM 2757 O OD2 . ASP A 1 357 ? -17.079 55.189 13.035 1.00 104.13 ? 357 ASP A OD2 1 ATOM 2758 N N . ILE A 1 358 ? -13.612 52.944 16.464 1.00 74.17 ? 358 ILE A N 1 ATOM 2759 C CA . ILE A 1 358 ? -12.295 52.483 16.890 1.00 71.98 ? 358 ILE A CA 1 ATOM 2760 C C . ILE A 1 358 ? -11.930 51.147 16.244 1.00 74.51 ? 358 ILE A C 1 ATOM 2761 O O . ILE A 1 358 ? -12.802 50.408 15.784 1.00 73.87 ? 358 ILE A O 1 ATOM 2762 C CB . ILE A 1 358 ? -12.226 52.360 18.433 1.00 82.15 ? 358 ILE A CB 1 ATOM 2763 C CG1 . ILE A 1 358 ? -10.800 52.588 18.941 1.00 81.58 ? 358 ILE A CG1 1 ATOM 2764 C CG2 . ILE A 1 358 ? -12.785 51.021 18.904 1.00 65.62 ? 358 ILE A CG2 1 ATOM 2765 C CD1 . ILE A 1 358 ? -10.710 52.725 20.444 1.00 79.10 ? 358 ILE A CD1 1 ATOM 2766 N N . ALA A 1 359 ? -10.634 50.849 16.201 1.00 76.23 ? 359 ALA A N 1 ATOM 2767 C CA . ALA A 1 359 ? -10.152 49.607 15.605 1.00 65.53 ? 359 ALA A CA 1 ATOM 2768 C C . ALA A 1 359 ? -9.281 48.825 16.581 1.00 62.55 ? 359 ALA A C 1 ATOM 2769 O O . ALA A 1 359 ? -8.373 49.378 17.201 1.00 76.00 ? 359 ALA A O 1 ATOM 2770 C CB . ALA A 1 359 ? -9.382 49.895 14.328 1.00 62.96 ? 359 ALA A CB 1 ATOM 2771 N N . ILE A 1 360 ? -9.566 47.533 16.712 1.00 68.49 ? 360 ILE A N 1 ATOM 2772 C CA . ILE A 1 360 ? -8.799 46.656 17.588 1.00 71.16 ? 360 ILE A CA 1 ATOM 2773 C C . ILE A 1 360 ? -8.205 45.508 16.777 1.00 70.15 ? 360 ILE A C 1 ATOM 2774 O O . ILE A 1 360 ? -8.909 44.855 16.009 1.00 76.26 ? 360 ILE A O 1 ATOM 2775 C CB . ILE A 1 360 ? -9.670 46.102 18.731 1.00 58.02 ? 360 ILE A CB 1 ATOM 2776 C CG1 . ILE A 1 360 ? -10.333 47.250 19.498 1.00 58.30 ? 360 ILE A CG1 1 ATOM 2777 C CG2 . ILE A 1 360 ? -8.843 45.250 19.670 1.00 56.63 ? 360 ILE A CG2 1 ATOM 2778 C CD1 . ILE A 1 360 ? -11.185 46.799 20.663 1.00 59.07 ? 360 ILE A CD1 1 ATOM 2779 N N . ALA A 1 361 ? -6.908 45.267 16.947 1.00 57.88 ? 361 ALA A N 1 ATOM 2780 C CA . ALA A 1 361 ? -6.199 44.316 16.096 1.00 69.86 ? 361 ALA A CA 1 ATOM 2781 C C . ALA A 1 361 ? -5.713 43.078 16.840 1.00 81.55 ? 361 ALA A C 1 ATOM 2782 O O . ALA A 1 361 ? -5.201 43.166 17.956 1.00 89.58 ? 361 ALA A O 1 ATOM 2783 C CB . ALA A 1 361 ? -5.023 45.000 15.421 1.00 83.88 ? 361 ALA A CB 1 ATOM 2784 N N . ALA A 1 362 ? -5.859 41.927 16.192 1.00 95.25 ? 362 ALA A N 1 ATOM 2785 C CA . ALA A 1 362 ? -5.338 40.665 16.704 1.00 72.35 ? 362 ALA A CA 1 ATOM 2786 C C . ALA A 1 362 ? -4.323 40.108 15.711 1.00 63.22 ? 362 ALA A C 1 ATOM 2787 O O . ALA A 1 362 ? -4.667 39.298 14.848 1.00 63.83 ? 362 ALA A O 1 ATOM 2788 C CB . ALA A 1 362 ? -6.461 39.672 16.940 1.00 61.48 ? 362 ALA A CB 1 ATOM 2789 N N . PRO A 1 363 ? -3.062 40.548 15.838 1.00 60.37 ? 363 PRO A N 1 ATOM 2790 C CA . PRO A 1 363 ? -1.977 40.353 14.867 1.00 61.65 ? 363 PRO A CA 1 ATOM 2791 C C . PRO A 1 363 ? -1.685 38.901 14.505 1.00 92.25 ? 363 PRO A C 1 ATOM 2792 O O . PRO A 1 363 ? -1.309 38.616 13.369 1.00 107.53 ? 363 PRO A O 1 ATOM 2793 C CB . PRO A 1 363 ? -0.761 40.962 15.575 1.00 81.75 ? 363 PRO A CB 1 ATOM 2794 C CG . PRO A 1 363 ? -1.330 41.912 16.562 1.00 57.53 ? 363 PRO A CG 1 ATOM 2795 C CD . PRO A 1 363 ? -2.607 41.294 17.022 1.00 57.88 ? 363 PRO A CD 1 ATOM 2796 N N . TYR A 1 364 ? -1.802 38.003 15.472 1.00 90.81 ? 364 TYR A N 1 ATOM 2797 C CA . TYR A 1 364 ? -1.485 36.602 15.241 1.00 65.57 ? 364 TYR A CA 1 ATOM 2798 C C . TYR A 1 364 ? -2.738 35.763 14.987 1.00 75.18 ? 364 TYR A C 1 ATOM 2799 O O . TYR A 1 364 ? -2.660 34.545 14.838 1.00 110.60 ? 364 TYR A O 1 ATOM 2800 C CB . TYR A 1 364 ? -0.665 36.072 16.414 1.00 80.26 ? 364 TYR A CB 1 ATOM 2801 C CG . TYR A 1 364 ? 0.544 36.949 16.682 1.00 69.57 ? 364 TYR A CG 1 ATOM 2802 C CD1 . TYR A 1 364 ? 0.528 37.900 17.693 1.00 64.58 ? 364 TYR A CD1 1 ATOM 2803 C CD2 . TYR A 1 364 ? 1.682 36.857 15.890 1.00 77.66 ? 364 TYR A CD2 1 ATOM 2804 C CE1 . TYR A 1 364 ? 1.620 38.715 17.928 1.00 81.05 ? 364 TYR A CE1 1 ATOM 2805 C CE2 . TYR A 1 364 ? 2.781 37.669 16.117 1.00 95.76 ? 364 TYR A CE2 1 ATOM 2806 C CZ . TYR A 1 364 ? 2.743 38.596 17.138 1.00 89.97 ? 364 TYR A CZ 1 ATOM 2807 O OH . TYR A 1 364 ? 3.830 39.408 17.372 1.00 95.21 ? 364 TYR A OH 1 ATOM 2808 N N . GLY A 1 365 ? -3.892 36.421 14.940 1.00 80.67 ? 365 GLY A N 1 ATOM 2809 C CA . GLY A 1 365 ? -5.138 35.746 14.621 1.00 81.80 ? 365 GLY A CA 1 ATOM 2810 C C . GLY A 1 365 ? -5.379 35.640 13.125 1.00 92.00 ? 365 GLY A C 1 ATOM 2811 O O . GLY A 1 365 ? -4.463 35.828 12.324 1.00 93.15 ? 365 GLY A O 1 ATOM 2812 N N . GLY A 1 366 ? -6.616 35.332 12.748 1.00 73.61 ? 366 GLY A N 1 ATOM 2813 C CA . GLY A 1 366 ? -6.983 35.230 11.348 1.00 76.60 ? 366 GLY A CA 1 ATOM 2814 C C . GLY A 1 366 ? -6.712 33.861 10.752 1.00 127.55 ? 366 GLY A C 1 ATOM 2815 O O . GLY A 1 366 ? -6.428 32.902 11.472 1.00 106.38 ? 366 GLY A O 1 ATOM 2816 N N . GLU A 1 367 ? -6.803 33.770 9.429 1.00 133.99 ? 367 GLU A N 1 ATOM 2817 C CA . GLU A 1 367 ? -6.539 32.519 8.730 1.00 132.04 ? 367 GLU A CA 1 ATOM 2818 C C . GLU A 1 367 ? -5.042 32.250 8.631 1.00 132.19 ? 367 GLU A C 1 ATOM 2819 O O . GLU A 1 367 ? -4.296 33.055 8.074 1.00 122.90 ? 367 GLU A O 1 ATOM 2820 C CB . GLU A 1 367 ? -7.155 32.547 7.332 1.00 134.38 ? 367 GLU A CB 1 ATOM 2821 C CG . GLU A 1 367 ? -6.823 31.331 6.486 1.00 146.12 ? 367 GLU A CG 1 ATOM 2822 C CD . GLU A 1 367 ? -7.076 31.567 5.011 1.00 160.36 ? 367 GLU A CD 1 ATOM 2823 O OE1 . GLU A 1 367 ? -7.162 32.745 4.605 1.00 157.09 ? 367 GLU A OE1 1 ATOM 2824 O OE2 . GLU A 1 367 ? -7.190 30.576 4.258 1.00 160.30 ? 367 GLU A OE2 1 ATOM 2825 N N . ASP A 1 368 ? -4.620 31.107 9.168 1.00 138.58 ? 368 ASP A N 1 ATOM 2826 C CA . ASP A 1 368 ? -3.221 30.683 9.147 1.00 128.88 ? 368 ASP A CA 1 ATOM 2827 C C . ASP A 1 368 ? -2.281 31.751 9.708 1.00 96.85 ? 368 ASP A C 1 ATOM 2828 O O . ASP A 1 368 ? -1.196 31.978 9.172 1.00 91.79 ? 368 ASP A O 1 ATOM 2829 C CB . ASP A 1 368 ? -2.801 30.306 7.723 1.00 134.56 ? 368 ASP A CB 1 ATOM 2830 C CG . ASP A 1 368 ? -1.570 29.419 7.693 1.00 157.71 ? 368 ASP A CG 1 ATOM 2831 O OD1 . ASP A 1 368 ? -1.363 28.655 8.659 1.00 154.86 ? 368 ASP A OD1 1 ATOM 2832 O OD2 . ASP A 1 368 ? -0.811 29.488 6.704 1.00 174.28 ? 368 ASP A OD2 1 ATOM 2833 N N . LYS A 1 369 ? -2.719 32.406 10.781 1.00 81.22 ? 369 LYS A N 1 ATOM 2834 C CA . LYS A 1 369 ? -1.904 33.375 11.509 1.00 99.08 ? 369 LYS A CA 1 ATOM 2835 C C . LYS A 1 369 ? -1.411 34.519 10.619 1.00 100.25 ? 369 LYS A C 1 ATOM 2836 O O . LYS A 1 369 ? -0.277 34.979 10.756 1.00 118.07 ? 369 LYS A O 1 ATOM 2837 C CB . LYS A 1 369 ? -0.715 32.667 12.170 1.00 127.25 ? 369 LYS A CB 1 ATOM 2838 C CG . LYS A 1 369 ? -0.148 33.374 13.392 1.00 137.15 ? 369 LYS A CG 1 ATOM 2839 C CD . LYS A 1 369 ? 0.850 32.494 14.124 1.00 141.44 ? 369 LYS A CD 1 ATOM 2840 C CE . LYS A 1 369 ? 1.357 33.170 15.386 1.00 124.41 ? 369 LYS A CE 1 ATOM 2841 N NZ . LYS A 1 369 ? 2.236 32.272 16.181 1.00 111.57 ? 369 LYS A NZ 1 ATOM 2842 N N . LYS A 1 370 ? -2.262 34.974 9.704 1.00 85.35 ? 370 LYS A N 1 ATOM 2843 C CA . LYS A 1 370 ? -1.895 36.076 8.816 1.00 80.08 ? 370 LYS A CA 1 ATOM 2844 C C . LYS A 1 370 ? -2.245 37.444 9.395 1.00 89.73 ? 370 LYS A C 1 ATOM 2845 O O . LYS A 1 370 ? -1.799 38.472 8.885 1.00 91.60 ? 370 LYS A O 1 ATOM 2846 C CB . LYS A 1 370 ? -2.566 35.913 7.451 1.00 82.57 ? 370 LYS A CB 1 ATOM 2847 C CG . LYS A 1 370 ? -1.969 34.817 6.587 1.00 86.49 ? 370 LYS A CG 1 ATOM 2848 C CD . LYS A 1 370 ? -2.360 34.998 5.128 1.00 91.20 ? 370 LYS A CD 1 ATOM 2849 C CE . LYS A 1 370 ? -3.868 34.982 4.943 1.00 133.75 ? 370 LYS A CE 1 ATOM 2850 N NZ . LYS A 1 370 ? -4.248 35.140 3.511 1.00 149.53 ? 370 LYS A NZ 1 ATOM 2851 N N . GLY A 1 371 ? -3.038 37.455 10.462 1.00 87.54 ? 371 GLY A N 1 ATOM 2852 C CA . GLY A 1 371 ? -3.423 38.697 11.111 1.00 70.66 ? 371 GLY A CA 1 ATOM 2853 C C . GLY A 1 371 ? -4.816 39.179 10.760 1.00 82.33 ? 371 GLY A C 1 ATOM 2854 O O . GLY A 1 371 ? -5.311 38.941 9.658 1.00 105.76 ? 371 GLY A O 1 ATOM 2855 N N . ILE A 1 372 ? -5.448 39.864 11.708 1.00 68.98 ? 372 ILE A N 1 ATOM 2856 C CA . ILE A 1 372 ? -6.800 40.365 11.515 1.00 75.19 ? 372 ILE A CA 1 ATOM 2857 C C . ILE A 1 372 ? -7.032 41.637 12.331 1.00 79.09 ? 372 ILE A C 1 ATOM 2858 O O . ILE A 1 372 ? -6.463 41.809 13.411 1.00 76.61 ? 372 ILE A O 1 ATOM 2859 C CB . ILE A 1 372 ? -7.847 39.289 11.891 1.00 89.55 ? 372 ILE A CB 1 ATOM 2860 C CG1 . ILE A 1 372 ? -9.245 39.688 11.408 1.00 78.24 ? 372 ILE A CG1 1 ATOM 2861 C CG2 . ILE A 1 372 ? -7.829 39.009 13.389 1.00 113.10 ? 372 ILE A CG2 1 ATOM 2862 C CD1 . ILE A 1 372 ? -10.306 38.667 11.739 1.00 101.73 ? 372 ILE A CD1 1 ATOM 2863 N N . VAL A 1 373 ? -7.855 42.535 11.796 1.00 80.86 ? 373 VAL A N 1 ATOM 2864 C CA . VAL A 1 373 ? -8.176 43.791 12.465 1.00 71.87 ? 373 VAL A CA 1 ATOM 2865 C C . VAL A 1 373 ? -9.688 43.998 12.517 1.00 79.20 ? 373 VAL A C 1 ATOM 2866 O O . VAL A 1 373 ? -10.369 43.919 11.494 1.00 73.32 ? 373 VAL A O 1 ATOM 2867 C CB . VAL A 1 373 ? -7.520 44.992 11.758 1.00 81.58 ? 373 VAL A CB 1 ATOM 2868 C CG1 . VAL A 1 373 ? -7.954 46.295 12.409 1.00 82.91 ? 373 VAL A CG1 1 ATOM 2869 C CG2 . VAL A 1 373 ? -6.005 44.859 11.777 1.00 85.04 ? 373 VAL A CG2 1 ATOM 2870 N N . TYR A 1 374 ? -10.205 44.260 13.715 1.00 81.31 ? 374 TYR A N 1 ATOM 2871 C CA . TYR A 1 374 ? -11.639 44.436 13.916 1.00 67.57 ? 374 TYR A CA 1 ATOM 2872 C C . TYR A 1 374 ? -12.010 45.910 14.033 1.00 69.60 ? 374 TYR A C 1 ATOM 2873 O O . TYR A 1 374 ? -11.322 46.679 14.701 1.00 80.09 ? 374 TYR A O 1 ATOM 2874 C CB . TYR A 1 374 ? -12.099 43.683 15.166 1.00 65.44 ? 374 TYR A CB 1 ATOM 2875 C CG . TYR A 1 374 ? -11.854 42.192 15.115 1.00 76.06 ? 374 TYR A CG 1 ATOM 2876 C CD1 . TYR A 1 374 ? -12.809 41.331 14.591 1.00 80.67 ? 374 TYR A CD1 1 ATOM 2877 C CD2 . TYR A 1 374 ? -10.670 41.646 15.590 1.00 68.66 ? 374 TYR A CD2 1 ATOM 2878 C CE1 . TYR A 1 374 ? -12.591 39.967 14.541 1.00 74.96 ? 374 TYR A CE1 1 ATOM 2879 C CE2 . TYR A 1 374 ? -10.442 40.283 15.544 1.00 75.74 ? 374 TYR A CE2 1 ATOM 2880 C CZ . TYR A 1 374 ? -11.405 39.449 15.019 1.00 78.92 ? 374 TYR A CZ 1 ATOM 2881 O OH . TYR A 1 374 ? -11.183 38.091 14.972 1.00 95.31 ? 374 TYR A OH 1 ATOM 2882 N N . ILE A 1 375 ? -13.104 46.294 13.382 1.00 77.00 ? 375 ILE A N 1 ATOM 2883 C CA . ILE A 1 375 ? -13.595 47.667 13.439 1.00 74.90 ? 375 ILE A CA 1 ATOM 2884 C C . ILE A 1 375 ? -14.865 47.739 14.282 1.00 78.03 ? 375 ILE A C 1 ATOM 2885 O O . ILE A 1 375 ? -15.829 47.017 14.029 1.00 81.60 ? 375 ILE A O 1 ATOM 2886 C CB . ILE A 1 375 ? -13.878 48.237 12.027 1.00 71.36 ? 375 ILE A CB 1 ATOM 2887 C CG1 . ILE A 1 375 ? -12.587 48.728 11.370 1.00 71.07 ? 375 ILE A CG1 1 ATOM 2888 C CG2 . ILE A 1 375 ? -14.871 49.387 12.098 1.00 73.17 ? 375 ILE A CG2 1 ATOM 2889 C CD1 . ILE A 1 375 ? -11.685 47.628 10.868 1.00 97.52 ? 375 ILE A CD1 1 ATOM 2890 N N . PHE A 1 376 ? -14.858 48.604 15.291 1.00 69.76 ? 376 PHE A N 1 ATOM 2891 C CA . PHE A 1 376 ? -16.012 48.755 16.170 1.00 79.00 ? 376 PHE A CA 1 ATOM 2892 C C . PHE A 1 376 ? -16.592 50.163 16.090 1.00 81.56 ? 376 PHE A C 1 ATOM 2893 O O . PHE A 1 376 ? -15.921 51.138 16.426 1.00 73.90 ? 376 PHE A O 1 ATOM 2894 C CB . PHE A 1 376 ? -15.630 48.429 17.616 1.00 74.65 ? 376 PHE A CB 1 ATOM 2895 C CG . PHE A 1 376 ? -15.166 47.016 17.820 1.00 89.53 ? 376 PHE A CG 1 ATOM 2896 C CD1 . PHE A 1 376 ? -13.821 46.695 17.733 1.00 83.78 ? 376 PHE A CD1 1 ATOM 2897 C CD2 . PHE A 1 376 ? -16.073 46.008 18.105 1.00 91.04 ? 376 PHE A CD2 1 ATOM 2898 C CE1 . PHE A 1 376 ? -13.391 45.396 17.924 1.00 75.82 ? 376 PHE A CE1 1 ATOM 2899 C CE2 . PHE A 1 376 ? -15.648 44.707 18.296 1.00 66.54 ? 376 PHE A CE2 1 ATOM 2900 C CZ . PHE A 1 376 ? -14.305 44.401 18.203 1.00 78.35 ? 376 PHE A CZ 1 ATOM 2901 N N . ASN A 1 377 ? -17.840 50.265 15.642 1.00 85.43 ? 377 ASN A N 1 ATOM 2902 C CA . ASN A 1 377 ? -18.521 51.552 15.574 1.00 79.95 ? 377 ASN A CA 1 ATOM 2903 C C . ASN A 1 377 ? -19.010 52.005 16.945 1.00 82.65 ? 377 ASN A C 1 ATOM 2904 O O . ASN A 1 377 ? -19.409 51.187 17.772 1.00 81.59 ? 377 ASN A O 1 ATOM 2905 C CB . ASN A 1 377 ? -19.698 51.490 14.597 1.00 83.13 ? 377 ASN A CB 1 ATOM 2906 C CG . ASN A 1 377 ? -19.253 51.319 13.159 1.00 86.79 ? 377 ASN A CG 1 ATOM 2907 O OD1 . ASN A 1 377 ? -19.733 50.435 12.450 1.00 117.96 ? 377 ASN A OD1 1 ATOM 2908 N ND2 . ASN A 1 377 ? -18.334 52.169 12.718 1.00 82.19 ? 377 ASN A ND2 1 ATOM 2909 N N . GLY A 1 378 ? -18.971 53.310 17.185 1.00 86.45 ? 378 GLY A N 1 ATOM 2910 C CA . GLY A 1 378 ? -19.448 53.859 18.440 1.00 88.39 ? 378 GLY A CA 1 ATOM 2911 C C . GLY A 1 378 ? -20.913 54.241 18.375 1.00 95.31 ? 378 GLY A C 1 ATOM 2912 O O . GLY A 1 378 ? -21.437 54.549 17.304 1.00 94.55 ? 378 GLY A O 1 ATOM 2913 N N . ARG A 1 379 ? -21.576 54.221 19.526 1.00 98.70 ? 379 ARG A N 1 ATOM 2914 C CA . ARG A 1 379 ? -22.976 54.618 19.615 1.00 105.51 ? 379 ARG A CA 1 ATOM 2915 C C . ARG A 1 379 ? -23.188 55.573 20.785 1.00 118.93 ? 379 ARG A C 1 ATOM 2916 O O . ARG A 1 379 ? -22.251 55.888 21.516 1.00 121.11 ? 379 ARG A O 1 ATOM 2917 C CB . ARG A 1 379 ? -23.878 53.390 19.766 1.00 102.97 ? 379 ARG A CB 1 ATOM 2918 C CG . ARG A 1 379 ? -23.892 52.467 18.557 1.00 105.22 ? 379 ARG A CG 1 ATOM 2919 C CD . ARG A 1 379 ? -24.729 51.226 18.824 1.00 114.16 ? 379 ARG A CD 1 ATOM 2920 N NE . ARG A 1 379 ? -24.217 50.458 19.956 1.00 119.22 ? 379 ARG A NE 1 ATOM 2921 C CZ . ARG A 1 379 ? -24.745 49.317 20.386 1.00 122.05 ? 379 ARG A CZ 1 ATOM 2922 N NH1 . ARG A 1 379 ? -25.807 48.803 19.778 1.00 129.75 ? 379 ARG A NH1 1 ATOM 2923 N NH2 . ARG A 1 379 ? -24.212 48.688 21.424 1.00 111.17 ? 379 ARG A NH2 1 ATOM 2924 N N . SER A 1 380 ? -24.425 56.027 20.960 1.00 118.42 ? 380 SER A N 1 ATOM 2925 C CA . SER A 1 380 ? -24.757 56.946 22.043 1.00 111.37 ? 380 SER A CA 1 ATOM 2926 C C . SER A 1 380 ? -24.698 56.243 23.395 1.00 112.56 ? 380 SER A C 1 ATOM 2927 O O . SER A 1 380 ? -24.513 56.880 24.432 1.00 115.19 ? 380 SER A O 1 ATOM 2928 C CB . SER A 1 380 ? -26.145 57.552 21.822 1.00 112.48 ? 380 SER A CB 1 ATOM 2929 O OG . SER A 1 380 ? -27.129 56.539 21.716 1.00 113.62 ? 380 SER A OG 1 ATOM 2930 N N . THR A 1 381 ? -24.851 54.924 23.370 1.00 111.47 ? 381 THR A N 1 ATOM 2931 C CA . THR A 1 381 ? -24.822 54.112 24.580 1.00 115.42 ? 381 THR A CA 1 ATOM 2932 C C . THR A 1 381 ? -23.406 53.639 24.886 1.00 110.16 ? 381 THR A C 1 ATOM 2933 O O . THR A 1 381 ? -23.189 52.850 25.806 1.00 109.02 ? 381 THR A O 1 ATOM 2934 C CB . THR A 1 381 ? -25.743 52.885 24.459 1.00 120.69 ? 381 THR A CB 1 ATOM 2935 O OG1 . THR A 1 381 ? -25.223 51.989 23.468 1.00 127.18 ? 381 THR A OG1 1 ATOM 2936 C CG2 . THR A 1 381 ? -27.149 53.311 24.066 1.00 120.27 ? 381 THR A CG2 1 ATOM 2937 N N . GLY A 1 382 ? -22.445 54.125 24.108 1.00 108.08 ? 382 GLY A N 1 ATOM 2938 C CA . GLY A 1 382 ? -21.079 53.646 24.196 1.00 102.20 ? 382 GLY A CA 1 ATOM 2939 C C . GLY A 1 382 ? -20.741 52.746 23.024 1.00 96.27 ? 382 GLY A C 1 ATOM 2940 O O . GLY A 1 382 ? -21.487 52.686 22.047 1.00 101.61 ? 382 GLY A O 1 ATOM 2941 N N . LEU A 1 383 ? -19.610 52.055 23.116 1.00 91.36 ? 383 LEU A N 1 ATOM 2942 C CA . LEU A 1 383 ? -19.128 51.214 22.025 1.00 92.19 ? 383 LEU A CA 1 ATOM 2943 C C . LEU A 1 383 ? -20.077 50.064 21.692 1.00 92.64 ? 383 LEU A C 1 ATOM 2944 O O . LEU A 1 383 ? -20.591 49.393 22.585 1.00 104.31 ? 383 LEU A O 1 ATOM 2945 C CB . LEU A 1 383 ? -17.749 50.646 22.363 1.00 82.62 ? 383 LEU A CB 1 ATOM 2946 C CG . LEU A 1 383 ? -17.095 49.833 21.245 1.00 78.06 ? 383 LEU A CG 1 ATOM 2947 C CD1 . LEU A 1 383 ? -16.718 50.747 20.089 1.00 83.20 ? 383 LEU A CD1 1 ATOM 2948 C CD2 . LEU A 1 383 ? -15.886 49.065 21.754 1.00 72.73 ? 383 LEU A CD2 1 ATOM 2949 N N . ASN A 1 384 ? -20.300 49.844 20.399 1.00 85.04 ? 384 ASN A N 1 ATOM 2950 C CA . ASN A 1 384 ? -21.032 48.672 19.936 1.00 84.93 ? 384 ASN A CA 1 ATOM 2951 C C . ASN A 1 384 ? -20.125 47.452 20.041 1.00 86.04 ? 384 ASN A C 1 ATOM 2952 O O . ASN A 1 384 ? -19.044 47.422 19.453 1.00 81.03 ? 384 ASN A O 1 ATOM 2953 C CB . ASN A 1 384 ? -21.521 48.869 18.499 1.00 84.63 ? 384 ASN A CB 1 ATOM 2954 C CG . ASN A 1 384 ? -22.543 47.827 18.073 1.00 87.76 ? 384 ASN A CG 1 ATOM 2955 O OD1 . ASN A 1 384 ? -22.484 46.669 18.488 1.00 91.69 ? 384 ASN A OD1 1 ATOM 2956 N ND2 . ASN A 1 384 ? -23.487 48.238 17.234 1.00 102.68 ? 384 ASN A ND2 1 ATOM 2957 N N . ALA A 1 385 ? -20.571 46.446 20.786 1.00 81.17 ? 385 ALA A N 1 ATOM 2958 C CA . ALA A 1 385 ? -19.730 45.295 21.108 1.00 75.64 ? 385 ALA A CA 1 ATOM 2959 C C . ALA A 1 385 ? -19.548 44.344 19.928 1.00 75.45 ? 385 ALA A C 1 ATOM 2960 O O . ALA A 1 385 ? -18.713 43.441 19.977 1.00 78.70 ? 385 ALA A O 1 ATOM 2961 C CB . ALA A 1 385 ? -20.308 44.546 22.297 1.00 94.65 ? 385 ALA A CB 1 ATOM 2962 N N . VAL A 1 386 ? -20.331 44.544 18.874 1.00 83.30 ? 386 VAL A N 1 ATOM 2963 C CA . VAL A 1 386 ? -20.237 43.698 17.691 1.00 75.22 ? 386 VAL A CA 1 ATOM 2964 C C . VAL A 1 386 ? -19.522 44.427 16.559 1.00 86.83 ? 386 VAL A C 1 ATOM 2965 O O . VAL A 1 386 ? -19.987 45.471 16.100 1.00 120.95 ? 386 VAL A O 1 ATOM 2966 C CB . VAL A 1 386 ? -21.627 43.249 17.209 1.00 77.85 ? 386 VAL A CB 1 ATOM 2967 C CG1 . VAL A 1 386 ? -21.497 42.313 16.020 1.00 78.01 ? 386 VAL A CG1 1 ATOM 2968 C CG2 . VAL A 1 386 ? -22.385 42.578 18.342 1.00 76.95 ? 386 VAL A CG2 1 ATOM 2969 N N . PRO A 1 387 ? -18.379 43.882 16.112 1.00 73.49 ? 387 PRO A N 1 ATOM 2970 C CA . PRO A 1 387 ? -17.588 44.499 15.041 1.00 93.97 ? 387 PRO A CA 1 ATOM 2971 C C . PRO A 1 387 ? -18.351 44.559 13.721 1.00 88.93 ? 387 PRO A C 1 ATOM 2972 O O . PRO A 1 387 ? -18.902 43.548 13.285 1.00 86.68 ? 387 PRO A O 1 ATOM 2973 C CB . PRO A 1 387 ? -16.369 43.577 14.929 1.00 70.86 ? 387 PRO A CB 1 ATOM 2974 C CG . PRO A 1 387 ? -16.842 42.266 15.450 1.00 80.16 ? 387 PRO A CG 1 ATOM 2975 C CD . PRO A 1 387 ? -17.804 42.600 16.553 1.00 78.56 ? 387 PRO A CD 1 ATOM 2976 N N . SER A 1 388 ? -18.382 45.733 13.098 1.00 75.51 ? 388 SER A N 1 ATOM 2977 C CA . SER A 1 388 ? -19.127 45.919 11.859 1.00 88.53 ? 388 SER A CA 1 ATOM 2978 C C . SER A 1 388 ? -18.312 45.544 10.629 1.00 87.21 ? 388 SER A C 1 ATOM 2979 O O . SER A 1 388 ? -18.864 45.347 9.546 1.00 82.33 ? 388 SER A O 1 ATOM 2980 C CB . SER A 1 388 ? -19.598 47.367 11.737 1.00 92.16 ? 388 SER A CB 1 ATOM 2981 O OG . SER A 1 388 ? -18.496 48.254 11.660 1.00 86.15 ? 388 SER A OG 1 ATOM 2982 N N . GLN A 1 389 ? -16.998 45.444 10.796 1.00 84.67 ? 389 GLN A N 1 ATOM 2983 C CA . GLN A 1 389 ? -16.125 45.097 9.684 1.00 98.58 ? 389 GLN A CA 1 ATOM 2984 C C . GLN A 1 389 ? -14.896 44.330 10.152 1.00 86.92 ? 389 GLN A C 1 ATOM 2985 O O . GLN A 1 389 ? -14.352 44.598 11.223 1.00 73.66 ? 389 GLN A O 1 ATOM 2986 C CB . GLN A 1 389 ? -15.701 46.354 8.921 1.00 79.07 ? 389 GLN A CB 1 ATOM 2987 C CG . GLN A 1 389 ? -15.002 46.073 7.600 1.00 81.07 ? 389 GLN A CG 1 ATOM 2988 C CD . GLN A 1 389 ? -14.716 47.334 6.808 1.00 87.42 ? 389 GLN A CD 1 ATOM 2989 O OE1 . GLN A 1 389 ? -14.842 48.444 7.321 1.00 129.33 ? 389 GLN A OE1 1 ATOM 2990 N NE2 . GLN A 1 389 ? -14.331 47.167 5.548 1.00 84.78 ? 389 GLN A NE2 1 ATOM 2991 N N . ILE A 1 390 ? -14.468 43.371 9.338 1.00 87.62 ? 390 ILE A N 1 ATOM 2992 C CA . ILE A 1 390 ? -13.269 42.596 9.624 1.00 95.01 ? 390 ILE A CA 1 ATOM 2993 C C . ILE A 1 390 ? -12.224 42.839 8.539 1.00 106.20 ? 390 ILE A C 1 ATOM 2994 O O . ILE A 1 390 ? -12.520 42.751 7.346 1.00 127.01 ? 390 ILE A O 1 ATOM 2995 C CB . ILE A 1 390 ? -13.581 41.081 9.735 1.00 77.84 ? 390 ILE A CB 1 ATOM 2996 C CG1 . ILE A 1 390 ? -13.852 40.692 11.190 1.00 92.78 ? 390 ILE A CG1 1 ATOM 2997 C CG2 . ILE A 1 390 ? -12.430 40.240 9.200 1.00 78.56 ? 390 ILE A CG2 1 ATOM 2998 C CD1 . ILE A 1 390 ? -15.120 41.277 11.769 1.00 109.40 ? 390 ILE A CD1 1 ATOM 2999 N N . LEU A 1 391 ? -11.007 43.168 8.958 1.00 91.60 ? 391 LEU A N 1 ATOM 3000 C CA . LEU A 1 391 ? -9.902 43.334 8.024 1.00 89.11 ? 391 LEU A CA 1 ATOM 3001 C C . LEU A 1 391 ? -8.888 42.213 8.194 1.00 76.10 ? 391 LEU A C 1 ATOM 3002 O O . LEU A 1 391 ? -8.202 42.137 9.212 1.00 73.48 ? 391 LEU A O 1 ATOM 3003 C CB . LEU A 1 391 ? -9.215 44.688 8.220 1.00 91.15 ? 391 LEU A CB 1 ATOM 3004 C CG . LEU A 1 391 ? -10.070 45.948 8.081 1.00 81.82 ? 391 LEU A CG 1 ATOM 3005 C CD1 . LEU A 1 391 ? -9.197 47.187 8.171 1.00 83.12 ? 391 LEU A CD1 1 ATOM 3006 C CD2 . LEU A 1 391 ? -10.851 45.936 6.781 1.00 83.68 ? 391 LEU A CD2 1 ATOM 3007 N N . GLU A 1 392 ? -8.798 41.340 7.197 1.00 79.06 ? 392 GLU A N 1 ATOM 3008 C CA . GLU A 1 392 ? -7.798 40.283 7.215 1.00 81.21 ? 392 GLU A CA 1 ATOM 3009 C C . GLU A 1 392 ? -6.768 40.509 6.115 1.00 90.88 ? 392 GLU A C 1 ATOM 3010 O O . GLU A 1 392 ? -7.057 40.345 4.930 1.00 113.67 ? 392 GLU A O 1 ATOM 3011 C CB . GLU A 1 392 ? -8.460 38.910 7.064 1.00 91.87 ? 392 GLU A CB 1 ATOM 3012 C CG . GLU A 1 392 ? -9.565 38.857 6.018 1.00 110.28 ? 392 GLU A CG 1 ATOM 3013 C CD . GLU A 1 392 ? -10.193 37.481 5.900 1.00 134.86 ? 392 GLU A CD 1 ATOM 3014 O OE1 . GLU A 1 392 ? -9.806 36.579 6.672 1.00 134.35 ? 392 GLU A OE1 1 ATOM 3015 O OE2 . GLU A 1 392 ? -11.075 37.302 5.034 1.00 137.90 ? 392 GLU A OE2 1 ATOM 3016 N N . GLY A 1 393 ? -5.562 40.895 6.518 1.00 79.34 ? 393 GLY A N 1 ATOM 3017 C CA . GLY A 1 393 ? -4.485 41.128 5.576 1.00 103.03 ? 393 GLY A CA 1 ATOM 3018 C C . GLY A 1 393 ? -3.933 39.823 5.047 1.00 99.13 ? 393 GLY A C 1 ATOM 3019 O O . GLY A 1 393 ? -3.709 38.884 5.811 1.00 112.61 ? 393 GLY A O 1 ATOM 3020 N N . GLN A 1 394 ? -3.710 39.758 3.739 1.00 93.93 ? 394 GLN A N 1 ATOM 3021 C CA . GLN A 1 394 ? -3.166 38.549 3.143 1.00 127.79 ? 394 GLN A CA 1 ATOM 3022 C C . GLN A 1 394 ? -1.687 38.718 2.823 1.00 120.76 ? 394 GLN A C 1 ATOM 3023 O O . GLN A 1 394 ? -1.324 39.399 1.864 1.00 107.69 ? 394 GLN A O 1 ATOM 3024 C CB . GLN A 1 394 ? -3.935 38.178 1.872 1.00 151.37 ? 394 GLN A CB 1 ATOM 3025 C CG . GLN A 1 394 ? -5.441 38.030 2.053 1.00 159.27 ? 394 GLN A CG 1 ATOM 3026 C CD . GLN A 1 394 ? -6.189 39.340 1.879 1.00 159.30 ? 394 GLN A CD 1 ATOM 3027 O OE1 . GLN A 1 394 ? -5.586 40.413 1.824 1.00 148.26 ? 394 GLN A OE1 1 ATOM 3028 N NE2 . GLN A 1 394 ? -7.512 39.256 1.786 1.00 150.48 ? 394 GLN A NE2 1 ATOM 3029 N N . TRP A 1 395 ? -0.844 38.078 3.625 1.00 135.70 ? 395 TRP A N 1 ATOM 3030 C CA . TRP A 1 395 ? 0.590 38.022 3.373 1.00 117.89 ? 395 TRP A CA 1 ATOM 3031 C C . TRP A 1 395 ? 1.148 36.727 3.951 1.00 129.82 ? 395 TRP A C 1 ATOM 3032 O O . TRP A 1 395 ? 0.722 36.280 5.016 1.00 130.37 ? 395 TRP A O 1 ATOM 3033 C CB . TRP A 1 395 ? 1.309 39.240 3.963 1.00 99.28 ? 395 TRP A CB 1 ATOM 3034 C CG . TRP A 1 395 ? 0.984 40.525 3.257 1.00 107.81 ? 395 TRP A CG 1 ATOM 3035 C CD1 . TRP A 1 395 ? 0.250 41.568 3.745 1.00 107.55 ? 395 TRP A CD1 1 ATOM 3036 C CD2 . TRP A 1 395 ? 1.361 40.890 1.923 1.00 95.53 ? 395 TRP A CD2 1 ATOM 3037 N NE1 . TRP A 1 395 ? 0.157 42.565 2.802 1.00 94.46 ? 395 TRP A NE1 1 ATOM 3038 C CE2 . TRP A 1 395 ? 0.830 42.172 1.674 1.00 93.11 ? 395 TRP A CE2 1 ATOM 3039 C CE3 . TRP A 1 395 ? 2.100 40.260 0.916 1.00 116.57 ? 395 TRP A CE3 1 ATOM 3040 C CZ2 . TRP A 1 395 ? 1.015 42.835 0.463 1.00 126.14 ? 395 TRP A CZ2 1 ATOM 3041 C CZ3 . TRP A 1 395 ? 2.282 40.920 -0.286 1.00 136.97 ? 395 TRP A CZ3 1 ATOM 3042 C CH2 . TRP A 1 395 ? 1.742 42.194 -0.503 1.00 144.18 ? 395 TRP A CH2 1 ATOM 3043 N N . ALA A 1 396 ? 2.104 36.129 3.248 1.00 137.80 ? 396 ALA A N 1 ATOM 3044 C CA . ALA A 1 396 ? 2.647 34.838 3.651 1.00 126.33 ? 396 ALA A CA 1 ATOM 3045 C C . ALA A 1 396 ? 3.770 34.993 4.669 1.00 120.10 ? 396 ALA A C 1 ATOM 3046 O O . ALA A 1 396 ? 4.652 35.836 4.513 1.00 121.10 ? 396 ALA A O 1 ATOM 3047 C CB . ALA A 1 396 ? 3.138 34.072 2.433 1.00 132.45 ? 396 ALA A CB 1 ATOM 3048 N N . ALA A 1 397 ? 3.730 34.169 5.711 1.00 115.71 ? 397 ALA A N 1 ATOM 3049 C CA . ALA A 1 397 ? 4.770 34.165 6.732 1.00 105.09 ? 397 ALA A CA 1 ATOM 3050 C C . ALA A 1 397 ? 6.021 33.459 6.228 1.00 131.27 ? 397 ALA A C 1 ATOM 3051 O O . ALA A 1 397 ? 5.958 32.307 5.795 1.00 153.29 ? 397 ALA A O 1 ATOM 3052 C CB . ALA A 1 397 ? 4.267 33.499 7.998 1.00 104.24 ? 397 ALA A CB 1 ATOM 3053 N N . ARG A 1 398 ? 7.155 34.147 6.283 1.00 125.52 ? 398 ARG A N 1 ATOM 3054 C CA . ARG A 1 398 ? 8.418 33.550 5.869 1.00 126.67 ? 398 ARG A CA 1 ATOM 3055 C C . ARG A 1 398 ? 9.376 33.377 7.047 1.00 116.80 ? 398 ARG A C 1 ATOM 3056 O O . ARG A 1 398 ? 9.569 32.266 7.538 1.00 132.35 ? 398 ARG A O 1 ATOM 3057 C CB . ARG A 1 398 ? 9.071 34.393 4.769 1.00 118.71 ? 398 ARG A CB 1 ATOM 3058 C CG . ARG A 1 398 ? 8.844 35.892 4.902 1.00 115.15 ? 398 ARG A CG 1 ATOM 3059 C CD . ARG A 1 398 ? 9.716 36.667 3.929 1.00 125.37 ? 398 ARG A CD 1 ATOM 3060 N NE . ARG A 1 398 ? 9.591 38.110 4.111 1.00 141.56 ? 398 ARG A NE 1 ATOM 3061 C CZ . ARG A 1 398 ? 10.276 38.813 5.007 1.00 137.04 ? 398 ARG A CZ 1 ATOM 3062 N NH1 . ARG A 1 398 ? 11.136 38.206 5.814 1.00 132.07 ? 398 ARG A NH1 1 ATOM 3063 N NH2 . ARG A 1 398 ? 10.098 40.124 5.099 1.00 129.04 ? 398 ARG A NH2 1 ATOM 3064 N N . SER A 1 399 ? 9.970 34.476 7.500 1.00 111.23 ? 399 SER A N 1 ATOM 3065 C CA . SER A 1 399 ? 10.909 34.435 8.615 1.00 125.60 ? 399 SER A CA 1 ATOM 3066 C C . SER A 1 399 ? 10.196 34.296 9.956 1.00 135.56 ? 399 SER A C 1 ATOM 3067 O O . SER A 1 399 ? 10.547 33.446 10.775 1.00 124.33 ? 399 SER A O 1 ATOM 3068 C CB . SER A 1 399 ? 11.782 35.690 8.622 1.00 117.53 ? 399 SER A CB 1 ATOM 3069 O OG . SER A 1 399 ? 12.635 35.707 9.753 1.00 118.18 ? 399 SER A OG 1 ATOM 3070 N N . MET A 1 400 ? 9.190 35.136 10.167 1.00 134.75 ? 400 MET A N 1 ATOM 3071 C CA . MET A 1 400 ? 8.469 35.177 11.431 1.00 108.42 ? 400 MET A CA 1 ATOM 3072 C C . MET A 1 400 ? 6.983 35.383 11.139 1.00 116.94 ? 400 MET A C 1 ATOM 3073 O O . MET A 1 400 ? 6.606 35.512 9.973 1.00 131.18 ? 400 MET A O 1 ATOM 3074 C CB . MET A 1 400 ? 9.030 36.294 12.319 1.00 78.34 ? 400 MET A CB 1 ATOM 3075 C CG . MET A 1 400 ? 8.724 37.697 11.829 1.00 74.17 ? 400 MET A CG 1 ATOM 3076 S SD . MET A 1 400 ? 9.183 38.952 13.041 1.00 83.15 ? 400 MET A SD 1 ATOM 3077 C CE . MET A 1 400 ? 8.215 38.436 14.458 1.00 103.05 ? 400 MET A CE 1 ATOM 3078 N N . PRO A 1 401 ? 6.128 35.395 12.181 1.00 107.78 ? 401 PRO A N 1 ATOM 3079 C CA . PRO A 1 401 ? 4.731 35.729 11.888 1.00 90.23 ? 401 PRO A CA 1 ATOM 3080 C C . PRO A 1 401 ? 4.597 37.109 11.260 1.00 77.15 ? 401 PRO A C 1 ATOM 3081 O O . PRO A 1 401 ? 5.171 38.070 11.770 1.00 82.38 ? 401 PRO A O 1 ATOM 3082 C CB . PRO A 1 401 ? 4.054 35.684 13.266 1.00 75.81 ? 401 PRO A CB 1 ATOM 3083 C CG . PRO A 1 401 ? 5.176 35.662 14.265 1.00 87.71 ? 401 PRO A CG 1 ATOM 3084 C CD . PRO A 1 401 ? 6.286 34.945 13.574 1.00 114.62 ? 401 PRO A CD 1 ATOM 3085 N N . PRO A 1 402 ? 3.841 37.204 10.159 1.00 79.98 ? 402 PRO A N 1 ATOM 3086 C CA . PRO A 1 402 ? 3.661 38.476 9.466 1.00 89.82 ? 402 PRO A CA 1 ATOM 3087 C C . PRO A 1 402 ? 2.650 39.313 10.218 1.00 97.86 ? 402 PRO A C 1 ATOM 3088 O O . PRO A 1 402 ? 1.529 39.469 9.735 1.00 124.92 ? 402 PRO A O 1 ATOM 3089 C CB . PRO A 1 402 ? 3.131 38.053 8.096 1.00 105.25 ? 402 PRO A CB 1 ATOM 3090 C CG . PRO A 1 402 ? 2.475 36.701 8.327 1.00 79.08 ? 402 PRO A CG 1 ATOM 3091 C CD . PRO A 1 402 ? 2.864 36.203 9.703 1.00 76.68 ? 402 PRO A CD 1 ATOM 3092 N N . SER A 1 403 ? 3.038 39.822 11.384 1.00 76.39 ? 403 SER A N 1 ATOM 3093 C CA . SER A 1 403 ? 2.071 40.404 12.300 1.00 68.51 ? 403 SER A CA 1 ATOM 3094 C C . SER A 1 403 ? 1.312 41.525 11.618 1.00 78.05 ? 403 SER A C 1 ATOM 3095 O O . SER A 1 403 ? 1.897 42.524 11.218 1.00 106.49 ? 403 SER A O 1 ATOM 3096 C CB . SER A 1 403 ? 2.765 40.922 13.559 1.00 71.62 ? 403 SER A CB 1 ATOM 3097 O OG . SER A 1 403 ? 3.717 39.989 14.045 1.00 66.86 ? 403 SER A OG 1 ATOM 3098 N N . PHE A 1 404 ? -0.002 41.368 11.535 1.00 94.03 ? 404 PHE A N 1 ATOM 3099 C CA . PHE A 1 404 ? -0.839 42.314 10.815 1.00 66.84 ? 404 PHE A CA 1 ATOM 3100 C C . PHE A 1 404 ? -1.708 43.018 11.831 1.00 75.73 ? 404 PHE A C 1 ATOM 3101 O O . PHE A 1 404 ? -2.486 42.386 12.542 1.00 109.85 ? 404 PHE A O 1 ATOM 3102 C CB . PHE A 1 404 ? -1.679 41.606 9.752 1.00 79.96 ? 404 PHE A CB 1 ATOM 3103 C CG . PHE A 1 404 ? -2.574 42.525 8.974 1.00 79.58 ? 404 PHE A CG 1 ATOM 3104 C CD1 . PHE A 1 404 ? -2.089 43.227 7.884 1.00 80.79 ? 404 PHE A CD1 1 ATOM 3105 C CD2 . PHE A 1 404 ? -3.903 42.679 9.328 1.00 81.49 ? 404 PHE A CD2 1 ATOM 3106 C CE1 . PHE A 1 404 ? -2.912 44.070 7.165 1.00 74.16 ? 404 PHE A CE1 1 ATOM 3107 C CE2 . PHE A 1 404 ? -4.730 43.521 8.613 1.00 75.54 ? 404 PHE A CE2 1 ATOM 3108 C CZ . PHE A 1 404 ? -4.235 44.217 7.531 1.00 79.16 ? 404 PHE A CZ 1 ATOM 3109 N N . GLY A 1 405 ? -1.589 44.336 11.881 1.00 73.48 ? 405 GLY A N 1 ATOM 3110 C CA . GLY A 1 405 ? -1.966 45.064 13.072 1.00 61.20 ? 405 GLY A CA 1 ATOM 3111 C C . GLY A 1 405 ? -0.683 45.201 13.866 1.00 98.17 ? 405 GLY A C 1 ATOM 3112 O O . GLY A 1 405 ? 0.397 45.214 13.273 1.00 142.18 ? 405 GLY A O 1 ATOM 3113 N N . TYR A 1 406 ? -0.807 45.344 15.185 1.00 85.53 ? 406 TYR A N 1 ATOM 3114 C CA . TYR A 1 406 ? 0.321 45.515 16.112 1.00 77.64 ? 406 TYR A CA 1 ATOM 3115 C C . TYR A 1 406 ? 0.889 46.928 15.970 1.00 56.74 ? 406 TYR A C 1 ATOM 3116 O O . TYR A 1 406 ? 1.595 47.420 16.848 1.00 87.36 ? 406 TYR A O 1 ATOM 3117 C CB . TYR A 1 406 ? 1.412 44.453 15.874 1.00 56.13 ? 406 TYR A CB 1 ATOM 3118 C CG . TYR A 1 406 ? 2.482 44.367 16.945 1.00 74.02 ? 406 TYR A CG 1 ATOM 3119 C CD1 . TYR A 1 406 ? 2.338 43.513 18.030 1.00 73.49 ? 406 TYR A CD1 1 ATOM 3120 C CD2 . TYR A 1 406 ? 3.647 45.122 16.859 1.00 82.75 ? 406 TYR A CD2 1 ATOM 3121 C CE1 . TYR A 1 406 ? 3.315 43.423 19.008 1.00 93.18 ? 406 TYR A CE1 1 ATOM 3122 C CE2 . TYR A 1 406 ? 4.630 45.040 17.834 1.00 80.76 ? 406 TYR A CE2 1 ATOM 3123 C CZ . TYR A 1 406 ? 4.458 44.188 18.905 1.00 91.94 ? 406 TYR A CZ 1 ATOM 3124 O OH . TYR A 1 406 ? 5.433 44.102 19.876 1.00 82.85 ? 406 TYR A OH 1 ATOM 3125 N N . SER A 1 407 ? 0.563 47.570 14.852 1.00 56.56 ? 407 SER A N 1 ATOM 3126 C CA . SER A 1 407 ? 0.750 49.000 14.659 1.00 93.40 ? 407 SER A CA 1 ATOM 3127 C C . SER A 1 407 ? -0.395 49.526 13.799 1.00 73.94 ? 407 SER A C 1 ATOM 3128 O O . SER A 1 407 ? -0.648 48.995 12.719 1.00 60.26 ? 407 SER A O 1 ATOM 3129 C CB . SER A 1 407 ? 2.096 49.291 13.999 1.00 91.79 ? 407 SER A CB 1 ATOM 3130 O OG . SER A 1 407 ? 2.190 48.638 12.744 1.00 103.83 ? 407 SER A OG 1 ATOM 3131 N N . MET A 1 408 ? -1.065 50.579 14.256 1.00 83.32 ? 408 MET A N 1 ATOM 3132 C CA . MET A 1 408 ? -2.178 51.163 13.507 1.00 75.71 ? 408 MET A CA 1 ATOM 3133 C C . MET A 1 408 ? -2.313 52.658 13.774 1.00 78.05 ? 408 MET A C 1 ATOM 3134 O O . MET A 1 408 ? -2.022 53.125 14.874 1.00 93.32 ? 408 MET A O 1 ATOM 3135 C CB . MET A 1 408 ? -3.499 50.469 13.859 1.00 63.92 ? 408 MET A CB 1 ATOM 3136 C CG . MET A 1 408 ? -3.701 49.079 13.278 1.00 62.44 ? 408 MET A CG 1 ATOM 3137 S SD . MET A 1 408 ? -5.302 48.393 13.741 1.00 74.29 ? 408 MET A SD 1 ATOM 3138 C CE . MET A 1 408 ? -5.280 48.649 15.514 1.00 57.96 ? 408 MET A CE 1 ATOM 3139 N N . LYS A 1 409 ? -2.741 53.409 12.762 1.00 65.00 ? 409 LYS A N 1 ATOM 3140 C CA . LYS A 1 409 ? -3.075 54.819 12.949 1.00 73.49 ? 409 LYS A CA 1 ATOM 3141 C C . LYS A 1 409 ? -4.324 55.210 12.157 1.00 67.02 ? 409 LYS A C 1 ATOM 3142 O O . LYS A 1 409 ? -4.365 55.050 10.937 1.00 66.84 ? 409 LYS A O 1 ATOM 3143 C CB . LYS A 1 409 ? -1.895 55.706 12.545 1.00 76.50 ? 409 LYS A CB 1 ATOM 3144 C CG . LYS A 1 409 ? -1.886 57.063 13.229 1.00 89.59 ? 409 LYS A CG 1 ATOM 3145 C CD . LYS A 1 409 ? -1.828 56.901 14.741 1.00 104.08 ? 409 LYS A CD 1 ATOM 3146 C CE . LYS A 1 409 ? -1.850 58.244 15.452 1.00 121.81 ? 409 LYS A CE 1 ATOM 3147 N NZ . LYS A 1 409 ? -1.783 58.084 16.933 1.00 128.04 ? 409 LYS A NZ 1 ATOM 3148 N N . GLY A 1 410 ? -5.342 55.707 12.853 1.00 72.84 ? 410 GLY A N 1 ATOM 3149 C CA . GLY A 1 410 ? -6.550 56.188 12.206 1.00 84.29 ? 410 GLY A CA 1 ATOM 3150 C C . GLY A 1 410 ? -6.735 57.693 12.283 1.00 83.69 ? 410 GLY A C 1 ATOM 3151 O O . GLY A 1 410 ? -5.772 58.443 12.442 1.00 81.55 ? 410 GLY A O 1 ATOM 3152 N N . ALA A 1 411 ? -7.989 58.122 12.156 1.00 89.67 ? 411 ALA A N 1 ATOM 3153 C CA . ALA A 1 411 ? -8.415 59.498 12.429 1.00 91.22 ? 411 ALA A CA 1 ATOM 3154 C C . ALA A 1 411 ? -7.766 60.576 11.556 1.00 86.32 ? 411 ALA A C 1 ATOM 3155 O O . ALA A 1 411 ? -7.577 61.707 12.005 1.00 100.23 ? 411 ALA A O 1 ATOM 3156 C CB . ALA A 1 411 ? -8.178 59.824 13.902 1.00 91.00 ? 411 ALA A CB 1 ATOM 3157 N N . THR A 1 412 ? -7.431 60.237 10.316 1.00 75.28 ? 412 THR A N 1 ATOM 3158 C CA . THR A 1 412 ? -6.929 61.234 9.373 1.00 77.98 ? 412 THR A CA 1 ATOM 3159 C C . THR A 1 412 ? -7.413 60.923 7.960 1.00 80.80 ? 412 THR A C 1 ATOM 3160 O O . THR A 1 412 ? -7.376 59.771 7.529 1.00 94.70 ? 412 THR A O 1 ATOM 3161 C CB . THR A 1 412 ? -5.387 61.305 9.393 1.00 89.60 ? 412 THR A CB 1 ATOM 3162 O OG1 . THR A 1 412 ? -4.938 61.619 10.718 1.00 108.19 ? 412 THR A OG1 1 ATOM 3163 C CG2 . THR A 1 412 ? -4.881 62.370 8.433 1.00 79.98 ? 412 THR A CG2 1 ATOM 3164 N N . ASP A 1 413 ? -7.864 61.946 7.241 1.00 84.15 ? 413 ASP A N 1 ATOM 3165 C CA . ASP A 1 413 ? -8.371 61.750 5.889 1.00 87.34 ? 413 ASP A CA 1 ATOM 3166 C C . ASP A 1 413 ? -7.315 62.160 4.868 1.00 102.96 ? 413 ASP A C 1 ATOM 3167 O O . ASP A 1 413 ? -7.062 63.347 4.665 1.00 128.16 ? 413 ASP A O 1 ATOM 3168 C CB . ASP A 1 413 ? -9.660 62.552 5.686 1.00 90.19 ? 413 ASP A CB 1 ATOM 3169 C CG . ASP A 1 413 ? -10.326 62.268 4.355 1.00 118.60 ? 413 ASP A CG 1 ATOM 3170 O OD1 . ASP A 1 413 ? -10.126 61.164 3.807 1.00 149.74 ? 413 ASP A OD1 1 ATOM 3171 O OD2 . ASP A 1 413 ? -11.061 63.149 3.862 1.00 96.94 ? 413 ASP A OD2 1 ATOM 3172 N N . ILE A 1 414 ? -6.707 61.166 4.226 1.00 95.67 ? 414 ILE A N 1 ATOM 3173 C CA . ILE A 1 414 ? -5.615 61.405 3.289 1.00 91.24 ? 414 ILE A CA 1 ATOM 3174 C C . ILE A 1 414 ? -6.112 61.601 1.856 1.00 95.76 ? 414 ILE A C 1 ATOM 3175 O O . ILE A 1 414 ? -5.381 62.091 0.995 1.00 98.45 ? 414 ILE A O 1 ATOM 3176 C CB . ILE A 1 414 ? -4.597 60.239 3.330 1.00 89.04 ? 414 ILE A CB 1 ATOM 3177 C CG1 . ILE A 1 414 ? -3.253 60.660 2.735 1.00 103.86 ? 414 ILE A CG1 1 ATOM 3178 C CG2 . ILE A 1 414 ? -5.157 59.004 2.633 1.00 89.87 ? 414 ILE A CG2 1 ATOM 3179 C CD1 . ILE A 1 414 ? -2.162 59.631 2.922 1.00 96.29 ? 414 ILE A CD1 1 ATOM 3180 N N . ASP A 1 415 ? -7.359 61.217 1.608 1.00 107.37 ? 415 ASP A N 1 ATOM 3181 C CA . ASP A 1 415 ? -7.957 61.343 0.284 1.00 101.28 ? 415 ASP A CA 1 ATOM 3182 C C . ASP A 1 415 ? -8.735 62.644 0.139 1.00 104.16 ? 415 ASP A C 1 ATOM 3183 O O . ASP A 1 415 ? -9.163 63.000 -0.961 1.00 109.61 ? 415 ASP A O 1 ATOM 3184 C CB . ASP A 1 415 ? -8.874 60.151 -0.001 1.00 101.33 ? 415 ASP A CB 1 ATOM 3185 C CG . ASP A 1 415 ? -9.349 59.472 1.267 1.00 138.49 ? 415 ASP A CG 1 ATOM 3186 O OD1 . ASP A 1 415 ? -8.879 59.869 2.352 1.00 160.22 ? 415 ASP A OD1 1 ATOM 3187 O OD2 . ASP A 1 415 ? -10.188 58.550 1.189 1.00 131.38 ? 415 ASP A OD2 1 ATOM 3188 N N . LYS A 1 416 ? -8.905 63.344 1.258 1.00 102.14 ? 416 LYS A N 1 ATOM 3189 C CA . LYS A 1 416 ? -9.765 64.523 1.332 1.00 104.66 ? 416 LYS A CA 1 ATOM 3190 C C . LYS A 1 416 ? -11.165 64.203 0.810 1.00 116.49 ? 416 LYS A C 1 ATOM 3191 O O . LYS A 1 416 ? -11.812 65.041 0.182 1.00 112.55 ? 416 LYS A O 1 ATOM 3192 C CB . LYS A 1 416 ? -9.156 65.694 0.557 1.00 108.41 ? 416 LYS A CB 1 ATOM 3193 C CG . LYS A 1 416 ? -7.838 66.188 1.131 1.00 106.56 ? 416 LYS A CG 1 ATOM 3194 C CD . LYS A 1 416 ? -7.357 67.443 0.421 1.00 137.05 ? 416 LYS A CD 1 ATOM 3195 C CE . LYS A 1 416 ? -6.095 67.991 1.067 1.00 138.98 ? 416 LYS A CE 1 ATOM 3196 N NZ . LYS A 1 416 ? -5.652 69.262 0.429 1.00 113.25 ? 416 LYS A NZ 1 ATOM 3197 N N . ASN A 1 417 ? -11.622 62.982 1.080 1.00 120.39 ? 417 ASN A N 1 ATOM 3198 C CA . ASN A 1 417 ? -12.912 62.512 0.587 1.00 106.72 ? 417 ASN A CA 1 ATOM 3199 C C . ASN A 1 417 ? -14.036 62.707 1.598 1.00 105.50 ? 417 ASN A C 1 ATOM 3200 O O . ASN A 1 417 ? -15.177 62.321 1.350 1.00 127.18 ? 417 ASN A O 1 ATOM 3201 C CB . ASN A 1 417 ? -12.827 61.037 0.189 1.00 120.76 ? 417 ASN A CB 1 ATOM 3202 C CG . ASN A 1 417 ? -12.737 60.108 1.389 1.00 118.39 ? 417 ASN A CG 1 ATOM 3203 O OD1 . ASN A 1 417 ? -11.984 60.357 2.333 1.00 116.62 ? 417 ASN A OD1 1 ATOM 3204 N ND2 . ASN A 1 417 ? -13.509 59.028 1.356 1.00 100.55 ? 417 ASN A ND2 1 ATOM 3205 N N . GLY A 1 418 ? -13.709 63.298 2.742 1.00 103.02 ? 418 GLY A N 1 ATOM 3206 C CA . GLY A 1 418 ? -14.703 63.564 3.764 1.00 102.14 ? 418 GLY A CA 1 ATOM 3207 C C . GLY A 1 418 ? -14.743 62.505 4.848 1.00 104.29 ? 418 GLY A C 1 ATOM 3208 O O . GLY A 1 418 ? -15.373 62.697 5.887 1.00 108.67 ? 418 GLY A O 1 ATOM 3209 N N . TYR A 1 419 ? -14.066 61.386 4.611 1.00 95.83 ? 419 TYR A N 1 ATOM 3210 C CA . TYR A 1 419 ? -14.025 60.309 5.592 1.00 91.98 ? 419 TYR A CA 1 ATOM 3211 C C . TYR A 1 419 ? -12.585 59.960 5.954 1.00 88.99 ? 419 TYR A C 1 ATOM 3212 O O . TYR A 1 419 ? -11.716 59.902 5.080 1.00 89.98 ? 419 TYR A O 1 ATOM 3213 C CB . TYR A 1 419 ? -14.751 59.069 5.058 1.00 108.22 ? 419 TYR A CB 1 ATOM 3214 C CG . TYR A 1 419 ? -16.230 59.269 4.789 1.00 101.00 ? 419 TYR A CG 1 ATOM 3215 C CD1 . TYR A 1 419 ? -16.668 59.904 3.634 1.00 104.03 ? 419 TYR A CD1 1 ATOM 3216 C CD2 . TYR A 1 419 ? -17.187 58.805 5.682 1.00 94.09 ? 419 TYR A CD2 1 ATOM 3217 C CE1 . TYR A 1 419 ? -18.015 60.084 3.383 1.00 116.93 ? 419 TYR A CE1 1 ATOM 3218 C CE2 . TYR A 1 419 ? -18.538 58.977 5.438 1.00 96.86 ? 419 TYR A CE2 1 ATOM 3219 C CZ . TYR A 1 419 ? -18.946 59.618 4.287 1.00 110.62 ? 419 TYR A CZ 1 ATOM 3220 O OH . TYR A 1 419 ? -20.289 59.795 4.038 1.00 103.93 ? 419 TYR A OH 1 ATOM 3221 N N . PRO A 1 420 ? -12.335 59.703 7.248 1.00 85.53 ? 420 PRO A N 1 ATOM 3222 C CA . PRO A 1 420 ? -11.004 59.349 7.749 1.00 82.58 ? 420 PRO A CA 1 ATOM 3223 C C . PRO A 1 420 ? -10.620 57.936 7.342 1.00 85.73 ? 420 PRO A C 1 ATOM 3224 O O . PRO A 1 420 ? -11.498 57.121 7.070 1.00 117.05 ? 420 PRO A O 1 ATOM 3225 C CB . PRO A 1 420 ? -11.158 59.465 9.265 1.00 79.86 ? 420 PRO A CB 1 ATOM 3226 C CG . PRO A 1 420 ? -12.586 59.168 9.504 1.00 80.67 ? 420 PRO A CG 1 ATOM 3227 C CD . PRO A 1 420 ? -13.329 59.753 8.333 1.00 87.52 ? 420 PRO A CD 1 ATOM 3228 N N . ASP A 1 421 ? -9.325 57.650 7.310 1.00 88.28 ? 421 ASP A N 1 ATOM 3229 C CA . ASP A 1 421 ? -8.843 56.377 6.797 1.00 83.24 ? 421 ASP A CA 1 ATOM 3230 C C . ASP A 1 421 ? -7.857 55.733 7.772 1.00 87.40 ? 421 ASP A C 1 ATOM 3231 O O . ASP A 1 421 ? -7.572 56.293 8.830 1.00 80.00 ? 421 ASP A O 1 ATOM 3232 C CB . ASP A 1 421 ? -8.216 56.589 5.421 1.00 82.43 ? 421 ASP A CB 1 ATOM 3233 C CG . ASP A 1 421 ? -9.016 57.563 4.569 1.00 104.97 ? 421 ASP A CG 1 ATOM 3234 O OD1 . ASP A 1 421 ? -9.744 57.120 3.656 1.00 113.34 ? 421 ASP A OD1 1 ATOM 3235 O OD2 . ASP A 1 421 ? -8.940 58.780 4.832 1.00 135.69 ? 421 ASP A OD2 1 ATOM 3236 N N . LEU A 1 422 ? -7.341 54.559 7.421 1.00 88.88 ? 422 LEU A N 1 ATOM 3237 C CA . LEU A 1 422 ? -6.583 53.760 8.381 1.00 80.53 ? 422 LEU A CA 1 ATOM 3238 C C . LEU A 1 422 ? -5.309 53.127 7.817 1.00 79.18 ? 422 LEU A C 1 ATOM 3239 O O . LEU A 1 422 ? -5.326 52.514 6.751 1.00 80.63 ? 422 LEU A O 1 ATOM 3240 C CB . LEU A 1 422 ? -7.487 52.661 8.949 1.00 75.07 ? 422 LEU A CB 1 ATOM 3241 C CG . LEU A 1 422 ? -6.830 51.608 9.843 1.00 72.20 ? 422 LEU A CG 1 ATOM 3242 C CD1 . LEU A 1 422 ? -6.312 52.233 11.127 1.00 74.62 ? 422 LEU A CD1 1 ATOM 3243 C CD2 . LEU A 1 422 ? -7.801 50.480 10.141 1.00 79.71 ? 422 LEU A CD2 1 ATOM 3244 N N . ILE A 1 423 ? -4.211 53.271 8.556 1.00 75.85 ? 423 ILE A N 1 ATOM 3245 C CA . ILE A 1 423 ? -2.955 52.611 8.214 1.00 78.26 ? 423 ILE A CA 1 ATOM 3246 C C . ILE A 1 423 ? -2.724 51.404 9.118 1.00 74.20 ? 423 ILE A C 1 ATOM 3247 O O . ILE A 1 423 ? -2.802 51.514 10.341 1.00 74.98 ? 423 ILE A O 1 ATOM 3248 C CB . ILE A 1 423 ? -1.748 53.563 8.343 1.00 76.36 ? 423 ILE A CB 1 ATOM 3249 C CG1 . ILE A 1 423 ? -1.984 54.847 7.549 1.00 79.82 ? 423 ILE A CG1 1 ATOM 3250 C CG2 . ILE A 1 423 ? -0.472 52.875 7.878 1.00 77.07 ? 423 ILE A CG2 1 ATOM 3251 C CD1 . ILE A 1 423 ? -0.876 55.866 7.699 1.00 97.91 ? 423 ILE A CD1 1 ATOM 3252 N N . VAL A 1 424 ? -2.445 50.253 8.516 1.00 74.10 ? 424 VAL A N 1 ATOM 3253 C CA . VAL A 1 424 ? -2.125 49.055 9.283 1.00 71.21 ? 424 VAL A CA 1 ATOM 3254 C C . VAL A 1 424 ? -0.804 48.459 8.814 1.00 71.93 ? 424 VAL A C 1 ATOM 3255 O O . VAL A 1 424 ? -0.704 47.950 7.697 1.00 95.96 ? 424 VAL A O 1 ATOM 3256 C CB . VAL A 1 424 ? -3.231 47.988 9.159 1.00 73.90 ? 424 VAL A CB 1 ATOM 3257 C CG1 . VAL A 1 424 ? -2.840 46.731 9.916 1.00 67.82 ? 424 VAL A CG1 1 ATOM 3258 C CG2 . VAL A 1 424 ? -4.559 48.533 9.663 1.00 86.20 ? 424 VAL A CG2 1 ATOM 3259 N N . GLY A 1 425 ? 0.211 48.524 9.668 1.00 69.65 ? 425 GLY A N 1 ATOM 3260 C CA . GLY A 1 425 ? 1.515 47.992 9.322 1.00 78.34 ? 425 GLY A CA 1 ATOM 3261 C C . GLY A 1 425 ? 1.654 46.512 9.612 1.00 75.22 ? 425 GLY A C 1 ATOM 3262 O O . GLY A 1 425 ? 1.127 46.015 10.607 1.00 65.28 ? 425 GLY A O 1 ATOM 3263 N N . ALA A 1 426 ? 2.365 45.806 8.738 1.00 81.36 ? 426 ALA A N 1 ATOM 3264 C CA . ALA A 1 426 ? 2.767 44.433 9.011 1.00 67.95 ? 426 ALA A CA 1 ATOM 3265 C C . ALA A 1 426 ? 4.282 44.323 8.928 1.00 70.49 ? 426 ALA A C 1 ATOM 3266 O O . ALA A 1 426 ? 4.855 44.398 7.841 1.00 96.45 ? 426 ALA A O 1 ATOM 3267 C CB . ALA A 1 426 ? 2.103 43.473 8.039 1.00 70.24 ? 426 ALA A CB 1 ATOM 3268 N N . PHE A 1 427 ? 4.931 44.128 10.073 1.00 74.46 ? 427 PHE A N 1 ATOM 3269 C CA . PHE A 1 427 ? 6.390 44.171 10.120 1.00 72.24 ? 427 PHE A CA 1 ATOM 3270 C C . PHE A 1 427 ? 7.022 42.794 9.945 1.00 82.11 ? 427 PHE A C 1 ATOM 3271 O O . PHE A 1 427 ? 8.240 42.679 9.814 1.00 98.31 ? 427 PHE A O 1 ATOM 3272 C CB . PHE A 1 427 ? 6.865 44.813 11.429 1.00 72.64 ? 427 PHE A CB 1 ATOM 3273 C CG . PHE A 1 427 ? 6.680 43.948 12.643 1.00 71.00 ? 427 PHE A CG 1 ATOM 3274 C CD1 . PHE A 1 427 ? 7.705 43.130 13.088 1.00 61.31 ? 427 PHE A CD1 1 ATOM 3275 C CD2 . PHE A 1 427 ? 5.491 43.970 13.352 1.00 81.51 ? 427 PHE A CD2 1 ATOM 3276 C CE1 . PHE A 1 427 ? 7.543 42.339 14.206 1.00 70.45 ? 427 PHE A CE1 1 ATOM 3277 C CE2 . PHE A 1 427 ? 5.325 43.183 14.475 1.00 91.52 ? 427 PHE A CE2 1 ATOM 3278 C CZ . PHE A 1 427 ? 6.353 42.365 14.902 1.00 90.07 ? 427 PHE A CZ 1 ATOM 3279 N N . GLY A 1 428 ? 6.195 41.754 9.949 1.00 82.04 ? 428 GLY A N 1 ATOM 3280 C CA . GLY A 1 428 ? 6.678 40.413 9.685 1.00 70.89 ? 428 GLY A CA 1 ATOM 3281 C C . GLY A 1 428 ? 7.052 40.280 8.223 1.00 92.27 ? 428 GLY A C 1 ATOM 3282 O O . GLY A 1 428 ? 8.101 39.733 7.883 1.00 105.79 ? 428 GLY A O 1 ATOM 3283 N N . VAL A 1 429 ? 6.184 40.789 7.355 1.00 96.89 ? 429 VAL A N 1 ATOM 3284 C CA . VAL A 1 429 ? 6.456 40.818 5.922 1.00 79.62 ? 429 VAL A CA 1 ATOM 3285 C C . VAL A 1 429 ? 7.076 42.147 5.508 1.00 83.47 ? 429 VAL A C 1 ATOM 3286 O O . VAL A 1 429 ? 7.306 42.388 4.322 1.00 87.57 ? 429 VAL A O 1 ATOM 3287 C CB . VAL A 1 429 ? 5.179 40.580 5.091 1.00 88.43 ? 429 VAL A CB 1 ATOM 3288 C CG1 . VAL A 1 429 ? 4.814 39.107 5.086 1.00 78.00 ? 429 VAL A CG1 1 ATOM 3289 C CG2 . VAL A 1 429 ? 4.031 41.428 5.617 1.00 88.53 ? 429 VAL A CG2 1 ATOM 3290 N N . ASP A 1 430 ? 7.336 43.000 6.497 1.00 108.18 ? 430 ASP A N 1 ATOM 3291 C CA . ASP A 1 430 ? 7.895 44.333 6.278 1.00 96.73 ? 430 ASP A CA 1 ATOM 3292 C C . ASP A 1 430 ? 7.036 45.136 5.308 1.00 82.51 ? 430 ASP A C 1 ATOM 3293 O O . ASP A 1 430 ? 7.485 45.502 4.222 1.00 86.28 ? 430 ASP A O 1 ATOM 3294 C CB . ASP A 1 430 ? 9.332 44.243 5.758 1.00 84.42 ? 430 ASP A CB 1 ATOM 3295 C CG . ASP A 1 430 ? 10.244 43.479 6.696 1.00 103.20 ? 430 ASP A CG 1 ATOM 3296 O OD1 . ASP A 1 430 ? 11.448 43.807 6.756 1.00 132.32 ? 430 ASP A OD1 1 ATOM 3297 O OD2 . ASP A 1 430 ? 9.759 42.550 7.374 1.00 120.36 ? 430 ASP A OD2 1 ATOM 3298 N N . ARG A 1 431 ? 5.801 45.413 5.714 1.00 81.60 ? 431 ARG A N 1 ATOM 3299 C CA . ARG A 1 431 ? 4.843 46.091 4.849 1.00 84.49 ? 431 ARG A CA 1 ATOM 3300 C C . ARG A 1 431 ? 3.879 46.978 5.633 1.00 81.66 ? 431 ARG A C 1 ATOM 3301 O O . ARG A 1 431 ? 3.700 46.811 6.839 1.00 77.23 ? 431 ARG A O 1 ATOM 3302 C CB . ARG A 1 431 ? 4.056 45.068 4.028 1.00 87.33 ? 431 ARG A CB 1 ATOM 3303 C CG . ARG A 1 431 ? 4.795 44.551 2.803 1.00 98.81 ? 431 ARG A CG 1 ATOM 3304 C CD . ARG A 1 431 ? 4.047 43.405 2.147 1.00 96.81 ? 431 ARG A CD 1 ATOM 3305 N NE . ARG A 1 431 ? 4.489 43.181 0.773 1.00 112.68 ? 431 ARG A NE 1 ATOM 3306 C CZ . ARG A 1 431 ? 5.519 42.413 0.432 1.00 125.71 ? 431 ARG A CZ 1 ATOM 3307 N NH1 . ARG A 1 431 ? 6.222 41.790 1.368 1.00 129.08 ? 431 ARG A NH1 1 ATOM 3308 N NH2 . ARG A 1 431 ? 5.846 42.269 -0.845 1.00 128.03 ? 431 ARG A NH2 1 ATOM 3309 N N . ALA A 1 432 ? 3.266 47.926 4.933 1.00 84.12 ? 432 ALA A N 1 ATOM 3310 C CA . ALA A 1 432 ? 2.267 48.808 5.524 1.00 82.53 ? 432 ALA A CA 1 ATOM 3311 C C . ALA A 1 432 ? 1.128 49.024 4.536 1.00 85.67 ? 432 ALA A C 1 ATOM 3312 O O . ALA A 1 432 ? 1.364 49.285 3.357 1.00 89.43 ? 432 ALA A O 1 ATOM 3313 C CB . ALA A 1 432 ? 2.891 50.133 5.924 1.00 89.78 ? 432 ALA A CB 1 ATOM 3314 N N . ILE A 1 433 ? -0.106 48.911 5.017 1.00 84.09 ? 433 ILE A N 1 ATOM 3315 C CA . ILE A 1 433 ? -1.271 48.996 4.144 1.00 87.22 ? 433 ILE A CA 1 ATOM 3316 C C . ILE A 1 433 ? -2.214 50.125 4.560 1.00 86.19 ? 433 ILE A C 1 ATOM 3317 O O . ILE A 1 433 ? -2.592 50.235 5.726 1.00 82.99 ? 433 ILE A O 1 ATOM 3318 C CB . ILE A 1 433 ? -2.055 47.662 4.115 1.00 87.22 ? 433 ILE A CB 1 ATOM 3319 C CG1 . ILE A 1 433 ? -1.155 46.512 3.651 1.00 90.07 ? 433 ILE A CG1 1 ATOM 3320 C CG2 . ILE A 1 433 ? -3.266 47.771 3.204 1.00 90.96 ? 433 ILE A CG2 1 ATOM 3321 C CD1 . ILE A 1 433 ? -0.482 45.748 4.778 1.00 95.74 ? 433 ILE A CD1 1 ATOM 3322 N N . LEU A 1 434 ? -2.589 50.960 3.595 1.00 88.80 ? 434 LEU A N 1 ATOM 3323 C CA . LEU A 1 434 ? -3.488 52.080 3.848 1.00 88.09 ? 434 LEU A CA 1 ATOM 3324 C C . LEU A 1 434 ? -4.881 51.781 3.305 1.00 90.07 ? 434 LEU A C 1 ATOM 3325 O O . LEU A 1 434 ? -5.079 51.699 2.093 1.00 93.53 ? 434 LEU A O 1 ATOM 3326 C CB . LEU A 1 434 ? -2.926 53.364 3.222 1.00 89.69 ? 434 LEU A CB 1 ATOM 3327 C CG . LEU A 1 434 ? -3.621 54.722 3.413 1.00 89.43 ? 434 LEU A CG 1 ATOM 3328 C CD1 . LEU A 1 434 ? -4.611 55.007 2.296 1.00 98.14 ? 434 LEU A CD1 1 ATOM 3329 C CD2 . LEU A 1 434 ? -4.307 54.824 4.768 1.00 91.29 ? 434 LEU A CD2 1 ATOM 3330 N N . TYR A 1 435 ? -5.840 51.612 4.210 1.00 90.61 ? 435 TYR A N 1 ATOM 3331 C CA . TYR A 1 435 ? -7.226 51.369 3.824 1.00 88.91 ? 435 TYR A CA 1 ATOM 3332 C C . TYR A 1 435 ? -7.998 52.680 3.764 1.00 89.07 ? 435 TYR A C 1 ATOM 3333 O O . TYR A 1 435 ? -7.912 53.501 4.676 1.00 86.67 ? 435 TYR A O 1 ATOM 3334 C CB . TYR A 1 435 ? -7.899 50.399 4.797 1.00 85.60 ? 435 TYR A CB 1 ATOM 3335 C CG . TYR A 1 435 ? -7.314 49.007 4.778 1.00 85.32 ? 435 TYR A CG 1 ATOM 3336 C CD1 . TYR A 1 435 ? -6.328 48.635 5.681 1.00 82.40 ? 435 TYR A CD1 1 ATOM 3337 C CD2 . TYR A 1 435 ? -7.746 48.065 3.855 1.00 92.49 ? 435 TYR A CD2 1 ATOM 3338 C CE1 . TYR A 1 435 ? -5.789 47.364 5.667 1.00 81.96 ? 435 TYR A CE1 1 ATOM 3339 C CE2 . TYR A 1 435 ? -7.212 46.790 3.832 1.00 87.84 ? 435 TYR A CE2 1 ATOM 3340 C CZ . TYR A 1 435 ? -6.234 46.446 4.739 1.00 84.50 ? 435 TYR A CZ 1 ATOM 3341 O OH . TYR A 1 435 ? -5.700 45.179 4.721 1.00 83.78 ? 435 TYR A OH 1 ATOM 3342 N N . ARG A 1 436 ? -8.752 52.870 2.687 1.00 91.81 ? 436 ARG A N 1 ATOM 3343 C CA . ARG A 1 436 ? -9.480 54.115 2.474 1.00 92.77 ? 436 ARG A CA 1 ATOM 3344 C C . ARG A 1 436 ? -10.976 53.925 2.690 1.00 92.76 ? 436 ARG A C 1 ATOM 3345 O O . ARG A 1 436 ? -11.557 52.936 2.244 1.00 123.71 ? 436 ARG A O 1 ATOM 3346 C CB . ARG A 1 436 ? -9.207 54.652 1.067 1.00 98.74 ? 436 ARG A CB 1 ATOM 3347 C CG . ARG A 1 436 ? -7.751 54.522 0.654 1.00 106.24 ? 436 ARG A CG 1 ATOM 3348 C CD . ARG A 1 436 ? -7.385 55.431 -0.507 1.00 102.81 ? 436 ARG A CD 1 ATOM 3349 N NE . ARG A 1 436 ? -8.079 55.067 -1.738 1.00 120.53 ? 436 ARG A NE 1 ATOM 3350 C CZ . ARG A 1 436 ? -9.015 55.812 -2.313 1.00 128.37 ? 436 ARG A CZ 1 ATOM 3351 N NH1 . ARG A 1 436 ? -9.369 56.968 -1.770 1.00 125.50 ? 436 ARG A NH1 1 ATOM 3352 N NH2 . ARG A 1 436 ? -9.594 55.404 -3.434 1.00 125.44 ? 436 ARG A NH2 1 ATOM 3353 N N . ALA A 1 437 ? -11.596 54.880 3.375 1.00 90.52 ? 437 ALA A N 1 ATOM 3354 C CA . ALA A 1 437 ? -13.006 54.773 3.725 1.00 89.59 ? 437 ALA A CA 1 ATOM 3355 C C . ALA A 1 437 ? -13.917 55.156 2.567 1.00 103.98 ? 437 ALA A C 1 ATOM 3356 O O . ALA A 1 437 ? -13.756 56.212 1.954 1.00 112.40 ? 437 ALA A O 1 ATOM 3357 C CB . ALA A 1 437 ? -13.311 55.634 4.936 1.00 86.04 ? 437 ALA A CB 1 ATOM 3358 N N . ARG A 1 438 ? -14.875 54.284 2.272 1.00 108.37 ? 438 ARG A N 1 ATOM 3359 C CA . ARG A 1 438 ? -15.888 54.563 1.264 1.00 98.66 ? 438 ARG A CA 1 ATOM 3360 C C . ARG A 1 438 ? -16.955 55.482 1.846 1.00 95.09 ? 438 ARG A C 1 ATOM 3361 O O . ARG A 1 438 ? -17.258 55.406 3.038 1.00 92.32 ? 438 ARG A O 1 ATOM 3362 C CB . ARG A 1 438 ? -16.525 53.264 0.764 1.00 100.33 ? 438 ARG A CB 1 ATOM 3363 C CG . ARG A 1 438 ? -15.528 52.225 0.274 1.00 112.55 ? 438 ARG A CG 1 ATOM 3364 C CD . ARG A 1 438 ? -15.986 50.815 0.627 1.00 125.89 ? 438 ARG A CD 1 ATOM 3365 N NE . ARG A 1 438 ? -17.291 50.491 0.058 1.00 109.03 ? 438 ARG A NE 1 ATOM 3366 C CZ . ARG A 1 438 ? -17.468 49.743 -1.026 1.00 106.09 ? 438 ARG A CZ 1 ATOM 3367 N NH1 . ARG A 1 438 ? -16.420 49.240 -1.665 1.00 109.26 ? 438 ARG A NH1 1 ATOM 3368 N NH2 . ARG A 1 438 ? -18.692 49.500 -1.474 1.00 107.47 ? 438 ARG A NH2 1 ATOM 3369 N N . PRO A 1 439 ? -17.522 56.363 1.011 1.00 96.67 ? 439 PRO A N 1 ATOM 3370 C CA . PRO A 1 439 ? -18.620 57.228 1.455 1.00 95.81 ? 439 PRO A CA 1 ATOM 3371 C C . PRO A 1 439 ? -19.861 56.423 1.838 1.00 98.70 ? 439 PRO A C 1 ATOM 3372 O O . PRO A 1 439 ? -20.062 55.324 1.322 1.00 125.91 ? 439 PRO A O 1 ATOM 3373 C CB . PRO A 1 439 ? -18.891 58.110 0.231 1.00 98.40 ? 439 PRO A CB 1 ATOM 3374 C CG . PRO A 1 439 ? -17.622 58.069 -0.558 1.00 99.89 ? 439 PRO A CG 1 ATOM 3375 C CD . PRO A 1 439 ? -17.082 56.688 -0.356 1.00 99.84 ? 439 PRO A CD 1 ATOM 3376 N N . VAL A 1 440 ? -20.678 56.964 2.735 1.00 93.85 ? 440 VAL A N 1 ATOM 3377 C CA . VAL A 1 440 ? -21.884 56.276 3.185 1.00 95.85 ? 440 VAL A CA 1 ATOM 3378 C C . VAL A 1 440 ? -23.140 56.963 2.660 1.00 97.99 ? 440 VAL A C 1 ATOM 3379 O O . VAL A 1 440 ? -23.320 58.167 2.840 1.00 94.05 ? 440 VAL A O 1 ATOM 3380 C CB . VAL A 1 440 ? -21.951 56.204 4.724 1.00 93.12 ? 440 VAL A CB 1 ATOM 3381 C CG1 . VAL A 1 440 ? -23.274 55.604 5.174 1.00 88.72 ? 440 VAL A CG1 1 ATOM 3382 C CG2 . VAL A 1 440 ? -20.783 55.398 5.266 1.00 98.26 ? 440 VAL A CG2 1 ATOM 3383 N N . ILE A 1 441 ? -24.005 56.190 2.010 1.00 99.83 ? 441 ILE A N 1 ATOM 3384 C CA . ILE A 1 441 ? -25.241 56.724 1.449 1.00 102.91 ? 441 ILE A CA 1 ATOM 3385 C C . ILE A 1 441 ? -26.466 56.222 2.206 1.00 96.67 ? 441 ILE A C 1 ATOM 3386 O O . ILE A 1 441 ? -26.640 55.018 2.393 1.00 96.38 ? 441 ILE A O 1 ATOM 3387 C CB . ILE A 1 441 ? -25.389 56.355 -0.041 1.00 102.23 ? 441 ILE A CB 1 ATOM 3388 C CG1 . ILE A 1 441 ? -24.167 56.828 -0.830 1.00 117.31 ? 441 ILE A CG1 1 ATOM 3389 C CG2 . ILE A 1 441 ? -26.663 56.952 -0.618 1.00 102.69 ? 441 ILE A CG2 1 ATOM 3390 C CD1 . ILE A 1 441 ? -24.236 56.515 -2.309 1.00 109.00 ? 441 ILE A CD1 1 ATOM 3391 N N . THR A 1 442 ? -27.310 57.151 2.644 1.00 107.51 ? 442 THR A N 1 ATOM 3392 C CA . THR A 1 442 ? -28.566 56.799 3.295 1.00 115.00 ? 442 THR A CA 1 ATOM 3393 C C . THR A 1 442 ? -29.724 56.981 2.317 1.00 111.65 ? 442 THR A C 1 ATOM 3394 O O . THR A 1 442 ? -30.047 58.104 1.930 1.00 105.95 ? 442 THR A O 1 ATOM 3395 C CB . THR A 1 442 ? -28.815 57.650 4.555 1.00 120.46 ? 442 THR A CB 1 ATOM 3396 O OG1 . THR A 1 442 ? -27.739 57.460 5.482 1.00 125.77 ? 442 THR A OG1 1 ATOM 3397 C CG2 . THR A 1 442 ? -30.126 57.253 5.218 1.00 107.30 ? 442 THR A CG2 1 ATOM 3398 N N . VAL A 1 443 ? -30.341 55.873 1.919 1.00 107.21 ? 443 VAL A N 1 ATOM 3399 C CA . VAL A 1 443 ? -31.408 55.903 0.924 1.00 100.83 ? 443 VAL A CA 1 ATOM 3400 C C . VAL A 1 443 ? -32.737 55.416 1.501 1.00 101.32 ? 443 VAL A C 1 ATOM 3401 O O . VAL A 1 443 ? -32.802 54.359 2.130 1.00 109.81 ? 443 VAL A O 1 ATOM 3402 C CB . VAL A 1 443 ? -31.038 55.050 -0.313 1.00 103.39 ? 443 VAL A CB 1 ATOM 3403 C CG1 . VAL A 1 443 ? -30.497 53.692 0.110 1.00 106.42 ? 443 VAL A CG1 1 ATOM 3404 C CG2 . VAL A 1 443 ? -32.233 54.894 -1.241 1.00 105.66 ? 443 VAL A CG2 1 ATOM 3405 N N . ASN A 1 444 ? -33.794 56.198 1.299 1.00 104.40 ? 444 ASN A N 1 ATOM 3406 C CA . ASN A 1 444 ? -35.116 55.817 1.780 1.00 109.85 ? 444 ASN A CA 1 ATOM 3407 C C . ASN A 1 444 ? -36.100 55.546 0.645 1.00 107.68 ? 444 ASN A C 1 ATOM 3408 O O . ASN A 1 444 ? -36.553 56.467 -0.036 1.00 108.17 ? 444 ASN A O 1 ATOM 3409 C CB . ASN A 1 444 ? -35.677 56.902 2.701 1.00 127.57 ? 444 ASN A CB 1 ATOM 3410 C CG . ASN A 1 444 ? -34.751 57.217 3.860 1.00 124.84 ? 444 ASN A CG 1 ATOM 3411 O OD1 . ASN A 1 444 ? -34.454 58.380 4.134 1.00 119.12 ? 444 ASN A OD1 1 ATOM 3412 N ND2 . ASN A 1 444 ? -34.287 56.178 4.546 1.00 111.85 ? 444 ASN A ND2 1 ATOM 3413 N N . ALA A 1 445 ? -36.425 54.272 0.455 1.00 118.38 ? 445 ALA A N 1 ATOM 3414 C CA . ALA A 1 445 ? -37.426 53.850 -0.519 1.00 109.54 ? 445 ALA A CA 1 ATOM 3415 C C . ALA A 1 445 ? -38.844 54.089 -0.008 1.00 105.51 ? 445 ALA A C 1 ATOM 3416 O O . ALA A 1 445 ? -39.061 54.253 1.192 1.00 106.75 ? 445 ALA A O 1 ATOM 3417 C CB . ALA A 1 445 ? -37.233 52.385 -0.872 1.00 108.15 ? 445 ALA A CB 1 ATOM 3418 N N . GLY A 1 446 ? -39.806 54.109 -0.925 1.00 113.33 ? 446 GLY A N 1 ATOM 3419 C CA . GLY A 1 446 ? -41.208 54.167 -0.554 1.00 126.22 ? 446 GLY A CA 1 ATOM 3420 C C . GLY A 1 446 ? -42.076 53.512 -1.610 1.00 116.56 ? 446 GLY A C 1 ATOM 3421 O O . GLY A 1 446 ? -41.700 53.448 -2.779 1.00 112.44 ? 446 GLY A O 1 ATOM 3422 N N . LEU A 1 447 ? -43.240 53.019 -1.197 1.00 109.74 ? 447 LEU A N 1 ATOM 3423 C CA . LEU A 1 447 ? -44.119 52.284 -2.101 1.00 112.10 ? 447 LEU A CA 1 ATOM 3424 C C . LEU A 1 447 ? -45.588 52.401 -1.693 1.00 113.94 ? 447 LEU A C 1 ATOM 3425 O O . LEU A 1 447 ? -45.907 52.434 -0.504 1.00 113.57 ? 447 LEU A O 1 ATOM 3426 C CB . LEU A 1 447 ? -43.696 50.813 -2.153 1.00 112.65 ? 447 LEU A CB 1 ATOM 3427 C CG . LEU A 1 447 ? -44.379 49.892 -3.162 1.00 115.00 ? 447 LEU A CG 1 ATOM 3428 C CD1 . LEU A 1 447 ? -44.232 50.433 -4.572 1.00 116.96 ? 447 LEU A CD1 1 ATOM 3429 C CD2 . LEU A 1 447 ? -43.797 48.492 -3.066 1.00 114.85 ? 447 LEU A CD2 1 ATOM 3430 N N . GLU A 1 448 ? -46.476 52.460 -2.681 1.00 113.47 ? 448 GLU A N 1 ATOM 3431 C CA . GLU A 1 448 ? -47.915 52.491 -2.425 1.00 117.62 ? 448 GLU A CA 1 ATOM 3432 C C . GLU A 1 448 ? -48.706 52.014 -3.642 1.00 122.69 ? 448 GLU A C 1 ATOM 3433 O O . GLU A 1 448 ? -48.189 51.997 -4.759 1.00 119.91 ? 448 GLU A O 1 ATOM 3434 C CB . GLU A 1 448 ? -48.361 53.898 -2.022 1.00 116.76 ? 448 GLU A CB 1 ATOM 3435 C CG . GLU A 1 448 ? -48.035 54.978 -3.037 1.00 138.32 ? 448 GLU A CG 1 ATOM 3436 C CD . GLU A 1 448 ? -48.592 56.329 -2.639 1.00 163.05 ? 448 GLU A CD 1 ATOM 3437 O OE1 . GLU A 1 448 ? -48.113 57.354 -3.169 1.00 164.95 ? 448 GLU A OE1 1 ATOM 3438 O OE2 . GLU A 1 448 ? -49.517 56.367 -1.799 1.00 166.66 ? 448 GLU A OE2 1 ATOM 3439 N N . VAL A 1 449 ? -49.960 51.630 -3.422 1.00 116.76 ? 449 VAL A N 1 ATOM 3440 C CA . VAL A 1 449 ? -50.793 51.098 -4.497 1.00 118.49 ? 449 VAL A CA 1 ATOM 3441 C C . VAL A 1 449 ? -52.141 51.814 -4.613 1.00 122.40 ? 449 VAL A C 1 ATOM 3442 O O . VAL A 1 449 ? -52.800 52.091 -3.611 1.00 114.81 ? 449 VAL A O 1 ATOM 3443 C CB . VAL A 1 449 ? -51.038 49.589 -4.308 1.00 117.65 ? 449 VAL A CB 1 ATOM 3444 C CG1 . VAL A 1 449 ? -49.800 48.801 -4.705 1.00 116.85 ? 449 VAL A CG1 1 ATOM 3445 C CG2 . VAL A 1 449 ? -51.427 49.289 -2.869 1.00 118.77 ? 449 VAL A CG2 1 ATOM 3446 N N . TYR A 1 450 ? -52.539 52.113 -5.847 1.00 124.95 ? 450 TYR A N 1 ATOM 3447 C CA . TYR A 1 450 ? -53.792 52.815 -6.117 1.00 123.85 ? 450 TYR A CA 1 ATOM 3448 C C . TYR A 1 450 ? -54.791 51.971 -6.904 1.00 127.53 ? 450 TYR A C 1 ATOM 3449 O O . TYR A 1 450 ? -54.567 51.704 -8.082 1.00 139.12 ? 450 TYR A O 1 ATOM 3450 C CB . TYR A 1 450 ? -53.535 54.098 -6.916 1.00 128.00 ? 450 TYR A CB 1 ATOM 3451 C CG . TYR A 1 450 ? -52.637 55.130 -6.274 1.00 124.44 ? 450 TYR A CG 1 ATOM 3452 C CD1 . TYR A 1 450 ? -52.546 55.256 -4.894 1.00 124.69 ? 450 TYR A CD1 1 ATOM 3453 C CD2 . TYR A 1 450 ? -51.889 55.997 -7.061 1.00 135.23 ? 450 TYR A CD2 1 ATOM 3454 C CE1 . TYR A 1 450 ? -51.724 56.213 -4.317 1.00 147.00 ? 450 TYR A CE1 1 ATOM 3455 C CE2 . TYR A 1 450 ? -51.069 56.952 -6.498 1.00 159.33 ? 450 TYR A CE2 1 ATOM 3456 C CZ . TYR A 1 450 ? -50.988 57.058 -5.128 1.00 165.21 ? 450 TYR A CZ 1 ATOM 3457 O OH . TYR A 1 450 ? -50.168 58.015 -4.573 1.00 156.89 ? 450 TYR A OH 1 ATOM 3458 N N . PRO A 1 451 ? -55.902 51.552 -6.274 1.00 116.95 ? 451 PRO A N 1 ATOM 3459 C CA . PRO A 1 451 ? -56.244 51.468 -4.849 1.00 115.38 ? 451 PRO A CA 1 ATOM 3460 C C . PRO A 1 451 ? -55.678 50.205 -4.204 1.00 115.76 ? 451 PRO A C 1 ATOM 3461 O O . PRO A 1 451 ? -55.358 49.254 -4.918 1.00 115.82 ? 451 PRO A O 1 ATOM 3462 C CB . PRO A 1 451 ? -57.771 51.440 -4.860 1.00 116.39 ? 451 PRO A CB 1 ATOM 3463 C CG . PRO A 1 451 ? -58.100 50.757 -6.132 1.00 121.20 ? 451 PRO A CG 1 ATOM 3464 C CD . PRO A 1 451 ? -57.054 51.200 -7.123 1.00 117.02 ? 451 PRO A CD 1 ATOM 3465 N N . SER A 1 452 ? -55.559 50.192 -2.880 1.00 123.65 ? 452 SER A N 1 ATOM 3466 C CA . SER A 1 452 ? -55.051 49.019 -2.173 1.00 117.16 ? 452 SER A CA 1 ATOM 3467 C C . SER A 1 452 ? -56.032 47.847 -2.220 1.00 113.30 ? 452 SER A C 1 ATOM 3468 O O . SER A 1 452 ? -55.622 46.691 -2.313 1.00 112.72 ? 452 SER A O 1 ATOM 3469 C CB . SER A 1 452 ? -54.732 49.366 -0.717 1.00 120.40 ? 452 SER A CB 1 ATOM 3470 O OG . SER A 1 452 ? -55.915 49.586 0.030 1.00 116.82 ? 452 SER A OG 1 ATOM 3471 N N . ILE A 1 453 ? -57.325 48.145 -2.151 1.00 126.58 ? 453 ILE A N 1 ATOM 3472 C CA . ILE A 1 453 ? -58.346 47.103 -2.180 1.00 111.42 ? 453 ILE A CA 1 ATOM 3473 C C . ILE A 1 453 ? -58.930 46.951 -3.581 1.00 112.00 ? 453 ILE A C 1 ATOM 3474 O O . ILE A 1 453 ? -59.593 47.854 -4.090 1.00 112.49 ? 453 ILE A O 1 ATOM 3475 C CB . ILE A 1 453 ? -59.476 47.394 -1.177 1.00 110.16 ? 453 ILE A CB 1 ATOM 3476 C CG1 . ILE A 1 453 ? -58.909 47.470 0.244 1.00 109.19 ? 453 ILE A CG1 1 ATOM 3477 C CG2 . ILE A 1 453 ? -60.557 46.328 -1.266 1.00 109.24 ? 453 ILE A CG2 1 ATOM 3478 C CD1 . ILE A 1 453 ? -59.912 47.906 1.286 1.00 115.03 ? 453 ILE A CD1 1 ATOM 3479 N N . LEU A 1 454 ? -58.681 45.800 -4.197 1.00 111.70 ? 454 LEU A N 1 ATOM 3480 C CA . LEU A 1 454 ? -59.059 45.574 -5.587 1.00 113.12 ? 454 LEU A CA 1 ATOM 3481 C C . LEU A 1 454 ? -60.473 45.013 -5.732 1.00 113.32 ? 454 LEU A C 1 ATOM 3482 O O . LEU A 1 454 ? -60.807 43.986 -5.142 1.00 113.90 ? 454 LEU A O 1 ATOM 3483 C CB . LEU A 1 454 ? -58.057 44.627 -6.255 1.00 113.50 ? 454 LEU A CB 1 ATOM 3484 C CG . LEU A 1 454 ? -56.575 44.961 -6.074 1.00 113.48 ? 454 LEU A CG 1 ATOM 3485 C CD1 . LEU A 1 454 ? -55.695 43.979 -6.838 1.00 113.52 ? 454 LEU A CD1 1 ATOM 3486 C CD2 . LEU A 1 454 ? -56.290 46.390 -6.502 1.00 114.56 ? 454 LEU A CD2 1 ATOM 3487 N N . ASN A 1 455 ? -61.297 45.696 -6.522 1.00 117.78 ? 455 ASN A N 1 ATOM 3488 C CA . ASN A 1 455 ? -62.615 45.183 -6.872 1.00 114.58 ? 455 ASN A CA 1 ATOM 3489 C C . ASN A 1 455 ? -62.531 44.416 -8.187 1.00 115.13 ? 455 ASN A C 1 ATOM 3490 O O . ASN A 1 455 ? -62.297 44.999 -9.246 1.00 116.17 ? 455 ASN A O 1 ATOM 3491 C CB . ASN A 1 455 ? -63.635 46.321 -6.974 1.00 114.99 ? 455 ASN A CB 1 ATOM 3492 C CG . ASN A 1 455 ? -65.037 45.826 -7.289 1.00 115.21 ? 455 ASN A CG 1 ATOM 3493 O OD1 . ASN A 1 455 ? -65.343 44.646 -7.134 1.00 126.11 ? 455 ASN A OD1 1 ATOM 3494 N ND2 . ASN A 1 455 ? -65.898 46.736 -7.731 1.00 116.39 ? 455 ASN A ND2 1 ATOM 3495 N N . GLN A 1 456 ? -62.726 43.104 -8.106 1.00 114.06 ? 456 GLN A N 1 ATOM 3496 C CA . GLN A 1 456 ? -62.543 42.219 -9.250 1.00 114.92 ? 456 GLN A CA 1 ATOM 3497 C C . GLN A 1 456 ? -63.609 42.453 -10.317 1.00 120.07 ? 456 GLN A C 1 ATOM 3498 O O . GLN A 1 456 ? -63.426 42.093 -11.480 1.00 126.75 ? 456 GLN A O 1 ATOM 3499 C CB . GLN A 1 456 ? -62.563 40.761 -8.784 1.00 113.60 ? 456 GLN A CB 1 ATOM 3500 C CG . GLN A 1 456 ? -61.795 39.794 -9.671 1.00 114.22 ? 456 GLN A CG 1 ATOM 3501 C CD . GLN A 1 456 ? -61.642 38.426 -9.034 1.00 115.09 ? 456 GLN A CD 1 ATOM 3502 O OE1 . GLN A 1 456 ? -62.250 38.138 -8.002 1.00 111.58 ? 456 GLN A OE1 1 ATOM 3503 N NE2 . GLN A 1 456 ? -60.823 37.577 -9.643 1.00 133.10 ? 456 GLN A NE2 1 ATOM 3504 N N . ASP A 1 457 ? -64.719 43.063 -9.915 1.00 127.52 ? 457 ASP A N 1 ATOM 3505 C CA . ASP A 1 457 ? -65.827 43.322 -10.826 1.00 130.89 ? 457 ASP A CA 1 ATOM 3506 C C . ASP A 1 457 ? -65.725 44.715 -11.445 1.00 136.21 ? 457 ASP A C 1 ATOM 3507 O O . ASP A 1 457 ? -66.551 45.099 -12.274 1.00 135.11 ? 457 ASP A O 1 ATOM 3508 C CB . ASP A 1 457 ? -67.163 43.162 -10.095 1.00 138.71 ? 457 ASP A CB 1 ATOM 3509 C CG . ASP A 1 457 ? -68.351 43.167 -11.037 1.00 146.58 ? 457 ASP A CG 1 ATOM 3510 O OD1 . ASP A 1 457 ? -68.225 42.643 -12.165 1.00 148.53 ? 457 ASP A OD1 1 ATOM 3511 O OD2 . ASP A 1 457 ? -69.411 43.701 -10.650 1.00 144.19 ? 457 ASP A OD2 1 ATOM 3512 N N . ASN A 1 458 ? -64.700 45.467 -11.056 1.00 145.97 ? 458 ASN A N 1 ATOM 3513 C CA . ASN A 1 458 ? -64.518 46.807 -11.596 1.00 146.25 ? 458 ASN A CA 1 ATOM 3514 C C . ASN A 1 458 ? -63.432 46.776 -12.672 1.00 140.01 ? 458 ASN A C 1 ATOM 3515 O O . ASN A 1 458 ? -62.238 46.737 -12.384 1.00 146.90 ? 458 ASN A O 1 ATOM 3516 C CB . ASN A 1 458 ? -64.178 47.768 -10.448 1.00 150.66 ? 458 ASN A CB 1 ATOM 3517 C CG . ASN A 1 458 ? -63.665 49.117 -10.913 1.00 155.69 ? 458 ASN A CG 1 ATOM 3518 O OD1 . ASN A 1 458 ? -63.932 49.563 -12.029 1.00 156.19 ? 458 ASN A OD1 1 ATOM 3519 N ND2 . ASN A 1 458 ? -62.921 49.781 -10.033 1.00 174.82 ? 458 ASN A ND2 1 ATOM 3520 N N . LYS A 1 459 ? -63.890 46.811 -13.921 1.00 127.78 ? 459 LYS A N 1 ATOM 3521 C CA . LYS A 1 459 ? -63.061 46.592 -15.107 1.00 136.53 ? 459 LYS A CA 1 ATOM 3522 C C . LYS A 1 459 ? -62.649 47.861 -15.856 1.00 163.09 ? 459 LYS A C 1 ATOM 3523 O O . LYS A 1 459 ? -62.067 47.776 -16.937 1.00 179.63 ? 459 LYS A O 1 ATOM 3524 C CB . LYS A 1 459 ? -63.780 45.639 -16.062 1.00 143.20 ? 459 LYS A CB 1 ATOM 3525 C CG . LYS A 1 459 ? -64.176 44.322 -15.409 1.00 132.86 ? 459 LYS A CG 1 ATOM 3526 C CD . LYS A 1 459 ? -64.384 43.223 -16.436 1.00 150.10 ? 459 LYS A CD 1 ATOM 3527 C CE . LYS A 1 459 ? -64.828 41.928 -15.773 1.00 150.03 ? 459 LYS A CE 1 ATOM 3528 N NZ . LYS A 1 459 ? -66.177 42.058 -15.152 1.00 148.45 ? 459 LYS A NZ 1 ATOM 3529 N N . THR A 1 460 ? -62.954 49.021 -15.281 1.00 167.02 ? 460 THR A N 1 ATOM 3530 C CA . THR A 1 460 ? -63.071 50.286 -16.013 1.00 180.23 ? 460 THR A CA 1 ATOM 3531 C C . THR A 1 460 ? -61.998 50.602 -17.065 1.00 171.68 ? 460 THR A C 1 ATOM 3532 O O . THR A 1 460 ? -62.315 51.173 -18.109 1.00 183.26 ? 460 THR A O 1 ATOM 3533 C CB . THR A 1 460 ? -63.100 51.470 -15.024 1.00 169.02 ? 460 THR A CB 1 ATOM 3534 O OG1 . THR A 1 460 ? -62.943 52.702 -15.741 1.00 185.15 ? 460 THR A OG1 1 ATOM 3535 C CG2 . THR A 1 460 ? -61.980 51.340 -14.014 1.00 130.62 ? 460 THR A CG2 1 ATOM 3536 N N . CYS A 1 461 ? -60.742 50.254 -16.807 1.00 129.77 ? 461 CYS A N 1 ATOM 3537 C CA . CYS A 1 461 ? -59.677 50.621 -17.738 1.00 138.79 ? 461 CYS A CA 1 ATOM 3538 C C . CYS A 1 461 ? -58.787 49.455 -18.165 1.00 141.79 ? 461 CYS A C 1 ATOM 3539 O O . CYS A 1 461 ? -58.409 48.626 -17.336 1.00 148.27 ? 461 CYS A O 1 ATOM 3540 C CB . CYS A 1 461 ? -58.803 51.716 -17.120 1.00 158.48 ? 461 CYS A CB 1 ATOM 3541 S SG . CYS A 1 461 ? -57.895 51.203 -15.637 1.00 219.41 ? 461 CYS A SG 1 ATOM 3542 N N . SER A 1 462 ? -58.463 49.414 -19.460 1.00 144.45 ? 462 SER A N 1 ATOM 3543 C CA . SER A 1 462 ? -57.385 48.572 -19.992 1.00 147.34 ? 462 SER A CA 1 ATOM 3544 C C . SER A 1 462 ? -57.200 48.733 -21.499 1.00 150.58 ? 462 SER A C 1 ATOM 3545 O O . SER A 1 462 ? -58.119 49.136 -22.214 1.00 142.56 ? 462 SER A O 1 ATOM 3546 C CB . SER A 1 462 ? -57.648 47.095 -19.699 1.00 155.67 ? 462 SER A CB 1 ATOM 3547 O OG . SER A 1 462 ? -56.480 46.323 -19.915 1.00 176.89 ? 462 SER A OG 1 ATOM 3548 N N . LEU A 1 463 ? -55.998 48.412 -21.967 1.00 167.84 ? 463 LEU A N 1 ATOM 3549 C CA . LEU A 1 463 ? -55.710 48.270 -23.390 1.00 179.19 ? 463 LEU A CA 1 ATOM 3550 C C . LEU A 1 463 ? -54.643 47.194 -23.597 1.00 180.23 ? 463 LEU A C 1 ATOM 3551 O O . LEU A 1 463 ? -53.515 47.509 -23.979 1.00 174.16 ? 463 LEU A O 1 ATOM 3552 C CB . LEU A 1 463 ? -55.257 49.605 -23.990 1.00 167.58 ? 463 LEU A CB 1 ATOM 3553 C CG . LEU A 1 463 ? -55.734 49.947 -25.407 1.00 158.94 ? 463 LEU A CG 1 ATOM 3554 C CD1 . LEU A 1 463 ? -55.283 51.348 -25.794 1.00 150.14 ? 463 LEU A CD1 1 ATOM 3555 C CD2 . LEU A 1 463 ? -55.251 48.927 -26.430 1.00 149.43 ? 463 LEU A CD2 1 ATOM 3556 N N . PRO A 1 464 ? -54.987 45.923 -23.343 1.00 169.59 ? 464 PRO A N 1 ATOM 3557 C CA . PRO A 1 464 ? -53.965 44.873 -23.363 1.00 162.51 ? 464 PRO A CA 1 ATOM 3558 C C . PRO A 1 464 ? -53.707 44.302 -24.755 1.00 176.47 ? 464 PRO A C 1 ATOM 3559 O O . PRO A 1 464 ? -53.874 43.098 -24.956 1.00 183.24 ? 464 PRO A O 1 ATOM 3560 C CB . PRO A 1 464 ? -54.554 43.794 -22.440 1.00 135.74 ? 464 PRO A CB 1 ATOM 3561 C CG . PRO A 1 464 ? -56.004 44.210 -22.174 1.00 132.52 ? 464 PRO A CG 1 ATOM 3562 C CD . PRO A 1 464 ? -56.319 45.366 -23.075 1.00 147.78 ? 464 PRO A CD 1 ATOM 3563 N N . GLY A 1 465 ? -53.298 45.148 -25.695 1.00 173.43 ? 465 GLY A N 1 ATOM 3564 C CA . GLY A 1 465 ? -52.992 44.687 -27.037 1.00 170.85 ? 465 GLY A CA 1 ATOM 3565 C C . GLY A 1 465 ? -54.216 44.159 -27.759 1.00 167.07 ? 465 GLY A C 1 ATOM 3566 O O . GLY A 1 465 ? -54.236 43.001 -28.181 1.00 167.70 ? 465 GLY A O 1 ATOM 3567 N N . THR A 1 466 ? -55.234 45.008 -27.884 1.00 163.63 ? 466 THR A N 1 ATOM 3568 C CA . THR A 1 466 ? -56.509 44.642 -28.499 1.00 180.44 ? 466 THR A CA 1 ATOM 3569 C C . THR A 1 466 ? -57.160 43.487 -27.742 1.00 185.33 ? 466 THR A C 1 ATOM 3570 O O . THR A 1 466 ? -57.219 42.357 -28.229 1.00 197.83 ? 466 THR A O 1 ATOM 3571 C CB . THR A 1 466 ? -56.343 44.265 -29.990 1.00 176.32 ? 466 THR A CB 1 ATOM 3572 O OG1 . THR A 1 466 ? -55.461 45.198 -30.627 1.00 186.93 ? 466 THR A OG1 1 ATOM 3573 C CG2 . THR A 1 466 ? -57.689 44.275 -30.702 1.00 159.87 ? 466 THR A CG2 1 ATOM 3574 N N . ALA A 1 467 ? -57.633 43.783 -26.535 1.00 170.45 ? 467 ALA A N 1 ATOM 3575 C CA . ALA A 1 467 ? -58.259 42.777 -25.687 1.00 170.77 ? 467 ALA A CA 1 ATOM 3576 C C . ALA A 1 467 ? -59.385 43.377 -24.848 1.00 192.48 ? 467 ALA A C 1 ATOM 3577 O O . ALA A 1 467 ? -59.796 44.518 -25.062 1.00 200.52 ? 467 ALA A O 1 ATOM 3578 C CB . ALA A 1 467 ? -57.222 42.120 -24.793 1.00 140.67 ? 467 ALA A CB 1 ATOM 3579 N N . LEU A 1 468 ? -59.880 42.596 -23.893 1.00 188.02 ? 468 LEU A N 1 ATOM 3580 C CA . LEU A 1 468 ? -61.024 42.991 -23.076 1.00 170.96 ? 468 LEU A CA 1 ATOM 3581 C C . LEU A 1 468 ? -60.643 43.992 -21.988 1.00 156.63 ? 468 LEU A C 1 ATOM 3582 O O . LEU A 1 468 ? -59.509 44.469 -21.935 1.00 159.83 ? 468 LEU A O 1 ATOM 3583 C CB . LEU A 1 468 ? -61.673 41.761 -22.432 1.00 165.63 ? 468 LEU A CB 1 ATOM 3584 C CG . LEU A 1 468 ? -62.259 40.664 -23.329 1.00 172.84 ? 468 LEU A CG 1 ATOM 3585 C CD1 . LEU A 1 468 ? -61.186 39.702 -23.829 1.00 167.43 ? 468 LEU A CD1 1 ATOM 3586 C CD2 . LEU A 1 468 ? -63.355 39.908 -22.592 1.00 173.93 ? 468 LEU A CD2 1 ATOM 3587 N N . LYS A 1 469 ? -61.605 44.302 -21.123 1.00 153.40 ? 469 LYS A N 1 ATOM 3588 C CA . LYS A 1 469 ? -61.374 45.184 -19.983 1.00 145.55 ? 469 LYS A CA 1 ATOM 3589 C C . LYS A 1 469 ? -61.018 44.383 -18.735 1.00 136.29 ? 469 LYS A C 1 ATOM 3590 O O . LYS A 1 469 ? -61.585 43.319 -18.488 1.00 134.60 ? 469 LYS A O 1 ATOM 3591 C CB . LYS A 1 469 ? -62.605 46.051 -19.713 1.00 138.30 ? 469 LYS A CB 1 ATOM 3592 C CG . LYS A 1 469 ? -62.593 47.400 -20.411 1.00 141.87 ? 469 LYS A CG 1 ATOM 3593 C CD . LYS A 1 469 ? -63.825 48.213 -20.044 1.00 142.75 ? 469 LYS A CD 1 ATOM 3594 C CE . LYS A 1 469 ? -63.713 49.646 -20.536 1.00 134.49 ? 469 LYS A CE 1 ATOM 3595 N NZ . LYS A 1 469 ? -63.481 49.722 -22.003 1.00 138.47 ? 469 LYS A NZ 1 ATOM 3596 N N . VAL A 1 470 ? -60.078 44.899 -17.950 1.00 133.01 ? 470 VAL A N 1 ATOM 3597 C CA . VAL A 1 470 ? -59.642 44.226 -16.730 1.00 147.87 ? 470 VAL A CA 1 ATOM 3598 C C . VAL A 1 470 ? -59.577 45.195 -15.554 1.00 140.76 ? 470 VAL A C 1 ATOM 3599 O O . VAL A 1 470 ? -59.665 46.410 -15.732 1.00 124.62 ? 470 VAL A O 1 ATOM 3600 C CB . VAL A 1 470 ? -58.258 43.568 -16.902 1.00 149.61 ? 470 VAL A CB 1 ATOM 3601 C CG1 . VAL A 1 470 ? -58.299 42.497 -17.983 1.00 156.65 ? 470 VAL A CG1 1 ATOM 3602 C CG2 . VAL A 1 470 ? -57.215 44.618 -17.226 1.00 130.88 ? 470 VAL A CG2 1 ATOM 3603 N N . SER A 1 471 ? -59.439 44.648 -14.349 1.00 138.94 ? 471 SER A N 1 ATOM 3604 C CA . SER A 1 471 ? -59.313 45.467 -13.151 1.00 128.40 ? 471 SER A CA 1 ATOM 3605 C C . SER A 1 471 ? -57.854 45.847 -12.936 1.00 128.60 ? 471 SER A C 1 ATOM 3606 O O . SER A 1 471 ? -57.008 44.983 -12.707 1.00 120.71 ? 471 SER A O 1 ATOM 3607 C CB . SER A 1 471 ? -59.861 44.723 -11.931 1.00 121.08 ? 471 SER A CB 1 ATOM 3608 O OG . SER A 1 471 ? -59.848 45.549 -10.781 1.00 131.39 ? 471 SER A OG 1 ATOM 3609 N N . CYS A 1 472 ? -57.567 47.144 -12.987 1.00 139.74 ? 472 CYS A N 1 ATOM 3610 C CA . CYS A 1 472 ? -56.188 47.615 -12.947 1.00 127.75 ? 472 CYS A CA 1 ATOM 3611 C C . CYS A 1 472 ? -55.922 48.573 -11.794 1.00 127.60 ? 472 CYS A C 1 ATOM 3612 O O . CYS A 1 472 ? -56.646 49.549 -11.602 1.00 137.02 ? 472 CYS A O 1 ATOM 3613 C CB . CYS A 1 472 ? -55.825 48.293 -14.272 1.00 129.49 ? 472 CYS A CB 1 ATOM 3614 S SG . CYS A 1 472 ? -56.893 49.685 -14.729 1.00 181.27 ? 472 CYS A SG 1 ATOM 3615 N N . PHE A 1 473 ? -54.881 48.282 -11.022 1.00 124.81 ? 473 PHE A N 1 ATOM 3616 C CA . PHE A 1 473 ? -54.417 49.201 -9.989 1.00 119.92 ? 473 PHE A CA 1 ATOM 3617 C C . PHE A 1 473 ? -53.120 49.877 -10.426 1.00 120.80 ? 473 PHE A C 1 ATOM 3618 O O . PHE A 1 473 ? -52.606 49.605 -11.511 1.00 121.19 ? 473 PHE A O 1 ATOM 3619 C CB . PHE A 1 473 ? -54.227 48.473 -8.654 1.00 118.19 ? 473 PHE A CB 1 ATOM 3620 C CG . PHE A 1 473 ? -53.350 47.254 -8.738 1.00 117.81 ? 473 PHE A CG 1 ATOM 3621 C CD1 . PHE A 1 473 ? -52.005 47.330 -8.417 1.00 118.08 ? 473 PHE A CD1 1 ATOM 3622 C CD2 . PHE A 1 473 ? -53.874 46.031 -9.123 1.00 117.38 ? 473 PHE A CD2 1 ATOM 3623 C CE1 . PHE A 1 473 ? -51.197 46.210 -8.488 1.00 117.56 ? 473 PHE A CE1 1 ATOM 3624 C CE2 . PHE A 1 473 ? -53.072 44.908 -9.196 1.00 117.48 ? 473 PHE A CE2 1 ATOM 3625 C CZ . PHE A 1 473 ? -51.733 44.997 -8.878 1.00 116.91 ? 473 PHE A CZ 1 ATOM 3626 N N . ASN A 1 474 ? -52.594 50.759 -9.584 1.00 123.43 ? 474 ASN A N 1 ATOM 3627 C CA . ASN A 1 474 ? -51.360 51.469 -9.903 1.00 122.63 ? 474 ASN A CA 1 ATOM 3628 C C . ASN A 1 474 ? -50.267 51.215 -8.873 1.00 121.46 ? 474 ASN A C 1 ATOM 3629 O O . ASN A 1 474 ? -50.548 51.043 -7.689 1.00 120.27 ? 474 ASN A O 1 ATOM 3630 C CB . ASN A 1 474 ? -51.622 52.972 -10.021 1.00 132.61 ? 474 ASN A CB 1 ATOM 3631 C CG . ASN A 1 474 ? -52.425 53.328 -11.256 1.00 167.80 ? 474 ASN A CG 1 ATOM 3632 O OD1 . ASN A 1 474 ? -53.655 53.383 -11.218 1.00 182.51 ? 474 ASN A OD1 1 ATOM 3633 N ND2 . ASN A 1 474 ? -51.731 53.573 -12.362 1.00 173.42 ? 474 ASN A ND2 1 ATOM 3634 N N . VAL A 1 475 ? -49.021 51.188 -9.334 1.00 129.99 ? 475 VAL A N 1 ATOM 3635 C CA . VAL A 1 475 ? -47.884 50.997 -8.443 1.00 127.82 ? 475 VAL A CA 1 ATOM 3636 C C . VAL A 1 475 ? -46.947 52.198 -8.501 1.00 140.83 ? 475 VAL A C 1 ATOM 3637 O O . VAL A 1 475 ? -46.317 52.459 -9.526 1.00 153.49 ? 475 VAL A O 1 ATOM 3638 C CB . VAL A 1 475 ? -47.098 49.720 -8.792 1.00 120.65 ? 475 VAL A CB 1 ATOM 3639 C CG1 . VAL A 1 475 ? -45.899 49.567 -7.869 1.00 119.83 ? 475 VAL A CG1 1 ATOM 3640 C CG2 . VAL A 1 475 ? -48.003 48.501 -8.703 1.00 119.76 ? 475 VAL A CG2 1 ATOM 3641 N N . ARG A 1 476 ? -46.864 52.929 -7.394 1.00 138.43 ? 476 ARG A N 1 ATOM 3642 C CA . ARG A 1 476 ? -46.013 54.110 -7.314 1.00 132.66 ? 476 ARG A CA 1 ATOM 3643 C C . ARG A 1 476 ? -44.907 53.909 -6.287 1.00 127.08 ? 476 ARG A C 1 ATOM 3644 O O . ARG A 1 476 ? -45.177 53.718 -5.101 1.00 132.67 ? 476 ARG A O 1 ATOM 3645 C CB . ARG A 1 476 ? -46.844 55.347 -6.962 1.00 127.05 ? 476 ARG A CB 1 ATOM 3646 C CG . ARG A 1 476 ? -46.052 56.645 -6.909 1.00 117.51 ? 476 ARG A CG 1 ATOM 3647 C CD . ARG A 1 476 ? -46.935 57.806 -6.476 1.00 116.56 ? 476 ARG A CD 1 ATOM 3648 N NE . ARG A 1 476 ? -46.208 59.071 -6.438 1.00 138.02 ? 476 ARG A NE 1 ATOM 3649 C CZ . ARG A 1 476 ? -46.173 59.945 -7.439 1.00 161.67 ? 476 ARG A CZ 1 ATOM 3650 N NH1 . ARG A 1 476 ? -46.829 59.693 -8.562 1.00 164.53 ? 476 ARG A NH1 1 ATOM 3651 N NH2 . ARG A 1 476 ? -45.485 61.071 -7.314 1.00 159.20 ? 476 ARG A NH2 1 ATOM 3652 N N . PHE A 1 477 ? -43.661 53.948 -6.747 1.00 124.50 ? 477 PHE A N 1 ATOM 3653 C CA . PHE A 1 477 ? -42.520 53.784 -5.855 1.00 132.09 ? 477 PHE A CA 1 ATOM 3654 C C . PHE A 1 477 ? -41.616 55.013 -5.881 1.00 135.80 ? 477 PHE A C 1 ATOM 3655 O O . PHE A 1 477 ? -41.252 55.511 -6.947 1.00 135.93 ? 477 PHE A O 1 ATOM 3656 C CB . PHE A 1 477 ? -41.727 52.520 -6.212 1.00 126.45 ? 477 PHE A CB 1 ATOM 3657 C CG . PHE A 1 477 ? -41.208 52.495 -7.624 1.00 124.44 ? 477 PHE A CG 1 ATOM 3658 C CD1 . PHE A 1 477 ? -39.899 52.851 -7.901 1.00 136.33 ? 477 PHE A CD1 1 ATOM 3659 C CD2 . PHE A 1 477 ? -42.022 52.091 -8.671 1.00 122.24 ? 477 PHE A CD2 1 ATOM 3660 C CE1 . PHE A 1 477 ? -39.415 52.820 -9.195 1.00 142.87 ? 477 PHE A CE1 1 ATOM 3661 C CE2 . PHE A 1 477 ? -41.545 52.058 -9.968 1.00 124.38 ? 477 PHE A CE2 1 ATOM 3662 C CZ . PHE A 1 477 ? -40.238 52.423 -10.229 1.00 133.31 ? 477 PHE A CZ 1 ATOM 3663 N N . CYS A 1 478 ? -41.265 55.499 -4.695 1.00 134.81 ? 478 CYS A N 1 ATOM 3664 C CA . CYS A 1 478 ? -40.456 56.704 -4.563 1.00 138.26 ? 478 CYS A CA 1 ATOM 3665 C C . CYS A 1 478 ? -39.094 56.392 -3.954 1.00 131.91 ? 478 CYS A C 1 ATOM 3666 O O . CYS A 1 478 ? -38.989 55.599 -3.019 1.00 123.89 ? 478 CYS A O 1 ATOM 3667 C CB . CYS A 1 478 ? -41.188 57.745 -3.715 1.00 137.41 ? 478 CYS A CB 1 ATOM 3668 S SG . CYS A 1 478 ? -42.815 58.210 -4.348 1.00 220.75 ? 478 CYS A SG 1 ATOM 3669 N N . LEU A 1 479 ? -38.052 57.016 -4.492 1.00 128.53 ? 479 LEU A N 1 ATOM 3670 C CA . LEU A 1 479 ? -36.691 56.746 -4.045 1.00 121.16 ? 479 LEU A CA 1 ATOM 3671 C C . LEU A 1 479 ? -35.874 58.027 -3.880 1.00 114.11 ? 479 LEU A C 1 ATOM 3672 O O . LEU A 1 479 ? -35.709 58.789 -4.831 1.00 117.31 ? 479 LEU A O 1 ATOM 3673 C CB . LEU A 1 479 ? -35.998 55.804 -5.031 1.00 123.68 ? 479 LEU A CB 1 ATOM 3674 C CG . LEU A 1 479 ? -34.745 55.072 -4.555 1.00 115.17 ? 479 LEU A CG 1 ATOM 3675 C CD1 . LEU A 1 479 ? -35.081 54.122 -3.418 1.00 114.02 ? 479 LEU A CD1 1 ATOM 3676 C CD2 . LEU A 1 479 ? -34.112 54.321 -5.711 1.00 117.43 ? 479 LEU A CD2 1 ATOM 3677 N N . LYS A 1 480 ? -35.370 58.260 -2.671 1.00 121.52 ? 480 LYS A N 1 ATOM 3678 C CA . LYS A 1 480 ? -34.467 59.382 -2.427 1.00 137.31 ? 480 LYS A CA 1 ATOM 3679 C C . LYS A 1 480 ? -33.209 58.915 -1.708 1.00 127.95 ? 480 LYS A C 1 ATOM 3680 O O . LYS A 1 480 ? -33.241 57.957 -0.936 1.00 123.78 ? 480 LYS A O 1 ATOM 3681 C CB . LYS A 1 480 ? -35.154 60.482 -1.612 1.00 141.34 ? 480 LYS A CB 1 ATOM 3682 C CG . LYS A 1 480 ? -35.393 60.143 -0.146 1.00 135.91 ? 480 LYS A CG 1 ATOM 3683 C CD . LYS A 1 480 ? -35.942 61.347 0.608 1.00 134.95 ? 480 LYS A CD 1 ATOM 3684 C CE . LYS A 1 480 ? -36.235 61.014 2.062 1.00 136.49 ? 480 LYS A CE 1 ATOM 3685 N NZ . LYS A 1 480 ? -35.021 60.547 2.785 1.00 146.16 ? 480 LYS A NZ 1 ATOM 3686 N N . ALA A 1 481 ? -32.101 59.598 -1.969 1.00 117.00 ? 481 ALA A N 1 ATOM 3687 C CA . ALA A 1 481 ? -30.831 59.249 -1.351 1.00 116.74 ? 481 ALA A CA 1 ATOM 3688 C C . ALA A 1 481 ? -30.010 60.494 -1.046 1.00 134.95 ? 481 ALA A C 1 ATOM 3689 O O . ALA A 1 481 ? -29.968 61.431 -1.842 1.00 151.51 ? 481 ALA A O 1 ATOM 3690 C CB . ALA A 1 481 ? -30.047 58.304 -2.250 1.00 115.23 ? 481 ALA A CB 1 ATOM 3691 N N . ASP A 1 482 ? -29.362 60.499 0.113 1.00 135.30 ? 482 ASP A N 1 ATOM 3692 C CA . ASP A 1 482 ? -28.476 61.590 0.492 1.00 138.21 ? 482 ASP A CA 1 ATOM 3693 C C . ASP A 1 482 ? -27.251 61.014 1.195 1.00 125.62 ? 482 ASP A C 1 ATOM 3694 O O . ASP A 1 482 ? -27.162 59.803 1.403 1.00 115.57 ? 482 ASP A O 1 ATOM 3695 C CB . ASP A 1 482 ? -29.206 62.594 1.391 1.00 140.74 ? 482 ASP A CB 1 ATOM 3696 C CG . ASP A 1 482 ? -28.503 63.939 1.462 1.00 152.16 ? 482 ASP A CG 1 ATOM 3697 O OD1 . ASP A 1 482 ? -27.748 64.267 0.522 1.00 144.65 ? 482 ASP A OD1 1 ATOM 3698 O OD2 . ASP A 1 482 ? -28.707 64.666 2.456 1.00 167.43 ? 482 ASP A OD2 1 ATOM 3699 N N . GLY A 1 483 ? -26.311 61.877 1.563 1.00 122.19 ? 483 GLY A N 1 ATOM 3700 C CA . GLY A 1 483 ? -25.094 61.437 2.219 1.00 117.62 ? 483 GLY A CA 1 ATOM 3701 C C . GLY A 1 483 ? -24.233 62.594 2.680 1.00 118.80 ? 483 GLY A C 1 ATOM 3702 O O . GLY A 1 483 ? -24.675 63.742 2.701 1.00 129.94 ? 483 GLY A O 1 ATOM 3703 N N . LYS A 1 484 ? -22.995 62.286 3.053 1.00 122.65 ? 484 LYS A N 1 ATOM 3704 C CA . LYS A 1 484 ? -22.061 63.293 3.543 1.00 117.11 ? 484 LYS A CA 1 ATOM 3705 C C . LYS A 1 484 ? -20.679 63.088 2.931 1.00 104.31 ? 484 LYS A C 1 ATOM 3706 O O . LYS A 1 484 ? -20.348 61.991 2.482 1.00 98.86 ? 484 LYS A O 1 ATOM 3707 C CB . LYS A 1 484 ? -21.982 63.249 5.071 1.00 100.13 ? 484 LYS A CB 1 ATOM 3708 C CG . LYS A 1 484 ? -23.272 63.658 5.774 1.00 105.38 ? 484 LYS A CG 1 ATOM 3709 C CD . LYS A 1 484 ? -23.365 63.066 7.173 1.00 114.97 ? 484 LYS A CD 1 ATOM 3710 C CE . LYS A 1 484 ? -22.202 63.501 8.047 1.00 126.74 ? 484 LYS A CE 1 ATOM 3711 N NZ . LYS A 1 484 ? -22.286 62.904 9.410 1.00 126.15 ? 484 LYS A NZ 1 ATOM 3712 N N . GLY A 1 485 ? -19.877 64.148 2.910 1.00 99.66 ? 485 GLY A N 1 ATOM 3713 C CA . GLY A 1 485 ? -18.533 64.074 2.370 1.00 109.68 ? 485 GLY A CA 1 ATOM 3714 C C . GLY A 1 485 ? -18.492 64.191 0.858 1.00 115.23 ? 485 GLY A C 1 ATOM 3715 O O . GLY A 1 485 ? -19.330 64.862 0.255 1.00 125.84 ? 485 GLY A O 1 ATOM 3716 N N . VAL A 1 486 ? -17.512 63.533 0.246 1.00 114.33 ? 486 VAL A N 1 ATOM 3717 C CA . VAL A 1 486 ? -17.344 63.582 -1.202 1.00 122.95 ? 486 VAL A CA 1 ATOM 3718 C C . VAL A 1 486 ? -18.065 62.424 -1.883 1.00 121.74 ? 486 VAL A C 1 ATOM 3719 O O . VAL A 1 486 ? -17.780 61.256 -1.616 1.00 105.79 ? 486 VAL A O 1 ATOM 3720 C CB . VAL A 1 486 ? -15.854 63.562 -1.596 1.00 112.64 ? 486 VAL A CB 1 ATOM 3721 C CG1 . VAL A 1 486 ? -15.699 63.394 -3.100 1.00 111.27 ? 486 VAL A CG1 1 ATOM 3722 C CG2 . VAL A 1 486 ? -15.167 64.834 -1.125 1.00 107.85 ? 486 VAL A CG2 1 ATOM 3723 N N . LEU A 1 487 ? -18.984 62.773 -2.780 1.00 131.61 ? 487 LEU A N 1 ATOM 3724 C CA . LEU A 1 487 ? -19.823 61.820 -3.499 1.00 128.28 ? 487 LEU A CA 1 ATOM 3725 C C . LEU A 1 487 ? -20.673 62.617 -4.484 1.00 144.67 ? 487 LEU A C 1 ATOM 3726 O O . LEU A 1 487 ? -21.061 63.748 -4.187 1.00 157.71 ? 487 LEU A O 1 ATOM 3727 C CB . LEU A 1 487 ? -20.704 60.999 -2.545 1.00 114.50 ? 487 LEU A CB 1 ATOM 3728 C CG . LEU A 1 487 ? -21.912 61.631 -1.843 1.00 121.91 ? 487 LEU A CG 1 ATOM 3729 C CD1 . LEU A 1 487 ? -22.761 60.548 -1.192 1.00 120.48 ? 487 LEU A CD1 1 ATOM 3730 C CD2 . LEU A 1 487 ? -21.492 62.661 -0.805 1.00 120.77 ? 487 LEU A CD2 1 ATOM 3731 N N . PRO A 1 488 ? -20.959 62.039 -5.663 1.00 140.00 ? 488 PRO A N 1 ATOM 3732 C CA . PRO A 1 488 ? -21.577 62.820 -6.743 1.00 142.92 ? 488 PRO A CA 1 ATOM 3733 C C . PRO A 1 488 ? -22.980 63.329 -6.416 1.00 145.72 ? 488 PRO A C 1 ATOM 3734 O O . PRO A 1 488 ? -23.538 62.992 -5.372 1.00 147.28 ? 488 PRO A O 1 ATOM 3735 C CB . PRO A 1 488 ? -21.628 61.823 -7.906 1.00 133.50 ? 488 PRO A CB 1 ATOM 3736 C CG . PRO A 1 488 ? -21.635 60.482 -7.250 1.00 114.80 ? 488 PRO A CG 1 ATOM 3737 C CD . PRO A 1 488 ? -20.752 60.633 -6.048 1.00 114.05 ? 488 PRO A CD 1 ATOM 3738 N N . ARG A 1 489 ? -23.541 64.125 -7.320 1.00 142.46 ? 489 ARG A N 1 ATOM 3739 C CA . ARG A 1 489 ? -24.849 64.733 -7.103 1.00 147.78 ? 489 ARG A CA 1 ATOM 3740 C C . ARG A 1 489 ? -25.977 63.887 -7.686 1.00 155.93 ? 489 ARG A C 1 ATOM 3741 O O . ARG A 1 489 ? -27.153 64.159 -7.446 1.00 161.16 ? 489 ARG A O 1 ATOM 3742 C CB . ARG A 1 489 ? -24.882 66.142 -7.697 1.00 124.55 ? 489 ARG A CB 1 ATOM 3743 C CG . ARG A 1 489 ? -23.897 67.102 -7.049 1.00 141.37 ? 489 ARG A CG 1 ATOM 3744 C CD . ARG A 1 489 ? -24.002 68.510 -7.620 1.00 153.57 ? 489 ARG A CD 1 ATOM 3745 N NE . ARG A 1 489 ? -23.568 68.584 -9.013 1.00 164.87 ? 489 ARG A NE 1 ATOM 3746 C CZ . ARG A 1 489 ? -24.394 68.643 -10.053 1.00 173.29 ? 489 ARG A CZ 1 ATOM 3747 N NH1 . ARG A 1 489 ? -25.706 68.637 -9.862 1.00 164.56 ? 489 ARG A NH1 1 ATOM 3748 N NH2 . ARG A 1 489 ? -23.907 68.710 -11.284 1.00 179.00 ? 489 ARG A NH2 1 ATOM 3749 N N . LYS A 1 490 ? -25.614 62.862 -8.451 1.00 150.68 ? 490 LYS A N 1 ATOM 3750 C CA . LYS A 1 490 ? -26.602 61.951 -9.018 1.00 139.96 ? 490 LYS A CA 1 ATOM 3751 C C . LYS A 1 490 ? -26.135 60.503 -8.937 1.00 137.75 ? 490 LYS A C 1 ATOM 3752 O O . LYS A 1 490 ? -24.977 60.192 -9.218 1.00 129.24 ? 490 LYS A O 1 ATOM 3753 C CB . LYS A 1 490 ? -26.914 62.323 -10.471 1.00 126.12 ? 490 LYS A CB 1 ATOM 3754 C CG . LYS A 1 490 ? -27.799 63.552 -10.620 1.00 134.18 ? 490 LYS A CG 1 ATOM 3755 C CD . LYS A 1 490 ? -28.546 63.542 -11.945 1.00 143.41 ? 490 LYS A CD 1 ATOM 3756 C CE . LYS A 1 490 ? -27.601 63.695 -13.124 1.00 152.54 ? 490 LYS A CE 1 ATOM 3757 N NZ . LYS A 1 490 ? -26.952 65.035 -13.139 1.00 135.43 ? 490 LYS A NZ 1 ATOM 3758 N N . LEU A 1 491 ? -27.051 59.621 -8.550 1.00 133.47 ? 491 LEU A N 1 ATOM 3759 C CA . LEU A 1 491 ? -26.746 58.205 -8.388 1.00 128.49 ? 491 LEU A CA 1 ATOM 3760 C C . LEU A 1 491 ? -27.638 57.356 -9.286 1.00 140.38 ? 491 LEU A C 1 ATOM 3761 O O . LEU A 1 491 ? -28.742 57.768 -9.639 1.00 155.38 ? 491 LEU A O 1 ATOM 3762 C CB . LEU A 1 491 ? -26.918 57.787 -6.928 1.00 117.12 ? 491 LEU A CB 1 ATOM 3763 C CG . LEU A 1 491 ? -26.182 58.639 -5.891 1.00 112.59 ? 491 LEU A CG 1 ATOM 3764 C CD1 . LEU A 1 491 ? -26.636 58.287 -4.484 1.00 109.55 ? 491 LEU A CD1 1 ATOM 3765 C CD2 . LEU A 1 491 ? -24.676 58.473 -6.028 1.00 116.12 ? 491 LEU A CD2 1 ATOM 3766 N N . ASN A 1 492 ? -27.156 56.175 -9.658 1.00 132.71 ? 492 ASN A N 1 ATOM 3767 C CA . ASN A 1 492 ? -27.934 55.270 -10.496 1.00 138.13 ? 492 ASN A CA 1 ATOM 3768 C C . ASN A 1 492 ? -28.419 54.037 -9.741 1.00 137.38 ? 492 ASN A C 1 ATOM 3769 O O . ASN A 1 492 ? -27.630 53.170 -9.369 1.00 130.02 ? 492 ASN A O 1 ATOM 3770 C CB . ASN A 1 492 ? -27.118 54.839 -11.717 1.00 141.20 ? 492 ASN A CB 1 ATOM 3771 C CG . ASN A 1 492 ? -27.237 55.816 -12.870 1.00 148.19 ? 492 ASN A CG 1 ATOM 3772 O OD1 . ASN A 1 492 ? -27.615 56.973 -12.683 1.00 148.92 ? 492 ASN A OD1 1 ATOM 3773 N ND2 . ASN A 1 492 ? -26.920 55.352 -14.074 1.00 153.74 ? 492 ASN A ND2 1 ATOM 3774 N N . PHE A 1 493 ? -29.729 53.968 -9.527 1.00 146.40 ? 493 PHE A N 1 ATOM 3775 C CA . PHE A 1 493 ? -30.344 52.834 -8.850 1.00 139.70 ? 493 PHE A CA 1 ATOM 3776 C C . PHE A 1 493 ? -31.034 51.906 -9.843 1.00 145.16 ? 493 PHE A C 1 ATOM 3777 O O . PHE A 1 493 ? -31.589 52.357 -10.845 1.00 154.21 ? 493 PHE A O 1 ATOM 3778 C CB . PHE A 1 493 ? -31.355 53.312 -7.806 1.00 127.78 ? 493 PHE A CB 1 ATOM 3779 C CG . PHE A 1 493 ? -30.732 53.808 -6.533 1.00 119.83 ? 493 PHE A CG 1 ATOM 3780 C CD1 . PHE A 1 493 ? -30.265 55.108 -6.431 1.00 129.47 ? 493 PHE A CD1 1 ATOM 3781 C CD2 . PHE A 1 493 ? -30.629 52.977 -5.430 1.00 117.10 ? 493 PHE A CD2 1 ATOM 3782 C CE1 . PHE A 1 493 ? -29.697 55.567 -5.256 1.00 128.99 ? 493 PHE A CE1 1 ATOM 3783 C CE2 . PHE A 1 493 ? -30.062 53.428 -4.253 1.00 114.01 ? 493 PHE A CE2 1 ATOM 3784 C CZ . PHE A 1 493 ? -29.596 54.726 -4.166 1.00 112.87 ? 493 PHE A CZ 1 ATOM 3785 N N . GLN A 1 494 ? -30.991 50.608 -9.562 1.00 132.39 ? 494 GLN A N 1 ATOM 3786 C CA . GLN A 1 494 ? -31.716 49.633 -10.366 1.00 136.70 ? 494 GLN A CA 1 ATOM 3787 C C . GLN A 1 494 ? -32.828 49.005 -9.535 1.00 130.35 ? 494 GLN A C 1 ATOM 3788 O O . GLN A 1 494 ? -32.566 48.237 -8.609 1.00 122.55 ? 494 GLN A O 1 ATOM 3789 C CB . GLN A 1 494 ? -30.768 48.557 -10.897 1.00 143.17 ? 494 GLN A CB 1 ATOM 3790 C CG . GLN A 1 494 ? -29.520 49.111 -11.560 1.00 160.43 ? 494 GLN A CG 1 ATOM 3791 C CD . GLN A 1 494 ? -29.829 49.974 -12.767 1.00 173.43 ? 494 GLN A CD 1 ATOM 3792 O OE1 . GLN A 1 494 ? -30.825 49.762 -13.457 1.00 169.87 ? 494 GLN A OE1 1 ATOM 3793 N NE2 . GLN A 1 494 ? -28.975 50.958 -13.025 1.00 175.39 ? 494 GLN A NE2 1 ATOM 3794 N N . VAL A 1 495 ? -34.070 49.332 -9.875 1.00 134.56 ? 495 VAL A N 1 ATOM 3795 C CA . VAL A 1 495 ? -35.220 48.904 -9.087 1.00 134.66 ? 495 VAL A CA 1 ATOM 3796 C C . VAL A 1 495 ? -35.894 47.674 -9.690 1.00 136.29 ? 495 VAL A C 1 ATOM 3797 O O . VAL A 1 495 ? -36.054 47.575 -10.907 1.00 141.90 ? 495 VAL A O 1 ATOM 3798 C CB . VAL A 1 495 ? -36.256 50.040 -8.957 1.00 127.47 ? 495 VAL A CB 1 ATOM 3799 C CG1 . VAL A 1 495 ? -37.354 49.657 -7.976 1.00 128.33 ? 495 VAL A CG1 1 ATOM 3800 C CG2 . VAL A 1 495 ? -35.575 51.323 -8.514 1.00 122.42 ? 495 VAL A CG2 1 ATOM 3801 N N . GLU A 1 496 ? -36.284 46.739 -8.830 1.00 133.48 ? 496 GLU A N 1 ATOM 3802 C CA . GLU A 1 496 ? -36.962 45.524 -9.265 1.00 129.08 ? 496 GLU A CA 1 ATOM 3803 C C . GLU A 1 496 ? -38.333 45.400 -8.605 1.00 125.62 ? 496 GLU A C 1 ATOM 3804 O O . GLU A 1 496 ? -38.456 45.519 -7.386 1.00 119.92 ? 496 GLU A O 1 ATOM 3805 C CB . GLU A 1 496 ? -36.110 44.294 -8.949 1.00 129.01 ? 496 GLU A CB 1 ATOM 3806 C CG . GLU A 1 496 ? -36.650 42.997 -9.527 1.00 138.50 ? 496 GLU A CG 1 ATOM 3807 C CD . GLU A 1 496 ? -36.543 42.943 -11.039 1.00 157.52 ? 496 GLU A CD 1 ATOM 3808 O OE1 . GLU A 1 496 ? -37.300 42.171 -11.665 1.00 156.90 ? 496 GLU A OE1 1 ATOM 3809 O OE2 . GLU A 1 496 ? -35.696 43.669 -11.604 1.00 159.53 ? 496 GLU A OE2 1 ATOM 3810 N N . LEU A 1 497 ? -39.361 45.162 -9.414 1.00 130.43 ? 497 LEU A N 1 ATOM 3811 C CA . LEU A 1 497 ? -40.723 45.045 -8.901 1.00 118.24 ? 497 LEU A CA 1 ATOM 3812 C C . LEU A 1 497 ? -41.274 43.631 -9.068 1.00 117.98 ? 497 LEU A C 1 ATOM 3813 O O . LEU A 1 497 ? -41.232 43.059 -10.157 1.00 117.62 ? 497 LEU A O 1 ATOM 3814 C CB . LEU A 1 497 ? -41.644 46.051 -9.597 1.00 119.30 ? 497 LEU A CB 1 ATOM 3815 C CG . LEU A 1 497 ? -41.424 47.530 -9.265 1.00 120.07 ? 497 LEU A CG 1 ATOM 3816 C CD1 . LEU A 1 497 ? -42.416 48.404 -10.020 1.00 121.04 ? 497 LEU A CD1 1 ATOM 3817 C CD2 . LEU A 1 497 ? -41.534 47.767 -7.767 1.00 119.07 ? 497 LEU A CD2 1 ATOM 3818 N N . LEU A 1 498 ? -41.787 43.075 -7.975 1.00 128.95 ? 498 LEU A N 1 ATOM 3819 C CA . LEU A 1 498 ? -42.380 41.742 -7.987 1.00 125.57 ? 498 LEU A CA 1 ATOM 3820 C C . LEU A 1 498 ? -43.822 41.790 -7.493 1.00 114.35 ? 498 LEU A C 1 ATOM 3821 O O . LEU A 1 498 ? -44.101 42.304 -6.410 1.00 113.05 ? 498 LEU A O 1 ATOM 3822 C CB . LEU A 1 498 ? -41.559 40.776 -7.129 1.00 134.45 ? 498 LEU A CB 1 ATOM 3823 C CG . LEU A 1 498 ? -40.502 39.915 -7.830 1.00 139.75 ? 498 LEU A CG 1 ATOM 3824 C CD1 . LEU A 1 498 ? -41.153 38.996 -8.854 1.00 144.34 ? 498 LEU A CD1 1 ATOM 3825 C CD2 . LEU A 1 498 ? -39.419 40.765 -8.479 1.00 123.95 ? 498 LEU A CD2 1 ATOM 3826 N N . LEU A 1 499 ? -44.736 41.253 -8.294 1.00 114.69 ? 499 LEU A N 1 ATOM 3827 C CA . LEU A 1 499 ? -46.151 41.252 -7.943 1.00 121.53 ? 499 LEU A CA 1 ATOM 3828 C C . LEU A 1 499 ? -46.566 39.953 -7.261 1.00 133.54 ? 499 LEU A C 1 ATOM 3829 O O . LEU A 1 499 ? -46.244 38.862 -7.734 1.00 111.86 ? 499 LEU A O 1 ATOM 3830 C CB . LEU A 1 499 ? -47.009 41.487 -9.189 1.00 114.52 ? 499 LEU A CB 1 ATOM 3831 C CG . LEU A 1 499 ? -46.949 42.890 -9.797 1.00 116.47 ? 499 LEU A CG 1 ATOM 3832 C CD1 . LEU A 1 499 ? -47.817 42.967 -11.041 1.00 122.33 ? 499 LEU A CD1 1 ATOM 3833 C CD2 . LEU A 1 499 ? -47.377 43.931 -8.774 1.00 116.46 ? 499 LEU A CD2 1 ATOM 3834 N N . ASP A 1 500 ? -47.284 40.092 -6.148 1.00 139.02 ? 500 ASP A N 1 ATOM 3835 C CA . ASP A 1 500 ? -47.790 38.958 -5.379 1.00 128.28 ? 500 ASP A CA 1 ATOM 3836 C C . ASP A 1 500 ? -46.663 38.011 -4.980 1.00 113.39 ? 500 ASP A C 1 ATOM 3837 O O . ASP A 1 500 ? -46.576 36.888 -5.475 1.00 113.08 ? 500 ASP A O 1 ATOM 3838 C CB . ASP A 1 500 ? -48.862 38.206 -6.173 1.00 121.64 ? 500 ASP A CB 1 ATOM 3839 C CG . ASP A 1 500 ? -49.703 37.301 -5.298 1.00 123.29 ? 500 ASP A CG 1 ATOM 3840 O OD1 . ASP A 1 500 ? -50.331 36.365 -5.835 1.00 111.87 ? 500 ASP A OD1 1 ATOM 3841 O OD2 . ASP A 1 500 ? -49.731 37.525 -4.071 1.00 130.97 ? 500 ASP A OD2 1 ATOM 3842 N N . LYS A 1 501 ? -45.798 38.473 -4.083 1.00 114.47 ? 501 LYS A N 1 ATOM 3843 C CA . LYS A 1 501 ? -44.631 37.697 -3.681 1.00 123.11 ? 501 LYS A CA 1 ATOM 3844 C C . LYS A 1 501 ? -45.000 36.537 -2.762 1.00 127.23 ? 501 LYS A C 1 ATOM 3845 O O . LYS A 1 501 ? -44.253 35.562 -2.664 1.00 127.93 ? 501 LYS A O 1 ATOM 3846 C CB . LYS A 1 501 ? -43.600 38.596 -2.992 1.00 122.83 ? 501 LYS A CB 1 ATOM 3847 C CG . LYS A 1 501 ? -42.228 37.952 -2.835 1.00 113.68 ? 501 LYS A CG 1 ATOM 3848 C CD . LYS A 1 501 ? -41.263 38.855 -2.088 1.00 113.63 ? 501 LYS A CD 1 ATOM 3849 C CE . LYS A 1 501 ? -41.579 38.900 -0.602 1.00 119.52 ? 501 LYS A CE 1 ATOM 3850 N NZ . LYS A 1 501 ? -41.377 37.574 0.045 1.00 120.47 ? 501 LYS A NZ 1 ATOM 3851 N N . LEU A 1 502 ? -46.146 36.640 -2.090 1.00 128.60 ? 502 LEU A N 1 ATOM 3852 C CA . LEU A 1 502 ? -46.561 35.597 -1.155 1.00 124.52 ? 502 LEU A CA 1 ATOM 3853 C C . LEU A 1 502 ? -46.687 34.259 -1.866 1.00 134.89 ? 502 LEU A C 1 ATOM 3854 O O . LEU A 1 502 ? -45.989 33.305 -1.522 1.00 155.72 ? 502 LEU A O 1 ATOM 3855 C CB . LEU A 1 502 ? -47.881 35.963 -0.476 1.00 117.75 ? 502 LEU A CB 1 ATOM 3856 C CG . LEU A 1 502 ? -47.744 36.725 0.843 1.00 118.25 ? 502 LEU A CG 1 ATOM 3857 C CD1 . LEU A 1 502 ? -49.099 36.890 1.512 1.00 127.41 ? 502 LEU A CD1 1 ATOM 3858 C CD2 . LEU A 1 502 ? -46.765 36.016 1.768 1.00 100.61 ? 502 LEU A CD2 1 ATOM 3859 N N . LYS A 1 503 ? -47.569 34.176 -2.856 1.00 130.70 ? 503 LYS A N 1 ATOM 3860 C CA . LYS A 1 503 ? -47.478 33.066 -3.786 1.00 136.80 ? 503 LYS A CA 1 ATOM 3861 C C . LYS A 1 503 ? -47.202 33.578 -5.196 1.00 148.27 ? 503 LYS A C 1 ATOM 3862 O O . LYS A 1 503 ? -48.120 33.973 -5.919 1.00 147.18 ? 503 LYS A O 1 ATOM 3863 C CB . LYS A 1 503 ? -48.779 32.254 -3.738 1.00 148.09 ? 503 LYS A CB 1 ATOM 3864 C CG . LYS A 1 503 ? -48.986 31.258 -4.864 1.00 157.32 ? 503 LYS A CG 1 ATOM 3865 C CD . LYS A 1 503 ? -50.427 30.748 -4.897 1.00 160.73 ? 503 LYS A CD 1 ATOM 3866 C CE . LYS A 1 503 ? -51.438 31.878 -5.086 1.00 152.37 ? 503 LYS A CE 1 ATOM 3867 N NZ . LYS A 1 503 ? -51.971 32.416 -3.799 1.00 136.52 ? 503 LYS A NZ 1 ATOM 3868 N N . GLN A 1 504 ? -45.927 33.607 -5.572 1.00 151.36 ? 504 GLN A N 1 ATOM 3869 C CA . GLN A 1 504 ? -45.504 33.505 -6.961 1.00 156.62 ? 504 GLN A CA 1 ATOM 3870 C C . GLN A 1 504 ? -44.793 32.175 -7.195 1.00 153.47 ? 504 GLN A C 1 ATOM 3871 O O . GLN A 1 504 ? -44.421 31.842 -8.320 1.00 163.78 ? 504 GLN A O 1 ATOM 3872 C CB . GLN A 1 504 ? -44.609 34.685 -7.343 1.00 156.04 ? 504 GLN A CB 1 ATOM 3873 C CG . GLN A 1 504 ? -43.671 35.151 -6.249 1.00 155.54 ? 504 GLN A CG 1 ATOM 3874 C CD . GLN A 1 504 ? -43.010 36.473 -6.585 1.00 176.13 ? 504 GLN A CD 1 ATOM 3875 O OE1 . GLN A 1 504 ? -43.488 37.218 -7.440 1.00 188.89 ? 504 GLN A OE1 1 ATOM 3876 N NE2 . GLN A 1 504 ? -41.904 36.770 -5.913 1.00 175.23 ? 504 GLN A NE2 1 ATOM 3877 N N . LYS A 1 505 ? -44.608 31.422 -6.115 1.00 133.44 ? 505 LYS A N 1 ATOM 3878 C CA . LYS A 1 505 ? -43.643 30.325 -6.096 1.00 127.41 ? 505 LYS A CA 1 ATOM 3879 C C . LYS A 1 505 ? -44.278 28.962 -6.335 1.00 137.85 ? 505 LYS A C 1 ATOM 3880 O O . LYS A 1 505 ? -45.067 28.482 -5.522 1.00 146.37 ? 505 LYS A O 1 ATOM 3881 C CB . LYS A 1 505 ? -42.894 30.309 -4.760 1.00 123.11 ? 505 LYS A CB 1 ATOM 3882 C CG . LYS A 1 505 ? -42.310 31.654 -4.350 1.00 135.36 ? 505 LYS A CG 1 ATOM 3883 C CD . LYS A 1 505 ? -41.428 32.237 -5.443 1.00 144.29 ? 505 LYS A CD 1 ATOM 3884 C CE . LYS A 1 505 ? -40.770 33.530 -4.990 1.00 139.09 ? 505 LYS A CE 1 ATOM 3885 N NZ . LYS A 1 505 ? -40.104 34.239 -6.118 1.00 144.12 ? 505 LYS A NZ 1 ATOM 3886 N N . GLY A 1 506 ? -43.914 28.341 -7.452 1.00 130.36 ? 506 GLY A N 1 ATOM 3887 C CA . GLY A 1 506 ? -44.422 27.029 -7.808 1.00 128.00 ? 506 GLY A CA 1 ATOM 3888 C C . GLY A 1 506 ? -45.930 27.001 -7.946 1.00 136.85 ? 506 GLY A C 1 ATOM 3889 O O . GLY A 1 506 ? -46.557 25.951 -7.799 1.00 149.70 ? 506 GLY A O 1 ATOM 3890 N N . ALA A 1 507 ? -46.515 28.161 -8.230 1.00 141.75 ? 507 ALA A N 1 ATOM 3891 C CA . ALA A 1 507 ? -47.963 28.283 -8.334 1.00 155.55 ? 507 ALA A CA 1 ATOM 3892 C C . ALA A 1 507 ? -48.365 29.471 -9.204 1.00 149.70 ? 507 ALA A C 1 ATOM 3893 O O . ALA A 1 507 ? -47.526 30.083 -9.866 1.00 146.75 ? 507 ALA A O 1 ATOM 3894 C CB . ALA A 1 507 ? -48.580 28.404 -6.953 1.00 151.01 ? 507 ALA A CB 1 ATOM 3895 N N . ILE A 1 508 ? -49.654 29.790 -9.195 1.00 135.65 ? 508 ILE A N 1 ATOM 3896 C CA . ILE A 1 508 ? -50.207 30.810 -10.078 1.00 127.69 ? 508 ILE A CA 1 ATOM 3897 C C . ILE A 1 508 ? -50.021 32.233 -9.541 1.00 132.28 ? 508 ILE A C 1 ATOM 3898 O O . ILE A 1 508 ? -50.314 32.517 -8.378 1.00 135.11 ? 508 ILE A O 1 ATOM 3899 C CB . ILE A 1 508 ? -51.713 30.550 -10.338 1.00 145.14 ? 508 ILE A CB 1 ATOM 3900 C CG1 . ILE A 1 508 ? -52.338 31.698 -11.137 1.00 130.00 ? 508 ILE A CG1 1 ATOM 3901 C CG2 . ILE A 1 508 ? -52.459 30.321 -9.028 1.00 148.77 ? 508 ILE A CG2 1 ATOM 3902 C CD1 . ILE A 1 508 ? -51.791 31.833 -12.543 1.00 119.75 ? 508 ILE A CD1 1 ATOM 3903 N N . ARG A 1 509 ? -49.514 33.117 -10.398 1.00 135.70 ? 509 ARG A N 1 ATOM 3904 C CA . ARG A 1 509 ? -49.422 34.538 -10.081 1.00 126.64 ? 509 ARG A CA 1 ATOM 3905 C C . ARG A 1 509 ? -50.689 35.250 -10.544 1.00 122.93 ? 509 ARG A C 1 ATOM 3906 O O . ARG A 1 509 ? -51.092 35.134 -11.703 1.00 136.38 ? 509 ARG A O 1 ATOM 3907 C CB . ARG A 1 509 ? -48.188 35.167 -10.732 1.00 132.50 ? 509 ARG A CB 1 ATOM 3908 C CG . ARG A 1 509 ? -46.872 34.486 -10.378 1.00 143.28 ? 509 ARG A CG 1 ATOM 3909 C CD . ARG A 1 509 ? -45.680 35.305 -10.866 1.00 140.55 ? 509 ARG A CD 1 ATOM 3910 N NE . ARG A 1 509 ? -44.402 34.671 -10.556 1.00 133.18 ? 509 ARG A NE 1 ATOM 3911 C CZ . ARG A 1 509 ? -43.240 35.314 -10.505 1.00 154.35 ? 509 ARG A CZ 1 ATOM 3912 N NH1 . ARG A 1 509 ? -43.189 36.619 -10.737 1.00 164.23 ? 509 ARG A NH1 1 ATOM 3913 N NH2 . ARG A 1 509 ? -42.126 34.657 -10.214 1.00 162.87 ? 509 ARG A NH2 1 ATOM 3914 N N . ARG A 1 510 ? -51.312 35.986 -9.630 1.00 113.22 ? 510 ARG A N 1 ATOM 3915 C CA . ARG A 1 510 ? -52.640 36.543 -9.872 1.00 112.06 ? 510 ARG A CA 1 ATOM 3916 C C . ARG A 1 510 ? -52.635 37.994 -10.368 1.00 113.24 ? 510 ARG A C 1 ATOM 3917 O O . ARG A 1 510 ? -53.695 38.577 -10.605 1.00 113.73 ? 510 ARG A O 1 ATOM 3918 C CB . ARG A 1 510 ? -53.482 36.430 -8.594 1.00 110.28 ? 510 ARG A CB 1 ATOM 3919 C CG . ARG A 1 510 ? -53.583 34.998 -8.058 1.00 117.52 ? 510 ARG A CG 1 ATOM 3920 C CD . ARG A 1 510 ? -53.098 34.913 -6.613 1.00 113.41 ? 510 ARG A CD 1 ATOM 3921 N NE . ARG A 1 510 ? -54.074 35.462 -5.684 1.00 108.79 ? 510 ARG A NE 1 ATOM 3922 C CZ . ARG A 1 510 ? -53.790 35.888 -4.452 1.00 106.19 ? 510 ARG A CZ 1 ATOM 3923 N NH1 . ARG A 1 510 ? -52.536 35.850 -4.013 1.00 108.82 ? 510 ARG A NH1 1 ATOM 3924 N NH2 . ARG A 1 510 ? -54.752 36.357 -3.644 1.00 105.67 ? 510 ARG A NH2 1 ATOM 3925 N N . ALA A 1 511 ? -51.450 38.577 -10.530 1.00 118.54 ? 511 ALA A N 1 ATOM 3926 C CA . ALA A 1 511 ? -51.357 39.963 -10.980 1.00 115.58 ? 511 ALA A CA 1 ATOM 3927 C C . ALA A 1 511 ? -50.207 40.191 -11.958 1.00 117.14 ? 511 ALA A C 1 ATOM 3928 O O . ALA A 1 511 ? -49.100 39.694 -11.759 1.00 120.19 ? 511 ALA A O 1 ATOM 3929 C CB . ALA A 1 511 ? -51.216 40.892 -9.784 1.00 114.83 ? 511 ALA A CB 1 ATOM 3930 N N . LEU A 1 512 ? -50.481 40.960 -13.009 1.00 120.01 ? 512 LEU A N 1 ATOM 3931 C CA . LEU A 1 512 ? -49.481 41.288 -14.020 1.00 137.68 ? 512 LEU A CA 1 ATOM 3932 C C . LEU A 1 512 ? -49.496 42.783 -14.317 1.00 138.82 ? 512 LEU A C 1 ATOM 3933 O O . LEU A 1 512 ? -50.491 43.461 -14.061 1.00 149.18 ? 512 LEU A O 1 ATOM 3934 C CB . LEU A 1 512 ? -49.735 40.503 -15.309 1.00 150.75 ? 512 LEU A CB 1 ATOM 3935 C CG . LEU A 1 512 ? -49.956 38.993 -15.204 1.00 144.59 ? 512 LEU A CG 1 ATOM 3936 C CD1 . LEU A 1 512 ? -50.325 38.418 -16.563 1.00 142.74 ? 512 LEU A CD1 1 ATOM 3937 C CD2 . LEU A 1 512 ? -48.724 38.301 -14.648 1.00 136.23 ? 512 LEU A CD2 1 ATOM 3938 N N . PHE A 1 513 ? -48.395 43.293 -14.859 1.00 131.19 ? 513 PHE A N 1 ATOM 3939 C CA . PHE A 1 513 ? -48.333 44.688 -15.285 1.00 136.39 ? 513 PHE A CA 1 ATOM 3940 C C . PHE A 1 513 ? -49.033 44.857 -16.630 1.00 137.27 ? 513 PHE A C 1 ATOM 3941 O O . PHE A 1 513 ? -48.966 43.975 -17.483 1.00 143.15 ? 513 PHE A O 1 ATOM 3942 C CB . PHE A 1 513 ? -46.882 45.169 -15.365 1.00 141.27 ? 513 PHE A CB 1 ATOM 3943 C CG . PHE A 1 513 ? -46.210 45.296 -14.025 1.00 130.49 ? 513 PHE A CG 1 ATOM 3944 C CD1 . PHE A 1 513 ? -45.230 44.397 -13.636 1.00 127.96 ? 513 PHE A CD1 1 ATOM 3945 C CD2 . PHE A 1 513 ? -46.561 46.313 -13.154 1.00 122.85 ? 513 PHE A CD2 1 ATOM 3946 C CE1 . PHE A 1 513 ? -44.611 44.514 -12.403 1.00 120.99 ? 513 PHE A CE1 1 ATOM 3947 C CE2 . PHE A 1 513 ? -45.947 46.434 -11.921 1.00 121.71 ? 513 PHE A CE2 1 ATOM 3948 C CZ . PHE A 1 513 ? -44.971 45.533 -11.545 1.00 120.86 ? 513 PHE A CZ 1 ATOM 3949 N N . LEU A 1 514 ? -49.710 45.988 -16.807 1.00 129.54 ? 514 LEU A N 1 ATOM 3950 C CA . LEU A 1 514 ? -50.526 46.230 -17.996 1.00 129.56 ? 514 LEU A CA 1 ATOM 3951 C C . LEU A 1 514 ? -49.743 46.144 -19.306 1.00 131.49 ? 514 LEU A C 1 ATOM 3952 O O . LEU A 1 514 ? -49.943 45.221 -20.096 1.00 130.74 ? 514 LEU A O 1 ATOM 3953 C CB . LEU A 1 514 ? -51.206 47.599 -17.896 1.00 131.95 ? 514 LEU A CB 1 ATOM 3954 C CG . LEU A 1 514 ? -52.249 47.920 -18.970 1.00 148.93 ? 514 LEU A CG 1 ATOM 3955 C CD1 . LEU A 1 514 ? -53.528 48.437 -18.330 1.00 143.52 ? 514 LEU A CD1 1 ATOM 3956 C CD2 . LEU A 1 514 ? -51.709 48.925 -19.976 1.00 160.69 ? 514 LEU A CD2 1 ATOM 3957 N N . TYR A 1 515 ? -48.856 47.108 -19.532 1.00 147.36 ? 515 TYR A N 1 ATOM 3958 C CA . TYR A 1 515 ? -48.128 47.195 -20.795 1.00 149.88 ? 515 TYR A CA 1 ATOM 3959 C C . TYR A 1 515 ? -47.166 46.029 -20.994 1.00 145.10 ? 515 TYR A C 1 ATOM 3960 O O . TYR A 1 515 ? -47.016 45.520 -22.105 1.00 136.85 ? 515 TYR A O 1 ATOM 3961 C CB . TYR A 1 515 ? -47.358 48.516 -20.879 1.00 155.53 ? 515 TYR A CB 1 ATOM 3962 C CG . TYR A 1 515 ? -48.238 49.739 -21.000 1.00 156.66 ? 515 TYR A CG 1 ATOM 3963 C CD1 . TYR A 1 515 ? -48.511 50.535 -19.895 1.00 154.60 ? 515 TYR A CD1 1 ATOM 3964 C CD2 . TYR A 1 515 ? -48.794 50.101 -22.221 1.00 161.89 ? 515 TYR A CD2 1 ATOM 3965 C CE1 . TYR A 1 515 ? -49.313 51.656 -20.002 1.00 158.83 ? 515 TYR A CE1 1 ATOM 3966 C CE2 . TYR A 1 515 ? -49.597 51.220 -22.338 1.00 165.36 ? 515 TYR A CE2 1 ATOM 3967 C CZ . TYR A 1 515 ? -49.854 51.994 -21.225 1.00 164.72 ? 515 TYR A CZ 1 ATOM 3968 O OH . TYR A 1 515 ? -50.652 53.108 -21.336 1.00 166.24 ? 515 TYR A OH 1 ATOM 3969 N N . SER A 1 516 ? -46.516 45.609 -19.915 1.00 147.64 ? 516 SER A N 1 ATOM 3970 C CA . SER A 1 516 ? -45.509 44.558 -19.991 1.00 151.88 ? 516 SER A CA 1 ATOM 3971 C C . SER A 1 516 ? -46.127 43.166 -20.092 1.00 143.73 ? 516 SER A C 1 ATOM 3972 O O . SER A 1 516 ? -45.499 42.242 -20.612 1.00 133.98 ? 516 SER A O 1 ATOM 3973 C CB . SER A 1 516 ? -44.579 44.628 -18.777 1.00 156.29 ? 516 SER A CB 1 ATOM 3974 O OG . SER A 1 516 ? -43.933 45.887 -18.701 1.00 159.86 ? 516 SER A OG 1 ATOM 3975 N N . ARG A 1 517 ? -47.354 43.028 -19.593 1.00 148.47 ? 517 ARG A N 1 ATOM 3976 C CA . ARG A 1 517 ? -48.048 41.740 -19.531 1.00 148.70 ? 517 ARG A CA 1 ATOM 3977 C C . ARG A 1 517 ? -47.190 40.707 -18.801 1.00 140.40 ? 517 ARG A C 1 ATOM 3978 O O . ARG A 1 517 ? -47.160 39.531 -19.167 1.00 136.62 ? 517 ARG A O 1 ATOM 3979 C CB . ARG A 1 517 ? -48.412 41.246 -20.935 1.00 146.25 ? 517 ARG A CB 1 ATOM 3980 C CG . ARG A 1 517 ? -49.590 40.282 -20.971 1.00 137.76 ? 517 ARG A CG 1 ATOM 3981 C CD . ARG A 1 517 ? -49.785 39.692 -22.357 1.00 142.65 ? 517 ARG A CD 1 ATOM 3982 N NE . ARG A 1 517 ? -50.019 40.722 -23.366 1.00 150.30 ? 517 ARG A NE 1 ATOM 3983 C CZ . ARG A 1 517 ? -51.221 41.186 -23.694 1.00 148.60 ? 517 ARG A CZ 1 ATOM 3984 N NH1 . ARG A 1 517 ? -52.304 40.712 -23.092 1.00 138.70 ? 517 ARG A NH1 1 ATOM 3985 N NH2 . ARG A 1 517 ? -51.340 42.123 -24.623 1.00 154.63 ? 517 ARG A NH2 1 ATOM 3986 N N . SER A 1 518 ? -46.491 41.161 -17.766 1.00 142.99 ? 518 SER A N 1 ATOM 3987 C CA . SER A 1 518 ? -45.574 40.311 -17.018 1.00 145.70 ? 518 SER A CA 1 ATOM 3988 C C . SER A 1 518 ? -45.647 40.615 -15.525 1.00 133.97 ? 518 SER A C 1 ATOM 3989 O O . SER A 1 518 ? -45.927 41.747 -15.134 1.00 143.91 ? 518 SER A O 1 ATOM 3990 C CB . SER A 1 518 ? -44.142 40.496 -17.528 1.00 150.11 ? 518 SER A CB 1 ATOM 3991 O OG . SER A 1 518 ? -43.711 41.835 -17.364 1.00 151.05 ? 518 SER A OG 1 ATOM 3992 N N . PRO A 1 519 ? -45.402 39.600 -14.684 1.00 121.67 ? 519 PRO A N 1 ATOM 3993 C CA . PRO A 1 519 ? -45.424 39.781 -13.228 1.00 123.32 ? 519 PRO A CA 1 ATOM 3994 C C . PRO A 1 519 ? -44.265 40.631 -12.710 1.00 148.93 ? 519 PRO A C 1 ATOM 3995 O O . PRO A 1 519 ? -44.331 41.129 -11.586 1.00 154.43 ? 519 PRO A O 1 ATOM 3996 C CB . PRO A 1 519 ? -45.324 38.349 -12.699 1.00 117.07 ? 519 PRO A CB 1 ATOM 3997 C CG . PRO A 1 519 ? -44.613 37.606 -13.776 1.00 117.70 ? 519 PRO A CG 1 ATOM 3998 C CD . PRO A 1 519 ? -45.109 38.205 -15.059 1.00 120.61 ? 519 PRO A CD 1 ATOM 3999 N N . SER A 1 520 ? -43.220 40.791 -13.516 1.00 151.11 ? 520 SER A N 1 ATOM 4000 C CA . SER A 1 520 ? -42.035 41.529 -13.089 1.00 136.02 ? 520 SER A CA 1 ATOM 4001 C C . SER A 1 520 ? -41.661 42.643 -14.063 1.00 129.15 ? 520 SER A C 1 ATOM 4002 O O . SER A 1 520 ? -41.892 42.534 -15.267 1.00 133.14 ? 520 SER A O 1 ATOM 4003 C CB . SER A 1 520 ? -40.853 40.575 -12.919 1.00 128.71 ? 520 SER A CB 1 ATOM 4004 O OG . SER A 1 520 ? -41.175 39.521 -12.029 1.00 118.18 ? 520 SER A OG 1 ATOM 4005 N N . HIS A 1 521 ? -41.073 43.711 -13.531 1.00 124.80 ? 521 HIS A N 1 ATOM 4006 C CA . HIS A 1 521 ? -40.634 44.839 -14.345 1.00 136.88 ? 521 HIS A CA 1 ATOM 4007 C C . HIS A 1 521 ? -39.345 45.435 -13.788 1.00 145.25 ? 521 HIS A C 1 ATOM 4008 O O . HIS A 1 521 ? -39.151 45.489 -12.573 1.00 143.73 ? 521 HIS A O 1 ATOM 4009 C CB . HIS A 1 521 ? -41.723 45.911 -14.415 1.00 143.33 ? 521 HIS A CB 1 ATOM 4010 C CG . HIS A 1 521 ? -41.366 47.080 -15.280 1.00 141.90 ? 521 HIS A CG 1 ATOM 4011 N ND1 . HIS A 1 521 ? -40.736 48.204 -14.790 1.00 128.63 ? 521 HIS A ND1 1 ATOM 4012 C CD2 . HIS A 1 521 ? -41.554 47.301 -16.603 1.00 146.80 ? 521 HIS A CD2 1 ATOM 4013 C CE1 . HIS A 1 521 ? -40.550 49.066 -15.775 1.00 131.58 ? 521 HIS A CE1 1 ATOM 4014 N NE2 . HIS A 1 521 ? -41.037 48.542 -16.885 1.00 148.52 ? 521 HIS A NE2 1 ATOM 4015 N N . SER A 1 522 ? -38.466 45.881 -14.680 1.00 149.13 ? 522 SER A N 1 ATOM 4016 C CA . SER A 1 522 ? -37.195 46.471 -14.276 1.00 138.51 ? 522 SER A CA 1 ATOM 4017 C C . SER A 1 522 ? -37.062 47.902 -14.785 1.00 143.93 ? 522 SER A C 1 ATOM 4018 O O . SER A 1 522 ? -37.547 48.233 -15.866 1.00 171.22 ? 522 SER A O 1 ATOM 4019 C CB . SER A 1 522 ? -36.026 45.624 -14.784 1.00 136.02 ? 522 SER A CB 1 ATOM 4020 O OG . SER A 1 522 ? -36.074 44.313 -14.248 1.00 134.82 ? 522 SER A OG 1 ATOM 4021 N N . LYS A 1 523 ? -36.404 48.748 -13.998 1.00 134.76 ? 523 LYS A N 1 ATOM 4022 C CA . LYS A 1 523 ? -36.222 50.145 -14.373 1.00 145.94 ? 523 LYS A CA 1 ATOM 4023 C C . LYS A 1 523 ? -34.852 50.668 -13.949 1.00 147.80 ? 523 LYS A C 1 ATOM 4024 O O . LYS A 1 523 ? -34.403 50.425 -12.828 1.00 127.21 ? 523 LYS A O 1 ATOM 4025 C CB . LYS A 1 523 ? -37.328 51.008 -13.755 1.00 140.21 ? 523 LYS A CB 1 ATOM 4026 C CG . LYS A 1 523 ? -37.925 52.048 -14.696 1.00 140.80 ? 523 LYS A CG 1 ATOM 4027 C CD . LYS A 1 523 ? -36.934 53.151 -15.034 1.00 143.46 ? 523 LYS A CD 1 ATOM 4028 C CE . LYS A 1 523 ? -37.551 54.182 -15.966 1.00 157.12 ? 523 LYS A CE 1 ATOM 4029 N NZ . LYS A 1 523 ? -37.994 53.577 -17.252 1.00 166.84 ? 523 LYS A NZ 1 ATOM 4030 N N . ASN A 1 524 ? -34.196 51.388 -14.854 1.00 159.92 ? 524 ASN A N 1 ATOM 4031 C CA . ASN A 1 524 ? -32.960 52.085 -14.531 1.00 156.19 ? 524 ASN A CA 1 ATOM 4032 C C . ASN A 1 524 ? -33.271 53.518 -14.118 1.00 147.25 ? 524 ASN A C 1 ATOM 4033 O O . ASN A 1 524 ? -33.702 54.323 -14.943 1.00 153.41 ? 524 ASN A O 1 ATOM 4034 C CB . ASN A 1 524 ? -32.003 52.086 -15.727 1.00 175.39 ? 524 ASN A CB 1 ATOM 4035 C CG . ASN A 1 524 ? -31.646 50.688 -16.200 1.00 194.29 ? 524 ASN A CG 1 ATOM 4036 O OD1 . ASN A 1 524 ? -32.311 49.710 -15.858 1.00 186.41 ? 524 ASN A OD1 1 ATOM 4037 N ND2 . ASN A 1 524 ? -30.587 50.593 -17.000 1.00 240.10 ? 524 ASN A ND2 1 ATOM 4038 N N . MET A 1 525 ? -33.057 53.843 -12.847 1.00 132.09 ? 525 MET A N 1 ATOM 4039 C CA . MET A 1 525 ? -33.381 55.183 -12.368 1.00 143.38 ? 525 MET A CA 1 ATOM 4040 C C . MET A 1 525 ? -32.152 56.063 -12.177 1.00 158.72 ? 525 MET A C 1 ATOM 4041 O O . MET A 1 525 ? -31.015 55.612 -12.312 1.00 158.12 ? 525 MET A O 1 ATOM 4042 C CB . MET A 1 525 ? -34.153 55.104 -11.048 1.00 126.43 ? 525 MET A CB 1 ATOM 4043 C CG . MET A 1 525 ? -35.551 54.522 -11.164 1.00 131.29 ? 525 MET A CG 1 ATOM 4044 S SD . MET A 1 525 ? -36.476 54.656 -9.622 1.00 157.44 ? 525 MET A SD 1 ATOM 4045 C CE . MET A 1 525 ? -36.516 56.433 -9.397 1.00 125.88 ? 525 MET A CE 1 ATOM 4046 N N . THR A 1 526 ? -32.405 57.327 -11.854 1.00 156.00 ? 526 THR A N 1 ATOM 4047 C CA . THR A 1 526 ? -31.365 58.267 -11.459 1.00 139.43 ? 526 THR A CA 1 ATOM 4048 C C . THR A 1 526 ? -31.951 59.219 -10.423 1.00 143.49 ? 526 THR A C 1 ATOM 4049 O O . THR A 1 526 ? -33.060 59.720 -10.599 1.00 157.02 ? 526 THR A O 1 ATOM 4050 C CB . THR A 1 526 ? -30.817 59.060 -12.660 1.00 139.66 ? 526 THR A CB 1 ATOM 4051 O OG1 . THR A 1 526 ? -30.336 58.149 -13.656 1.00 140.06 ? 526 THR A OG1 1 ATOM 4052 C CG2 . THR A 1 526 ? -29.681 59.978 -12.226 1.00 150.02 ? 526 THR A CG2 1 ATOM 4053 N N . ILE A 1 527 ? -31.217 59.469 -9.344 1.00 142.77 ? 527 ILE A N 1 ATOM 4054 C CA . ILE A 1 527 ? -31.734 60.313 -8.273 1.00 143.28 ? 527 ILE A CA 1 ATOM 4055 C C . ILE A 1 527 ? -30.834 61.525 -8.043 1.00 137.68 ? 527 ILE A C 1 ATOM 4056 O O . ILE A 1 527 ? -29.783 61.661 -8.666 1.00 130.22 ? 527 ILE A O 1 ATOM 4057 C CB . ILE A 1 527 ? -31.871 59.519 -6.946 1.00 132.82 ? 527 ILE A CB 1 ATOM 4058 C CG1 . ILE A 1 527 ? -32.087 58.029 -7.219 1.00 137.06 ? 527 ILE A CG1 1 ATOM 4059 C CG2 . ILE A 1 527 ? -33.013 60.065 -6.092 1.00 127.83 ? 527 ILE A CG2 1 ATOM 4060 C CD1 . ILE A 1 527 ? -33.479 57.689 -7.711 1.00 143.03 ? 527 ILE A CD1 1 ATOM 4061 N N . SER A 1 528 ? -31.261 62.398 -7.137 1.00 132.62 ? 528 SER A N 1 ATOM 4062 C CA . SER A 1 528 ? -30.454 63.513 -6.668 1.00 120.41 ? 528 SER A CA 1 ATOM 4063 C C . SER A 1 528 ? -30.396 63.434 -5.150 1.00 136.83 ? 528 SER A C 1 ATOM 4064 O O . SER A 1 528 ? -30.876 62.466 -4.561 1.00 161.57 ? 528 SER A O 1 ATOM 4065 C CB . SER A 1 528 ? -31.032 64.852 -7.127 1.00 120.96 ? 528 SER A CB 1 ATOM 4066 O OG . SER A 1 528 ? -31.080 64.929 -8.540 1.00 124.21 ? 528 SER A OG 1 ATOM 4067 N N . ARG A 1 529 ? -29.812 64.441 -4.511 1.00 130.91 ? 529 ARG A N 1 ATOM 4068 C CA . ARG A 1 529 ? -29.647 64.398 -3.064 1.00 128.12 ? 529 ARG A CA 1 ATOM 4069 C C . ARG A 1 529 ? -30.456 65.467 -2.336 1.00 158.51 ? 529 ARG A C 1 ATOM 4070 O O . ARG A 1 529 ? -31.099 66.314 -2.958 1.00 173.81 ? 529 ARG A O 1 ATOM 4071 C CB . ARG A 1 529 ? -28.167 64.543 -2.709 1.00 138.43 ? 529 ARG A CB 1 ATOM 4072 C CG . ARG A 1 529 ? -27.278 63.460 -3.296 1.00 146.23 ? 529 ARG A CG 1 ATOM 4073 C CD . ARG A 1 529 ? -25.814 63.857 -3.215 1.00 163.59 ? 529 ARG A CD 1 ATOM 4074 N NE . ARG A 1 529 ? -25.414 64.196 -1.852 1.00 147.70 ? 529 ARG A NE 1 ATOM 4075 C CZ . ARG A 1 529 ? -24.272 64.798 -1.537 1.00 128.79 ? 529 ARG A CZ 1 ATOM 4076 N NH1 . ARG A 1 529 ? -23.413 65.135 -2.490 1.00 112.92 ? 529 ARG A NH1 1 ATOM 4077 N NH2 . ARG A 1 529 ? -23.990 65.068 -0.270 1.00 141.40 ? 529 ARG A NH2 1 ATOM 4078 N N . GLY A 1 530 ? -30.412 65.417 -1.008 1.00 157.86 ? 530 GLY A N 1 ATOM 4079 C CA . GLY A 1 530 ? -31.039 66.416 -0.161 1.00 168.42 ? 530 GLY A CA 1 ATOM 4080 C C . GLY A 1 530 ? -32.484 66.141 0.215 1.00 172.95 ? 530 GLY A C 1 ATOM 4081 O O . GLY A 1 530 ? -32.960 66.626 1.242 1.00 180.97 ? 530 GLY A O 1 ATOM 4082 N N . GLY A 1 531 ? -33.187 65.364 -0.604 1.00 151.94 ? 531 GLY A N 1 ATOM 4083 C CA . GLY A 1 531 ? -34.574 65.037 -0.319 1.00 143.04 ? 531 GLY A CA 1 ATOM 4084 C C . GLY A 1 531 ? -35.433 64.902 -1.562 1.00 162.67 ? 531 GLY A C 1 ATOM 4085 O O . GLY A 1 531 ? -34.914 64.761 -2.670 1.00 172.36 ? 531 GLY A O 1 ATOM 4086 N N . LEU A 1 532 ? -36.751 64.943 -1.367 1.00 164.09 ? 532 LEU A N 1 ATOM 4087 C CA . LEU A 1 532 ? -37.714 64.975 -2.471 1.00 155.53 ? 532 LEU A CA 1 ATOM 4088 C C . LEU A 1 532 ? -37.581 63.784 -3.415 1.00 147.61 ? 532 LEU A C 1 ATOM 4089 O O . LEU A 1 532 ? -37.057 63.920 -4.521 1.00 144.90 ? 532 LEU A O 1 ATOM 4090 C CB . LEU A 1 532 ? -37.583 66.281 -3.261 1.00 148.05 ? 532 LEU A CB 1 ATOM 4091 C CG . LEU A 1 532 ? -38.287 67.524 -2.706 1.00 149.74 ? 532 LEU A CG 1 ATOM 4092 C CD1 . LEU A 1 532 ? -39.223 68.107 -3.754 1.00 156.84 ? 532 LEU A CD1 1 ATOM 4093 C CD2 . LEU A 1 532 ? -39.047 67.231 -1.416 1.00 145.68 ? 532 LEU A CD2 1 ATOM 4094 N N . MET A 1 533 ? -38.037 62.619 -2.958 1.00 132.67 ? 533 MET A N 1 ATOM 4095 C CA . MET A 1 533 ? -37.934 61.381 -3.726 1.00 126.86 ? 533 MET A CA 1 ATOM 4096 C C . MET A 1 533 ? -38.464 61.518 -5.148 1.00 127.70 ? 533 MET A C 1 ATOM 4097 O O . MET A 1 533 ? -39.558 62.039 -5.366 1.00 140.22 ? 533 MET A O 1 ATOM 4098 C CB . MET A 1 533 ? -38.696 60.250 -3.028 1.00 113.63 ? 533 MET A CB 1 ATOM 4099 C CG . MET A 1 533 ? -38.677 60.294 -1.513 1.00 117.78 ? 533 MET A CG 1 ATOM 4100 S SD . MET A 1 533 ? -39.321 58.769 -0.794 1.00 173.89 ? 533 MET A SD 1 ATOM 4101 C CE . MET A 1 533 ? -39.149 59.107 0.956 1.00 129.64 ? 533 MET A CE 1 ATOM 4102 N N . GLN A 1 534 ? -37.677 61.050 -6.112 1.00 132.14 ? 534 GLN A N 1 ATOM 4103 C CA . GLN A 1 534 ? -38.123 60.993 -7.498 1.00 136.78 ? 534 GLN A CA 1 ATOM 4104 C C . GLN A 1 534 ? -38.915 59.712 -7.713 1.00 151.88 ? 534 GLN A C 1 ATOM 4105 O O . GLN A 1 534 ? -38.393 58.611 -7.535 1.00 141.80 ? 534 GLN A O 1 ATOM 4106 C CB . GLN A 1 534 ? -36.939 61.057 -8.463 1.00 127.80 ? 534 GLN A CB 1 ATOM 4107 C CG . GLN A 1 534 ? -37.336 60.959 -9.928 1.00 134.30 ? 534 GLN A CG 1 ATOM 4108 C CD . GLN A 1 534 ? -36.143 60.825 -10.853 1.00 154.91 ? 534 GLN A CD 1 ATOM 4109 O OE1 . GLN A 1 534 ? -35.851 59.738 -11.354 1.00 158.31 ? 534 GLN A OE1 1 ATOM 4110 N NE2 . GLN A 1 534 ? -35.447 61.932 -11.090 1.00 157.12 ? 534 GLN A NE2 1 ATOM 4111 N N . CYS A 1 535 ? -40.178 59.858 -8.095 1.00 157.45 ? 535 CYS A N 1 ATOM 4112 C CA . CYS A 1 535 ? -41.070 58.715 -8.205 1.00 128.64 ? 535 CYS A CA 1 ATOM 4113 C C . CYS A 1 535 ? -41.378 58.365 -9.654 1.00 122.73 ? 535 CYS A C 1 ATOM 4114 O O . CYS A 1 535 ? -41.576 59.248 -10.489 1.00 122.90 ? 535 CYS A O 1 ATOM 4115 C CB . CYS A 1 535 ? -42.373 58.986 -7.450 1.00 120.07 ? 535 CYS A CB 1 ATOM 4116 S SG . CYS A 1 535 ? -42.141 59.526 -5.741 1.00 171.97 ? 535 CYS A SG 1 ATOM 4117 N N . GLU A 1 536 ? -41.410 57.070 -9.945 1.00 137.62 ? 536 GLU A N 1 ATOM 4118 C CA . GLU A 1 536 ? -41.852 56.598 -11.248 1.00 143.74 ? 536 GLU A CA 1 ATOM 4119 C C . GLU A 1 536 ? -43.291 56.117 -11.132 1.00 140.50 ? 536 GLU A C 1 ATOM 4120 O O . GLU A 1 536 ? -43.869 56.125 -10.044 1.00 123.03 ? 536 GLU A O 1 ATOM 4121 C CB . GLU A 1 536 ? -40.946 55.479 -11.763 1.00 141.40 ? 536 GLU A CB 1 ATOM 4122 C CG . GLU A 1 536 ? -39.481 55.872 -11.887 1.00 146.09 ? 536 GLU A CG 1 ATOM 4123 C CD . GLU A 1 536 ? -39.250 56.946 -12.932 1.00 148.85 ? 536 GLU A CD 1 ATOM 4124 O OE1 . GLU A 1 536 ? -39.972 56.952 -13.951 1.00 155.85 ? 536 GLU A OE1 1 ATOM 4125 O OE2 . GLU A 1 536 ? -38.347 57.786 -12.734 1.00 149.48 ? 536 GLU A OE2 1 ATOM 4126 N N . GLU A 1 537 ? -43.867 55.692 -12.249 1.00 154.49 ? 537 GLU A N 1 ATOM 4127 C CA . GLU A 1 537 ? -45.250 55.240 -12.253 1.00 144.01 ? 537 GLU A CA 1 ATOM 4128 C C . GLU A 1 537 ? -45.422 54.023 -13.152 1.00 127.72 ? 537 GLU A C 1 ATOM 4129 O O . GLU A 1 537 ? -44.863 53.961 -14.247 1.00 137.05 ? 537 GLU A O 1 ATOM 4130 C CB . GLU A 1 537 ? -46.182 56.369 -12.702 1.00 155.29 ? 537 GLU A CB 1 ATOM 4131 C CG . GLU A 1 537 ? -47.659 56.108 -12.437 1.00 153.96 ? 537 GLU A CG 1 ATOM 4132 C CD . GLU A 1 537 ? -48.019 56.206 -10.965 1.00 143.06 ? 537 GLU A CD 1 ATOM 4133 O OE1 . GLU A 1 537 ? -47.205 56.741 -10.183 1.00 122.84 ? 537 GLU A OE1 1 ATOM 4134 O OE2 . GLU A 1 537 ? -49.120 55.748 -10.590 1.00 151.39 ? 537 GLU A OE2 1 ATOM 4135 N N . LEU A 1 538 ? -46.194 53.055 -12.675 1.00 125.97 ? 538 LEU A N 1 ATOM 4136 C CA . LEU A 1 538 ? -46.447 51.840 -13.434 1.00 138.10 ? 538 LEU A CA 1 ATOM 4137 C C . LEU A 1 538 ? -47.845 51.315 -13.124 1.00 129.68 ? 538 LEU A C 1 ATOM 4138 O O . LEU A 1 538 ? -48.337 51.462 -12.004 1.00 124.44 ? 538 LEU A O 1 ATOM 4139 C CB . LEU A 1 538 ? -45.388 50.783 -13.120 1.00 128.51 ? 538 LEU A CB 1 ATOM 4140 C CG . LEU A 1 538 ? -45.079 49.784 -14.235 1.00 127.75 ? 538 LEU A CG 1 ATOM 4141 C CD1 . LEU A 1 538 ? -44.649 50.517 -15.496 1.00 131.29 ? 538 LEU A CD1 1 ATOM 4142 C CD2 . LEU A 1 538 ? -44.004 48.809 -13.789 1.00 125.35 ? 538 LEU A CD2 1 ATOM 4143 N N . ILE A 1 539 ? -48.484 50.708 -14.118 1.00 125.87 ? 539 ILE A N 1 ATOM 4144 C CA . ILE A 1 539 ? -49.847 50.223 -13.952 1.00 134.27 ? 539 ILE A CA 1 ATOM 4145 C C . ILE A 1 539 ? -49.933 48.704 -14.112 1.00 135.08 ? 539 ILE A C 1 ATOM 4146 O O . ILE A 1 539 ? -49.462 48.136 -15.099 1.00 135.78 ? 539 ILE A O 1 ATOM 4147 C CB . ILE A 1 539 ? -50.807 50.914 -14.951 1.00 140.90 ? 539 ILE A CB 1 ATOM 4148 C CG1 . ILE A 1 539 ? -52.205 50.297 -14.875 1.00 127.97 ? 539 ILE A CG1 1 ATOM 4149 C CG2 . ILE A 1 539 ? -50.252 50.857 -16.370 1.00 148.81 ? 539 ILE A CG2 1 ATOM 4150 C CD1 . ILE A 1 539 ? -53.241 51.044 -15.685 1.00 130.76 ? 539 ILE A CD1 1 ATOM 4151 N N . ALA A 1 540 ? -50.527 48.050 -13.119 1.00 123.53 ? 540 ALA A N 1 ATOM 4152 C CA . ALA A 1 540 ? -50.693 46.601 -13.136 1.00 122.16 ? 540 ALA A CA 1 ATOM 4153 C C . ALA A 1 540 ? -52.171 46.245 -13.106 1.00 127.01 ? 540 ALA A C 1 ATOM 4154 O O . ALA A 1 540 ? -52.996 47.046 -12.670 1.00 140.66 ? 540 ALA A O 1 ATOM 4155 C CB . ALA A 1 540 ? -49.967 45.966 -11.962 1.00 120.75 ? 540 ALA A CB 1 ATOM 4156 N N . TYR A 1 541 ? -52.509 45.044 -13.563 1.00 131.03 ? 541 TYR A N 1 ATOM 4157 C CA . TYR A 1 541 ? -53.909 44.647 -13.652 1.00 123.09 ? 541 TYR A CA 1 ATOM 4158 C C . TYR A 1 541 ? -54.167 43.277 -13.033 1.00 120.73 ? 541 TYR A C 1 ATOM 4159 O O . TYR A 1 541 ? -53.236 42.527 -12.738 1.00 119.66 ? 541 TYR A O 1 ATOM 4160 C CB . TYR A 1 541 ? -54.372 44.658 -15.112 1.00 124.76 ? 541 TYR A CB 1 ATOM 4161 C CG . TYR A 1 541 ? -53.822 43.528 -15.955 1.00 137.34 ? 541 TYR A CG 1 ATOM 4162 C CD1 . TYR A 1 541 ? -52.552 43.603 -16.510 1.00 140.55 ? 541 TYR A CD1 1 ATOM 4163 C CD2 . TYR A 1 541 ? -54.580 42.390 -16.206 1.00 139.56 ? 541 TYR A CD2 1 ATOM 4164 C CE1 . TYR A 1 541 ? -52.046 42.573 -17.285 1.00 144.09 ? 541 TYR A CE1 1 ATOM 4165 C CE2 . TYR A 1 541 ? -54.083 41.356 -16.979 1.00 135.15 ? 541 TYR A CE2 1 ATOM 4166 C CZ . TYR A 1 541 ? -52.816 41.453 -17.515 1.00 142.59 ? 541 TYR A CZ 1 ATOM 4167 O OH . TYR A 1 541 ? -52.317 40.427 -18.284 1.00 143.53 ? 541 TYR A OH 1 ATOM 4168 N N . LEU A 1 542 ? -55.443 42.964 -12.838 1.00 129.60 ? 542 LEU A N 1 ATOM 4169 C CA . LEU A 1 542 ? -55.847 41.722 -12.193 1.00 118.09 ? 542 LEU A CA 1 ATOM 4170 C C . LEU A 1 542 ? -56.516 40.781 -13.190 1.00 118.61 ? 542 LEU A C 1 ATOM 4171 O O . LEU A 1 542 ? -57.316 41.212 -14.021 1.00 120.01 ? 542 LEU A O 1 ATOM 4172 C CB . LEU A 1 542 ? -56.793 42.020 -11.027 1.00 116.83 ? 542 LEU A CB 1 ATOM 4173 C CG . LEU A 1 542 ? -56.959 40.960 -9.939 1.00 115.91 ? 542 LEU A CG 1 ATOM 4174 C CD1 . LEU A 1 542 ? -55.642 40.724 -9.224 1.00 126.48 ? 542 LEU A CD1 1 ATOM 4175 C CD2 . LEU A 1 542 ? -58.036 41.379 -8.951 1.00 114.90 ? 542 LEU A CD2 1 ATOM 4176 N N . ARG A 1 543 ? -56.182 39.497 -13.108 1.00 117.75 ? 543 ARG A N 1 ATOM 4177 C CA . ARG A 1 543 ? -56.804 38.493 -13.964 1.00 120.94 ? 543 ARG A CA 1 ATOM 4178 C C . ARG A 1 543 ? -58.286 38.354 -13.637 1.00 123.65 ? 543 ARG A C 1 ATOM 4179 O O . ARG A 1 543 ? -58.706 38.609 -12.507 1.00 127.41 ? 543 ARG A O 1 ATOM 4180 C CB . ARG A 1 543 ? -56.108 37.138 -13.809 1.00 118.34 ? 543 ARG A CB 1 ATOM 4181 C CG . ARG A 1 543 ? -54.638 37.123 -14.200 1.00 121.01 ? 543 ARG A CG 1 ATOM 4182 C CD . ARG A 1 543 ? -54.023 35.757 -13.916 1.00 120.84 ? 543 ARG A CD 1 ATOM 4183 N NE . ARG A 1 543 ? -52.602 35.702 -14.243 1.00 129.44 ? 543 ARG A NE 1 ATOM 4184 C CZ . ARG A 1 543 ? -52.114 35.208 -15.376 1.00 139.96 ? 543 ARG A CZ 1 ATOM 4185 N NH1 . ARG A 1 543 ? -52.933 34.723 -16.299 1.00 144.51 ? 543 ARG A NH1 1 ATOM 4186 N NH2 . ARG A 1 543 ? -50.805 35.195 -15.588 1.00 144.94 ? 543 ARG A NH2 1 ATOM 4187 N N . ASP A 1 544 ? -59.078 37.951 -14.625 1.00 120.11 ? 544 ASP A N 1 ATOM 4188 C CA . ASP A 1 544 ? -60.501 37.719 -14.405 1.00 123.46 ? 544 ASP A CA 1 ATOM 4189 C C . ASP A 1 544 ? -60.699 36.490 -13.521 1.00 121.15 ? 544 ASP A C 1 ATOM 4190 O O . ASP A 1 544 ? -59.796 35.665 -13.380 1.00 117.69 ? 544 ASP A O 1 ATOM 4191 C CB . ASP A 1 544 ? -61.244 37.559 -15.734 1.00 137.03 ? 544 ASP A CB 1 ATOM 4192 C CG . ASP A 1 544 ? -60.656 36.470 -16.605 1.00 156.61 ? 544 ASP A CG 1 ATOM 4193 O OD1 . ASP A 1 544 ? -61.437 35.708 -17.211 1.00 157.96 ? 544 ASP A OD1 1 ATOM 4194 O OD2 . ASP A 1 544 ? -59.414 36.381 -16.687 1.00 165.41 ? 544 ASP A OD2 1 ATOM 4195 N N . GLU A 1 545 ? -61.883 36.387 -12.923 1.00 123.51 ? 545 GLU A N 1 ATOM 4196 C CA . GLU A 1 545 ? -62.184 35.369 -11.916 1.00 125.74 ? 545 GLU A CA 1 ATOM 4197 C C . GLU A 1 545 ? -61.898 33.935 -12.365 1.00 136.61 ? 545 GLU A C 1 ATOM 4198 O O . GLU A 1 545 ? -61.625 33.065 -11.538 1.00 135.94 ? 545 GLU A O 1 ATOM 4199 C CB . GLU A 1 545 ? -63.653 35.476 -11.493 1.00 137.56 ? 545 GLU A CB 1 ATOM 4200 C CG . GLU A 1 545 ? -64.110 36.877 -11.103 1.00 148.52 ? 545 GLU A CG 1 ATOM 4201 C CD . GLU A 1 545 ? -64.564 37.708 -12.292 1.00 158.36 ? 545 GLU A CD 1 ATOM 4202 O OE1 . GLU A 1 545 ? -64.066 37.477 -13.414 1.00 158.44 ? 545 GLU A OE1 1 ATOM 4203 O OE2 . GLU A 1 545 ? -65.427 38.592 -12.104 1.00 161.57 ? 545 GLU A OE2 1 ATOM 4204 N N . SER A 1 546 ? -61.962 33.692 -13.670 1.00 147.62 ? 546 SER A N 1 ATOM 4205 C CA . SER A 1 546 ? -61.836 32.340 -14.206 1.00 141.86 ? 546 SER A CA 1 ATOM 4206 C C . SER A 1 546 ? -60.408 31.796 -14.168 1.00 137.40 ? 546 SER A C 1 ATOM 4207 O O . SER A 1 546 ? -60.200 30.606 -13.930 1.00 140.67 ? 546 SER A O 1 ATOM 4208 C CB . SER A 1 546 ? -62.356 32.296 -15.643 1.00 136.31 ? 546 SER A CB 1 ATOM 4209 O OG . SER A 1 546 ? -61.594 33.140 -16.489 1.00 130.62 ? 546 SER A OG 1 ATOM 4210 N N . GLU A 1 547 ? -59.429 32.665 -14.405 1.00 128.12 ? 547 GLU A N 1 ATOM 4211 C CA . GLU A 1 547 ? -58.041 32.230 -14.553 1.00 124.20 ? 547 GLU A CA 1 ATOM 4212 C C . GLU A 1 547 ? -57.451 31.624 -13.281 1.00 118.73 ? 547 GLU A C 1 ATOM 4213 O O . GLU A 1 547 ? -56.595 30.744 -13.352 1.00 123.95 ? 547 GLU A O 1 ATOM 4214 C CB . GLU A 1 547 ? -57.165 33.396 -15.017 1.00 136.52 ? 547 GLU A CB 1 ATOM 4215 C CG . GLU A 1 547 ? -57.462 33.866 -16.432 1.00 150.41 ? 547 GLU A CG 1 ATOM 4216 C CD . GLU A 1 547 ? -56.390 34.789 -16.976 1.00 157.30 ? 547 GLU A CD 1 ATOM 4217 O OE1 . GLU A 1 547 ? -55.193 34.456 -16.844 1.00 150.52 ? 547 GLU A OE1 1 ATOM 4218 O OE2 . GLU A 1 547 ? -56.742 35.850 -17.536 1.00 158.37 ? 547 GLU A OE2 1 ATOM 4219 N N . PHE A 1 548 ? -57.901 32.093 -12.122 1.00 117.25 ? 548 PHE A N 1 ATOM 4220 C CA . PHE A 1 548 ? -57.390 31.576 -10.856 1.00 120.85 ? 548 PHE A CA 1 ATOM 4221 C C . PHE A 1 548 ? -58.512 31.336 -9.852 1.00 122.84 ? 548 PHE A C 1 ATOM 4222 O O . PHE A 1 548 ? -59.687 31.513 -10.169 1.00 130.89 ? 548 PHE A O 1 ATOM 4223 C CB . PHE A 1 548 ? -56.344 32.528 -10.267 1.00 122.04 ? 548 PHE A CB 1 ATOM 4224 C CG . PHE A 1 548 ? -56.906 33.842 -9.804 1.00 117.04 ? 548 PHE A CG 1 ATOM 4225 C CD1 . PHE A 1 548 ? -57.177 34.060 -8.462 1.00 111.22 ? 548 PHE A CD1 1 ATOM 4226 C CD2 . PHE A 1 548 ? -57.158 34.861 -10.707 1.00 119.29 ? 548 PHE A CD2 1 ATOM 4227 C CE1 . PHE A 1 548 ? -57.691 35.267 -8.031 1.00 110.59 ? 548 PHE A CE1 1 ATOM 4228 C CE2 . PHE A 1 548 ? -57.672 36.071 -10.282 1.00 116.19 ? 548 PHE A CE2 1 ATOM 4229 C CZ . PHE A 1 548 ? -57.939 36.274 -8.942 1.00 114.38 ? 548 PHE A CZ 1 ATOM 4230 N N . ARG A 1 549 ? -58.142 30.933 -8.640 1.00 116.41 ? 549 ARG A N 1 ATOM 4231 C CA . ARG A 1 549 ? -59.127 30.572 -7.628 1.00 117.57 ? 549 ARG A CA 1 ATOM 4232 C C . ARG A 1 549 ? -59.046 31.431 -6.368 1.00 123.43 ? 549 ARG A C 1 ATOM 4233 O O . ARG A 1 549 ? -59.986 32.158 -6.050 1.00 130.06 ? 549 ARG A O 1 ATOM 4234 C CB . ARG A 1 549 ? -58.980 29.095 -7.251 1.00 126.17 ? 549 ARG A CB 1 ATOM 4235 C CG . ARG A 1 549 ? -59.321 28.133 -8.378 1.00 137.69 ? 549 ARG A CG 1 ATOM 4236 C CD . ARG A 1 549 ? -59.376 26.697 -7.883 1.00 148.11 ? 549 ARG A CD 1 ATOM 4237 N NE . ARG A 1 549 ? -59.778 25.772 -8.939 1.00 165.02 ? 549 ARG A NE 1 ATOM 4238 C CZ . ARG A 1 549 ? -61.041 25.504 -9.258 1.00 157.42 ? 549 ARG A CZ 1 ATOM 4239 N NH1 . ARG A 1 549 ? -62.032 26.094 -8.605 1.00 148.23 ? 549 ARG A NH1 1 ATOM 4240 N NH2 . ARG A 1 549 ? -61.313 24.647 -10.233 1.00 154.15 ? 549 ARG A NH2 1 ATOM 4241 N N . ASP A 1 550 ? -57.926 31.340 -5.655 1.00 119.61 ? 550 ASP A N 1 ATOM 4242 C CA . ASP A 1 550 ? -57.809 31.943 -4.329 1.00 116.51 ? 550 ASP A CA 1 ATOM 4243 C C . ASP A 1 550 ? -58.000 33.460 -4.338 1.00 105.71 ? 550 ASP A C 1 ATOM 4244 O O . ASP A 1 550 ? -57.268 34.192 -5.003 1.00 105.60 ? 550 ASP A O 1 ATOM 4245 C CB . ASP A 1 550 ? -56.444 31.591 -3.732 1.00 113.26 ? 550 ASP A CB 1 ATOM 4246 C CG . ASP A 1 550 ? -56.113 32.399 -2.495 1.00 110.86 ? 550 ASP A CG 1 ATOM 4247 O OD1 . ASP A 1 550 ? -57.012 32.621 -1.657 1.00 114.15 ? 550 ASP A OD1 1 ATOM 4248 O OD2 . ASP A 1 550 ? -54.942 32.808 -2.362 1.00 118.17 ? 550 ASP A OD2 1 ATOM 4249 N N . LYS A 1 551 ? -59.002 33.914 -3.588 1.00 107.60 ? 551 LYS A N 1 ATOM 4250 C CA . LYS A 1 551 ? -59.268 35.337 -3.399 1.00 105.44 ? 551 LYS A CA 1 ATOM 4251 C C . LYS A 1 551 ? -58.773 35.863 -2.051 1.00 104.13 ? 551 LYS A C 1 ATOM 4252 O O . LYS A 1 551 ? -58.903 37.051 -1.758 1.00 119.75 ? 551 LYS A O 1 ATOM 4253 C CB . LYS A 1 551 ? -60.765 35.613 -3.547 1.00 115.10 ? 551 LYS A CB 1 ATOM 4254 C CG . LYS A 1 551 ? -61.327 35.221 -4.906 1.00 114.94 ? 551 LYS A CG 1 ATOM 4255 C CD . LYS A 1 551 ? -62.823 35.476 -4.994 1.00 114.62 ? 551 LYS A CD 1 ATOM 4256 C CE . LYS A 1 551 ? -63.355 35.117 -6.372 1.00 116.09 ? 551 LYS A CE 1 ATOM 4257 N NZ . LYS A 1 551 ? -64.823 35.325 -6.473 1.00 122.86 ? 551 LYS A NZ 1 ATOM 4258 N N . LEU A 1 552 ? -58.216 34.976 -1.232 1.00 101.93 ? 552 LEU A N 1 ATOM 4259 C CA . LEU A 1 552 ? -57.905 35.314 0.157 1.00 101.00 ? 552 LEU A CA 1 ATOM 4260 C C . LEU A 1 552 ? -56.489 35.849 0.354 1.00 100.04 ? 552 LEU A C 1 ATOM 4261 O O . LEU A 1 552 ? -56.317 36.984 0.801 1.00 100.34 ? 552 LEU A O 1 ATOM 4262 C CB . LEU A 1 552 ? -58.133 34.101 1.063 1.00 112.21 ? 552 LEU A CB 1 ATOM 4263 C CG . LEU A 1 552 ? -59.565 33.924 1.563 1.00 117.67 ? 552 LEU A CG 1 ATOM 4264 C CD1 . LEU A 1 552 ? -59.703 32.671 2.419 1.00 118.33 ? 552 LEU A CD1 1 ATOM 4265 C CD2 . LEU A 1 552 ? -60.015 35.158 2.336 1.00 100.17 ? 552 LEU A CD2 1 ATOM 4266 N N . THR A 1 553 ? -55.487 35.028 0.051 1.00 99.32 ? 553 THR A N 1 ATOM 4267 C CA . THR A 1 553 ? -54.092 35.402 0.262 1.00 104.68 ? 553 THR A CA 1 ATOM 4268 C C . THR A 1 553 ? -53.778 36.745 -0.398 1.00 115.12 ? 553 THR A C 1 ATOM 4269 O O . THR A 1 553 ? -53.990 36.919 -1.601 1.00 118.29 ? 553 THR A O 1 ATOM 4270 C CB . THR A 1 553 ? -53.132 34.318 -0.288 1.00 107.19 ? 553 THR A CB 1 ATOM 4271 O OG1 . THR A 1 553 ? -53.421 33.064 0.340 1.00 110.74 ? 553 THR A OG1 1 ATOM 4272 C CG2 . THR A 1 553 ? -51.685 34.694 -0.019 1.00 112.61 ? 553 THR A CG2 1 ATOM 4273 N N . PRO A 1 554 ? -53.299 37.713 0.399 1.00 106.13 ? 554 PRO A N 1 ATOM 4274 C CA . PRO A 1 554 ? -53.034 39.077 -0.071 1.00 101.89 ? 554 PRO A CA 1 ATOM 4275 C C . PRO A 1 554 ? -52.045 39.122 -1.228 1.00 103.53 ? 554 PRO A C 1 ATOM 4276 O O . PRO A 1 554 ? -51.200 38.237 -1.351 1.00 102.09 ? 554 PRO A O 1 ATOM 4277 C CB . PRO A 1 554 ? -52.448 39.769 1.168 1.00 100.52 ? 554 PRO A CB 1 ATOM 4278 C CG . PRO A 1 554 ? -52.969 38.986 2.319 1.00 100.06 ? 554 PRO A CG 1 ATOM 4279 C CD . PRO A 1 554 ? -53.034 37.568 1.839 1.00 101.44 ? 554 PRO A CD 1 ATOM 4280 N N . ILE A 1 555 ? -52.151 40.150 -2.061 1.00 104.91 ? 555 ILE A N 1 ATOM 4281 C CA . ILE A 1 555 ? -51.207 40.334 -3.153 1.00 106.15 ? 555 ILE A CA 1 ATOM 4282 C C . ILE A 1 555 ? -50.079 41.243 -2.680 1.00 106.44 ? 555 ILE A C 1 ATOM 4283 O O . ILE A 1 555 ? -50.284 42.434 -2.454 1.00 108.06 ? 555 ILE A O 1 ATOM 4284 C CB . ILE A 1 555 ? -51.890 40.934 -4.398 1.00 108.18 ? 555 ILE A CB 1 ATOM 4285 C CG1 . ILE A 1 555 ? -53.037 40.033 -4.861 1.00 107.97 ? 555 ILE A CG1 1 ATOM 4286 C CG2 . ILE A 1 555 ? -50.882 41.138 -5.517 1.00 114.44 ? 555 ILE A CG2 1 ATOM 4287 C CD1 . ILE A 1 555 ? -53.815 40.585 -6.032 1.00 110.92 ? 555 ILE A CD1 1 ATOM 4288 N N . THR A 1 556 ? -48.886 40.676 -2.532 1.00 105.55 ? 556 THR A N 1 ATOM 4289 C CA . THR A 1 556 ? -47.759 41.412 -1.971 1.00 105.04 ? 556 THR A CA 1 ATOM 4290 C C . THR A 1 556 ? -46.890 42.030 -3.057 1.00 116.63 ? 556 THR A C 1 ATOM 4291 O O . THR A 1 556 ? -46.233 41.324 -3.821 1.00 108.65 ? 556 THR A O 1 ATOM 4292 C CB . THR A 1 556 ? -46.881 40.509 -1.082 1.00 102.29 ? 556 THR A CB 1 ATOM 4293 O OG1 . THR A 1 556 ? -47.629 40.088 0.066 1.00 100.15 ? 556 THR A OG1 1 ATOM 4294 C CG2 . THR A 1 556 ? -45.643 41.260 -0.619 1.00 111.54 ? 556 THR A CG2 1 ATOM 4295 N N . ILE A 1 557 ? -46.887 43.357 -3.115 1.00 128.02 ? 557 ILE A N 1 ATOM 4296 C CA . ILE A 1 557 ? -46.049 44.075 -4.064 1.00 110.72 ? 557 ILE A CA 1 ATOM 4297 C C . ILE A 1 557 ? -44.654 44.240 -3.473 1.00 109.84 ? 557 ILE A C 1 ATOM 4298 O O . ILE A 1 557 ? -44.492 44.814 -2.397 1.00 108.80 ? 557 ILE A O 1 ATOM 4299 C CB . ILE A 1 557 ? -46.634 45.456 -4.424 1.00 113.13 ? 557 ILE A CB 1 ATOM 4300 C CG1 . ILE A 1 557 ? -47.969 45.307 -5.163 1.00 114.73 ? 557 ILE A CG1 1 ATOM 4301 C CG2 . ILE A 1 557 ? -45.658 46.240 -5.282 1.00 116.19 ? 557 ILE A CG2 1 ATOM 4302 C CD1 . ILE A 1 557 ? -49.186 45.198 -4.260 1.00 112.73 ? 557 ILE A CD1 1 ATOM 4303 N N . PHE A 1 558 ? -43.651 43.728 -4.178 1.00 110.23 ? 558 PHE A N 1 ATOM 4304 C CA . PHE A 1 558 ? -42.289 43.700 -3.656 1.00 109.36 ? 558 PHE A CA 1 ATOM 4305 C C . PHE A 1 558 ? -41.339 44.565 -4.479 1.00 113.91 ? 558 PHE A C 1 ATOM 4306 O O . PHE A 1 558 ? -41.112 44.307 -5.661 1.00 123.16 ? 558 PHE A O 1 ATOM 4307 C CB . PHE A 1 558 ? -41.780 42.258 -3.603 1.00 107.41 ? 558 PHE A CB 1 ATOM 4308 C CG . PHE A 1 558 ? -40.396 42.122 -3.041 1.00 106.26 ? 558 PHE A CG 1 ATOM 4309 C CD1 . PHE A 1 558 ? -40.176 42.199 -1.676 1.00 104.06 ? 558 PHE A CD1 1 ATOM 4310 C CD2 . PHE A 1 558 ? -39.313 41.902 -3.877 1.00 107.18 ? 558 PHE A CD2 1 ATOM 4311 C CE1 . PHE A 1 558 ? -38.903 42.069 -1.157 1.00 102.94 ? 558 PHE A CE1 1 ATOM 4312 C CE2 . PHE A 1 558 ? -38.040 41.771 -3.363 1.00 106.49 ? 558 PHE A CE2 1 ATOM 4313 C CZ . PHE A 1 558 ? -37.834 41.854 -2.002 1.00 104.80 ? 558 PHE A CZ 1 ATOM 4314 N N . MET A 1 559 ? -40.787 45.590 -3.838 1.00 112.58 ? 559 MET A N 1 ATOM 4315 C CA . MET A 1 559 ? -39.837 46.494 -4.477 1.00 114.70 ? 559 MET A CA 1 ATOM 4316 C C . MET A 1 559 ? -38.433 46.271 -3.929 1.00 113.59 ? 559 MET A C 1 ATOM 4317 O O . MET A 1 559 ? -38.250 46.156 -2.721 1.00 110.70 ? 559 MET A O 1 ATOM 4318 C CB . MET A 1 559 ? -40.256 47.951 -4.262 1.00 124.83 ? 559 MET A CB 1 ATOM 4319 C CG . MET A 1 559 ? -39.218 48.970 -4.708 1.00 123.49 ? 559 MET A CG 1 ATOM 4320 S SD . MET A 1 559 ? -39.549 50.634 -4.096 1.00 118.15 ? 559 MET A SD 1 ATOM 4321 C CE . MET A 1 559 ? -38.182 51.536 -4.819 1.00 152.35 ? 559 MET A CE 1 ATOM 4322 N N . GLU A 1 560 ? -37.445 46.210 -4.817 1.00 115.70 ? 560 GLU A N 1 ATOM 4323 C CA . GLU A 1 560 ? -36.058 46.028 -4.401 1.00 116.73 ? 560 GLU A CA 1 ATOM 4324 C C . GLU A 1 560 ? -35.124 46.864 -5.273 1.00 123.78 ? 560 GLU A C 1 ATOM 4325 O O . GLU A 1 560 ? -35.261 46.884 -6.496 1.00 122.65 ? 560 GLU A O 1 ATOM 4326 C CB . GLU A 1 560 ? -35.672 44.548 -4.465 1.00 117.80 ? 560 GLU A CB 1 ATOM 4327 C CG . GLU A 1 560 ? -34.390 44.193 -3.725 1.00 143.05 ? 560 GLU A CG 1 ATOM 4328 C CD . GLU A 1 560 ? -34.143 42.693 -3.669 1.00 150.84 ? 560 GLU A CD 1 ATOM 4329 O OE1 . GLU A 1 560 ? -34.529 41.987 -4.625 1.00 140.77 ? 560 GLU A OE1 1 ATOM 4330 O OE2 . GLU A 1 560 ? -33.570 42.222 -2.665 1.00 148.65 ? 560 GLU A OE2 1 ATOM 4331 N N . TYR A 1 561 ? -34.175 47.552 -4.645 1.00 134.91 ? 561 TYR A N 1 ATOM 4332 C CA . TYR A 1 561 ? -33.254 48.408 -5.388 1.00 132.25 ? 561 TYR A CA 1 ATOM 4333 C C . TYR A 1 561 ? -31.806 47.933 -5.273 1.00 132.95 ? 561 TYR A C 1 ATOM 4334 O O . TYR A 1 561 ? -31.430 47.263 -4.310 1.00 125.60 ? 561 TYR A O 1 ATOM 4335 C CB . TYR A 1 561 ? -33.375 49.863 -4.925 1.00 121.11 ? 561 TYR A CB 1 ATOM 4336 C CG . TYR A 1 561 ? -33.326 50.072 -3.428 1.00 116.00 ? 561 TYR A CG 1 ATOM 4337 C CD1 . TYR A 1 561 ? -32.128 50.352 -2.785 1.00 119.58 ? 561 TYR A CD1 1 ATOM 4338 C CD2 . TYR A 1 561 ? -34.483 50.012 -2.660 1.00 113.95 ? 561 TYR A CD2 1 ATOM 4339 C CE1 . TYR A 1 561 ? -32.080 50.554 -1.418 1.00 130.44 ? 561 TYR A CE1 1 ATOM 4340 C CE2 . TYR A 1 561 ? -34.444 50.210 -1.293 1.00 121.12 ? 561 TYR A CE2 1 ATOM 4341 C CZ . TYR A 1 561 ? -33.242 50.481 -0.678 1.00 135.87 ? 561 TYR A CZ 1 ATOM 4342 O OH . TYR A 1 561 ? -33.199 50.681 0.683 1.00 147.50 ? 561 TYR A OH 1 ATOM 4343 N N . ARG A 1 562 ? -31.004 48.297 -6.269 1.00 142.94 ? 562 ARG A N 1 ATOM 4344 C CA . ARG A 1 562 ? -29.661 47.752 -6.444 1.00 149.66 ? 562 ARG A CA 1 ATOM 4345 C C . ARG A 1 562 ? -28.567 48.783 -6.182 1.00 154.14 ? 562 ARG A C 1 ATOM 4346 O O . ARG A 1 562 ? -27.720 48.586 -5.309 1.00 161.30 ? 562 ARG A O 1 ATOM 4347 C CB . ARG A 1 562 ? -29.505 47.180 -7.853 1.00 160.01 ? 562 ARG A CB 1 ATOM 4348 C CG . ARG A 1 562 ? -28.296 46.279 -8.026 1.00 159.08 ? 562 ARG A CG 1 ATOM 4349 C CD . ARG A 1 562 ? -28.454 44.981 -7.247 1.00 152.90 ? 562 ARG A CD 1 ATOM 4350 N NE . ARG A 1 562 ? -29.629 44.223 -7.673 1.00 154.05 ? 562 ARG A NE 1 ATOM 4351 C CZ . ARG A 1 562 ? -30.736 44.084 -6.950 1.00 150.11 ? 562 ARG A CZ 1 ATOM 4352 N NH1 . ARG A 1 562 ? -30.825 44.648 -5.754 1.00 150.44 ? 562 ARG A NH1 1 ATOM 4353 N NH2 . ARG A 1 562 ? -31.753 43.376 -7.422 1.00 145.61 ? 562 ARG A NH2 1 ATOM 4354 N N . LEU A 1 563 ? -28.590 49.865 -6.960 1.00 149.85 ? 563 LEU A N 1 ATOM 4355 C CA . LEU A 1 563 ? -27.534 50.879 -6.955 1.00 147.74 ? 563 LEU A CA 1 ATOM 4356 C C . LEU A 1 563 ? -26.204 50.275 -7.383 1.00 138.04 ? 563 LEU A C 1 ATOM 4357 O O . LEU A 1 563 ? -25.324 50.024 -6.560 1.00 126.40 ? 563 LEU A O 1 ATOM 4358 C CB . LEU A 1 563 ? -27.399 51.545 -5.578 1.00 142.87 ? 563 LEU A CB 1 ATOM 4359 C CG . LEU A 1 563 ? -26.376 52.679 -5.430 1.00 127.95 ? 563 LEU A CG 1 ATOM 4360 C CD1 . LEU A 1 563 ? -26.740 53.874 -6.299 1.00 132.84 ? 563 LEU A CD1 1 ATOM 4361 C CD2 . LEU A 1 563 ? -26.224 53.093 -3.972 1.00 118.52 ? 563 LEU A CD2 1 ATOM 4362 N N . ASP A 1 564 ? -26.093 49.983 -8.676 1.00 146.29 ? 564 ASP A N 1 ATOM 4363 C CA . ASP A 1 564 ? -24.808 49.623 -9.261 1.00 141.81 ? 564 ASP A CA 1 ATOM 4364 C C . ASP A 1 564 ? -23.843 50.743 -8.938 1.00 142.31 ? 564 ASP A C 1 ATOM 4365 O O . ASP A 1 564 ? -24.144 51.898 -9.223 1.00 130.16 ? 564 ASP A O 1 ATOM 4366 C CB . ASP A 1 564 ? -24.904 49.444 -10.778 1.00 143.61 ? 564 ASP A CB 1 ATOM 4367 C CG . ASP A 1 564 ? -26.063 48.568 -11.193 1.00 155.80 ? 564 ASP A CG 1 ATOM 4368 O OD1 . ASP A 1 564 ? -26.551 47.795 -10.345 1.00 164.90 ? 564 ASP A OD1 1 ATOM 4369 O OD2 . ASP A 1 564 ? -26.475 48.645 -12.370 1.00 152.64 ? 564 ASP A OD2 1 ATOM 4370 N N . TYR A 1 565 ? -22.688 50.438 -8.358 1.00 155.64 ? 565 TYR A N 1 ATOM 4371 C CA . TYR A 1 565 ? -21.831 51.535 -7.942 1.00 145.89 ? 565 TYR A CA 1 ATOM 4372 C C . TYR A 1 565 ? -20.834 51.898 -9.024 1.00 139.73 ? 565 TYR A C 1 ATOM 4373 O O . TYR A 1 565 ? -19.856 51.188 -9.248 1.00 132.87 ? 565 TYR A O 1 ATOM 4374 C CB . TYR A 1 565 ? -21.069 51.194 -6.654 1.00 142.42 ? 565 TYR A CB 1 ATOM 4375 C CG . TYR A 1 565 ? -21.856 50.412 -5.628 1.00 141.68 ? 565 TYR A CG 1 ATOM 4376 C CD1 . TYR A 1 565 ? -22.838 51.023 -4.857 1.00 156.24 ? 565 TYR A CD1 1 ATOM 4377 C CD2 . TYR A 1 565 ? -21.598 49.064 -5.409 1.00 129.83 ? 565 TYR A CD2 1 ATOM 4378 C CE1 . TYR A 1 565 ? -23.551 50.309 -3.907 1.00 161.76 ? 565 TYR A CE1 1 ATOM 4379 C CE2 . TYR A 1 565 ? -22.309 48.340 -4.458 1.00 140.01 ? 565 TYR A CE2 1 ATOM 4380 C CZ . TYR A 1 565 ? -23.283 48.968 -3.710 1.00 150.78 ? 565 TYR A CZ 1 ATOM 4381 O OH . TYR A 1 565 ? -23.991 48.256 -2.764 1.00 150.48 ? 565 TYR A OH 1 ATOM 4382 N N . ARG A 1 566 ? -21.053 53.035 -9.667 1.00 145.70 ? 566 ARG A N 1 ATOM 4383 C CA . ARG A 1 566 ? -19.956 53.641 -10.372 1.00 141.29 ? 566 ARG A CA 1 ATOM 4384 C C . ARG A 1 566 ? -19.886 55.081 -9.929 1.00 139.81 ? 566 ARG A C 1 ATOM 4385 O O . ARG A 1 566 ? -20.679 55.932 -10.330 1.00 127.78 ? 566 ARG A O 1 ATOM 4386 C CB . ARG A 1 566 ? -20.125 53.514 -11.887 1.00 143.81 ? 566 ARG A CB 1 ATOM 4387 C CG . ARG A 1 566 ? -19.848 52.103 -12.430 1.00 147.47 ? 566 ARG A CG 1 ATOM 4388 C CD . ARG A 1 566 ? -18.453 51.610 -12.042 1.00 148.53 ? 566 ARG A CD 1 ATOM 4389 N NE . ARG A 1 566 ? -18.233 50.208 -12.418 1.00 157.59 ? 566 ARG A NE 1 ATOM 4390 C CZ . ARG A 1 566 ? -18.653 49.178 -11.691 1.00 143.46 ? 566 ARG A CZ 1 ATOM 4391 N NH1 . ARG A 1 566 ? -19.311 49.409 -10.563 1.00 149.30 ? 566 ARG A NH1 1 ATOM 4392 N NH2 . ARG A 1 566 ? -18.428 47.933 -12.088 1.00 128.24 ? 566 ARG A NH2 1 ATOM 4393 N N . THR A 1 567 ? -18.900 55.336 -9.082 1.00 149.44 ? 567 THR A N 1 ATOM 4394 C CA . THR A 1 567 ? -18.474 56.677 -8.713 1.00 150.99 ? 567 THR A CA 1 ATOM 4395 C C . THR A 1 567 ? -16.988 56.568 -8.384 1.00 138.18 ? 567 THR A C 1 ATOM 4396 O O . THR A 1 567 ? -16.548 55.590 -7.769 1.00 142.49 ? 567 THR A O 1 ATOM 4397 C CB . THR A 1 567 ? -19.257 57.266 -7.504 1.00 129.24 ? 567 THR A CB 1 ATOM 4398 O OG1 . THR A 1 567 ? -18.370 57.422 -6.391 1.00 131.03 ? 567 THR A OG1 1 ATOM 4399 C CG2 . THR A 1 567 ? -20.431 56.388 -7.099 1.00 121.36 ? 567 THR A CG2 1 ATOM 4400 N N . ALA A 1 568 ? -16.227 57.569 -8.803 1.00 144.22 ? 568 ALA A N 1 ATOM 4401 C CA . ALA A 1 568 ? -14.788 57.538 -8.683 1.00 142.39 ? 568 ALA A CA 1 ATOM 4402 C C . ALA A 1 568 ? -14.334 58.817 -7.983 1.00 127.15 ? 568 ALA A C 1 ATOM 4403 O O . ALA A 1 568 ? -13.803 58.774 -6.875 1.00 117.58 ? 568 ALA A O 1 ATOM 4404 C CB . ALA A 1 568 ? -14.123 57.382 -10.077 1.00 142.79 ? 568 ALA A CB 1 ATOM 4405 N N . ALA A 1 569 ? -14.636 59.943 -8.627 1.00 136.70 ? 569 ALA A N 1 ATOM 4406 C CA . ALA A 1 569 ? -13.948 61.228 -8.497 1.00 157.85 ? 569 ALA A CA 1 ATOM 4407 C C . ALA A 1 569 ? -12.565 61.032 -9.099 1.00 170.43 ? 569 ALA A C 1 ATOM 4408 O O . ALA A 1 569 ? -11.622 61.776 -8.825 1.00 161.46 ? 569 ALA A O 1 ATOM 4409 C CB . ALA A 1 569 ? -13.875 61.720 -7.029 1.00 151.49 ? 569 ALA A CB 1 ATOM 4410 N N . ASP A 1 570 ? -12.490 60.020 -9.960 1.00 178.76 ? 570 ASP A N 1 ATOM 4411 C CA . ASP A 1 570 ? -11.285 59.581 -10.658 1.00 178.51 ? 570 ASP A CA 1 ATOM 4412 C C . ASP A 1 570 ? -10.216 59.076 -9.700 1.00 167.59 ? 570 ASP A C 1 ATOM 4413 O O . ASP A 1 570 ? -9.187 58.580 -10.142 1.00 173.06 ? 570 ASP A O 1 ATOM 4414 C CB . ASP A 1 570 ? -10.724 60.677 -11.574 1.00 177.41 ? 570 ASP A CB 1 ATOM 4415 C CG . ASP A 1 570 ? -9.972 60.093 -12.757 1.00 176.12 ? 570 ASP A CG 1 ATOM 4416 O OD1 . ASP A 1 570 ? -10.121 58.868 -12.980 1.00 184.06 ? 570 ASP A OD1 1 ATOM 4417 O OD2 . ASP A 1 570 ? -9.238 60.828 -13.450 1.00 160.99 ? 570 ASP A OD2 1 ATOM 4418 N N . THR A 1 571 ? -10.459 59.162 -8.393 1.00 158.92 ? 571 THR A N 1 ATOM 4419 C CA . THR A 1 571 ? -9.439 58.688 -7.461 1.00 164.38 ? 571 THR A CA 1 ATOM 4420 C C . THR A 1 571 ? -9.523 57.166 -7.460 1.00 143.63 ? 571 THR A C 1 ATOM 4421 O O . THR A 1 571 ? -10.445 56.578 -6.878 1.00 125.49 ? 571 THR A O 1 ATOM 4422 C CB . THR A 1 571 ? -9.641 59.279 -6.063 1.00 167.91 ? 571 THR A CB 1 ATOM 4423 O OG1 . THR A 1 571 ? -9.177 60.638 -6.058 1.00 172.88 ? 571 THR A OG1 1 ATOM 4424 C CG2 . THR A 1 571 ? -8.876 58.484 -5.003 1.00 159.96 ? 571 THR A CG2 1 ATOM 4425 N N . THR A 1 572 ? -8.495 56.563 -8.070 1.00 145.50 ? 572 THR A N 1 ATOM 4426 C CA . THR A 1 572 ? -8.465 55.133 -8.302 1.00 153.48 ? 572 THR A CA 1 ATOM 4427 C C . THR A 1 572 ? -9.848 54.810 -8.844 1.00 156.73 ? 572 THR A C 1 ATOM 4428 O O . THR A 1 572 ? -10.210 55.226 -9.938 1.00 145.56 ? 572 THR A O 1 ATOM 4429 C CB . THR A 1 572 ? -8.108 54.313 -7.027 1.00 175.37 ? 572 THR A CB 1 ATOM 4430 O OG1 . THR A 1 572 ? -7.028 54.942 -6.329 1.00 177.23 ? 572 THR A OG1 1 ATOM 4431 C CG2 . THR A 1 572 ? -7.683 52.903 -7.416 1.00 170.33 ? 572 THR A CG2 1 ATOM 4432 N N . GLY A 1 573 ? -10.623 54.086 -8.045 1.00 154.51 ? 573 GLY A N 1 ATOM 4433 C CA . GLY A 1 573 ? -12.072 54.204 -8.092 1.00 146.41 ? 573 GLY A CA 1 ATOM 4434 C C . GLY A 1 573 ? -12.439 53.927 -6.654 1.00 134.20 ? 573 GLY A C 1 ATOM 4435 O O . GLY A 1 573 ? -11.796 53.112 -6.013 1.00 135.23 ? 573 GLY A O 1 ATOM 4436 N N . LEU A 1 574 ? -13.490 54.560 -6.150 1.00 128.07 ? 574 LEU A N 1 ATOM 4437 C CA . LEU A 1 574 ? -13.960 54.287 -4.790 1.00 124.85 ? 574 LEU A CA 1 ATOM 4438 C C . LEU A 1 574 ? -15.470 54.252 -4.786 1.00 124.97 ? 574 LEU A C 1 ATOM 4439 O O . LEU A 1 574 ? -16.121 55.240 -5.113 1.00 134.46 ? 574 LEU A O 1 ATOM 4440 C CB . LEU A 1 574 ? -13.456 55.332 -3.776 1.00 114.69 ? 574 LEU A CB 1 ATOM 4441 C CG . LEU A 1 574 ? -13.391 54.925 -2.284 1.00 105.23 ? 574 LEU A CG 1 ATOM 4442 C CD1 . LEU A 1 574 ? -12.309 53.887 -2.066 1.00 104.69 ? 574 LEU A CD1 1 ATOM 4443 C CD2 . LEU A 1 574 ? -13.147 56.140 -1.406 1.00 102.19 ? 574 LEU A CD2 1 ATOM 4444 N N . GLN A 1 575 ? -16.032 53.105 -4.438 1.00 114.58 ? 575 GLN A N 1 ATOM 4445 C CA . GLN A 1 575 ? -17.478 52.941 -4.479 1.00 117.00 ? 575 GLN A CA 1 ATOM 4446 C C . GLN A 1 575 ? -18.076 53.133 -3.098 1.00 115.51 ? 575 GLN A C 1 ATOM 4447 O O . GLN A 1 575 ? -17.663 52.473 -2.146 1.00 136.00 ? 575 GLN A O 1 ATOM 4448 C CB . GLN A 1 575 ? -17.852 51.561 -5.012 1.00 143.06 ? 575 GLN A CB 1 ATOM 4449 C CG . GLN A 1 575 ? -16.795 50.951 -5.914 1.00 144.96 ? 575 GLN A CG 1 ATOM 4450 C CD . GLN A 1 575 ? -17.139 49.539 -6.345 1.00 141.58 ? 575 GLN A CD 1 ATOM 4451 O OE1 . GLN A 1 575 ? -18.178 48.990 -5.968 1.00 147.76 ? 575 GLN A OE1 1 ATOM 4452 N NE2 . GLN A 1 575 ? -16.264 48.941 -7.140 1.00 138.43 ? 575 GLN A NE2 1 ATOM 4453 N N . PRO A 1 576 ? -19.051 54.042 -2.977 1.00 108.53 ? 576 PRO A N 1 ATOM 4454 C CA . PRO A 1 576 ? -19.726 54.210 -1.691 1.00 105.38 ? 576 PRO A CA 1 ATOM 4455 C C . PRO A 1 576 ? -20.588 53.001 -1.369 1.00 107.42 ? 576 PRO A C 1 ATOM 4456 O O . PRO A 1 576 ? -21.108 52.360 -2.281 1.00 114.50 ? 576 PRO A O 1 ATOM 4457 C CB . PRO A 1 576 ? -20.588 55.456 -1.907 1.00 104.60 ? 576 PRO A CB 1 ATOM 4458 C CG . PRO A 1 576 ? -20.850 55.466 -3.371 1.00 107.67 ? 576 PRO A CG 1 ATOM 4459 C CD . PRO A 1 576 ? -19.578 54.964 -3.995 1.00 109.51 ? 576 PRO A CD 1 ATOM 4460 N N . ILE A 1 577 ? -20.727 52.689 -0.088 1.00 102.28 ? 577 ILE A N 1 ATOM 4461 C CA . ILE A 1 577 ? -21.600 51.606 0.327 1.00 105.31 ? 577 ILE A CA 1 ATOM 4462 C C . ILE A 1 577 ? -22.817 52.194 1.035 1.00 108.19 ? 577 ILE A C 1 ATOM 4463 O O . ILE A 1 577 ? -22.728 53.244 1.673 1.00 108.06 ? 577 ILE A O 1 ATOM 4464 C CB . ILE A 1 577 ? -20.866 50.601 1.247 1.00 110.04 ? 577 ILE A CB 1 ATOM 4465 C CG1 . ILE A 1 577 ? -21.707 49.337 1.450 1.00 131.56 ? 577 ILE A CG1 1 ATOM 4466 C CG2 . ILE A 1 577 ? -20.494 51.248 2.576 1.00 107.78 ? 577 ILE A CG2 1 ATOM 4467 C CD1 . ILE A 1 577 ? -22.107 48.656 0.158 1.00 123.33 ? 577 ILE A CD1 1 ATOM 4468 N N . LEU A 1 578 ? -23.957 51.524 0.901 1.00 102.70 ? 578 LEU A N 1 ATOM 4469 C CA . LEU A 1 578 ? -25.186 51.971 1.541 1.00 100.73 ? 578 LEU A CA 1 ATOM 4470 C C . LEU A 1 578 ? -25.046 51.871 3.053 1.00 101.27 ? 578 LEU A C 1 ATOM 4471 O O . LEU A 1 578 ? -24.166 51.167 3.552 1.00 101.03 ? 578 LEU A O 1 ATOM 4472 C CB . LEU A 1 578 ? -26.386 51.148 1.061 1.00 100.48 ? 578 LEU A CB 1 ATOM 4473 C CG . LEU A 1 578 ? -26.826 51.275 -0.401 1.00 104.96 ? 578 LEU A CG 1 ATOM 4474 C CD1 . LEU A 1 578 ? -25.943 50.456 -1.335 1.00 112.78 ? 578 LEU A CD1 1 ATOM 4475 C CD2 . LEU A 1 578 ? -28.284 50.874 -0.556 1.00 111.88 ? 578 LEU A CD2 1 ATOM 4476 N N . ASN A 1 579 ? -25.899 52.594 3.772 1.00 103.84 ? 579 ASN A N 1 ATOM 4477 C CA . ASN A 1 579 ? -25.901 52.564 5.230 1.00 93.88 ? 579 ASN A CA 1 ATOM 4478 C C . ASN A 1 579 ? -25.984 51.128 5.732 1.00 94.38 ? 579 ASN A C 1 ATOM 4479 O O . ASN A 1 579 ? -26.740 50.320 5.190 1.00 97.12 ? 579 ASN A O 1 ATOM 4480 C CB . ASN A 1 579 ? -27.065 53.395 5.777 1.00 117.36 ? 579 ASN A CB 1 ATOM 4481 C CG . ASN A 1 579 ? -26.955 53.653 7.270 1.00 126.47 ? 579 ASN A CG 1 ATOM 4482 O OD1 . ASN A 1 579 ? -26.654 52.753 8.054 1.00 122.54 ? 579 ASN A OD1 1 ATOM 4483 N ND2 . ASN A 1 579 ? -27.201 54.896 7.670 1.00 125.76 ? 579 ASN A ND2 1 ATOM 4484 N N . GLN A 1 580 ? -25.187 50.823 6.754 1.00 111.63 ? 580 GLN A N 1 ATOM 4485 C CA . GLN A 1 580 ? -25.079 49.474 7.303 1.00 106.36 ? 580 GLN A CA 1 ATOM 4486 C C . GLN A 1 580 ? -26.445 48.859 7.579 1.00 104.43 ? 580 GLN A C 1 ATOM 4487 O O . GLN A 1 580 ? -26.821 47.860 6.965 1.00 95.04 ? 580 GLN A O 1 ATOM 4488 C CB . GLN A 1 580 ? -24.245 49.486 8.584 1.00 107.39 ? 580 GLN A CB 1 ATOM 4489 C CG . GLN A 1 580 ? -23.963 48.104 9.146 1.00 110.92 ? 580 GLN A CG 1 ATOM 4490 C CD . GLN A 1 580 ? -23.185 48.154 10.445 1.00 122.73 ? 580 GLN A CD 1 ATOM 4491 O OE1 . GLN A 1 580 ? -22.946 49.227 11.000 1.00 118.02 ? 580 GLN A OE1 1 ATOM 4492 N NE2 . GLN A 1 580 ? -22.783 46.987 10.938 1.00 115.42 ? 580 GLN A NE2 1 ATOM 4493 N N . PHE A 1 581 ? -27.188 49.460 8.501 1.00 121.83 ? 581 PHE A N 1 ATOM 4494 C CA . PHE A 1 581 ? -28.548 49.017 8.769 1.00 132.06 ? 581 PHE A CA 1 ATOM 4495 C C . PHE A 1 581 ? -29.528 49.815 7.920 1.00 136.81 ? 581 PHE A C 1 ATOM 4496 O O . PHE A 1 581 ? -29.718 51.014 8.131 1.00 152.25 ? 581 PHE A O 1 ATOM 4497 C CB . PHE A 1 581 ? -28.886 49.155 10.253 1.00 132.51 ? 581 PHE A CB 1 ATOM 4498 C CG . PHE A 1 581 ? -28.121 48.212 11.135 1.00 130.77 ? 581 PHE A CG 1 ATOM 4499 C CD1 . PHE A 1 581 ? -27.037 48.656 11.872 1.00 130.48 ? 581 PHE A CD1 1 ATOM 4500 C CD2 . PHE A 1 581 ? -28.479 46.875 11.217 1.00 112.88 ? 581 PHE A CD2 1 ATOM 4501 C CE1 . PHE A 1 581 ? -26.330 47.787 12.682 1.00 115.00 ? 581 PHE A CE1 1 ATOM 4502 C CE2 . PHE A 1 581 ? -27.775 46.002 12.023 1.00 122.33 ? 581 PHE A CE2 1 ATOM 4503 C CZ . PHE A 1 581 ? -26.698 46.458 12.757 1.00 118.12 ? 581 PHE A CZ 1 ATOM 4504 N N . THR A 1 582 ? -30.156 49.124 6.973 1.00 114.21 ? 582 THR A N 1 ATOM 4505 C CA . THR A 1 582 ? -31.058 49.729 6.002 1.00 112.77 ? 582 THR A CA 1 ATOM 4506 C C . THR A 1 582 ? -31.631 48.628 5.120 1.00 122.82 ? 582 THR A C 1 ATOM 4507 O O . THR A 1 582 ? -30.896 47.752 4.662 1.00 129.39 ? 582 THR A O 1 ATOM 4508 C CB . THR A 1 582 ? -30.333 50.782 5.119 1.00 121.46 ? 582 THR A CB 1 ATOM 4509 O OG1 . THR A 1 582 ? -30.116 51.980 5.877 1.00 121.77 ? 582 THR A OG1 1 ATOM 4510 C CG2 . THR A 1 582 ? -31.145 51.121 3.877 1.00 119.54 ? 582 THR A CG2 1 ATOM 4511 N N . PRO A 1 583 ? -32.949 48.665 4.878 1.00 121.75 ? 583 PRO A N 1 ATOM 4512 C CA . PRO A 1 583 ? -33.573 47.658 4.017 1.00 111.28 ? 583 PRO A CA 1 ATOM 4513 C C . PRO A 1 583 ? -33.464 47.788 2.503 1.00 112.48 ? 583 PRO A C 1 ATOM 4514 O O . PRO A 1 583 ? -33.853 48.811 1.946 1.00 113.55 ? 583 PRO A O 1 ATOM 4515 C CB . PRO A 1 583 ? -35.070 47.882 4.245 1.00 125.93 ? 583 PRO A CB 1 ATOM 4516 C CG . PRO A 1 583 ? -35.176 49.310 4.657 1.00 131.43 ? 583 PRO A CG 1 ATOM 4517 C CD . PRO A 1 583 ? -33.939 49.589 5.459 1.00 121.24 ? 583 PRO A CD 1 ATOM 4518 N N . ALA A 1 584 ? -32.939 46.757 1.852 1.00 124.30 ? 584 ALA A N 1 ATOM 4519 C CA . ALA A 1 584 ? -32.679 46.814 0.420 1.00 125.39 ? 584 ALA A CA 1 ATOM 4520 C C . ALA A 1 584 ? -33.991 46.664 -0.333 1.00 118.28 ? 584 ALA A C 1 ATOM 4521 O O . ALA A 1 584 ? -34.029 46.731 -1.562 1.00 112.30 ? 584 ALA A O 1 ATOM 4522 C CB . ALA A 1 584 ? -31.695 45.734 0.007 1.00 142.89 ? 584 ALA A CB 1 ATOM 4523 N N . ASN A 1 585 ? -35.067 46.461 0.421 1.00 125.09 ? 585 ASN A N 1 ATOM 4524 C CA . ASN A 1 585 ? -36.382 46.251 -0.163 1.00 110.71 ? 585 ASN A CA 1 ATOM 4525 C C . ASN A 1 585 ? -37.517 46.709 0.750 1.00 104.12 ? 585 ASN A C 1 ATOM 4526 O O . ASN A 1 585 ? -37.360 46.781 1.968 1.00 100.33 ? 585 ASN A O 1 ATOM 4527 C CB . ASN A 1 585 ? -36.567 44.774 -0.517 1.00 111.12 ? 585 ASN A CB 1 ATOM 4528 C CG . ASN A 1 585 ? -36.520 43.870 0.699 1.00 129.98 ? 585 ASN A CG 1 ATOM 4529 O OD1 . ASN A 1 585 ? -37.476 43.794 1.471 1.00 125.91 ? 585 ASN A OD1 1 ATOM 4530 N ND2 . ASN A 1 585 ? -35.405 43.173 0.872 1.00 176.29 ? 585 ASN A ND2 1 ATOM 4531 N N . ILE A 1 586 ? -38.660 47.016 0.145 1.00 105.16 ? 586 ILE A N 1 ATOM 4532 C CA . ILE A 1 586 ? -39.859 47.378 0.891 1.00 103.72 ? 586 ILE A CA 1 ATOM 4533 C C . ILE A 1 586 ? -41.071 46.720 0.236 1.00 105.40 ? 586 ILE A C 1 ATOM 4534 O O . ILE A 1 586 ? -41.075 46.477 -0.972 1.00 107.81 ? 586 ILE A O 1 ATOM 4535 C CB . ILE A 1 586 ? -40.053 48.912 0.962 1.00 110.86 ? 586 ILE A CB 1 ATOM 4536 C CG1 . ILE A 1 586 ? -41.095 49.277 2.021 1.00 125.47 ? 586 ILE A CG1 1 ATOM 4537 C CG2 . ILE A 1 586 ? -40.431 49.479 -0.403 1.00 106.77 ? 586 ILE A CG2 1 ATOM 4538 C CD1 . ILE A 1 586 ? -40.735 48.817 3.418 1.00 127.56 ? 586 ILE A CD1 1 ATOM 4539 N N . SER A 1 587 ? -42.092 46.419 1.031 1.00 104.14 ? 587 SER A N 1 ATOM 4540 C CA . SER A 1 587 ? -43.247 45.694 0.519 1.00 105.27 ? 587 SER A CA 1 ATOM 4541 C C . SER A 1 587 ? -44.582 46.323 0.911 1.00 105.11 ? 587 SER A C 1 ATOM 4542 O O . SER A 1 587 ? -44.741 46.849 2.012 1.00 102.69 ? 587 SER A O 1 ATOM 4543 C CB . SER A 1 587 ? -43.207 44.241 0.997 1.00 113.40 ? 587 SER A CB 1 ATOM 4544 O OG . SER A 1 587 ? -42.082 43.563 0.467 1.00 135.47 ? 587 SER A OG 1 ATOM 4545 N N . ARG A 1 588 ? -45.535 46.264 -0.013 1.00 114.68 ? 588 ARG A N 1 ATOM 4546 C CA . ARG A 1 588 ? -46.909 46.676 0.248 1.00 107.44 ? 588 ARG A CA 1 ATOM 4547 C C . ARG A 1 588 ? -47.849 45.558 -0.183 1.00 107.32 ? 588 ARG A C 1 ATOM 4548 O O . ARG A 1 588 ? -47.470 44.694 -0.973 1.00 107.51 ? 588 ARG A O 1 ATOM 4549 C CB . ARG A 1 588 ? -47.244 47.976 -0.485 1.00 110.40 ? 588 ARG A CB 1 ATOM 4550 C CG . ARG A 1 588 ? -46.625 49.225 0.131 1.00 114.68 ? 588 ARG A CG 1 ATOM 4551 C CD . ARG A 1 588 ? -47.238 49.537 1.489 1.00 127.90 ? 588 ARG A CD 1 ATOM 4552 N NE . ARG A 1 588 ? -46.684 50.753 2.078 1.00 136.66 ? 588 ARG A NE 1 ATOM 4553 C CZ . ARG A 1 588 ? -45.681 50.772 2.949 1.00 134.93 ? 588 ARG A CZ 1 ATOM 4554 N NH1 . ARG A 1 588 ? -45.115 49.638 3.339 1.00 122.74 ? 588 ARG A NH1 1 ATOM 4555 N NH2 . ARG A 1 588 ? -45.242 51.927 3.432 1.00 141.84 ? 588 ARG A NH2 1 ATOM 4556 N N . GLN A 1 589 ? -49.072 45.571 0.335 1.00 110.26 ? 589 GLN A N 1 ATOM 4557 C CA . GLN A 1 589 ? -50.026 44.508 0.032 1.00 106.28 ? 589 GLN A CA 1 ATOM 4558 C C . GLN A 1 589 ? -51.353 45.031 -0.505 1.00 108.12 ? 589 GLN A C 1 ATOM 4559 O O . GLN A 1 589 ? -51.877 46.042 -0.036 1.00 108.88 ? 589 GLN A O 1 ATOM 4560 C CB . GLN A 1 589 ? -50.276 43.648 1.273 1.00 103.13 ? 589 GLN A CB 1 ATOM 4561 C CG . GLN A 1 589 ? -49.104 42.762 1.661 1.00 101.55 ? 589 GLN A CG 1 ATOM 4562 C CD . GLN A 1 589 ? -49.433 41.826 2.808 1.00 102.77 ? 589 GLN A CD 1 ATOM 4563 O OE1 . GLN A 1 589 ? -50.512 41.903 3.396 1.00 98.54 ? 589 GLN A OE1 1 ATOM 4564 N NE2 . GLN A 1 589 ? -48.503 40.935 3.130 1.00 114.48 ? 589 GLN A NE2 1 ATOM 4565 N N . ALA A 1 590 ? -51.885 44.326 -1.497 1.00 108.47 ? 590 ALA A N 1 ATOM 4566 C CA . ALA A 1 590 ? -53.203 44.619 -2.042 1.00 109.55 ? 590 ALA A CA 1 ATOM 4567 C C . ALA A 1 590 ? -54.154 43.473 -1.719 1.00 108.29 ? 590 ALA A C 1 ATOM 4568 O O . ALA A 1 590 ? -53.730 42.322 -1.613 1.00 106.86 ? 590 ALA A O 1 ATOM 4569 C CB . ALA A 1 590 ? -53.127 44.846 -3.543 1.00 111.22 ? 590 ALA A CB 1 ATOM 4570 N N . HIS A 1 591 ? -55.434 43.785 -1.558 1.00 109.27 ? 591 HIS A N 1 ATOM 4571 C CA . HIS A 1 591 ? -56.422 42.768 -1.217 1.00 107.31 ? 591 HIS A CA 1 ATOM 4572 C C . HIS A 1 591 ? -57.606 42.779 -2.179 1.00 108.31 ? 591 HIS A C 1 ATOM 4573 O O . HIS A 1 591 ? -58.143 43.836 -2.504 1.00 109.63 ? 591 HIS A O 1 ATOM 4574 C CB . HIS A 1 591 ? -56.918 42.963 0.218 1.00 106.19 ? 591 HIS A CB 1 ATOM 4575 C CG . HIS A 1 591 ? -55.855 42.784 1.257 1.00 110.27 ? 591 HIS A CG 1 ATOM 4576 N ND1 . HIS A 1 591 ? -54.863 43.716 1.477 1.00 132.55 ? 591 HIS A ND1 1 ATOM 4577 C CD2 . HIS A 1 591 ? -55.630 41.780 2.139 1.00 106.78 ? 591 HIS A CD2 1 ATOM 4578 C CE1 . HIS A 1 591 ? -54.073 43.294 2.449 1.00 127.77 ? 591 HIS A CE1 1 ATOM 4579 N NE2 . HIS A 1 591 ? -54.516 42.122 2.868 1.00 111.70 ? 591 HIS A NE2 1 ATOM 4580 N N . ILE A 1 592 ? -58.003 41.595 -2.633 1.00 108.17 ? 592 ILE A N 1 ATOM 4581 C CA . ILE A 1 592 ? -59.187 41.453 -3.471 1.00 109.07 ? 592 ILE A CA 1 ATOM 4582 C C . ILE A 1 592 ? -60.431 41.597 -2.602 1.00 108.52 ? 592 ILE A C 1 ATOM 4583 O O . ILE A 1 592 ? -60.464 41.093 -1.479 1.00 112.37 ? 592 ILE A O 1 ATOM 4584 C CB . ILE A 1 592 ? -59.206 40.098 -4.204 1.00 108.74 ? 592 ILE A CB 1 ATOM 4585 C CG1 . ILE A 1 592 ? -57.882 39.873 -4.938 1.00 109.07 ? 592 ILE A CG1 1 ATOM 4586 C CG2 . ILE A 1 592 ? -60.375 40.025 -5.174 1.00 112.52 ? 592 ILE A CG2 1 ATOM 4587 C CD1 . ILE A 1 592 ? -57.820 38.572 -5.707 1.00 108.81 ? 592 ILE A CD1 1 ATOM 4588 N N . LEU A 1 593 ? -61.447 42.286 -3.113 1.00 109.39 ? 593 LEU A N 1 ATOM 4589 C CA . LEU A 1 593 ? -62.650 42.543 -2.331 1.00 109.08 ? 593 LEU A CA 1 ATOM 4590 C C . LEU A 1 593 ? -63.431 41.248 -2.124 1.00 108.04 ? 593 LEU A C 1 ATOM 4591 O O . LEU A 1 593 ? -63.838 40.597 -3.086 1.00 116.11 ? 593 LEU A O 1 ATOM 4592 C CB . LEU A 1 593 ? -63.520 43.597 -3.027 1.00 110.24 ? 593 LEU A CB 1 ATOM 4593 C CG . LEU A 1 593 ? -64.596 44.357 -2.244 1.00 110.15 ? 593 LEU A CG 1 ATOM 4594 C CD1 . LEU A 1 593 ? -64.965 45.636 -2.978 1.00 110.88 ? 593 LEU A CD1 1 ATOM 4595 C CD2 . LEU A 1 593 ? -65.842 43.511 -2.018 1.00 127.35 ? 593 LEU A CD2 1 ATOM 4596 N N . LEU A 1 594 ? -63.636 40.882 -0.862 1.00 106.23 ? 594 LEU A N 1 ATOM 4597 C CA . LEU A 1 594 ? -64.408 39.693 -0.521 1.00 104.95 ? 594 LEU A CA 1 ATOM 4598 C C . LEU A 1 594 ? -65.258 39.925 0.727 1.00 104.64 ? 594 LEU A C 1 ATOM 4599 O O . LEU A 1 594 ? -64.739 40.327 1.769 1.00 104.11 ? 594 LEU A O 1 ATOM 4600 C CB . LEU A 1 594 ? -63.478 38.495 -0.314 1.00 103.64 ? 594 LEU A CB 1 ATOM 4601 C CG . LEU A 1 594 ? -64.132 37.130 -0.095 1.00 103.87 ? 594 LEU A CG 1 ATOM 4602 C CD1 . LEU A 1 594 ? -64.979 36.737 -1.296 1.00 117.27 ? 594 LEU A CD1 1 ATOM 4603 C CD2 . LEU A 1 594 ? -63.081 36.068 0.192 1.00 101.89 ? 594 LEU A CD2 1 ATOM 4604 N N . ASP A 1 595 ? -66.556 39.653 0.611 1.00 107.03 ? 595 ASP A N 1 ATOM 4605 C CA . ASP A 1 595 ? -67.503 39.771 1.722 1.00 113.46 ? 595 ASP A CA 1 ATOM 4606 C C . ASP A 1 595 ? -67.412 41.100 2.473 1.00 114.26 ? 595 ASP A C 1 ATOM 4607 O O . ASP A 1 595 ? -67.339 41.119 3.701 1.00 108.99 ? 595 ASP A O 1 ATOM 4608 C CB . ASP A 1 595 ? -67.305 38.619 2.711 1.00 112.48 ? 595 ASP A CB 1 ATOM 4609 C CG . ASP A 1 595 ? -67.642 37.267 2.109 1.00 121.43 ? 595 ASP A CG 1 ATOM 4610 O OD1 . ASP A 1 595 ? -66.707 36.487 1.831 1.00 114.77 ? 595 ASP A OD1 1 ATOM 4611 O OD2 . ASP A 1 595 ? -68.843 36.986 1.914 1.00 113.48 ? 595 ASP A OD2 1 ATOM 4612 N N . CYS A 1 596 ? -67.416 42.207 1.735 1.00 116.47 ? 596 CYS A N 1 ATOM 4613 C CA . CYS A 1 596 ? -67.343 43.528 2.353 1.00 132.49 ? 596 CYS A CA 1 ATOM 4614 C C . CYS A 1 596 ? -68.725 44.151 2.548 1.00 136.69 ? 596 CYS A C 1 ATOM 4615 O O . CYS A 1 596 ? -68.843 45.281 3.021 1.00 145.95 ? 596 CYS A O 1 ATOM 4616 C CB . CYS A 1 596 ? -66.458 44.460 1.523 1.00 146.57 ? 596 CYS A CB 1 ATOM 4617 S SG . CYS A 1 596 ? -64.684 44.173 1.736 1.00 210.29 ? 596 CYS A SG 1 ATOM 4618 N N . GLY A 1 597 ? -69.766 43.412 2.178 1.00 132.55 ? 597 GLY A N 1 ATOM 4619 C CA . GLY A 1 597 ? -71.131 43.861 2.391 1.00 135.14 ? 597 GLY A CA 1 ATOM 4620 C C . GLY A 1 597 ? -71.675 44.751 1.290 1.00 123.94 ? 597 GLY A C 1 ATOM 4621 O O . GLY A 1 597 ? -71.045 44.924 0.246 1.00 117.07 ? 597 GLY A O 1 ATOM 4622 N N . GLU A 1 598 ? -72.853 45.321 1.530 1.00 121.45 ? 598 GLU A N 1 ATOM 4623 C CA . GLU A 1 598 ? -73.525 46.161 0.543 1.00 122.88 ? 598 GLU A CA 1 ATOM 4624 C C . GLU A 1 598 ? -72.818 47.501 0.361 1.00 130.74 ? 598 GLU A C 1 ATOM 4625 O O . GLU A 1 598 ? -72.991 48.172 -0.657 1.00 143.82 ? 598 GLU A O 1 ATOM 4626 C CB . GLU A 1 598 ? -74.981 46.394 0.948 1.00 125.52 ? 598 GLU A CB 1 ATOM 4627 C CG . GLU A 1 598 ? -75.757 45.118 1.239 1.00 149.57 ? 598 GLU A CG 1 ATOM 4628 C CD . GLU A 1 598 ? -77.198 45.382 1.630 1.00 156.44 ? 598 GLU A CD 1 ATOM 4629 O OE1 . GLU A 1 598 ? -77.860 44.448 2.129 1.00 155.13 ? 598 GLU A OE1 1 ATOM 4630 O OE2 . GLU A 1 598 ? -77.671 46.523 1.437 1.00 147.64 ? 598 GLU A OE2 1 ATOM 4631 N N . ASP A 1 599 ? -72.023 47.884 1.355 1.00 130.26 ? 599 ASP A N 1 ATOM 4632 C CA . ASP A 1 599 ? -71.297 49.149 1.315 1.00 112.11 ? 599 ASP A CA 1 ATOM 4633 C C . ASP A 1 599 ? -70.067 49.070 0.413 1.00 112.60 ? 599 ASP A C 1 ATOM 4634 O O . ASP A 1 599 ? -69.430 50.087 0.132 1.00 108.69 ? 599 ASP A O 1 ATOM 4635 C CB . ASP A 1 599 ? -70.886 49.569 2.730 1.00 114.92 ? 599 ASP A CB 1 ATOM 4636 C CG . ASP A 1 599 ? -70.209 48.449 3.502 1.00 140.33 ? 599 ASP A CG 1 ATOM 4637 O OD1 . ASP A 1 599 ? -69.668 47.520 2.867 1.00 132.52 ? 599 ASP A OD1 1 ATOM 4638 O OD2 . ASP A 1 599 ? -70.216 48.496 4.751 1.00 151.37 ? 599 ASP A OD2 1 ATOM 4639 N N . ASN A 1 600 ? -69.744 47.856 -0.029 1.00 136.37 ? 600 ASN A N 1 ATOM 4640 C CA . ASN A 1 600 ? -68.539 47.585 -0.812 1.00 134.47 ? 600 ASN A CA 1 ATOM 4641 C C . ASN A 1 600 ? -67.269 48.041 -0.096 1.00 130.92 ? 600 ASN A C 1 ATOM 4642 O O . ASN A 1 600 ? -66.279 48.400 -0.734 1.00 132.27 ? 600 ASN A O 1 ATOM 4643 C CB . ASN A 1 600 ? -68.629 48.244 -2.193 1.00 125.90 ? 600 ASN A CB 1 ATOM 4644 C CG . ASN A 1 600 ? -69.544 47.490 -3.141 1.00 134.17 ? 600 ASN A CG 1 ATOM 4645 O OD1 . ASN A 1 600 ? -69.673 46.268 -3.056 1.00 134.13 ? 600 ASN A OD1 1 ATOM 4646 N ND2 . ASN A 1 600 ? -70.180 48.217 -4.052 1.00 137.45 ? 600 ASN A ND2 1 ATOM 4647 N N . VAL A 1 601 ? -67.309 48.024 1.232 1.00 126.75 ? 601 VAL A N 1 ATOM 4648 C CA . VAL A 1 601 ? -66.149 48.358 2.051 1.00 133.01 ? 601 VAL A CA 1 ATOM 4649 C C . VAL A 1 601 ? -66.218 47.569 3.359 1.00 123.93 ? 601 VAL A C 1 ATOM 4650 O O . VAL A 1 601 ? -67.301 47.336 3.897 1.00 105.72 ? 601 VAL A O 1 ATOM 4651 C CB . VAL A 1 601 ? -66.066 49.881 2.334 1.00 106.87 ? 601 VAL A CB 1 ATOM 4652 C CG1 . VAL A 1 601 ? -67.294 50.361 3.096 1.00 105.87 ? 601 VAL A CG1 1 ATOM 4653 C CG2 . VAL A 1 601 ? -64.791 50.226 3.090 1.00 105.89 ? 601 VAL A CG2 1 ATOM 4654 N N . CYS A 1 602 ? -65.063 47.141 3.858 1.00 107.79 ? 602 CYS A N 1 ATOM 4655 C CA . CYS A 1 602 ? -65.014 46.342 5.077 1.00 105.15 ? 602 CYS A CA 1 ATOM 4656 C C . CYS A 1 602 ? -64.853 47.211 6.325 1.00 105.48 ? 602 CYS A C 1 ATOM 4657 O O . CYS A 1 602 ? -63.908 47.994 6.435 1.00 114.96 ? 602 CYS A O 1 ATOM 4658 C CB . CYS A 1 602 ? -63.884 45.314 4.993 1.00 108.69 ? 602 CYS A CB 1 ATOM 4659 S SG . CYS A 1 602 ? -64.107 44.082 3.682 1.00 108.51 ? 602 CYS A SG 1 ATOM 4660 N N . LYS A 1 603 ? -65.788 47.062 7.259 1.00 109.94 ? 603 LYS A N 1 ATOM 4661 C CA . LYS A 1 603 ? -65.781 47.821 8.506 1.00 119.19 ? 603 LYS A CA 1 ATOM 4662 C C . LYS A 1 603 ? -65.769 46.886 9.710 1.00 115.42 ? 603 LYS A C 1 ATOM 4663 O O . LYS A 1 603 ? -66.825 46.488 10.201 1.00 108.72 ? 603 LYS A O 1 ATOM 4664 C CB . LYS A 1 603 ? -66.995 48.749 8.582 1.00 121.72 ? 603 LYS A CB 1 ATOM 4665 C CG . LYS A 1 603 ? -66.948 49.940 7.642 1.00 110.23 ? 603 LYS A CG 1 ATOM 4666 C CD . LYS A 1 603 ? -68.291 50.653 7.612 1.00 128.47 ? 603 LYS A CD 1 ATOM 4667 C CE . LYS A 1 603 ? -68.214 51.969 6.856 1.00 142.30 ? 603 LYS A CE 1 ATOM 4668 N NZ . LYS A 1 603 ? -67.502 53.017 7.638 1.00 130.09 ? 603 LYS A NZ 1 ATOM 4669 N N . PRO A 1 604 ? -64.568 46.531 10.188 1.00 114.67 ? 604 PRO A N 1 ATOM 4670 C CA . PRO A 1 604 ? -64.400 45.590 11.301 1.00 102.54 ? 604 PRO A CA 1 ATOM 4671 C C . PRO A 1 604 ? -64.833 46.164 12.647 1.00 107.39 ? 604 PRO A C 1 ATOM 4672 O O . PRO A 1 604 ? -64.719 47.368 12.878 1.00 128.52 ? 604 PRO A O 1 ATOM 4673 C CB . PRO A 1 604 ? -62.889 45.311 11.307 1.00 102.09 ? 604 PRO A CB 1 ATOM 4674 C CG . PRO A 1 604 ? -62.375 45.841 10.005 1.00 101.91 ? 604 PRO A CG 1 ATOM 4675 C CD . PRO A 1 604 ? -63.274 46.970 9.644 1.00 107.59 ? 604 PRO A CD 1 ATOM 4676 N N . LYS A 1 605 ? -65.327 45.296 13.522 1.00 103.47 ? 605 LYS A N 1 ATOM 4677 C CA . LYS A 1 605 ? -65.599 45.667 14.904 1.00 116.80 ? 605 LYS A CA 1 ATOM 4678 C C . LYS A 1 605 ? -64.639 44.898 15.804 1.00 114.24 ? 605 LYS A C 1 ATOM 4679 O O . LYS A 1 605 ? -64.775 43.689 15.979 1.00 111.47 ? 605 LYS A O 1 ATOM 4680 C CB . LYS A 1 605 ? -67.054 45.372 15.271 1.00 126.55 ? 605 LYS A CB 1 ATOM 4681 C CG . LYS A 1 605 ? -67.491 45.935 16.614 1.00 139.22 ? 605 LYS A CG 1 ATOM 4682 C CD . LYS A 1 605 ? -68.982 45.726 16.829 1.00 142.18 ? 605 LYS A CD 1 ATOM 4683 C CE . LYS A 1 605 ? -69.459 46.389 18.111 1.00 138.12 ? 605 LYS A CE 1 ATOM 4684 N NZ . LYS A 1 605 ? -68.815 45.804 19.318 1.00 141.35 ? 605 LYS A NZ 1 ATOM 4685 N N . LEU A 1 606 ? -63.675 45.607 16.380 1.00 114.81 ? 606 LEU A N 1 ATOM 4686 C CA . LEU A 1 606 ? -62.568 44.958 17.072 1.00 115.80 ? 606 LEU A CA 1 ATOM 4687 C C . LEU A 1 606 ? -62.623 45.162 18.582 1.00 124.00 ? 606 LEU A C 1 ATOM 4688 O O . LEU A 1 606 ? -62.821 46.277 19.064 1.00 134.57 ? 606 LEU A O 1 ATOM 4689 C CB . LEU A 1 606 ? -61.237 45.475 16.519 1.00 110.51 ? 606 LEU A CB 1 ATOM 4690 C CG . LEU A 1 606 ? -61.031 45.296 15.013 1.00 102.43 ? 606 LEU A CG 1 ATOM 4691 C CD1 . LEU A 1 606 ? -59.816 46.073 14.536 1.00 105.29 ? 606 LEU A CD1 1 ATOM 4692 C CD2 . LEU A 1 606 ? -60.896 43.823 14.666 1.00 101.68 ? 606 LEU A CD2 1 ATOM 4693 N N . GLU A 1 607 ? -62.445 44.071 19.323 1.00 111.03 ? 607 GLU A N 1 ATOM 4694 C CA . GLU A 1 607 ? -62.480 44.111 20.780 1.00 108.98 ? 607 GLU A CA 1 ATOM 4695 C C . GLU A 1 607 ? -61.296 43.356 21.373 1.00 105.47 ? 607 GLU A C 1 ATOM 4696 O O . GLU A 1 607 ? -60.896 42.312 20.860 1.00 104.47 ? 607 GLU A O 1 ATOM 4697 C CB . GLU A 1 607 ? -63.792 43.520 21.301 1.00 127.48 ? 607 GLU A CB 1 ATOM 4698 C CG . GLU A 1 607 ? -65.039 44.199 20.758 1.00 148.09 ? 607 GLU A CG 1 ATOM 4699 C CD . GLU A 1 607 ? -66.314 43.490 21.164 1.00 146.46 ? 607 GLU A CD 1 ATOM 4700 O OE1 . GLU A 1 607 ? -66.253 42.607 22.045 1.00 146.29 ? 607 GLU A OE1 1 ATOM 4701 O OE2 . GLU A 1 607 ? -67.380 43.812 20.598 1.00 136.88 ? 607 GLU A OE2 1 ATOM 4702 N N . VAL A 1 608 ? -60.738 43.888 22.456 1.00 116.18 ? 608 VAL A N 1 ATOM 4703 C CA . VAL A 1 608 ? -59.605 43.252 23.117 1.00 109.01 ? 608 VAL A CA 1 ATOM 4704 C C . VAL A 1 608 ? -59.832 43.124 24.624 1.00 107.87 ? 608 VAL A C 1 ATOM 4705 O O . VAL A 1 608 ? -59.999 44.120 25.330 1.00 107.86 ? 608 VAL A O 1 ATOM 4706 C CB . VAL A 1 608 ? -58.292 44.023 22.852 1.00 109.30 ? 608 VAL A CB 1 ATOM 4707 C CG1 . VAL A 1 608 ? -58.514 45.528 22.958 1.00 124.82 ? 608 VAL A CG1 1 ATOM 4708 C CG2 . VAL A 1 608 ? -57.196 43.558 23.800 1.00 106.42 ? 608 VAL A CG2 1 ATOM 4709 N N . SER A 1 609 ? -59.844 41.885 25.107 1.00 109.36 ? 609 SER A N 1 ATOM 4710 C CA . SER A 1 609 ? -60.049 41.618 26.526 1.00 107.18 ? 609 SER A CA 1 ATOM 4711 C C . SER A 1 609 ? -58.794 41.013 27.146 1.00 106.92 ? 609 SER A C 1 ATOM 4712 O O . SER A 1 609 ? -58.039 40.307 26.477 1.00 105.97 ? 609 SER A O 1 ATOM 4713 C CB . SER A 1 609 ? -61.242 40.686 26.734 1.00 111.92 ? 609 SER A CB 1 ATOM 4714 O OG . SER A 1 609 ? -62.429 41.249 26.199 1.00 114.01 ? 609 SER A OG 1 ATOM 4715 N N . VAL A 1 610 ? -58.577 41.297 28.426 1.00 111.64 ? 610 VAL A N 1 ATOM 4716 C CA . VAL A 1 610 ? -57.402 40.805 29.138 1.00 111.68 ? 610 VAL A CA 1 ATOM 4717 C C . VAL A 1 610 ? -57.740 40.545 30.606 1.00 121.74 ? 610 VAL A C 1 ATOM 4718 O O . VAL A 1 610 ? -58.489 41.305 31.220 1.00 133.27 ? 610 VAL A O 1 ATOM 4719 C CB . VAL A 1 610 ? -56.231 41.806 29.023 1.00 108.17 ? 610 VAL A CB 1 ATOM 4720 C CG1 . VAL A 1 610 ? -56.685 43.210 29.399 1.00 118.84 ? 610 VAL A CG1 1 ATOM 4721 C CG2 . VAL A 1 610 ? -55.038 41.365 29.865 1.00 108.41 ? 610 VAL A CG2 1 ATOM 4722 N N . ASP A 1 611 ? -57.192 39.471 31.169 1.00 127.83 ? 611 ASP A N 1 ATOM 4723 C CA . ASP A 1 611 ? -57.487 39.119 32.553 1.00 142.50 ? 611 ASP A CA 1 ATOM 4724 C C . ASP A 1 611 ? -56.258 39.266 33.449 1.00 152.68 ? 611 ASP A C 1 ATOM 4725 O O . ASP A 1 611 ? -55.169 39.598 32.980 1.00 150.54 ? 611 ASP A O 1 ATOM 4726 C CB . ASP A 1 611 ? -58.033 37.692 32.636 1.00 146.75 ? 611 ASP A CB 1 ATOM 4727 C CG . ASP A 1 611 ? -59.078 37.532 33.722 1.00 150.42 ? 611 ASP A CG 1 ATOM 4728 O OD1 . ASP A 1 611 ? -58.960 38.203 34.769 1.00 132.26 ? 611 ASP A OD1 1 ATOM 4729 O OD2 . ASP A 1 611 ? -60.022 36.738 33.527 1.00 166.68 ? 611 ASP A OD2 1 ATOM 4730 N N . SER A 1 612 ? -56.444 39.009 34.740 1.00 158.99 ? 612 SER A N 1 ATOM 4731 C CA . SER A 1 612 ? -55.439 39.323 35.754 1.00 156.80 ? 612 SER A CA 1 ATOM 4732 C C . SER A 1 612 ? -54.281 38.333 35.848 1.00 152.31 ? 612 SER A C 1 ATOM 4733 O O . SER A 1 612 ? -53.120 38.744 35.923 1.00 142.46 ? 612 SER A O 1 ATOM 4734 C CB . SER A 1 612 ? -56.107 39.432 37.126 1.00 151.20 ? 612 SER A CB 1 ATOM 4735 O OG . SER A 1 612 ? -56.580 38.170 37.562 1.00 144.30 ? 612 SER A OG 1 ATOM 4736 N N . ASP A 1 613 ? -54.601 37.039 35.846 1.00 150.26 ? 613 ASP A N 1 ATOM 4737 C CA . ASP A 1 613 ? -53.645 35.996 36.225 1.00 144.31 ? 613 ASP A CA 1 ATOM 4738 C C . ASP A 1 613 ? -53.130 36.320 37.625 1.00 150.45 ? 613 ASP A C 1 ATOM 4739 O O . ASP A 1 613 ? -53.899 36.317 38.585 1.00 147.37 ? 613 ASP A O 1 ATOM 4740 C CB . ASP A 1 613 ? -52.498 35.883 35.215 1.00 142.01 ? 613 ASP A CB 1 ATOM 4741 C CG . ASP A 1 613 ? -51.627 34.662 35.452 1.00 155.31 ? 613 ASP A CG 1 ATOM 4742 O OD1 . ASP A 1 613 ? -51.984 33.568 34.965 1.00 161.44 ? 613 ASP A OD1 1 ATOM 4743 O OD2 . ASP A 1 613 ? -50.582 34.798 36.125 1.00 144.46 ? 613 ASP A OD2 1 ATOM 4744 N N . GLN A 1 614 ? -51.835 36.595 37.746 1.00 149.99 ? 614 GLN A N 1 ATOM 4745 C CA . GLN A 1 614 ? -51.292 37.064 39.013 1.00 135.77 ? 614 GLN A CA 1 ATOM 4746 C C . GLN A 1 614 ? -51.801 38.474 39.295 1.00 136.66 ? 614 GLN A C 1 ATOM 4747 O O . GLN A 1 614 ? -51.607 39.382 38.488 1.00 143.88 ? 614 GLN A O 1 ATOM 4748 C CB . GLN A 1 614 ? -49.761 37.046 38.992 1.00 134.19 ? 614 GLN A CB 1 ATOM 4749 C CG . GLN A 1 614 ? -49.141 35.661 39.093 1.00 152.15 ? 614 GLN A CG 1 ATOM 4750 C CD . GLN A 1 614 ? -49.025 35.174 40.525 1.00 160.44 ? 614 GLN A CD 1 ATOM 4751 O OE1 . GLN A 1 614 ? -49.412 35.872 41.465 1.00 164.66 ? 614 GLN A OE1 1 ATOM 4752 N NE2 . GLN A 1 614 ? -48.484 33.974 40.699 1.00 151.58 ? 614 GLN A NE2 1 ATOM 4753 N N . LYS A 1 615 ? -52.455 38.653 40.438 1.00 139.35 ? 615 LYS A N 1 ATOM 4754 C CA . LYS A 1 615 ? -52.963 39.965 40.821 1.00 140.31 ? 615 LYS A CA 1 ATOM 4755 C C . LYS A 1 615 ? -51.867 40.792 41.478 1.00 147.70 ? 615 LYS A C 1 ATOM 4756 O O . LYS A 1 615 ? -52.007 42.003 41.650 1.00 148.43 ? 615 LYS A O 1 ATOM 4757 C CB . LYS A 1 615 ? -54.161 39.836 41.765 1.00 119.75 ? 615 LYS A CB 1 ATOM 4758 C CG . LYS A 1 615 ? -55.492 39.631 41.060 1.00 115.52 ? 615 LYS A CG 1 ATOM 4759 C CD . LYS A 1 615 ? -56.656 39.791 42.027 1.00 125.56 ? 615 LYS A CD 1 ATOM 4760 C CE . LYS A 1 615 ? -57.993 39.681 41.311 1.00 120.81 ? 615 LYS A CE 1 ATOM 4761 N NZ . LYS A 1 615 ? -58.159 40.734 40.271 1.00 114.07 ? 615 LYS A NZ 1 ATOM 4762 N N . LYS A 1 616 ? -50.776 40.128 41.843 1.00 126.76 ? 616 LYS A N 1 ATOM 4763 C CA . LYS A 1 616 ? -49.668 40.801 42.505 1.00 118.45 ? 616 LYS A CA 1 ATOM 4764 C C . LYS A 1 616 ? -48.316 40.252 42.061 1.00 113.15 ? 616 LYS A C 1 ATOM 4765 O O . LYS A 1 616 ? -48.128 39.040 41.950 1.00 119.82 ? 616 LYS A O 1 ATOM 4766 C CB . LYS A 1 616 ? -49.814 40.682 44.024 1.00 124.90 ? 616 LYS A CB 1 ATOM 4767 C CG . LYS A 1 616 ? -49.988 39.255 44.524 1.00 132.22 ? 616 LYS A CG 1 ATOM 4768 C CD . LYS A 1 616 ? -50.365 39.226 45.995 1.00 132.77 ? 616 LYS A CD 1 ATOM 4769 C CE . LYS A 1 616 ? -51.705 39.904 46.232 1.00 126.93 ? 616 LYS A CE 1 ATOM 4770 N NZ . LYS A 1 616 ? -52.800 39.246 45.466 1.00 117.07 ? 616 LYS A NZ 1 ATOM 4771 N N . ILE A 1 617 ? -47.381 41.156 41.794 1.00 110.29 ? 617 ILE A N 1 ATOM 4772 C CA . ILE A 1 617 ? -46.004 40.777 41.511 1.00 111.04 ? 617 ILE A CA 1 ATOM 4773 C C . ILE A 1 617 ? -45.097 41.436 42.544 1.00 123.19 ? 617 ILE A C 1 ATOM 4774 O O . ILE A 1 617 ? -45.381 42.534 43.017 1.00 132.19 ? 617 ILE A O 1 ATOM 4775 C CB . ILE A 1 617 ? -45.573 41.171 40.082 1.00 109.83 ? 617 ILE A CB 1 ATOM 4776 C CG1 . ILE A 1 617 ? -45.730 42.676 39.858 1.00 117.64 ? 617 ILE A CG1 1 ATOM 4777 C CG2 . ILE A 1 617 ? -46.385 40.398 39.054 1.00 109.94 ? 617 ILE A CG2 1 ATOM 4778 C CD1 . ILE A 1 617 ? -45.282 43.133 38.485 1.00 129.34 ? 617 ILE A CD1 1 ATOM 4779 N N . TYR A 1 618 ? -44.013 40.761 42.906 1.00 116.45 ? 618 TYR A N 1 ATOM 4780 C CA . TYR A 1 618 ? -43.178 41.230 44.006 1.00 107.77 ? 618 TYR A CA 1 ATOM 4781 C C . TYR A 1 618 ? -42.009 42.073 43.503 1.00 112.61 ? 618 TYR A C 1 ATOM 4782 O O . TYR A 1 618 ? -41.321 41.710 42.549 1.00 108.07 ? 618 TYR A O 1 ATOM 4783 C CB . TYR A 1 618 ? -42.706 40.037 44.837 1.00 107.07 ? 618 TYR A CB 1 ATOM 4784 C CG . TYR A 1 618 ? -43.872 39.211 45.336 1.00 109.31 ? 618 TYR A CG 1 ATOM 4785 C CD1 . TYR A 1 618 ? -44.185 37.989 44.756 1.00 129.75 ? 618 TYR A CD1 1 ATOM 4786 C CD2 . TYR A 1 618 ? -44.688 39.676 46.359 1.00 113.31 ? 618 TYR A CD2 1 ATOM 4787 C CE1 . TYR A 1 618 ? -45.263 37.240 45.201 1.00 132.66 ? 618 TYR A CE1 1 ATOM 4788 C CE2 . TYR A 1 618 ? -45.764 38.935 46.812 1.00 113.31 ? 618 TYR A CE2 1 ATOM 4789 C CZ . TYR A 1 618 ? -46.048 37.719 46.229 1.00 119.51 ? 618 TYR A CZ 1 ATOM 4790 O OH . TYR A 1 618 ? -47.120 36.981 46.677 1.00 116.77 ? 618 TYR A OH 1 ATOM 4791 N N . ILE A 1 619 ? -41.801 43.207 44.167 1.00 122.74 ? 619 ILE A N 1 ATOM 4792 C CA . ILE A 1 619 ? -40.971 44.294 43.655 1.00 123.34 ? 619 ILE A CA 1 ATOM 4793 C C . ILE A 1 619 ? -39.477 43.968 43.584 1.00 117.75 ? 619 ILE A C 1 ATOM 4794 O O . ILE A 1 619 ? -38.718 44.665 42.907 1.00 124.62 ? 619 ILE A O 1 ATOM 4795 C CB . ILE A 1 619 ? -41.171 45.568 44.516 1.00 117.28 ? 619 ILE A CB 1 ATOM 4796 C CG1 . ILE A 1 619 ? -40.816 46.831 43.726 1.00 124.74 ? 619 ILE A CG1 1 ATOM 4797 C CG2 . ILE A 1 619 ? -40.379 45.471 45.813 1.00 133.26 ? 619 ILE A CG2 1 ATOM 4798 C CD1 . ILE A 1 619 ? -41.267 48.116 44.393 1.00 118.16 ? 619 ILE A CD1 1 ATOM 4799 N N . GLY A 1 620 ? -39.051 42.912 44.270 1.00 107.99 ? 620 GLY A N 1 ATOM 4800 C CA . GLY A 1 620 ? -37.643 42.555 44.277 1.00 117.47 ? 620 GLY A CA 1 ATOM 4801 C C . GLY A 1 620 ? -37.264 41.394 43.373 1.00 130.71 ? 620 GLY A C 1 ATOM 4802 O O . GLY A 1 620 ? -36.083 41.168 43.110 1.00 114.40 ? 620 GLY A O 1 ATOM 4803 N N . ASP A 1 621 ? -38.262 40.661 42.889 1.00 148.19 ? 621 ASP A N 1 ATOM 4804 C CA . ASP A 1 621 ? -38.013 39.432 42.140 1.00 146.21 ? 621 ASP A CA 1 ATOM 4805 C C . ASP A 1 621 ? -38.239 39.613 40.642 1.00 137.86 ? 621 ASP A C 1 ATOM 4806 O O . ASP A 1 621 ? -38.625 40.688 40.183 1.00 144.31 ? 621 ASP A O 1 ATOM 4807 C CB . ASP A 1 621 ? -38.911 38.308 42.671 1.00 144.66 ? 621 ASP A CB 1 ATOM 4808 C CG . ASP A 1 621 ? -38.334 36.926 42.424 1.00 153.60 ? 621 ASP A CG 1 ATOM 4809 O OD1 . ASP A 1 621 ? -37.605 36.750 41.424 1.00 163.46 ? 621 ASP A OD1 1 ATOM 4810 O OD2 . ASP A 1 621 ? -38.611 36.012 43.230 1.00 146.24 ? 621 ASP A OD2 1 ATOM 4811 N N . ASP A 1 622 ? -37.992 38.548 39.886 1.00 121.69 ? 622 ASP A N 1 ATOM 4812 C CA . ASP A 1 622 ? -38.364 38.492 38.480 1.00 120.73 ? 622 ASP A CA 1 ATOM 4813 C C . ASP A 1 622 ? -39.625 37.646 38.365 1.00 125.52 ? 622 ASP A C 1 ATOM 4814 O O . ASP A 1 622 ? -39.587 36.430 38.554 1.00 128.37 ? 622 ASP A O 1 ATOM 4815 C CB . ASP A 1 622 ? -37.233 37.908 37.631 1.00 121.35 ? 622 ASP A CB 1 ATOM 4816 C CG . ASP A 1 622 ? -35.936 38.684 37.773 1.00 147.82 ? 622 ASP A CG 1 ATOM 4817 O OD1 . ASP A 1 622 ? -35.995 39.895 38.075 1.00 155.46 ? 622 ASP A OD1 1 ATOM 4818 O OD2 . ASP A 1 622 ? -34.858 38.082 37.581 1.00 148.97 ? 622 ASP A OD2 1 ATOM 4819 N N . ASN A 1 623 ? -40.742 38.294 38.054 1.00 115.97 ? 623 ASN A N 1 ATOM 4820 C CA . ASN A 1 623 ? -42.046 37.647 38.145 1.00 122.03 ? 623 ASN A CA 1 ATOM 4821 C C . ASN A 1 623 ? -42.541 37.067 36.825 1.00 124.74 ? 623 ASN A C 1 ATOM 4822 O O . ASN A 1 623 ? -42.560 37.755 35.805 1.00 142.26 ? 623 ASN A O 1 ATOM 4823 C CB . ASN A 1 623 ? -43.077 38.637 38.688 1.00 131.86 ? 623 ASN A CB 1 ATOM 4824 C CG . ASN A 1 623 ? -42.688 39.196 40.044 1.00 137.53 ? 623 ASN A CG 1 ATOM 4825 O OD1 . ASN A 1 623 ? -43.087 38.669 41.083 1.00 141.80 ? 623 ASN A OD1 1 ATOM 4826 N ND2 . ASN A 1 623 ? -41.905 40.269 40.041 1.00 137.06 ? 623 ASN A ND2 1 ATOM 4827 N N . PRO A 1 624 ? -42.944 35.787 36.847 1.00 114.48 ? 624 PRO A N 1 ATOM 4828 C CA . PRO A 1 624 ? -43.540 35.108 35.692 1.00 118.77 ? 624 PRO A CA 1 ATOM 4829 C C . PRO A 1 624 ? -44.948 35.616 35.406 1.00 132.07 ? 624 PRO A C 1 ATOM 4830 O O . PRO A 1 624 ? -45.924 34.933 35.714 1.00 138.46 ? 624 PRO A O 1 ATOM 4831 C CB . PRO A 1 624 ? -43.570 33.633 36.122 1.00 121.74 ? 624 PRO A CB 1 ATOM 4832 C CG . PRO A 1 624 ? -42.629 33.539 37.285 1.00 123.19 ? 624 PRO A CG 1 ATOM 4833 C CD . PRO A 1 624 ? -42.725 34.861 37.970 1.00 118.20 ? 624 PRO A CD 1 ATOM 4834 N N . LEU A 1 625 ? -45.044 36.808 34.826 1.00 127.69 ? 625 LEU A N 1 ATOM 4835 C CA . LEU A 1 625 ? -46.337 37.412 34.532 1.00 126.46 ? 625 LEU A CA 1 ATOM 4836 C C . LEU A 1 625 ? -46.866 36.962 33.174 1.00 108.27 ? 625 LEU A C 1 ATOM 4837 O O . LEU A 1 625 ? -46.178 37.073 32.159 1.00 107.41 ? 625 LEU A O 1 ATOM 4838 C CB . LEU A 1 625 ? -46.236 38.938 34.580 1.00 121.74 ? 625 LEU A CB 1 ATOM 4839 C CG . LEU A 1 625 ? -47.530 39.712 34.325 1.00 115.75 ? 625 LEU A CG 1 ATOM 4840 C CD1 . LEU A 1 625 ? -48.604 39.315 35.325 1.00 120.62 ? 625 LEU A CD1 1 ATOM 4841 C CD2 . LEU A 1 625 ? -47.275 41.210 34.376 1.00 119.42 ? 625 LEU A CD2 1 ATOM 4842 N N . THR A 1 626 ? -48.094 36.453 33.165 1.00 107.33 ? 626 THR A N 1 ATOM 4843 C CA . THR A 1 626 ? -48.712 35.966 31.939 1.00 107.52 ? 626 THR A CA 1 ATOM 4844 C C . THR A 1 626 ? -50.073 36.613 31.712 1.00 123.87 ? 626 THR A C 1 ATOM 4845 O O . THR A 1 626 ? -50.979 36.472 32.531 1.00 129.57 ? 626 THR A O 1 ATOM 4846 C CB . THR A 1 626 ? -48.887 34.437 31.964 1.00 105.36 ? 626 THR A CB 1 ATOM 4847 O OG1 . THR A 1 626 ? -47.630 33.813 32.255 1.00 115.10 ? 626 THR A OG1 1 ATOM 4848 C CG2 . THR A 1 626 ? -49.402 33.937 30.623 1.00 103.94 ? 626 THR A CG2 1 ATOM 4849 N N . LEU A 1 627 ? -50.214 37.320 30.596 1.00 119.99 ? 627 LEU A N 1 ATOM 4850 C CA . LEU A 1 627 ? -51.474 37.977 30.271 1.00 106.82 ? 627 LEU A CA 1 ATOM 4851 C C . LEU A 1 627 ? -52.319 37.131 29.327 1.00 105.61 ? 627 LEU A C 1 ATOM 4852 O O . LEU A 1 627 ? -51.857 36.718 28.265 1.00 109.60 ? 627 LEU A O 1 ATOM 4853 C CB . LEU A 1 627 ? -51.220 39.351 29.650 1.00 106.48 ? 627 LEU A CB 1 ATOM 4854 C CG . LEU A 1 627 ? -50.511 40.372 30.541 1.00 107.77 ? 627 LEU A CG 1 ATOM 4855 C CD1 . LEU A 1 627 ? -50.476 41.733 29.866 1.00 107.57 ? 627 LEU A CD1 1 ATOM 4856 C CD2 . LEU A 1 627 ? -51.185 40.459 31.902 1.00 119.33 ? 627 LEU A CD2 1 ATOM 4857 N N . ILE A 1 628 ? -53.563 36.883 29.722 1.00 105.42 ? 628 ILE A N 1 ATOM 4858 C CA . ILE A 1 628 ? -54.498 36.139 28.891 1.00 104.44 ? 628 ILE A CA 1 ATOM 4859 C C . ILE A 1 628 ? -55.308 37.112 28.041 1.00 104.56 ? 628 ILE A C 1 ATOM 4860 O O . ILE A 1 628 ? -56.100 37.896 28.563 1.00 105.21 ? 628 ILE A O 1 ATOM 4861 C CB . ILE A 1 628 ? -55.439 35.267 29.744 1.00 104.35 ? 628 ILE A CB 1 ATOM 4862 C CG1 . ILE A 1 628 ? -54.659 34.124 30.394 1.00 104.06 ? 628 ILE A CG1 1 ATOM 4863 C CG2 . ILE A 1 628 ? -56.573 34.718 28.899 1.00 103.65 ? 628 ILE A CG2 1 ATOM 4864 C CD1 . ILE A 1 628 ? -53.981 33.202 29.400 1.00 103.01 ? 628 ILE A CD1 1 ATOM 4865 N N . VAL A 1 629 ? -55.099 37.059 26.730 1.00 103.77 ? 629 VAL A N 1 ATOM 4866 C CA . VAL A 1 629 ? -55.687 38.035 25.820 1.00 103.84 ? 629 VAL A CA 1 ATOM 4867 C C . VAL A 1 629 ? -56.836 37.452 25.005 1.00 107.24 ? 629 VAL A C 1 ATOM 4868 O O . VAL A 1 629 ? -56.709 36.381 24.413 1.00 109.94 ? 629 VAL A O 1 ATOM 4869 C CB . VAL A 1 629 ? -54.625 38.598 24.854 1.00 103.31 ? 629 VAL A CB 1 ATOM 4870 C CG1 . VAL A 1 629 ? -55.229 39.669 23.962 1.00 104.33 ? 629 VAL A CG1 1 ATOM 4871 C CG2 . VAL A 1 629 ? -53.444 39.154 25.631 1.00 103.73 ? 629 VAL A CG2 1 ATOM 4872 N N . LYS A 1 630 ? -57.959 38.163 24.986 1.00 112.25 ? 630 LYS A N 1 ATOM 4873 C CA . LYS A 1 630 ? -59.091 37.785 24.150 1.00 108.99 ? 630 LYS A CA 1 ATOM 4874 C C . LYS A 1 630 ? -59.307 38.826 23.061 1.00 112.46 ? 630 LYS A C 1 ATOM 4875 O O . LYS A 1 630 ? -59.717 39.952 23.339 1.00 129.77 ? 630 LYS A O 1 ATOM 4876 C CB . LYS A 1 630 ? -60.360 37.625 24.990 1.00 107.66 ? 630 LYS A CB 1 ATOM 4877 C CG . LYS A 1 630 ? -61.592 37.247 24.183 1.00 111.49 ? 630 LYS A CG 1 ATOM 4878 C CD . LYS A 1 630 ? -62.805 37.065 25.080 1.00 124.78 ? 630 LYS A CD 1 ATOM 4879 C CE . LYS A 1 630 ? -64.034 36.670 24.276 1.00 131.36 ? 630 LYS A CE 1 ATOM 4880 N NZ . LYS A 1 630 ? -65.231 36.494 25.145 1.00 125.69 ? 630 LYS A NZ 1 ATOM 4881 N N . ALA A 1 631 ? -59.025 38.444 21.820 1.00 104.57 ? 631 ALA A N 1 ATOM 4882 C CA . ALA A 1 631 ? -59.182 39.345 20.687 1.00 104.81 ? 631 ALA A CA 1 ATOM 4883 C C . ALA A 1 631 ? -60.235 38.814 19.724 1.00 111.67 ? 631 ALA A C 1 ATOM 4884 O O . ALA A 1 631 ? -60.142 37.680 19.256 1.00 118.77 ? 631 ALA A O 1 ATOM 4885 C CB . ALA A 1 631 ? -57.855 39.538 19.971 1.00 103.10 ? 631 ALA A CB 1 ATOM 4886 N N . GLN A 1 632 ? -61.237 39.636 19.432 1.00 106.46 ? 632 GLN A N 1 ATOM 4887 C CA . GLN A 1 632 ? -62.323 39.212 18.559 1.00 108.78 ? 632 GLN A CA 1 ATOM 4888 C C . GLN A 1 632 ? -62.732 40.292 17.560 1.00 106.15 ? 632 GLN A C 1 ATOM 4889 O O . GLN A 1 632 ? -62.704 41.484 17.867 1.00 108.93 ? 632 GLN A O 1 ATOM 4890 C CB . GLN A 1 632 ? -63.536 38.787 19.392 1.00 117.79 ? 632 GLN A CB 1 ATOM 4891 C CG . GLN A 1 632 ? -64.160 39.904 20.213 1.00 130.33 ? 632 GLN A CG 1 ATOM 4892 C CD . GLN A 1 632 ? -65.341 39.431 21.037 1.00 137.37 ? 632 GLN A CD 1 ATOM 4893 O OE1 . GLN A 1 632 ? -65.388 38.280 21.471 1.00 137.05 ? 632 GLN A OE1 1 ATOM 4894 N NE2 . GLN A 1 632 ? -66.306 40.317 21.251 1.00 138.84 ? 632 GLN A NE2 1 ATOM 4895 N N . ASN A 1 633 ? -63.102 39.859 16.359 1.00 106.79 ? 633 ASN A N 1 ATOM 4896 C CA . ASN A 1 633 ? -63.638 40.761 15.346 1.00 112.86 ? 633 ASN A CA 1 ATOM 4897 C C . ASN A 1 633 ? -65.100 40.436 15.063 1.00 102.14 ? 633 ASN A C 1 ATOM 4898 O O . ASN A 1 633 ? -65.411 39.409 14.461 1.00 101.33 ? 633 ASN A O 1 ATOM 4899 C CB . ASN A 1 633 ? -62.815 40.675 14.058 1.00 116.52 ? 633 ASN A CB 1 ATOM 4900 C CG . ASN A 1 633 ? -63.319 41.614 12.977 1.00 105.02 ? 633 ASN A CG 1 ATOM 4901 O OD1 . ASN A 1 633 ? -64.001 42.599 13.260 1.00 104.18 ? 633 ASN A OD1 1 ATOM 4902 N ND2 . ASN A 1 633 ? -62.982 41.311 11.728 1.00 102.58 ? 633 ASN A ND2 1 ATOM 4903 N N . GLN A 1 634 ? -65.994 41.316 15.502 1.00 111.60 ? 634 GLN A N 1 ATOM 4904 C CA . GLN A 1 634 ? -67.426 41.090 15.341 1.00 133.91 ? 634 GLN A CA 1 ATOM 4905 C C . GLN A 1 634 ? -67.982 41.804 14.114 1.00 140.23 ? 634 GLN A C 1 ATOM 4906 O O . GLN A 1 634 ? -69.179 41.738 13.835 1.00 152.68 ? 634 GLN A O 1 ATOM 4907 C CB . GLN A 1 634 ? -68.178 41.535 16.597 1.00 135.32 ? 634 GLN A CB 1 ATOM 4908 C CG . GLN A 1 634 ? -67.699 40.857 17.872 1.00 120.94 ? 634 GLN A CG 1 ATOM 4909 C CD . GLN A 1 634 ? -67.806 39.344 17.811 1.00 124.58 ? 634 GLN A CD 1 ATOM 4910 O OE1 . GLN A 1 634 ? -66.929 38.630 18.297 1.00 143.54 ? 634 GLN A OE1 1 ATOM 4911 N NE2 . GLN A 1 634 ? -68.888 38.847 17.220 1.00 127.95 ? 634 GLN A NE2 1 ATOM 4912 N N . GLY A 1 635 ? -67.108 42.490 13.385 1.00 117.55 ? 635 GLY A N 1 ATOM 4913 C CA . GLY A 1 635 ? -67.503 43.173 12.168 1.00 106.66 ? 635 GLY A CA 1 ATOM 4914 C C . GLY A 1 635 ? -67.015 42.436 10.938 1.00 117.56 ? 635 GLY A C 1 ATOM 4915 O O . GLY A 1 635 ? -66.761 41.235 10.986 1.00 102.00 ? 635 GLY A O 1 ATOM 4916 N N . GLU A 1 636 ? -66.878 43.158 9.831 1.00 122.31 ? 636 GLU A N 1 ATOM 4917 C CA . GLU A 1 636 ? -66.391 42.569 8.589 1.00 117.67 ? 636 GLU A CA 1 ATOM 4918 C C . GLU A 1 636 ? -64.887 42.303 8.656 1.00 113.17 ? 636 GLU A C 1 ATOM 4919 O O . GLU A 1 636 ? -64.251 42.539 9.684 1.00 103.18 ? 636 GLU A O 1 ATOM 4920 C CB . GLU A 1 636 ? -66.724 43.479 7.403 1.00 110.19 ? 636 GLU A CB 1 ATOM 4921 C CG . GLU A 1 636 ? -68.207 43.505 7.049 1.00 110.03 ? 636 GLU A CG 1 ATOM 4922 C CD . GLU A 1 636 ? -68.571 44.644 6.113 1.00 137.23 ? 636 GLU A CD 1 ATOM 4923 O OE1 . GLU A 1 636 ? -69.507 44.478 5.302 1.00 128.14 ? 636 GLU A OE1 1 ATOM 4924 O OE2 . GLU A 1 636 ? -67.930 45.711 6.196 1.00 161.55 ? 636 GLU A OE2 1 ATOM 4925 N N . GLY A 1 637 ? -64.325 41.809 7.557 1.00 99.25 ? 637 GLY A N 1 ATOM 4926 C CA . GLY A 1 637 ? -62.926 41.424 7.516 1.00 97.96 ? 637 GLY A CA 1 ATOM 4927 C C . GLY A 1 637 ? -61.953 42.554 7.793 1.00 111.47 ? 637 GLY A C 1 ATOM 4928 O O . GLY A 1 637 ? -62.129 43.672 7.307 1.00 117.49 ? 637 GLY A O 1 ATOM 4929 N N . ALA A 1 638 ? -60.922 42.256 8.577 1.00 116.10 ? 638 ALA A N 1 ATOM 4930 C CA . ALA A 1 638 ? -59.893 43.236 8.906 1.00 99.15 ? 638 ALA A CA 1 ATOM 4931 C C . ALA A 1 638 ? -58.558 42.857 8.275 1.00 100.76 ? 638 ALA A C 1 ATOM 4932 O O . ALA A 1 638 ? -57.931 41.876 8.676 1.00 101.94 ? 638 ALA A O 1 ATOM 4933 C CB . ALA A 1 638 ? -59.749 43.367 10.412 1.00 98.78 ? 638 ALA A CB 1 ATOM 4934 N N . TYR A 1 639 ? -58.125 43.643 7.294 1.00 101.75 ? 639 TYR A N 1 ATOM 4935 C CA . TYR A 1 639 ? -56.882 43.368 6.581 1.00 104.69 ? 639 TYR A CA 1 ATOM 4936 C C . TYR A 1 639 ? -55.660 43.676 7.436 1.00 104.42 ? 639 TYR A C 1 ATOM 4937 O O . TYR A 1 639 ? -55.589 44.729 8.071 1.00 102.44 ? 639 TYR A O 1 ATOM 4938 C CB . TYR A 1 639 ? -56.814 44.177 5.284 1.00 110.31 ? 639 TYR A CB 1 ATOM 4939 C CG . TYR A 1 639 ? -58.062 44.097 4.440 1.00 118.89 ? 639 TYR A CG 1 ATOM 4940 C CD1 . TYR A 1 639 ? -58.401 42.925 3.776 1.00 104.97 ? 639 TYR A CD1 1 ATOM 4941 C CD2 . TYR A 1 639 ? -58.897 45.196 4.297 1.00 129.45 ? 639 TYR A CD2 1 ATOM 4942 C CE1 . TYR A 1 639 ? -59.541 42.850 3.001 1.00 117.24 ? 639 TYR A CE1 1 ATOM 4943 C CE2 . TYR A 1 639 ? -60.038 45.131 3.524 1.00 121.64 ? 639 TYR A CE2 1 ATOM 4944 C CZ . TYR A 1 639 ? -60.355 43.955 2.878 1.00 130.85 ? 639 TYR A CZ 1 ATOM 4945 O OH . TYR A 1 639 ? -61.491 43.885 2.106 1.00 152.57 ? 639 TYR A OH 1 ATOM 4946 N N . GLU A 1 640 ? -54.702 42.752 7.435 1.00 111.77 ? 640 GLU A N 1 ATOM 4947 C CA . GLU A 1 640 ? -53.444 42.911 8.160 1.00 105.27 ? 640 GLU A CA 1 ATOM 4948 C C . GLU A 1 640 ? -53.679 43.259 9.628 1.00 103.94 ? 640 GLU A C 1 ATOM 4949 O O . GLU A 1 640 ? -53.115 44.222 10.147 1.00 104.71 ? 640 GLU A O 1 ATOM 4950 C CB . GLU A 1 640 ? -52.577 43.982 7.491 1.00 105.80 ? 640 GLU A CB 1 ATOM 4951 C CG . GLU A 1 640 ? -52.377 43.763 5.998 1.00 113.77 ? 640 GLU A CG 1 ATOM 4952 C CD . GLU A 1 640 ? -51.551 44.856 5.348 1.00 132.00 ? 640 GLU A CD 1 ATOM 4953 O OE1 . GLU A 1 640 ? -51.900 45.277 4.225 1.00 137.68 ? 640 GLU A OE1 1 ATOM 4954 O OE2 . GLU A 1 640 ? -50.550 45.290 5.955 1.00 143.67 ? 640 GLU A OE2 1 ATOM 4955 N N . ALA A 1 641 ? -54.521 42.468 10.286 1.00 103.89 ? 641 ALA A N 1 ATOM 4956 C CA . ALA A 1 641 ? -54.858 42.695 11.686 1.00 103.25 ? 641 ALA A CA 1 ATOM 4957 C C . ALA A 1 641 ? -53.693 42.341 12.602 1.00 104.16 ? 641 ALA A C 1 ATOM 4958 O O . ALA A 1 641 ? -53.070 41.291 12.449 1.00 105.71 ? 641 ALA A O 1 ATOM 4959 C CB . ALA A 1 641 ? -56.091 41.892 12.066 1.00 107.95 ? 641 ALA A CB 1 ATOM 4960 N N . GLU A 1 642 ? -53.402 43.222 13.553 1.00 103.46 ? 642 GLU A N 1 ATOM 4961 C CA . GLU A 1 642 ? -52.317 42.994 14.501 1.00 104.64 ? 642 GLU A CA 1 ATOM 4962 C C . GLU A 1 642 ? -52.704 43.407 15.918 1.00 105.31 ? 642 GLU A C 1 ATOM 4963 O O . GLU A 1 642 ? -53.424 44.385 16.116 1.00 103.24 ? 642 GLU A O 1 ATOM 4964 C CB . GLU A 1 642 ? -51.058 43.750 14.068 1.00 104.87 ? 642 GLU A CB 1 ATOM 4965 C CG . GLU A 1 642 ? -50.367 43.174 12.844 1.00 115.11 ? 642 GLU A CG 1 ATOM 4966 C CD . GLU A 1 642 ? -49.149 43.979 12.432 1.00 127.01 ? 642 GLU A CD 1 ATOM 4967 O OE1 . GLU A 1 642 ? -49.058 45.161 12.823 1.00 129.61 ? 642 GLU A OE1 1 ATOM 4968 O OE2 . GLU A 1 642 ? -48.281 43.428 11.724 1.00 138.87 ? 642 GLU A OE2 1 ATOM 4969 N N . LEU A 1 643 ? -52.218 42.654 16.900 1.00 111.96 ? 643 LEU A N 1 ATOM 4970 C CA . LEU A 1 643 ? -52.415 42.999 18.303 1.00 106.29 ? 643 LEU A CA 1 ATOM 4971 C C . LEU A 1 643 ? -51.215 43.776 18.830 1.00 107.45 ? 643 LEU A C 1 ATOM 4972 O O . LEU A 1 643 ? -50.112 43.239 18.921 1.00 108.82 ? 643 LEU A O 1 ATOM 4973 C CB . LEU A 1 643 ? -52.642 41.744 19.147 1.00 103.81 ? 643 LEU A CB 1 ATOM 4974 C CG . LEU A 1 643 ? -52.687 41.960 20.661 1.00 102.70 ? 643 LEU A CG 1 ATOM 4975 C CD1 . LEU A 1 643 ? -53.875 42.830 21.052 1.00 102.30 ? 643 LEU A CD1 1 ATOM 4976 C CD2 . LEU A 1 643 ? -52.723 40.628 21.397 1.00 102.63 ? 643 LEU A CD2 1 ATOM 4977 N N . ILE A 1 644 ? -51.435 45.039 19.177 1.00 105.05 ? 644 ILE A N 1 ATOM 4978 C CA . ILE A 1 644 ? -50.358 45.888 19.672 1.00 104.95 ? 644 ILE A CA 1 ATOM 4979 C C . ILE A 1 644 ? -50.334 45.922 21.196 1.00 105.93 ? 644 ILE A C 1 ATOM 4980 O O . ILE A 1 644 ? -51.260 46.426 21.833 1.00 110.86 ? 644 ILE A O 1 ATOM 4981 C CB . ILE A 1 644 ? -50.481 47.325 19.134 1.00 103.42 ? 644 ILE A CB 1 ATOM 4982 C CG1 . ILE A 1 644 ? -50.434 47.326 17.605 1.00 102.36 ? 644 ILE A CG1 1 ATOM 4983 C CG2 . ILE A 1 644 ? -49.382 48.206 19.709 1.00 104.52 ? 644 ILE A CG2 1 ATOM 4984 C CD1 . ILE A 1 644 ? -49.186 46.690 17.029 1.00 102.45 ? 644 ILE A CD1 1 ATOM 4985 N N . VAL A 1 645 ? -49.267 45.379 21.771 1.00 106.52 ? 645 VAL A N 1 ATOM 4986 C CA . VAL A 1 645 ? -49.090 45.359 23.216 1.00 107.53 ? 645 VAL A CA 1 ATOM 4987 C C . VAL A 1 645 ? -47.925 46.254 23.618 1.00 111.96 ? 645 VAL A C 1 ATOM 4988 O O . VAL A 1 645 ? -46.772 45.968 23.293 1.00 118.86 ? 645 VAL A O 1 ATOM 4989 C CB . VAL A 1 645 ? -48.840 43.929 23.733 1.00 107.71 ? 645 VAL A CB 1 ATOM 4990 C CG1 . VAL A 1 645 ? -48.523 43.943 25.220 1.00 108.91 ? 645 VAL A CG1 1 ATOM 4991 C CG2 . VAL A 1 645 ? -50.035 43.039 23.437 1.00 106.60 ? 645 VAL A CG2 1 ATOM 4992 N N . SER A 1 646 ? -48.229 47.340 24.321 1.00 111.61 ? 646 SER A N 1 ATOM 4993 C CA . SER A 1 646 ? -47.203 48.287 24.745 1.00 110.58 ? 646 SER A CA 1 ATOM 4994 C C . SER A 1 646 ? -46.705 47.963 26.148 1.00 114.59 ? 646 SER A C 1 ATOM 4995 O O . SER A 1 646 ? -47.448 48.084 27.121 1.00 127.22 ? 646 SER A O 1 ATOM 4996 C CB . SER A 1 646 ? -47.742 49.718 24.695 1.00 110.12 ? 646 SER A CB 1 ATOM 4997 O OG . SER A 1 646 ? -48.234 50.034 23.405 1.00 115.82 ? 646 SER A OG 1 ATOM 4998 N N . ILE A 1 647 ? -45.445 47.551 26.247 1.00 110.78 ? 647 ILE A N 1 ATOM 4999 C CA . ILE A 1 647 ? -44.862 47.206 27.537 1.00 118.82 ? 647 ILE A CA 1 ATOM 5000 C C . ILE A 1 647 ? -43.802 48.227 27.956 1.00 149.20 ? 647 ILE A C 1 ATOM 5001 O O . ILE A 1 647 ? -42.724 48.307 27.367 1.00 168.71 ? 647 ILE A O 1 ATOM 5002 C CB . ILE A 1 647 ? -44.255 45.782 27.522 1.00 126.69 ? 647 ILE A CB 1 ATOM 5003 C CG1 . ILE A 1 647 ? -43.315 45.586 26.330 1.00 126.24 ? 647 ILE A CG1 1 ATOM 5004 C CG2 . ILE A 1 647 ? -45.357 44.748 27.441 1.00 134.97 ? 647 ILE A CG2 1 ATOM 5005 C CD1 . ILE A 1 647 ? -42.513 44.303 26.397 1.00 121.53 ? 647 ILE A CD1 1 ATOM 5006 N N . PRO A 1 648 ? -44.124 49.041 28.970 1.00 159.02 ? 648 PRO A N 1 ATOM 5007 C CA . PRO A 1 648 ? -43.188 50.061 29.449 1.00 157.62 ? 648 PRO A CA 1 ATOM 5008 C C . PRO A 1 648 ? -42.042 49.497 30.284 1.00 143.07 ? 648 PRO A C 1 ATOM 5009 O O . PRO A 1 648 ? -42.257 48.595 31.094 1.00 115.61 ? 648 PRO A O 1 ATOM 5010 C CB . PRO A 1 648 ? -44.076 50.967 30.305 1.00 158.33 ? 648 PRO A CB 1 ATOM 5011 C CG . PRO A 1 648 ? -45.141 50.056 30.812 1.00 159.63 ? 648 PRO A CG 1 ATOM 5012 C CD . PRO A 1 648 ? -45.406 49.081 29.696 1.00 161.51 ? 648 PRO A CD 1 ATOM 5013 N N . LEU A 1 649 ? -40.843 50.035 30.074 1.00 152.42 ? 649 LEU A N 1 ATOM 5014 C CA . LEU A 1 649 ? -39.732 49.882 31.011 1.00 140.60 ? 649 LEU A CA 1 ATOM 5015 C C . LEU A 1 649 ? -39.370 48.437 31.364 1.00 136.92 ? 649 LEU A C 1 ATOM 5016 O O . LEU A 1 649 ? -38.935 47.665 30.508 1.00 135.74 ? 649 LEU A O 1 ATOM 5017 C CB . LEU A 1 649 ? -40.050 50.658 32.292 1.00 136.50 ? 649 LEU A CB 1 ATOM 5018 C CG . LEU A 1 649 ? -40.536 52.090 32.046 1.00 146.00 ? 649 LEU A CG 1 ATOM 5019 C CD1 . LEU A 1 649 ? -40.974 52.762 33.339 1.00 152.06 ? 649 LEU A CD1 1 ATOM 5020 C CD2 . LEU A 1 649 ? -39.460 52.910 31.346 1.00 143.74 ? 649 LEU A CD2 1 ATOM 5021 N N . GLN A 1 650 ? -39.551 48.103 32.639 1.00 132.73 ? 650 GLN A N 1 ATOM 5022 C CA . GLN A 1 650 ? -39.086 46.855 33.245 1.00 127.43 ? 650 GLN A CA 1 ATOM 5023 C C . GLN A 1 650 ? -39.412 45.585 32.460 1.00 140.63 ? 650 GLN A C 1 ATOM 5024 O O . GLN A 1 650 ? -38.577 44.687 32.348 1.00 150.61 ? 650 GLN A O 1 ATOM 5025 C CB . GLN A 1 650 ? -39.674 46.718 34.655 1.00 121.61 ? 650 GLN A CB 1 ATOM 5026 C CG . GLN A 1 650 ? -40.052 48.034 35.326 1.00 133.21 ? 650 GLN A CG 1 ATOM 5027 C CD . GLN A 1 650 ? -41.415 48.556 34.898 1.00 120.11 ? 650 GLN A CD 1 ATOM 5028 O OE1 . GLN A 1 650 ? -42.039 48.020 33.983 1.00 131.87 ? 650 GLN A OE1 1 ATOM 5029 N NE2 . GLN A 1 650 ? -41.879 49.609 35.561 1.00 119.20 ? 650 GLN A NE2 1 ATOM 5030 N N . ALA A 1 651 ? -40.626 45.512 31.926 1.00 134.76 ? 651 ALA A N 1 ATOM 5031 C CA . ALA A 1 651 ? -41.107 44.296 31.278 1.00 119.13 ? 651 ALA A CA 1 ATOM 5032 C C . ALA A 1 651 ? -40.352 43.969 29.992 1.00 108.42 ? 651 ALA A C 1 ATOM 5033 O O . ALA A 1 651 ? -40.119 44.842 29.156 1.00 114.34 ? 651 ALA A O 1 ATOM 5034 C CB . ALA A 1 651 ? -42.595 44.414 30.991 1.00 127.72 ? 651 ALA A CB 1 ATOM 5035 N N . ASP A 1 652 ? -39.974 42.703 29.847 1.00 107.51 ? 652 ASP A N 1 ATOM 5036 C CA . ASP A 1 652 ? -39.398 42.202 28.604 1.00 121.78 ? 652 ASP A CA 1 ATOM 5037 C C . ASP A 1 652 ? -40.105 40.914 28.184 1.00 108.60 ? 652 ASP A C 1 ATOM 5038 O O . ASP A 1 652 ? -40.405 40.058 29.016 1.00 104.04 ? 652 ASP A O 1 ATOM 5039 C CB . ASP A 1 652 ? -37.890 41.974 28.746 1.00 133.14 ? 652 ASP A CB 1 ATOM 5040 C CG . ASP A 1 652 ? -37.534 41.167 29.975 1.00 147.87 ? 652 ASP A CG 1 ATOM 5041 O OD1 . ASP A 1 652 ? -38.297 41.220 30.959 1.00 156.13 ? 652 ASP A OD1 1 ATOM 5042 O OD2 . ASP A 1 652 ? -36.487 40.485 29.961 1.00 146.50 ? 652 ASP A OD2 1 ATOM 5043 N N . PHE A 1 653 ? -40.365 40.791 26.887 1.00 112.34 ? 653 PHE A N 1 ATOM 5044 C CA . PHE A 1 653 ? -41.167 39.698 26.348 1.00 117.38 ? 653 PHE A CA 1 ATOM 5045 C C . PHE A 1 653 ? -40.397 38.380 26.282 1.00 114.40 ? 653 PHE A C 1 ATOM 5046 O O . PHE A 1 653 ? -39.294 38.320 25.740 1.00 132.62 ? 653 PHE A O 1 ATOM 5047 C CB . PHE A 1 653 ? -41.681 40.080 24.957 1.00 126.41 ? 653 PHE A CB 1 ATOM 5048 C CG . PHE A 1 653 ? -42.608 39.069 24.345 1.00 118.20 ? 653 PHE A CG 1 ATOM 5049 C CD1 . PHE A 1 653 ? -43.815 38.759 24.949 1.00 121.55 ? 653 PHE A CD1 1 ATOM 5050 C CD2 . PHE A 1 653 ? -42.284 38.449 23.150 1.00 112.94 ? 653 PHE A CD2 1 ATOM 5051 C CE1 . PHE A 1 653 ? -44.673 37.836 24.382 1.00 120.05 ? 653 PHE A CE1 1 ATOM 5052 C CE2 . PHE A 1 653 ? -43.138 37.527 22.578 1.00 113.80 ? 653 PHE A CE2 1 ATOM 5053 C CZ . PHE A 1 653 ? -44.335 37.221 23.194 1.00 116.52 ? 653 PHE A CZ 1 ATOM 5054 N N . ILE A 1 654 ? -40.991 37.329 26.839 1.00 105.65 ? 654 ILE A N 1 ATOM 5055 C CA . ILE A 1 654 ? -40.402 35.993 26.800 1.00 114.53 ? 654 ILE A CA 1 ATOM 5056 C C . ILE A 1 654 ? -40.850 35.270 25.532 1.00 119.12 ? 654 ILE A C 1 ATOM 5057 O O . ILE A 1 654 ? -40.028 34.923 24.684 1.00 123.30 ? 654 ILE A O 1 ATOM 5058 C CB . ILE A 1 654 ? -40.773 35.152 28.050 1.00 131.31 ? 654 ILE A CB 1 ATOM 5059 C CG1 . ILE A 1 654 ? -39.902 35.541 29.248 1.00 131.35 ? 654 ILE A CG1 1 ATOM 5060 C CG2 . ILE A 1 654 ? -40.578 33.667 27.782 1.00 119.40 ? 654 ILE A CG2 1 ATOM 5061 C CD1 . ILE A 1 654 ? -40.245 36.869 29.875 1.00 122.73 ? 654 ILE A CD1 1 ATOM 5062 N N . GLY A 1 655 ? -42.154 35.042 25.408 1.00 116.06 ? 655 GLY A N 1 ATOM 5063 C CA . GLY A 1 655 ? -42.699 34.367 24.245 1.00 123.44 ? 655 GLY A CA 1 ATOM 5064 C C . GLY A 1 655 ? -44.182 34.083 24.372 1.00 126.74 ? 655 GLY A C 1 ATOM 5065 O O . GLY A 1 655 ? -44.834 34.533 25.315 1.00 124.60 ? 655 GLY A O 1 ATOM 5066 N N . VAL A 1 656 ? -44.719 33.335 23.414 1.00 129.15 ? 656 VAL A N 1 ATOM 5067 C CA . VAL A 1 656 ? -46.120 32.937 23.451 1.00 124.85 ? 656 VAL A CA 1 ATOM 5068 C C . VAL A 1 656 ? -46.269 31.737 24.382 1.00 118.83 ? 656 VAL A C 1 ATOM 5069 O O . VAL A 1 656 ? -45.304 31.326 25.027 1.00 114.38 ? 656 VAL A O 1 ATOM 5070 C CB . VAL A 1 656 ? -46.650 32.590 22.046 1.00 128.97 ? 656 VAL A CB 1 ATOM 5071 C CG1 . VAL A 1 656 ? -48.102 33.025 21.902 1.00 121.73 ? 656 VAL A CG1 1 ATOM 5072 C CG2 . VAL A 1 656 ? -45.794 33.258 20.982 1.00 132.97 ? 656 VAL A CG2 1 ATOM 5073 N N . VAL A 1 657 ? -47.469 31.174 24.455 1.00 121.08 ? 657 VAL A N 1 ATOM 5074 C CA . VAL A 1 657 ? -47.698 30.013 25.306 1.00 127.51 ? 657 VAL A CA 1 ATOM 5075 C C . VAL A 1 657 ? -47.733 28.729 24.481 1.00 134.46 ? 657 VAL A C 1 ATOM 5076 O O . VAL A 1 657 ? -48.679 28.476 23.734 1.00 140.49 ? 657 VAL A O 1 ATOM 5077 C CB . VAL A 1 657 ? -49.007 30.157 26.105 1.00 124.54 ? 657 VAL A CB 1 ATOM 5078 C CG1 . VAL A 1 657 ? -48.758 30.925 27.395 1.00 116.18 ? 657 VAL A CG1 1 ATOM 5079 C CG2 . VAL A 1 657 ? -50.066 30.848 25.263 1.00 138.59 ? 657 VAL A CG2 1 ATOM 5080 N N . ARG A 1 658 ? -46.684 27.926 24.618 1.00 132.30 ? 658 ARG A N 1 ATOM 5081 C CA . ARG A 1 658 ? -46.567 26.670 23.885 1.00 136.16 ? 658 ARG A CA 1 ATOM 5082 C C . ARG A 1 658 ? -47.342 25.542 24.557 1.00 147.88 ? 658 ARG A C 1 ATOM 5083 O O . ARG A 1 658 ? -48.004 24.745 23.892 1.00 151.56 ? 658 ARG A O 1 ATOM 5084 C CB . ARG A 1 658 ? -45.096 26.273 23.742 1.00 148.35 ? 658 ARG A CB 1 ATOM 5085 C CG . ARG A 1 658 ? -44.183 27.394 23.269 1.00 146.37 ? 658 ARG A CG 1 ATOM 5086 C CD . ARG A 1 658 ? -44.518 27.844 21.856 1.00 140.94 ? 658 ARG A CD 1 ATOM 5087 N NE . ARG A 1 658 ? -43.553 28.823 21.361 1.00 141.78 ? 658 ARG A NE 1 ATOM 5088 C CZ . ARG A 1 658 ? -43.554 29.320 20.128 1.00 145.08 ? 658 ARG A CZ 1 ATOM 5089 N NH1 . ARG A 1 658 ? -44.472 28.931 19.253 1.00 139.02 ? 658 ARG A NH1 1 ATOM 5090 N NH2 . ARG A 1 658 ? -42.633 30.204 19.769 1.00 135.46 ? 658 ARG A NH2 1 ATOM 5091 N N . ASN A 1 659 ? -47.251 25.485 25.883 1.00 149.61 ? 659 ASN A N 1 ATOM 5092 C CA . ASN A 1 659 ? -47.776 24.363 26.656 1.00 136.50 ? 659 ASN A CA 1 ATOM 5093 C C . ASN A 1 659 ? -49.292 24.194 26.570 1.00 120.25 ? 659 ASN A C 1 ATOM 5094 O O . ASN A 1 659 ? -49.780 23.096 26.302 1.00 131.62 ? 659 ASN A O 1 ATOM 5095 C CB . ASN A 1 659 ? -47.357 24.502 28.123 1.00 125.87 ? 659 ASN A CB 1 ATOM 5096 C CG . ASN A 1 659 ? -47.664 25.874 28.691 1.00 129.49 ? 659 ASN A CG 1 ATOM 5097 O OD1 . ASN A 1 659 ? -46.923 26.831 28.467 1.00 129.07 ? 659 ASN A OD1 1 ATOM 5098 N ND2 . ASN A 1 659 ? -48.759 25.975 29.434 1.00 126.75 ? 659 ASN A ND2 1 ATOM 5099 N N . ASN A 1 660 ? -50.033 25.273 26.796 1.00 107.73 ? 660 ASN A N 1 ATOM 5100 C CA . ASN A 1 660 ? -51.490 25.199 26.802 1.00 127.41 ? 660 ASN A CA 1 ATOM 5101 C C . ASN A 1 660 ? -52.050 24.945 25.405 1.00 135.84 ? 660 ASN A C 1 ATOM 5102 O O . ASN A 1 660 ? -51.694 25.631 24.446 1.00 139.18 ? 660 ASN A O 1 ATOM 5103 C CB . ASN A 1 660 ? -52.088 26.481 27.384 1.00 142.19 ? 660 ASN A CB 1 ATOM 5104 C CG . ASN A 1 660 ? -53.526 26.303 27.839 1.00 127.60 ? 660 ASN A CG 1 ATOM 5105 O OD1 . ASN A 1 660 ? -54.308 25.587 27.213 1.00 109.12 ? 660 ASN A OD1 1 ATOM 5106 N ND2 . ASN A 1 660 ? -53.881 26.955 28.940 1.00 122.49 ? 660 ASN A ND2 1 ATOM 5107 N N . GLU A 1 661 ? -52.925 23.950 25.300 1.00 134.07 ? 661 GLU A N 1 ATOM 5108 C CA . GLU A 1 661 ? -53.521 23.585 24.022 1.00 128.26 ? 661 GLU A CA 1 ATOM 5109 C C . GLU A 1 661 ? -54.826 24.345 23.791 1.00 104.12 ? 661 GLU A C 1 ATOM 5110 O O . GLU A 1 661 ? -55.400 24.296 22.703 1.00 113.39 ? 661 GLU A O 1 ATOM 5111 C CB . GLU A 1 661 ? -53.759 22.073 23.960 1.00 140.23 ? 661 GLU A CB 1 ATOM 5112 C CG . GLU A 1 661 ? -53.804 21.498 22.551 1.00 145.44 ? 661 GLU A CG 1 ATOM 5113 C CD . GLU A 1 661 ? -55.219 21.293 22.044 1.00 162.12 ? 661 GLU A CD 1 ATOM 5114 O OE1 . GLU A 1 661 ? -56.154 21.302 22.870 1.00 167.85 ? 661 GLU A OE1 1 ATOM 5115 O OE2 . GLU A 1 661 ? -55.394 21.121 20.820 1.00 164.17 ? 661 GLU A OE2 1 ATOM 5116 N N . ALA A 1 662 ? -55.285 25.053 24.818 1.00 101.77 ? 662 ALA A N 1 ATOM 5117 C CA . ALA A 1 662 ? -56.501 25.854 24.711 1.00 125.65 ? 662 ALA A CA 1 ATOM 5118 C C . ALA A 1 662 ? -56.174 27.302 24.357 1.00 141.25 ? 662 ALA A C 1 ATOM 5119 O O . ALA A 1 662 ? -57.071 28.132 24.208 1.00 129.94 ? 662 ALA A O 1 ATOM 5120 C CB . ALA A 1 662 ? -57.296 25.790 26.006 1.00 121.81 ? 662 ALA A CB 1 ATOM 5121 N N . LEU A 1 663 ? -54.886 27.598 24.224 1.00 136.36 ? 663 LEU A N 1 ATOM 5122 C CA . LEU A 1 663 ? -54.439 28.941 23.876 1.00 119.28 ? 663 LEU A CA 1 ATOM 5123 C C . LEU A 1 663 ? -53.812 28.959 22.485 1.00 126.14 ? 663 LEU A C 1 ATOM 5124 O O . LEU A 1 663 ? -53.232 27.966 22.046 1.00 140.59 ? 663 LEU A O 1 ATOM 5125 C CB . LEU A 1 663 ? -53.447 29.463 24.919 1.00 117.42 ? 663 LEU A CB 1 ATOM 5126 C CG . LEU A 1 663 ? -54.030 29.722 26.313 1.00 124.08 ? 663 LEU A CG 1 ATOM 5127 C CD1 . LEU A 1 663 ? -52.942 30.089 27.312 1.00 118.95 ? 663 LEU A CD1 1 ATOM 5128 C CD2 . LEU A 1 663 ? -55.087 30.812 26.252 1.00 117.00 ? 663 LEU A CD2 1 ATOM 5129 N N . ALA A 1 664 ? -53.934 30.088 21.794 1.00 119.86 ? 664 ALA A N 1 ATOM 5130 C CA . ALA A 1 664 ? -53.441 30.200 20.425 1.00 108.82 ? 664 ALA A CA 1 ATOM 5131 C C . ALA A 1 664 ? -51.916 30.224 20.370 1.00 112.41 ? 664 ALA A C 1 ATOM 5132 O O . ALA A 1 664 ? -51.252 30.689 21.296 1.00 112.69 ? 664 ALA A O 1 ATOM 5133 C CB . ALA A 1 664 ? -54.015 31.436 19.756 1.00 110.75 ? 664 ALA A CB 1 ATOM 5134 N N . ARG A 1 665 ? -51.378 29.721 19.266 1.00 121.73 ? 665 ARG A N 1 ATOM 5135 C CA . ARG A 1 665 ? -49.939 29.589 19.066 1.00 137.02 ? 665 ARG A CA 1 ATOM 5136 C C . ARG A 1 665 ? -49.343 30.820 18.386 1.00 134.10 ? 665 ARG A C 1 ATOM 5137 O O . ARG A 1 665 ? -48.183 30.801 17.973 1.00 131.80 ? 665 ARG A O 1 ATOM 5138 C CB . ARG A 1 665 ? -49.624 28.335 18.247 1.00 141.45 ? 665 ARG A CB 1 ATOM 5139 C CG . ARG A 1 665 ? -48.283 27.701 18.584 1.00 148.22 ? 665 ARG A CG 1 ATOM 5140 C CD . ARG A 1 665 ? -47.772 26.846 17.441 1.00 157.61 ? 665 ARG A CD 1 ATOM 5141 N NE . ARG A 1 665 ? -47.510 27.644 16.247 1.00 161.62 ? 665 ARG A NE 1 ATOM 5142 C CZ . ARG A 1 665 ? -46.947 27.170 15.141 1.00 154.22 ? 665 ARG A CZ 1 ATOM 5143 N NH1 . ARG A 1 665 ? -46.581 25.897 15.076 1.00 157.93 ? 665 ARG A NH1 1 ATOM 5144 N NH2 . ARG A 1 665 ? -46.748 27.970 14.102 1.00 140.72 ? 665 ARG A NH2 1 ATOM 5145 N N . LEU A 1 666 ? -50.148 31.875 18.269 1.00 122.89 ? 666 LEU A N 1 ATOM 5146 C CA . LEU A 1 666 ? -49.879 33.001 17.370 1.00 124.33 ? 666 LEU A CA 1 ATOM 5147 C C . LEU A 1 666 ? -48.456 33.542 17.448 1.00 122.32 ? 666 LEU A C 1 ATOM 5148 O O . LEU A 1 666 ? -47.908 33.739 18.532 1.00 120.39 ? 666 LEU A O 1 ATOM 5149 C CB . LEU A 1 666 ? -50.851 34.148 17.666 1.00 119.34 ? 666 LEU A CB 1 ATOM 5150 C CG . LEU A 1 666 ? -52.355 33.881 17.603 1.00 128.04 ? 666 LEU A CG 1 ATOM 5151 C CD1 . LEU A 1 666 ? -53.131 35.086 18.119 1.00 117.15 ? 666 LEU A CD1 1 ATOM 5152 C CD2 . LEU A 1 666 ? -52.780 33.533 16.185 1.00 139.85 ? 666 LEU A CD2 1 ATOM 5153 N N . SER A 1 667 ? -47.867 33.776 16.278 1.00 127.00 ? 667 SER A N 1 ATOM 5154 C CA . SER A 1 667 ? -46.502 34.275 16.179 1.00 129.04 ? 667 SER A CA 1 ATOM 5155 C C . SER A 1 667 ? -46.419 35.730 16.619 1.00 121.05 ? 667 SER A C 1 ATOM 5156 O O . SER A 1 667 ? -47.150 36.582 16.116 1.00 117.02 ? 667 SER A O 1 ATOM 5157 C CB . SER A 1 667 ? -45.980 34.128 14.748 1.00 128.51 ? 667 SER A CB 1 ATOM 5158 O OG . SER A 1 667 ? -46.795 34.838 13.832 1.00 131.42 ? 667 SER A OG 1 ATOM 5159 N N . CYS A 1 668 ? -45.524 36.007 17.560 1.00 121.69 ? 668 CYS A N 1 ATOM 5160 C CA . CYS A 1 668 ? -45.334 37.362 18.058 1.00 117.63 ? 668 CYS A CA 1 ATOM 5161 C C . CYS A 1 668 ? -43.865 37.757 17.999 1.00 121.86 ? 668 CYS A C 1 ATOM 5162 O O . CYS A 1 668 ? -42.980 36.904 18.061 1.00 142.62 ? 668 CYS A O 1 ATOM 5163 C CB . CYS A 1 668 ? -45.858 37.487 19.489 1.00 115.49 ? 668 CYS A CB 1 ATOM 5164 S SG . CYS A 1 668 ? -47.606 37.068 19.679 1.00 157.19 ? 668 CYS A SG 1 ATOM 5165 N N . ALA A 1 669 ? -43.612 39.055 17.876 1.00 116.49 ? 669 ALA A N 1 ATOM 5166 C CA . ALA A 1 669 ? -42.249 39.564 17.811 1.00 116.78 ? 669 ALA A CA 1 ATOM 5167 C C . ALA A 1 669 ? -42.128 40.889 18.553 1.00 117.83 ? 669 ALA A C 1 ATOM 5168 O O . ALA A 1 669 ? -43.011 41.743 18.466 1.00 108.20 ? 669 ALA A O 1 ATOM 5169 C CB . ALA A 1 669 ? -41.811 39.723 16.363 1.00 113.31 ? 669 ALA A CB 1 ATOM 5170 N N . PHE A 1 670 ? -41.031 41.053 19.284 1.00 125.11 ? 670 PHE A N 1 ATOM 5171 C CA . PHE A 1 670 ? -40.786 42.282 20.028 1.00 118.80 ? 670 PHE A CA 1 ATOM 5172 C C . PHE A 1 670 ? -40.148 43.336 19.131 1.00 119.14 ? 670 PHE A C 1 ATOM 5173 O O . PHE A 1 670 ? -39.095 43.104 18.538 1.00 126.68 ? 670 PHE A O 1 ATOM 5174 C CB . PHE A 1 670 ? -39.894 42.009 21.242 1.00 107.67 ? 670 PHE A CB 1 ATOM 5175 C CG . PHE A 1 670 ? -39.594 43.232 22.062 1.00 115.73 ? 670 PHE A CG 1 ATOM 5176 C CD1 . PHE A 1 670 ? -40.494 43.683 23.013 1.00 128.83 ? 670 PHE A CD1 1 ATOM 5177 C CD2 . PHE A 1 670 ? -38.409 43.928 21.884 1.00 116.27 ? 670 PHE A CD2 1 ATOM 5178 C CE1 . PHE A 1 670 ? -40.219 44.807 23.767 1.00 133.66 ? 670 PHE A CE1 1 ATOM 5179 C CE2 . PHE A 1 670 ? -38.130 45.054 22.636 1.00 131.59 ? 670 PHE A CE2 1 ATOM 5180 C CZ . PHE A 1 670 ? -39.037 45.493 23.580 1.00 137.82 ? 670 PHE A CZ 1 ATOM 5181 N N . LYS A 1 671 ? -40.794 44.493 19.035 1.00 108.62 ? 671 LYS A N 1 ATOM 5182 C CA . LYS A 1 671 ? -40.287 45.582 18.210 1.00 115.85 ? 671 LYS A CA 1 ATOM 5183 C C . LYS A 1 671 ? -39.949 46.817 19.033 1.00 126.64 ? 671 LYS A C 1 ATOM 5184 O O . LYS A 1 671 ? -40.637 47.140 20.002 1.00 111.62 ? 671 LYS A O 1 ATOM 5185 C CB . LYS A 1 671 ? -41.304 45.960 17.133 1.00 128.35 ? 671 LYS A CB 1 ATOM 5186 C CG . LYS A 1 671 ? -41.381 44.996 15.966 1.00 137.64 ? 671 LYS A CG 1 ATOM 5187 C CD . LYS A 1 671 ? -42.312 45.536 14.893 1.00 144.26 ? 671 LYS A CD 1 ATOM 5188 C CE . LYS A 1 671 ? -41.888 46.929 14.449 1.00 148.23 ? 671 LYS A CE 1 ATOM 5189 N NZ . LYS A 1 671 ? -42.832 47.507 13.451 1.00 141.03 ? 671 LYS A NZ 1 ATOM 5190 N N . THR A 1 672 ? -38.884 47.504 18.637 1.00 142.27 ? 672 THR A N 1 ATOM 5191 C CA . THR A 1 672 ? -38.573 48.811 19.193 1.00 133.48 ? 672 THR A CA 1 ATOM 5192 C C . THR A 1 672 ? -38.442 49.829 18.063 1.00 125.35 ? 672 THR A C 1 ATOM 5193 O O . THR A 1 672 ? -37.501 49.781 17.269 1.00 129.99 ? 672 THR A O 1 ATOM 5194 C CB . THR A 1 672 ? -37.282 48.782 20.038 1.00 132.07 ? 672 THR A CB 1 ATOM 5195 O OG1 . THR A 1 672 ? -36.736 50.104 20.129 1.00 147.76 ? 672 THR A OG1 1 ATOM 5196 C CG2 . THR A 1 672 ? -36.248 47.850 19.417 1.00 129.82 ? 672 THR A CG2 1 ATOM 5197 N N . GLU A 1 673 ? -39.395 50.754 18.003 1.00 128.79 ? 673 GLU A N 1 ATOM 5198 C CA . GLU A 1 673 ? -39.459 51.753 16.940 1.00 149.06 ? 673 GLU A CA 1 ATOM 5199 C C . GLU A 1 673 ? -40.059 53.049 17.471 1.00 150.66 ? 673 GLU A C 1 ATOM 5200 O O . GLU A 1 673 ? -40.927 53.017 18.344 1.00 148.62 ? 673 GLU A O 1 ATOM 5201 C CB . GLU A 1 673 ? -40.292 51.243 15.757 1.00 145.35 ? 673 GLU A CB 1 ATOM 5202 C CG . GLU A 1 673 ? -39.656 50.118 14.953 1.00 139.29 ? 673 GLU A CG 1 ATOM 5203 C CD . GLU A 1 673 ? -38.430 50.570 14.185 1.00 146.90 ? 673 GLU A CD 1 ATOM 5204 O OE1 . GLU A 1 673 ? -37.356 49.956 14.360 1.00 147.91 ? 673 GLU A OE1 1 ATOM 5205 O OE2 . GLU A 1 673 ? -38.542 51.536 13.401 1.00 147.95 ? 673 GLU A OE2 1 ATOM 5206 N N . ASN A 1 674 ? -39.595 54.178 16.939 1.00 147.05 ? 674 ASN A N 1 ATOM 5207 C CA . ASN A 1 674 ? -40.103 55.493 17.326 1.00 151.93 ? 674 ASN A CA 1 ATOM 5208 C C . ASN A 1 674 ? -40.033 55.692 18.839 1.00 143.67 ? 674 ASN A C 1 ATOM 5209 O O . ASN A 1 674 ? -40.943 56.257 19.446 1.00 149.49 ? 674 ASN A O 1 ATOM 5210 C CB . ASN A 1 674 ? -41.541 55.672 16.826 1.00 157.01 ? 674 ASN A CB 1 ATOM 5211 C CG . ASN A 1 674 ? -41.948 57.130 16.698 1.00 188.19 ? 674 ASN A CG 1 ATOM 5212 O OD1 . ASN A 1 674 ? -41.377 58.013 17.340 1.00 183.86 ? 674 ASN A OD1 1 ATOM 5213 N ND2 . ASN A 1 674 ? -42.950 57.384 15.861 1.00 233.53 ? 674 ASN A ND2 1 ATOM 5214 N N . GLN A 1 675 ? -38.943 55.208 19.432 1.00 128.38 ? 675 GLN A N 1 ATOM 5215 C CA . GLN A 1 675 ? -38.729 55.255 20.878 1.00 131.93 ? 675 GLN A CA 1 ATOM 5216 C C . GLN A 1 675 ? -39.883 54.624 21.655 1.00 135.28 ? 675 GLN A C 1 ATOM 5217 O O . GLN A 1 675 ? -40.340 55.173 22.658 1.00 135.70 ? 675 GLN A O 1 ATOM 5218 C CB . GLN A 1 675 ? -38.509 56.698 21.347 1.00 135.35 ? 675 GLN A CB 1 ATOM 5219 C CG . GLN A 1 675 ? -37.112 57.243 21.080 1.00 136.81 ? 675 GLN A CG 1 ATOM 5220 C CD . GLN A 1 675 ? -36.847 57.503 19.610 1.00 144.74 ? 675 GLN A CD 1 ATOM 5221 O OE1 . GLN A 1 675 ? -37.773 57.708 18.826 1.00 141.99 ? 675 GLN A OE1 1 ATOM 5222 N NE2 . GLN A 1 675 ? -35.575 57.496 19.228 1.00 138.69 ? 675 GLN A NE2 1 ATOM 5223 N N . THR A 1 676 ? -40.350 53.471 21.186 1.00 139.65 ? 676 THR A N 1 ATOM 5224 C CA . THR A 1 676 ? -41.418 52.738 21.862 1.00 135.18 ? 676 THR A CA 1 ATOM 5225 C C . THR A 1 676 ? -41.059 51.264 22.025 1.00 130.38 ? 676 THR A C 1 ATOM 5226 O O . THR A 1 676 ? -40.376 50.686 21.181 1.00 136.99 ? 676 THR A O 1 ATOM 5227 C CB . THR A 1 676 ? -42.755 52.841 21.100 1.00 127.15 ? 676 THR A CB 1 ATOM 5228 O OG1 . THR A 1 676 ? -42.598 52.312 19.778 1.00 129.70 ? 676 THR A OG1 1 ATOM 5229 C CG2 . THR A 1 676 ? -43.221 54.287 21.014 1.00 131.37 ? 676 THR A CG2 1 ATOM 5230 N N . ARG A 1 677 ? -41.524 50.661 23.115 1.00 117.39 ? 677 ARG A N 1 ATOM 5231 C CA . ARG A 1 677 ? -41.312 49.238 23.350 1.00 125.74 ? 677 ARG A CA 1 ATOM 5232 C C . ARG A 1 677 ? -42.627 48.483 23.189 1.00 138.65 ? 677 ARG A C 1 ATOM 5233 O O . ARG A 1 677 ? -43.536 48.626 24.006 1.00 145.74 ? 677 ARG A O 1 ATOM 5234 C CB . ARG A 1 677 ? -40.724 49.000 24.743 1.00 121.75 ? 677 ARG A CB 1 ATOM 5235 C CG . ARG A 1 677 ? -39.529 49.884 25.064 1.00 131.97 ? 677 ARG A CG 1 ATOM 5236 C CD . ARG A 1 677 ? -38.954 49.590 26.443 1.00 118.66 ? 677 ARG A CD 1 ATOM 5237 N NE . ARG A 1 677 ? -38.252 48.311 26.493 1.00 117.76 ? 677 ARG A NE 1 ATOM 5238 C CZ . ARG A 1 677 ? -38.722 47.221 27.092 1.00 115.78 ? 677 ARG A CZ 1 ATOM 5239 N NH1 . ARG A 1 677 ? -39.897 47.252 27.704 1.00 122.95 ? 677 ARG A NH1 1 ATOM 5240 N NH2 . ARG A 1 677 ? -38.011 46.101 27.085 1.00 101.14 ? 677 ARG A NH2 1 ATOM 5241 N N . GLN A 1 678 ? -42.724 47.683 22.132 1.00 136.17 ? 678 GLN A N 1 ATOM 5242 C CA . GLN A 1 678 ? -43.969 46.993 21.812 1.00 117.71 ? 678 GLN A CA 1 ATOM 5243 C C . GLN A 1 678 ? -43.753 45.553 21.358 1.00 108.28 ? 678 GLN A C 1 ATOM 5244 O O . GLN A 1 678 ? -42.693 45.202 20.841 1.00 105.43 ? 678 GLN A O 1 ATOM 5245 C CB . GLN A 1 678 ? -44.730 47.755 20.722 1.00 120.75 ? 678 GLN A CB 1 ATOM 5246 C CG . GLN A 1 678 ? -45.277 49.105 21.151 1.00 129.56 ? 678 GLN A CG 1 ATOM 5247 C CD . GLN A 1 678 ? -45.935 49.852 20.007 1.00 127.33 ? 678 GLN A CD 1 ATOM 5248 O OE1 . GLN A 1 678 ? -45.601 49.643 18.841 1.00 120.58 ? 678 GLN A OE1 1 ATOM 5249 N NE2 . GLN A 1 678 ? -46.880 50.726 20.337 1.00 127.02 ? 678 GLN A NE2 1 ATOM 5250 N N . VAL A 1 679 ? -44.775 44.726 21.556 1.00 112.29 ? 679 VAL A N 1 ATOM 5251 C CA . VAL A 1 679 ? -44.801 43.378 21.002 1.00 115.44 ? 679 VAL A CA 1 ATOM 5252 C C . VAL A 1 679 ? -46.064 43.207 20.161 1.00 107.52 ? 679 VAL A C 1 ATOM 5253 O O . VAL A 1 679 ? -47.181 43.386 20.649 1.00 107.26 ? 679 VAL A O 1 ATOM 5254 C CB . VAL A 1 679 ? -44.737 42.298 22.105 1.00 117.64 ? 679 VAL A CB 1 ATOM 5255 C CG1 . VAL A 1 679 ? -45.505 42.742 23.338 1.00 113.66 ? 679 VAL A CG1 1 ATOM 5256 C CG2 . VAL A 1 679 ? -45.250 40.960 21.583 1.00 110.39 ? 679 VAL A CG2 1 ATOM 5257 N N . VAL A 1 680 ? -45.874 42.872 18.889 1.00 106.87 ? 680 VAL A N 1 ATOM 5258 C CA . VAL A 1 680 ? -46.975 42.796 17.937 1.00 106.93 ? 680 VAL A CA 1 ATOM 5259 C C . VAL A 1 680 ? -47.232 41.357 17.492 1.00 108.60 ? 680 VAL A C 1 ATOM 5260 O O . VAL A 1 680 ? -46.305 40.634 17.128 1.00 110.01 ? 680 VAL A O 1 ATOM 5261 C CB . VAL A 1 680 ? -46.696 43.688 16.702 1.00 109.89 ? 680 VAL A CB 1 ATOM 5262 C CG1 . VAL A 1 680 ? -45.217 43.654 16.340 1.00 119.89 ? 680 VAL A CG1 1 ATOM 5263 C CG2 . VAL A 1 680 ? -47.561 43.275 15.519 1.00 117.17 ? 680 VAL A CG2 1 ATOM 5264 N N . CYS A 1 681 ? -48.497 40.947 17.534 1.00 108.69 ? 681 CYS A N 1 ATOM 5265 C CA . CYS A 1 681 ? -48.880 39.591 17.154 1.00 112.05 ? 681 CYS A CA 1 ATOM 5266 C C . CYS A 1 681 ? -49.824 39.593 15.956 1.00 115.93 ? 681 CYS A C 1 ATOM 5267 O O . CYS A 1 681 ? -50.750 40.402 15.887 1.00 118.55 ? 681 CYS A O 1 ATOM 5268 C CB . CYS A 1 681 ? -49.539 38.873 18.334 1.00 117.20 ? 681 CYS A CB 1 ATOM 5269 S SG . CYS A 1 681 ? -48.553 38.857 19.847 1.00 148.30 ? 681 CYS A SG 1 ATOM 5270 N N . ASP A 1 682 ? -49.590 38.681 15.016 1.00 119.57 ? 682 ASP A N 1 ATOM 5271 C CA . ASP A 1 682 ? -50.445 38.570 13.839 1.00 115.44 ? 682 ASP A CA 1 ATOM 5272 C C . ASP A 1 682 ? -51.801 37.971 14.198 1.00 112.47 ? 682 ASP A C 1 ATOM 5273 O O . ASP A 1 682 ? -51.881 36.870 14.742 1.00 113.76 ? 682 ASP A O 1 ATOM 5274 C CB . ASP A 1 682 ? -49.769 37.716 12.762 1.00 116.99 ? 682 ASP A CB 1 ATOM 5275 C CG . ASP A 1 682 ? -48.519 38.366 12.201 1.00 128.65 ? 682 ASP A CG 1 ATOM 5276 O OD1 . ASP A 1 682 ? -47.559 37.635 11.875 1.00 133.99 ? 682 ASP A OD1 1 ATOM 5277 O OD2 . ASP A 1 682 ? -48.496 39.609 12.087 1.00 140.19 ? 682 ASP A OD2 1 ATOM 5278 N N . LEU A 1 683 ? -52.866 38.706 13.895 1.00 114.21 ? 683 LEU A N 1 ATOM 5279 C CA . LEU A 1 683 ? -54.224 38.225 14.124 1.00 110.50 ? 683 LEU A CA 1 ATOM 5280 C C . LEU A 1 683 ? -54.816 37.632 12.848 1.00 111.99 ? 683 LEU A C 1 ATOM 5281 O O . LEU A 1 683 ? -55.984 37.244 12.813 1.00 109.23 ? 683 LEU A O 1 ATOM 5282 C CB . LEU A 1 683 ? -55.109 39.351 14.661 1.00 106.16 ? 683 LEU A CB 1 ATOM 5283 C CG . LEU A 1 683 ? -54.754 39.800 16.080 1.00 103.32 ? 683 LEU A CG 1 ATOM 5284 C CD1 . LEU A 1 683 ? -55.697 40.887 16.561 1.00 99.80 ? 683 LEU A CD1 1 ATOM 5285 C CD2 . LEU A 1 683 ? -54.766 38.616 17.035 1.00 102.53 ? 683 LEU A CD2 1 ATOM 5286 N N . GLY A 1 684 ? -53.997 37.568 11.804 1.00 115.70 ? 684 GLY A N 1 ATOM 5287 C CA . GLY A 1 684 ? -54.413 37.034 10.521 1.00 119.62 ? 684 GLY A CA 1 ATOM 5288 C C . GLY A 1 684 ? -54.663 38.108 9.481 1.00 113.93 ? 684 GLY A C 1 ATOM 5289 O O . GLY A 1 684 ? -55.073 39.223 9.800 1.00 110.91 ? 684 GLY A O 1 ATOM 5290 N N . ASN A 1 685 ? -54.413 37.758 8.224 1.00 113.72 ? 685 ASN A N 1 ATOM 5291 C CA . ASN A 1 685 ? -54.497 38.702 7.116 1.00 111.87 ? 685 ASN A CA 1 ATOM 5292 C C . ASN A 1 685 ? -55.241 38.117 5.919 1.00 115.83 ? 685 ASN A C 1 ATOM 5293 O O . ASN A 1 685 ? -54.631 37.460 5.075 1.00 130.24 ? 685 ASN A O 1 ATOM 5294 C CB . ASN A 1 685 ? -53.096 39.151 6.698 1.00 111.98 ? 685 ASN A CB 1 ATOM 5295 C CG . ASN A 1 685 ? -53.120 40.284 5.690 1.00 112.68 ? 685 ASN A CG 1 ATOM 5296 O OD1 . ASN A 1 685 ? -54.150 40.926 5.481 1.00 126.53 ? 685 ASN A OD1 1 ATOM 5297 N ND2 . ASN A 1 685 ? -51.978 40.540 5.064 1.00 111.99 ? 685 ASN A ND2 1 ATOM 5298 N N . PRO A 1 686 ? -56.560 38.350 5.834 1.00 110.25 ? 686 PRO A N 1 ATOM 5299 C CA . PRO A 1 686 ? -57.412 39.133 6.736 1.00 107.33 ? 686 PRO A CA 1 ATOM 5300 C C . PRO A 1 686 ? -57.787 38.405 8.023 1.00 110.58 ? 686 PRO A C 1 ATOM 5301 O O . PRO A 1 686 ? -57.637 37.187 8.115 1.00 112.65 ? 686 PRO A O 1 ATOM 5302 C CB . PRO A 1 686 ? -58.674 39.397 5.896 1.00 105.33 ? 686 PRO A CB 1 ATOM 5303 C CG . PRO A 1 686 ? -58.349 38.928 4.503 1.00 113.22 ? 686 PRO A CG 1 ATOM 5304 C CD . PRO A 1 686 ? -57.323 37.863 4.676 1.00 111.08 ? 686 PRO A CD 1 ATOM 5305 N N . MET A 1 687 ? -58.269 39.159 9.006 1.00 110.84 ? 687 MET A N 1 ATOM 5306 C CA . MET A 1 687 ? -58.922 38.568 10.164 1.00 103.31 ? 687 MET A CA 1 ATOM 5307 C C . MET A 1 687 ? -60.414 38.509 9.869 1.00 100.62 ? 687 MET A C 1 ATOM 5308 O O . MET A 1 687 ? -61.084 39.539 9.809 1.00 99.18 ? 687 MET A O 1 ATOM 5309 C CB . MET A 1 687 ? -58.647 39.379 11.431 1.00 101.85 ? 687 MET A CB 1 ATOM 5310 C CG . MET A 1 687 ? -59.319 38.833 12.683 1.00 105.35 ? 687 MET A CG 1 ATOM 5311 S SD . MET A 1 687 ? -58.964 39.825 14.148 1.00 105.45 ? 687 MET A SD 1 ATOM 5312 C CE . MET A 1 687 ? -59.844 38.912 15.412 1.00 96.18 ? 687 MET A CE 1 ATOM 5313 N N . LYS A 1 688 ? -60.929 37.297 9.691 1.00 117.46 ? 688 LYS A N 1 ATOM 5314 C CA . LYS A 1 688 ? -62.290 37.105 9.203 1.00 102.63 ? 688 LYS A CA 1 ATOM 5315 C C . LYS A 1 688 ? -63.342 37.448 10.249 1.00 97.10 ? 688 LYS A C 1 ATOM 5316 O O . LYS A 1 688 ? -63.051 37.519 11.442 1.00 106.75 ? 688 LYS A O 1 ATOM 5317 C CB . LYS A 1 688 ? -62.482 35.665 8.724 1.00 99.64 ? 688 LYS A CB 1 ATOM 5318 C CG . LYS A 1 688 ? -61.595 35.290 7.550 1.00 102.53 ? 688 LYS A CG 1 ATOM 5319 C CD . LYS A 1 688 ? -61.858 33.868 7.090 1.00 106.26 ? 688 LYS A CD 1 ATOM 5320 C CE . LYS A 1 688 ? -63.289 33.703 6.608 1.00 119.14 ? 688 LYS A CE 1 ATOM 5321 N NZ . LYS A 1 688 ? -63.568 32.305 6.182 1.00 123.30 ? 688 LYS A NZ 1 ATOM 5322 N N . ALA A 1 689 ? -64.563 37.678 9.777 1.00 98.80 ? 689 ALA A N 1 ATOM 5323 C CA . ALA A 1 689 ? -65.685 38.035 10.638 1.00 116.43 ? 689 ALA A CA 1 ATOM 5324 C C . ALA A 1 689 ? -65.980 36.961 11.681 1.00 124.97 ? 689 ALA A C 1 ATOM 5325 O O . ALA A 1 689 ? -65.862 35.766 11.409 1.00 115.56 ? 689 ALA A O 1 ATOM 5326 C CB . ALA A 1 689 ? -66.922 38.299 9.794 1.00 112.35 ? 689 ALA A CB 1 ATOM 5327 N N . GLY A 1 690 ? -66.358 37.398 12.878 1.00 122.83 ? 690 GLY A N 1 ATOM 5328 C CA . GLY A 1 690 ? -66.745 36.489 13.942 1.00 126.93 ? 690 GLY A CA 1 ATOM 5329 C C . GLY A 1 690 ? -65.585 35.766 14.600 1.00 132.31 ? 690 GLY A C 1 ATOM 5330 O O . GLY A 1 690 ? -65.786 34.964 15.512 1.00 145.96 ? 690 GLY A O 1 ATOM 5331 N N . THR A 1 691 ? -64.369 36.052 14.144 1.00 132.58 ? 691 THR A N 1 ATOM 5332 C CA . THR A 1 691 ? -63.177 35.402 14.678 1.00 117.46 ? 691 THR A CA 1 ATOM 5333 C C . THR A 1 691 ? -62.932 35.779 16.134 1.00 123.50 ? 691 THR A C 1 ATOM 5334 O O . THR A 1 691 ? -62.884 36.957 16.475 1.00 126.56 ? 691 THR A O 1 ATOM 5335 C CB . THR A 1 691 ? -61.922 35.760 13.856 1.00 97.12 ? 691 THR A CB 1 ATOM 5336 O OG1 . THR A 1 691 ? -62.034 35.204 12.540 1.00 105.90 ? 691 THR A OG1 1 ATOM 5337 C CG2 . THR A 1 691 ? -60.669 35.215 14.524 1.00 97.61 ? 691 THR A CG2 1 ATOM 5338 N N . GLN A 1 692 ? -62.780 34.770 16.987 1.00 123.32 ? 692 GLN A N 1 ATOM 5339 C CA . GLN A 1 692 ? -62.424 34.987 18.383 1.00 112.74 ? 692 GLN A CA 1 ATOM 5340 C C . GLN A 1 692 ? -61.176 34.184 18.732 1.00 110.04 ? 692 GLN A C 1 ATOM 5341 O O . GLN A 1 692 ? -61.198 32.954 18.715 1.00 129.03 ? 692 GLN A O 1 ATOM 5342 C CB . GLN A 1 692 ? -63.577 34.597 19.310 1.00 130.47 ? 692 GLN A CB 1 ATOM 5343 C CG . GLN A 1 692 ? -64.860 35.374 19.080 1.00 144.60 ? 692 GLN A CG 1 ATOM 5344 C CD . GLN A 1 692 ? -65.938 35.023 20.087 1.00 150.91 ? 692 GLN A CD 1 ATOM 5345 O OE1 . GLN A 1 692 ? -65.675 34.354 21.086 1.00 133.49 ? 692 GLN A OE1 1 ATOM 5346 N NE2 . GLN A 1 692 ? -67.159 35.472 19.827 1.00 161.11 ? 692 GLN A NE2 1 ATOM 5347 N N . LEU A 1 693 ? -60.091 34.882 19.049 1.00 98.63 ? 693 LEU A N 1 ATOM 5348 C CA . LEU A 1 693 ? -58.829 34.220 19.364 1.00 105.45 ? 693 LEU A CA 1 ATOM 5349 C C . LEU A 1 693 ? -58.466 34.352 20.840 1.00 111.08 ? 693 LEU A C 1 ATOM 5350 O O . LEU A 1 693 ? -58.759 35.364 21.476 1.00 109.02 ? 693 LEU A O 1 ATOM 5351 C CB . LEU A 1 693 ? -57.699 34.780 18.494 1.00 97.91 ? 693 LEU A CB 1 ATOM 5352 C CG . LEU A 1 693 ? -57.796 34.493 16.994 1.00 104.33 ? 693 LEU A CG 1 ATOM 5353 C CD1 . LEU A 1 693 ? -56.515 34.897 16.281 1.00 117.06 ? 693 LEU A CD1 1 ATOM 5354 C CD2 . LEU A 1 693 ? -58.114 33.026 16.742 1.00 104.92 ? 693 LEU A CD2 1 ATOM 5355 N N . LEU A 1 694 ? -57.827 33.316 21.374 1.00 112.34 ? 694 LEU A N 1 ATOM 5356 C CA . LEU A 1 694 ? -57.421 33.292 22.773 1.00 111.70 ? 694 LEU A CA 1 ATOM 5357 C C . LEU A 1 694 ? -55.968 32.845 22.901 1.00 114.21 ? 694 LEU A C 1 ATOM 5358 O O . LEU A 1 694 ? -55.629 31.716 22.549 1.00 134.71 ? 694 LEU A O 1 ATOM 5359 C CB . LEU A 1 694 ? -58.333 32.361 23.576 1.00 129.28 ? 694 LEU A CB 1 ATOM 5360 C CG . LEU A 1 694 ? -58.887 32.888 24.901 1.00 135.25 ? 694 LEU A CG 1 ATOM 5361 C CD1 . LEU A 1 694 ? -57.762 33.283 25.839 1.00 138.27 ? 694 LEU A CD1 1 ATOM 5362 C CD2 . LEU A 1 694 ? -59.824 34.057 24.660 1.00 131.48 ? 694 LEU A CD2 1 ATOM 5363 N N . ALA A 1 695 ? -55.113 33.731 23.405 1.00 106.54 ? 695 ALA A N 1 ATOM 5364 C CA . ALA A 1 695 ? -53.692 33.425 23.540 1.00 116.00 ? 695 ALA A CA 1 ATOM 5365 C C . ALA A 1 695 ? -53.068 34.125 24.742 1.00 112.65 ? 695 ALA A C 1 ATOM 5366 O O . ALA A 1 695 ? -53.405 35.267 25.052 1.00 116.57 ? 695 ALA A O 1 ATOM 5367 C CB . ALA A 1 695 ? -52.951 33.808 22.271 1.00 114.31 ? 695 ALA A CB 1 ATOM 5368 N N . GLY A 1 696 ? -52.154 33.432 25.415 1.00 108.91 ? 696 GLY A N 1 ATOM 5369 C CA . GLY A 1 696 ? -51.435 34.007 26.536 1.00 110.61 ? 696 GLY A CA 1 ATOM 5370 C C . GLY A 1 696 ? -50.103 34.605 26.127 1.00 111.73 ? 696 GLY A C 1 ATOM 5371 O O . GLY A 1 696 ? -49.514 34.201 25.125 1.00 109.37 ? 696 GLY A O 1 ATOM 5372 N N . LEU A 1 697 ? -49.626 35.568 26.909 1.00 117.90 ? 697 LEU A N 1 ATOM 5373 C CA . LEU A 1 697 ? -48.335 36.199 26.658 1.00 111.21 ? 697 LEU A CA 1 ATOM 5374 C C . LEU A 1 697 ? -47.521 36.276 27.946 1.00 111.06 ? 697 LEU A C 1 ATOM 5375 O O . LEU A 1 697 ? -47.928 36.932 28.906 1.00 110.11 ? 697 LEU A O 1 ATOM 5376 C CB . LEU A 1 697 ? -48.522 37.597 26.064 1.00 110.20 ? 697 LEU A CB 1 ATOM 5377 C CG . LEU A 1 697 ? -49.190 37.693 24.690 1.00 108.86 ? 697 LEU A CG 1 ATOM 5378 C CD1 . LEU A 1 697 ? -49.349 39.146 24.267 1.00 108.17 ? 697 LEU A CD1 1 ATOM 5379 C CD2 . LEU A 1 697 ? -48.399 36.915 23.651 1.00 110.75 ? 697 LEU A CD2 1 ATOM 5380 N N . ARG A 1 698 ? -46.370 35.610 27.965 1.00 113.48 ? 698 ARG A N 1 ATOM 5381 C CA . ARG A 1 698 ? -45.540 35.559 29.166 1.00 108.34 ? 698 ARG A CA 1 ATOM 5382 C C . ARG A 1 698 ? -44.511 36.685 29.210 1.00 109.78 ? 698 ARG A C 1 ATOM 5383 O O . ARG A 1 698 ? -43.804 36.939 28.235 1.00 109.67 ? 698 ARG A O 1 ATOM 5384 C CB . ARG A 1 698 ? -44.837 34.202 29.270 1.00 111.28 ? 698 ARG A CB 1 ATOM 5385 C CG . ARG A 1 698 ? -45.747 33.083 29.751 1.00 118.77 ? 698 ARG A CG 1 ATOM 5386 C CD . ARG A 1 698 ? -44.989 31.785 29.974 1.00 107.85 ? 698 ARG A CD 1 ATOM 5387 N NE . ARG A 1 698 ? -44.777 31.049 28.732 1.00 116.64 ? 698 ARG A NE 1 ATOM 5388 C CZ . ARG A 1 698 ? -44.226 29.842 28.668 1.00 134.63 ? 698 ARG A CZ 1 ATOM 5389 N NH1 . ARG A 1 698 ? -43.830 29.234 29.777 1.00 147.52 ? 698 ARG A NH1 1 ATOM 5390 N NH2 . ARG A 1 698 ? -44.072 29.242 27.496 1.00 122.34 ? 698 ARG A NH2 1 ATOM 5391 N N . PHE A 1 699 ? -44.437 37.355 30.356 1.00 114.14 ? 699 PHE A N 1 ATOM 5392 C CA . PHE A 1 699 ? -43.501 38.455 30.554 1.00 126.82 ? 699 PHE A CA 1 ATOM 5393 C C . PHE A 1 699 ? -42.734 38.305 31.865 1.00 135.50 ? 699 PHE A C 1 ATOM 5394 O O . PHE A 1 699 ? -43.110 37.514 32.730 1.00 130.72 ? 699 PHE A O 1 ATOM 5395 C CB . PHE A 1 699 ? -44.235 39.797 30.539 1.00 121.06 ? 699 PHE A CB 1 ATOM 5396 C CG . PHE A 1 699 ? -44.781 40.181 29.194 1.00 116.42 ? 699 PHE A CG 1 ATOM 5397 C CD1 . PHE A 1 699 ? -44.033 40.961 28.328 1.00 126.44 ? 699 PHE A CD1 1 ATOM 5398 C CD2 . PHE A 1 699 ? -46.044 39.772 28.800 1.00 113.84 ? 699 PHE A CD2 1 ATOM 5399 C CE1 . PHE A 1 699 ? -44.533 41.321 27.091 1.00 129.78 ? 699 PHE A CE1 1 ATOM 5400 C CE2 . PHE A 1 699 ? -46.549 40.131 27.564 1.00 116.40 ? 699 PHE A CE2 1 ATOM 5401 C CZ . PHE A 1 699 ? -45.792 40.906 26.709 1.00 127.42 ? 699 PHE A CZ 1 ATOM 5402 N N . SER A 1 700 ? -41.656 39.071 32.002 1.00 128.97 ? 700 SER A N 1 ATOM 5403 C CA . SER A 1 700 ? -40.879 39.094 33.236 1.00 128.51 ? 700 SER A CA 1 ATOM 5404 C C . SER A 1 700 ? -40.687 40.528 33.714 1.00 122.61 ? 700 SER A C 1 ATOM 5405 O O . SER A 1 700 ? -40.055 41.338 33.038 1.00 112.40 ? 700 SER A O 1 ATOM 5406 C CB . SER A 1 700 ? -39.521 38.416 33.039 1.00 141.77 ? 700 SER A CB 1 ATOM 5407 O OG . SER A 1 700 ? -38.767 38.419 34.238 1.00 149.99 ? 700 SER A OG 1 ATOM 5408 N N . VAL A 1 701 ? -41.242 40.842 34.879 1.00 122.18 ? 701 VAL A N 1 ATOM 5409 C CA . VAL A 1 701 ? -41.118 42.179 35.442 1.00 117.31 ? 701 VAL A CA 1 ATOM 5410 C C . VAL A 1 701 ? -40.107 42.186 36.580 1.00 123.82 ? 701 VAL A C 1 ATOM 5411 O O . VAL A 1 701 ? -40.149 41.326 37.459 1.00 127.68 ? 701 VAL A O 1 ATOM 5412 C CB . VAL A 1 701 ? -42.472 42.704 35.958 1.00 113.38 ? 701 VAL A CB 1 ATOM 5413 C CG1 . VAL A 1 701 ? -42.337 44.138 36.447 1.00 118.55 ? 701 VAL A CG1 1 ATOM 5414 C CG2 . VAL A 1 701 ? -43.528 42.607 34.869 1.00 114.22 ? 701 VAL A CG2 1 ATOM 5415 N N . HIS A 1 702 ? -39.195 43.153 36.561 1.00 127.79 ? 702 HIS A N 1 ATOM 5416 C CA . HIS A 1 702 ? -38.201 43.259 37.620 1.00 145.47 ? 702 HIS A CA 1 ATOM 5417 C C . HIS A 1 702 ? -38.587 44.369 38.593 1.00 149.63 ? 702 HIS A C 1 ATOM 5418 O O . HIS A 1 702 ? -39.112 44.093 39.673 1.00 136.48 ? 702 HIS A O 1 ATOM 5419 C CB . HIS A 1 702 ? -36.817 43.527 37.027 1.00 146.79 ? 702 HIS A CB 1 ATOM 5420 C CG . HIS A 1 702 ? -36.549 42.780 35.757 1.00 147.83 ? 702 HIS A CG 1 ATOM 5421 N ND1 . HIS A 1 702 ? -36.287 41.427 35.731 1.00 147.81 ? 702 HIS A ND1 1 ATOM 5422 C CD2 . HIS A 1 702 ? -36.503 43.197 34.470 1.00 140.76 ? 702 HIS A CD2 1 ATOM 5423 C CE1 . HIS A 1 702 ? -36.091 41.043 34.482 1.00 144.19 ? 702 HIS A CE1 1 ATOM 5424 N NE2 . HIS A 1 702 ? -36.217 42.098 33.697 1.00 135.55 ? 702 HIS A NE2 1 ATOM 5425 N N . GLN A 1 703 ? -38.348 45.613 38.179 1.00 153.41 ? 703 GLN A N 1 ATOM 5426 C CA . GLN A 1 703 ? -38.755 46.813 38.914 1.00 150.19 ? 703 GLN A CA 1 ATOM 5427 C C . GLN A 1 703 ? -38.263 48.069 38.204 1.00 150.23 ? 703 GLN A C 1 ATOM 5428 O O . GLN A 1 703 ? -37.358 48.010 37.372 1.00 151.32 ? 703 GLN A O 1 ATOM 5429 C CB . GLN A 1 703 ? -38.223 46.805 40.351 1.00 138.53 ? 703 GLN A CB 1 ATOM 5430 C CG . GLN A 1 703 ? -36.714 46.687 40.465 1.00 127.80 ? 703 GLN A CG 1 ATOM 5431 C CD . GLN A 1 703 ? -36.232 46.797 41.897 1.00 152.96 ? 703 GLN A CD 1 ATOM 5432 O OE1 . GLN A 1 703 ? -36.885 47.416 42.738 1.00 158.75 ? 703 GLN A OE1 1 ATOM 5433 N NE2 . GLN A 1 703 ? -35.086 46.190 42.185 1.00 161.93 ? 703 GLN A NE2 1 ATOM 5434 N N . GLN A 1 704 ? -38.866 49.205 38.537 1.00 145.61 ? 704 GLN A N 1 ATOM 5435 C CA . GLN A 1 704 ? -38.377 50.500 38.076 1.00 149.25 ? 704 GLN A CA 1 ATOM 5436 C C . GLN A 1 704 ? -38.239 51.435 39.266 1.00 156.83 ? 704 GLN A C 1 ATOM 5437 O O . GLN A 1 704 ? -39.241 51.831 39.863 1.00 153.69 ? 704 GLN A O 1 ATOM 5438 C CB . GLN A 1 704 ? -39.318 51.102 37.031 1.00 139.03 ? 704 GLN A CB 1 ATOM 5439 C CG . GLN A 1 704 ? -38.676 51.328 35.671 1.00 132.81 ? 704 GLN A CG 1 ATOM 5440 C CD . GLN A 1 704 ? -37.805 52.569 35.625 1.00 143.84 ? 704 GLN A CD 1 ATOM 5441 O OE1 . GLN A 1 704 ? -37.672 53.288 36.615 1.00 160.07 ? 704 GLN A OE1 1 ATOM 5442 N NE2 . GLN A 1 704 ? -37.212 52.829 34.465 1.00 135.89 ? 704 GLN A NE2 1 ATOM 5443 N N . SER A 1 705 ? -37.000 51.798 39.590 1.00 164.72 ? 705 SER A N 1 ATOM 5444 C CA . SER A 1 705 ? -36.707 52.565 40.796 1.00 173.20 ? 705 SER A CA 1 ATOM 5445 C C . SER A 1 705 ? -37.403 51.933 41.999 1.00 171.74 ? 705 SER A C 1 ATOM 5446 O O . SER A 1 705 ? -37.301 50.726 42.222 1.00 166.97 ? 705 SER A O 1 ATOM 5447 C CB . SER A 1 705 ? -37.136 54.025 40.632 1.00 166.49 ? 705 SER A CB 1 ATOM 5448 O OG . SER A 1 705 ? -36.493 54.625 39.522 1.00 159.23 ? 705 SER A OG 1 ATOM 5449 N N . GLU A 1 706 ? -38.119 52.753 42.762 1.00 158.26 ? 706 GLU A N 1 ATOM 5450 C CA . GLU A 1 706 ? -38.946 52.265 43.860 1.00 136.22 ? 706 GLU A CA 1 ATOM 5451 C C . GLU A 1 706 ? -40.236 53.079 43.940 1.00 139.24 ? 706 GLU A C 1 ATOM 5452 O O . GLU A 1 706 ? -40.410 54.042 43.194 1.00 134.40 ? 706 GLU A O 1 ATOM 5453 C CB . GLU A 1 706 ? -38.181 52.337 45.186 1.00 126.68 ? 706 GLU A CB 1 ATOM 5454 C CG . GLU A 1 706 ? -37.025 51.349 45.301 1.00 130.37 ? 706 GLU A CG 1 ATOM 5455 C CD . GLU A 1 706 ? -35.992 51.768 46.329 1.00 149.80 ? 706 GLU A CD 1 ATOM 5456 O OE1 . GLU A 1 706 ? -36.225 52.772 47.033 1.00 172.90 ? 706 GLU A OE1 1 ATOM 5457 O OE2 . GLU A 1 706 ? -34.943 51.096 46.428 1.00 125.88 ? 706 GLU A OE2 1 ATOM 5458 N N . MET A 1 707 ? -41.122 52.693 44.856 1.00 149.90 ? 707 MET A N 1 ATOM 5459 C CA . MET A 1 707 ? -42.386 53.396 45.092 1.00 155.22 ? 707 MET A CA 1 ATOM 5460 C C . MET A 1 707 ? -43.223 53.586 43.822 1.00 144.75 ? 707 MET A C 1 ATOM 5461 O O . MET A 1 707 ? -43.814 54.647 43.622 1.00 147.41 ? 707 MET A O 1 ATOM 5462 C CB . MET A 1 707 ? -42.122 54.766 45.728 1.00 157.87 ? 707 MET A CB 1 ATOM 5463 C CG . MET A 1 707 ? -41.025 54.781 46.783 1.00 167.64 ? 707 MET A CG 1 ATOM 5464 S SD . MET A 1 707 ? -40.632 56.457 47.322 1.00 197.89 ? 707 MET A SD 1 ATOM 5465 C CE . MET A 1 707 ? -39.178 56.168 48.326 1.00 147.78 ? 707 MET A CE 1 ATOM 5466 N N . ASP A 1 708 ? -43.275 52.565 42.972 1.00 139.97 ? 708 ASP A N 1 ATOM 5467 C CA . ASP A 1 708 ? -43.963 52.684 41.686 1.00 139.55 ? 708 ASP A CA 1 ATOM 5468 C C . ASP A 1 708 ? -45.409 52.193 41.700 1.00 141.41 ? 708 ASP A C 1 ATOM 5469 O O . ASP A 1 708 ? -46.106 52.305 40.691 1.00 140.95 ? 708 ASP A O 1 ATOM 5470 C CB . ASP A 1 708 ? -43.193 51.924 40.604 1.00 140.50 ? 708 ASP A CB 1 ATOM 5471 C CG . ASP A 1 708 ? -42.108 52.762 39.963 1.00 141.09 ? 708 ASP A CG 1 ATOM 5472 O OD1 . ASP A 1 708 ? -41.518 53.610 40.663 1.00 154.98 ? 708 ASP A OD1 1 ATOM 5473 O OD2 . ASP A 1 708 ? -41.847 52.575 38.756 1.00 127.85 ? 708 ASP A OD2 1 ATOM 5474 N N . THR A 1 709 ? -45.850 51.660 42.837 1.00 142.86 ? 709 THR A N 1 ATOM 5475 C CA . THR A 1 709 ? -47.187 51.082 42.968 1.00 145.04 ? 709 THR A CA 1 ATOM 5476 C C . THR A 1 709 ? -47.433 50.042 41.872 1.00 147.60 ? 709 THR A C 1 ATOM 5477 O O . THR A 1 709 ? -46.715 49.051 41.785 1.00 163.83 ? 709 THR A O 1 ATOM 5478 C CB . THR A 1 709 ? -48.287 52.165 42.925 1.00 153.59 ? 709 THR A CB 1 ATOM 5479 O OG1 . THR A 1 709 ? -47.795 53.372 43.520 1.00 164.17 ? 709 THR A OG1 1 ATOM 5480 C CG2 . THR A 1 709 ? -49.529 51.703 43.681 1.00 154.21 ? 709 THR A CG2 1 ATOM 5481 N N . SER A 1 710 ? -48.432 50.273 41.026 1.00 140.94 ? 710 SER A N 1 ATOM 5482 C CA . SER A 1 710 ? -48.781 49.317 39.977 1.00 138.45 ? 710 SER A CA 1 ATOM 5483 C C . SER A 1 710 ? -47.912 49.473 38.729 1.00 135.66 ? 710 SER A C 1 ATOM 5484 O O . SER A 1 710 ? -47.028 50.327 38.675 1.00 138.80 ? 710 SER A O 1 ATOM 5485 C CB . SER A 1 710 ? -50.258 49.464 39.601 1.00 151.34 ? 710 SER A CB 1 ATOM 5486 O OG . SER A 1 710 ? -50.532 50.763 39.106 1.00 144.36 ? 710 SER A OG 1 ATOM 5487 N N . VAL A 1 711 ? -48.171 48.634 37.729 1.00 132.81 ? 711 VAL A N 1 ATOM 5488 C CA . VAL A 1 711 ? -47.474 48.707 36.448 1.00 132.34 ? 711 VAL A CA 1 ATOM 5489 C C . VAL A 1 711 ? -48.466 48.428 35.314 1.00 142.62 ? 711 VAL A C 1 ATOM 5490 O O . VAL A 1 711 ? -49.328 47.557 35.434 1.00 149.05 ? 711 VAL A O 1 ATOM 5491 C CB . VAL A 1 711 ? -46.282 47.720 36.395 1.00 128.99 ? 711 VAL A CB 1 ATOM 5492 C CG1 . VAL A 1 711 ? -46.734 46.307 36.722 1.00 128.18 ? 711 VAL A CG1 1 ATOM 5493 C CG2 . VAL A 1 711 ? -45.587 47.775 35.041 1.00 125.46 ? 711 VAL A CG2 1 ATOM 5494 N N . LYS A 1 712 ? -48.349 49.176 34.220 1.00 138.57 ? 712 LYS A N 1 ATOM 5495 C CA . LYS A 1 712 ? -49.377 49.180 33.182 1.00 134.97 ? 712 LYS A CA 1 ATOM 5496 C C . LYS A 1 712 ? -49.033 48.351 31.945 1.00 138.70 ? 712 LYS A C 1 ATOM 5497 O O . LYS A 1 712 ? -47.868 48.208 31.573 1.00 147.59 ? 712 LYS A O 1 ATOM 5498 C CB . LYS A 1 712 ? -49.679 50.617 32.746 1.00 138.78 ? 712 LYS A CB 1 ATOM 5499 C CG . LYS A 1 712 ? -48.582 51.254 31.909 1.00 142.69 ? 712 LYS A CG 1 ATOM 5500 C CD . LYS A 1 712 ? -49.082 52.495 31.190 1.00 143.71 ? 712 LYS A CD 1 ATOM 5501 C CE . LYS A 1 712 ? -48.064 52.984 30.173 1.00 142.16 ? 712 LYS A CE 1 ATOM 5502 N NZ . LYS A 1 712 ? -47.784 51.953 29.134 1.00 125.76 ? 712 LYS A NZ 1 ATOM 5503 N N . PHE A 1 713 ? -50.069 47.787 31.332 1.00 129.14 ? 713 PHE A N 1 ATOM 5504 C CA . PHE A 1 713 ? -49.965 47.152 30.022 1.00 115.68 ? 713 PHE A CA 1 ATOM 5505 C C . PHE A 1 713 ? -51.059 47.706 29.109 1.00 112.54 ? 713 PHE A C 1 ATOM 5506 O O . PHE A 1 713 ? -52.240 47.653 29.450 1.00 110.18 ? 713 PHE A O 1 ATOM 5507 C CB . PHE A 1 713 ? -50.087 45.631 30.136 1.00 114.07 ? 713 PHE A CB 1 ATOM 5508 C CG . PHE A 1 713 ? -48.857 44.956 30.678 1.00 121.18 ? 713 PHE A CG 1 ATOM 5509 C CD1 . PHE A 1 713 ? -48.564 44.994 32.032 1.00 130.57 ? 713 PHE A CD1 1 ATOM 5510 C CD2 . PHE A 1 713 ? -48.003 44.266 29.835 1.00 121.44 ? 713 PHE A CD2 1 ATOM 5511 C CE1 . PHE A 1 713 ? -47.435 44.369 32.532 1.00 124.93 ? 713 PHE A CE1 1 ATOM 5512 C CE2 . PHE A 1 713 ? -46.875 43.636 30.328 1.00 117.85 ? 713 PHE A CE2 1 ATOM 5513 C CZ . PHE A 1 713 ? -46.591 43.688 31.678 1.00 118.16 ? 713 PHE A CZ 1 ATOM 5514 N N . ASP A 1 714 ? -50.668 48.244 27.957 1.00 112.55 ? 714 ASP A N 1 ATOM 5515 C CA . ASP A 1 714 ? -51.628 48.838 27.028 1.00 112.04 ? 714 ASP A CA 1 ATOM 5516 C C . ASP A 1 714 ? -51.866 47.945 25.814 1.00 111.63 ? 714 ASP A C 1 ATOM 5517 O O . ASP A 1 714 ? -50.925 47.563 25.118 1.00 114.47 ? 714 ASP A O 1 ATOM 5518 C CB . ASP A 1 714 ? -51.152 50.220 26.578 1.00 121.01 ? 714 ASP A CB 1 ATOM 5519 C CG . ASP A 1 714 ? -51.182 51.239 27.700 1.00 139.66 ? 714 ASP A CG 1 ATOM 5520 O OD1 . ASP A 1 714 ? -50.201 51.999 27.842 1.00 151.96 ? 714 ASP A OD1 1 ATOM 5521 O OD2 . ASP A 1 714 ? -52.189 51.283 28.439 1.00 135.36 ? 714 ASP A OD2 1 ATOM 5522 N N . LEU A 1 715 ? -53.131 47.619 25.564 1.00 106.80 ? 715 LEU A N 1 ATOM 5523 C CA . LEU A 1 715 ? -53.487 46.703 24.485 1.00 100.97 ? 715 LEU A CA 1 ATOM 5524 C C . LEU A 1 715 ? -54.501 47.309 23.519 1.00 100.31 ? 715 LEU A C 1 ATOM 5525 O O . LEU A 1 715 ? -55.488 47.914 23.941 1.00 99.70 ? 715 LEU A O 1 ATOM 5526 C CB . LEU A 1 715 ? -54.053 45.400 25.056 1.00 98.80 ? 715 LEU A CB 1 ATOM 5527 C CG . LEU A 1 715 ? -53.424 44.793 26.310 1.00 100.70 ? 715 LEU A CG 1 ATOM 5528 C CD1 . LEU A 1 715 ? -54.135 43.505 26.669 1.00 98.88 ? 715 LEU A CD1 1 ATOM 5529 C CD2 . LEU A 1 715 ? -51.945 44.538 26.121 1.00 109.66 ? 715 LEU A CD2 1 ATOM 5530 N N . GLN A 1 716 ? -54.249 47.145 22.224 1.00 98.07 ? 716 GLN A N 1 ATOM 5531 C CA . GLN A 1 716 ? -55.225 47.502 21.199 1.00 99.44 ? 716 GLN A CA 1 ATOM 5532 C C . GLN A 1 716 ? -54.949 46.744 19.902 1.00 99.96 ? 716 GLN A C 1 ATOM 5533 O O . GLN A 1 716 ? -53.857 46.213 19.700 1.00 98.07 ? 716 GLN A O 1 ATOM 5534 C CB . GLN A 1 716 ? -55.226 49.009 20.936 1.00 98.97 ? 716 GLN A CB 1 ATOM 5535 C CG . GLN A 1 716 ? -54.170 49.480 19.954 1.00 110.90 ? 716 GLN A CG 1 ATOM 5536 C CD . GLN A 1 716 ? -54.566 50.768 19.258 1.00 114.18 ? 716 GLN A CD 1 ATOM 5537 O OE1 . GLN A 1 716 ? -53.747 51.407 18.600 1.00 111.00 ? 716 GLN A OE1 1 ATOM 5538 N NE2 . GLN A 1 716 ? -55.829 51.153 19.399 1.00 104.94 ? 716 GLN A NE2 1 ATOM 5539 N N . ILE A 1 717 ? -55.951 46.695 19.030 1.00 97.26 ? 717 ILE A N 1 ATOM 5540 C CA . ILE A 1 717 ? -55.831 46.014 17.746 1.00 94.62 ? 717 ILE A CA 1 ATOM 5541 C C . ILE A 1 717 ? -55.794 47.028 16.605 1.00 97.40 ? 717 ILE A C 1 ATOM 5542 O O . ILE A 1 717 ? -56.519 48.019 16.633 1.00 98.11 ? 717 ILE A O 1 ATOM 5543 C CB . ILE A 1 717 ? -56.999 45.029 17.528 1.00 93.41 ? 717 ILE A CB 1 ATOM 5544 C CG1 . ILE A 1 717 ? -57.091 44.046 18.697 1.00 93.33 ? 717 ILE A CG1 1 ATOM 5545 C CG2 . ILE A 1 717 ? -56.845 44.287 16.209 1.00 94.89 ? 717 ILE A CG2 1 ATOM 5546 C CD1 . ILE A 1 717 ? -58.237 43.063 18.583 1.00 92.44 ? 717 ILE A CD1 1 ATOM 5547 N N . GLN A 1 718 ? -54.944 46.789 15.610 1.00 96.90 ? 718 GLN A N 1 ATOM 5548 C CA . GLN A 1 718 ? -54.851 47.678 14.456 1.00 97.54 ? 718 GLN A CA 1 ATOM 5549 C C . GLN A 1 718 ? -55.001 46.910 13.146 1.00 99.39 ? 718 GLN A C 1 ATOM 5550 O O . GLN A 1 718 ? -54.713 45.715 13.083 1.00 100.94 ? 718 GLN A O 1 ATOM 5551 C CB . GLN A 1 718 ? -53.521 48.437 14.466 1.00 102.59 ? 718 GLN A CB 1 ATOM 5552 C CG . GLN A 1 718 ? -53.364 49.412 15.621 1.00 115.95 ? 718 GLN A CG 1 ATOM 5553 C CD . GLN A 1 718 ? -52.044 50.158 15.576 1.00 127.90 ? 718 GLN A CD 1 ATOM 5554 O OE1 . GLN A 1 718 ? -51.203 49.903 14.715 1.00 126.89 ? 718 GLN A OE1 1 ATOM 5555 N NE2 . GLN A 1 718 ? -51.858 51.088 16.506 1.00 134.08 ? 718 GLN A NE2 1 ATOM 5556 N N . SER A 1 719 ? -55.451 47.600 12.103 1.00 99.95 ? 719 SER A N 1 ATOM 5557 C CA . SER A 1 719 ? -55.597 46.987 10.785 1.00 100.95 ? 719 SER A CA 1 ATOM 5558 C C . SER A 1 719 ? -55.453 48.023 9.672 1.00 101.40 ? 719 SER A C 1 ATOM 5559 O O . SER A 1 719 ? -55.281 49.212 9.938 1.00 101.21 ? 719 SER A O 1 ATOM 5560 C CB . SER A 1 719 ? -56.945 46.274 10.673 1.00 99.80 ? 719 SER A CB 1 ATOM 5561 O OG . SER A 1 719 ? -58.014 47.152 10.975 1.00 98.98 ? 719 SER A OG 1 ATOM 5562 N N . SER A 1 720 ? -55.524 47.563 8.427 1.00 102.29 ? 720 SER A N 1 ATOM 5563 C CA . SER A 1 720 ? -55.284 48.426 7.275 1.00 103.06 ? 720 SER A CA 1 ATOM 5564 C C . SER A 1 720 ? -56.567 48.980 6.661 1.00 104.62 ? 720 SER A C 1 ATOM 5565 O O . SER A 1 720 ? -56.518 49.739 5.692 1.00 114.86 ? 720 SER A O 1 ATOM 5566 C CB . SER A 1 720 ? -54.491 47.667 6.210 1.00 104.32 ? 720 SER A CB 1 ATOM 5567 O OG . SER A 1 720 ? -53.248 47.223 6.727 1.00 107.21 ? 720 SER A OG 1 ATOM 5568 N N . ASN A 1 721 ? -57.711 48.599 7.220 1.00 106.79 ? 721 ASN A N 1 ATOM 5569 C CA . ASN A 1 721 ? -58.999 49.032 6.687 1.00 116.58 ? 721 ASN A CA 1 ATOM 5570 C C . ASN A 1 721 ? -59.188 50.541 6.784 1.00 126.99 ? 721 ASN A C 1 ATOM 5571 O O . ASN A 1 721 ? -58.697 51.179 7.712 1.00 130.03 ? 721 ASN A O 1 ATOM 5572 C CB . ASN A 1 721 ? -60.141 48.315 7.407 1.00 111.30 ? 721 ASN A CB 1 ATOM 5573 C CG . ASN A 1 721 ? -60.079 46.812 7.236 1.00 106.13 ? 721 ASN A CG 1 ATOM 5574 O OD1 . ASN A 1 721 ? -59.007 46.212 7.313 1.00 109.27 ? 721 ASN A OD1 1 ATOM 5575 N ND2 . ASN A 1 721 ? -61.228 46.197 6.986 1.00 115.58 ? 721 ASN A ND2 1 ATOM 5576 N N . LEU A 1 722 ? -59.903 51.103 5.815 1.00 132.43 ? 722 LEU A N 1 ATOM 5577 C CA . LEU A 1 722 ? -60.092 52.548 5.727 1.00 115.68 ? 722 LEU A CA 1 ATOM 5578 C C . LEU A 1 722 ? -60.936 53.092 6.877 1.00 101.07 ? 722 LEU A C 1 ATOM 5579 O O . LEU A 1 722 ? -60.707 54.204 7.352 1.00 108.67 ? 722 LEU A O 1 ATOM 5580 C CB . LEU A 1 722 ? -60.735 52.921 4.387 1.00 126.41 ? 722 LEU A CB 1 ATOM 5581 C CG . LEU A 1 722 ? -59.806 53.168 3.194 1.00 121.15 ? 722 LEU A CG 1 ATOM 5582 C CD1 . LEU A 1 722 ? -58.959 51.945 2.866 1.00 147.78 ? 722 LEU A CD1 1 ATOM 5583 C CD2 . LEU A 1 722 ? -60.607 53.606 1.975 1.00 114.91 ? 722 LEU A CD2 1 ATOM 5584 N N . PHE A 1 723 ? -61.908 52.302 7.323 1.00 100.22 ? 723 PHE A N 1 ATOM 5585 C CA . PHE A 1 723 ? -62.810 52.727 8.388 1.00 97.10 ? 723 PHE A CA 1 ATOM 5586 C C . PHE A 1 723 ? -62.850 51.719 9.533 1.00 98.29 ? 723 PHE A C 1 ATOM 5587 O O . PHE A 1 723 ? -62.828 50.509 9.302 1.00 96.53 ? 723 PHE A O 1 ATOM 5588 C CB . PHE A 1 723 ? -64.221 52.940 7.836 1.00 109.38 ? 723 PHE A CB 1 ATOM 5589 C CG . PHE A 1 723 ? -64.295 53.958 6.733 1.00 120.27 ? 723 PHE A CG 1 ATOM 5590 C CD1 . PHE A 1 723 ? -64.399 55.307 7.025 1.00 122.19 ? 723 PHE A CD1 1 ATOM 5591 C CD2 . PHE A 1 723 ? -64.269 53.564 5.405 1.00 113.86 ? 723 PHE A CD2 1 ATOM 5592 C CE1 . PHE A 1 723 ? -64.470 56.246 6.013 1.00 133.03 ? 723 PHE A CE1 1 ATOM 5593 C CE2 . PHE A 1 723 ? -64.341 54.498 4.389 1.00 117.60 ? 723 PHE A CE2 1 ATOM 5594 C CZ . PHE A 1 723 ? -64.441 55.840 4.695 1.00 143.45 ? 723 PHE A CZ 1 ATOM 5595 N N . ASP A 1 724 ? -62.919 52.232 10.761 1.00 109.51 ? 724 ASP A N 1 ATOM 5596 C CA . ASP A 1 724 ? -62.963 51.406 11.968 1.00 113.90 ? 724 ASP A CA 1 ATOM 5597 C C . ASP A 1 724 ? -61.811 50.406 11.992 1.00 103.96 ? 724 ASP A C 1 ATOM 5598 O O . ASP A 1 724 ? -62.016 49.206 12.176 1.00 99.70 ? 724 ASP A O 1 ATOM 5599 C CB . ASP A 1 724 ? -64.306 50.680 12.070 1.00 119.35 ? 724 ASP A CB 1 ATOM 5600 C CG . ASP A 1 724 ? -65.485 51.635 12.089 1.00 145.78 ? 724 ASP A CG 1 ATOM 5601 O OD1 . ASP A 1 724 ? -65.962 51.972 13.194 1.00 157.77 ? 724 ASP A OD1 1 ATOM 5602 O OD2 . ASP A 1 724 ? -65.931 52.053 11.000 1.00 156.92 ? 724 ASP A OD2 1 ATOM 5603 N N . LYS A 1 725 ? -60.598 50.917 11.807 1.00 104.27 ? 725 LYS A N 1 ATOM 5604 C CA . LYS A 1 725 ? -59.417 50.076 11.659 1.00 102.54 ? 725 LYS A CA 1 ATOM 5605 C C . LYS A 1 725 ? -58.834 49.617 12.991 1.00 98.71 ? 725 LYS A C 1 ATOM 5606 O O . LYS A 1 725 ? -57.940 48.770 13.020 1.00 95.64 ? 725 LYS A O 1 ATOM 5607 C CB . LYS A 1 725 ? -58.340 50.821 10.867 1.00 98.22 ? 725 LYS A CB 1 ATOM 5608 C CG . LYS A 1 725 ? -57.759 52.024 11.593 1.00 104.83 ? 725 LYS A CG 1 ATOM 5609 C CD . LYS A 1 725 ? -56.671 52.699 10.770 1.00 116.81 ? 725 LYS A CD 1 ATOM 5610 C CE . LYS A 1 725 ? -57.240 53.331 9.511 1.00 115.53 ? 725 LYS A CE 1 ATOM 5611 N NZ . LYS A 1 725 ? -56.172 53.877 8.627 1.00 137.22 ? 725 LYS A NZ 1 ATOM 5612 N N . VAL A 1 726 ? -59.329 50.173 14.092 1.00 91.84 ? 726 VAL A N 1 ATOM 5613 C CA . VAL A 1 726 ? -58.744 49.884 15.398 1.00 90.87 ? 726 VAL A CA 1 ATOM 5614 C C . VAL A 1 726 ? -59.762 49.517 16.472 1.00 91.64 ? 726 VAL A C 1 ATOM 5615 O O . VAL A 1 726 ? -60.942 49.852 16.374 1.00 103.60 ? 726 VAL A O 1 ATOM 5616 C CB . VAL A 1 726 ? -57.918 51.081 15.914 1.00 89.68 ? 726 VAL A CB 1 ATOM 5617 C CG1 . VAL A 1 726 ? -56.654 51.258 15.083 1.00 91.31 ? 726 VAL A CG1 1 ATOM 5618 C CG2 . VAL A 1 726 ? -58.758 52.348 15.906 1.00 103.85 ? 726 VAL A CG2 1 ATOM 5619 N N . SER A 1 727 ? -59.283 48.814 17.494 1.00 94.96 ? 727 SER A N 1 ATOM 5620 C CA . SER A 1 727 ? -60.075 48.508 18.679 1.00 96.44 ? 727 SER A CA 1 ATOM 5621 C C . SER A 1 727 ? -59.902 49.614 19.714 1.00 112.41 ? 727 SER A C 1 ATOM 5622 O O . SER A 1 727 ? -58.910 50.343 19.681 1.00 103.06 ? 727 SER A O 1 ATOM 5623 C CB . SER A 1 727 ? -59.659 47.159 19.272 1.00 99.01 ? 727 SER A CB 1 ATOM 5624 O OG . SER A 1 727 ? -58.353 47.224 19.821 1.00 93.94 ? 727 SER A OG 1 ATOM 5625 N N . PRO A 1 728 ? -60.869 49.754 20.634 1.00 118.04 ? 728 PRO A N 1 ATOM 5626 C CA . PRO A 1 728 ? -60.667 50.695 21.740 1.00 106.48 ? 728 PRO A CA 1 ATOM 5627 C C . PRO A 1 728 ? -59.530 50.227 22.641 1.00 115.93 ? 728 PRO A C 1 ATOM 5628 O O . PRO A 1 728 ? -59.463 49.041 22.963 1.00 119.41 ? 728 PRO A O 1 ATOM 5629 C CB . PRO A 1 728 ? -62.010 50.671 22.477 1.00 112.16 ? 728 PRO A CB 1 ATOM 5630 C CG . PRO A 1 728 ? -62.633 49.367 22.097 1.00 109.94 ? 728 PRO A CG 1 ATOM 5631 C CD . PRO A 1 728 ? -62.194 49.113 20.687 1.00 122.53 ? 728 PRO A CD 1 ATOM 5632 N N . VAL A 1 729 ? -58.646 51.138 23.036 1.00 106.69 ? 729 VAL A N 1 ATOM 5633 C CA . VAL A 1 729 ? -57.484 50.759 23.833 1.00 101.50 ? 729 VAL A CA 1 ATOM 5634 C C . VAL A 1 729 ? -57.902 50.331 25.238 1.00 110.01 ? 729 VAL A C 1 ATOM 5635 O O . VAL A 1 729 ? -58.567 51.078 25.956 1.00 130.40 ? 729 VAL A O 1 ATOM 5636 C CB . VAL A 1 729 ? -56.465 51.911 23.928 1.00 98.70 ? 729 VAL A CB 1 ATOM 5637 C CG1 . VAL A 1 729 ? -55.231 51.464 24.697 1.00 103.64 ? 729 VAL A CG1 1 ATOM 5638 C CG2 . VAL A 1 729 ? -56.081 52.396 22.538 1.00 102.36 ? 729 VAL A CG2 1 ATOM 5639 N N . VAL A 1 730 ? -57.508 49.120 25.619 1.00 102.20 ? 730 VAL A N 1 ATOM 5640 C CA . VAL A 1 730 ? -57.838 48.581 26.933 1.00 104.44 ? 730 VAL A CA 1 ATOM 5641 C C . VAL A 1 730 ? -56.575 48.379 27.758 1.00 116.71 ? 730 VAL A C 1 ATOM 5642 O O . VAL A 1 730 ? -55.697 47.598 27.388 1.00 121.55 ? 730 VAL A O 1 ATOM 5643 C CB . VAL A 1 730 ? -58.594 47.241 26.829 1.00 111.13 ? 730 VAL A CB 1 ATOM 5644 C CG1 . VAL A 1 730 ? -58.882 46.682 28.216 1.00 119.92 ? 730 VAL A CG1 1 ATOM 5645 C CG2 . VAL A 1 730 ? -59.884 47.416 26.040 1.00 121.03 ? 730 VAL A CG2 1 ATOM 5646 N N . SER A 1 731 ? -56.488 49.087 28.878 1.00 121.35 ? 731 SER A N 1 ATOM 5647 C CA . SER A 1 731 ? -55.321 49.006 29.746 1.00 112.90 ? 731 SER A CA 1 ATOM 5648 C C . SER A 1 731 ? -55.572 48.083 30.933 1.00 110.20 ? 731 SER A C 1 ATOM 5649 O O . SER A 1 731 ? -56.645 48.105 31.536 1.00 110.31 ? 731 SER A O 1 ATOM 5650 C CB . SER A 1 731 ? -54.927 50.398 30.241 1.00 114.04 ? 731 SER A CB 1 ATOM 5651 O OG . SER A 1 731 ? -53.783 50.340 31.075 1.00 126.48 ? 731 SER A OG 1 ATOM 5652 N N . HIS A 1 732 ? -54.575 47.269 31.261 1.00 115.01 ? 732 HIS A N 1 ATOM 5653 C CA . HIS A 1 732 ? -54.660 46.378 32.411 1.00 122.82 ? 732 HIS A CA 1 ATOM 5654 C C . HIS A 1 732 ? -53.414 46.510 33.274 1.00 119.34 ? 732 HIS A C 1 ATOM 5655 O O . HIS A 1 732 ? -52.294 46.528 32.763 1.00 116.04 ? 732 HIS A O 1 ATOM 5656 C CB . HIS A 1 732 ? -54.840 44.928 31.960 1.00 123.99 ? 732 HIS A CB 1 ATOM 5657 C CG . HIS A 1 732 ? -54.801 43.937 33.082 1.00 118.34 ? 732 HIS A CG 1 ATOM 5658 N ND1 . HIS A 1 732 ? -53.726 43.104 33.301 1.00 110.46 ? 732 HIS A ND1 1 ATOM 5659 C CD2 . HIS A 1 732 ? -55.704 43.648 34.048 1.00 120.71 ? 732 HIS A CD2 1 ATOM 5660 C CE1 . HIS A 1 732 ? -53.968 42.343 34.353 1.00 117.49 ? 732 HIS A CE1 1 ATOM 5661 N NE2 . HIS A 1 732 ? -55.162 42.654 34.826 1.00 120.40 ? 732 HIS A NE2 1 ATOM 5662 N N . LYS A 1 733 ? -53.611 46.605 34.584 1.00 120.08 ? 733 LYS A N 1 ATOM 5663 C CA . LYS A 1 733 ? -52.495 46.783 35.502 1.00 119.02 ? 733 LYS A CA 1 ATOM 5664 C C . LYS A 1 733 ? -52.438 45.680 36.551 1.00 119.41 ? 733 LYS A C 1 ATOM 5665 O O . LYS A 1 733 ? -53.456 45.080 36.897 1.00 123.51 ? 733 LYS A O 1 ATOM 5666 C CB . LYS A 1 733 ? -52.581 48.147 36.191 1.00 121.66 ? 733 LYS A CB 1 ATOM 5667 C CG . LYS A 1 733 ? -53.756 48.284 37.146 1.00 125.99 ? 733 LYS A CG 1 ATOM 5668 C CD . LYS A 1 733 ? -53.737 49.625 37.863 1.00 141.27 ? 733 LYS A CD 1 ATOM 5669 C CE . LYS A 1 733 ? -54.887 49.737 38.852 1.00 144.41 ? 733 LYS A CE 1 ATOM 5670 N NZ . LYS A 1 733 ? -54.806 48.700 39.918 1.00 142.55 ? 733 LYS A NZ 1 ATOM 5671 N N . VAL A 1 734 ? -51.233 45.415 37.045 1.00 120.44 ? 734 VAL A N 1 ATOM 5672 C CA . VAL A 1 734 ? -51.040 44.502 38.163 1.00 122.59 ? 734 VAL A CA 1 ATOM 5673 C C . VAL A 1 734 ? -50.273 45.219 39.269 1.00 124.18 ? 734 VAL A C 1 ATOM 5674 O O . VAL A 1 734 ? -49.297 45.922 39.006 1.00 125.49 ? 734 VAL A O 1 ATOM 5675 C CB . VAL A 1 734 ? -50.293 43.221 37.743 1.00 124.91 ? 734 VAL A CB 1 ATOM 5676 C CG1 . VAL A 1 734 ? -51.227 42.283 36.994 1.00 127.20 ? 734 VAL A CG1 1 ATOM 5677 C CG2 . VAL A 1 734 ? -49.077 43.560 36.897 1.00 123.26 ? 734 VAL A CG2 1 ATOM 5678 N N . ASP A 1 735 ? -50.726 45.050 40.506 1.00 123.67 ? 735 ASP A N 1 ATOM 5679 C CA . ASP A 1 735 ? -50.149 45.769 41.635 1.00 128.58 ? 735 ASP A CA 1 ATOM 5680 C C . ASP A 1 735 ? -48.854 45.127 42.120 1.00 137.01 ? 735 ASP A C 1 ATOM 5681 O O . ASP A 1 735 ? -48.710 43.906 42.099 1.00 141.39 ? 735 ASP A O 1 ATOM 5682 C CB . ASP A 1 735 ? -51.157 45.845 42.784 1.00 138.83 ? 735 ASP A CB 1 ATOM 5683 C CG . ASP A 1 735 ? -52.447 46.532 42.380 1.00 144.75 ? 735 ASP A CG 1 ATOM 5684 O OD1 . ASP A 1 735 ? -52.391 47.459 41.545 1.00 146.54 ? 735 ASP A OD1 1 ATOM 5685 O OD2 . ASP A 1 735 ? -53.516 46.145 42.896 1.00 148.92 ? 735 ASP A OD2 1 ATOM 5686 N N . LEU A 1 736 ? -47.913 45.959 42.555 1.00 135.26 ? 736 LEU A N 1 ATOM 5687 C CA . LEU A 1 736 ? -46.660 45.466 43.111 1.00 128.37 ? 736 LEU A CA 1 ATOM 5688 C C . LEU A 1 736 ? -46.814 45.189 44.600 1.00 129.32 ? 736 LEU A C 1 ATOM 5689 O O . LEU A 1 736 ? -47.216 46.064 45.366 1.00 132.89 ? 736 LEU A O 1 ATOM 5690 C CB . LEU A 1 736 ? -45.522 46.463 42.879 1.00 129.08 ? 736 LEU A CB 1 ATOM 5691 C CG . LEU A 1 736 ? -44.703 46.374 41.587 1.00 126.65 ? 736 LEU A CG 1 ATOM 5692 C CD1 . LEU A 1 736 ? -45.588 46.368 40.350 1.00 130.84 ? 736 LEU A CD1 1 ATOM 5693 C CD2 . LEU A 1 736 ? -43.712 47.524 41.520 1.00 127.13 ? 736 LEU A CD2 1 ATOM 5694 N N . ALA A 1 737 ? -46.498 43.964 45.004 1.00 126.24 ? 737 ALA A N 1 ATOM 5695 C CA . ALA A 1 737 ? -46.574 43.580 46.406 1.00 126.22 ? 737 ALA A CA 1 ATOM 5696 C C . ALA A 1 737 ? -45.185 43.553 47.027 1.00 125.93 ? 737 ALA A C 1 ATOM 5697 O O . ALA A 1 737 ? -44.211 43.184 46.374 1.00 123.38 ? 737 ALA A O 1 ATOM 5698 C CB . ALA A 1 737 ? -47.249 42.227 46.553 1.00 122.52 ? 737 ALA A CB 1 ATOM 5699 N N . VAL A 1 738 ? -45.099 43.956 48.290 1.00 111.95 ? 738 VAL A N 1 ATOM 5700 C CA . VAL A 1 738 ? -43.839 43.903 49.018 1.00 107.71 ? 738 VAL A CA 1 ATOM 5701 C C . VAL A 1 738 ? -43.776 42.637 49.857 1.00 107.87 ? 738 VAL A C 1 ATOM 5702 O O . VAL A 1 738 ? -44.546 42.470 50.804 1.00 107.52 ? 738 VAL A O 1 ATOM 5703 C CB . VAL A 1 738 ? -43.652 45.129 49.929 1.00 103.03 ? 738 VAL A CB 1 ATOM 5704 C CG1 . VAL A 1 738 ? -42.428 44.949 50.816 1.00 98.18 ? 738 VAL A CG1 1 ATOM 5705 C CG2 . VAL A 1 738 ? -43.532 46.396 49.098 1.00 110.46 ? 738 VAL A CG2 1 ATOM 5706 N N . LEU A 1 739 ? -42.863 41.742 49.502 1.00 111.15 ? 739 LEU A N 1 ATOM 5707 C CA . LEU A 1 739 ? -42.683 40.508 50.252 1.00 110.07 ? 739 LEU A CA 1 ATOM 5708 C C . LEU A 1 739 ? -41.211 40.297 50.567 1.00 105.93 ? 739 LEU A C 1 ATOM 5709 O O . LEU A 1 739 ? -40.389 40.126 49.666 1.00 107.59 ? 739 LEU A O 1 ATOM 5710 C CB . LEU A 1 739 ? -43.245 39.314 49.473 1.00 121.45 ? 739 LEU A CB 1 ATOM 5711 C CG . LEU A 1 739 ? -43.444 37.983 50.206 1.00 119.63 ? 739 LEU A CG 1 ATOM 5712 C CD1 . LEU A 1 739 ? -42.187 37.124 50.177 1.00 118.56 ? 739 LEU A CD1 1 ATOM 5713 C CD2 . LEU A 1 739 ? -43.899 38.227 51.639 1.00 117.24 ? 739 LEU A CD2 1 ATOM 5714 N N . ALA A 1 740 ? -40.885 40.309 51.852 1.00 100.90 ? 740 ALA A N 1 ATOM 5715 C CA . ALA A 1 740 ? -39.520 40.069 52.288 1.00 96.77 ? 740 ALA A CA 1 ATOM 5716 C C . ALA A 1 740 ? -39.488 38.967 53.335 1.00 98.85 ? 740 ALA A C 1 ATOM 5717 O O . ALA A 1 740 ? -40.016 39.126 54.435 1.00 100.13 ? 740 ALA A O 1 ATOM 5718 C CB . ALA A 1 740 ? -38.904 41.346 52.836 1.00 90.49 ? 740 ALA A CB 1 ATOM 5719 N N . ALA A 1 741 ? -38.868 37.845 52.989 1.00 102.57 ? 741 ALA A N 1 ATOM 5720 C CA . ALA A 1 741 ? -38.711 36.757 53.939 1.00 99.04 ? 741 ALA A CA 1 ATOM 5721 C C . ALA A 1 741 ? -37.461 37.006 54.767 1.00 89.73 ? 741 ALA A C 1 ATOM 5722 O O . ALA A 1 741 ? -36.348 37.019 54.242 1.00 113.03 ? 741 ALA A O 1 ATOM 5723 C CB . ALA A 1 741 ? -38.629 35.421 53.221 1.00 97.41 ? 741 ALA A CB 1 ATOM 5724 N N . VAL A 1 742 ? -37.652 37.201 56.067 1.00 82.37 ? 742 VAL A N 1 ATOM 5725 C CA . VAL A 1 742 ? -36.550 37.530 56.958 1.00 77.18 ? 742 VAL A CA 1 ATOM 5726 C C . VAL A 1 742 ? -36.492 36.549 58.119 1.00 77.88 ? 742 VAL A C 1 ATOM 5727 O O . VAL A 1 742 ? -37.441 36.431 58.893 1.00 83.68 ? 742 VAL A O 1 ATOM 5728 C CB . VAL A 1 742 ? -36.671 38.962 57.515 1.00 79.44 ? 742 VAL A CB 1 ATOM 5729 C CG1 . VAL A 1 742 ? -35.347 39.406 58.108 1.00 70.04 ? 742 VAL A CG1 1 ATOM 5730 C CG2 . VAL A 1 742 ? -37.109 39.927 56.426 1.00 77.87 ? 742 VAL A CG2 1 ATOM 5731 N N . GLU A 1 743 ? -35.373 35.843 58.234 1.00 76.52 ? 743 GLU A N 1 ATOM 5732 C CA . GLU A 1 743 ? -35.184 34.889 59.318 1.00 86.24 ? 743 GLU A CA 1 ATOM 5733 C C . GLU A 1 743 ? -33.998 35.292 60.183 1.00 78.80 ? 743 GLU A C 1 ATOM 5734 O O . GLU A 1 743 ? -33.100 36.002 59.729 1.00 67.08 ? 743 GLU A O 1 ATOM 5735 C CB . GLU A 1 743 ? -34.977 33.477 58.768 1.00 87.62 ? 743 GLU A CB 1 ATOM 5736 C CG . GLU A 1 743 ? -33.680 33.301 57.994 1.00 95.37 ? 743 GLU A CG 1 ATOM 5737 C CD . GLU A 1 743 ? -33.483 31.880 57.502 1.00 127.24 ? 743 GLU A CD 1 ATOM 5738 O OE1 . GLU A 1 743 ? -34.456 31.099 57.536 1.00 147.49 ? 743 GLU A OE1 1 ATOM 5739 O OE2 . GLU A 1 743 ? -32.354 31.545 57.086 1.00 128.20 ? 743 GLU A OE2 1 ATOM 5740 N N . ILE A 1 744 ? -34.003 34.841 61.432 1.00 68.67 ? 744 ILE A N 1 ATOM 5741 C CA . ILE A 1 744 ? -32.889 35.098 62.336 1.00 60.09 ? 744 ILE A CA 1 ATOM 5742 C C . ILE A 1 744 ? -32.297 33.774 62.820 1.00 66.66 ? 744 ILE A C 1 ATOM 5743 O O . ILE A 1 744 ? -33.018 32.873 63.248 1.00 87.31 ? 744 ILE A O 1 ATOM 5744 C CB . ILE A 1 744 ? -33.321 35.975 63.535 1.00 64.04 ? 744 ILE A CB 1 ATOM 5745 C CG1 . ILE A 1 744 ? -32.152 36.179 64.502 1.00 66.83 ? 744 ILE A CG1 1 ATOM 5746 C CG2 . ILE A 1 744 ? -34.531 35.378 64.246 1.00 62.96 ? 744 ILE A CG2 1 ATOM 5747 C CD1 . ILE A 1 744 ? -32.464 37.122 65.643 1.00 60.36 ? 744 ILE A CD1 1 ATOM 5748 N N . ARG A 1 745 ? -30.977 33.655 62.727 1.00 74.97 ? 745 ARG A N 1 ATOM 5749 C CA . ARG A 1 745 ? -30.298 32.417 63.084 1.00 60.44 ? 745 ARG A CA 1 ATOM 5750 C C . ARG A 1 745 ? -29.222 32.652 64.133 1.00 79.15 ? 745 ARG A C 1 ATOM 5751 O O . ARG A 1 745 ? -28.727 33.768 64.287 1.00 73.93 ? 745 ARG A O 1 ATOM 5752 C CB . ARG A 1 745 ? -29.680 31.770 61.845 1.00 58.82 ? 745 ARG A CB 1 ATOM 5753 C CG . ARG A 1 745 ? -30.687 31.355 60.789 1.00 64.21 ? 745 ARG A CG 1 ATOM 5754 C CD . ARG A 1 745 ? -29.996 30.638 59.646 1.00 75.88 ? 745 ARG A CD 1 ATOM 5755 N NE . ARG A 1 745 ? -29.056 29.640 60.143 1.00 108.32 ? 745 ARG A NE 1 ATOM 5756 C CZ . ARG A 1 745 ? -29.399 28.413 60.522 1.00 115.07 ? 745 ARG A CZ 1 ATOM 5757 N NH1 . ARG A 1 745 ? -30.665 28.025 60.458 1.00 114.66 ? 745 ARG A NH1 1 ATOM 5758 N NH2 . ARG A 1 745 ? -28.473 27.574 60.965 1.00 85.90 ? 745 ARG A NH2 1 ATOM 5759 N N . GLY A 1 746 ? -28.862 31.594 64.853 1.00 95.69 ? 746 GLY A N 1 ATOM 5760 C CA . GLY A 1 746 ? -27.842 31.701 65.877 1.00 66.38 ? 746 GLY A CA 1 ATOM 5761 C C . GLY A 1 746 ? -27.136 30.399 66.195 1.00 60.85 ? 746 GLY A C 1 ATOM 5762 O O . GLY A 1 746 ? -27.682 29.316 65.987 1.00 90.16 ? 746 GLY A O 1 ATOM 5763 N N . VAL A 1 747 ? -25.916 30.512 66.713 1.00 59.19 ? 747 VAL A N 1 ATOM 5764 C CA . VAL A 1 747 ? -25.130 29.349 67.113 1.00 79.06 ? 747 VAL A CA 1 ATOM 5765 C C . VAL A 1 747 ? -24.311 29.639 68.366 1.00 76.68 ? 747 VAL A C 1 ATOM 5766 O O . VAL A 1 747 ? -24.142 30.793 68.760 1.00 74.46 ? 747 VAL A O 1 ATOM 5767 C CB . VAL A 1 747 ? -24.171 28.888 65.993 1.00 72.85 ? 747 VAL A CB 1 ATOM 5768 C CG1 . VAL A 1 747 ? -24.923 28.130 64.906 1.00 77.45 ? 747 VAL A CG1 1 ATOM 5769 C CG2 . VAL A 1 747 ? -23.419 30.076 65.417 1.00 86.58 ? 747 VAL A CG2 1 ATOM 5770 N N . SER A 1 748 ? -23.809 28.579 68.988 1.00 84.91 ? 748 SER A N 1 ATOM 5771 C CA . SER A 1 748 ? -22.925 28.703 70.139 1.00 77.80 ? 748 SER A CA 1 ATOM 5772 C C . SER A 1 748 ? -21.640 27.921 69.892 1.00 87.38 ? 748 SER A C 1 ATOM 5773 O O . SER A 1 748 ? -21.677 26.710 69.674 1.00 82.99 ? 748 SER A O 1 ATOM 5774 C CB . SER A 1 748 ? -23.613 28.207 71.411 1.00 75.62 ? 748 SER A CB 1 ATOM 5775 O OG . SER A 1 748 ? -22.728 28.243 72.517 1.00 81.38 ? 748 SER A OG 1 ATOM 5776 N N . SER A 1 749 ? -20.510 28.621 69.902 1.00 68.95 ? 749 SER A N 1 ATOM 5777 C CA . SER A 1 749 ? -19.214 27.980 69.712 1.00 69.66 ? 749 SER A CA 1 ATOM 5778 C C . SER A 1 749 ? -18.327 28.123 70.947 1.00 86.71 ? 749 SER A C 1 ATOM 5779 O O . SER A 1 749 ? -17.834 29.214 71.233 1.00 84.97 ? 749 SER A O 1 ATOM 5780 C CB . SER A 1 749 ? -18.501 28.570 68.494 1.00 82.53 ? 749 SER A CB 1 ATOM 5781 O OG . SER A 1 749 ? -19.307 28.468 67.333 1.00 109.94 ? 749 SER A OG 1 ATOM 5782 N N . PRO A 1 750 ? -18.113 27.019 71.684 1.00 91.03 ? 750 PRO A N 1 ATOM 5783 C CA . PRO A 1 750 ? -18.732 25.701 71.496 1.00 78.56 ? 750 PRO A CA 1 ATOM 5784 C C . PRO A 1 750 ? -20.171 25.657 72.006 1.00 74.47 ? 750 PRO A C 1 ATOM 5785 O O . PRO A 1 750 ? -20.578 26.529 72.773 1.00 73.82 ? 750 PRO A O 1 ATOM 5786 C CB . PRO A 1 750 ? -17.833 24.775 72.315 1.00 79.65 ? 750 PRO A CB 1 ATOM 5787 C CG . PRO A 1 750 ? -17.311 25.643 73.401 1.00 79.33 ? 750 PRO A CG 1 ATOM 5788 C CD . PRO A 1 750 ? -17.147 27.014 72.798 1.00 94.30 ? 750 PRO A CD 1 ATOM 5789 N N . ASP A 1 751 ? -20.931 24.654 71.578 1.00 108.64 ? 751 ASP A N 1 ATOM 5790 C CA . ASP A 1 751 ? -22.320 24.516 71.998 1.00 94.71 ? 751 ASP A CA 1 ATOM 5791 C C . ASP A 1 751 ? -22.418 23.856 73.370 1.00 93.27 ? 751 ASP A C 1 ATOM 5792 O O . ASP A 1 751 ? -23.498 23.770 73.952 1.00 94.28 ? 751 ASP A O 1 ATOM 5793 C CB . ASP A 1 751 ? -23.116 23.711 70.968 1.00 88.53 ? 751 ASP A CB 1 ATOM 5794 C CG . ASP A 1 751 ? -22.618 22.285 70.831 1.00 120.98 ? 751 ASP A CG 1 ATOM 5795 O OD1 . ASP A 1 751 ? -23.460 21.372 70.702 1.00 143.25 ? 751 ASP A OD1 1 ATOM 5796 O OD2 . ASP A 1 751 ? -21.387 22.078 70.850 1.00 126.15 ? 751 ASP A OD2 1 ATOM 5797 N N . HIS A 1 752 ? -21.282 23.389 73.880 1.00 89.24 ? 752 HIS A N 1 ATOM 5798 C CA . HIS A 1 752 ? -21.233 22.771 75.199 1.00 100.85 ? 752 HIS A CA 1 ATOM 5799 C C . HIS A 1 752 ? -19.871 22.948 75.863 1.00 98.42 ? 752 HIS A C 1 ATOM 5800 O O . HIS A 1 752 ? -18.842 23.024 75.190 1.00 112.20 ? 752 HIS A O 1 ATOM 5801 C CB . HIS A 1 752 ? -21.578 21.283 75.105 1.00 116.15 ? 752 HIS A CB 1 ATOM 5802 C CG . HIS A 1 752 ? -20.743 20.530 74.117 1.00 137.40 ? 752 HIS A CG 1 ATOM 5803 N ND1 . HIS A 1 752 ? -19.374 20.420 74.229 1.00 142.89 ? 752 HIS A ND1 1 ATOM 5804 C CD2 . HIS A 1 752 ? -21.085 19.849 72.997 1.00 148.65 ? 752 HIS A CD2 1 ATOM 5805 C CE1 . HIS A 1 752 ? -18.908 19.705 73.221 1.00 142.08 ? 752 HIS A CE1 1 ATOM 5806 N NE2 . HIS A 1 752 ? -19.925 19.346 72.459 1.00 153.40 ? 752 HIS A NE2 1 ATOM 5807 N N . VAL A 1 753 ? -19.878 23.012 77.190 1.00 86.76 ? 753 VAL A N 1 ATOM 5808 C CA . VAL A 1 753 ? -18.648 23.091 77.969 1.00 96.84 ? 753 VAL A CA 1 ATOM 5809 C C . VAL A 1 753 ? -18.626 22.002 79.037 1.00 116.97 ? 753 VAL A C 1 ATOM 5810 O O . VAL A 1 753 ? -19.525 21.927 79.875 1.00 117.30 ? 753 VAL A O 1 ATOM 5811 C CB . VAL A 1 753 ? -18.485 24.465 78.643 1.00 86.92 ? 753 VAL A CB 1 ATOM 5812 C CG1 . VAL A 1 753 ? -17.293 24.450 79.583 1.00 90.06 ? 753 VAL A CG1 1 ATOM 5813 C CG2 . VAL A 1 753 ? -18.329 25.556 77.597 1.00 83.05 ? 753 VAL A CG2 1 ATOM 5814 N N . PHE A 1 754 ? -17.595 21.164 79.006 1.00 97.27 ? 754 PHE A N 1 ATOM 5815 C CA . PHE A 1 754 ? -17.491 20.047 79.938 1.00 102.33 ? 754 PHE A CA 1 ATOM 5816 C C . PHE A 1 754 ? -16.665 20.390 81.175 1.00 104.63 ? 754 PHE A C 1 ATOM 5817 O O . PHE A 1 754 ? -15.487 20.736 81.075 1.00 105.17 ? 754 PHE A O 1 ATOM 5818 C CB . PHE A 1 754 ? -16.893 18.827 79.235 1.00 105.87 ? 754 PHE A CB 1 ATOM 5819 C CG . PHE A 1 754 ? -17.845 18.139 78.298 1.00 105.49 ? 754 PHE A CG 1 ATOM 5820 C CD1 . PHE A 1 754 ? -17.891 18.482 76.956 1.00 117.04 ? 754 PHE A CD1 1 ATOM 5821 C CD2 . PHE A 1 754 ? -18.693 17.147 78.761 1.00 108.73 ? 754 PHE A CD2 1 ATOM 5822 C CE1 . PHE A 1 754 ? -18.767 17.847 76.095 1.00 118.82 ? 754 PHE A CE1 1 ATOM 5823 C CE2 . PHE A 1 754 ? -19.570 16.510 77.906 1.00 108.89 ? 754 PHE A CE2 1 ATOM 5824 C CZ . PHE A 1 754 ? -19.608 16.860 76.571 1.00 111.81 ? 754 PHE A CZ 1 ATOM 5825 N N . LEU A 1 755 ? -17.298 20.296 82.341 1.00 113.41 ? 755 LEU A N 1 ATOM 5826 C CA . LEU A 1 755 ? -16.625 20.515 83.617 1.00 109.37 ? 755 LEU A CA 1 ATOM 5827 C C . LEU A 1 755 ? -16.025 19.207 84.131 1.00 119.72 ? 755 LEU A C 1 ATOM 5828 O O . LEU A 1 755 ? -16.539 18.129 83.828 1.00 138.65 ? 755 LEU A O 1 ATOM 5829 C CB . LEU A 1 755 ? -17.603 21.098 84.642 1.00 111.77 ? 755 LEU A CB 1 ATOM 5830 C CG . LEU A 1 755 ? -18.101 22.523 84.380 1.00 111.42 ? 755 LEU A CG 1 ATOM 5831 C CD1 . LEU A 1 755 ? -19.179 22.918 85.376 1.00 116.24 ? 755 LEU A CD1 1 ATOM 5832 C CD2 . LEU A 1 755 ? -16.946 23.507 84.432 1.00 102.76 ? 755 LEU A CD2 1 ATOM 5833 N N . PRO A 1 756 ? -14.931 19.289 84.907 1.00 118.59 ? 756 PRO A N 1 ATOM 5834 C CA . PRO A 1 756 ? -14.200 20.501 85.294 1.00 117.02 ? 756 PRO A CA 1 ATOM 5835 C C . PRO A 1 756 ? -13.283 21.020 84.190 1.00 121.50 ? 756 PRO A C 1 ATOM 5836 O O . PRO A 1 756 ? -12.822 20.240 83.356 1.00 120.32 ? 756 PRO A O 1 ATOM 5837 C CB . PRO A 1 756 ? -13.384 20.039 86.502 1.00 122.83 ? 756 PRO A CB 1 ATOM 5838 C CG . PRO A 1 756 ? -13.117 18.606 86.222 1.00 136.00 ? 756 PRO A CG 1 ATOM 5839 C CD . PRO A 1 756 ? -14.337 18.081 85.508 1.00 124.93 ? 756 PRO A CD 1 ATOM 5840 N N . ILE A 1 757 ? -13.025 22.324 84.192 1.00 117.97 ? 757 ILE A N 1 ATOM 5841 C CA . ILE A 1 757 ? -12.111 22.922 83.227 1.00 120.88 ? 757 ILE A CA 1 ATOM 5842 C C . ILE A 1 757 ? -10.675 22.535 83.573 1.00 121.46 ? 757 ILE A C 1 ATOM 5843 O O . ILE A 1 757 ? -10.262 22.628 84.731 1.00 127.24 ? 757 ILE A O 1 ATOM 5844 C CB . ILE A 1 757 ? -12.263 24.466 83.178 1.00 120.05 ? 757 ILE A CB 1 ATOM 5845 C CG1 . ILE A 1 757 ? -13.124 24.883 81.984 1.00 106.85 ? 757 ILE A CG1 1 ATOM 5846 C CG2 . ILE A 1 757 ? -10.909 25.154 83.065 1.00 129.23 ? 757 ILE A CG2 1 ATOM 5847 C CD1 . ILE A 1 757 ? -14.467 24.202 81.916 1.00 107.11 ? 757 ILE A CD1 1 ATOM 5848 N N . PRO A 1 758 ? -9.920 22.067 82.568 1.00 121.60 ? 758 PRO A N 1 ATOM 5849 C CA . PRO A 1 758 ? -8.510 21.694 82.733 1.00 133.93 ? 758 PRO A CA 1 ATOM 5850 C C . PRO A 1 758 ? -7.651 22.876 83.167 1.00 133.71 ? 758 PRO A C 1 ATOM 5851 O O . PRO A 1 758 ? -7.796 23.966 82.610 1.00 116.50 ? 758 PRO A O 1 ATOM 5852 C CB . PRO A 1 758 ? -8.107 21.213 81.335 1.00 141.47 ? 758 PRO A CB 1 ATOM 5853 C CG . PRO A 1 758 ? -9.386 20.821 80.683 1.00 136.14 ? 758 PRO A CG 1 ATOM 5854 C CD . PRO A 1 758 ? -10.409 21.777 81.209 1.00 118.12 ? 758 PRO A CD 1 ATOM 5855 N N . ASN A 1 759 ? -6.773 22.651 84.143 1.00 136.81 ? 759 ASN A N 1 ATOM 5856 C CA . ASN A 1 759 ? -5.896 23.692 84.673 1.00 144.22 ? 759 ASN A CA 1 ATOM 5857 C C . ASN A 1 759 ? -6.666 24.927 85.126 1.00 154.55 ? 759 ASN A C 1 ATOM 5858 O O . ASN A 1 759 ? -6.533 26.001 84.542 1.00 150.97 ? 759 ASN A O 1 ATOM 5859 C CB . ASN A 1 759 ? -4.846 24.090 83.632 1.00 136.69 ? 759 ASN A CB 1 ATOM 5860 C CG . ASN A 1 759 ? -3.970 22.927 83.213 1.00 156.42 ? 759 ASN A CG 1 ATOM 5861 O OD1 . ASN A 1 759 ? -3.675 22.038 84.011 1.00 163.87 ? 759 ASN A OD1 1 ATOM 5862 N ND2 . ASN A 1 759 ? -3.550 22.928 81.953 1.00 156.15 ? 759 ASN A ND2 1 ATOM 5863 N N . TRP A 1 760 ? -7.475 24.768 86.168 1.00 164.06 ? 760 TRP A N 1 ATOM 5864 C CA . TRP A 1 760 ? -8.275 25.875 86.677 1.00 161.36 ? 760 TRP A CA 1 ATOM 5865 C C . TRP A 1 760 ? -7.804 26.356 88.045 1.00 157.92 ? 760 TRP A C 1 ATOM 5866 O O . TRP A 1 760 ? -7.925 25.645 89.044 1.00 146.91 ? 760 TRP A O 1 ATOM 5867 C CB . TRP A 1 760 ? -9.753 25.483 86.751 1.00 157.14 ? 760 TRP A CB 1 ATOM 5868 C CG . TRP A 1 760 ? -10.574 26.444 87.557 1.00 150.93 ? 760 TRP A CG 1 ATOM 5869 C CD1 . TRP A 1 760 ? -11.267 26.172 88.702 1.00 146.62 ? 760 TRP A CD1 1 ATOM 5870 C CD2 . TRP A 1 760 ? -10.767 27.838 87.292 1.00 132.50 ? 760 TRP A CD2 1 ATOM 5871 N NE1 . TRP A 1 760 ? -11.889 27.310 89.159 1.00 124.96 ? 760 TRP A NE1 1 ATOM 5872 C CE2 . TRP A 1 760 ? -11.597 28.346 88.312 1.00 126.95 ? 760 TRP A CE2 1 ATOM 5873 C CE3 . TRP A 1 760 ? -10.324 28.705 86.290 1.00 123.73 ? 760 TRP A CE3 1 ATOM 5874 C CZ2 . TRP A 1 760 ? -11.990 29.682 88.358 1.00 131.34 ? 760 TRP A CZ2 1 ATOM 5875 C CZ3 . TRP A 1 760 ? -10.715 30.029 86.337 1.00 139.11 ? 760 TRP A CZ3 1 ATOM 5876 C CH2 . TRP A 1 760 ? -11.541 30.505 87.363 1.00 141.89 ? 760 TRP A CH2 1 ATOM 5877 N N . GLU A 1 761 ? -7.266 27.571 88.079 1.00 153.92 ? 761 GLU A N 1 ATOM 5878 C CA . GLU A 1 761 ? -6.902 28.219 89.332 1.00 146.28 ? 761 GLU A CA 1 ATOM 5879 C C . GLU A 1 761 ? -7.659 29.533 89.472 1.00 142.50 ? 761 GLU A C 1 ATOM 5880 O O . GLU A 1 761 ? -7.546 30.419 88.625 1.00 137.56 ? 761 GLU A O 1 ATOM 5881 C CB . GLU A 1 761 ? -5.394 28.462 89.407 1.00 137.36 ? 761 GLU A CB 1 ATOM 5882 C CG . GLU A 1 761 ? -4.571 27.199 89.602 1.00 148.78 ? 761 GLU A CG 1 ATOM 5883 C CD . GLU A 1 761 ? -3.108 27.496 89.864 1.00 164.00 ? 761 GLU A CD 1 ATOM 5884 O OE1 . GLU A 1 761 ? -2.353 26.549 90.173 1.00 169.20 ? 761 GLU A OE1 1 ATOM 5885 O OE2 . GLU A 1 761 ? -2.712 28.676 89.762 1.00 165.47 ? 761 GLU A OE2 1 ATOM 5886 N N . HIS A 1 762 ? -8.435 29.651 90.544 1.00 143.12 ? 762 HIS A N 1 ATOM 5887 C CA . HIS A 1 762 ? -9.263 30.830 90.759 1.00 149.55 ? 762 HIS A CA 1 ATOM 5888 C C . HIS A 1 762 ? -8.510 31.923 91.511 1.00 145.69 ? 762 HIS A C 1 ATOM 5889 O O . HIS A 1 762 ? -7.852 31.665 92.520 1.00 147.71 ? 762 HIS A O 1 ATOM 5890 C CB . HIS A 1 762 ? -10.541 30.447 91.514 1.00 147.60 ? 762 HIS A CB 1 ATOM 5891 C CG . HIS A 1 762 ? -10.796 31.269 92.738 1.00 149.41 ? 762 HIS A CG 1 ATOM 5892 N ND1 . HIS A 1 762 ? -11.344 32.533 92.689 1.00 143.96 ? 762 HIS A ND1 1 ATOM 5893 C CD2 . HIS A 1 762 ? -10.579 31.005 94.049 1.00 161.61 ? 762 HIS A CD2 1 ATOM 5894 C CE1 . HIS A 1 762 ? -11.452 33.012 93.916 1.00 149.92 ? 762 HIS A CE1 1 ATOM 5895 N NE2 . HIS A 1 762 ? -10.995 32.105 94.759 1.00 164.62 ? 762 HIS A NE2 1 ATOM 5896 N N . LYS A 1 763 ? -8.603 33.145 90.995 1.00 133.28 ? 763 LYS A N 1 ATOM 5897 C CA . LYS A 1 763 ? -8.039 34.311 91.661 1.00 145.65 ? 763 LYS A CA 1 ATOM 5898 C C . LYS A 1 763 ? -9.114 35.382 91.805 1.00 156.81 ? 763 LYS A C 1 ATOM 5899 O O . LYS A 1 763 ? -9.916 35.592 90.895 1.00 161.21 ? 763 LYS A O 1 ATOM 5900 C CB . LYS A 1 763 ? -6.834 34.854 90.889 1.00 151.69 ? 763 LYS A CB 1 ATOM 5901 C CG . LYS A 1 763 ? -5.634 33.916 90.878 1.00 172.95 ? 763 LYS A CG 1 ATOM 5902 C CD . LYS A 1 763 ? -4.409 34.584 90.272 1.00 174.89 ? 763 LYS A CD 1 ATOM 5903 C CE . LYS A 1 763 ? -3.187 33.679 90.354 1.00 171.40 ? 763 LYS A CE 1 ATOM 5904 N NZ . LYS A 1 763 ? -1.963 34.349 89.831 1.00 165.70 ? 763 LYS A NZ 1 ATOM 5905 N N . GLU A 1 764 ? -9.129 36.050 92.955 1.00 155.67 ? 764 GLU A N 1 ATOM 5906 C CA . GLU A 1 764 ? -10.160 37.036 93.266 1.00 154.81 ? 764 GLU A CA 1 ATOM 5907 C C . GLU A 1 764 ? -10.164 38.204 92.282 1.00 158.52 ? 764 GLU A C 1 ATOM 5908 O O . GLU A 1 764 ? -11.213 38.783 91.999 1.00 156.18 ? 764 GLU A O 1 ATOM 5909 C CB . GLU A 1 764 ? -9.982 37.558 94.694 1.00 151.51 ? 764 GLU A CB 1 ATOM 5910 C CG . GLU A 1 764 ? -10.135 36.492 95.768 1.00 160.57 ? 764 GLU A CG 1 ATOM 5911 C CD . GLU A 1 764 ? -10.054 37.061 97.171 1.00 183.73 ? 764 GLU A CD 1 ATOM 5912 O OE1 . GLU A 1 764 ? -9.866 38.288 97.308 1.00 191.14 ? 764 GLU A OE1 1 ATOM 5913 O OE2 . GLU A 1 764 ? -10.179 36.280 98.140 1.00 192.55 ? 764 GLU A OE2 1 ATOM 5914 N N . ASN A 1 765 ? -8.988 38.548 91.766 1.00 162.15 ? 765 ASN A N 1 ATOM 5915 C CA . ASN A 1 765 ? -8.865 39.619 90.783 1.00 156.65 ? 765 ASN A CA 1 ATOM 5916 C C . ASN A 1 765 ? -8.298 39.103 89.463 1.00 149.76 ? 765 ASN A C 1 ATOM 5917 O O . ASN A 1 765 ? -7.102 39.244 89.205 1.00 164.03 ? 765 ASN A O 1 ATOM 5918 C CB . ASN A 1 765 ? -7.975 40.745 91.322 1.00 161.87 ? 765 ASN A CB 1 ATOM 5919 C CG . ASN A 1 765 ? -8.580 41.454 92.521 1.00 165.95 ? 765 ASN A CG 1 ATOM 5920 O OD1 . ASN A 1 765 ? -9.451 40.916 93.205 1.00 171.07 ? 765 ASN A OD1 1 ATOM 5921 N ND2 . ASN A 1 765 ? -8.116 42.670 92.782 1.00 166.17 ? 765 ASN A ND2 1 ATOM 5922 N N . PRO A 1 766 ? -9.153 38.493 88.625 1.00 132.82 ? 766 PRO A N 1 ATOM 5923 C CA . PRO A 1 766 ? -8.687 37.915 87.359 1.00 133.75 ? 766 PRO A CA 1 ATOM 5924 C C . PRO A 1 766 ? -8.119 38.959 86.404 1.00 133.71 ? 766 PRO A C 1 ATOM 5925 O O . PRO A 1 766 ? -8.782 39.951 86.104 1.00 131.50 ? 766 PRO A O 1 ATOM 5926 C CB . PRO A 1 766 ? -9.956 37.286 86.769 1.00 126.89 ? 766 PRO A CB 1 ATOM 5927 C CG . PRO A 1 766 ? -10.888 37.127 87.925 1.00 127.19 ? 766 PRO A CG 1 ATOM 5928 C CD . PRO A 1 766 ? -10.594 38.277 88.833 1.00 129.04 ? 766 PRO A CD 1 ATOM 5929 N N . GLU A 1 767 ? -6.896 38.729 85.938 1.00 148.14 ? 767 GLU A N 1 ATOM 5930 C CA . GLU A 1 767 ? -6.259 39.617 84.972 1.00 148.69 ? 767 GLU A CA 1 ATOM 5931 C C . GLU A 1 767 ? -6.656 39.308 83.530 1.00 136.30 ? 767 GLU A C 1 ATOM 5932 O O . GLU A 1 767 ? -6.903 40.216 82.736 1.00 133.33 ? 767 GLU A O 1 ATOM 5933 C CB . GLU A 1 767 ? -4.739 39.550 85.120 1.00 160.31 ? 767 GLU A CB 1 ATOM 5934 C CG . GLU A 1 767 ? -4.244 39.954 86.499 1.00 162.06 ? 767 GLU A CG 1 ATOM 5935 C CD . GLU A 1 767 ? -2.732 40.020 86.580 1.00 162.79 ? 767 GLU A CD 1 ATOM 5936 O OE1 . GLU A 1 767 ? -2.192 39.918 87.701 1.00 158.09 ? 767 GLU A OE1 1 ATOM 5937 O OE2 . GLU A 1 767 ? -2.087 40.179 85.524 1.00 167.74 ? 767 GLU A OE2 1 ATOM 5938 N N . THR A 1 768 ? -6.715 38.021 83.199 1.00 135.89 ? 768 THR A N 1 ATOM 5939 C CA . THR A 1 768 ? -6.863 37.590 81.811 1.00 135.10 ? 768 THR A CA 1 ATOM 5940 C C . THR A 1 768 ? -7.958 36.545 81.627 1.00 129.30 ? 768 THR A C 1 ATOM 5941 O O . THR A 1 768 ? -8.497 36.013 82.599 1.00 124.28 ? 768 THR A O 1 ATOM 5942 C CB . THR A 1 768 ? -5.545 37.005 81.259 1.00 135.51 ? 768 THR A CB 1 ATOM 5943 O OG1 . THR A 1 768 ? -5.156 35.872 82.045 1.00 135.94 ? 768 THR A OG1 1 ATOM 5944 C CG2 . THR A 1 768 ? -4.434 38.045 81.290 1.00 139.15 ? 768 THR A CG2 1 ATOM 5945 N N . GLU A 1 769 ? -8.286 36.271 80.366 1.00 129.53 ? 769 GLU A N 1 ATOM 5946 C CA . GLU A 1 769 ? -9.271 35.255 80.008 1.00 116.24 ? 769 GLU A CA 1 ATOM 5947 C C . GLU A 1 769 ? -8.922 33.893 80.595 1.00 112.67 ? 769 GLU A C 1 ATOM 5948 O O . GLU A 1 769 ? -9.806 33.114 80.952 1.00 109.55 ? 769 GLU A O 1 ATOM 5949 C CB . GLU A 1 769 ? -9.384 35.136 78.487 1.00 111.68 ? 769 GLU A CB 1 ATOM 5950 C CG . GLU A 1 769 ? -9.499 36.460 77.760 1.00 118.60 ? 769 GLU A CG 1 ATOM 5951 C CD . GLU A 1 769 ? -9.485 36.294 76.253 1.00 123.87 ? 769 GLU A CD 1 ATOM 5952 O OE1 . GLU A 1 769 ? -9.916 35.227 75.768 1.00 106.27 ? 769 GLU A OE1 1 ATOM 5953 O OE2 . GLU A 1 769 ? -9.037 37.228 75.555 1.00 142.05 ? 769 GLU A OE2 1 ATOM 5954 N N . GLU A 1 770 ? -7.626 33.614 80.680 1.00 114.63 ? 770 GLU A N 1 ATOM 5955 C CA . GLU A 1 770 ? -7.131 32.350 81.209 1.00 119.06 ? 770 GLU A CA 1 ATOM 5956 C C . GLU A 1 770 ? -7.543 32.158 82.666 1.00 122.70 ? 770 GLU A C 1 ATOM 5957 O O . GLU A 1 770 ? -7.802 31.037 83.107 1.00 122.41 ? 770 GLU A O 1 ATOM 5958 C CB . GLU A 1 770 ? -5.607 32.288 81.082 1.00 135.50 ? 770 GLU A CB 1 ATOM 5959 C CG . GLU A 1 770 ? -5.013 30.903 81.277 1.00 146.28 ? 770 GLU A CG 1 ATOM 5960 C CD . GLU A 1 770 ? -5.178 30.020 80.056 1.00 148.78 ? 770 GLU A CD 1 ATOM 5961 O OE1 . GLU A 1 770 ? -5.579 30.538 78.992 1.00 150.70 ? 770 GLU A OE1 1 ATOM 5962 O OE2 . GLU A 1 770 ? -4.905 28.806 80.160 1.00 137.62 ? 770 GLU A OE2 1 ATOM 5963 N N . ASP A 1 771 ? -7.607 33.262 83.404 1.00 122.34 ? 771 ASP A N 1 ATOM 5964 C CA . ASP A 1 771 ? -7.930 33.225 84.826 1.00 119.46 ? 771 ASP A CA 1 ATOM 5965 C C . ASP A 1 771 ? -9.435 33.200 85.073 1.00 116.02 ? 771 ASP A C 1 ATOM 5966 O O . ASP A 1 771 ? -9.880 33.048 86.209 1.00 118.42 ? 771 ASP A O 1 ATOM 5967 C CB . ASP A 1 771 ? -7.311 34.429 85.541 1.00 127.42 ? 771 ASP A CB 1 ATOM 5968 C CG . ASP A 1 771 ? -5.826 34.568 85.272 1.00 154.96 ? 771 ASP A CG 1 ATOM 5969 O OD1 . ASP A 1 771 ? -5.024 33.969 86.020 1.00 171.74 ? 771 ASP A OD1 1 ATOM 5970 O OD2 . ASP A 1 771 ? -5.459 35.280 84.313 1.00 155.45 ? 771 ASP A OD2 1 ATOM 5971 N N . VAL A 1 772 ? -10.216 33.355 84.008 1.00 117.34 ? 772 VAL A N 1 ATOM 5972 C CA . VAL A 1 772 ? -11.670 33.391 84.128 1.00 113.37 ? 772 VAL A CA 1 ATOM 5973 C C . VAL A 1 772 ? -12.303 32.069 83.701 1.00 106.40 ? 772 VAL A C 1 ATOM 5974 O O . VAL A 1 772 ? -12.906 31.370 84.514 1.00 111.90 ? 772 VAL A O 1 ATOM 5975 C CB . VAL A 1 772 ? -12.274 34.534 83.291 1.00 107.64 ? 772 VAL A CB 1 ATOM 5976 C CG1 . VAL A 1 772 ? -13.789 34.535 83.409 1.00 104.92 ? 772 VAL A CG1 1 ATOM 5977 C CG2 . VAL A 1 772 ? -11.703 35.871 83.735 1.00 111.78 ? 772 VAL A CG2 1 ATOM 5978 N N . GLY A 1 773 ? -12.167 31.735 82.422 1.00 101.40 ? 773 GLY A N 1 ATOM 5979 C CA . GLY A 1 773 ? -12.709 30.494 81.898 1.00 97.65 ? 773 GLY A CA 1 ATOM 5980 C C . GLY A 1 773 ? -12.604 30.402 80.388 1.00 94.83 ? 773 GLY A C 1 ATOM 5981 O O . GLY A 1 773 ? -12.054 31.297 79.747 1.00 95.81 ? 773 GLY A O 1 ATOM 5982 N N . PRO A 1 774 ? -13.137 29.314 79.811 1.00 103.17 ? 774 PRO A N 1 ATOM 5983 C CA . PRO A 1 774 ? -13.112 29.092 78.361 1.00 99.47 ? 774 PRO A CA 1 ATOM 5984 C C . PRO A 1 774 ? -13.902 30.155 77.606 1.00 90.48 ? 774 PRO A C 1 ATOM 5985 O O . PRO A 1 774 ? -14.745 30.826 78.201 1.00 91.35 ? 774 PRO A O 1 ATOM 5986 C CB . PRO A 1 774 ? -13.760 27.713 78.206 1.00 100.42 ? 774 PRO A CB 1 ATOM 5987 C CG . PRO A 1 774 ? -14.616 27.564 79.417 1.00 100.34 ? 774 PRO A CG 1 ATOM 5988 C CD . PRO A 1 774 ? -13.860 28.244 80.519 1.00 109.01 ? 774 PRO A CD 1 ATOM 5989 N N . VAL A 1 775 ? -13.640 30.299 76.312 1.00 93.94 ? 775 VAL A N 1 ATOM 5990 C CA . VAL A 1 775 ? -14.319 31.314 75.518 1.00 89.54 ? 775 VAL A CA 1 ATOM 5991 C C . VAL A 1 775 ? -15.572 30.746 74.860 1.00 92.26 ? 775 VAL A C 1 ATOM 5992 O O . VAL A 1 775 ? -15.489 29.908 73.962 1.00 100.90 ? 775 VAL A O 1 ATOM 5993 C CB . VAL A 1 775 ? -13.396 31.892 74.424 1.00 86.19 ? 775 VAL A CB 1 ATOM 5994 C CG1 . VAL A 1 775 ? -14.119 32.972 73.636 1.00 86.64 ? 775 VAL A CG1 1 ATOM 5995 C CG2 . VAL A 1 775 ? -12.120 32.442 75.039 1.00 106.87 ? 775 VAL A CG2 1 ATOM 5996 N N . VAL A 1 776 ? -16.732 31.209 75.316 1.00 88.43 ? 776 VAL A N 1 ATOM 5997 C CA . VAL A 1 776 ? -18.002 30.827 74.714 1.00 78.65 ? 776 VAL A CA 1 ATOM 5998 C C . VAL A 1 776 ? -18.468 31.935 73.780 1.00 92.53 ? 776 VAL A C 1 ATOM 5999 O O . VAL A 1 776 ? -18.607 33.086 74.191 1.00 90.10 ? 776 VAL A O 1 ATOM 6000 C CB . VAL A 1 776 ? -19.087 30.555 75.775 1.00 80.50 ? 776 VAL A CB 1 ATOM 6001 C CG1 . VAL A 1 776 ? -20.437 30.333 75.110 1.00 80.84 ? 776 VAL A CG1 1 ATOM 6002 C CG2 . VAL A 1 776 ? -18.705 29.357 76.631 1.00 91.23 ? 776 VAL A CG2 1 ATOM 6003 N N . GLN A 1 777 ? -18.702 31.587 72.520 1.00 108.96 ? 777 GLN A N 1 ATOM 6004 C CA . GLN A 1 777 ? -19.038 32.582 71.513 1.00 98.95 ? 777 GLN A CA 1 ATOM 6005 C C . GLN A 1 777 ? -20.428 32.359 70.928 1.00 84.67 ? 777 GLN A C 1 ATOM 6006 O O . GLN A 1 777 ? -20.716 31.301 70.367 1.00 76.90 ? 777 GLN A O 1 ATOM 6007 C CB . GLN A 1 777 ? -17.990 32.573 70.398 1.00 98.47 ? 777 GLN A CB 1 ATOM 6008 C CG . GLN A 1 777 ? -18.202 33.629 69.326 1.00 112.53 ? 777 GLN A CG 1 ATOM 6009 C CD . GLN A 1 777 ? -17.057 33.682 68.334 1.00 133.15 ? 777 GLN A CD 1 ATOM 6010 O OE1 . GLN A 1 777 ? -15.982 33.132 68.577 1.00 131.54 ? 777 GLN A OE1 1 ATOM 6011 N NE2 . GLN A 1 777 ? -17.283 34.345 67.206 1.00 134.81 ? 777 GLN A NE2 1 ATOM 6012 N N . HIS A 1 778 ? -21.286 33.363 71.070 1.00 70.51 ? 778 HIS A N 1 ATOM 6013 C CA . HIS A 1 778 ? -22.609 33.330 70.465 1.00 78.43 ? 778 HIS A CA 1 ATOM 6014 C C . HIS A 1 778 ? -22.636 34.198 69.216 1.00 79.93 ? 778 HIS A C 1 ATOM 6015 O O . HIS A 1 778 ? -22.186 35.344 69.234 1.00 91.92 ? 778 HIS A O 1 ATOM 6016 C CB . HIS A 1 778 ? -23.677 33.798 71.457 1.00 71.53 ? 778 HIS A CB 1 ATOM 6017 C CG . HIS A 1 778 ? -24.018 32.782 72.502 1.00 88.90 ? 778 HIS A CG 1 ATOM 6018 N ND1 . HIS A 1 778 ? -25.205 32.802 73.201 1.00 90.29 ? 778 HIS A ND1 1 ATOM 6019 C CD2 . HIS A 1 778 ? -23.327 31.714 72.966 1.00 95.63 ? 778 HIS A CD2 1 ATOM 6020 C CE1 . HIS A 1 778 ? -25.232 31.791 74.050 1.00 87.44 ? 778 HIS A CE1 1 ATOM 6021 N NE2 . HIS A 1 778 ? -24.103 31.116 73.928 1.00 98.32 ? 778 HIS A NE2 1 ATOM 6022 N N . ILE A 1 779 ? -23.159 33.645 68.128 1.00 75.65 ? 779 ILE A N 1 ATOM 6023 C CA . ILE A 1 779 ? -23.265 34.383 66.877 1.00 63.67 ? 779 ILE A CA 1 ATOM 6024 C C . ILE A 1 779 ? -24.718 34.480 66.433 1.00 68.52 ? 779 ILE A C 1 ATOM 6025 O O . ILE A 1 779 ? -25.399 33.468 66.307 1.00 55.90 ? 779 ILE A O 1 ATOM 6026 C CB . ILE A 1 779 ? -22.438 33.723 65.758 1.00 62.57 ? 779 ILE A CB 1 ATOM 6027 C CG1 . ILE A 1 779 ? -20.962 33.649 66.156 1.00 91.03 ? 779 ILE A CG1 1 ATOM 6028 C CG2 . ILE A 1 779 ? -22.603 34.485 64.454 1.00 64.34 ? 779 ILE A CG2 1 ATOM 6029 C CD1 . ILE A 1 779 ? -20.078 33.010 65.107 1.00 113.95 ? 779 ILE A CD1 1 ATOM 6030 N N . TYR A 1 780 ? -25.192 35.700 66.204 1.00 70.68 ? 780 TYR A N 1 ATOM 6031 C CA . TYR A 1 780 ? -26.547 35.907 65.705 1.00 54.44 ? 780 TYR A CA 1 ATOM 6032 C C . TYR A 1 780 ? -26.520 36.560 64.329 1.00 55.81 ? 780 TYR A C 1 ATOM 6033 O O . TYR A 1 780 ? -25.820 37.550 64.116 1.00 69.58 ? 780 TYR A O 1 ATOM 6034 C CB . TYR A 1 780 ? -27.362 36.763 66.675 1.00 53.92 ? 780 TYR A CB 1 ATOM 6035 C CG . TYR A 1 780 ? -27.750 36.052 67.951 1.00 62.34 ? 780 TYR A CG 1 ATOM 6036 C CD1 . TYR A 1 780 ? -26.958 36.141 69.088 1.00 68.49 ? 780 TYR A CD1 1 ATOM 6037 C CD2 . TYR A 1 780 ? -28.911 35.293 68.019 1.00 72.94 ? 780 TYR A CD2 1 ATOM 6038 C CE1 . TYR A 1 780 ? -27.309 35.493 70.256 1.00 91.28 ? 780 TYR A CE1 1 ATOM 6039 C CE2 . TYR A 1 780 ? -29.273 34.643 69.184 1.00 72.99 ? 780 TYR A CE2 1 ATOM 6040 C CZ . TYR A 1 780 ? -28.469 34.746 70.299 1.00 87.39 ? 780 TYR A CZ 1 ATOM 6041 O OH . TYR A 1 780 ? -28.822 34.100 71.461 1.00 82.22 ? 780 TYR A OH 1 ATOM 6042 N N . GLU A 1 781 ? -27.284 36.001 63.397 1.00 53.62 ? 781 GLU A N 1 ATOM 6043 C CA . GLU A 1 781 ? -27.343 36.545 62.047 1.00 58.55 ? 781 GLU A CA 1 ATOM 6044 C C . GLU A 1 781 ? -28.769 36.847 61.607 1.00 74.14 ? 781 GLU A C 1 ATOM 6045 O O . GLU A 1 781 ? -29.638 35.976 61.640 1.00 57.52 ? 781 GLU A O 1 ATOM 6046 C CB . GLU A 1 781 ? -26.700 35.583 61.049 1.00 68.57 ? 781 GLU A CB 1 ATOM 6047 C CG . GLU A 1 781 ? -26.744 36.097 59.622 1.00 76.89 ? 781 GLU A CG 1 ATOM 6048 C CD . GLU A 1 781 ? -26.221 35.096 58.614 1.00 120.74 ? 781 GLU A CD 1 ATOM 6049 O OE1 . GLU A 1 781 ? -25.989 33.928 58.993 1.00 142.64 ? 781 GLU A OE1 1 ATOM 6050 O OE2 . GLU A 1 781 ? -26.042 35.481 57.440 1.00 120.39 ? 781 GLU A OE2 1 ATOM 6051 N N . LEU A 1 782 ? -28.998 38.089 61.192 1.00 77.36 ? 782 LEU A N 1 ATOM 6052 C CA . LEU A 1 782 ? -30.271 38.483 60.603 1.00 68.37 ? 782 LEU A CA 1 ATOM 6053 C C . LEU A 1 782 ? -30.105 38.640 59.096 1.00 59.86 ? 782 LEU A C 1 ATOM 6054 O O . LEU A 1 782 ? -29.433 39.561 58.631 1.00 75.02 ? 782 LEU A O 1 ATOM 6055 C CB . LEU A 1 782 ? -30.777 39.786 61.224 1.00 73.37 ? 782 LEU A CB 1 ATOM 6056 C CG . LEU A 1 782 ? -32.135 40.293 60.734 1.00 61.17 ? 782 LEU A CG 1 ATOM 6057 C CD1 . LEU A 1 782 ? -33.222 39.280 61.047 1.00 77.54 ? 782 LEU A CD1 1 ATOM 6058 C CD2 . LEU A 1 782 ? -32.459 41.639 61.354 1.00 56.73 ? 782 LEU A CD2 1 ATOM 6059 N N . ARG A 1 783 ? -30.716 37.738 58.334 1.00 61.71 ? 783 ARG A N 1 ATOM 6060 C CA . ARG A 1 783 ? -30.553 37.740 56.886 1.00 70.40 ? 783 ARG A CA 1 ATOM 6061 C C . ARG A 1 783 ? -31.874 37.949 56.158 1.00 71.47 ? 783 ARG A C 1 ATOM 6062 O O . ARG A 1 783 ? -32.870 37.288 56.451 1.00 69.37 ? 783 ARG A O 1 ATOM 6063 C CB . ARG A 1 783 ? -29.907 36.433 56.419 1.00 90.82 ? 783 ARG A CB 1 ATOM 6064 C CG . ARG A 1 783 ? -29.654 36.377 54.920 1.00 72.48 ? 783 ARG A CG 1 ATOM 6065 C CD . ARG A 1 783 ? -28.705 35.249 54.551 1.00 73.58 ? 783 ARG A CD 1 ATOM 6066 N NE . ARG A 1 783 ? -28.365 35.273 53.131 1.00 88.84 ? 783 ARG A NE 1 ATOM 6067 C CZ . ARG A 1 783 ? -27.348 35.957 52.618 1.00 98.45 ? 783 ARG A CZ 1 ATOM 6068 N NH1 . ARG A 1 783 ? -26.563 36.675 53.408 1.00 87.23 ? 783 ARG A NH1 1 ATOM 6069 N NH2 . ARG A 1 783 ? -27.114 35.922 51.313 1.00 114.30 ? 783 ARG A NH2 1 ATOM 6070 N N . ASN A 1 784 ? -31.870 38.879 55.208 1.00 72.03 ? 784 ASN A N 1 ATOM 6071 C CA . ASN A 1 784 ? -33.023 39.104 54.349 1.00 76.17 ? 784 ASN A CA 1 ATOM 6072 C C . ASN A 1 784 ? -32.935 38.219 53.111 1.00 81.33 ? 784 ASN A C 1 ATOM 6073 O O . ASN A 1 784 ? -31.970 38.292 52.353 1.00 83.66 ? 784 ASN A O 1 ATOM 6074 C CB . ASN A 1 784 ? -33.121 40.579 53.949 1.00 91.19 ? 784 ASN A CB 1 ATOM 6075 C CG . ASN A 1 784 ? -34.361 40.882 53.128 1.00 84.00 ? 784 ASN A CG 1 ATOM 6076 O OD1 . ASN A 1 784 ? -35.308 40.096 53.097 1.00 85.86 ? 784 ASN A OD1 1 ATOM 6077 N ND2 . ASN A 1 784 ? -34.363 42.032 52.463 1.00 84.71 ? 784 ASN A ND2 1 ATOM 6078 N N . ASN A 1 785 ? -33.943 37.375 52.924 1.00 86.01 ? 785 ASN A N 1 ATOM 6079 C CA . ASN A 1 785 ? -33.991 36.452 51.795 1.00 102.22 ? 785 ASN A CA 1 ATOM 6080 C C . ASN A 1 785 ? -34.950 36.928 50.710 1.00 111.44 ? 785 ASN A C 1 ATOM 6081 O O . ASN A 1 785 ? -34.549 37.135 49.564 1.00 107.86 ? 785 ASN A O 1 ATOM 6082 C CB . ASN A 1 785 ? -34.383 35.050 52.264 1.00 94.34 ? 785 ASN A CB 1 ATOM 6083 C CG . ASN A 1 785 ? -33.260 34.351 53.007 1.00 103.52 ? 785 ASN A CG 1 ATOM 6084 O OD1 . ASN A 1 785 ? -33.392 34.020 54.185 1.00 100.70 ? 785 ASN A OD1 1 ATOM 6085 N ND2 . ASN A 1 785 ? -32.147 34.122 52.319 1.00 116.47 ? 785 ASN A ND2 1 ATOM 6086 N N . GLY A 1 786 ? -36.221 37.073 51.083 1.00 117.41 ? 786 GLY A N 1 ATOM 6087 C CA . GLY A 1 786 ? -37.278 37.450 50.160 1.00 108.55 ? 786 GLY A CA 1 ATOM 6088 C C . GLY A 1 786 ? -36.958 38.675 49.326 1.00 125.48 ? 786 GLY A C 1 ATOM 6089 O O . GLY A 1 786 ? -36.252 39.574 49.783 1.00 149.74 ? 786 GLY A O 1 ATOM 6090 N N . PRO A 1 787 ? -37.488 38.710 48.094 1.00 114.45 ? 787 PRO A N 1 ATOM 6091 C CA . PRO A 1 787 ? -37.135 39.649 47.021 1.00 114.22 ? 787 PRO A CA 1 ATOM 6092 C C . PRO A 1 787 ? -37.094 41.113 47.454 1.00 109.42 ? 787 PRO A C 1 ATOM 6093 O O . PRO A 1 787 ? -36.175 41.835 47.068 1.00 108.86 ? 787 PRO A O 1 ATOM 6094 C CB . PRO A 1 787 ? -38.247 39.426 45.987 1.00 118.30 ? 787 PRO A CB 1 ATOM 6095 C CG . PRO A 1 787 ? -39.347 38.731 46.727 1.00 119.16 ? 787 PRO A CG 1 ATOM 6096 C CD . PRO A 1 787 ? -38.647 37.881 47.727 1.00 118.09 ? 787 PRO A CD 1 ATOM 6097 N N . SER A 1 788 ? -38.068 41.540 48.249 1.00 106.22 ? 788 SER A N 1 ATOM 6098 C CA . SER A 1 788 ? -38.127 42.926 48.697 1.00 102.25 ? 788 SER A CA 1 ATOM 6099 C C . SER A 1 788 ? -37.074 43.216 49.760 1.00 96.74 ? 788 SER A C 1 ATOM 6100 O O . SER A 1 788 ? -36.696 42.335 50.531 1.00 94.27 ? 788 SER A O 1 ATOM 6101 C CB . SER A 1 788 ? -39.517 43.254 49.243 1.00 101.53 ? 788 SER A CB 1 ATOM 6102 O OG . SER A 1 788 ? -40.516 43.017 48.267 1.00 107.72 ? 788 SER A OG 1 ATOM 6103 N N . SER A 1 789 ? -36.601 44.458 49.794 1.00 95.52 ? 789 SER A N 1 ATOM 6104 C CA . SER A 1 789 ? -35.660 44.889 50.819 1.00 92.61 ? 789 SER A CA 1 ATOM 6105 C C . SER A 1 789 ? -36.400 45.601 51.946 1.00 86.80 ? 789 SER A C 1 ATOM 6106 O O . SER A 1 789 ? -37.617 45.777 51.880 1.00 90.31 ? 789 SER A O 1 ATOM 6107 C CB . SER A 1 789 ? -34.599 45.811 50.220 1.00 94.65 ? 789 SER A CB 1 ATOM 6108 O OG . SER A 1 789 ? -34.054 45.260 49.036 1.00 100.40 ? 789 SER A OG 1 ATOM 6109 N N . PHE A 1 790 ? -35.667 46.012 52.975 1.00 81.44 ? 790 PHE A N 1 ATOM 6110 C CA . PHE A 1 790 ? -36.245 46.845 54.024 1.00 79.10 ? 790 PHE A CA 1 ATOM 6111 C C . PHE A 1 790 ? -35.236 47.884 54.499 1.00 76.90 ? 790 PHE A C 1 ATOM 6112 O O . PHE A 1 790 ? -34.044 47.605 54.608 1.00 76.82 ? 790 PHE A O 1 ATOM 6113 C CB . PHE A 1 790 ? -36.751 45.994 55.197 1.00 76.22 ? 790 PHE A CB 1 ATOM 6114 C CG . PHE A 1 790 ? -35.684 45.195 55.894 1.00 75.65 ? 790 PHE A CG 1 ATOM 6115 C CD1 . PHE A 1 790 ? -34.932 45.755 56.914 1.00 83.78 ? 790 PHE A CD1 1 ATOM 6116 C CD2 . PHE A 1 790 ? -35.463 43.870 55.557 1.00 88.15 ? 790 PHE A CD2 1 ATOM 6117 C CE1 . PHE A 1 790 ? -33.958 45.020 57.561 1.00 76.43 ? 790 PHE A CE1 1 ATOM 6118 C CE2 . PHE A 1 790 ? -34.494 43.128 56.205 1.00 86.63 ? 790 PHE A CE2 1 ATOM 6119 C CZ . PHE A 1 790 ? -33.745 43.704 57.210 1.00 74.71 ? 790 PHE A CZ 1 ATOM 6120 N N . SER A 1 791 ? -35.729 49.088 54.768 1.00 84.48 ? 791 SER A N 1 ATOM 6121 C CA . SER A 1 791 ? -34.874 50.229 55.076 1.00 75.78 ? 791 SER A CA 1 ATOM 6122 C C . SER A 1 791 ? -34.368 50.257 56.517 1.00 72.05 ? 791 SER A C 1 ATOM 6123 O O . SER A 1 791 ? -33.253 50.706 56.768 1.00 81.77 ? 791 SER A O 1 ATOM 6124 C CB . SER A 1 791 ? -35.619 51.528 54.769 1.00 80.13 ? 791 SER A CB 1 ATOM 6125 O OG . SER A 1 791 ? -36.924 51.502 55.315 1.00 115.04 ? 791 SER A OG 1 ATOM 6126 N N . LYS A 1 792 ? -35.187 49.798 57.459 1.00 70.55 ? 792 LYS A N 1 ATOM 6127 C CA . LYS A 1 792 ? -34.808 49.817 58.873 1.00 70.17 ? 792 LYS A CA 1 ATOM 6128 C C . LYS A 1 792 ? -35.367 48.624 59.646 1.00 68.94 ? 792 LYS A C 1 ATOM 6129 O O . LYS A 1 792 ? -36.471 48.156 59.370 1.00 74.80 ? 792 LYS A O 1 ATOM 6130 C CB . LYS A 1 792 ? -35.276 51.114 59.539 1.00 69.51 ? 792 LYS A CB 1 ATOM 6131 C CG . LYS A 1 792 ? -34.460 52.348 59.194 1.00 84.04 ? 792 LYS A CG 1 ATOM 6132 C CD . LYS A 1 792 ? -35.041 53.590 59.850 1.00 117.95 ? 792 LYS A CD 1 ATOM 6133 C CE . LYS A 1 792 ? -34.236 54.830 59.496 1.00 139.37 ? 792 LYS A CE 1 ATOM 6134 N NZ . LYS A 1 792 ? -32.848 54.764 60.031 1.00 146.83 ? 792 LYS A NZ 1 ATOM 6135 N N . ALA A 1 793 ? -34.601 48.144 60.621 1.00 69.95 ? 793 ALA A N 1 ATOM 6136 C CA . ALA A 1 793 ? -35.051 47.059 61.487 1.00 69.85 ? 793 ALA A CA 1 ATOM 6137 C C . ALA A 1 793 ? -34.412 47.147 62.869 1.00 81.76 ? 793 ALA A C 1 ATOM 6138 O O . ALA A 1 793 ? -33.309 47.671 63.024 1.00 79.73 ? 793 ALA A O 1 ATOM 6139 C CB . ALA A 1 793 ? -34.746 45.715 60.856 1.00 60.02 ? 793 ALA A CB 1 ATOM 6140 N N . MET A 1 794 ? -35.117 46.630 63.870 1.00 78.14 ? 794 MET A N 1 ATOM 6141 C CA . MET A 1 794 ? -34.611 46.604 65.238 1.00 78.90 ? 794 MET A CA 1 ATOM 6142 C C . MET A 1 794 ? -34.285 45.180 65.674 1.00 68.89 ? 794 MET A C 1 ATOM 6143 O O . MET A 1 794 ? -35.025 44.246 65.368 1.00 72.11 ? 794 MET A O 1 ATOM 6144 C CB . MET A 1 794 ? -35.626 47.229 66.197 1.00 66.18 ? 794 MET A CB 1 ATOM 6145 C CG . MET A 1 794 ? -35.848 48.716 65.986 1.00 65.54 ? 794 MET A CG 1 ATOM 6146 S SD . MET A 1 794 ? -34.354 49.683 66.267 1.00 109.61 ? 794 MET A SD 1 ATOM 6147 C CE . MET A 1 794 ? -34.042 49.326 67.992 1.00 68.48 ? 794 MET A CE 1 ATOM 6148 N N . LEU A 1 795 ? -33.174 45.021 66.388 1.00 78.49 ? 795 LEU A N 1 ATOM 6149 C CA . LEU A 1 795 ? -32.749 43.713 66.880 1.00 65.98 ? 795 LEU A CA 1 ATOM 6150 C C . LEU A 1 795 ? -32.463 43.764 68.377 1.00 75.02 ? 795 LEU A C 1 ATOM 6151 O O . LEU A 1 795 ? -31.634 44.551 68.833 1.00 103.72 ? 795 LEU A O 1 ATOM 6152 C CB . LEU A 1 795 ? -31.511 43.228 66.120 1.00 55.34 ? 795 LEU A CB 1 ATOM 6153 C CG . LEU A 1 795 ? -30.986 41.824 66.438 1.00 65.64 ? 795 LEU A CG 1 ATOM 6154 C CD1 . LEU A 1 795 ? -30.625 41.093 65.158 1.00 62.05 ? 795 LEU A CD1 1 ATOM 6155 C CD2 . LEU A 1 795 ? -29.781 41.882 67.366 1.00 72.43 ? 795 LEU A CD2 1 ATOM 6156 N N . HIS A 1 796 ? -33.152 42.919 69.136 1.00 66.09 ? 796 HIS A N 1 ATOM 6157 C CA . HIS A 1 796 ? -33.006 42.899 70.587 1.00 71.39 ? 796 HIS A CA 1 ATOM 6158 C C . HIS A 1 796 ? -32.378 41.595 71.068 1.00 83.54 ? 796 HIS A C 1 ATOM 6159 O O . HIS A 1 796 ? -32.889 40.513 70.789 1.00 75.84 ? 796 HIS A O 1 ATOM 6160 C CB . HIS A 1 796 ? -34.366 43.106 71.258 1.00 61.01 ? 796 HIS A CB 1 ATOM 6161 C CG . HIS A 1 796 ? -34.972 44.447 70.990 1.00 66.36 ? 796 HIS A CG 1 ATOM 6162 N ND1 . HIS A 1 796 ? -34.912 45.484 71.896 1.00 73.24 ? 796 HIS A ND1 1 ATOM 6163 C CD2 . HIS A 1 796 ? -35.648 44.923 69.917 1.00 75.86 ? 796 HIS A CD2 1 ATOM 6164 C CE1 . HIS A 1 796 ? -35.526 46.540 71.393 1.00 86.13 ? 796 HIS A CE1 1 ATOM 6165 N NE2 . HIS A 1 796 ? -35.981 46.226 70.193 1.00 103.64 ? 796 HIS A NE2 1 ATOM 6166 N N . LEU A 1 797 ? -31.268 41.707 71.791 1.00 79.60 ? 797 LEU A N 1 ATOM 6167 C CA . LEU A 1 797 ? -30.590 40.535 72.333 1.00 67.62 ? 797 LEU A CA 1 ATOM 6168 C C . LEU A 1 797 ? -30.726 40.463 73.849 1.00 77.91 ? 797 LEU A C 1 ATOM 6169 O O . LEU A 1 797 ? -30.322 41.382 74.562 1.00 87.76 ? 797 LEU A O 1 ATOM 6170 C CB . LEU A 1 797 ? -29.109 40.537 71.949 1.00 65.51 ? 797 LEU A CB 1 ATOM 6171 C CG . LEU A 1 797 ? -28.258 39.435 72.589 1.00 73.31 ? 797 LEU A CG 1 ATOM 6172 C CD1 . LEU A 1 797 ? -28.758 38.059 72.174 1.00 60.30 ? 797 LEU A CD1 1 ATOM 6173 C CD2 . LEU A 1 797 ? -26.786 39.605 72.240 1.00 92.89 ? 797 LEU A CD2 1 ATOM 6174 N N . GLN A 1 798 ? -31.299 39.368 74.334 1.00 68.26 ? 798 GLN A N 1 ATOM 6175 C CA . GLN A 1 798 ? -31.378 39.125 75.768 1.00 68.77 ? 798 GLN A CA 1 ATOM 6176 C C . GLN A 1 798 ? -30.261 38.179 76.188 1.00 75.15 ? 798 GLN A C 1 ATOM 6177 O O . GLN A 1 798 ? -30.128 37.081 75.647 1.00 90.25 ? 798 GLN A O 1 ATOM 6178 C CB . GLN A 1 798 ? -32.743 38.552 76.151 1.00 72.16 ? 798 GLN A CB 1 ATOM 6179 C CG . GLN A 1 798 ? -33.912 39.442 75.763 1.00 76.92 ? 798 GLN A CG 1 ATOM 6180 C CD . GLN A 1 798 ? -35.218 38.987 76.382 1.00 83.59 ? 798 GLN A CD 1 ATOM 6181 O OE1 . GLN A 1 798 ? -35.229 38.199 77.328 1.00 85.97 ? 798 GLN A OE1 1 ATOM 6182 N NE2 . GLN A 1 798 ? -36.330 39.481 75.850 1.00 103.66 ? 798 GLN A NE2 1 ATOM 6183 N N . TRP A 1 799 ? -29.460 38.611 77.156 1.00 74.69 ? 799 TRP A N 1 ATOM 6184 C CA . TRP A 1 799 ? -28.282 37.856 77.568 1.00 75.95 ? 799 TRP A CA 1 ATOM 6185 C C . TRP A 1 799 ? -28.319 37.536 79.060 1.00 93.11 ? 799 TRP A C 1 ATOM 6186 O O . TRP A 1 799 ? -28.729 38.370 79.866 1.00 96.46 ? 799 TRP A O 1 ATOM 6187 C CB . TRP A 1 799 ? -27.016 38.644 77.223 1.00 72.24 ? 799 TRP A CB 1 ATOM 6188 C CG . TRP A 1 799 ? -25.747 37.874 77.380 1.00 79.76 ? 799 TRP A CG 1 ATOM 6189 C CD1 . TRP A 1 799 ? -24.976 37.782 78.502 1.00 93.39 ? 799 TRP A CD1 1 ATOM 6190 C CD2 . TRP A 1 799 ? -25.090 37.091 76.377 1.00 85.43 ? 799 TRP A CD2 1 ATOM 6191 N NE1 . TRP A 1 799 ? -23.883 36.986 78.261 1.00 91.84 ? 799 TRP A NE1 1 ATOM 6192 C CE2 . TRP A 1 799 ? -23.930 36.550 76.963 1.00 80.00 ? 799 TRP A CE2 1 ATOM 6193 C CE3 . TRP A 1 799 ? -25.373 36.793 75.040 1.00 90.87 ? 799 TRP A CE3 1 ATOM 6194 C CZ2 . TRP A 1 799 ? -23.052 35.728 76.259 1.00 71.51 ? 799 TRP A CZ2 1 ATOM 6195 C CZ3 . TRP A 1 799 ? -24.501 35.977 74.343 1.00 74.35 ? 799 TRP A CZ3 1 ATOM 6196 C CH2 . TRP A 1 799 ? -23.354 35.454 74.953 1.00 67.79 ? 799 TRP A CH2 1 ATOM 6197 N N . PRO A 1 800 ? -27.888 36.320 79.428 1.00 93.41 ? 800 PRO A N 1 ATOM 6198 C CA . PRO A 1 800 ? -27.841 35.866 80.822 1.00 88.69 ? 800 PRO A CA 1 ATOM 6199 C C . PRO A 1 800 ? -26.590 36.352 81.543 1.00 91.84 ? 800 PRO A C 1 ATOM 6200 O O . PRO A 1 800 ? -25.635 35.588 81.683 1.00 106.20 ? 800 PRO A O 1 ATOM 6201 C CB . PRO A 1 800 ? -27.829 34.334 80.700 1.00 87.11 ? 800 PRO A CB 1 ATOM 6202 C CG . PRO A 1 800 ? -28.077 34.032 79.242 1.00 81.59 ? 800 PRO A CG 1 ATOM 6203 C CD . PRO A 1 800 ? -27.591 35.223 78.495 1.00 79.17 ? 800 PRO A CD 1 ATOM 6204 N N . TYR A 1 801 ? -26.594 37.605 81.986 1.00 93.40 ? 801 TYR A N 1 ATOM 6205 C CA . TYR A 1 801 ? -25.425 38.184 82.636 1.00 104.02 ? 801 TYR A CA 1 ATOM 6206 C C . TYR A 1 801 ? -25.077 37.492 83.953 1.00 106.95 ? 801 TYR A C 1 ATOM 6207 O O . TYR A 1 801 ? -23.966 36.987 84.119 1.00 102.15 ? 801 TYR A O 1 ATOM 6208 C CB . TYR A 1 801 ? -25.638 39.679 82.878 1.00 105.06 ? 801 TYR A CB 1 ATOM 6209 C CG . TYR A 1 801 ? -24.410 40.377 83.411 1.00 114.90 ? 801 TYR A CG 1 ATOM 6210 C CD1 . TYR A 1 801 ? -23.189 40.263 82.759 1.00 118.26 ? 801 TYR A CD1 1 ATOM 6211 C CD2 . TYR A 1 801 ? -24.469 41.155 84.559 1.00 117.54 ? 801 TYR A CD2 1 ATOM 6212 C CE1 . TYR A 1 801 ? -22.061 40.897 83.238 1.00 125.87 ? 801 TYR A CE1 1 ATOM 6213 C CE2 . TYR A 1 801 ? -23.345 41.795 85.046 1.00 136.32 ? 801 TYR A CE2 1 ATOM 6214 C CZ . TYR A 1 801 ? -22.143 41.662 84.382 1.00 144.70 ? 801 TYR A CZ 1 ATOM 6215 O OH . TYR A 1 801 ? -21.020 42.297 84.861 1.00 155.17 ? 801 TYR A OH 1 ATOM 6216 N N . LYS A 1 802 ? -26.025 37.465 84.885 1.00 107.71 ? 802 LYS A N 1 ATOM 6217 C CA . LYS A 1 802 ? -25.773 36.890 86.203 1.00 110.42 ? 802 LYS A CA 1 ATOM 6218 C C . LYS A 1 802 ? -26.947 36.076 86.734 1.00 112.16 ? 802 LYS A C 1 ATOM 6219 O O . LYS A 1 802 ? -28.100 36.320 86.383 1.00 112.85 ? 802 LYS A O 1 ATOM 6220 C CB . LYS A 1 802 ? -25.431 37.991 87.212 1.00 114.43 ? 802 LYS A CB 1 ATOM 6221 C CG . LYS A 1 802 ? -24.064 38.627 87.020 1.00 114.60 ? 802 LYS A CG 1 ATOM 6222 C CD . LYS A 1 802 ? -23.705 39.521 88.198 1.00 118.37 ? 802 LYS A CD 1 ATOM 6223 C CE . LYS A 1 802 ? -22.295 40.075 88.065 1.00 120.25 ? 802 LYS A CE 1 ATOM 6224 N NZ . LYS A 1 802 ? -21.884 40.853 89.268 1.00 127.28 ? 802 LYS A NZ 1 ATOM 6225 N N . TYR A 1 803 ? -26.634 35.107 87.589 1.00 120.98 ? 803 TYR A N 1 ATOM 6226 C CA . TYR A 1 803 ? -27.647 34.347 88.308 1.00 120.07 ? 803 TYR A CA 1 ATOM 6227 C C . TYR A 1 803 ? -27.338 34.387 89.800 1.00 119.73 ? 803 TYR A C 1 ATOM 6228 O O . TYR A 1 803 ? -26.338 33.822 90.248 1.00 121.31 ? 803 TYR A O 1 ATOM 6229 C CB . TYR A 1 803 ? -27.705 32.904 87.801 1.00 115.07 ? 803 TYR A CB 1 ATOM 6230 C CG . TYR A 1 803 ? -28.747 32.046 88.484 1.00 122.10 ? 803 TYR A CG 1 ATOM 6231 C CD1 . TYR A 1 803 ? -28.376 30.967 89.277 1.00 128.57 ? 803 TYR A CD1 1 ATOM 6232 C CD2 . TYR A 1 803 ? -30.100 32.317 88.338 1.00 130.32 ? 803 TYR A CD2 1 ATOM 6233 C CE1 . TYR A 1 803 ? -29.326 30.179 89.902 1.00 127.97 ? 803 TYR A CE1 1 ATOM 6234 C CE2 . TYR A 1 803 ? -31.057 31.536 88.960 1.00 134.18 ? 803 TYR A CE2 1 ATOM 6235 C CZ . TYR A 1 803 ? -30.665 30.469 89.740 1.00 128.42 ? 803 TYR A CZ 1 ATOM 6236 O OH . TYR A 1 803 ? -31.614 29.691 90.361 1.00 127.23 ? 803 TYR A OH 1 ATOM 6237 N N . ASN A 1 804 ? -28.208 35.051 90.557 1.00 122.04 ? 804 ASN A N 1 ATOM 6238 C CA . ASN A 1 804 ? -28.010 35.277 91.987 1.00 124.73 ? 804 ASN A CA 1 ATOM 6239 C C . ASN A 1 804 ? -26.641 35.875 92.298 1.00 124.49 ? 804 ASN A C 1 ATOM 6240 O O . ASN A 1 804 ? -25.807 35.236 92.942 1.00 140.29 ? 804 ASN A O 1 ATOM 6241 C CB . ASN A 1 804 ? -28.197 33.972 92.765 1.00 126.37 ? 804 ASN A CB 1 ATOM 6242 C CG . ASN A 1 804 ? -29.534 33.314 92.484 1.00 128.30 ? 804 ASN A CG 1 ATOM 6243 O OD1 . ASN A 1 804 ? -30.122 33.510 91.420 1.00 125.98 ? 804 ASN A OD1 1 ATOM 6244 N ND2 . ASN A 1 804 ? -30.023 32.531 93.439 1.00 134.68 ? 804 ASN A ND2 1 ATOM 6245 N N . ASN A 1 805 ? -26.416 37.094 91.807 1.00 123.99 ? 805 ASN A N 1 ATOM 6246 C CA . ASN A 1 805 ? -25.205 37.872 92.086 1.00 126.65 ? 805 ASN A CA 1 ATOM 6247 C C . ASN A 1 805 ? -23.920 37.277 91.504 1.00 139.84 ? 805 ASN A C 1 ATOM 6248 O O . ASN A 1 805 ? -22.851 37.877 91.614 1.00 142.57 ? 805 ASN A O 1 ATOM 6249 C CB . ASN A 1 805 ? -25.036 38.072 93.597 1.00 143.94 ? 805 ASN A CB 1 ATOM 6250 C CG . ASN A 1 805 ? -26.210 38.801 94.224 1.00 155.51 ? 805 ASN A CG 1 ATOM 6251 O OD1 . ASN A 1 805 ? -26.854 39.635 93.584 1.00 147.16 ? 805 ASN A OD1 1 ATOM 6252 N ND2 . ASN A 1 805 ? -26.494 38.490 95.482 1.00 157.37 ? 805 ASN A ND2 1 ATOM 6253 N N . ASN A 1 806 ? -24.018 36.101 90.890 1.00 141.60 ? 806 ASN A N 1 ATOM 6254 C CA . ASN A 1 806 ? -22.845 35.442 90.326 1.00 118.37 ? 806 ASN A CA 1 ATOM 6255 C C . ASN A 1 806 ? -22.869 35.403 88.798 1.00 113.56 ? 806 ASN A C 1 ATOM 6256 O O . ASN A 1 806 ? -23.865 35.008 88.191 1.00 111.59 ? 806 ASN A O 1 ATOM 6257 C CB . ASN A 1 806 ? -22.718 34.026 90.890 1.00 118.62 ? 806 ASN A CB 1 ATOM 6258 C CG . ASN A 1 806 ? -22.515 34.016 92.394 1.00 124.65 ? 806 ASN A CG 1 ATOM 6259 O OD1 . ASN A 1 806 ? -21.397 34.186 92.881 1.00 145.80 ? 806 ASN A OD1 1 ATOM 6260 N ND2 . ASN A 1 806 ? -23.597 33.820 93.137 1.00 125.03 ? 806 ASN A ND2 1 ATOM 6261 N N . THR A 1 807 ? -21.759 35.813 88.188 1.00 112.06 ? 807 THR A N 1 ATOM 6262 C CA . THR A 1 807 ? -21.649 35.920 86.734 1.00 108.34 ? 807 THR A CA 1 ATOM 6263 C C . THR A 1 807 ? -21.742 34.564 86.037 1.00 106.59 ? 807 THR A C 1 ATOM 6264 O O . THR A 1 807 ? -21.150 33.585 86.488 1.00 134.19 ? 807 THR A O 1 ATOM 6265 C CB . THR A 1 807 ? -20.320 36.595 86.327 1.00 108.45 ? 807 THR A CB 1 ATOM 6266 O OG1 . THR A 1 807 ? -20.156 37.819 87.054 1.00 112.74 ? 807 THR A OG1 1 ATOM 6267 C CG2 . THR A 1 807 ? -20.295 36.890 84.833 1.00 104.54 ? 807 THR A CG2 1 ATOM 6268 N N . LEU A 1 808 ? -22.487 34.515 84.936 1.00 101.00 ? 808 LEU A N 1 ATOM 6269 C CA . LEU A 1 808 ? -22.597 33.303 84.132 1.00 96.67 ? 808 LEU A CA 1 ATOM 6270 C C . LEU A 1 808 ? -21.730 33.408 82.883 1.00 93.46 ? 808 LEU A C 1 ATOM 6271 O O . LEU A 1 808 ? -20.678 32.775 82.786 1.00 99.35 ? 808 LEU A O 1 ATOM 6272 C CB . LEU A 1 808 ? -24.053 33.044 83.739 1.00 95.16 ? 808 LEU A CB 1 ATOM 6273 C CG . LEU A 1 808 ? -25.068 32.966 84.877 1.00 100.20 ? 808 LEU A CG 1 ATOM 6274 C CD1 . LEU A 1 808 ? -26.445 32.618 84.337 1.00 101.23 ? 808 LEU A CD1 1 ATOM 6275 C CD2 . LEU A 1 808 ? -24.628 31.954 85.920 1.00 102.94 ? 808 LEU A CD2 1 ATOM 6276 N N . LEU A 1 809 ? -22.182 34.214 81.928 1.00 94.38 ? 809 LEU A N 1 ATOM 6277 C CA . LEU A 1 809 ? -21.408 34.486 80.725 1.00 87.50 ? 809 LEU A CA 1 ATOM 6278 C C . LEU A 1 809 ? -20.931 35.933 80.727 1.00 91.31 ? 809 LEU A C 1 ATOM 6279 O O . LEU A 1 809 ? -21.728 36.862 80.594 1.00 107.54 ? 809 LEU A O 1 ATOM 6280 C CB . LEU A 1 809 ? -22.232 34.194 79.469 1.00 84.91 ? 809 LEU A CB 1 ATOM 6281 C CG . LEU A 1 809 ? -22.523 32.716 79.194 1.00 87.24 ? 809 LEU A CG 1 ATOM 6282 C CD1 . LEU A 1 809 ? -23.396 32.553 77.959 1.00 99.66 ? 809 LEU A CD1 1 ATOM 6283 C CD2 . LEU A 1 809 ? -21.226 31.936 79.041 1.00 87.00 ? 809 LEU A CD2 1 ATOM 6284 N N . TYR A 1 810 ? -19.624 36.114 80.876 1.00 92.71 ? 810 TYR A N 1 ATOM 6285 C CA . TYR A 1 810 ? -19.036 37.442 80.982 1.00 94.02 ? 810 TYR A CA 1 ATOM 6286 C C . TYR A 1 810 ? -18.607 37.931 79.606 1.00 91.19 ? 810 TYR A C 1 ATOM 6287 O O . TYR A 1 810 ? -17.648 37.420 79.029 1.00 90.88 ? 810 TYR A O 1 ATOM 6288 C CB . TYR A 1 810 ? -17.846 37.408 81.945 1.00 98.86 ? 810 TYR A CB 1 ATOM 6289 C CG . TYR A 1 810 ? -17.107 38.717 82.114 1.00 103.08 ? 810 TYR A CG 1 ATOM 6290 C CD1 . TYR A 1 810 ? -17.462 39.614 83.113 1.00 107.63 ? 810 TYR A CD1 1 ATOM 6291 C CD2 . TYR A 1 810 ? -16.035 39.042 81.293 1.00 103.69 ? 810 TYR A CD2 1 ATOM 6292 C CE1 . TYR A 1 810 ? -16.781 40.804 83.278 1.00 112.23 ? 810 TYR A CE1 1 ATOM 6293 C CE2 . TYR A 1 810 ? -15.351 40.229 81.449 1.00 108.61 ? 810 TYR A CE2 1 ATOM 6294 C CZ . TYR A 1 810 ? -15.726 41.106 82.442 1.00 112.66 ? 810 TYR A CZ 1 ATOM 6295 O OH . TYR A 1 810 ? -15.040 42.287 82.595 1.00 117.53 ? 810 TYR A OH 1 ATOM 6296 N N . ILE A 1 811 ? -19.311 38.934 79.091 1.00 89.97 ? 811 ILE A N 1 ATOM 6297 C CA . ILE A 1 811 ? -19.053 39.427 77.745 1.00 88.37 ? 811 ILE A CA 1 ATOM 6298 C C . ILE A 1 811 ? -17.758 40.227 77.687 1.00 93.91 ? 811 ILE A C 1 ATOM 6299 O O . ILE A 1 811 ? -17.572 41.190 78.432 1.00 99.66 ? 811 ILE A O 1 ATOM 6300 C CB . ILE A 1 811 ? -20.217 40.299 77.228 1.00 87.38 ? 811 ILE A CB 1 ATOM 6301 C CG1 . ILE A 1 811 ? -21.516 39.490 77.190 1.00 80.12 ? 811 ILE A CG1 1 ATOM 6302 C CG2 . ILE A 1 811 ? -19.897 40.854 75.848 1.00 82.46 ? 811 ILE A CG2 1 ATOM 6303 C CD1 . ILE A 1 811 ? -22.705 40.267 76.663 1.00 78.32 ? 811 ILE A CD1 1 ATOM 6304 N N . LEU A 1 812 ? -16.867 39.813 76.794 1.00 92.71 ? 812 LEU A N 1 ATOM 6305 C CA . LEU A 1 812 ? -15.583 40.472 76.611 1.00 98.40 ? 812 LEU A CA 1 ATOM 6306 C C . LEU A 1 812 ? -15.697 41.595 75.591 1.00 99.06 ? 812 LEU A C 1 ATOM 6307 O O . LEU A 1 812 ? -15.511 42.770 75.910 1.00 104.10 ? 812 LEU A O 1 ATOM 6308 C CB . LEU A 1 812 ? -14.529 39.461 76.162 1.00 114.01 ? 812 LEU A CB 1 ATOM 6309 C CG . LEU A 1 812 ? -13.279 39.327 77.029 1.00 108.73 ? 812 LEU A CG 1 ATOM 6310 C CD1 . LEU A 1 812 ? -13.665 39.187 78.489 1.00 113.25 ? 812 LEU A CD1 1 ATOM 6311 C CD2 . LEU A 1 812 ? -12.462 38.135 76.576 1.00 102.61 ? 812 LEU A CD2 1 ATOM 6312 N N . HIS A 1 813 ? -16.002 41.213 74.357 1.00 94.75 ? 813 HIS A N 1 ATOM 6313 C CA . HIS A 1 813 ? -16.101 42.151 73.251 1.00 96.08 ? 813 HIS A CA 1 ATOM 6314 C C . HIS A 1 813 ? -17.110 41.629 72.238 1.00 90.27 ? 813 HIS A C 1 ATOM 6315 O O . HIS A 1 813 ? -17.264 40.418 72.084 1.00 105.21 ? 813 HIS A O 1 ATOM 6316 C CB . HIS A 1 813 ? -14.731 42.349 72.600 1.00 110.09 ? 813 HIS A CB 1 ATOM 6317 C CG . HIS A 1 813 ? -14.713 43.382 71.519 1.00 126.92 ? 813 HIS A CG 1 ATOM 6318 N ND1 . HIS A 1 813 ? -14.969 44.716 71.759 1.00 140.26 ? 813 HIS A ND1 1 ATOM 6319 C CD2 . HIS A 1 813 ? -14.462 43.280 70.193 1.00 123.77 ? 813 HIS A CD2 1 ATOM 6320 C CE1 . HIS A 1 813 ? -14.880 45.389 70.626 1.00 145.48 ? 813 HIS A CE1 1 ATOM 6321 N NE2 . HIS A 1 813 ? -14.574 44.542 69.660 1.00 139.81 ? 813 HIS A NE2 1 ATOM 6322 N N . TYR A 1 814 ? -17.807 42.530 71.553 1.00 88.80 ? 814 TYR A N 1 ATOM 6323 C CA . TYR A 1 814 ? -18.733 42.100 70.513 1.00 83.29 ? 814 TYR A CA 1 ATOM 6324 C C . TYR A 1 814 ? -18.507 42.869 69.214 1.00 84.62 ? 814 TYR A C 1 ATOM 6325 O O . TYR A 1 814 ? -18.342 44.090 69.217 1.00 90.81 ? 814 TYR A O 1 ATOM 6326 C CB . TYR A 1 814 ? -20.189 42.236 70.984 1.00 76.98 ? 814 TYR A CB 1 ATOM 6327 C CG . TYR A 1 814 ? -20.711 43.652 71.105 1.00 89.95 ? 814 TYR A CG 1 ATOM 6328 C CD1 . TYR A 1 814 ? -20.533 44.383 72.273 1.00 104.07 ? 814 TYR A CD1 1 ATOM 6329 C CD2 . TYR A 1 814 ? -21.408 44.247 70.061 1.00 89.85 ? 814 TYR A CD2 1 ATOM 6330 C CE1 . TYR A 1 814 ? -21.019 45.674 72.390 1.00 97.51 ? 814 TYR A CE1 1 ATOM 6331 C CE2 . TYR A 1 814 ? -21.895 45.536 70.168 1.00 75.81 ? 814 TYR A CE2 1 ATOM 6332 C CZ . TYR A 1 814 ? -21.700 46.244 71.334 1.00 79.35 ? 814 TYR A CZ 1 ATOM 6333 O OH . TYR A 1 814 ? -22.186 47.528 71.444 1.00 78.88 ? 814 TYR A OH 1 ATOM 6334 N N . ASP A 1 815 ? -18.493 42.135 68.105 1.00 82.00 ? 815 ASP A N 1 ATOM 6335 C CA . ASP A 1 815 ? -18.206 42.709 66.796 1.00 86.03 ? 815 ASP A CA 1 ATOM 6336 C C . ASP A 1 815 ? -19.410 42.613 65.867 1.00 80.30 ? 815 ASP A C 1 ATOM 6337 O O . ASP A 1 815 ? -20.265 41.742 66.027 1.00 74.19 ? 815 ASP A O 1 ATOM 6338 C CB . ASP A 1 815 ? -16.998 42.015 66.164 1.00 91.01 ? 815 ASP A CB 1 ATOM 6339 C CG . ASP A 1 815 ? -15.715 42.268 66.929 1.00 105.27 ? 815 ASP A CG 1 ATOM 6340 O OD1 . ASP A 1 815 ? -14.954 41.304 67.158 1.00 117.67 ? 815 ASP A OD1 1 ATOM 6341 O OD2 . ASP A 1 815 ? -15.466 43.434 67.300 1.00 105.93 ? 815 ASP A OD2 1 ATOM 6342 N N . ILE A 1 816 ? -19.465 43.515 64.892 1.00 82.03 ? 816 ILE A N 1 ATOM 6343 C CA . ILE A 1 816 ? -20.613 43.613 63.999 1.00 78.20 ? 816 ILE A CA 1 ATOM 6344 C C . ILE A 1 816 ? -20.214 43.545 62.528 1.00 82.45 ? 816 ILE A C 1 ATOM 6345 O O . ILE A 1 816 ? -19.300 44.245 62.090 1.00 90.36 ? 816 ILE A O 1 ATOM 6346 C CB . ILE A 1 816 ? -21.389 44.923 64.241 1.00 77.71 ? 816 ILE A CB 1 ATOM 6347 C CG1 . ILE A 1 816 ? -21.809 45.033 65.707 1.00 76.84 ? 816 ILE A CG1 1 ATOM 6348 C CG2 . ILE A 1 816 ? -22.598 45.009 63.323 1.00 74.15 ? 816 ILE A CG2 1 ATOM 6349 C CD1 . ILE A 1 816 ? -22.299 46.405 66.092 1.00 85.65 ? 816 ILE A CD1 1 ATOM 6350 N N . ASP A 1 817 ? -20.903 42.695 61.773 1.00 79.17 ? 817 ASP A N 1 ATOM 6351 C CA . ASP A 1 817 ? -20.729 42.638 60.327 1.00 85.96 ? 817 ASP A CA 1 ATOM 6352 C C . ASP A 1 817 ? -22.018 43.048 59.621 1.00 83.47 ? 817 ASP A C 1 ATOM 6353 O O . ASP A 1 817 ? -23.080 42.478 59.869 1.00 96.46 ? 817 ASP A O 1 ATOM 6354 C CB . ASP A 1 817 ? -20.303 41.238 59.883 1.00 114.21 ? 817 ASP A CB 1 ATOM 6355 C CG . ASP A 1 817 ? -18.823 41.154 59.564 1.00 133.91 ? 817 ASP A CG 1 ATOM 6356 O OD1 . ASP A 1 817 ? -18.241 42.187 59.169 1.00 144.51 ? 817 ASP A OD1 1 ATOM 6357 O OD2 . ASP A 1 817 ? -18.242 40.058 59.706 1.00 123.33 ? 817 ASP A OD2 1 ATOM 6358 N N . GLY A 1 818 ? -21.916 44.036 58.740 1.00 86.66 ? 818 GLY A N 1 ATOM 6359 C CA . GLY A 1 818 ? -23.071 44.536 58.021 1.00 84.08 ? 818 GLY A CA 1 ATOM 6360 C C . GLY A 1 818 ? -23.544 45.885 58.529 1.00 83.86 ? 818 GLY A C 1 ATOM 6361 O O . GLY A 1 818 ? -22.935 46.462 59.430 1.00 84.62 ? 818 GLY A O 1 ATOM 6362 N N . PRO A 1 819 ? -24.642 46.394 57.951 1.00 88.09 ? 819 PRO A N 1 ATOM 6363 C CA . PRO A 1 819 ? -25.188 47.717 58.273 1.00 80.44 ? 819 PRO A CA 1 ATOM 6364 C C . PRO A 1 819 ? -25.940 47.741 59.600 1.00 73.59 ? 819 PRO A C 1 ATOM 6365 O O . PRO A 1 819 ? -27.166 47.855 59.608 1.00 70.62 ? 819 PRO A O 1 ATOM 6366 C CB . PRO A 1 819 ? -26.139 47.987 57.108 1.00 80.15 ? 819 PRO A CB 1 ATOM 6367 C CG . PRO A 1 819 ? -26.603 46.631 56.702 1.00 78.01 ? 819 PRO A CG 1 ATOM 6368 C CD . PRO A 1 819 ? -25.434 45.706 56.915 1.00 85.48 ? 819 PRO A CD 1 ATOM 6369 N N . MET A 1 820 ? -25.214 47.634 60.707 1.00 73.10 ? 820 MET A N 1 ATOM 6370 C CA . MET A 1 820 ? -25.846 47.595 62.020 1.00 68.84 ? 820 MET A CA 1 ATOM 6371 C C . MET A 1 820 ? -25.023 48.314 63.089 1.00 71.25 ? 820 MET A C 1 ATOM 6372 O O . MET A 1 820 ? -23.807 48.143 63.172 1.00 99.78 ? 820 MET A O 1 ATOM 6373 C CB . MET A 1 820 ? -26.091 46.140 62.432 1.00 75.50 ? 820 MET A CB 1 ATOM 6374 C CG . MET A 1 820 ? -26.799 45.961 63.763 1.00 78.27 ? 820 MET A CG 1 ATOM 6375 S SD . MET A 1 820 ? -27.359 44.262 64.005 1.00 102.03 ? 820 MET A SD 1 ATOM 6376 C CE . MET A 1 820 ? -25.854 43.347 63.684 1.00 60.25 ? 820 MET A CE 1 ATOM 6377 N N . ASN A 1 821 ? -25.700 49.125 63.897 1.00 69.41 ? 821 ASN A N 1 ATOM 6378 C CA . ASN A 1 821 ? -25.100 49.714 65.089 1.00 71.18 ? 821 ASN A CA 1 ATOM 6379 C C . ASN A 1 821 ? -25.703 49.062 66.325 1.00 68.25 ? 821 ASN A C 1 ATOM 6380 O O . ASN A 1 821 ? -26.883 48.724 66.327 1.00 75.79 ? 821 ASN A O 1 ATOM 6381 C CB . ASN A 1 821 ? -25.319 51.227 65.133 1.00 74.48 ? 821 ASN A CB 1 ATOM 6382 C CG . ASN A 1 821 ? -24.607 51.960 64.013 1.00 99.80 ? 821 ASN A CG 1 ATOM 6383 O OD1 . ASN A 1 821 ? -23.614 51.478 63.469 1.00 114.64 ? 821 ASN A OD1 1 ATOM 6384 N ND2 . ASN A 1 821 ? -25.113 53.140 63.667 1.00 134.69 ? 821 ASN A ND2 1 ATOM 6385 N N . CYS A 1 822 ? -24.906 48.885 67.374 1.00 77.59 ? 822 CYS A N 1 ATOM 6386 C CA . CYS A 1 822 ? -25.394 48.212 68.575 1.00 80.51 ? 822 CYS A CA 1 ATOM 6387 C C . CYS A 1 822 ? -24.978 48.915 69.864 1.00 90.27 ? 822 CYS A C 1 ATOM 6388 O O . CYS A 1 822 ? -23.978 49.632 69.905 1.00 102.24 ? 822 CYS A O 1 ATOM 6389 C CB . CYS A 1 822 ? -24.911 46.760 68.601 1.00 66.16 ? 822 CYS A CB 1 ATOM 6390 S SG . CYS A 1 822 ? -25.613 45.722 67.299 1.00 154.91 ? 822 CYS A SG 1 ATOM 6391 N N . THR A 1 823 ? -25.761 48.693 70.916 1.00 83.71 ? 823 THR A N 1 ATOM 6392 C CA . THR A 1 823 ? -25.526 49.319 72.211 1.00 91.75 ? 823 THR A CA 1 ATOM 6393 C C . THR A 1 823 ? -25.917 48.362 73.335 1.00 84.28 ? 823 THR A C 1 ATOM 6394 O O . THR A 1 823 ? -26.892 47.621 73.217 1.00 90.91 ? 823 THR A O 1 ATOM 6395 C CB . THR A 1 823 ? -26.319 50.638 72.350 1.00 71.20 ? 823 THR A CB 1 ATOM 6396 O OG1 . THR A 1 823 ? -26.062 51.477 71.218 1.00 78.38 ? 823 THR A OG1 1 ATOM 6397 C CG2 . THR A 1 823 ? -25.929 51.381 73.621 1.00 74.69 ? 823 THR A CG2 1 ATOM 6398 N N . SER A 1 824 ? -25.150 48.376 74.420 1.00 74.09 ? 824 SER A N 1 ATOM 6399 C CA . SER A 1 824 ? -25.445 47.539 75.576 1.00 74.22 ? 824 SER A CA 1 ATOM 6400 C C . SER A 1 824 ? -25.944 48.382 76.747 1.00 77.58 ? 824 SER A C 1 ATOM 6401 O O . SER A 1 824 ? -25.403 49.452 77.027 1.00 93.73 ? 824 SER A O 1 ATOM 6402 C CB . SER A 1 824 ? -24.207 46.738 75.986 1.00 77.52 ? 824 SER A CB 1 ATOM 6403 O OG . SER A 1 824 ? -24.421 46.056 77.208 1.00 83.29 ? 824 SER A OG 1 ATOM 6404 N N . ASP A 1 825 ? -26.979 47.897 77.429 1.00 76.25 ? 825 ASP A N 1 ATOM 6405 C CA . ASP A 1 825 ? -27.547 48.613 78.569 1.00 79.15 ? 825 ASP A CA 1 ATOM 6406 C C . ASP A 1 825 ? -26.604 48.565 79.768 1.00 99.22 ? 825 ASP A C 1 ATOM 6407 O O . ASP A 1 825 ? -26.761 49.320 80.727 1.00 106.42 ? 825 ASP A O 1 ATOM 6408 C CB . ASP A 1 825 ? -28.914 48.037 78.943 1.00 78.32 ? 825 ASP A CB 1 ATOM 6409 C CG . ASP A 1 825 ? -28.836 46.592 79.398 1.00 111.35 ? 825 ASP A CG 1 ATOM 6410 O OD1 . ASP A 1 825 ? -27.869 45.897 79.024 1.00 119.19 ? 825 ASP A OD1 1 ATOM 6411 O OD2 . ASP A 1 825 ? -29.749 46.150 80.129 1.00 106.20 ? 825 ASP A OD2 1 ATOM 6412 N N . MET A 1 826 ? -25.630 47.664 79.707 1.00 101.90 ? 826 MET A N 1 ATOM 6413 C CA . MET A 1 826 ? -24.580 47.591 80.714 1.00 92.18 ? 826 MET A CA 1 ATOM 6414 C C . MET A 1 826 ? -23.219 47.742 80.046 1.00 94.59 ? 826 MET A C 1 ATOM 6415 O O . MET A 1 826 ? -23.082 47.513 78.845 1.00 100.16 ? 826 MET A O 1 ATOM 6416 C CB . MET A 1 826 ? -24.649 46.271 81.484 1.00 94.03 ? 826 MET A CB 1 ATOM 6417 C CG . MET A 1 826 ? -25.962 46.038 82.213 1.00 97.21 ? 826 MET A CG 1 ATOM 6418 S SD . MET A 1 826 ? -25.965 44.490 83.139 1.00 108.79 ? 826 MET A SD 1 ATOM 6419 C CE . MET A 1 826 ? -27.620 44.504 83.822 1.00 103.47 ? 826 MET A CE 1 ATOM 6420 N N . GLU A 1 827 ? -22.214 48.126 80.825 1.00 100.91 ? 827 GLU A N 1 ATOM 6421 C CA . GLU A 1 827 ? -20.866 48.283 80.295 1.00 105.46 ? 827 GLU A CA 1 ATOM 6422 C C . GLU A 1 827 ? -20.221 46.923 80.066 1.00 106.02 ? 827 GLU A C 1 ATOM 6423 O O . GLU A 1 827 ? -20.110 46.119 80.991 1.00 109.19 ? 827 GLU A O 1 ATOM 6424 C CB . GLU A 1 827 ? -20.004 49.117 81.243 1.00 117.29 ? 827 GLU A CB 1 ATOM 6425 C CG . GLU A 1 827 ? -18.537 49.177 80.848 1.00 127.21 ? 827 GLU A CG 1 ATOM 6426 C CD . GLU A 1 827 ? -17.661 49.773 81.934 1.00 137.13 ? 827 GLU A CD 1 ATOM 6427 O OE1 . GLU A 1 827 ? -18.208 50.217 82.966 1.00 139.19 ? 827 GLU A OE1 1 ATOM 6428 O OE2 . GLU A 1 827 ? -16.425 49.792 81.757 1.00 142.78 ? 827 GLU A OE2 1 ATOM 6429 N N . ILE A 1 828 ? -19.797 46.666 78.834 1.00 105.08 ? 828 ILE A N 1 ATOM 6430 C CA . ILE A 1 828 ? -19.141 45.404 78.517 1.00 110.71 ? 828 ILE A CA 1 ATOM 6431 C C . ILE A 1 828 ? -17.692 45.437 78.988 1.00 117.16 ? 828 ILE A C 1 ATOM 6432 O O . ILE A 1 828 ? -17.012 46.459 78.868 1.00 118.82 ? 828 ILE A O 1 ATOM 6433 C CB . ILE A 1 828 ? -19.205 45.086 77.004 1.00 97.73 ? 828 ILE A CB 1 ATOM 6434 C CG1 . ILE A 1 828 ? -18.625 46.234 76.175 1.00 127.52 ? 828 ILE A CG1 1 ATOM 6435 C CG2 . ILE A 1 828 ? -20.638 44.804 76.582 1.00 88.47 ? 828 ILE A CG2 1 ATOM 6436 C CD1 . ILE A 1 828 ? -17.244 45.955 75.619 1.00 136.50 ? 828 ILE A CD1 1 ATOM 6437 N N . ASN A 1 829 ? -17.239 44.316 79.543 1.00 114.43 ? 829 ASN A N 1 ATOM 6438 C CA . ASN A 1 829 ? -15.877 44.180 80.055 1.00 118.66 ? 829 ASN A CA 1 ATOM 6439 C C . ASN A 1 829 ? -15.497 45.249 81.086 1.00 125.21 ? 829 ASN A C 1 ATOM 6440 O O . ASN A 1 829 ? -14.543 45.996 80.874 1.00 148.52 ? 829 ASN A O 1 ATOM 6441 C CB . ASN A 1 829 ? -14.885 44.214 78.887 1.00 118.22 ? 829 ASN A CB 1 ATOM 6442 C CG . ASN A 1 829 ? -13.670 43.346 79.124 1.00 118.97 ? 829 ASN A CG 1 ATOM 6443 O OD1 . ASN A 1 829 ? -13.720 42.387 79.891 1.00 119.68 ? 829 ASN A OD1 1 ATOM 6444 N ND2 . ASN A 1 829 ? -12.571 43.673 78.455 1.00 121.87 ? 829 ASN A ND2 1 ATOM 6445 N N . PRO A 1 830 ? -16.237 45.325 82.209 1.00 124.14 ? 830 PRO A N 1 ATOM 6446 C CA . PRO A 1 830 ? -15.980 46.371 83.208 1.00 127.36 ? 830 PRO A CA 1 ATOM 6447 C C . PRO A 1 830 ? -14.659 46.189 83.959 1.00 133.02 ? 830 PRO A C 1 ATOM 6448 O O . PRO A 1 830 ? -14.073 47.169 84.422 1.00 143.86 ? 830 PRO A O 1 ATOM 6449 C CB . PRO A 1 830 ? -17.166 46.232 84.166 1.00 126.06 ? 830 PRO A CB 1 ATOM 6450 C CG . PRO A 1 830 ? -17.563 44.807 84.060 1.00 123.77 ? 830 PRO A CG 1 ATOM 6451 C CD . PRO A 1 830 ? -17.337 44.433 82.624 1.00 121.28 ? 830 PRO A CD 1 ATOM 6452 N N . LEU A 1 831 ? -14.209 44.946 84.082 1.00 128.65 ? 831 LEU A N 1 ATOM 6453 C CA . LEU A 1 831 ? -12.955 44.627 84.759 1.00 130.48 ? 831 LEU A CA 1 ATOM 6454 C C . LEU A 1 831 ? -11.815 44.620 83.746 1.00 132.04 ? 831 LEU A C 1 ATOM 6455 O O . LEU A 1 831 ? -10.675 44.276 84.061 1.00 133.33 ? 831 LEU A O 1 ATOM 6456 C CB . LEU A 1 831 ? -13.057 43.272 85.460 1.00 127.98 ? 831 LEU A CB 1 ATOM 6457 C CG . LEU A 1 831 ? -14.411 42.960 86.108 1.00 126.11 ? 831 LEU A CG 1 ATOM 6458 C CD1 . LEU A 1 831 ? -14.450 41.528 86.619 1.00 130.14 ? 831 LEU A CD1 1 ATOM 6459 C CD2 . LEU A 1 831 ? -14.721 43.940 87.230 1.00 133.69 ? 831 LEU A CD2 1 ATOM 6460 N N . ARG A 1 832 ? -12.163 45.011 82.525 1.00 138.99 ? 832 ARG A N 1 ATOM 6461 C CA . ARG A 1 832 ? -11.354 44.823 81.326 1.00 150.75 ? 832 ARG A CA 1 ATOM 6462 C C . ARG A 1 832 ? -10.936 43.362 81.168 1.00 153.72 ? 832 ARG A C 1 ATOM 6463 O O . ARG A 1 832 ? -11.643 42.461 81.622 1.00 164.77 ? 832 ARG A O 1 ATOM 6464 C CB . ARG A 1 832 ? -10.112 45.719 81.366 1.00 142.34 ? 832 ARG A CB 1 ATOM 6465 C CG . ARG A 1 832 ? -10.393 47.209 81.530 1.00 142.05 ? 832 ARG A CG 1 ATOM 6466 C CD . ARG A 1 832 ? -10.964 47.823 80.261 1.00 149.83 ? 832 ARG A CD 1 ATOM 6467 N NE . ARG A 1 832 ? -12.421 47.750 80.214 1.00 166.58 ? 832 ARG A NE 1 ATOM 6468 C CZ . ARG A 1 832 ? -13.155 48.157 79.183 1.00 167.01 ? 832 ARG A CZ 1 ATOM 6469 N NH1 . ARG A 1 832 ? -12.567 48.664 78.108 1.00 168.64 ? 832 ARG A NH1 1 ATOM 6470 N NH2 . ARG A 1 832 ? -14.477 48.056 79.226 1.00 159.55 ? 832 ARG A NH2 1 ATOM 6471 N N . ILE A 1 833 ? -9.754 43.153 80.592 1.00 132.03 ? 833 ILE A N 1 ATOM 6472 C CA . ILE A 1 833 ? -9.206 41.823 80.315 1.00 128.33 ? 833 ILE A CA 1 ATOM 6473 C C . ILE A 1 833 ? -7.945 41.994 79.471 1.00 135.83 ? 833 ILE A C 1 ATOM 6474 O O . ILE A 1 833 ? -7.685 43.086 78.966 1.00 155.76 ? 833 ILE A O 1 ATOM 6475 C CB . ILE A 1 833 ? -10.220 40.903 79.576 1.00 122.23 ? 833 ILE A CB 1 ATOM 6476 C CG1 . ILE A 1 833 ? -10.124 39.468 80.104 1.00 126.46 ? 833 ILE A CG1 1 ATOM 6477 C CG2 . ILE A 1 833 ? -10.055 40.983 78.058 1.00 126.55 ? 833 ILE A CG2 1 ATOM 6478 C CD1 . ILE A 1 833 ? -10.517 39.333 81.563 1.00 117.87 ? 833 ILE A CD1 1 ATOM 6479 N N . LYS A 1 834 ? -7.158 40.933 79.318 1.00 133.18 ? 834 LYS A N 1 ATOM 6480 C CA . LYS A 1 834 ? -6.068 40.966 78.347 1.00 147.49 ? 834 LYS A CA 1 ATOM 6481 C C . LYS A 1 834 ? -6.184 39.836 77.325 1.00 143.65 ? 834 LYS A C 1 ATOM 6482 O O . LYS A 1 834 ? -6.606 40.060 76.190 1.00 138.20 ? 834 LYS A O 1 ATOM 6483 C CB . LYS A 1 834 ? -4.714 40.899 79.055 1.00 160.03 ? 834 LYS A CB 1 ATOM 6484 C CG . LYS A 1 834 ? -3.858 42.149 78.884 1.00 162.87 ? 834 LYS A CG 1 ATOM 6485 C CD . LYS A 1 834 ? -3.512 42.397 77.420 1.00 165.91 ? 834 LYS A CD 1 ATOM 6486 C CE . LYS A 1 834 ? -4.218 43.632 76.875 1.00 162.03 ? 834 LYS A CE 1 ATOM 6487 N NZ . LYS A 1 834 ? -3.920 43.849 75.433 1.00 153.52 ? 834 LYS A NZ 1 ATOM 6488 N N . ILE A 1 835 ? -5.833 38.623 77.742 1.00 151.09 ? 835 ILE A N 1 ATOM 6489 C CA . ILE A 1 835 ? -5.876 37.454 76.864 1.00 147.69 ? 835 ILE A CA 1 ATOM 6490 C C . ILE A 1 835 ? -6.086 36.172 77.666 1.00 146.16 ? 835 ILE A C 1 ATOM 6491 O O . ILE A 1 835 ? -5.246 35.273 77.650 1.00 139.62 ? 835 ILE A O 1 ATOM 6492 C CB . ILE A 1 835 ? -4.584 37.310 76.027 1.00 154.30 ? 835 ILE A CB 1 ATOM 6493 C CG1 . ILE A 1 835 ? -3.369 37.793 76.824 1.00 149.56 ? 835 ILE A CG1 1 ATOM 6494 C CG2 . ILE A 1 835 ? -4.700 38.069 74.711 1.00 146.15 ? 835 ILE A CG2 1 ATOM 6495 C CD1 . ILE A 1 835 ? -2.058 37.654 76.080 1.00 139.42 ? 835 ILE A CD1 1 ATOM 6496 N N . ASP A 1 868 ? -32.906 17.755 87.085 1.00 173.42 ? 868 ASP A N 1 ATOM 6497 C CA . ASP A 1 868 ? -31.473 17.648 86.840 1.00 169.34 ? 868 ASP A CA 1 ATOM 6498 C C . ASP A 1 868 ? -30.963 18.805 85.981 1.00 159.11 ? 868 ASP A C 1 ATOM 6499 O O . ASP A 1 868 ? -30.199 19.646 86.453 1.00 157.90 ? 868 ASP A O 1 ATOM 6500 C CB . ASP A 1 868 ? -31.144 16.307 86.177 1.00 167.98 ? 868 ASP A CB 1 ATOM 6501 C CG . ASP A 1 868 ? -32.185 15.889 85.154 1.00 166.09 ? 868 ASP A CG 1 ATOM 6502 O OD1 . ASP A 1 868 ? -32.372 14.669 84.961 1.00 167.39 ? 868 ASP A OD1 1 ATOM 6503 O OD2 . ASP A 1 868 ? -32.816 16.779 84.547 1.00 150.76 ? 868 ASP A OD2 1 ATOM 6504 N N . ILE A 1 869 ? -31.391 18.845 84.723 1.00 150.48 ? 869 ILE A N 1 ATOM 6505 C CA . ILE A 1 869 ? -30.987 19.916 83.820 1.00 139.67 ? 869 ILE A CA 1 ATOM 6506 C C . ILE A 1 869 ? -31.855 21.154 84.040 1.00 139.34 ? 869 ILE A C 1 ATOM 6507 O O . ILE A 1 869 ? -33.085 21.077 84.039 1.00 141.93 ? 869 ILE A O 1 ATOM 6508 C CB . ILE A 1 869 ? -31.053 19.466 82.339 1.00 131.89 ? 869 ILE A CB 1 ATOM 6509 C CG1 . ILE A 1 869 ? -30.763 20.641 81.403 1.00 107.64 ? 869 ILE A CG1 1 ATOM 6510 C CG2 . ILE A 1 869 ? -32.398 18.822 82.018 1.00 145.68 ? 869 ILE A CG2 1 ATOM 6511 C CD1 . ILE A 1 869 ? -29.352 21.178 81.515 1.00 102.71 ? 869 ILE A CD1 1 ATOM 6512 N N . HIS A 1 870 ? -31.205 22.295 84.248 1.00 131.29 ? 870 HIS A N 1 ATOM 6513 C CA . HIS A 1 870 ? -31.916 23.530 84.550 1.00 127.53 ? 870 HIS A CA 1 ATOM 6514 C C . HIS A 1 870 ? -31.548 24.639 83.570 1.00 119.51 ? 870 HIS A C 1 ATOM 6515 O O . HIS A 1 870 ? -30.371 24.934 83.360 1.00 106.55 ? 870 HIS A O 1 ATOM 6516 C CB . HIS A 1 870 ? -31.623 23.975 85.984 1.00 140.74 ? 870 HIS A CB 1 ATOM 6517 C CG . HIS A 1 870 ? -32.640 24.918 86.545 1.00 155.66 ? 870 HIS A CG 1 ATOM 6518 N ND1 . HIS A 1 870 ? -32.540 25.456 87.810 1.00 159.75 ? 870 HIS A ND1 1 ATOM 6519 C CD2 . HIS A 1 870 ? -33.784 25.415 86.015 1.00 155.48 ? 870 HIS A CD2 1 ATOM 6520 C CE1 . HIS A 1 870 ? -33.575 26.247 88.034 1.00 160.49 ? 870 HIS A CE1 1 ATOM 6521 N NE2 . HIS A 1 870 ? -34.345 26.238 86.961 1.00 160.91 ? 870 HIS A NE2 1 ATOM 6522 N N . THR A 1 871 ? -32.564 25.248 82.971 1.00 125.94 ? 871 THR A N 1 ATOM 6523 C CA . THR A 1 871 ? -32.355 26.329 82.018 1.00 108.13 ? 871 THR A CA 1 ATOM 6524 C C . THR A 1 871 ? -32.276 27.674 82.725 1.00 106.65 ? 871 THR A C 1 ATOM 6525 O O . THR A 1 871 ? -33.121 27.994 83.560 1.00 111.14 ? 871 THR A O 1 ATOM 6526 C CB . THR A 1 871 ? -33.484 26.380 80.968 1.00 105.89 ? 871 THR A CB 1 ATOM 6527 O OG1 . THR A 1 871 ? -33.572 25.118 80.294 1.00 121.54 ? 871 THR A OG1 1 ATOM 6528 C CG2 . THR A 1 871 ? -33.223 27.479 79.948 1.00 100.19 ? 871 THR A CG2 1 ATOM 6529 N N . LEU A 1 872 ? -31.255 28.459 82.396 1.00 103.24 ? 872 LEU A N 1 ATOM 6530 C CA . LEU A 1 872 ? -31.169 29.820 82.903 1.00 103.38 ? 872 LEU A CA 1 ATOM 6531 C C . LEU A 1 872 ? -31.344 30.805 81.755 1.00 100.48 ? 872 LEU A C 1 ATOM 6532 O O . LEU A 1 872 ? -30.457 30.971 80.918 1.00 94.30 ? 872 LEU A O 1 ATOM 6533 C CB . LEU A 1 872 ? -29.835 30.052 83.614 1.00 102.11 ? 872 LEU A CB 1 ATOM 6534 C CG . LEU A 1 872 ? -29.539 29.139 84.807 1.00 106.29 ? 872 LEU A CG 1 ATOM 6535 C CD1 . LEU A 1 872 ? -28.180 29.460 85.411 1.00 104.76 ? 872 LEU A CD1 1 ATOM 6536 C CD2 . LEU A 1 872 ? -30.635 29.247 85.859 1.00 117.20 ? 872 LEU A CD2 1 ATOM 6537 N N . GLY A 1 873 ? -32.502 31.455 81.724 1.00 108.94 ? 873 GLY A N 1 ATOM 6538 C CA . GLY A 1 873 ? -32.807 32.434 80.700 1.00 99.97 ? 873 GLY A CA 1 ATOM 6539 C C . GLY A 1 873 ? -32.767 33.834 81.270 1.00 109.11 ? 873 GLY A C 1 ATOM 6540 O O . GLY A 1 873 ? -32.445 34.025 82.441 1.00 107.88 ? 873 GLY A O 1 ATOM 6541 N N . CYS A 1 874 ? -33.106 34.816 80.445 1.00 125.54 ? 874 CYS A N 1 ATOM 6542 C CA . CYS A 1 874 ? -33.134 36.199 80.895 1.00 105.11 ? 874 CYS A CA 1 ATOM 6543 C C . CYS A 1 874 ? -34.326 36.438 81.818 1.00 105.78 ? 874 CYS A C 1 ATOM 6544 O O . CYS A 1 874 ? -34.404 37.460 82.496 1.00 122.66 ? 874 CYS A O 1 ATOM 6545 C CB . CYS A 1 874 ? -33.181 37.152 79.701 1.00 89.81 ? 874 CYS A CB 1 ATOM 6546 S SG . CYS A 1 874 ? -32.185 38.643 79.911 1.00 180.92 ? 874 CYS A SG 1 ATOM 6547 N N . GLY A 1 875 ? -35.254 35.486 81.836 1.00 107.98 ? 875 GLY A N 1 ATOM 6548 C CA . GLY A 1 875 ? -36.410 35.562 82.709 1.00 115.27 ? 875 GLY A CA 1 ATOM 6549 C C . GLY A 1 875 ? -36.091 35.233 84.156 1.00 120.46 ? 875 GLY A C 1 ATOM 6550 O O . GLY A 1 875 ? -36.504 35.946 85.071 1.00 125.05 ? 875 GLY A O 1 ATOM 6551 N N . VAL A 1 876 ? -35.354 34.146 84.364 1.00 122.88 ? 876 VAL A N 1 ATOM 6552 C CA . VAL A 1 876 ? -35.024 33.695 85.712 1.00 125.56 ? 876 VAL A CA 1 ATOM 6553 C C . VAL A 1 876 ? -33.697 34.284 86.194 1.00 126.60 ? 876 VAL A C 1 ATOM 6554 O O . VAL A 1 876 ? -33.351 34.178 87.370 1.00 123.17 ? 876 VAL A O 1 ATOM 6555 C CB . VAL A 1 876 ? -34.960 32.152 85.783 1.00 122.25 ? 876 VAL A CB 1 ATOM 6556 C CG1 . VAL A 1 876 ? -33.643 31.644 85.214 1.00 117.53 ? 876 VAL A CG1 1 ATOM 6557 C CG2 . VAL A 1 876 ? -35.157 31.668 87.214 1.00 130.96 ? 876 VAL A CG2 1 ATOM 6558 N N . ALA A 1 877 ? -32.963 34.921 85.287 1.00 121.43 ? 877 ALA A N 1 ATOM 6559 C CA . ALA A 1 877 ? -31.661 35.488 85.626 1.00 116.89 ? 877 ALA A CA 1 ATOM 6560 C C . ALA A 1 877 ? -31.585 36.967 85.267 1.00 115.47 ? 877 ALA A C 1 ATOM 6561 O O . ALA A 1 877 ? -32.415 37.472 84.512 1.00 131.17 ? 877 ALA A O 1 ATOM 6562 C CB . ALA A 1 877 ? -30.550 34.719 84.930 1.00 110.99 ? 877 ALA A CB 1 ATOM 6563 N N . GLN A 1 878 ? -30.592 37.658 85.820 1.00 114.62 ? 878 GLN A N 1 ATOM 6564 C CA . GLN A 1 878 ? -30.375 39.067 85.508 1.00 111.23 ? 878 GLN A CA 1 ATOM 6565 C C . GLN A 1 878 ? -30.060 39.237 84.026 1.00 103.91 ? 878 GLN A C 1 ATOM 6566 O O . GLN A 1 878 ? -29.173 38.574 83.490 1.00 101.27 ? 878 GLN A O 1 ATOM 6567 C CB . GLN A 1 878 ? -29.243 39.643 86.362 1.00 120.56 ? 878 GLN A CB 1 ATOM 6568 C CG . GLN A 1 878 ? -28.978 41.120 86.119 1.00 131.47 ? 878 GLN A CG 1 ATOM 6569 C CD . GLN A 1 878 ? -27.854 41.662 86.980 1.00 143.17 ? 878 GLN A CD 1 ATOM 6570 O OE1 . GLN A 1 878 ? -27.248 40.930 87.761 1.00 157.78 ? 878 GLN A OE1 1 ATOM 6571 N NE2 . GLN A 1 878 ? -27.572 42.952 86.841 1.00 140.55 ? 878 GLN A NE2 1 ATOM 6572 N N . CYS A 1 879 ? -30.793 40.128 83.368 1.00 112.20 ? 879 CYS A N 1 ATOM 6573 C CA . CYS A 1 879 ? -30.685 40.276 81.923 1.00 104.20 ? 879 CYS A CA 1 ATOM 6574 C C . CYS A 1 879 ? -29.752 41.410 81.512 1.00 90.89 ? 879 CYS A C 1 ATOM 6575 O O . CYS A 1 879 ? -29.775 42.494 82.094 1.00 100.70 ? 879 CYS A O 1 ATOM 6576 C CB . CYS A 1 879 ? -32.070 40.504 81.313 1.00 106.12 ? 879 CYS A CB 1 ATOM 6577 S SG . CYS A 1 879 ? -32.083 40.631 79.509 1.00 154.92 ? 879 CYS A SG 1 ATOM 6578 N N . LEU A 1 880 ? -28.925 41.141 80.506 1.00 84.77 ? 880 LEU A N 1 ATOM 6579 C CA . LEU A 1 880 ? -28.102 42.171 79.886 1.00 87.50 ? 880 LEU A CA 1 ATOM 6580 C C . LEU A 1 880 ? -28.585 42.381 78.456 1.00 90.48 ? 880 LEU A C 1 ATOM 6581 O O . LEU A 1 880 ? -28.416 41.513 77.600 1.00 92.03 ? 880 LEU A O 1 ATOM 6582 C CB . LEU A 1 880 ? -26.621 41.780 79.916 1.00 84.17 ? 880 LEU A CB 1 ATOM 6583 C CG . LEU A 1 880 ? -25.587 42.830 79.495 1.00 83.17 ? 880 LEU A CG 1 ATOM 6584 C CD1 . LEU A 1 880 ? -24.318 42.677 80.316 1.00 88.83 ? 880 LEU A CD1 1 ATOM 6585 C CD2 . LEU A 1 880 ? -25.266 42.730 78.010 1.00 78.18 ? 880 LEU A CD2 1 ATOM 6586 N N . LYS A 1 881 ? -29.190 43.536 78.200 1.00 76.43 ? 881 LYS A N 1 ATOM 6587 C CA . LYS A 1 881 ? -29.809 43.795 76.906 1.00 75.40 ? 881 LYS A CA 1 ATOM 6588 C C . LYS A 1 881 ? -28.850 44.452 75.923 1.00 82.90 ? 881 LYS A C 1 ATOM 6589 O O . LYS A 1 881 ? -28.161 45.415 76.259 1.00 108.90 ? 881 LYS A O 1 ATOM 6590 C CB . LYS A 1 881 ? -31.048 44.674 77.075 1.00 72.11 ? 881 LYS A CB 1 ATOM 6591 C CG . LYS A 1 881 ? -32.088 44.102 78.018 1.00 84.04 ? 881 LYS A CG 1 ATOM 6592 C CD . LYS A 1 881 ? -33.263 45.048 78.177 1.00 78.56 ? 881 LYS A CD 1 ATOM 6593 C CE . LYS A 1 881 ? -34.164 44.604 79.314 1.00 113.91 ? 881 LYS A CE 1 ATOM 6594 N NZ . LYS A 1 881 ? -33.427 44.529 80.606 1.00 128.59 ? 881 LYS A NZ 1 ATOM 6595 N N . ILE A 1 882 ? -28.813 43.920 74.707 1.00 66.86 ? 882 ILE A N 1 ATOM 6596 C CA . ILE A 1 882 ? -28.056 44.533 73.627 1.00 65.28 ? 882 ILE A CA 1 ATOM 6597 C C . ILE A 1 882 ? -29.006 44.911 72.500 1.00 70.08 ? 882 ILE A C 1 ATOM 6598 O O . ILE A 1 882 ? -29.574 44.046 71.833 1.00 91.06 ? 882 ILE A O 1 ATOM 6599 C CB . ILE A 1 882 ? -26.957 43.596 73.092 1.00 71.02 ? 882 ILE A CB 1 ATOM 6600 C CG1 . ILE A 1 882 ? -25.946 43.280 74.196 1.00 78.12 ? 882 ILE A CG1 1 ATOM 6601 C CG2 . ILE A 1 882 ? -26.258 44.221 71.895 1.00 67.83 ? 882 ILE A CG2 1 ATOM 6602 C CD1 . ILE A 1 882 ? -24.766 42.459 73.724 1.00 86.29 ? 882 ILE A CD1 1 ATOM 6603 N N . VAL A 1 883 ? -29.178 46.213 72.297 1.00 77.85 ? 883 VAL A N 1 ATOM 6604 C CA . VAL A 1 883 ? -30.104 46.719 71.292 1.00 77.20 ? 883 VAL A CA 1 ATOM 6605 C C . VAL A 1 883 ? -29.358 47.168 70.043 1.00 86.10 ? 883 VAL A C 1 ATOM 6606 O O . VAL A 1 883 ? -28.417 47.956 70.124 1.00 116.69 ? 883 VAL A O 1 ATOM 6607 C CB . VAL A 1 883 ? -30.938 47.893 71.836 1.00 65.34 ? 883 VAL A CB 1 ATOM 6608 C CG1 . VAL A 1 883 ? -31.723 48.547 70.715 1.00 76.15 ? 883 VAL A CG1 1 ATOM 6609 C CG2 . VAL A 1 883 ? -31.869 47.415 72.940 1.00 85.42 ? 883 VAL A CG2 1 ATOM 6610 N N . CYS A 1 884 ? -29.782 46.664 68.889 1.00 65.33 ? 884 CYS A N 1 ATOM 6611 C CA . CYS A 1 884 ? -29.113 46.985 67.636 1.00 75.69 ? 884 CYS A CA 1 ATOM 6612 C C . CYS A 1 884 ? -30.045 47.644 66.624 1.00 76.86 ? 884 CYS A C 1 ATOM 6613 O O . CYS A 1 884 ? -31.196 47.237 66.465 1.00 69.00 ? 884 CYS A O 1 ATOM 6614 C CB . CYS A 1 884 ? -28.502 45.723 67.028 1.00 57.76 ? 884 CYS A CB 1 ATOM 6615 S SG . CYS A 1 884 ? -27.294 44.898 68.085 1.00 103.72 ? 884 CYS A SG 1 ATOM 6616 N N . GLN A 1 885 ? -29.538 48.664 65.940 1.00 87.29 ? 885 GLN A N 1 ATOM 6617 C CA . GLN A 1 885 ? -30.293 49.320 64.880 1.00 90.68 ? 885 GLN A CA 1 ATOM 6618 C C . GLN A 1 885 ? -29.824 48.823 63.517 1.00 87.98 ? 885 GLN A C 1 ATOM 6619 O O . GLN A 1 885 ? -28.680 49.049 63.123 1.00 105.02 ? 885 GLN A O 1 ATOM 6620 C CB . GLN A 1 885 ? -30.153 50.842 64.966 1.00 87.77 ? 885 GLN A CB 1 ATOM 6621 C CG . GLN A 1 885 ? -30.646 51.452 66.271 1.00 104.49 ? 885 GLN A CG 1 ATOM 6622 C CD . GLN A 1 885 ? -29.586 51.458 67.357 1.00 124.95 ? 885 GLN A CD 1 ATOM 6623 O OE1 . GLN A 1 885 ? -28.462 51.001 67.147 1.00 135.45 ? 885 GLN A OE1 1 ATOM 6624 N NE2 . GLN A 1 885 ? -29.939 51.981 68.527 1.00 117.59 ? 885 GLN A NE2 1 ATOM 6625 N N . VAL A 1 886 ? -30.715 48.145 62.801 1.00 74.81 ? 886 VAL A N 1 ATOM 6626 C CA . VAL A 1 886 ? -30.389 47.597 61.491 1.00 71.39 ? 886 VAL A CA 1 ATOM 6627 C C . VAL A 1 886 ? -31.029 48.442 60.398 1.00 84.33 ? 886 VAL A C 1 ATOM 6628 O O . VAL A 1 886 ? -32.112 48.994 60.589 1.00 96.30 ? 886 VAL A O 1 ATOM 6629 C CB . VAL A 1 886 ? -30.863 46.134 61.355 1.00 59.07 ? 886 VAL A CB 1 ATOM 6630 C CG1 . VAL A 1 886 ? -30.291 45.495 60.098 1.00 61.25 ? 886 VAL A CG1 1 ATOM 6631 C CG2 . VAL A 1 886 ? -30.465 45.332 62.579 1.00 74.57 ? 886 VAL A CG2 1 ATOM 6632 N N . GLY A 1 887 ? -30.358 48.548 59.255 1.00 67.67 ? 887 GLY A N 1 ATOM 6633 C CA . GLY A 1 887 ? -30.934 49.245 58.123 1.00 69.21 ? 887 GLY A CA 1 ATOM 6634 C C . GLY A 1 887 ? -30.445 48.791 56.761 1.00 86.74 ? 887 GLY A C 1 ATOM 6635 O O . GLY A 1 887 ? -29.328 48.297 56.616 1.00 135.98 ? 887 GLY A O 1 ATOM 6636 N N . ARG A 1 888 ? -31.301 48.990 55.762 1.00 78.98 ? 888 ARG A N 1 ATOM 6637 C CA . ARG A 1 888 ? -31.042 48.638 54.364 1.00 79.71 ? 888 ARG A CA 1 ATOM 6638 C C . ARG A 1 888 ? -30.405 47.262 54.151 1.00 80.40 ? 888 ARG A C 1 ATOM 6639 O O . ARG A 1 888 ? -29.230 47.156 53.796 1.00 83.93 ? 888 ARG A O 1 ATOM 6640 C CB . ARG A 1 888 ? -30.174 49.708 53.699 1.00 97.36 ? 888 ARG A CB 1 ATOM 6641 C CG . ARG A 1 888 ? -30.308 49.715 52.181 1.00 94.01 ? 888 ARG A CG 1 ATOM 6642 C CD . ARG A 1 888 ? -31.765 49.508 51.779 1.00 91.37 ? 888 ARG A CD 1 ATOM 6643 N NE . ARG A 1 888 ? -31.938 49.341 50.339 1.00 94.49 ? 888 ARG A NE 1 ATOM 6644 C CZ . ARG A 1 888 ? -32.649 50.160 49.571 1.00 95.24 ? 888 ARG A CZ 1 ATOM 6645 N NH1 . ARG A 1 888 ? -33.262 51.208 50.106 1.00 92.68 ? 888 ARG A NH1 1 ATOM 6646 N NH2 . ARG A 1 888 ? -32.753 49.929 48.271 1.00 99.23 ? 888 ARG A NH2 1 ATOM 6647 N N . LEU A 1 889 ? -31.183 46.210 54.381 1.00 78.00 ? 889 LEU A N 1 ATOM 6648 C CA . LEU A 1 889 ? -30.777 44.868 53.981 1.00 79.00 ? 889 LEU A CA 1 ATOM 6649 C C . LEU A 1 889 ? -31.518 44.461 52.711 1.00 85.05 ? 889 LEU A C 1 ATOM 6650 O O . LEU A 1 889 ? -32.741 44.321 52.713 1.00 85.58 ? 889 LEU A O 1 ATOM 6651 C CB . LEU A 1 889 ? -31.037 43.852 55.096 1.00 73.99 ? 889 LEU A CB 1 ATOM 6652 C CG . LEU A 1 889 ? -30.048 43.796 56.261 1.00 70.86 ? 889 LEU A CG 1 ATOM 6653 C CD1 . LEU A 1 889 ? -30.344 42.602 57.159 1.00 67.03 ? 889 LEU A CD1 1 ATOM 6654 C CD2 . LEU A 1 889 ? -28.619 43.737 55.750 1.00 74.74 ? 889 LEU A CD2 1 ATOM 6655 N N . ASP A 1 890 ? -30.772 44.282 51.626 1.00 90.97 ? 890 ASP A N 1 ATOM 6656 C CA . ASP A 1 890 ? -31.360 43.909 50.345 1.00 94.04 ? 890 ASP A CA 1 ATOM 6657 C C . ASP A 1 890 ? -31.550 42.397 50.244 1.00 94.20 ? 890 ASP A C 1 ATOM 6658 O O . ASP A 1 890 ? -31.399 41.678 51.231 1.00 89.61 ? 890 ASP A O 1 ATOM 6659 C CB . ASP A 1 890 ? -30.496 44.418 49.189 1.00 100.78 ? 890 ASP A CB 1 ATOM 6660 C CG . ASP A 1 890 ? -30.292 45.921 49.233 1.00 104.37 ? 890 ASP A CG 1 ATOM 6661 O OD1 . ASP A 1 890 ? -31.217 46.662 48.839 1.00 105.40 ? 890 ASP A OD1 1 ATOM 6662 O OD2 . ASP A 1 890 ? -29.205 46.363 49.663 1.00 117.33 ? 890 ASP A OD2 1 ATOM 6663 N N . ARG A 1 891 ? -31.886 41.924 49.047 1.00 100.21 ? 891 ARG A N 1 ATOM 6664 C CA . ARG A 1 891 ? -32.221 40.518 48.836 1.00 101.92 ? 891 ARG A CA 1 ATOM 6665 C C . ARG A 1 891 ? -31.068 39.562 49.143 1.00 105.19 ? 891 ARG A C 1 ATOM 6666 O O . ARG A 1 891 ? -31.280 38.491 49.710 1.00 119.49 ? 891 ARG A O 1 ATOM 6667 C CB . ARG A 1 891 ? -32.695 40.301 47.396 1.00 109.92 ? 891 ARG A CB 1 ATOM 6668 C CG . ARG A 1 891 ? -33.053 38.856 47.078 1.00 113.40 ? 891 ARG A CG 1 ATOM 6669 C CD . ARG A 1 891 ? -33.677 38.712 45.699 1.00 123.22 ? 891 ARG A CD 1 ATOM 6670 N NE . ARG A 1 891 ? -32.741 39.027 44.625 1.00 134.15 ? 891 ARG A NE 1 ATOM 6671 C CZ . ARG A 1 891 ? -32.748 40.162 43.933 1.00 134.33 ? 891 ARG A CZ 1 ATOM 6672 N NH1 . ARG A 1 891 ? -33.649 41.098 44.199 1.00 135.72 ? 891 ARG A NH1 1 ATOM 6673 N NH2 . ARG A 1 891 ? -31.858 40.360 42.971 1.00 138.63 ? 891 ARG A NH2 1 ATOM 6674 N N . GLY A 1 892 ? -29.851 39.945 48.771 1.00 106.03 ? 892 GLY A N 1 ATOM 6675 C CA . GLY A 1 892 ? -28.709 39.068 48.948 1.00 113.70 ? 892 GLY A CA 1 ATOM 6676 C C . GLY A 1 892 ? -27.796 39.428 50.106 1.00 112.94 ? 892 GLY A C 1 ATOM 6677 O O . GLY A 1 892 ? -26.676 38.925 50.193 1.00 133.09 ? 892 GLY A O 1 ATOM 6678 N N . LYS A 1 893 ? -28.271 40.288 51.002 1.00 95.37 ? 893 LYS A N 1 ATOM 6679 C CA . LYS A 1 893 ? -27.442 40.769 52.105 1.00 90.01 ? 893 LYS A CA 1 ATOM 6680 C C . LYS A 1 893 ? -27.936 40.291 53.469 1.00 83.90 ? 893 LYS A C 1 ATOM 6681 O O . LYS A 1 893 ? -28.931 39.571 53.564 1.00 81.00 ? 893 LYS A O 1 ATOM 6682 C CB . LYS A 1 893 ? -27.371 42.296 52.086 1.00 92.91 ? 893 LYS A CB 1 ATOM 6683 C CG . LYS A 1 893 ? -26.725 42.858 50.832 1.00 107.02 ? 893 LYS A CG 1 ATOM 6684 C CD . LYS A 1 893 ? -25.401 42.166 50.547 1.00 118.64 ? 893 LYS A CD 1 ATOM 6685 C CE . LYS A 1 893 ? -24.744 42.721 49.295 1.00 121.50 ? 893 LYS A CE 1 ATOM 6686 N NZ . LYS A 1 893 ? -24.351 44.147 49.463 1.00 117.37 ? 893 LYS A NZ 1 ATOM 6687 N N . SER A 1 894 ? -27.249 40.731 54.522 1.00 84.13 ? 894 SER A N 1 ATOM 6688 C CA . SER A 1 894 ? -27.466 40.221 55.873 1.00 73.55 ? 894 SER A CA 1 ATOM 6689 C C . SER A 1 894 ? -26.633 40.972 56.909 1.00 73.97 ? 894 SER A C 1 ATOM 6690 O O . SER A 1 894 ? -25.698 41.692 56.565 1.00 101.57 ? 894 SER A O 1 ATOM 6691 C CB . SER A 1 894 ? -27.128 38.729 55.939 1.00 73.99 ? 894 SER A CB 1 ATOM 6692 O OG . SER A 1 894 ? -27.215 38.244 57.264 1.00 101.60 ? 894 SER A OG 1 ATOM 6693 N N . ALA A 1 895 ? -26.983 40.796 58.181 1.00 66.38 ? 895 ALA A N 1 ATOM 6694 C CA . ALA A 1 895 ? -26.268 41.442 59.280 1.00 65.59 ? 895 ALA A CA 1 ATOM 6695 C C . ALA A 1 895 ? -25.944 40.434 60.379 1.00 74.27 ? 895 ALA A C 1 ATOM 6696 O O . ALA A 1 895 ? -26.783 39.609 60.740 1.00 85.00 ? 895 ALA A O 1 ATOM 6697 C CB . ALA A 1 895 ? -27.084 42.595 59.842 1.00 63.50 ? 895 ALA A CB 1 ATOM 6698 N N . ILE A 1 896 ? -24.726 40.505 60.910 1.00 64.51 ? 896 ILE A N 1 ATOM 6699 C CA . ILE A 1 896 ? -24.269 39.527 61.890 1.00 64.64 ? 896 ILE A CA 1 ATOM 6700 C C . ILE A 1 896 ? -23.722 40.179 63.161 1.00 66.54 ? 896 ILE A C 1 ATOM 6701 O O . ILE A 1 896 ? -22.942 41.131 63.097 1.00 68.26 ? 896 ILE A O 1 ATOM 6702 C CB . ILE A 1 896 ? -23.172 38.603 61.302 1.00 64.44 ? 896 ILE A CB 1 ATOM 6703 C CG1 . ILE A 1 896 ? -23.590 38.043 59.940 1.00 66.57 ? 896 ILE A CG1 1 ATOM 6704 C CG2 . ILE A 1 896 ? -22.862 37.468 62.262 1.00 70.95 ? 896 ILE A CG2 1 ATOM 6705 C CD1 . ILE A 1 896 ? -23.057 38.825 58.753 1.00 94.29 ? 896 ILE A CD1 1 ATOM 6706 N N . LEU A 1 897 ? -24.140 39.660 64.312 1.00 84.15 ? 897 LEU A N 1 ATOM 6707 C CA . LEU A 1 897 ? -23.622 40.105 65.601 1.00 85.74 ? 897 LEU A CA 1 ATOM 6708 C C . LEU A 1 897 ? -22.820 38.996 66.279 1.00 84.84 ? 897 LEU A C 1 ATOM 6709 O O . LEU A 1 897 ? -23.371 37.959 66.651 1.00 98.72 ? 897 LEU A O 1 ATOM 6710 C CB . LEU A 1 897 ? -24.764 40.559 66.514 1.00 68.80 ? 897 LEU A CB 1 ATOM 6711 C CG . LEU A 1 897 ? -24.394 40.872 67.968 1.00 58.86 ? 897 LEU A CG 1 ATOM 6712 C CD1 . LEU A 1 897 ? -23.380 42.005 68.041 1.00 63.41 ? 897 LEU A CD1 1 ATOM 6713 C CD2 . LEU A 1 897 ? -25.633 41.202 68.791 1.00 56.77 ? 897 LEU A CD2 1 ATOM 6714 N N . TYR A 1 898 ? -21.519 39.219 66.436 1.00 66.71 ? 898 TYR A N 1 ATOM 6715 C CA . TYR A 1 898 ? -20.655 38.262 67.118 1.00 65.97 ? 898 TYR A CA 1 ATOM 6716 C C . TYR A 1 898 ? -20.467 38.662 68.576 1.00 67.39 ? 898 TYR A C 1 ATOM 6717 O O . TYR A 1 898 ? -20.006 39.763 68.860 1.00 75.12 ? 898 TYR A O 1 ATOM 6718 C CB . TYR A 1 898 ? -19.292 38.169 66.429 1.00 70.46 ? 898 TYR A CB 1 ATOM 6719 C CG . TYR A 1 898 ? -19.353 37.893 64.945 1.00 71.35 ? 898 TYR A CG 1 ATOM 6720 C CD1 . TYR A 1 898 ? -19.352 38.934 64.026 1.00 76.89 ? 898 TYR A CD1 1 ATOM 6721 C CD2 . TYR A 1 898 ? -19.402 36.592 64.460 1.00 71.60 ? 898 TYR A CD2 1 ATOM 6722 C CE1 . TYR A 1 898 ? -19.405 38.688 62.666 1.00 87.52 ? 898 TYR A CE1 1 ATOM 6723 C CE2 . TYR A 1 898 ? -19.454 36.336 63.104 1.00 77.50 ? 898 TYR A CE2 1 ATOM 6724 C CZ . TYR A 1 898 ? -19.453 37.387 62.211 1.00 98.33 ? 898 TYR A CZ 1 ATOM 6725 O OH . TYR A 1 898 ? -19.507 37.135 60.859 1.00 110.73 ? 898 TYR A OH 1 ATOM 6726 N N . VAL A 1 899 ? -20.819 37.772 69.498 1.00 68.49 ? 899 VAL A N 1 ATOM 6727 C CA . VAL A 1 899 ? -20.656 38.056 70.920 1.00 67.70 ? 899 VAL A CA 1 ATOM 6728 C C . VAL A 1 899 ? -19.605 37.146 71.548 1.00 80.16 ? 899 VAL A C 1 ATOM 6729 O O . VAL A 1 899 ? -19.813 35.940 71.684 1.00 90.52 ? 899 VAL A O 1 ATOM 6730 C CB . VAL A 1 899 ? -21.983 37.897 71.685 1.00 64.60 ? 899 VAL A CB 1 ATOM 6731 C CG1 . VAL A 1 899 ? -21.814 38.338 73.130 1.00 72.00 ? 899 VAL A CG1 1 ATOM 6732 C CG2 . VAL A 1 899 ? -23.079 38.699 71.009 1.00 61.76 ? 899 VAL A CG2 1 ATOM 6733 N N . LYS A 1 900 ? -18.475 37.732 71.931 1.00 75.21 ? 900 LYS A N 1 ATOM 6734 C CA . LYS A 1 900 ? -17.384 36.977 72.537 1.00 79.66 ? 900 LYS A CA 1 ATOM 6735 C C . LYS A 1 900 ? -17.416 37.105 74.055 1.00 82.44 ? 900 LYS A C 1 ATOM 6736 O O . LYS A 1 900 ? -17.203 38.188 74.599 1.00 93.48 ? 900 LYS A O 1 ATOM 6737 C CB . LYS A 1 900 ? -16.035 37.451 71.986 1.00 83.07 ? 900 LYS A CB 1 ATOM 6738 C CG . LYS A 1 900 ? -14.833 36.667 72.491 1.00 86.25 ? 900 LYS A CG 1 ATOM 6739 C CD . LYS A 1 900 ? -13.583 37.018 71.694 1.00 91.41 ? 900 LYS A CD 1 ATOM 6740 C CE . LYS A 1 900 ? -12.365 36.254 72.188 1.00 94.47 ? 900 LYS A CE 1 ATOM 6741 N NZ . LYS A 1 900 ? -11.931 36.708 73.537 1.00 98.76 ? 900 LYS A NZ 1 ATOM 6742 N N . SER A 1 901 ? -17.683 35.995 74.735 1.00 89.21 ? 901 SER A N 1 ATOM 6743 C CA . SER A 1 901 ? -17.786 36.003 76.188 1.00 87.51 ? 901 SER A CA 1 ATOM 6744 C C . SER A 1 901 ? -16.995 34.867 76.824 1.00 89.04 ? 901 SER A C 1 ATOM 6745 O O . SER A 1 901 ? -16.680 33.872 76.173 1.00 88.87 ? 901 SER A O 1 ATOM 6746 C CB . SER A 1 901 ? -19.252 35.913 76.622 1.00 83.79 ? 901 SER A CB 1 ATOM 6747 O OG . SER A 1 901 ? -19.778 34.620 76.385 1.00 75.67 ? 901 SER A OG 1 ATOM 6748 N N . LEU A 1 902 ? -16.678 35.028 78.104 1.00 87.16 ? 902 LEU A N 1 ATOM 6749 C CA . LEU A 1 902 ? -15.991 33.991 78.860 1.00 88.70 ? 902 LEU A CA 1 ATOM 6750 C C . LEU A 1 902 ? -16.959 33.302 79.809 1.00 89.29 ? 902 LEU A C 1 ATOM 6751 O O . LEU A 1 902 ? -17.822 33.947 80.404 1.00 102.56 ? 902 LEU A O 1 ATOM 6752 C CB . LEU A 1 902 ? -14.822 34.579 79.652 1.00 94.03 ? 902 LEU A CB 1 ATOM 6753 C CG . LEU A 1 902 ? -13.783 35.404 78.893 1.00 100.97 ? 902 LEU A CG 1 ATOM 6754 C CD1 . LEU A 1 902 ? -12.773 35.982 79.866 1.00 105.88 ? 902 LEU A CD1 1 ATOM 6755 C CD2 . LEU A 1 902 ? -13.092 34.562 77.835 1.00 101.93 ? 902 LEU A CD2 1 ATOM 6756 N N . LEU A 1 903 ? -16.816 31.990 79.953 1.00 99.43 ? 903 LEU A N 1 ATOM 6757 C CA . LEU A 1 903 ? -17.584 31.266 80.951 1.00 101.26 ? 903 LEU A CA 1 ATOM 6758 C C . LEU A 1 903 ? -16.990 31.553 82.321 1.00 103.91 ? 903 LEU A C 1 ATOM 6759 O O . LEU A 1 903 ? -15.812 31.287 82.555 1.00 111.71 ? 903 LEU A O 1 ATOM 6760 C CB . LEU A 1 903 ? -17.572 29.760 80.673 1.00 98.38 ? 903 LEU A CB 1 ATOM 6761 C CG . LEU A 1 903 ? -18.320 28.902 81.695 1.00 88.33 ? 903 LEU A CG 1 ATOM 6762 C CD1 . LEU A 1 903 ? -19.822 29.059 81.523 1.00 86.88 ? 903 LEU A CD1 1 ATOM 6763 C CD2 . LEU A 1 903 ? -17.914 27.441 81.596 1.00 94.35 ? 903 LEU A CD2 1 ATOM 6764 N N . TRP A 1 904 ? -17.795 32.092 83.229 1.00 101.19 ? 904 TRP A N 1 ATOM 6765 C CA . TRP A 1 904 ? -17.284 32.390 84.558 1.00 105.13 ? 904 TRP A CA 1 ATOM 6766 C C . TRP A 1 904 ? -17.264 31.088 85.344 1.00 111.38 ? 904 TRP A C 1 ATOM 6767 O O . TRP A 1 904 ? -18.310 30.507 85.622 1.00 133.25 ? 904 TRP A O 1 ATOM 6768 C CB . TRP A 1 904 ? -18.151 33.446 85.250 1.00 103.93 ? 904 TRP A CB 1 ATOM 6769 C CG . TRP A 1 904 ? -17.459 34.207 86.344 1.00 107.19 ? 904 TRP A CG 1 ATOM 6770 C CD1 . TRP A 1 904 ? -17.400 33.873 87.665 1.00 110.49 ? 904 TRP A CD1 1 ATOM 6771 C CD2 . TRP A 1 904 ? -16.740 35.440 86.209 1.00 109.18 ? 904 TRP A CD2 1 ATOM 6772 N NE1 . TRP A 1 904 ? -16.683 34.817 88.361 1.00 116.54 ? 904 TRP A NE1 1 ATOM 6773 C CE2 . TRP A 1 904 ? -16.267 35.789 87.490 1.00 113.45 ? 904 TRP A CE2 1 ATOM 6774 C CE3 . TRP A 1 904 ? -16.447 36.279 85.130 1.00 108.17 ? 904 TRP A CE3 1 ATOM 6775 C CZ2 . TRP A 1 904 ? -15.518 36.942 87.720 1.00 116.51 ? 904 TRP A CZ2 1 ATOM 6776 C CZ3 . TRP A 1 904 ? -15.702 37.423 85.361 1.00 111.85 ? 904 TRP A CZ3 1 ATOM 6777 C CH2 . TRP A 1 904 ? -15.247 37.744 86.646 1.00 115.85 ? 904 TRP A CH2 1 ATOM 6778 N N . THR A 1 905 ? -16.068 30.640 85.712 1.00 103.40 ? 905 THR A N 1 ATOM 6779 C CA . THR A 1 905 ? -15.904 29.334 86.340 1.00 103.96 ? 905 THR A CA 1 ATOM 6780 C C . THR A 1 905 ? -16.200 29.384 87.836 1.00 108.23 ? 905 THR A C 1 ATOM 6781 O O . THR A 1 905 ? -16.753 28.439 88.399 1.00 122.33 ? 905 THR A O 1 ATOM 6782 C CB . THR A 1 905 ? -14.485 28.781 86.116 1.00 109.19 ? 905 THR A CB 1 ATOM 6783 O OG1 . THR A 1 905 ? -14.126 28.918 84.735 1.00 102.31 ? 905 THR A OG1 1 ATOM 6784 C CG2 . THR A 1 905 ? -14.415 27.311 86.508 1.00 120.50 ? 905 THR A CG2 1 ATOM 6785 N N . GLU A 1 906 ? -15.826 30.494 88.467 1.00 110.14 ? 906 GLU A N 1 ATOM 6786 C CA . GLU A 1 906 ? -15.988 30.675 89.909 1.00 115.55 ? 906 GLU A CA 1 ATOM 6787 C C . GLU A 1 906 ? -17.425 30.457 90.375 1.00 119.86 ? 906 GLU A C 1 ATOM 6788 O O . GLU A 1 906 ? -17.658 29.945 91.470 1.00 133.20 ? 906 GLU A O 1 ATOM 6789 C CB . GLU A 1 906 ? -15.524 32.074 90.318 1.00 134.58 ? 906 GLU A CB 1 ATOM 6790 C CG . GLU A 1 906 ? -14.048 32.338 90.084 1.00 154.27 ? 906 GLU A CG 1 ATOM 6791 C CD . GLU A 1 906 ? -13.659 33.763 90.421 1.00 159.78 ? 906 GLU A CD 1 ATOM 6792 O OE1 . GLU A 1 906 ? -12.769 33.952 91.276 1.00 163.45 ? 906 GLU A OE1 1 ATOM 6793 O OE2 . GLU A 1 906 ? -14.244 34.694 89.830 1.00 150.56 ? 906 GLU A OE2 1 ATOM 6794 N N . THR A 1 907 ? -18.380 30.856 89.540 1.00 121.70 ? 907 THR A N 1 ATOM 6795 C CA . THR A 1 907 ? -19.798 30.663 89.828 1.00 124.79 ? 907 THR A CA 1 ATOM 6796 C C . THR A 1 907 ? -20.124 29.186 90.013 1.00 117.86 ? 907 THR A C 1 ATOM 6797 O O . THR A 1 907 ? -20.782 28.794 90.977 1.00 132.87 ? 907 THR A O 1 ATOM 6798 C CB . THR A 1 907 ? -20.680 31.232 88.702 1.00 116.90 ? 907 THR A CB 1 ATOM 6799 O OG1 . THR A 1 907 ? -20.448 32.640 88.575 1.00 113.39 ? 907 THR A OG1 1 ATOM 6800 C CG2 . THR A 1 907 ? -22.151 30.982 88.997 1.00 119.91 ? 907 THR A CG2 1 ATOM 6801 N N . PHE A 1 908 ? -19.653 28.374 89.074 1.00 110.20 ? 908 PHE A N 1 ATOM 6802 C CA . PHE A 1 908 ? -19.833 26.929 89.120 1.00 119.83 ? 908 PHE A CA 1 ATOM 6803 C C . PHE A 1 908 ? -18.968 26.318 90.224 1.00 130.49 ? 908 PHE A C 1 ATOM 6804 O O . PHE A 1 908 ? -18.064 26.975 90.744 1.00 150.03 ? 908 PHE A O 1 ATOM 6805 C CB . PHE A 1 908 ? -19.526 26.313 87.755 1.00 119.60 ? 908 PHE A CB 1 ATOM 6806 C CG . PHE A 1 908 ? -20.368 26.878 86.640 1.00 113.60 ? 908 PHE A CG 1 ATOM 6807 C CD1 . PHE A 1 908 ? -21.613 26.343 86.348 1.00 120.78 ? 908 PHE A CD1 1 ATOM 6808 C CD2 . PHE A 1 908 ? -19.920 27.955 85.897 1.00 116.95 ? 908 PHE A CD2 1 ATOM 6809 C CE1 . PHE A 1 908 ? -22.390 26.869 85.327 1.00 116.43 ? 908 PHE A CE1 1 ATOM 6810 C CE2 . PHE A 1 908 ? -20.690 28.486 84.878 1.00 102.42 ? 908 PHE A CE2 1 ATOM 6811 C CZ . PHE A 1 908 ? -21.926 27.942 84.592 1.00 99.18 ? 908 PHE A CZ 1 ATOM 6812 N N . MET A 1 909 ? -19.273 25.069 90.579 1.00 116.42 ? 909 MET A N 1 ATOM 6813 C CA . MET A 1 909 ? -18.795 24.409 91.800 1.00 142.48 ? 909 MET A CA 1 ATOM 6814 C C . MET A 1 909 ? -19.347 25.104 93.045 1.00 148.01 ? 909 MET A C 1 ATOM 6815 O O . MET A 1 909 ? -20.542 25.374 93.118 1.00 130.79 ? 909 MET A O 1 ATOM 6816 C CB . MET A 1 909 ? -17.261 24.359 91.861 1.00 154.27 ? 909 MET A CB 1 ATOM 6817 C CG . MET A 1 909 ? -16.591 23.648 90.695 1.00 163.17 ? 909 MET A CG 1 ATOM 6818 S SD . MET A 1 909 ? -16.035 24.786 89.411 1.00 145.55 ? 909 MET A SD 1 ATOM 6819 C CE . MET A 1 909 ? -15.123 23.677 88.340 1.00 115.30 ? 909 MET A CE 1 ATOM 6820 N N . ASN A 1 910 ? -18.481 25.377 94.018 1.00 170.59 ? 910 ASN A N 1 ATOM 6821 C CA . ASN A 1 910 ? -18.878 26.000 95.285 1.00 173.96 ? 910 ASN A CA 1 ATOM 6822 C C . ASN A 1 910 ? -20.042 25.291 95.988 1.00 172.78 ? 910 ASN A C 1 ATOM 6823 O O . ASN A 1 910 ? -20.118 24.061 96.007 1.00 172.44 ? 910 ASN A O 1 ATOM 6824 C CB . ASN A 1 910 ? -19.253 27.468 95.060 1.00 156.50 ? 910 ASN A CB 1 ATOM 6825 C CG . ASN A 1 910 ? -18.167 28.247 94.346 1.00 155.01 ? 910 ASN A CG 1 ATOM 6826 O OD1 . ASN A 1 910 ? -16.983 27.933 94.461 1.00 170.87 ? 910 ASN A OD1 1 ATOM 6827 N ND2 . ASN A 1 910 ? -18.568 29.274 93.604 1.00 131.52 ? 910 ASN A ND2 1 ATOM 6828 N N . LYS A 1 911 ? -20.944 26.083 96.565 1.00 163.19 ? 911 LYS A N 1 ATOM 6829 C CA . LYS A 1 911 ? -22.169 25.574 97.180 1.00 166.14 ? 911 LYS A CA 1 ATOM 6830 C C . LYS A 1 911 ? -23.316 25.673 96.177 1.00 162.82 ? 911 LYS A C 1 ATOM 6831 O O . LYS A 1 911 ? -24.476 25.408 96.495 1.00 175.53 ? 911 LYS A O 1 ATOM 6832 C CB . LYS A 1 911 ? -22.501 26.333 98.467 1.00 171.57 ? 911 LYS A CB 1 ATOM 6833 C CG . LYS A 1 911 ? -23.370 25.540 99.436 1.00 167.30 ? 911 LYS A CG 1 ATOM 6834 C CD . LYS A 1 911 ? -23.654 26.318 100.709 1.00 174.12 ? 911 LYS A CD 1 ATOM 6835 C CE . LYS A 1 911 ? -24.483 25.492 101.681 1.00 182.85 ? 911 LYS A CE 1 ATOM 6836 N NZ . LYS A 1 911 ? -25.778 25.064 101.082 1.00 183.42 ? 911 LYS A NZ 1 ATOM 6837 N N . GLU A 1 912 ? -22.958 26.053 94.956 1.00 150.15 ? 912 GLU A N 1 ATOM 6838 C CA . GLU A 1 912 ? -23.884 26.238 93.839 1.00 150.38 ? 912 GLU A CA 1 ATOM 6839 C C . GLU A 1 912 ? -24.575 24.933 93.424 1.00 154.72 ? 912 GLU A C 1 ATOM 6840 O O . GLU A 1 912 ? -25.322 24.922 92.444 1.00 149.22 ? 912 GLU A O 1 ATOM 6841 C CB . GLU A 1 912 ? -23.152 26.857 92.644 1.00 136.63 ? 912 GLU A CB 1 ATOM 6842 C CG . GLU A 1 912 ? -24.007 27.773 91.783 1.00 124.85 ? 912 GLU A CG 1 ATOM 6843 C CD . GLU A 1 912 ? -24.438 27.118 90.487 1.00 133.38 ? 912 GLU A CD 1 ATOM 6844 O OE1 . GLU A 1 912 ? -23.916 26.029 90.173 1.00 158.21 ? 912 GLU A OE1 1 ATOM 6845 O OE2 . GLU A 1 912 ? -25.295 27.693 89.785 1.00 124.35 ? 912 GLU A OE2 1 ATOM 6846 N N . ASN A 1 913 ? -24.277 23.859 94.165 1.00 176.39 ? 913 ASN A N 1 ATOM 6847 C CA . ASN A 1 913 ? -24.649 22.456 93.912 1.00 191.94 ? 913 ASN A CA 1 ATOM 6848 C C . ASN A 1 913 ? -23.576 21.744 93.100 1.00 194.73 ? 913 ASN A C 1 ATOM 6849 O O . ASN A 1 913 ? -23.676 20.540 92.856 1.00 201.88 ? 913 ASN A O 1 ATOM 6850 C CB . ASN A 1 913 ? -26.015 22.330 93.216 1.00 179.22 ? 913 ASN A CB 1 ATOM 6851 C CG . ASN A 1 913 ? -26.590 20.927 93.291 1.00 189.31 ? 913 ASN A CG 1 ATOM 6852 O OD1 . ASN A 1 913 ? -27.565 20.682 94.000 1.00 193.39 ? 913 ASN A OD1 1 ATOM 6853 N ND2 . ASN A 1 913 ? -25.998 19.999 92.545 1.00 191.70 ? 913 ASN A ND2 1 ATOM 6854 N N . GLN A 1 914 ? -22.548 22.490 92.700 1.00 177.22 ? 914 GLN A N 1 ATOM 6855 C CA . GLN A 1 914 ? -21.354 21.904 92.093 1.00 151.29 ? 914 GLN A CA 1 ATOM 6856 C C . GLN A 1 914 ? -21.725 21.071 90.875 1.00 147.62 ? 914 GLN A C 1 ATOM 6857 O O . GLN A 1 914 ? -22.182 21.615 89.869 1.00 157.87 ? 914 GLN A O 1 ATOM 6858 C CB . GLN A 1 914 ? -20.588 21.062 93.118 1.00 158.94 ? 914 GLN A CB 1 ATOM 6859 C CG . GLN A 1 914 ? -19.109 20.894 92.803 1.00 163.30 ? 914 GLN A CG 1 ATOM 6860 C CD . GLN A 1 914 ? -18.316 20.383 93.989 1.00 168.02 ? 914 GLN A CD 1 ATOM 6861 O OE1 . GLN A 1 914 ? -18.799 20.387 95.122 1.00 165.13 ? 914 GLN A OE1 1 ATOM 6862 N NE2 . GLN A 1 914 ? -17.091 19.940 93.734 1.00 165.85 ? 914 GLN A NE2 1 ATOM 6863 N N . ASN A 1 915 ? -21.504 19.761 90.953 1.00 155.82 ? 915 ASN A N 1 ATOM 6864 C CA . ASN A 1 915 ? -21.929 18.877 89.880 1.00 152.02 ? 915 ASN A CA 1 ATOM 6865 C C . ASN A 1 915 ? -23.427 19.021 89.646 1.00 142.54 ? 915 ASN A C 1 ATOM 6866 O O . ASN A 1 915 ? -24.235 18.771 90.544 1.00 150.26 ? 915 ASN A O 1 ATOM 6867 C CB . ASN A 1 915 ? -21.582 17.422 90.201 1.00 159.71 ? 915 ASN A CB 1 ATOM 6868 C CG . ASN A 1 915 ? -20.106 17.222 90.481 1.00 158.22 ? 915 ASN A CG 1 ATOM 6869 O OD1 . ASN A 1 915 ? -19.414 18.143 90.912 1.00 165.69 ? 915 ASN A OD1 1 ATOM 6870 N ND2 . ASN A 1 915 ? -19.616 16.012 90.237 1.00 153.24 ? 915 ASN A ND2 1 ATOM 6871 N N . HIS A 1 916 ? -23.774 19.396 88.418 1.00 141.08 ? 916 HIS A N 1 ATOM 6872 C CA . HIS A 1 916 ? -25.144 19.683 88.008 1.00 149.12 ? 916 HIS A CA 1 ATOM 6873 C C . HIS A 1 916 ? -25.110 20.182 86.570 1.00 135.12 ? 916 HIS A C 1 ATOM 6874 O O . HIS A 1 916 ? -24.054 20.561 86.067 1.00 138.90 ? 916 HIS A O 1 ATOM 6875 C CB . HIS A 1 916 ? -25.802 20.724 88.918 1.00 144.27 ? 916 HIS A CB 1 ATOM 6876 C CG . HIS A 1 916 ? -27.187 20.355 89.355 1.00 150.61 ? 916 HIS A CG 1 ATOM 6877 N ND1 . HIS A 1 916 ? -27.470 19.174 90.008 1.00 146.94 ? 916 HIS A ND1 1 ATOM 6878 C CD2 . HIS A 1 916 ? -28.365 21.009 89.232 1.00 151.84 ? 916 HIS A CD2 1 ATOM 6879 C CE1 . HIS A 1 916 ? -28.763 19.116 90.269 1.00 139.85 ? 916 HIS A CE1 1 ATOM 6880 N NE2 . HIS A 1 916 ? -29.330 20.217 89.809 1.00 151.98 ? 916 HIS A NE2 1 ATOM 6881 N N . SER A 1 917 ? -26.263 20.197 85.912 1.00 114.47 ? 917 SER A N 1 ATOM 6882 C CA . SER A 1 917 ? -26.314 20.590 84.510 1.00 111.58 ? 917 SER A CA 1 ATOM 6883 C C . SER A 1 917 ? -27.137 21.856 84.285 1.00 123.17 ? 917 SER A C 1 ATOM 6884 O O . SER A 1 917 ? -28.332 21.892 84.576 1.00 129.63 ? 917 SER A O 1 ATOM 6885 C CB . SER A 1 917 ? -26.874 19.444 83.664 1.00 132.76 ? 917 SER A CB 1 ATOM 6886 O OG . SER A 1 917 ? -28.001 18.852 84.286 1.00 155.63 ? 917 SER A OG 1 ATOM 6887 N N . TYR A 1 918 ? -26.483 22.893 83.769 1.00 123.87 ? 918 TYR A N 1 ATOM 6888 C CA . TYR A 1 918 ? -27.164 24.131 83.407 1.00 99.19 ? 918 TYR A CA 1 ATOM 6889 C C . TYR A 1 918 ? -27.111 24.356 81.901 1.00 94.32 ? 918 TYR A C 1 ATOM 6890 O O . TYR A 1 918 ? -26.096 24.086 81.261 1.00 91.16 ? 918 TYR A O 1 ATOM 6891 C CB . TYR A 1 918 ? -26.540 25.332 84.124 1.00 98.92 ? 918 TYR A CB 1 ATOM 6892 C CG . TYR A 1 918 ? -26.622 25.280 85.632 1.00 103.67 ? 918 TYR A CG 1 ATOM 6893 C CD1 . TYR A 1 918 ? -27.827 25.486 86.289 1.00 107.84 ? 918 TYR A CD1 1 ATOM 6894 C CD2 . TYR A 1 918 ? -25.489 25.045 86.399 1.00 106.23 ? 918 TYR A CD2 1 ATOM 6895 C CE1 . TYR A 1 918 ? -27.905 25.444 87.669 1.00 123.51 ? 918 TYR A CE1 1 ATOM 6896 C CE2 . TYR A 1 918 ? -25.557 25.001 87.778 1.00 124.75 ? 918 TYR A CE2 1 ATOM 6897 C CZ . TYR A 1 918 ? -26.766 25.203 88.409 1.00 116.35 ? 918 TYR A CZ 1 ATOM 6898 O OH . TYR A 1 918 ? -26.836 25.162 89.783 1.00 117.57 ? 918 TYR A OH 1 ATOM 6899 N N . SER A 1 919 ? -28.208 24.849 81.338 1.00 111.63 ? 919 SER A N 1 ATOM 6900 C CA . SER A 1 919 ? -28.221 25.251 79.939 1.00 105.89 ? 919 SER A CA 1 ATOM 6901 C C . SER A 1 919 ? -28.381 26.761 79.857 1.00 90.27 ? 919 SER A C 1 ATOM 6902 O O . SER A 1 919 ? -29.447 27.298 80.157 1.00 91.81 ? 919 SER A O 1 ATOM 6903 C CB . SER A 1 919 ? -29.343 24.550 79.171 1.00 110.37 ? 919 SER A CB 1 ATOM 6904 O OG . SER A 1 919 ? -30.613 25.054 79.546 1.00 132.50 ? 919 SER A OG 1 ATOM 6905 N N . LEU A 1 920 ? -27.315 27.442 79.448 1.00 98.30 ? 920 LEU A N 1 ATOM 6906 C CA . LEU A 1 920 ? -27.327 28.896 79.376 1.00 83.07 ? 920 LEU A CA 1 ATOM 6907 C C . LEU A 1 920 ? -28.049 29.337 78.111 1.00 94.63 ? 920 LEU A C 1 ATOM 6908 O O . LEU A 1 920 ? -27.643 28.994 77.001 1.00 102.77 ? 920 LEU A O 1 ATOM 6909 C CB . LEU A 1 920 ? -25.900 29.444 79.412 1.00 80.92 ? 920 LEU A CB 1 ATOM 6910 C CG . LEU A 1 920 ? -25.048 28.906 80.568 1.00 83.93 ? 920 LEU A CG 1 ATOM 6911 C CD1 . LEU A 1 920 ? -23.642 29.483 80.529 1.00 90.00 ? 920 LEU A CD1 1 ATOM 6912 C CD2 . LEU A 1 920 ? -25.710 29.187 81.909 1.00 88.60 ? 920 LEU A CD2 1 ATOM 6913 N N . LYS A 1 921 ? -29.122 30.100 78.286 1.00 92.33 ? 921 LYS A N 1 ATOM 6914 C CA . LYS A 1 921 ? -30.012 30.424 77.178 1.00 79.60 ? 921 LYS A CA 1 ATOM 6915 C C . LYS A 1 921 ? -30.114 31.922 76.921 1.00 85.60 ? 921 LYS A C 1 ATOM 6916 O O . LYS A 1 921 ? -30.610 32.678 77.757 1.00 112.33 ? 921 LYS A O 1 ATOM 6917 C CB . LYS A 1 921 ? -31.403 29.841 77.443 1.00 84.47 ? 921 LYS A CB 1 ATOM 6918 C CG . LYS A 1 921 ? -32.504 30.388 76.551 1.00 85.70 ? 921 LYS A CG 1 ATOM 6919 C CD . LYS A 1 921 ? -33.814 29.662 76.811 1.00 101.93 ? 921 LYS A CD 1 ATOM 6920 C CE . LYS A 1 921 ? -35.006 30.487 76.361 1.00 116.09 ? 921 LYS A CE 1 ATOM 6921 N NZ . LYS A 1 921 ? -35.170 31.711 77.193 1.00 129.69 ? 921 LYS A NZ 1 ATOM 6922 N N . SER A 1 922 ? -29.636 32.340 75.754 1.00 89.92 ? 922 SER A N 1 ATOM 6923 C CA . SER A 1 922 ? -29.793 33.715 75.301 1.00 80.31 ? 922 SER A CA 1 ATOM 6924 C C . SER A 1 922 ? -30.759 33.746 74.125 1.00 71.78 ? 922 SER A C 1 ATOM 6925 O O . SER A 1 922 ? -30.799 32.814 73.323 1.00 76.21 ? 922 SER A O 1 ATOM 6926 C CB . SER A 1 922 ? -28.444 34.320 74.904 1.00 77.72 ? 922 SER A CB 1 ATOM 6927 O OG . SER A 1 922 ? -27.890 33.641 73.790 1.00 85.27 ? 922 SER A OG 1 ATOM 6928 N N . SER A 1 923 ? -31.540 34.815 74.025 1.00 76.19 ? 923 SER A N 1 ATOM 6929 C CA . SER A 1 923 ? -32.523 34.931 72.957 1.00 71.90 ? 923 SER A CA 1 ATOM 6930 C C . SER A 1 923 ? -32.364 36.240 72.195 1.00 66.30 ? 923 SER A C 1 ATOM 6931 O O . SER A 1 923 ? -31.932 37.246 72.755 1.00 78.84 ? 923 SER A O 1 ATOM 6932 C CB . SER A 1 923 ? -33.942 34.822 73.520 1.00 76.78 ? 923 SER A CB 1 ATOM 6933 O OG . SER A 1 923 ? -34.185 35.828 74.487 1.00 84.48 ? 923 SER A OG 1 ATOM 6934 N N . ALA A 1 924 ? -32.710 36.215 70.913 1.00 69.02 ? 924 ALA A N 1 ATOM 6935 C CA . ALA A 1 924 ? -32.668 37.416 70.092 1.00 62.20 ? 924 ALA A CA 1 ATOM 6936 C C . ALA A 1 924 ? -33.885 37.503 69.183 1.00 59.89 ? 924 ALA A C 1 ATOM 6937 O O . ALA A 1 924 ? -34.212 36.555 68.469 1.00 63.18 ? 924 ALA A O 1 ATOM 6938 C CB . ALA A 1 924 ? -31.393 37.457 69.271 1.00 73.75 ? 924 ALA A CB 1 ATOM 6939 N N . SER A 1 925 ? -34.552 38.652 69.217 1.00 60.52 ? 925 SER A N 1 ATOM 6940 C CA . SER A 1 925 ? -35.713 38.893 68.373 1.00 62.26 ? 925 SER A CA 1 ATOM 6941 C C . SER A 1 925 ? -35.446 40.062 67.437 1.00 70.35 ? 925 SER A C 1 ATOM 6942 O O . SER A 1 925 ? -34.605 40.913 67.723 1.00 72.81 ? 925 SER A O 1 ATOM 6943 C CB . SER A 1 925 ? -36.953 39.169 69.223 1.00 66.62 ? 925 SER A CB 1 ATOM 6944 O OG . SER A 1 925 ? -36.785 40.347 69.994 1.00 88.13 ? 925 SER A OG 1 ATOM 6945 N N . PHE A 1 926 ? -36.160 40.102 66.317 1.00 61.11 ? 926 PHE A N 1 ATOM 6946 C CA . PHE A 1 926 ? -36.014 41.202 65.375 1.00 63.43 ? 926 PHE A CA 1 ATOM 6947 C C . PHE A 1 926 ? -37.377 41.700 64.910 1.00 82.11 ? 926 PHE A C 1 ATOM 6948 O O . PHE A 1 926 ? -38.334 40.932 64.824 1.00 93.93 ? 926 PHE A O 1 ATOM 6949 C CB . PHE A 1 926 ? -35.161 40.779 64.175 1.00 73.32 ? 926 PHE A CB 1 ATOM 6950 C CG . PHE A 1 926 ? -35.912 39.997 63.133 1.00 68.55 ? 926 PHE A CG 1 ATOM 6951 C CD1 . PHE A 1 926 ? -36.447 40.635 62.024 1.00 64.04 ? 926 PHE A CD1 1 ATOM 6952 C CD2 . PHE A 1 926 ? -36.075 38.628 63.254 1.00 66.88 ? 926 PHE A CD2 1 ATOM 6953 C CE1 . PHE A 1 926 ? -37.137 39.925 61.063 1.00 77.76 ? 926 PHE A CE1 1 ATOM 6954 C CE2 . PHE A 1 926 ? -36.762 37.912 62.291 1.00 66.72 ? 926 PHE A CE2 1 ATOM 6955 C CZ . PHE A 1 926 ? -37.294 38.562 61.195 1.00 69.78 ? 926 PHE A CZ 1 ATOM 6956 N N . ASN A 1 927 ? -37.456 42.993 64.614 1.00 81.89 ? 927 ASN A N 1 ATOM 6957 C CA . ASN A 1 927 ? -38.676 43.590 64.085 1.00 69.67 ? 927 ASN A CA 1 ATOM 6958 C C . ASN A 1 927 ? -38.345 44.572 62.967 1.00 71.00 ? 927 ASN A C 1 ATOM 6959 O O . ASN A 1 927 ? -37.522 45.470 63.146 1.00 92.61 ? 927 ASN A O 1 ATOM 6960 C CB . ASN A 1 927 ? -39.459 44.290 65.201 1.00 73.61 ? 927 ASN A CB 1 ATOM 6961 C CG . ASN A 1 927 ? -40.869 44.665 64.783 1.00 87.11 ? 927 ASN A CG 1 ATOM 6962 O OD1 . ASN A 1 927 ? -41.452 44.042 63.896 1.00 91.75 ? 927 ASN A OD1 1 ATOM 6963 N ND2 . ASN A 1 927 ? -41.424 45.688 65.424 1.00 96.26 ? 927 ASN A ND2 1 ATOM 6964 N N . VAL A 1 928 ? -38.982 44.398 61.813 1.00 65.72 ? 928 VAL A N 1 ATOM 6965 C CA . VAL A 1 928 ? -38.741 45.278 60.674 1.00 66.05 ? 928 VAL A CA 1 ATOM 6966 C C . VAL A 1 928 ? -39.709 46.451 60.722 1.00 71.31 ? 928 VAL A C 1 ATOM 6967 O O . VAL A 1 928 ? -40.918 46.276 60.570 1.00 82.60 ? 928 VAL A O 1 ATOM 6968 C CB . VAL A 1 928 ? -38.893 44.532 59.336 1.00 68.91 ? 928 VAL A CB 1 ATOM 6969 C CG1 . VAL A 1 928 ? -38.751 45.498 58.175 1.00 71.84 ? 928 VAL A CG1 1 ATOM 6970 C CG2 . VAL A 1 928 ? -37.866 43.417 59.233 1.00 67.56 ? 928 VAL A CG2 1 ATOM 6971 N N . ILE A 1 929 ? -39.169 47.646 60.936 1.00 67.28 ? 929 ILE A N 1 ATOM 6972 C CA . ILE A 1 929 ? -39.998 48.802 61.258 1.00 77.05 ? 929 ILE A CA 1 ATOM 6973 C C . ILE A 1 929 ? -40.424 49.662 60.063 1.00 82.36 ? 929 ILE A C 1 ATOM 6974 O O . ILE A 1 929 ? -41.315 50.502 60.207 1.00 112.61 ? 929 ILE A O 1 ATOM 6975 C CB . ILE A 1 929 ? -39.280 49.704 62.275 1.00 71.25 ? 929 ILE A CB 1 ATOM 6976 C CG1 . ILE A 1 929 ? -37.973 50.237 61.692 1.00 94.65 ? 929 ILE A CG1 1 ATOM 6977 C CG2 . ILE A 1 929 ? -38.994 48.931 63.549 1.00 69.11 ? 929 ILE A CG2 1 ATOM 6978 C CD1 . ILE A 1 929 ? -37.158 51.054 62.670 1.00 88.71 ? 929 ILE A CD1 1 ATOM 6979 N N . GLU A 1 930 ? -39.829 49.431 58.892 1.00 75.22 ? 930 GLU A N 1 ATOM 6980 C CA . GLU A 1 930 ? -40.175 50.192 57.685 1.00 111.00 ? 930 GLU A CA 1 ATOM 6981 C C . GLU A 1 930 ? -39.441 49.712 56.434 1.00 101.71 ? 930 GLU A C 1 ATOM 6982 O O . GLU A 1 930 ? -38.456 48.977 56.513 1.00 78.36 ? 930 GLU A O 1 ATOM 6983 C CB . GLU A 1 930 ? -39.898 51.690 57.881 1.00 123.38 ? 930 GLU A CB 1 ATOM 6984 C CG . GLU A 1 930 ? -38.436 52.056 58.050 1.00 119.19 ? 930 GLU A CG 1 ATOM 6985 C CD . GLU A 1 930 ? -38.227 53.554 58.181 1.00 137.74 ? 930 GLU A CD 1 ATOM 6986 O OE1 . GLU A 1 930 ? -38.938 54.187 58.991 1.00 131.66 ? 930 GLU A OE1 1 ATOM 6987 O OE2 . GLU A 1 930 ? -37.357 54.101 57.471 1.00 139.15 ? 930 GLU A OE2 1 ATOM 6988 N N . PHE A 1 931 ? -39.935 50.150 55.278 1.00 106.54 ? 931 PHE A N 1 ATOM 6989 C CA . PHE A 1 931 ? -39.428 49.708 53.983 1.00 83.63 ? 931 PHE A CA 1 ATOM 6990 C C . PHE A 1 931 ? -39.159 50.905 53.069 1.00 94.18 ? 931 PHE A C 1 ATOM 6991 O O . PHE A 1 931 ? -39.766 51.963 53.239 1.00 109.13 ? 931 PHE A O 1 ATOM 6992 C CB . PHE A 1 931 ? -40.426 48.750 53.327 1.00 84.43 ? 931 PHE A CB 1 ATOM 6993 C CG . PHE A 1 931 ? -40.725 47.525 54.147 1.00 82.92 ? 931 PHE A CG 1 ATOM 6994 C CD1 . PHE A 1 931 ? -40.030 46.348 53.933 1.00 83.27 ? 931 PHE A CD1 1 ATOM 6995 C CD2 . PHE A 1 931 ? -41.704 47.549 55.128 1.00 83.17 ? 931 PHE A CD2 1 ATOM 6996 C CE1 . PHE A 1 931 ? -40.302 45.220 54.682 1.00 82.78 ? 931 PHE A CE1 1 ATOM 6997 C CE2 . PHE A 1 931 ? -41.981 46.424 55.881 1.00 91.27 ? 931 PHE A CE2 1 ATOM 6998 C CZ . PHE A 1 931 ? -41.279 45.259 55.658 1.00 83.06 ? 931 PHE A CZ 1 ATOM 6999 N N . PRO A 1 932 ? -38.244 50.746 52.096 1.00 88.75 ? 932 PRO A N 1 ATOM 7000 C CA . PRO A 1 932 ? -37.942 51.824 51.145 1.00 95.48 ? 932 PRO A CA 1 ATOM 7001 C C . PRO A 1 932 ? -39.095 52.120 50.189 1.00 100.24 ? 932 PRO A C 1 ATOM 7002 O O . PRO A 1 932 ? -39.101 53.170 49.548 1.00 116.20 ? 932 PRO A O 1 ATOM 7003 C CB . PRO A 1 932 ? -36.731 51.284 50.377 1.00 93.67 ? 932 PRO A CB 1 ATOM 7004 C CG . PRO A 1 932 ? -36.845 49.808 50.491 1.00 90.25 ? 932 PRO A CG 1 ATOM 7005 C CD . PRO A 1 932 ? -37.397 49.564 51.864 1.00 86.25 ? 932 PRO A CD 1 ATOM 7006 N N . TYR A 1 933 ? -40.052 51.204 50.094 1.00 95.00 ? 933 TYR A N 1 ATOM 7007 C CA . TYR A 1 933 ? -41.155 51.353 49.153 1.00 100.03 ? 933 TYR A CA 1 ATOM 7008 C C . TYR A 1 933 ? -42.331 52.085 49.793 1.00 98.00 ? 933 TYR A C 1 ATOM 7009 O O . TYR A 1 933 ? -42.959 51.585 50.726 1.00 110.88 ? 933 TYR A O 1 ATOM 7010 C CB . TYR A 1 933 ? -41.599 49.984 48.635 1.00 103.20 ? 933 TYR A CB 1 ATOM 7011 C CG . TYR A 1 933 ? -40.453 49.020 48.423 1.00 98.74 ? 933 TYR A CG 1 ATOM 7012 C CD1 . TYR A 1 933 ? -39.618 49.134 47.321 1.00 102.43 ? 933 TYR A CD1 1 ATOM 7013 C CD2 . TYR A 1 933 ? -40.203 48.000 49.332 1.00 96.52 ? 933 TYR A CD2 1 ATOM 7014 C CE1 . TYR A 1 933 ? -38.566 48.256 47.126 1.00 105.05 ? 933 TYR A CE1 1 ATOM 7015 C CE2 . TYR A 1 933 ? -39.155 47.118 49.146 1.00 101.79 ? 933 TYR A CE2 1 ATOM 7016 C CZ . TYR A 1 933 ? -38.340 47.250 48.042 1.00 105.01 ? 933 TYR A CZ 1 ATOM 7017 O OH . TYR A 1 933 ? -37.295 46.373 47.855 1.00 111.31 ? 933 TYR A OH 1 ATOM 7018 N N . LYS A 1 934 ? -42.623 53.273 49.274 1.00 103.09 ? 934 LYS A N 1 ATOM 7019 C CA . LYS A 1 934 ? -43.672 54.124 49.826 1.00 126.34 ? 934 LYS A CA 1 ATOM 7020 C C . LYS A 1 934 ? -44.984 53.984 49.059 1.00 133.43 ? 934 LYS A C 1 ATOM 7021 O O . LYS A 1 934 ? -44.984 53.782 47.844 1.00 137.16 ? 934 LYS A O 1 ATOM 7022 C CB . LYS A 1 934 ? -43.218 55.584 49.837 1.00 137.80 ? 934 LYS A CB 1 ATOM 7023 C CG . LYS A 1 934 ? -41.991 55.832 50.700 1.00 137.57 ? 934 LYS A CG 1 ATOM 7024 C CD . LYS A 1 934 ? -42.178 55.246 52.091 1.00 121.84 ? 934 LYS A CD 1 ATOM 7025 C CE . LYS A 1 934 ? -40.908 55.356 52.918 1.00 118.20 ? 934 LYS A CE 1 ATOM 7026 N NZ . LYS A 1 934 ? -41.071 54.737 54.262 1.00 125.15 ? 934 LYS A NZ 1 ATOM 7027 N N . ASN A 1 935 ? -46.091 54.084 49.794 1.00 130.55 ? 935 ASN A N 1 ATOM 7028 C CA . ASN A 1 935 ? -47.445 53.931 49.259 1.00 139.05 ? 935 ASN A CA 1 ATOM 7029 C C . ASN A 1 935 ? -47.704 52.524 48.732 1.00 134.81 ? 935 ASN A C 1 ATOM 7030 O O . ASN A 1 935 ? -48.451 52.333 47.773 1.00 132.08 ? 935 ASN A O 1 ATOM 7031 C CB . ASN A 1 935 ? -47.721 54.964 48.162 1.00 140.30 ? 935 ASN A CB 1 ATOM 7032 C CG . ASN A 1 935 ? -47.581 56.389 48.657 1.00 144.61 ? 935 ASN A CG 1 ATOM 7033 O OD1 . ASN A 1 935 ? -46.521 57.001 48.527 1.00 149.50 ? 935 ASN A OD1 1 ATOM 7034 N ND2 . ASN A 1 935 ? -48.652 56.925 49.230 1.00 143.42 ? 935 ASN A ND2 1 ATOM 7035 N N . LEU A 1 936 ? -47.075 51.543 49.370 1.00 132.61 ? 936 LEU A N 1 ATOM 7036 C CA . LEU A 1 936 ? -47.358 50.137 49.107 1.00 123.37 ? 936 LEU A CA 1 ATOM 7037 C C . LEU A 1 936 ? -47.733 49.444 50.412 1.00 108.77 ? 936 LEU A C 1 ATOM 7038 O O . LEU A 1 936 ? -47.169 49.755 51.462 1.00 101.91 ? 936 LEU A O 1 ATOM 7039 C CB . LEU A 1 936 ? -46.157 49.443 48.458 1.00 115.79 ? 936 LEU A CB 1 ATOM 7040 C CG . LEU A 1 936 ? -46.008 49.540 46.936 1.00 125.68 ? 936 LEU A CG 1 ATOM 7041 C CD1 . LEU A 1 936 ? -45.510 50.911 46.507 1.00 141.17 ? 936 LEU A CD1 1 ATOM 7042 C CD2 . LEU A 1 936 ? -45.085 48.448 46.417 1.00 130.88 ? 936 LEU A CD2 1 ATOM 7043 N N . PRO A 1 937 ? -48.691 48.506 50.353 1.00 120.87 ? 937 PRO A N 1 ATOM 7044 C CA . PRO A 1 937 ? -49.114 47.789 51.562 1.00 129.33 ? 937 PRO A CA 1 ATOM 7045 C C . PRO A 1 937 ? -47.970 46.986 52.173 1.00 135.36 ? 937 PRO A C 1 ATOM 7046 O O . PRO A 1 937 ? -47.306 46.220 51.475 1.00 112.10 ? 937 PRO A O 1 ATOM 7047 C CB . PRO A 1 937 ? -50.229 46.866 51.055 1.00 126.18 ? 937 PRO A CB 1 ATOM 7048 C CG . PRO A 1 937 ? -49.981 46.733 49.588 1.00 129.78 ? 937 PRO A CG 1 ATOM 7049 C CD . PRO A 1 937 ? -49.417 48.050 49.156 1.00 130.51 ? 937 PRO A CD 1 ATOM 7050 N N . ILE A 1 938 ? -47.753 47.162 53.472 1.00 143.93 ? 938 ILE A N 1 ATOM 7051 C CA . ILE A 1 938 ? -46.631 46.522 54.145 1.00 132.81 ? 938 ILE A CA 1 ATOM 7052 C C . ILE A 1 938 ? -47.046 45.878 55.465 1.00 134.64 ? 938 ILE A C 1 ATOM 7053 O O . ILE A 1 938 ? -47.520 46.550 56.381 1.00 146.74 ? 938 ILE A O 1 ATOM 7054 C CB . ILE A 1 938 ? -45.491 47.532 54.396 1.00 124.19 ? 938 ILE A CB 1 ATOM 7055 C CG1 . ILE A 1 938 ? -46.058 48.906 54.764 1.00 103.71 ? 938 ILE A CG1 1 ATOM 7056 C CG2 . ILE A 1 938 ? -44.624 47.664 53.158 1.00 128.59 ? 938 ILE A CG2 1 ATOM 7057 C CD1 . ILE A 1 938 ? -45.874 49.286 56.219 1.00 92.41 ? 938 ILE A CD1 1 ATOM 7058 N N . GLU A 1 939 ? -46.869 44.563 55.548 1.00 128.56 ? 939 GLU A N 1 ATOM 7059 C CA . GLU A 1 939 ? -47.177 43.823 56.765 1.00 135.44 ? 939 GLU A CA 1 ATOM 7060 C C . GLU A 1 939 ? -45.960 43.783 57.679 1.00 131.65 ? 939 GLU A C 1 ATOM 7061 O O . GLU A 1 939 ? -44.828 43.663 57.211 1.00 120.00 ? 939 GLU A O 1 ATOM 7062 C CB . GLU A 1 939 ? -47.646 42.406 56.431 1.00 140.86 ? 939 GLU A CB 1 ATOM 7063 C CG . GLU A 1 939 ? -48.893 42.360 55.563 1.00 143.42 ? 939 GLU A CG 1 ATOM 7064 C CD . GLU A 1 939 ? -49.378 40.946 55.308 1.00 152.15 ? 939 GLU A CD 1 ATOM 7065 O OE1 . GLU A 1 939 ? -50.250 40.765 54.433 1.00 150.80 ? 939 GLU A OE1 1 ATOM 7066 O OE2 . GLU A 1 939 ? -48.888 40.017 55.984 1.00 157.25 ? 939 GLU A OE2 1 ATOM 7067 N N . ASP A 1 940 ? -46.197 43.886 58.982 1.00 136.03 ? 940 ASP A N 1 ATOM 7068 C CA . ASP A 1 940 ? -45.110 43.933 59.951 1.00 134.65 ? 940 ASP A CA 1 ATOM 7069 C C . ASP A 1 940 ? -44.407 42.582 60.057 1.00 109.52 ? 940 ASP A C 1 ATOM 7070 O O . ASP A 1 940 ? -45.048 41.551 60.267 1.00 96.86 ? 940 ASP A O 1 ATOM 7071 C CB . ASP A 1 940 ? -45.635 44.368 61.320 1.00 147.62 ? 940 ASP A CB 1 ATOM 7072 C CG . ASP A 1 940 ? -44.645 45.234 62.073 1.00 148.31 ? 940 ASP A CG 1 ATOM 7073 O OD1 . ASP A 1 940 ? -43.425 45.024 61.909 1.00 138.26 ? 940 ASP A OD1 1 ATOM 7074 O OD2 . ASP A 1 940 ? -45.090 46.129 62.821 1.00 144.20 ? 940 ASP A OD2 1 ATOM 7075 N N . ILE A 1 941 ? -43.087 42.595 59.908 1.00 94.89 ? 941 ILE A N 1 ATOM 7076 C CA . ILE A 1 941 ? -42.296 41.371 59.938 1.00 83.75 ? 941 ILE A CA 1 ATOM 7077 C C . ILE A 1 941 ? -41.535 41.225 61.250 1.00 91.23 ? 941 ILE A C 1 ATOM 7078 O O . ILE A 1 941 ? -40.687 42.053 61.582 1.00 106.46 ? 941 ILE A O 1 ATOM 7079 C CB . ILE A 1 941 ? -41.293 41.324 58.773 1.00 81.24 ? 941 ILE A CB 1 ATOM 7080 C CG1 . ILE A 1 941 ? -42.028 41.427 57.436 1.00 85.99 ? 941 ILE A CG1 1 ATOM 7081 C CG2 . ILE A 1 941 ? -40.463 40.051 58.835 1.00 80.41 ? 941 ILE A CG2 1 ATOM 7082 C CD1 . ILE A 1 941 ? -41.112 41.563 56.243 1.00 85.14 ? 941 ILE A CD1 1 ATOM 7083 N N . THR A 1 942 ? -41.844 40.166 61.993 1.00 99.70 ? 942 THR A N 1 ATOM 7084 C CA . THR A 1 942 ? -41.172 39.899 63.260 1.00 101.16 ? 942 THR A CA 1 ATOM 7085 C C . THR A 1 942 ? -41.017 38.402 63.509 1.00 100.99 ? 942 THR A C 1 ATOM 7086 O O . THR A 1 942 ? -41.804 37.595 63.010 1.00 119.95 ? 942 THR A O 1 ATOM 7087 C CB . THR A 1 942 ? -41.928 40.528 64.447 1.00 105.26 ? 942 THR A CB 1 ATOM 7088 O OG1 . THR A 1 942 ? -41.261 40.194 65.670 1.00 117.48 ? 942 THR A OG1 1 ATOM 7089 C CG2 . THR A 1 942 ? -43.360 40.016 64.502 1.00 96.98 ? 942 THR A CG2 1 ATOM 7090 N N . ASN A 1 943 ? -40.007 38.052 64.303 1.00 88.95 ? 943 ASN A N 1 ATOM 7091 C CA . ASN A 1 943 ? -39.692 36.663 64.626 1.00 80.47 ? 943 ASN A CA 1 ATOM 7092 C C . ASN A 1 943 ? -38.533 36.602 65.617 1.00 76.83 ? 943 ASN A C 1 ATOM 7093 O O . ASN A 1 943 ? -37.819 37.587 65.805 1.00 81.98 ? 943 ASN A O 1 ATOM 7094 C CB . ASN A 1 943 ? -39.343 35.874 63.362 1.00 81.91 ? 943 ASN A CB 1 ATOM 7095 C CG . ASN A 1 943 ? -39.792 34.429 63.430 1.00 107.17 ? 943 ASN A CG 1 ATOM 7096 O OD1 . ASN A 1 943 ? -39.128 33.588 64.037 1.00 121.66 ? 943 ASN A OD1 1 ATOM 7097 N ND2 . ASN A 1 943 ? -40.925 34.130 62.799 1.00 137.50 ? 943 ASN A ND2 1 ATOM 7098 N N . SER A 1 944 ? -38.343 35.446 66.245 1.00 80.81 ? 944 SER A N 1 ATOM 7099 C CA . SER A 1 944 ? -37.323 35.310 67.280 1.00 79.65 ? 944 SER A CA 1 ATOM 7100 C C . SER A 1 944 ? -36.651 33.939 67.264 1.00 77.14 ? 944 SER A C 1 ATOM 7101 O O . SER A 1 944 ? -37.157 32.991 66.663 1.00 101.17 ? 944 SER A O 1 ATOM 7102 C CB . SER A 1 944 ? -37.934 35.569 68.659 1.00 89.14 ? 944 SER A CB 1 ATOM 7103 O OG . SER A 1 944 ? -36.985 35.350 69.688 1.00 111.64 ? 944 SER A OG 1 ATOM 7104 N N . THR A 1 945 ? -35.504 33.849 67.931 1.00 70.03 ? 945 THR A N 1 ATOM 7105 C CA . THR A 1 945 ? -34.776 32.591 68.063 1.00 75.27 ? 945 THR A CA 1 ATOM 7106 C C . THR A 1 945 ? -33.905 32.622 69.316 1.00 75.76 ? 945 THR A C 1 ATOM 7107 O O . THR A 1 945 ? -33.643 33.690 69.871 1.00 97.12 ? 945 THR A O 1 ATOM 7108 C CB . THR A 1 945 ? -33.898 32.306 66.831 1.00 75.87 ? 945 THR A CB 1 ATOM 7109 O OG1 . THR A 1 945 ? -33.441 30.949 66.870 1.00 101.87 ? 945 THR A OG1 1 ATOM 7110 C CG2 . THR A 1 945 ? -32.699 33.245 66.798 1.00 65.69 ? 945 THR A CG2 1 ATOM 7111 N N . LEU A 1 946 ? -33.462 31.451 69.763 1.00 70.34 ? 946 LEU A N 1 ATOM 7112 C CA . LEU A 1 946 ? -32.636 31.362 70.962 1.00 81.44 ? 946 LEU A CA 1 ATOM 7113 C C . LEU A 1 946 ? -31.385 30.516 70.735 1.00 81.04 ? 946 LEU A C 1 ATOM 7114 O O . LEU A 1 946 ? -31.381 29.599 69.914 1.00 80.27 ? 946 LEU A O 1 ATOM 7115 C CB . LEU A 1 946 ? -33.455 30.798 72.131 1.00 91.20 ? 946 LEU A CB 1 ATOM 7116 C CG . LEU A 1 946 ? -34.257 29.508 71.925 1.00 84.86 ? 946 LEU A CG 1 ATOM 7117 C CD1 . LEU A 1 946 ? -33.409 28.268 72.176 1.00 101.43 ? 946 LEU A CD1 1 ATOM 7118 C CD2 . LEU A 1 946 ? -35.494 29.500 72.814 1.00 89.19 ? 946 LEU A CD2 1 ATOM 7119 N N . VAL A 1 947 ? -30.324 30.836 71.470 1.00 76.39 ? 947 VAL A N 1 ATOM 7120 C CA . VAL A 1 947 ? -29.074 30.091 71.396 1.00 66.72 ? 947 VAL A CA 1 ATOM 7121 C C . VAL A 1 947 ? -28.717 29.524 72.765 1.00 68.98 ? 947 VAL A C 1 ATOM 7122 O O . VAL A 1 947 ? -28.621 30.263 73.747 1.00 72.66 ? 947 VAL A O 1 ATOM 7123 C CB . VAL A 1 947 ? -27.916 30.972 70.886 1.00 60.31 ? 947 VAL A CB 1 ATOM 7124 C CG1 . VAL A 1 947 ? -26.583 30.266 71.072 1.00 61.48 ? 947 VAL A CG1 1 ATOM 7125 C CG2 . VAL A 1 947 ? -28.135 31.332 69.430 1.00 58.83 ? 947 VAL A CG2 1 ATOM 7126 N N . THR A 1 948 ? -28.521 28.211 72.826 1.00 72.61 ? 948 THR A N 1 ATOM 7127 C CA . THR A 1 948 ? -28.274 27.535 74.094 1.00 79.40 ? 948 THR A CA 1 ATOM 7128 C C . THR A 1 948 ? -26.845 27.011 74.226 1.00 100.35 ? 948 THR A C 1 ATOM 7129 O O . THR A 1 948 ? -26.325 26.346 73.330 1.00 107.77 ? 948 THR A O 1 ATOM 7130 C CB . THR A 1 948 ? -29.252 26.359 74.293 1.00 92.26 ? 948 THR A CB 1 ATOM 7131 O OG1 . THR A 1 948 ? -28.800 25.538 75.376 1.00 128.09 ? 948 THR A OG1 1 ATOM 7132 C CG2 . THR A 1 948 ? -29.346 25.515 73.027 1.00 84.96 ? 948 THR A CG2 1 ATOM 7133 N N . THR A 1 949 ? -26.216 27.326 75.354 1.00 103.78 ? 949 THR A N 1 ATOM 7134 C CA . THR A 1 949 ? -24.906 26.778 75.684 1.00 99.28 ? 949 THR A CA 1 ATOM 7135 C C . THR A 1 949 ? -25.020 25.892 76.920 1.00 93.84 ? 949 THR A C 1 ATOM 7136 O O . THR A 1 949 ? -25.258 26.381 78.024 1.00 106.52 ? 949 THR A O 1 ATOM 7137 C CB . THR A 1 949 ? -23.871 27.890 75.935 1.00 92.60 ? 949 THR A CB 1 ATOM 7138 O OG1 . THR A 1 949 ? -23.705 28.668 74.744 1.00 104.35 ? 949 THR A OG1 1 ATOM 7139 C CG2 . THR A 1 949 ? -22.531 27.291 76.331 1.00 73.76 ? 949 THR A CG2 1 ATOM 7140 N N . ASN A 1 950 ? -24.853 24.587 76.731 1.00 86.12 ? 950 ASN A N 1 ATOM 7141 C CA . ASN A 1 950 ? -25.049 23.633 77.816 1.00 83.34 ? 950 ASN A CA 1 ATOM 7142 C C . ASN A 1 950 ? -23.747 23.276 78.527 1.00 95.35 ? 950 ASN A C 1 ATOM 7143 O O . ASN A 1 950 ? -22.866 22.641 77.951 1.00 124.81 ? 950 ASN A O 1 ATOM 7144 C CB . ASN A 1 950 ? -25.718 22.361 77.287 1.00 86.96 ? 950 ASN A CB 1 ATOM 7145 C CG . ASN A 1 950 ? -27.090 22.625 76.691 1.00 102.91 ? 950 ASN A CG 1 ATOM 7146 O OD1 . ASN A 1 950 ? -27.457 23.770 76.428 1.00 111.39 ? 950 ASN A OD1 1 ATOM 7147 N ND2 . ASN A 1 950 ? -27.856 21.559 76.472 1.00 134.71 ? 950 ASN A ND2 1 ATOM 7148 N N . VAL A 1 951 ? -23.637 23.687 79.786 1.00 91.28 ? 951 VAL A N 1 ATOM 7149 C CA . VAL A 1 951 ? -22.466 23.379 80.600 1.00 89.67 ? 951 VAL A CA 1 ATOM 7150 C C . VAL A 1 951 ? -22.802 22.295 81.624 1.00 94.46 ? 951 VAL A C 1 ATOM 7151 O O . VAL A 1 951 ? -23.771 22.415 82.374 1.00 95.43 ? 951 VAL A O 1 ATOM 7152 C CB . VAL A 1 951 ? -21.928 24.642 81.311 1.00 88.36 ? 951 VAL A CB 1 ATOM 7153 C CG1 . VAL A 1 951 ? -23.070 25.462 81.894 1.00 104.48 ? 951 VAL A CG1 1 ATOM 7154 C CG2 . VAL A 1 951 ? -20.918 24.269 82.385 1.00 96.13 ? 951 VAL A CG2 1 ATOM 7155 N N . THR A 1 952 ? -22.002 21.232 81.645 1.00 102.48 ? 952 THR A N 1 ATOM 7156 C CA . THR A 1 952 ? -22.285 20.084 82.500 1.00 103.04 ? 952 THR A CA 1 ATOM 7157 C C . THR A 1 952 ? -21.028 19.307 82.883 1.00 115.54 ? 952 THR A C 1 ATOM 7158 O O . THR A 1 952 ? -19.973 19.465 82.267 1.00 132.52 ? 952 THR A O 1 ATOM 7159 C CB . THR A 1 952 ? -23.269 19.115 81.820 1.00 108.16 ? 952 THR A CB 1 ATOM 7160 O OG1 . THR A 1 952 ? -23.456 17.962 82.650 1.00 147.23 ? 952 THR A OG1 1 ATOM 7161 C CG2 . THR A 1 952 ? -22.732 18.676 80.465 1.00 103.22 ? 952 THR A CG2 1 ATOM 7162 N N . TRP A 1 953 ? -21.154 18.469 83.908 1.00 112.10 ? 953 TRP A N 1 ATOM 7163 C CA . TRP A 1 953 ? -20.063 17.606 84.349 1.00 126.14 ? 953 TRP A CA 1 ATOM 7164 C C . TRP A 1 953 ? -20.140 16.241 83.674 1.00 137.90 ? 953 TRP A C 1 ATOM 7165 O O . TRP A 1 953 ? -21.210 15.639 83.598 1.00 140.30 ? 953 TRP A O 1 ATOM 7166 C CB . TRP A 1 953 ? -20.093 17.433 85.868 1.00 135.39 ? 953 TRP A CB 1 ATOM 7167 C CG . TRP A 1 953 ? -19.885 18.703 86.629 1.00 137.30 ? 953 TRP A CG 1 ATOM 7168 C CD1 . TRP A 1 953 ? -20.786 19.714 86.798 1.00 124.93 ? 953 TRP A CD1 1 ATOM 7169 C CD2 . TRP A 1 953 ? -18.704 19.094 87.338 1.00 142.13 ? 953 TRP A CD2 1 ATOM 7170 N NE1 . TRP A 1 953 ? -20.237 20.713 87.564 1.00 120.31 ? 953 TRP A NE1 1 ATOM 7171 C CE2 . TRP A 1 953 ? -18.959 20.357 87.908 1.00 125.31 ? 953 TRP A CE2 1 ATOM 7172 C CE3 . TRP A 1 953 ? -17.455 18.501 87.543 1.00 147.86 ? 953 TRP A CE3 1 ATOM 7173 C CZ2 . TRP A 1 953 ? -18.011 21.038 88.668 1.00 122.12 ? 953 TRP A CZ2 1 ATOM 7174 C CZ3 . TRP A 1 953 ? -16.516 19.178 88.299 1.00 143.20 ? 953 TRP A CZ3 1 ATOM 7175 C CH2 . TRP A 1 953 ? -16.798 20.433 88.852 1.00 135.20 ? 953 TRP A CH2 1 ATOM 7176 N N . GLY A 1 954 ? -19.003 15.757 83.185 1.00 142.89 ? 954 GLY A N 1 ATOM 7177 C CA . GLY A 1 954 ? -18.943 14.455 82.546 1.00 133.89 ? 954 GLY A CA 1 ATOM 7178 C C . GLY A 1 954 ? -18.696 13.323 83.525 1.00 148.77 ? 954 GLY A C 1 ATOM 7179 O O . GLY A 1 954 ? -19.081 12.180 83.277 1.00 164.00 ? 954 GLY A O 1 ATOM 7180 N N . ILE A 1 955 ? -18.051 13.645 84.642 1.00 159.47 ? 955 ILE A N 1 ATOM 7181 C CA . ILE A 1 955 ? -17.692 12.645 85.643 1.00 175.47 ? 955 ILE A CA 1 ATOM 7182 C C . ILE A 1 955 ? -18.763 12.546 86.730 1.00 181.01 ? 955 ILE A C 1 ATOM 7183 O O . ILE A 1 955 ? -18.596 11.832 87.719 1.00 185.39 ? 955 ILE A O 1 ATOM 7184 C CB . ILE A 1 955 ? -16.326 12.963 86.286 1.00 169.49 ? 955 ILE A CB 1 ATOM 7185 C CG1 . ILE A 1 955 ? -15.426 13.697 85.290 1.00 162.60 ? 955 ILE A CG1 1 ATOM 7186 C CG2 . ILE A 1 955 ? -15.648 11.690 86.779 1.00 162.16 ? 955 ILE A CG2 1 ATOM 7187 C CD1 . ILE A 1 955 ? -14.041 13.993 85.819 1.00 149.85 ? 955 ILE A CD1 1 ATOM 7188 N N . GLN A 1 956 ? -19.857 13.278 86.538 1.00 169.09 ? 956 GLN A N 1 ATOM 7189 C CA . GLN A 1 956 ? -20.960 13.307 87.497 1.00 160.44 ? 956 GLN A CA 1 ATOM 7190 C C . GLN A 1 956 ? -21.487 11.910 87.826 1.00 178.47 ? 956 GLN A C 1 ATOM 7191 O O . GLN A 1 956 ? -21.361 10.980 87.029 1.00 180.28 ? 956 GLN A O 1 ATOM 7192 C CB . GLN A 1 956 ? -22.103 14.171 86.963 1.00 139.78 ? 956 GLN A CB 1 ATOM 7193 C CG . GLN A 1 956 ? -22.795 13.589 85.740 1.00 151.54 ? 956 GLN A CG 1 ATOM 7194 C CD . GLN A 1 956 ? -23.932 14.459 85.246 1.00 177.87 ? 956 GLN A CD 1 ATOM 7195 O OE1 . GLN A 1 956 ? -24.040 15.629 85.614 1.00 183.75 ? 956 GLN A OE1 1 ATOM 7196 N NE2 . GLN A 1 956 ? -24.792 13.890 84.408 1.00 178.06 ? 956 GLN A NE2 1 ATOM 7197 N N . GLY B 2 1 ? -54.080 7.229 13.047 1.00 180.66 ? 1 GLY B N 1 ATOM 7198 C CA . GLY B 2 1 ? -53.353 7.904 14.106 1.00 187.01 ? 1 GLY B CA 1 ATOM 7199 C C . GLY B 2 1 ? -51.969 8.343 13.670 1.00 185.70 ? 1 GLY B C 1 ATOM 7200 O O . GLY B 2 1 ? -50.991 7.626 13.885 1.00 174.91 ? 1 GLY B O 1 ATOM 7201 N N . PRO B 2 2 ? -51.879 9.529 13.049 1.00 191.84 ? 2 PRO B N 1 ATOM 7202 C CA . PRO B 2 2 ? -50.611 10.098 12.576 1.00 183.56 ? 2 PRO B CA 1 ATOM 7203 C C . PRO B 2 2 ? -49.639 10.385 13.717 1.00 176.68 ? 2 PRO B C 1 ATOM 7204 O O . PRO B 2 2 ? -50.055 10.486 14.872 1.00 174.24 ? 2 PRO B O 1 ATOM 7205 C CB . PRO B 2 2 ? -51.042 11.401 11.892 1.00 188.00 ? 2 PRO B CB 1 ATOM 7206 C CG . PRO B 2 2 ? -52.492 11.216 11.583 1.00 192.30 ? 2 PRO B CG 1 ATOM 7207 C CD . PRO B 2 2 ? -53.026 10.384 12.702 1.00 195.42 ? 2 PRO B CD 1 ATOM 7208 N N . ASN B 2 3 ? -48.357 10.513 13.390 1.00 176.19 ? 3 ASN B N 1 ATOM 7209 C CA . ASN B 2 3 ? -47.344 10.839 14.387 1.00 172.68 ? 3 ASN B CA 1 ATOM 7210 C C . ASN B 2 3 ? -46.239 11.717 13.808 1.00 166.83 ? 3 ASN B C 1 ATOM 7211 O O . ASN B 2 3 ? -46.352 12.218 12.689 1.00 163.75 ? 3 ASN B O 1 ATOM 7212 C CB . ASN B 2 3 ? -46.744 9.563 14.985 1.00 170.94 ? 3 ASN B CB 1 ATOM 7213 C CG . ASN B 2 3 ? -46.091 8.678 13.942 1.00 172.99 ? 3 ASN B CG 1 ATOM 7214 O OD1 . ASN B 2 3 ? -44.988 8.959 13.474 1.00 163.62 ? 3 ASN B OD1 1 ATOM 7215 N ND2 . ASN B 2 3 ? -46.765 7.591 13.583 1.00 183.69 ? 3 ASN B ND2 1 ATOM 7216 N N . ILE B 2 4 ? -45.177 11.900 14.584 1.00 166.27 ? 4 ILE B N 1 ATOM 7217 C CA . ILE B 2 4 ? -44.077 12.782 14.211 1.00 165.51 ? 4 ILE B CA 1 ATOM 7218 C C . ILE B 2 4 ? -43.335 12.284 12.969 1.00 159.39 ? 4 ILE B C 1 ATOM 7219 O O . ILE B 2 4 ? -42.983 13.071 12.089 1.00 159.72 ? 4 ILE B O 1 ATOM 7220 C CB . ILE B 2 4 ? -43.068 12.940 15.374 1.00 153.69 ? 4 ILE B CB 1 ATOM 7221 C CG1 . ILE B 2 4 ? -43.774 13.431 16.642 1.00 162.62 ? 4 ILE B CG1 1 ATOM 7222 C CG2 . ILE B 2 4 ? -41.952 13.896 14.997 1.00 142.74 ? 4 ILE B CG2 1 ATOM 7223 C CD1 . ILE B 2 4 ? -44.172 12.326 17.601 1.00 163.09 ? 4 ILE B CD1 1 ATOM 7224 N N . CYS B 2 5 ? -43.109 10.976 12.902 1.00 155.69 ? 5 CYS B N 1 ATOM 7225 C CA . CYS B 2 5 ? -42.381 10.378 11.786 1.00 155.34 ? 5 CYS B CA 1 ATOM 7226 C C . CYS B 2 5 ? -43.156 10.486 10.475 1.00 157.41 ? 5 CYS B C 1 ATOM 7227 O O . CYS B 2 5 ? -42.564 10.614 9.403 1.00 156.16 ? 5 CYS B O 1 ATOM 7228 C CB . CYS B 2 5 ? -42.066 8.909 12.081 1.00 156.58 ? 5 CYS B CB 1 ATOM 7229 S SG . CYS B 2 5 ? -41.070 8.633 13.564 1.00 185.06 ? 5 CYS B SG 1 ATOM 7230 N N . THR B 2 6 ? -44.481 10.433 10.569 1.00 158.81 ? 6 THR B N 1 ATOM 7231 C CA . THR B 2 6 ? -45.339 10.463 9.390 1.00 163.16 ? 6 THR B CA 1 ATOM 7232 C C . THR B 2 6 ? -45.277 11.799 8.660 1.00 163.89 ? 6 THR B C 1 ATOM 7233 O O . THR B 2 6 ? -45.095 11.844 7.444 1.00 169.23 ? 6 THR B O 1 ATOM 7234 C CB . THR B 2 6 ? -46.808 10.182 9.756 1.00 171.66 ? 6 THR B CB 1 ATOM 7235 O OG1 . THR B 2 6 ? -47.328 11.271 10.530 1.00 178.46 ? 6 THR B OG1 1 ATOM 7236 C CG2 . THR B 2 6 ? -46.922 8.898 10.553 1.00 172.02 ? 6 THR B CG2 1 ATOM 7237 N N . THR B 2 7 ? -45.431 12.883 9.412 1.00 159.77 ? 7 THR B N 1 ATOM 7238 C CA . THR B 2 7 ? -45.532 14.219 8.835 1.00 149.87 ? 7 THR B CA 1 ATOM 7239 C C . THR B 2 7 ? -44.220 14.718 8.232 1.00 146.73 ? 7 THR B C 1 ATOM 7240 O O . THR B 2 7 ? -44.178 15.136 7.076 1.00 147.88 ? 7 THR B O 1 ATOM 7241 C CB . THR B 2 7 ? -46.005 15.238 9.888 1.00 142.36 ? 7 THR B CB 1 ATOM 7242 O OG1 . THR B 2 7 ? -45.061 15.288 10.965 1.00 139.66 ? 7 THR B OG1 1 ATOM 7243 C CG2 . THR B 2 7 ? -47.369 14.845 10.436 1.00 143.60 ? 7 THR B CG2 1 ATOM 7244 N N . ARG B 2 8 ? -43.151 14.674 9.018 1.00 150.67 ? 8 ARG B N 1 ATOM 7245 C CA . ARG B 2 8 ? -41.876 15.258 8.611 1.00 150.56 ? 8 ARG B CA 1 ATOM 7246 C C . ARG B 2 8 ? -41.063 14.361 7.676 1.00 156.76 ? 8 ARG B C 1 ATOM 7247 O O . ARG B 2 8 ? -40.159 14.835 6.988 1.00 160.72 ? 8 ARG B O 1 ATOM 7248 C CB . ARG B 2 8 ? -41.046 15.605 9.849 1.00 130.78 ? 8 ARG B CB 1 ATOM 7249 C CG . ARG B 2 8 ? -41.667 16.685 10.723 1.00 132.92 ? 8 ARG B CG 1 ATOM 7250 C CD . ARG B 2 8 ? -40.972 16.784 12.072 1.00 139.30 ? 8 ARG B CD 1 ATOM 7251 N NE . ARG B 2 8 ? -41.518 17.864 12.890 1.00 152.68 ? 8 ARG B NE 1 ATOM 7252 C CZ . ARG B 2 8 ? -42.622 17.762 13.622 1.00 167.97 ? 8 ARG B CZ 1 ATOM 7253 N NH1 . ARG B 2 8 ? -43.308 16.627 13.638 1.00 170.76 ? 8 ARG B NH1 1 ATOM 7254 N NH2 . ARG B 2 8 ? -43.045 18.796 14.337 1.00 183.85 ? 8 ARG B NH2 1 ATOM 7255 N N . GLY B 2 9 ? -41.381 13.071 7.651 1.00 155.91 ? 9 GLY B N 1 ATOM 7256 C CA . GLY B 2 9 ? -40.608 12.118 6.872 1.00 157.87 ? 9 GLY B CA 1 ATOM 7257 C C . GLY B 2 9 ? -41.229 11.694 5.554 1.00 161.52 ? 9 GLY B C 1 ATOM 7258 O O . GLY B 2 9 ? -40.858 10.664 4.991 1.00 162.77 ? 9 GLY B O 1 ATOM 7259 N N . VAL B 2 10 ? -42.181 12.485 5.065 1.00 156.00 ? 10 VAL B N 1 ATOM 7260 C CA . VAL B 2 10 ? -42.877 12.190 3.813 1.00 157.39 ? 10 VAL B CA 1 ATOM 7261 C C . VAL B 2 10 ? -41.960 12.081 2.594 1.00 163.96 ? 10 VAL B C 1 ATOM 7262 O O . VAL B 2 10 ? -41.846 11.016 1.987 1.00 170.59 ? 10 VAL B O 1 ATOM 7263 C CB . VAL B 2 10 ? -43.949 13.255 3.505 1.00 163.64 ? 10 VAL B CB 1 ATOM 7264 C CG1 . VAL B 2 10 ? -44.588 12.990 2.148 1.00 166.10 ? 10 VAL B CG1 1 ATOM 7265 C CG2 . VAL B 2 10 ? -45.005 13.274 4.593 1.00 161.70 ? 10 VAL B CG2 1 ATOM 7266 N N . SER B 2 11 ? -41.315 13.192 2.247 1.00 165.25 ? 11 SER B N 1 ATOM 7267 C CA . SER B 2 11 ? -40.664 13.360 0.947 1.00 171.55 ? 11 SER B CA 1 ATOM 7268 C C . SER B 2 11 ? -39.625 12.296 0.588 1.00 173.38 ? 11 SER B C 1 ATOM 7269 O O . SER B 2 11 ? -39.757 11.624 -0.435 1.00 184.22 ? 11 SER B O 1 ATOM 7270 C CB . SER B 2 11 ? -40.005 14.740 0.880 1.00 169.99 ? 11 SER B CB 1 ATOM 7271 O OG . SER B 2 11 ? -39.359 14.940 -0.366 1.00 176.52 ? 11 SER B OG 1 ATOM 7272 N N . SER B 2 12 ? -38.598 12.140 1.416 1.00 164.87 ? 12 SER B N 1 ATOM 7273 C CA . SER B 2 12 ? -37.501 11.239 1.075 1.00 163.59 ? 12 SER B CA 1 ATOM 7274 C C . SER B 2 12 ? -37.016 10.421 2.265 1.00 160.50 ? 12 SER B C 1 ATOM 7275 O O . SER B 2 12 ? -37.381 10.689 3.410 1.00 157.98 ? 12 SER B O 1 ATOM 7276 C CB . SER B 2 12 ? -36.331 12.026 0.481 1.00 173.23 ? 12 SER B CB 1 ATOM 7277 O OG . SER B 2 12 ? -35.769 12.908 1.435 1.00 175.19 ? 12 SER B OG 1 ATOM 7278 N N . CYS B 2 13 ? -36.195 9.416 1.978 1.00 166.92 ? 13 CYS B N 1 ATOM 7279 C CA . CYS B 2 13 ? -35.649 8.539 3.007 1.00 171.71 ? 13 CYS B CA 1 ATOM 7280 C C . CYS B 2 13 ? -34.749 9.300 3.976 1.00 169.31 ? 13 CYS B C 1 ATOM 7281 O O . CYS B 2 13 ? -34.738 9.016 5.174 1.00 161.16 ? 13 CYS B O 1 ATOM 7282 C CB . CYS B 2 13 ? -34.873 7.387 2.367 1.00 176.31 ? 13 CYS B CB 1 ATOM 7283 S SG . CYS B 2 13 ? -34.202 6.203 3.551 1.00 177.80 ? 13 CYS B SG 1 ATOM 7284 N N . GLN B 2 14 ? -33.994 10.262 3.453 1.00 168.50 ? 14 GLN B N 1 ATOM 7285 C CA . GLN B 2 14 ? -33.115 11.079 4.283 1.00 155.53 ? 14 GLN B CA 1 ATOM 7286 C C . GLN B 2 14 ? -33.917 11.977 5.218 1.00 142.47 ? 14 GLN B C 1 ATOM 7287 O O . GLN B 2 14 ? -33.638 12.046 6.415 1.00 136.17 ? 14 GLN B O 1 ATOM 7288 C CB . GLN B 2 14 ? -32.183 11.929 3.417 1.00 162.84 ? 14 GLN B CB 1 ATOM 7289 C CG . GLN B 2 14 ? -31.099 11.142 2.699 1.00 162.66 ? 14 GLN B CG 1 ATOM 7290 C CD . GLN B 2 14 ? -30.028 12.039 2.110 1.00 166.94 ? 14 GLN B CD 1 ATOM 7291 O OE1 . GLN B 2 14 ? -29.108 12.467 2.807 1.00 161.78 ? 14 GLN B OE1 1 ATOM 7292 N NE2 . GLN B 2 14 ? -30.144 12.331 0.819 1.00 175.80 ? 14 GLN B NE2 1 ATOM 7293 N N . GLN B 2 15 ? -34.913 12.664 4.663 1.00 151.60 ? 15 GLN B N 1 ATOM 7294 C CA . GLN B 2 15 ? -35.789 13.527 5.451 1.00 156.77 ? 15 GLN B CA 1 ATOM 7295 C C . GLN B 2 15 ? -36.549 12.719 6.494 1.00 153.55 ? 15 GLN B C 1 ATOM 7296 O O . GLN B 2 15 ? -36.962 13.248 7.524 1.00 151.69 ? 15 GLN B O 1 ATOM 7297 C CB . GLN B 2 15 ? -36.776 14.271 4.550 1.00 156.89 ? 15 GLN B CB 1 ATOM 7298 C CG . GLN B 2 15 ? -36.133 15.264 3.599 1.00 153.35 ? 15 GLN B CG 1 ATOM 7299 C CD . GLN B 2 15 ? -37.158 16.078 2.835 1.00 159.89 ? 15 GLN B CD 1 ATOM 7300 O OE1 . GLN B 2 15 ? -38.321 16.161 3.231 1.00 164.95 ? 15 GLN B OE1 1 ATOM 7301 N NE2 . GLN B 2 15 ? -36.732 16.684 1.733 1.00 165.91 ? 15 GLN B NE2 1 ATOM 7302 N N . CYS B 2 16 ? -36.728 11.434 6.212 1.00 151.44 ? 16 CYS B N 1 ATOM 7303 C CA . CYS B 2 16 ? -37.373 10.515 7.139 1.00 154.84 ? 16 CYS B CA 1 ATOM 7304 C C . CYS B 2 16 ? -36.399 10.106 8.234 1.00 146.99 ? 16 CYS B C 1 ATOM 7305 O O . CYS B 2 16 ? -36.661 10.325 9.418 1.00 136.26 ? 16 CYS B O 1 ATOM 7306 C CB . CYS B 2 16 ? -37.902 9.281 6.408 1.00 161.69 ? 16 CYS B CB 1 ATOM 7307 S SG . CYS B 2 16 ? -38.998 8.256 7.410 1.00 155.27 ? 16 CYS B SG 1 ATOM 7308 N N . LEU B 2 17 ? -35.290 9.490 7.824 1.00 154.18 ? 17 LEU B N 1 ATOM 7309 C CA . LEU B 2 17 ? -34.268 9.002 8.748 1.00 150.28 ? 17 LEU B CA 1 ATOM 7310 C C . LEU B 2 17 ? -33.888 10.038 9.799 1.00 135.20 ? 17 LEU B C 1 ATOM 7311 O O . LEU B 2 17 ? -33.670 9.689 10.959 1.00 127.45 ? 17 LEU B O 1 ATOM 7312 C CB . LEU B 2 17 ? -33.020 8.556 7.984 1.00 152.00 ? 17 LEU B CB 1 ATOM 7313 C CG . LEU B 2 17 ? -32.787 7.043 7.978 1.00 151.81 ? 17 LEU B CG 1 ATOM 7314 C CD1 . LEU B 2 17 ? -33.906 6.327 7.236 1.00 163.45 ? 17 LEU B CD1 1 ATOM 7315 C CD2 . LEU B 2 17 ? -31.433 6.696 7.382 1.00 153.76 ? 17 LEU B CD2 1 ATOM 7316 N N . ALA B 2 18 ? -33.808 11.309 9.414 1.00 125.93 ? 18 ALA B N 1 ATOM 7317 C CA . ALA B 2 18 ? -33.736 12.331 10.443 1.00 117.45 ? 18 ALA B CA 1 ATOM 7318 C C . ALA B 2 18 ? -35.080 13.034 10.591 1.00 118.82 ? 18 ALA B C 1 ATOM 7319 O O . ALA B 2 18 ? -35.413 13.952 9.841 1.00 138.44 ? 18 ALA B O 1 ATOM 7320 C CB . ALA B 2 18 ? -32.649 13.337 10.115 1.00 121.01 ? 18 ALA B CB 1 ATOM 7321 N N . VAL B 2 19 ? -35.835 12.581 11.585 1.00 118.53 ? 19 VAL B N 1 ATOM 7322 C CA . VAL B 2 19 ? -36.940 13.306 12.194 1.00 131.48 ? 19 VAL B CA 1 ATOM 7323 C C . VAL B 2 19 ? -36.769 13.084 13.684 1.00 133.41 ? 19 VAL B C 1 ATOM 7324 O O . VAL B 2 19 ? -36.480 13.996 14.460 1.00 129.32 ? 19 VAL B O 1 ATOM 7325 C CB . VAL B 2 19 ? -38.321 12.798 11.734 1.00 147.06 ? 19 VAL B CB 1 ATOM 7326 C CG1 . VAL B 2 19 ? -39.422 13.498 12.507 1.00 150.53 ? 19 VAL B CG1 1 ATOM 7327 C CG2 . VAL B 2 19 ? -38.504 13.005 10.243 1.00 158.70 ? 19 VAL B CG2 1 ATOM 7328 N N . SER B 2 20 ? -36.963 11.821 14.047 1.00 129.72 ? 20 SER B N 1 ATOM 7329 C CA . SER B 2 20 ? -36.651 11.275 15.356 1.00 127.54 ? 20 SER B CA 1 ATOM 7330 C C . SER B 2 20 ? -35.889 9.973 15.118 1.00 124.74 ? 20 SER B C 1 ATOM 7331 O O . SER B 2 20 ? -36.129 9.293 14.120 1.00 128.36 ? 20 SER B O 1 ATOM 7332 C CB . SER B 2 20 ? -37.925 11.034 16.170 1.00 136.99 ? 20 SER B CB 1 ATOM 7333 O OG . SER B 2 20 ? -37.659 10.306 17.356 1.00 139.57 ? 20 SER B OG 1 ATOM 7334 N N . PRO B 2 21 ? -34.960 9.625 16.021 1.00 127.58 ? 21 PRO B N 1 ATOM 7335 C CA . PRO B 2 21 ? -34.166 8.399 15.866 1.00 128.79 ? 21 PRO B CA 1 ATOM 7336 C C . PRO B 2 21 ? -35.007 7.120 15.828 1.00 132.41 ? 21 PRO B C 1 ATOM 7337 O O . PRO B 2 21 ? -34.501 6.073 15.422 1.00 132.60 ? 21 PRO B O 1 ATOM 7338 C CB . PRO B 2 21 ? -33.256 8.410 17.102 1.00 127.75 ? 21 PRO B CB 1 ATOM 7339 C CG . PRO B 2 21 ? -33.884 9.379 18.053 1.00 123.75 ? 21 PRO B CG 1 ATOM 7340 C CD . PRO B 2 21 ? -34.536 10.408 17.193 1.00 123.58 ? 21 PRO B CD 1 ATOM 7341 N N . MET B 2 22 ? -36.266 7.204 16.246 1.00 138.96 ? 22 MET B N 1 ATOM 7342 C CA . MET B 2 22 ? -37.143 6.040 16.264 1.00 151.48 ? 22 MET B CA 1 ATOM 7343 C C . MET B 2 22 ? -37.837 5.814 14.923 1.00 154.45 ? 22 MET B C 1 ATOM 7344 O O . MET B 2 22 ? -38.483 4.787 14.716 1.00 167.06 ? 22 MET B O 1 ATOM 7345 C CB . MET B 2 22 ? -38.191 6.182 17.368 1.00 154.50 ? 22 MET B CB 1 ATOM 7346 C CG . MET B 2 22 ? -39.220 7.272 17.111 1.00 156.77 ? 22 MET B CG 1 ATOM 7347 S SD . MET B 2 22 ? -40.453 7.372 18.421 1.00 181.83 ? 22 MET B SD 1 ATOM 7348 C CE . MET B 2 22 ? -41.042 5.680 18.461 1.00 173.84 ? 22 MET B CE 1 ATOM 7349 N N . CYS B 2 23 ? -37.707 6.777 14.014 1.00 148.37 ? 23 CYS B N 1 ATOM 7350 C CA . CYS B 2 23 ? -38.352 6.684 12.707 1.00 152.65 ? 23 CYS B CA 1 ATOM 7351 C C . CYS B 2 23 ? -37.683 5.648 11.809 1.00 154.66 ? 23 CYS B C 1 ATOM 7352 O O . CYS B 2 23 ? -36.466 5.467 11.855 1.00 148.85 ? 23 CYS B O 1 ATOM 7353 C CB . CYS B 2 23 ? -38.347 8.047 12.009 1.00 157.16 ? 23 CYS B CB 1 ATOM 7354 S SG . CYS B 2 23 ? -39.303 9.332 12.846 1.00 179.91 ? 23 CYS B SG 1 ATOM 7355 N N . ALA B 2 24 ? -38.486 4.969 10.995 1.00 167.96 ? 24 ALA B N 1 ATOM 7356 C CA . ALA B 2 24 ? -37.963 4.033 10.005 1.00 171.01 ? 24 ALA B CA 1 ATOM 7357 C C . ALA B 2 24 ? -38.432 4.429 8.610 1.00 173.42 ? 24 ALA B C 1 ATOM 7358 O O . ALA B 2 24 ? -39.213 5.363 8.458 1.00 180.19 ? 24 ALA B O 1 ATOM 7359 C CB . ALA B 2 24 ? -38.396 2.614 10.330 1.00 173.10 ? 24 ALA B CB 1 ATOM 7360 N N . TRP B 2 25 ? -37.974 3.704 7.596 1.00 175.35 ? 25 TRP B N 1 ATOM 7361 C CA . TRP B 2 25 ? -38.335 4.014 6.217 1.00 180.39 ? 25 TRP B CA 1 ATOM 7362 C C . TRP B 2 25 ? -38.744 2.755 5.462 1.00 185.80 ? 25 TRP B C 1 ATOM 7363 O O . TRP B 2 25 ? -38.348 1.650 5.830 1.00 186.28 ? 25 TRP B O 1 ATOM 7364 C CB . TRP B 2 25 ? -37.174 4.711 5.501 1.00 178.93 ? 25 TRP B CB 1 ATOM 7365 C CG . TRP B 2 25 ? -37.417 4.918 4.039 1.00 180.65 ? 25 TRP B CG 1 ATOM 7366 C CD1 . TRP B 2 25 ? -36.855 4.223 3.008 1.00 186.91 ? 25 TRP B CD1 1 ATOM 7367 C CD2 . TRP B 2 25 ? -38.310 5.865 3.445 1.00 178.80 ? 25 TRP B CD2 1 ATOM 7368 N NE1 . TRP B 2 25 ? -37.332 4.691 1.807 1.00 188.59 ? 25 TRP B NE1 1 ATOM 7369 C CE2 . TRP B 2 25 ? -38.229 5.698 2.049 1.00 182.72 ? 25 TRP B CE2 1 ATOM 7370 C CE3 . TRP B 2 25 ? -39.168 6.843 3.958 1.00 182.91 ? 25 TRP B CE3 1 ATOM 7371 C CZ2 . TRP B 2 25 ? -38.971 6.472 1.159 1.00 189.68 ? 25 TRP B CZ2 1 ATOM 7372 C CZ3 . TRP B 2 25 ? -39.904 7.612 3.073 1.00 186.12 ? 25 TRP B CZ3 1 ATOM 7373 C CH2 . TRP B 2 25 ? -39.800 7.422 1.690 1.00 190.18 ? 25 TRP B CH2 1 ATOM 7374 N N . CYS B 2 26 ? -39.538 2.920 4.407 1.00 191.65 ? 26 CYS B N 1 ATOM 7375 C CA . CYS B 2 26 ? -39.977 1.774 3.625 1.00 190.78 ? 26 CYS B CA 1 ATOM 7376 C C . CYS B 2 26 ? -39.691 1.901 2.128 1.00 191.19 ? 26 CYS B C 1 ATOM 7377 O O . CYS B 2 26 ? -40.025 2.893 1.481 1.00 198.30 ? 26 CYS B O 1 ATOM 7378 C CB . CYS B 2 26 ? -41.472 1.524 3.839 1.00 194.73 ? 26 CYS B CB 1 ATOM 7379 S SG . CYS B 2 26 ? -42.001 -0.177 3.478 1.00 204.59 ? 26 CYS B SG 1 ATOM 7380 N N . SER B 2 27 ? -39.056 0.856 1.614 1.00 186.43 ? 27 SER B N 1 ATOM 7381 C CA . SER B 2 27 ? -38.928 0.545 0.194 1.00 189.14 ? 27 SER B CA 1 ATOM 7382 C C . SER B 2 27 ? -40.230 -0.119 -0.233 1.00 194.45 ? 27 SER B C 1 ATOM 7383 O O . SER B 2 27 ? -41.289 0.230 0.293 1.00 191.94 ? 27 SER B O 1 ATOM 7384 C CB . SER B 2 27 ? -37.718 -0.339 -0.095 1.00 187.05 ? 27 SER B CB 1 ATOM 7385 O OG . SER B 2 27 ? -36.518 0.294 0.307 1.00 183.41 ? 27 SER B OG 1 ATOM 7386 N N . ASP B 2 28 ? -40.219 -0.947 -1.264 1.00 201.73 ? 28 ASP B N 1 ATOM 7387 C CA . ASP B 2 28 ? -41.492 -1.507 -1.697 1.00 209.53 ? 28 ASP B CA 1 ATOM 7388 C C . ASP B 2 28 ? -42.003 -1.082 -3.077 1.00 212.59 ? 28 ASP B C 1 ATOM 7389 O O . ASP B 2 28 ? -41.603 -1.671 -4.081 1.00 218.21 ? 28 ASP B O 1 ATOM 7390 C CB . ASP B 2 28 ? -42.572 -1.229 -0.645 1.00 209.69 ? 28 ASP B CB 1 ATOM 7391 C CG . ASP B 2 28 ? -42.788 -2.402 0.291 1.00 210.82 ? 28 ASP B CG 1 ATOM 7392 O OD1 . ASP B 2 28 ? -42.066 -3.412 0.158 1.00 211.35 ? 28 ASP B OD1 1 ATOM 7393 O OD2 . ASP B 2 28 ? -43.681 -2.314 1.160 1.00 212.23 ? 28 ASP B OD2 1 ATOM 7394 N N . GLU B 2 29 ? -42.881 -0.089 -3.111 1.00 208.02 ? 29 GLU B N 1 ATOM 7395 C CA . GLU B 2 29 ? -43.581 0.255 -4.333 1.00 207.00 ? 29 GLU B CA 1 ATOM 7396 C C . GLU B 2 29 ? -44.816 -0.630 -4.387 1.00 204.14 ? 29 GLU B C 1 ATOM 7397 O O . GLU B 2 29 ? -45.789 -0.321 -5.075 1.00 207.66 ? 29 GLU B O 1 ATOM 7398 C CB . GLU B 2 29 ? -42.694 0.006 -5.553 1.00 211.09 ? 29 GLU B CB 1 ATOM 7399 C CG . GLU B 2 29 ? -41.557 1.003 -5.708 1.00 216.04 ? 29 GLU B CG 1 ATOM 7400 C CD . GLU B 2 29 ? -40.695 0.719 -6.922 1.00 220.55 ? 29 GLU B CD 1 ATOM 7401 O OE1 . GLU B 2 29 ? -40.837 -0.373 -7.512 1.00 226.57 ? 29 GLU B OE1 1 ATOM 7402 O OE2 . GLU B 2 29 ? -39.875 1.588 -7.287 1.00 217.93 ? 29 GLU B OE2 1 ATOM 7403 N N . ALA B 2 30 ? -44.767 -1.734 -3.644 1.00 195.76 ? 30 ALA B N 1 ATOM 7404 C CA . ALA B 2 30 ? -45.915 -2.618 -3.523 1.00 194.37 ? 30 ALA B CA 1 ATOM 7405 C C . ALA B 2 30 ? -47.158 -1.753 -3.603 1.00 197.10 ? 30 ALA B C 1 ATOM 7406 O O . ALA B 2 30 ? -48.059 -2.009 -4.401 1.00 202.13 ? 30 ALA B O 1 ATOM 7407 C CB . ALA B 2 30 ? -45.871 -3.373 -2.205 1.00 191.72 ? 30 ALA B CB 1 ATOM 7408 N N . LEU B 2 31 ? -47.190 -0.712 -2.777 1.00 192.05 ? 31 LEU B N 1 ATOM 7409 C CA . LEU B 2 31 ? -48.217 0.311 -2.893 1.00 189.79 ? 31 LEU B CA 1 ATOM 7410 C C . LEU B 2 31 ? -49.025 0.600 -1.631 1.00 189.43 ? 31 LEU B C 1 ATOM 7411 O O . LEU B 2 31 ? -50.230 0.347 -1.599 1.00 191.51 ? 31 LEU B O 1 ATOM 7412 C CB . LEU B 2 31 ? -49.169 -0.026 -4.046 1.00 201.93 ? 31 LEU B CB 1 ATOM 7413 C CG . LEU B 2 31 ? -50.274 -1.039 -3.738 1.00 197.91 ? 31 LEU B CG 1 ATOM 7414 C CD1 . LEU B 2 31 ? -51.617 -0.340 -3.589 1.00 196.98 ? 31 LEU B CD1 1 ATOM 7415 C CD2 . LEU B 2 31 ? -50.339 -2.108 -4.817 1.00 197.94 ? 31 LEU B CD2 1 ATOM 7416 N N . PRO B 2 32 ? -48.386 1.156 -0.605 1.00 196.13 ? 32 PRO B N 1 ATOM 7417 C CA . PRO B 2 32 ? -49.162 1.783 0.466 1.00 199.17 ? 32 PRO B CA 1 ATOM 7418 C C . PRO B 2 32 ? -49.453 3.246 0.138 1.00 199.03 ? 32 PRO B C 1 ATOM 7419 O O . PRO B 2 32 ? -48.792 4.131 0.685 1.00 199.02 ? 32 PRO B O 1 ATOM 7420 C CB . PRO B 2 32 ? -48.239 1.677 1.690 1.00 191.04 ? 32 PRO B CB 1 ATOM 7421 C CG . PRO B 2 32 ? -47.005 0.926 1.223 1.00 186.83 ? 32 PRO B CG 1 ATOM 7422 C CD . PRO B 2 32 ? -46.958 1.100 -0.259 1.00 194.19 ? 32 PRO B CD 1 ATOM 7423 N N . LEU B 2 33 ? -50.411 3.500 -0.750 1.00 192.45 ? 33 LEU B N 1 ATOM 7424 C CA . LEU B 2 33 ? -50.785 4.870 -1.085 1.00 194.03 ? 33 LEU B CA 1 ATOM 7425 C C . LEU B 2 33 ? -51.693 5.408 0.013 1.00 201.41 ? 33 LEU B C 1 ATOM 7426 O O . LEU B 2 33 ? -52.766 4.861 0.265 1.00 207.91 ? 33 LEU B O 1 ATOM 7427 C CB . LEU B 2 33 ? -51.480 4.933 -2.446 1.00 189.00 ? 33 LEU B CB 1 ATOM 7428 C CG . LEU B 2 33 ? -51.405 6.274 -3.182 1.00 183.87 ? 33 LEU B CG 1 ATOM 7429 C CD1 . LEU B 2 33 ? -50.015 6.486 -3.764 1.00 182.45 ? 33 LEU B CD1 1 ATOM 7430 C CD2 . LEU B 2 33 ? -52.467 6.361 -4.266 1.00 180.47 ? 33 LEU B CD2 1 ATOM 7431 N N . GLY B 2 34 ? -51.261 6.483 0.664 1.00 198.10 ? 34 GLY B N 1 ATOM 7432 C CA . GLY B 2 34 ? -51.846 6.884 1.931 1.00 197.41 ? 34 GLY B CA 1 ATOM 7433 C C . GLY B 2 34 ? -51.256 5.957 2.976 1.00 196.65 ? 34 GLY B C 1 ATOM 7434 O O . GLY B 2 34 ? -50.504 5.052 2.615 1.00 198.51 ? 34 GLY B O 1 ATOM 7435 N N . SER B 2 35 ? -51.593 6.153 4.251 1.00 198.68 ? 35 SER B N 1 ATOM 7436 C CA . SER B 2 35 ? -51.008 5.341 5.321 1.00 196.89 ? 35 SER B CA 1 ATOM 7437 C C . SER B 2 35 ? -49.485 5.368 5.206 1.00 186.28 ? 35 SER B C 1 ATOM 7438 O O . SER B 2 35 ? -48.876 4.398 4.755 1.00 180.71 ? 35 SER B O 1 ATOM 7439 C CB . SER B 2 35 ? -51.530 3.902 5.276 1.00 199.61 ? 35 SER B CB 1 ATOM 7440 O OG . SER B 2 35 ? -51.075 3.230 4.115 1.00 200.01 ? 35 SER B OG 1 ATOM 7441 N N . PRO B 2 36 ? -48.874 6.485 5.629 1.00 186.61 ? 36 PRO B N 1 ATOM 7442 C CA . PRO B 2 36 ? -47.547 6.981 5.237 1.00 189.67 ? 36 PRO B CA 1 ATOM 7443 C C . PRO B 2 36 ? -46.426 5.945 5.269 1.00 188.85 ? 36 PRO B C 1 ATOM 7444 O O . PRO B 2 36 ? -46.432 5.007 6.066 1.00 187.14 ? 36 PRO B O 1 ATOM 7445 C CB . PRO B 2 36 ? -47.271 8.089 6.266 1.00 185.36 ? 36 PRO B CB 1 ATOM 7446 C CG . PRO B 2 36 ? -48.243 7.847 7.377 1.00 187.21 ? 36 PRO B CG 1 ATOM 7447 C CD . PRO B 2 36 ? -49.452 7.294 6.712 1.00 188.75 ? 36 PRO B CD 1 ATOM 7448 N N . ARG B 2 37 ? -45.462 6.147 4.377 1.00 185.05 ? 37 ARG B N 1 ATOM 7449 C CA . ARG B 2 37 ? -44.418 5.173 4.087 1.00 179.85 ? 37 ARG B CA 1 ATOM 7450 C C . ARG B 2 37 ? -43.272 5.204 5.094 1.00 187.55 ? 37 ARG B C 1 ATOM 7451 O O . ARG B 2 37 ? -42.314 4.442 4.970 1.00 192.83 ? 37 ARG B O 1 ATOM 7452 C CB . ARG B 2 37 ? -43.866 5.414 2.678 1.00 176.88 ? 37 ARG B CB 1 ATOM 7453 C CG . ARG B 2 37 ? -44.936 5.529 1.600 1.00 186.64 ? 37 ARG B CG 1 ATOM 7454 C CD . ARG B 2 37 ? -44.365 6.076 0.299 1.00 194.27 ? 37 ARG B CD 1 ATOM 7455 N NE . ARG B 2 37 ? -43.981 7.482 0.410 1.00 196.90 ? 37 ARG B NE 1 ATOM 7456 C CZ . ARG B 2 37 ? -44.750 8.500 0.035 1.00 199.93 ? 37 ARG B CZ 1 ATOM 7457 N NH1 . ARG B 2 37 ? -45.951 8.274 -0.480 1.00 199.90 ? 37 ARG B NH1 1 ATOM 7458 N NH2 . ARG B 2 37 ? -44.317 9.747 0.174 1.00 199.39 ? 37 ARG B NH2 1 ATOM 7459 N N . CYS B 2 38 ? -43.363 6.085 6.085 1.00 186.19 ? 38 CYS B N 1 ATOM 7460 C CA . CYS B 2 38 ? -42.277 6.237 7.046 1.00 168.96 ? 38 CYS B CA 1 ATOM 7461 C C . CYS B 2 38 ? -42.566 5.535 8.372 1.00 167.87 ? 38 CYS B C 1 ATOM 7462 O O . CYS B 2 38 ? -42.035 4.458 8.636 1.00 168.93 ? 38 CYS B O 1 ATOM 7463 C CB . CYS B 2 38 ? -42.006 7.725 7.291 1.00 161.86 ? 38 CYS B CB 1 ATOM 7464 S SG . CYS B 2 38 ? -40.707 8.080 8.496 1.00 174.29 ? 38 CYS B SG 1 ATOM 7465 N N . ASP B 2 39 ? -43.407 6.157 9.194 1.00 169.68 ? 39 ASP B N 1 ATOM 7466 C CA . ASP B 2 39 ? -43.811 5.626 10.499 1.00 173.08 ? 39 ASP B CA 1 ATOM 7467 C C . ASP B 2 39 ? -42.632 5.165 11.360 1.00 168.43 ? 39 ASP B C 1 ATOM 7468 O O . ASP B 2 39 ? -41.565 5.778 11.343 1.00 173.14 ? 39 ASP B O 1 ATOM 7469 C CB . ASP B 2 39 ? -44.797 4.470 10.314 1.00 182.45 ? 39 ASP B CB 1 ATOM 7470 C CG . ASP B 2 39 ? -46.241 4.930 10.336 1.00 191.07 ? 39 ASP B CG 1 ATOM 7471 O OD1 . ASP B 2 39 ? -46.580 5.774 11.192 1.00 190.40 ? 39 ASP B OD1 1 ATOM 7472 O OD2 . ASP B 2 39 ? -47.036 4.450 9.502 1.00 199.77 ? 39 ASP B OD2 1 ATOM 7473 N N . LEU B 2 40 ? -42.831 4.082 12.110 1.00 167.92 ? 40 LEU B N 1 ATOM 7474 C CA . LEU B 2 40 ? -41.743 3.468 12.870 1.00 169.12 ? 40 LEU B CA 1 ATOM 7475 C C . LEU B 2 40 ? -41.794 1.936 12.892 1.00 170.56 ? 40 LEU B C 1 ATOM 7476 O O . LEU B 2 40 ? -42.751 1.359 13.406 1.00 169.07 ? 40 LEU B O 1 ATOM 7477 C CB . LEU B 2 40 ? -41.746 4.009 14.305 1.00 171.17 ? 40 LEU B CB 1 ATOM 7478 C CG . LEU B 2 40 ? -43.087 4.042 15.045 1.00 164.43 ? 40 LEU B CG 1 ATOM 7479 C CD1 . LEU B 2 40 ? -43.123 3.007 16.161 1.00 161.59 ? 40 LEU B CD1 1 ATOM 7480 C CD2 . LEU B 2 40 ? -43.372 5.434 15.588 1.00 162.17 ? 40 LEU B CD2 1 ATOM 7481 N N . LYS B 2 41 ? -40.768 1.292 12.336 1.00 171.24 ? 41 LYS B N 1 ATOM 7482 C CA . LYS B 2 41 ? -40.471 -0.128 12.583 1.00 167.82 ? 41 LYS B CA 1 ATOM 7483 C C . LYS B 2 41 ? -41.693 -1.058 12.554 1.00 177.52 ? 41 LYS B C 1 ATOM 7484 O O . LYS B 2 41 ? -42.363 -1.186 11.533 1.00 182.99 ? 41 LYS B O 1 ATOM 7485 C CB . LYS B 2 41 ? -39.730 -0.286 13.914 1.00 163.48 ? 41 LYS B CB 1 ATOM 7486 C CG . LYS B 2 41 ? -38.856 -1.538 13.979 1.00 166.91 ? 41 LYS B CG 1 ATOM 7487 C CD . LYS B 2 41 ? -38.081 -1.733 12.683 1.00 152.40 ? 41 LYS B CD 1 ATOM 7488 C CE . LYS B 2 41 ? -37.552 -3.152 12.554 1.00 143.73 ? 41 LYS B CE 1 ATOM 7489 N NZ . LYS B 2 41 ? -36.581 -3.492 13.630 1.00 134.70 ? 41 LYS B NZ 1 ATOM 7490 N N . GLU B 2 42 ? -41.953 -1.719 13.681 1.00 181.37 ? 42 GLU B N 1 ATOM 7491 C CA . GLU B 2 42 ? -43.046 -2.684 13.805 1.00 177.08 ? 42 GLU B CA 1 ATOM 7492 C C . GLU B 2 42 ? -44.414 -2.086 13.469 1.00 165.76 ? 42 GLU B C 1 ATOM 7493 O O . GLU B 2 42 ? -45.340 -2.807 13.096 1.00 162.06 ? 42 GLU B O 1 ATOM 7494 C CB . GLU B 2 42 ? -43.058 -3.285 15.219 1.00 181.60 ? 42 GLU B CB 1 ATOM 7495 C CG . GLU B 2 42 ? -44.320 -3.021 16.036 1.00 184.26 ? 42 GLU B CG 1 ATOM 7496 C CD . GLU B 2 42 ? -44.346 -1.636 16.654 1.00 180.86 ? 42 GLU B CD 1 ATOM 7497 O OE1 . GLU B 2 42 ? -43.287 -0.972 16.680 1.00 170.74 ? 42 GLU B OE1 1 ATOM 7498 O OE2 . GLU B 2 42 ? -45.427 -1.209 17.112 1.00 184.68 ? 42 GLU B OE2 1 ATOM 7499 N N . ASN B 2 43 ? -44.542 -0.769 13.600 1.00 170.16 ? 43 ASN B N 1 ATOM 7500 C CA . ASN B 2 43 ? -45.775 -0.093 13.220 1.00 173.24 ? 43 ASN B CA 1 ATOM 7501 C C . ASN B 2 43 ? -45.875 0.044 11.702 1.00 168.05 ? 43 ASN B C 1 ATOM 7502 O O . ASN B 2 43 ? -46.968 0.139 11.147 1.00 169.08 ? 43 ASN B O 1 ATOM 7503 C CB . ASN B 2 43 ? -45.869 1.278 13.892 1.00 175.96 ? 43 ASN B CB 1 ATOM 7504 C CG . ASN B 2 43 ? -47.047 2.092 13.398 1.00 174.72 ? 43 ASN B CG 1 ATOM 7505 O OD1 . ASN B 2 43 ? -46.883 3.027 12.616 1.00 173.31 ? 43 ASN B OD1 1 ATOM 7506 N ND2 . ASN B 2 43 ? -48.245 1.734 13.845 1.00 181.33 ? 43 ASN B ND2 1 ATOM 7507 N N . LEU B 2 44 ? -44.725 0.038 11.033 1.00 169.26 ? 44 LEU B N 1 ATOM 7508 C CA . LEU B 2 44 ? -44.681 0.039 9.574 1.00 170.97 ? 44 LEU B CA 1 ATOM 7509 C C . LEU B 2 44 ? -45.077 -1.334 9.038 1.00 176.39 ? 44 LEU B C 1 ATOM 7510 O O . LEU B 2 44 ? -45.231 -1.523 7.832 1.00 181.39 ? 44 LEU B O 1 ATOM 7511 C CB . LEU B 2 44 ? -43.285 0.417 9.071 1.00 171.73 ? 44 LEU B CB 1 ATOM 7512 C CG . LEU B 2 44 ? -43.129 1.478 7.979 1.00 173.52 ? 44 LEU B CG 1 ATOM 7513 C CD1 . LEU B 2 44 ? -41.686 1.508 7.493 1.00 174.15 ? 44 LEU B CD1 1 ATOM 7514 C CD2 . LEU B 2 44 ? -44.084 1.248 6.819 1.00 183.53 ? 44 LEU B CD2 1 ATOM 7515 N N . LEU B 2 45 ? -45.239 -2.291 9.946 1.00 176.53 ? 45 LEU B N 1 ATOM 7516 C CA . LEU B 2 45 ? -45.545 -3.666 9.575 1.00 176.11 ? 45 LEU B CA 1 ATOM 7517 C C . LEU B 2 45 ? -47.050 -3.921 9.485 1.00 173.19 ? 45 LEU B C 1 ATOM 7518 O O . LEU B 2 45 ? -47.476 -5.064 9.320 1.00 167.60 ? 45 LEU B O 1 ATOM 7519 C CB . LEU B 2 45 ? -44.901 -4.643 10.562 1.00 174.05 ? 45 LEU B CB 1 ATOM 7520 C CG . LEU B 2 45 ? -43.379 -4.529 10.706 1.00 165.11 ? 45 LEU B CG 1 ATOM 7521 C CD1 . LEU B 2 45 ? -42.829 -5.659 11.567 1.00 168.65 ? 45 LEU B CD1 1 ATOM 7522 C CD2 . LEU B 2 45 ? -42.692 -4.497 9.348 1.00 165.05 ? 45 LEU B CD2 1 ATOM 7523 N N . LYS B 2 46 ? -47.848 -2.862 9.620 1.00 179.28 ? 46 LYS B N 1 ATOM 7524 C CA . LYS B 2 46 ? -49.285 -2.953 9.365 1.00 181.68 ? 46 LYS B CA 1 ATOM 7525 C C . LYS B 2 46 ? -49.491 -3.506 7.961 1.00 188.66 ? 46 LYS B C 1 ATOM 7526 O O . LYS B 2 46 ? -50.144 -4.532 7.772 1.00 200.95 ? 46 LYS B O 1 ATOM 7527 C CB . LYS B 2 46 ? -49.961 -1.591 9.515 1.00 180.30 ? 46 LYS B CB 1 ATOM 7528 C CG . LYS B 2 46 ? -49.943 -1.042 10.931 1.00 185.76 ? 46 LYS B CG 1 ATOM 7529 C CD . LYS B 2 46 ? -50.556 0.348 10.992 1.00 184.50 ? 46 LYS B CD 1 ATOM 7530 C CE . LYS B 2 46 ? -49.810 1.320 10.094 1.00 176.00 ? 46 LYS B CE 1 ATOM 7531 N NZ . LYS B 2 46 ? -50.380 2.694 10.167 1.00 174.60 ? 46 LYS B NZ 1 ATOM 7532 N N . ASP B 2 47 ? -48.924 -2.813 6.979 1.00 182.90 ? 47 ASP B N 1 ATOM 7533 C CA . ASP B 2 47 ? -48.643 -3.423 5.690 1.00 189.90 ? 47 ASP B CA 1 ATOM 7534 C C . ASP B 2 47 ? -47.367 -4.223 5.894 1.00 187.72 ? 47 ASP B C 1 ATOM 7535 O O . ASP B 2 47 ? -46.439 -3.727 6.529 1.00 187.78 ? 47 ASP B O 1 ATOM 7536 C CB . ASP B 2 47 ? -48.476 -2.374 4.591 1.00 192.48 ? 47 ASP B CB 1 ATOM 7537 C CG . ASP B 2 47 ? -47.979 -2.970 3.286 1.00 198.80 ? 47 ASP B CG 1 ATOM 7538 O OD1 . ASP B 2 47 ? -48.344 -4.124 2.980 1.00 201.06 ? 47 ASP B OD1 1 ATOM 7539 O OD2 . ASP B 2 47 ? -47.222 -2.283 2.570 1.00 201.27 ? 47 ASP B OD2 1 ATOM 7540 N N . ASN B 2 48 ? -47.321 -5.443 5.363 1.00 188.57 ? 48 ASN B N 1 ATOM 7541 C CA . ASN B 2 48 ? -46.265 -6.400 5.704 1.00 189.30 ? 48 ASN B CA 1 ATOM 7542 C C . ASN B 2 48 ? -44.858 -5.807 5.678 1.00 194.54 ? 48 ASN B C 1 ATOM 7543 O O . ASN B 2 48 ? -44.251 -5.623 6.733 1.00 200.38 ? 48 ASN B O 1 ATOM 7544 C CB . ASN B 2 48 ? -46.334 -7.608 4.767 1.00 189.73 ? 48 ASN B CB 1 ATOM 7545 C CG . ASN B 2 48 ? -47.591 -8.432 4.975 1.00 191.90 ? 48 ASN B CG 1 ATOM 7546 O OD1 . ASN B 2 48 ? -48.574 -7.954 5.541 1.00 189.81 ? 48 ASN B OD1 1 ATOM 7547 N ND2 . ASN B 2 48 ? -47.563 -9.680 4.520 1.00 192.08 ? 48 ASN B ND2 1 ATOM 7548 N N . CYS B 2 49 ? -44.353 -5.504 4.483 1.00 192.46 ? 49 CYS B N 1 ATOM 7549 C CA . CYS B 2 49 ? -43.088 -4.780 4.318 1.00 190.97 ? 49 CYS B CA 1 ATOM 7550 C C . CYS B 2 49 ? -41.946 -5.413 5.120 1.00 194.85 ? 49 CYS B C 1 ATOM 7551 O O . CYS B 2 49 ? -41.029 -4.724 5.570 1.00 196.32 ? 49 CYS B O 1 ATOM 7552 C CB . CYS B 2 49 ? -43.270 -3.311 4.724 1.00 188.96 ? 49 CYS B CB 1 ATOM 7553 S SG . CYS B 2 49 ? -42.084 -2.143 3.997 1.00 221.31 ? 49 CYS B SG 1 ATOM 7554 N N . ALA B 2 50 ? -42.018 -6.729 5.294 1.00 200.46 ? 50 ALA B N 1 ATOM 7555 C CA . ALA B 2 50 ? -41.058 -7.486 6.103 1.00 194.68 ? 50 ALA B CA 1 ATOM 7556 C C . ALA B 2 50 ? -39.606 -7.529 5.584 1.00 188.23 ? 50 ALA B C 1 ATOM 7557 O O . ALA B 2 50 ? -38.678 -7.425 6.387 1.00 171.63 ? 50 ALA B O 1 ATOM 7558 C CB . ALA B 2 50 ? -41.572 -8.913 6.294 1.00 192.73 ? 50 ALA B CB 1 ATOM 7559 N N . PRO B 2 51 ? -39.394 -7.687 4.258 1.00 195.55 ? 51 PRO B N 1 ATOM 7560 C CA . PRO B 2 51 ? -38.015 -7.812 3.762 1.00 192.19 ? 51 PRO B CA 1 ATOM 7561 C C . PRO B 2 51 ? -37.119 -6.611 4.067 1.00 177.65 ? 51 PRO B C 1 ATOM 7562 O O . PRO B 2 51 ? -37.612 -5.554 4.460 1.00 169.52 ? 51 PRO B O 1 ATOM 7563 C CB . PRO B 2 51 ? -38.199 -7.967 2.244 1.00 192.97 ? 51 PRO B CB 1 ATOM 7564 C CG . PRO B 2 51 ? -39.568 -7.464 1.962 1.00 188.77 ? 51 PRO B CG 1 ATOM 7565 C CD . PRO B 2 51 ? -40.361 -7.858 3.158 1.00 193.75 ? 51 PRO B CD 1 ATOM 7566 N N . GLU B 2 52 ? -35.813 -6.792 3.873 1.00 183.13 ? 52 GLU B N 1 ATOM 7567 C CA . GLU B 2 52 ? -34.786 -5.800 4.210 1.00 184.49 ? 52 GLU B CA 1 ATOM 7568 C C . GLU B 2 52 ? -35.067 -4.424 3.613 1.00 186.22 ? 52 GLU B C 1 ATOM 7569 O O . GLU B 2 52 ? -34.423 -3.439 3.976 1.00 184.54 ? 52 GLU B O 1 ATOM 7570 C CB . GLU B 2 52 ? -33.408 -6.276 3.745 1.00 184.47 ? 52 GLU B CB 1 ATOM 7571 C CG . GLU B 2 52 ? -32.866 -7.474 4.499 1.00 190.63 ? 52 GLU B CG 1 ATOM 7572 C CD . GLU B 2 52 ? -31.410 -7.748 4.175 1.00 198.80 ? 52 GLU B CD 1 ATOM 7573 O OE1 . GLU B 2 52 ? -30.798 -6.936 3.448 1.00 190.73 ? 52 GLU B OE1 1 ATOM 7574 O OE2 . GLU B 2 52 ? -30.876 -8.772 4.649 1.00 205.65 ? 52 GLU B OE2 1 ATOM 7575 N N . SER B 2 53 ? -36.009 -4.379 2.677 1.00 189.30 ? 53 SER B N 1 ATOM 7576 C CA . SER B 2 53 ? -36.468 -3.143 2.062 1.00 199.97 ? 53 SER B CA 1 ATOM 7577 C C . SER B 2 53 ? -36.793 -2.056 3.094 1.00 205.38 ? 53 SER B C 1 ATOM 7578 O O . SER B 2 53 ? -36.668 -0.866 2.809 1.00 199.48 ? 53 SER B O 1 ATOM 7579 C CB . SER B 2 53 ? -37.701 -3.436 1.205 1.00 199.38 ? 53 SER B CB 1 ATOM 7580 O OG . SER B 2 53 ? -38.779 -3.899 2.001 1.00 198.27 ? 53 SER B OG 1 ATOM 7581 N N . ILE B 2 54 ? -37.197 -2.465 4.294 1.00 205.86 ? 54 ILE B N 1 ATOM 7582 C CA . ILE B 2 54 ? -37.397 -1.522 5.391 1.00 187.63 ? 54 ILE B CA 1 ATOM 7583 C C . ILE B 2 54 ? -36.051 -1.044 5.943 1.00 170.92 ? 54 ILE B C 1 ATOM 7584 O O . ILE B 2 54 ? -35.157 -1.847 6.213 1.00 163.47 ? 54 ILE B O 1 ATOM 7585 C CB . ILE B 2 54 ? -38.243 -2.145 6.530 1.00 179.41 ? 54 ILE B CB 1 ATOM 7586 C CG1 . ILE B 2 54 ? -38.297 -1.205 7.736 1.00 174.80 ? 54 ILE B CG1 1 ATOM 7587 C CG2 . ILE B 2 54 ? -37.696 -3.507 6.937 1.00 182.59 ? 54 ILE B CG2 1 ATOM 7588 C CD1 . ILE B 2 54 ? -39.072 -1.762 8.912 1.00 179.87 ? 54 ILE B CD1 1 ATOM 7589 N N . GLU B 2 55 ? -35.907 0.269 6.094 1.00 174.75 ? 55 GLU B N 1 ATOM 7590 C CA . GLU B 2 55 ? -34.663 0.852 6.586 1.00 181.13 ? 55 GLU B CA 1 ATOM 7591 C C . GLU B 2 55 ? -34.792 1.343 8.025 1.00 170.19 ? 55 GLU B C 1 ATOM 7592 O O . GLU B 2 55 ? -35.525 2.293 8.301 1.00 164.14 ? 55 GLU B O 1 ATOM 7593 C CB . GLU B 2 55 ? -34.219 2.007 5.684 1.00 182.95 ? 55 GLU B CB 1 ATOM 7594 C CG . GLU B 2 55 ? -33.661 1.574 4.337 1.00 184.82 ? 55 GLU B CG 1 ATOM 7595 C CD . GLU B 2 55 ? -32.265 0.991 4.441 1.00 179.04 ? 55 GLU B CD 1 ATOM 7596 O OE1 . GLU B 2 55 ? -31.616 1.175 5.493 1.00 168.13 ? 55 GLU B OE1 1 ATOM 7597 O OE2 . GLU B 2 55 ? -31.814 0.349 3.468 1.00 182.56 ? 55 GLU B OE2 1 ATOM 7598 N N . PHE B 2 56 ? -34.078 0.691 8.936 1.00 167.57 ? 56 PHE B N 1 ATOM 7599 C CA . PHE B 2 56 ? -34.081 1.095 10.337 1.00 164.45 ? 56 PHE B CA 1 ATOM 7600 C C . PHE B 2 56 ? -32.693 0.970 10.965 1.00 163.17 ? 56 PHE B C 1 ATOM 7601 O O . PHE B 2 56 ? -32.416 0.007 11.679 1.00 160.60 ? 56 PHE B O 1 ATOM 7602 C CB . PHE B 2 56 ? -35.092 0.265 11.130 1.00 161.98 ? 56 PHE B CB 1 ATOM 7603 C CG . PHE B 2 56 ? -35.311 0.755 12.535 1.00 156.72 ? 56 PHE B CG 1 ATOM 7604 C CD1 . PHE B 2 56 ? -35.941 1.965 12.767 1.00 152.24 ? 56 PHE B CD1 1 ATOM 7605 C CD2 . PHE B 2 56 ? -34.896 0.002 13.620 1.00 154.92 ? 56 PHE B CD2 1 ATOM 7606 C CE1 . PHE B 2 56 ? -36.148 2.421 14.055 1.00 150.43 ? 56 PHE B CE1 1 ATOM 7607 C CE2 . PHE B 2 56 ? -35.099 0.452 14.913 1.00 150.57 ? 56 PHE B CE2 1 ATOM 7608 C CZ . PHE B 2 56 ? -35.727 1.663 15.129 1.00 148.52 ? 56 PHE B CZ 1 ATOM 7609 N N . PRO B 2 57 ? -31.811 1.946 10.689 1.00 151.04 ? 57 PRO B N 1 ATOM 7610 C CA . PRO B 2 57 ? -30.468 1.961 11.279 1.00 139.89 ? 57 PRO B CA 1 ATOM 7611 C C . PRO B 2 57 ? -30.512 2.156 12.791 1.00 129.29 ? 57 PRO B C 1 ATOM 7612 O O . PRO B 2 57 ? -31.236 3.025 13.275 1.00 131.93 ? 57 PRO B O 1 ATOM 7613 C CB . PRO B 2 57 ? -29.792 3.156 10.593 1.00 134.67 ? 57 PRO B CB 1 ATOM 7614 C CG . PRO B 2 57 ? -30.608 3.416 9.367 1.00 140.53 ? 57 PRO B CG 1 ATOM 7615 C CD . PRO B 2 57 ? -32.007 3.057 9.745 1.00 142.95 ? 57 PRO B CD 1 ATOM 7616 N N . VAL B 2 58 ? -29.744 1.356 13.523 1.00 116.13 ? 58 VAL B N 1 ATOM 7617 C CA . VAL B 2 58 ? -29.719 1.446 14.978 1.00 116.18 ? 58 VAL B CA 1 ATOM 7618 C C . VAL B 2 58 ? -28.382 1.977 15.482 1.00 118.84 ? 58 VAL B C 1 ATOM 7619 O O . VAL B 2 58 ? -27.335 1.377 15.238 1.00 117.12 ? 58 VAL B O 1 ATOM 7620 C CB . VAL B 2 58 ? -29.994 0.078 15.632 1.00 125.73 ? 58 VAL B CB 1 ATOM 7621 C CG1 . VAL B 2 58 ? -29.860 0.175 17.145 1.00 108.30 ? 58 VAL B CG1 1 ATOM 7622 C CG2 . VAL B 2 58 ? -31.375 -0.428 15.243 1.00 135.66 ? 58 VAL B CG2 1 ATOM 7623 N N . SER B 2 59 ? -28.424 3.108 16.181 1.00 97.45 ? 59 SER B N 1 ATOM 7624 C CA . SER B 2 59 ? -27.223 3.686 16.770 1.00 95.17 ? 59 SER B CA 1 ATOM 7625 C C . SER B 2 59 ? -26.643 2.754 17.825 1.00 112.38 ? 59 SER B C 1 ATOM 7626 O O . SER B 2 59 ? -27.380 2.122 18.582 1.00 121.77 ? 59 SER B O 1 ATOM 7627 C CB . SER B 2 59 ? -27.522 5.054 17.383 1.00 101.25 ? 59 SER B CB 1 ATOM 7628 O OG . SER B 2 59 ? -27.938 5.978 16.394 1.00 106.55 ? 59 SER B OG 1 ATOM 7629 N N . GLU B 2 60 ? -25.319 2.670 17.870 1.00 93.18 ? 60 GLU B N 1 ATOM 7630 C CA . GLU B 2 60 ? -24.657 1.750 18.783 1.00 91.95 ? 60 GLU B CA 1 ATOM 7631 C C . GLU B 2 60 ? -23.278 2.238 19.203 1.00 114.48 ? 60 GLU B C 1 ATOM 7632 O O . GLU B 2 60 ? -22.622 2.990 18.481 1.00 127.19 ? 60 GLU B O 1 ATOM 7633 C CB . GLU B 2 60 ? -24.531 0.367 18.139 1.00 94.72 ? 60 GLU B CB 1 ATOM 7634 C CG . GLU B 2 60 ? -23.672 0.352 16.882 1.00 108.07 ? 60 GLU B CG 1 ATOM 7635 C CD . GLU B 2 60 ? -23.472 -1.044 16.325 1.00 144.32 ? 60 GLU B CD 1 ATOM 7636 O OE1 . GLU B 2 60 ? -23.929 -2.013 16.967 1.00 150.95 ? 60 GLU B OE1 1 ATOM 7637 O OE2 . GLU B 2 60 ? -22.856 -1.171 15.245 1.00 150.21 ? 60 GLU B OE2 1 ATOM 7638 N N . ALA B 2 61 ? -22.848 1.804 20.382 1.00 109.98 ? 61 ALA B N 1 ATOM 7639 C CA . ALA B 2 61 ? -21.473 1.997 20.813 1.00 88.97 ? 61 ALA B CA 1 ATOM 7640 C C . ALA B 2 61 ? -20.898 0.657 21.246 1.00 94.18 ? 61 ALA B C 1 ATOM 7641 O O . ALA B 2 61 ? -21.319 0.090 22.254 1.00 115.94 ? 61 ALA B O 1 ATOM 7642 C CB . ALA B 2 61 ? -21.396 3.007 21.944 1.00 83.14 ? 61 ALA B CB 1 ATOM 7643 N N . ARG B 2 62 ? -19.933 0.154 20.484 1.00 87.91 ? 62 ARG B N 1 ATOM 7644 C CA . ARG B 2 62 ? -19.326 -1.134 20.786 1.00 96.23 ? 62 ARG B CA 1 ATOM 7645 C C . ARG B 2 62 ? -17.861 -0.963 21.154 1.00 100.79 ? 62 ARG B C 1 ATOM 7646 O O . ARG B 2 62 ? -17.159 -0.128 20.582 1.00 103.46 ? 62 ARG B O 1 ATOM 7647 C CB . ARG B 2 62 ? -19.465 -2.095 19.600 1.00 97.75 ? 62 ARG B CB 1 ATOM 7648 C CG . ARG B 2 62 ? -18.801 -1.616 18.318 1.00 99.93 ? 62 ARG B CG 1 ATOM 7649 C CD . ARG B 2 62 ? -18.730 -2.725 17.279 1.00 96.80 ? 62 ARG B CD 1 ATOM 7650 N NE . ARG B 2 62 ? -20.053 -3.221 16.911 1.00 99.04 ? 62 ARG B NE 1 ATOM 7651 C CZ . ARG B 2 62 ? -20.267 -4.205 16.042 1.00 153.67 ? 62 ARG B CZ 1 ATOM 7652 N NH1 . ARG B 2 62 ? -19.242 -4.802 15.449 1.00 151.99 ? 62 ARG B NH1 1 ATOM 7653 N NH2 . ARG B 2 62 ? -21.506 -4.591 15.767 1.00 146.98 ? 62 ARG B NH2 1 ATOM 7654 N N . VAL B 2 63 ? -17.403 -1.750 22.121 1.00 88.70 ? 63 VAL B N 1 ATOM 7655 C CA . VAL B 2 63 ? -16.010 -1.697 22.536 1.00 87.91 ? 63 VAL B CA 1 ATOM 7656 C C . VAL B 2 63 ? -15.142 -2.493 21.573 1.00 90.27 ? 63 VAL B C 1 ATOM 7657 O O . VAL B 2 63 ? -15.315 -3.702 21.423 1.00 108.62 ? 63 VAL B O 1 ATOM 7658 C CB . VAL B 2 63 ? -15.822 -2.246 23.960 1.00 88.11 ? 63 VAL B CB 1 ATOM 7659 C CG1 . VAL B 2 63 ? -14.347 -2.332 24.299 1.00 88.04 ? 63 VAL B CG1 1 ATOM 7660 C CG2 . VAL B 2 63 ? -16.553 -1.376 24.967 1.00 97.32 ? 63 VAL B CG2 1 ATOM 7661 N N . LEU B 2 64 ? -14.208 -1.808 20.921 1.00 92.37 ? 64 LEU B N 1 ATOM 7662 C CA . LEU B 2 64 ? -13.279 -2.468 20.015 1.00 103.15 ? 64 LEU B CA 1 ATOM 7663 C C . LEU B 2 64 ? -12.147 -3.120 20.794 1.00 100.93 ? 64 LEU B C 1 ATOM 7664 O O . LEU B 2 64 ? -11.737 -4.241 20.496 1.00 111.48 ? 64 LEU B O 1 ATOM 7665 C CB . LEU B 2 64 ? -12.722 -1.475 18.993 1.00 90.83 ? 64 LEU B CB 1 ATOM 7666 C CG . LEU B 2 64 ? -13.713 -1.004 17.927 1.00 97.29 ? 64 LEU B CG 1 ATOM 7667 C CD1 . LEU B 2 64 ? -13.064 0.003 16.987 1.00 101.74 ? 64 LEU B CD1 1 ATOM 7668 C CD2 . LEU B 2 64 ? -14.264 -2.194 17.152 1.00 94.86 ? 64 LEU B CD2 1 ATOM 7669 N N . GLU B 2 65 ? -11.632 -2.401 21.785 1.00 90.30 ? 65 GLU B N 1 ATOM 7670 C CA . GLU B 2 65 ? -10.596 -2.938 22.655 1.00 98.16 ? 65 GLU B CA 1 ATOM 7671 C C . GLU B 2 65 ? -10.811 -2.543 24.111 1.00 96.34 ? 65 GLU B C 1 ATOM 7672 O O . GLU B 2 65 ? -10.864 -1.356 24.435 1.00 92.71 ? 65 GLU B O 1 ATOM 7673 C CB . GLU B 2 65 ? -9.219 -2.463 22.186 1.00 98.36 ? 65 GLU B CB 1 ATOM 7674 C CG . GLU B 2 65 ? -8.075 -2.845 23.109 1.00 117.06 ? 65 GLU B CG 1 ATOM 7675 C CD . GLU B 2 65 ? -6.758 -2.228 22.685 1.00 135.20 ? 65 GLU B CD 1 ATOM 7676 O OE1 . GLU B 2 65 ? -5.703 -2.646 23.209 1.00 132.77 ? 65 GLU B OE1 1 ATOM 7677 O OE2 . GLU B 2 65 ? -6.774 -1.319 21.828 1.00 149.24 ? 65 GLU B OE2 1 ATOM 7678 N N . ASP B 2 66 ? -10.933 -3.534 24.989 1.00 102.52 ? 66 ASP B N 1 ATOM 7679 C CA . ASP B 2 66 ? -10.855 -3.269 26.420 1.00 107.38 ? 66 ASP B CA 1 ATOM 7680 C C . ASP B 2 66 ? -9.921 -4.267 27.095 1.00 93.11 ? 66 ASP B C 1 ATOM 7681 O O . ASP B 2 66 ? -10.208 -5.459 27.162 1.00 95.96 ? 66 ASP B O 1 ATOM 7682 C CB . ASP B 2 66 ? -12.246 -3.303 27.070 1.00 114.30 ? 66 ASP B CB 1 ATOM 7683 C CG . ASP B 2 66 ? -12.950 -4.634 26.893 1.00 110.04 ? 66 ASP B CG 1 ATOM 7684 O OD1 . ASP B 2 66 ? -12.754 -5.283 25.844 1.00 126.12 ? 66 ASP B OD1 1 ATOM 7685 O OD2 . ASP B 2 66 ? -13.701 -5.032 27.808 1.00 97.16 ? 66 ASP B OD2 1 ATOM 7686 N N . ARG B 2 67 ? -8.797 -3.768 27.590 1.00 106.66 ? 67 ARG B N 1 ATOM 7687 C CA . ARG B 2 67 ? -7.880 -4.585 28.368 1.00 104.87 ? 67 ARG B CA 1 ATOM 7688 C C . ARG B 2 67 ? -8.236 -4.457 29.842 1.00 97.23 ? 67 ARG B C 1 ATOM 7689 O O . ARG B 2 67 ? -8.754 -3.422 30.266 1.00 98.49 ? 67 ARG B O 1 ATOM 7690 C CB . ARG B 2 67 ? -6.428 -4.167 28.117 1.00 115.66 ? 67 ARG B CB 1 ATOM 7691 C CG . ARG B 2 67 ? -5.978 -4.309 26.669 1.00 104.24 ? 67 ARG B CG 1 ATOM 7692 C CD . ARG B 2 67 ? -4.487 -4.049 26.523 1.00 100.39 ? 67 ARG B CD 1 ATOM 7693 N NE . ARG B 2 67 ? -4.092 -2.767 27.101 1.00 106.71 ? 67 ARG B NE 1 ATOM 7694 C CZ . ARG B 2 67 ? -4.024 -1.626 26.421 1.00 99.33 ? 67 ARG B CZ 1 ATOM 7695 N NH1 . ARG B 2 67 ? -4.321 -1.602 25.128 1.00 109.19 ? 67 ARG B NH1 1 ATOM 7696 N NH2 . ARG B 2 67 ? -3.654 -0.509 27.032 1.00 88.78 ? 67 ARG B NH2 1 ATOM 7697 N N . PRO B 2 68 ? -7.973 -5.509 30.631 1.00 98.31 ? 68 PRO B N 1 ATOM 7698 C CA . PRO B 2 68 ? -8.195 -5.387 32.074 1.00 106.56 ? 68 PRO B CA 1 ATOM 7699 C C . PRO B 2 68 ? -7.272 -4.333 32.677 1.00 102.15 ? 68 PRO B C 1 ATOM 7700 O O . PRO B 2 68 ? -6.237 -4.024 32.085 1.00 96.74 ? 68 PRO B O 1 ATOM 7701 C CB . PRO B 2 68 ? -7.862 -6.786 32.603 1.00 102.93 ? 68 PRO B CB 1 ATOM 7702 C CG . PRO B 2 68 ? -6.965 -7.382 31.568 1.00 104.86 ? 68 PRO B CG 1 ATOM 7703 C CD . PRO B 2 68 ? -7.455 -6.837 30.260 1.00 102.25 ? 68 PRO B CD 1 ATOM 7704 N N . LEU B 2 69 ? -7.635 -3.788 33.832 1.00 96.20 ? 69 LEU B N 1 ATOM 7705 C CA . LEU B 2 69 ? -6.796 -2.789 34.479 1.00 95.00 ? 69 LEU B CA 1 ATOM 7706 C C . LEU B 2 69 ? -5.548 -3.451 35.053 1.00 98.46 ? 69 LEU B C 1 ATOM 7707 O O . LEU B 2 69 ? -5.360 -4.660 34.921 1.00 150.47 ? 69 LEU B O 1 ATOM 7708 C CB . LEU B 2 69 ? -7.569 -2.055 35.576 1.00 93.74 ? 69 LEU B CB 1 ATOM 7709 C CG . LEU B 2 69 ? -8.820 -1.303 35.114 1.00 90.62 ? 69 LEU B CG 1 ATOM 7710 C CD1 . LEU B 2 69 ? -9.548 -0.688 36.296 1.00 90.23 ? 69 LEU B CD1 1 ATOM 7711 C CD2 . LEU B 2 69 ? -8.462 -0.241 34.089 1.00 87.39 ? 69 LEU B CD2 1 ATOM 7712 N N . SER B 2 70 ? -4.690 -2.660 35.683 1.00 98.02 ? 70 SER B N 1 ATOM 7713 C CA . SER B 2 70 ? -3.443 -3.189 36.221 1.00 101.51 ? 70 SER B CA 1 ATOM 7714 C C . SER B 2 70 ? -3.387 -3.054 37.737 1.00 103.27 ? 70 SER B C 1 ATOM 7715 O O . SER B 2 70 ? -3.774 -2.029 38.294 1.00 109.64 ? 70 SER B O 1 ATOM 7716 C CB . SER B 2 70 ? -2.246 -2.479 35.586 1.00 125.72 ? 70 SER B CB 1 ATOM 7717 O OG . SER B 2 70 ? -2.256 -2.621 34.177 1.00 114.62 ? 70 SER B OG 1 ATOM 7718 N N . ASP B 2 71 ? -2.920 -4.105 38.400 1.00 107.71 ? 71 ASP B N 1 ATOM 7719 C CA . ASP B 2 71 ? -2.699 -4.058 39.838 1.00 121.04 ? 71 ASP B CA 1 ATOM 7720 C C . ASP B 2 71 ? -1.374 -3.370 40.157 1.00 122.91 ? 71 ASP B C 1 ATOM 7721 O O . ASP B 2 71 ? -1.256 -2.661 41.156 1.00 124.28 ? 71 ASP B O 1 ATOM 7722 C CB . ASP B 2 71 ? -2.730 -5.468 40.432 1.00 137.08 ? 71 ASP B CB 1 ATOM 7723 C CG . ASP B 2 71 ? -1.893 -6.453 39.640 1.00 157.97 ? 71 ASP B CG 1 ATOM 7724 O OD1 . ASP B 2 71 ? -1.740 -6.254 38.417 1.00 161.17 ? 71 ASP B OD1 1 ATOM 7725 O OD2 . ASP B 2 71 ? -1.392 -7.427 40.240 1.00 156.26 ? 71 ASP B OD2 1 ATOM 7726 N N . LYS B 2 72 ? -0.383 -3.577 39.294 1.00 123.34 ? 72 LYS B N 1 ATOM 7727 C CA . LYS B 2 72 ? 0.950 -3.018 39.497 1.00 130.38 ? 72 LYS B CA 1 ATOM 7728 C C . LYS B 2 72 ? 1.459 -2.314 38.243 1.00 129.98 ? 72 LYS B C 1 ATOM 7729 O O . LYS B 2 72 ? 0.897 -2.471 37.159 1.00 120.97 ? 72 LYS B O 1 ATOM 7730 C CB . LYS B 2 72 ? 1.935 -4.115 39.913 1.00 133.07 ? 72 LYS B CB 1 ATOM 7731 C CG . LYS B 2 72 ? 1.542 -4.869 41.175 1.00 143.93 ? 72 LYS B CG 1 ATOM 7732 C CD . LYS B 2 72 ? 1.438 -3.938 42.372 1.00 154.31 ? 72 LYS B CD 1 ATOM 7733 C CE . LYS B 2 72 ? 2.773 -3.285 42.688 1.00 158.48 ? 72 LYS B CE 1 ATOM 7734 N NZ . LYS B 2 72 ? 2.674 -2.364 43.853 1.00 154.28 ? 72 LYS B NZ 1 ATOM 7735 N N . GLY B 2 73 ? 2.526 -1.536 38.400 1.00 131.35 ? 73 GLY B N 1 ATOM 7736 C CA . GLY B 2 73 ? 3.101 -0.786 37.296 1.00 106.38 ? 73 GLY B CA 1 ATOM 7737 C C . GLY B 2 73 ? 4.393 -1.370 36.752 1.00 122.56 ? 73 GLY B C 1 ATOM 7738 O O . GLY B 2 73 ? 5.156 -0.677 36.079 1.00 121.63 ? 73 GLY B O 1 ATOM 7739 N N . SER B 2 74 ? 4.642 -2.643 37.041 1.00 128.16 ? 74 SER B N 1 ATOM 7740 C CA . SER B 2 74 ? 5.876 -3.294 36.604 1.00 139.81 ? 74 SER B CA 1 ATOM 7741 C C . SER B 2 74 ? 5.860 -3.609 35.110 1.00 154.83 ? 74 SER B C 1 ATOM 7742 O O . SER B 2 74 ? 4.890 -3.313 34.413 1.00 158.23 ? 74 SER B O 1 ATOM 7743 C CB . SER B 2 74 ? 6.115 -4.571 37.410 1.00 156.22 ? 74 SER B CB 1 ATOM 7744 O OG . SER B 2 74 ? 6.326 -4.270 38.779 1.00 171.13 ? 74 SER B OG 1 ATOM 7745 N N . GLY B 2 75 ? 6.944 -4.207 34.625 1.00 159.79 ? 75 GLY B N 1 ATOM 7746 C CA . GLY B 2 75 ? 7.129 -4.423 33.201 1.00 155.58 ? 75 GLY B CA 1 ATOM 7747 C C . GLY B 2 75 ? 6.575 -5.706 32.609 1.00 153.09 ? 75 GLY B C 1 ATOM 7748 O O . GLY B 2 75 ? 6.259 -5.750 31.420 1.00 165.07 ? 75 GLY B O 1 ATOM 7749 N N . ASP B 2 76 ? 6.455 -6.752 33.421 1.00 135.53 ? 76 ASP B N 1 ATOM 7750 C CA . ASP B 2 76 ? 6.054 -8.061 32.906 1.00 145.30 ? 76 ASP B CA 1 ATOM 7751 C C . ASP B 2 76 ? 4.572 -8.138 32.558 1.00 145.83 ? 76 ASP B C 1 ATOM 7752 O O . ASP B 2 76 ? 4.131 -9.095 31.921 1.00 132.06 ? 76 ASP B O 1 ATOM 7753 C CB . ASP B 2 76 ? 6.413 -9.163 33.903 1.00 166.37 ? 76 ASP B CB 1 ATOM 7754 C CG . ASP B 2 76 ? 7.834 -9.659 33.727 1.00 175.66 ? 76 ASP B CG 1 ATOM 7755 O OD1 . ASP B 2 76 ? 8.058 -10.883 33.844 1.00 147.11 ? 76 ASP B OD1 1 ATOM 7756 O OD2 . ASP B 2 76 ? 8.728 -8.825 33.466 1.00 163.14 ? 76 ASP B OD2 1 ATOM 7757 N N . SER B 2 77 ? 3.805 -7.139 32.980 1.00 162.19 ? 77 SER B N 1 ATOM 7758 C CA . SER B 2 77 ? 2.440 -6.995 32.494 1.00 166.54 ? 77 SER B CA 1 ATOM 7759 C C . SER B 2 77 ? 2.512 -6.755 30.991 1.00 173.21 ? 77 SER B C 1 ATOM 7760 O O . SER B 2 77 ? 3.500 -6.197 30.510 1.00 177.33 ? 77 SER B O 1 ATOM 7761 C CB . SER B 2 77 ? 1.720 -5.849 33.207 1.00 147.17 ? 77 SER B CB 1 ATOM 7762 O OG . SER B 2 77 ? 2.494 -4.661 33.178 1.00 126.17 ? 77 SER B OG 1 ATOM 7763 N N . SER B 2 78 ? 1.491 -7.190 30.254 1.00 170.18 ? 78 SER B N 1 ATOM 7764 C CA . SER B 2 78 ? 1.483 -7.047 28.797 1.00 160.14 ? 78 SER B CA 1 ATOM 7765 C C . SER B 2 78 ? 1.781 -5.601 28.426 1.00 141.84 ? 78 SER B C 1 ATOM 7766 O O . SER B 2 78 ? 2.723 -5.319 27.685 1.00 145.60 ? 78 SER B O 1 ATOM 7767 C CB . SER B 2 78 ? 0.140 -7.486 28.215 1.00 149.34 ? 78 SER B CB 1 ATOM 7768 O OG . SER B 2 78 ? 0.138 -7.390 26.801 1.00 151.60 ? 78 SER B OG 1 ATOM 7769 N N . GLN B 2 79 ? 0.968 -4.700 28.965 1.00 107.16 ? 79 GLN B N 1 ATOM 7770 C CA . GLN B 2 79 ? 1.290 -3.282 29.055 1.00 112.13 ? 79 GLN B CA 1 ATOM 7771 C C . GLN B 2 79 ? 0.641 -2.758 30.329 1.00 120.32 ? 79 GLN B C 1 ATOM 7772 O O . GLN B 2 79 ? -0.057 -3.500 31.018 1.00 142.73 ? 79 GLN B O 1 ATOM 7773 C CB . GLN B 2 79 ? 0.800 -2.504 27.830 1.00 124.77 ? 79 GLN B CB 1 ATOM 7774 C CG . GLN B 2 79 ? 1.657 -2.670 26.580 1.00 143.48 ? 79 GLN B CG 1 ATOM 7775 C CD . GLN B 2 79 ? 3.117 -2.324 26.817 1.00 152.66 ? 79 GLN B CD 1 ATOM 7776 O OE1 . GLN B 2 79 ? 3.436 -1.373 27.531 1.00 158.72 ? 79 GLN B OE1 1 ATOM 7777 N NE2 . GLN B 2 79 ? 4.013 -3.104 26.221 1.00 138.32 ? 79 GLN B NE2 1 ATOM 7778 N N . VAL B 2 80 ? 0.858 -1.487 30.645 1.00 98.16 ? 80 VAL B N 1 ATOM 7779 C CA . VAL B 2 80 ? 0.197 -0.886 31.795 1.00 107.61 ? 80 VAL B CA 1 ATOM 7780 C C . VAL B 2 80 ? -1.105 -0.235 31.348 1.00 122.30 ? 80 VAL B C 1 ATOM 7781 O O . VAL B 2 80 ? -1.102 0.687 30.532 1.00 129.55 ? 80 VAL B O 1 ATOM 7782 C CB . VAL B 2 80 ? 1.094 0.149 32.502 1.00 113.40 ? 80 VAL B CB 1 ATOM 7783 C CG1 . VAL B 2 80 ? 0.267 1.042 33.420 1.00 127.38 ? 80 VAL B CG1 1 ATOM 7784 C CG2 . VAL B 2 80 ? 2.194 -0.559 33.286 1.00 106.31 ? 80 VAL B CG2 1 ATOM 7785 N N . THR B 2 81 ? -2.219 -0.729 31.880 1.00 92.45 ? 81 THR B N 1 ATOM 7786 C CA . THR B 2 81 ? -3.528 -0.180 31.546 1.00 89.33 ? 81 THR B CA 1 ATOM 7787 C C . THR B 2 81 ? -4.160 0.514 32.750 1.00 87.81 ? 81 THR B C 1 ATOM 7788 O O . THR B 2 81 ? -4.610 -0.138 33.694 1.00 89.74 ? 81 THR B O 1 ATOM 7789 C CB . THR B 2 81 ? -4.477 -1.278 31.038 1.00 118.12 ? 81 THR B CB 1 ATOM 7790 O OG1 . THR B 2 81 ? -3.908 -1.905 29.883 1.00 116.72 ? 81 THR B OG1 1 ATOM 7791 C CG2 . THR B 2 81 ? -5.829 -0.694 30.680 1.00 117.40 ? 81 THR B CG2 1 ATOM 7792 N N . GLN B 2 82 ? -4.190 1.842 32.711 1.00 90.00 ? 82 GLN B N 1 ATOM 7793 C CA . GLN B 2 82 ? -4.839 2.621 33.759 1.00 88.84 ? 82 GLN B CA 1 ATOM 7794 C C . GLN B 2 82 ? -6.245 3.059 33.353 1.00 81.24 ? 82 GLN B C 1 ATOM 7795 O O . GLN B 2 82 ? -6.965 3.672 34.142 1.00 80.03 ? 82 GLN B O 1 ATOM 7796 C CB . GLN B 2 82 ? -3.987 3.841 34.117 1.00 82.15 ? 82 GLN B CB 1 ATOM 7797 C CG . GLN B 2 82 ? -2.737 3.504 34.919 1.00 91.34 ? 82 GLN B CG 1 ATOM 7798 C CD . GLN B 2 82 ? -1.971 4.739 35.346 1.00 99.45 ? 82 GLN B CD 1 ATOM 7799 O OE1 . GLN B 2 82 ? -1.470 4.815 36.467 1.00 120.67 ? 82 GLN B OE1 1 ATOM 7800 N NE2 . GLN B 2 82 ? -1.872 5.713 34.449 1.00 96.97 ? 82 GLN B NE2 1 ATOM 7801 N N . VAL B 2 83 ? -6.631 2.739 32.120 1.00 80.99 ? 83 VAL B N 1 ATOM 7802 C CA . VAL B 2 83 ? -7.924 3.160 31.583 1.00 79.19 ? 83 VAL B CA 1 ATOM 7803 C C . VAL B 2 83 ? -8.603 2.052 30.784 1.00 80.38 ? 83 VAL B C 1 ATOM 7804 O O . VAL B 2 83 ? -8.020 1.506 29.848 1.00 81.37 ? 83 VAL B O 1 ATOM 7805 C CB . VAL B 2 83 ? -7.778 4.401 30.672 1.00 80.63 ? 83 VAL B CB 1 ATOM 7806 C CG1 . VAL B 2 83 ? -9.053 4.635 29.874 1.00 83.94 ? 83 VAL B CG1 1 ATOM 7807 C CG2 . VAL B 2 83 ? -7.418 5.631 31.488 1.00 75.46 ? 83 VAL B CG2 1 ATOM 7808 N N . SER B 2 84 ? -9.843 1.732 31.142 1.00 85.18 ? 84 SER B N 1 ATOM 7809 C CA . SER B 2 84 ? -10.621 0.754 30.390 1.00 90.20 ? 84 SER B CA 1 ATOM 7810 C C . SER B 2 84 ? -12.053 1.241 30.188 1.00 88.19 ? 84 SER B C 1 ATOM 7811 O O . SER B 2 84 ? -12.649 1.809 31.103 1.00 87.39 ? 84 SER B O 1 ATOM 7812 C CB . SER B 2 84 ? -10.619 -0.599 31.106 1.00 85.01 ? 84 SER B CB 1 ATOM 7813 O OG . SER B 2 84 ? -11.399 -1.549 30.403 1.00 86.53 ? 84 SER B OG 1 ATOM 7814 N N . PRO B 2 85 ? -12.617 1.014 28.991 1.00 91.43 ? 85 PRO B N 1 ATOM 7815 C CA . PRO B 2 85 ? -11.983 0.421 27.806 1.00 91.13 ? 85 PRO B CA 1 ATOM 7816 C C . PRO B 2 85 ? -11.000 1.365 27.109 1.00 79.81 ? 85 PRO B C 1 ATOM 7817 O O . PRO B 2 85 ? -10.720 2.451 27.616 1.00 78.19 ? 85 PRO B O 1 ATOM 7818 C CB . PRO B 2 85 ? -13.175 0.118 26.893 1.00 82.13 ? 85 PRO B CB 1 ATOM 7819 C CG . PRO B 2 85 ? -14.198 1.117 27.281 1.00 80.17 ? 85 PRO B CG 1 ATOM 7820 C CD . PRO B 2 85 ? -14.048 1.284 28.765 1.00 79.94 ? 85 PRO B CD 1 ATOM 7821 N N . GLN B 2 86 ? -10.497 0.948 25.951 1.00 80.95 ? 86 GLN B N 1 ATOM 7822 C CA . GLN B 2 86 ? -9.531 1.741 25.196 1.00 79.76 ? 86 GLN B CA 1 ATOM 7823 C C . GLN B 2 86 ? -10.139 2.296 23.909 1.00 84.55 ? 86 GLN B C 1 ATOM 7824 O O . GLN B 2 86 ? -10.216 3.510 23.724 1.00 109.25 ? 86 GLN B O 1 ATOM 7825 C CB . GLN B 2 86 ? -8.287 0.911 24.876 1.00 84.75 ? 86 GLN B CB 1 ATOM 7826 C CG . GLN B 2 86 ? -7.439 0.567 26.093 1.00 85.41 ? 86 GLN B CG 1 ATOM 7827 C CD . GLN B 2 86 ? -7.980 -0.613 26.879 1.00 91.06 ? 86 GLN B CD 1 ATOM 7828 O OE1 . GLN B 2 86 ? -8.013 -1.739 26.384 1.00 88.15 ? 86 GLN B OE1 1 ATOM 7829 N NE2 . GLN B 2 86 ? -8.406 -0.361 28.112 1.00 88.08 ? 86 GLN B NE2 1 ATOM 7830 N N . ARG B 2 87 ? -10.546 1.407 23.011 1.00 81.21 ? 87 ARG B N 1 ATOM 7831 C CA . ARG B 2 87 ? -11.159 1.829 21.756 1.00 86.09 ? 87 ARG B CA 1 ATOM 7832 C C . ARG B 2 87 ? -12.657 1.540 21.740 1.00 84.82 ? 87 ARG B C 1 ATOM 7833 O O . ARG B 2 87 ? -13.094 0.457 22.130 1.00 83.50 ? 87 ARG B O 1 ATOM 7834 C CB . ARG B 2 87 ? -10.482 1.139 20.571 1.00 98.16 ? 87 ARG B CB 1 ATOM 7835 C CG . ARG B 2 87 ? -8.970 1.274 20.557 1.00 104.23 ? 87 ARG B CG 1 ATOM 7836 C CD . ARG B 2 87 ? -8.393 0.889 19.206 1.00 112.12 ? 87 ARG B CD 1 ATOM 7837 N NE . ARG B 2 87 ? -8.883 1.763 18.143 1.00 122.81 ? 87 ARG B NE 1 ATOM 7838 C CZ . ARG B 2 87 ? -8.379 2.964 17.873 1.00 124.67 ? 87 ARG B CZ 1 ATOM 7839 N NH1 . ARG B 2 87 ? -7.370 3.440 18.588 1.00 96.80 ? 87 ARG B NH1 1 ATOM 7840 N NH2 . ARG B 2 87 ? -8.888 3.689 16.887 1.00 137.88 ? 87 ARG B NH2 1 ATOM 7841 N N . ILE B 2 88 ? -13.441 2.516 21.293 1.00 95.84 ? 88 ILE B N 1 ATOM 7842 C CA . ILE B 2 88 ? -14.886 2.346 21.176 1.00 100.67 ? 88 ILE B CA 1 ATOM 7843 C C . ILE B 2 88 ? -15.390 2.837 19.822 1.00 95.05 ? 88 ILE B C 1 ATOM 7844 O O . ILE B 2 88 ? -15.143 3.979 19.433 1.00 79.74 ? 88 ILE B O 1 ATOM 7845 C CB . ILE B 2 88 ? -15.643 3.093 22.293 1.00 100.71 ? 88 ILE B CB 1 ATOM 7846 C CG1 . ILE B 2 88 ? -15.296 2.512 23.665 1.00 109.36 ? 88 ILE B CG1 1 ATOM 7847 C CG2 . ILE B 2 88 ? -17.145 3.022 22.060 1.00 79.80 ? 88 ILE B CG2 1 ATOM 7848 C CD1 . ILE B 2 88 ? -16.051 3.154 24.810 1.00 112.76 ? 88 ILE B CD1 1 ATOM 7849 N N . ALA B 2 89 ? -16.097 1.968 19.107 1.00 98.69 ? 89 ALA B N 1 ATOM 7850 C CA . ALA B 2 89 ? -16.692 2.338 17.831 1.00 97.13 ? 89 ALA B CA 1 ATOM 7851 C C . ALA B 2 89 ? -18.089 2.908 18.048 1.00 100.93 ? 89 ALA B C 1 ATOM 7852 O O . ALA B 2 89 ? -18.979 2.221 18.553 1.00 119.84 ? 89 ALA B O 1 ATOM 7853 C CB . ALA B 2 89 ? -16.741 1.140 16.896 1.00 108.02 ? 89 ALA B CB 1 ATOM 7854 N N . LEU B 2 90 ? -18.276 4.167 17.667 1.00 92.70 ? 90 LEU B N 1 ATOM 7855 C CA . LEU B 2 90 ? -19.549 4.848 17.872 1.00 97.72 ? 90 LEU B CA 1 ATOM 7856 C C . LEU B 2 90 ? -20.248 5.145 16.547 1.00 85.25 ? 90 LEU B C 1 ATOM 7857 O O . LEU B 2 90 ? -19.695 5.818 15.678 1.00 85.15 ? 90 LEU B O 1 ATOM 7858 C CB . LEU B 2 90 ? -19.335 6.145 18.657 1.00 103.88 ? 90 LEU B CB 1 ATOM 7859 C CG . LEU B 2 90 ? -20.581 6.952 19.027 1.00 99.92 ? 90 LEU B CG 1 ATOM 7860 C CD1 . LEU B 2 90 ? -21.491 6.150 19.941 1.00 94.50 ? 90 LEU B CD1 1 ATOM 7861 C CD2 . LEU B 2 90 ? -20.192 8.269 19.678 1.00 91.78 ? 90 LEU B CD2 1 ATOM 7862 N N . ARG B 2 91 ? -21.466 4.633 16.399 1.00 87.47 ? 91 ARG B N 1 ATOM 7863 C CA . ARG B 2 91 ? -22.262 4.874 15.202 1.00 90.04 ? 91 ARG B CA 1 ATOM 7864 C C . ARG B 2 91 ? -23.564 5.565 15.586 1.00 102.05 ? 91 ARG B C 1 ATOM 7865 O O . ARG B 2 91 ? -24.290 5.089 16.457 1.00 102.31 ? 91 ARG B O 1 ATOM 7866 C CB . ARG B 2 91 ? -22.542 3.564 14.462 1.00 115.09 ? 91 ARG B CB 1 ATOM 7867 C CG . ARG B 2 91 ? -21.319 2.670 14.320 1.00 128.60 ? 91 ARG B CG 1 ATOM 7868 C CD . ARG B 2 91 ? -21.589 1.461 13.436 1.00 139.85 ? 91 ARG B CD 1 ATOM 7869 N NE . ARG B 2 91 ? -21.631 1.811 12.019 1.00 148.59 ? 91 ARG B NE 1 ATOM 7870 C CZ . ARG B 2 91 ? -22.748 1.913 11.305 1.00 153.37 ? 91 ARG B CZ 1 ATOM 7871 N NH1 . ARG B 2 91 ? -23.924 1.684 11.873 1.00 147.30 ? 91 ARG B NH1 1 ATOM 7872 N NH2 . ARG B 2 91 ? -22.688 2.237 10.020 1.00 156.06 ? 91 ARG B NH2 1 ATOM 7873 N N . LEU B 2 92 ? -23.855 6.689 14.941 1.00 107.72 ? 92 LEU B N 1 ATOM 7874 C CA . LEU B 2 92 ? -25.007 7.501 15.320 1.00 100.14 ? 92 LEU B CA 1 ATOM 7875 C C . LEU B 2 92 ? -25.869 7.921 14.135 1.00 116.79 ? 92 LEU B C 1 ATOM 7876 O O . LEU B 2 92 ? -25.362 8.407 13.124 1.00 128.33 ? 92 LEU B O 1 ATOM 7877 C CB . LEU B 2 92 ? -24.542 8.748 16.079 1.00 87.34 ? 92 LEU B CB 1 ATOM 7878 C CG . LEU B 2 92 ? -24.059 8.553 17.518 1.00 85.37 ? 92 LEU B CG 1 ATOM 7879 C CD1 . LEU B 2 92 ? -23.390 9.817 18.040 1.00 97.18 ? 92 LEU B CD1 1 ATOM 7880 C CD2 . LEU B 2 92 ? -25.219 8.153 18.415 1.00 86.23 ? 92 LEU B CD2 1 ATOM 7881 N N . ARG B 2 93 ? -27.177 7.722 14.271 1.00 100.71 ? 93 ARG B N 1 ATOM 7882 C CA . ARG B 2 93 ? -28.141 8.295 13.341 1.00 104.42 ? 93 ARG B CA 1 ATOM 7883 C C . ARG B 2 93 ? -28.473 9.701 13.839 1.00 141.95 ? 93 ARG B C 1 ATOM 7884 O O . ARG B 2 93 ? -28.326 9.976 15.030 1.00 151.58 ? 93 ARG B O 1 ATOM 7885 C CB . ARG B 2 93 ? -29.393 7.417 13.232 1.00 118.67 ? 93 ARG B CB 1 ATOM 7886 C CG . ARG B 2 93 ? -30.217 7.304 14.505 1.00 131.76 ? 93 ARG B CG 1 ATOM 7887 C CD . ARG B 2 93 ? -31.410 6.383 14.291 1.00 114.84 ? 93 ARG B CD 1 ATOM 7888 N NE . ARG B 2 93 ? -32.280 6.858 13.218 1.00 109.33 ? 93 ARG B NE 1 ATOM 7889 C CZ . ARG B 2 93 ? -33.251 6.138 12.666 1.00 132.44 ? 93 ARG B CZ 1 ATOM 7890 N NH1 . ARG B 2 93 ? -33.481 4.900 13.081 1.00 143.27 ? 93 ARG B NH1 1 ATOM 7891 N NH2 . ARG B 2 93 ? -33.993 6.656 11.695 1.00 146.83 ? 93 ARG B NH2 1 ATOM 7892 N N . PRO B 2 94 ? -28.896 10.602 12.934 1.00 148.48 ? 94 PRO B N 1 ATOM 7893 C CA . PRO B 2 94 ? -29.090 12.018 13.279 1.00 139.65 ? 94 PRO B CA 1 ATOM 7894 C C . PRO B 2 94 ? -29.976 12.262 14.502 1.00 124.97 ? 94 PRO B C 1 ATOM 7895 O O . PRO B 2 94 ? -30.986 11.581 14.679 1.00 122.15 ? 94 PRO B O 1 ATOM 7896 C CB . PRO B 2 94 ? -29.750 12.591 12.023 1.00 142.20 ? 94 PRO B CB 1 ATOM 7897 C CG . PRO B 2 94 ? -29.266 11.724 10.923 1.00 141.03 ? 94 PRO B CG 1 ATOM 7898 C CD . PRO B 2 94 ? -29.168 10.347 11.507 1.00 136.27 ? 94 PRO B CD 1 ATOM 7899 N N . ASP B 2 95 ? -29.576 13.230 15.325 1.00 110.06 ? 95 ASP B N 1 ATOM 7900 C CA . ASP B 2 95 ? -30.311 13.627 16.526 1.00 113.32 ? 95 ASP B CA 1 ATOM 7901 C C . ASP B 2 95 ? -30.517 12.472 17.505 1.00 124.21 ? 95 ASP B C 1 ATOM 7902 O O . ASP B 2 95 ? -31.564 12.374 18.146 1.00 149.58 ? 95 ASP B O 1 ATOM 7903 C CB . ASP B 2 95 ? -31.667 14.236 16.149 1.00 130.29 ? 95 ASP B CB 1 ATOM 7904 C CG . ASP B 2 95 ? -31.530 15.554 15.410 1.00 146.86 ? 95 ASP B CG 1 ATOM 7905 O OD1 . ASP B 2 95 ? -30.582 16.312 15.708 1.00 133.96 ? 95 ASP B OD1 1 ATOM 7906 O OD2 . ASP B 2 95 ? -32.371 15.834 14.529 1.00 163.12 ? 95 ASP B OD2 1 ATOM 7907 N N . ASP B 2 96 ? -29.515 11.607 17.625 1.00 112.05 ? 96 ASP B N 1 ATOM 7908 C CA . ASP B 2 96 ? -29.596 10.473 18.541 1.00 110.99 ? 96 ASP B CA 1 ATOM 7909 C C . ASP B 2 96 ? -28.358 10.390 19.430 1.00 118.54 ? 96 ASP B C 1 ATOM 7910 O O . ASP B 2 96 ? -27.306 10.936 19.096 1.00 114.44 ? 96 ASP B O 1 ATOM 7911 C CB . ASP B 2 96 ? -29.777 9.167 17.763 1.00 99.93 ? 96 ASP B CB 1 ATOM 7912 C CG . ASP B 2 96 ? -30.167 8.005 18.656 1.00 124.69 ? 96 ASP B CG 1 ATOM 7913 O OD1 . ASP B 2 96 ? -30.609 8.255 19.797 1.00 128.22 ? 96 ASP B OD1 1 ATOM 7914 O OD2 . ASP B 2 96 ? -30.040 6.844 18.216 1.00 155.26 ? 96 ASP B OD2 1 ATOM 7915 N N . SER B 2 97 ? -28.489 9.706 20.563 1.00 116.06 ? 97 SER B N 1 ATOM 7916 C CA . SER B 2 97 ? -27.394 9.595 21.519 1.00 115.00 ? 97 SER B CA 1 ATOM 7917 C C . SER B 2 97 ? -27.313 8.217 22.168 1.00 112.01 ? 97 SER B C 1 ATOM 7918 O O . SER B 2 97 ? -28.331 7.631 22.539 1.00 128.44 ? 97 SER B O 1 ATOM 7919 C CB . SER B 2 97 ? -27.534 10.660 22.607 1.00 128.93 ? 97 SER B CB 1 ATOM 7920 O OG . SER B 2 97 ? -28.766 10.526 23.295 1.00 141.76 ? 97 SER B OG 1 ATOM 7921 N N . LYS B 2 98 ? -26.092 7.709 22.297 1.00 95.94 ? 98 LYS B N 1 ATOM 7922 C CA . LYS B 2 98 ? -25.836 6.486 23.049 1.00 107.52 ? 98 LYS B CA 1 ATOM 7923 C C . LYS B 2 98 ? -24.836 6.789 24.160 1.00 106.42 ? 98 LYS B C 1 ATOM 7924 O O . LYS B 2 98 ? -23.927 7.598 23.976 1.00 81.33 ? 98 LYS B O 1 ATOM 7925 C CB . LYS B 2 98 ? -25.307 5.378 22.136 1.00 110.74 ? 98 LYS B CB 1 ATOM 7926 C CG . LYS B 2 98 ? -26.212 5.055 20.957 1.00 116.61 ? 98 LYS B CG 1 ATOM 7927 C CD . LYS B 2 98 ? -27.583 4.582 21.416 1.00 114.62 ? 98 LYS B CD 1 ATOM 7928 C CE . LYS B 2 98 ? -27.490 3.269 22.177 1.00 112.71 ? 98 LYS B CE 1 ATOM 7929 N NZ . LYS B 2 98 ? -28.833 2.769 22.581 1.00 112.34 ? 98 LYS B NZ 1 ATOM 7930 N N . ASN B 2 99 ? -25.005 6.148 25.312 1.00 126.08 ? 99 ASN B N 1 ATOM 7931 C CA . ASN B 2 99 ? -24.128 6.412 26.446 1.00 115.67 ? 99 ASN B CA 1 ATOM 7932 C C . ASN B 2 99 ? -23.252 5.220 26.814 1.00 89.46 ? 99 ASN B C 1 ATOM 7933 O O . ASN B 2 99 ? -23.735 4.096 26.955 1.00 97.16 ? 99 ASN B O 1 ATOM 7934 C CB . ASN B 2 99 ? -24.947 6.852 27.664 1.00 132.92 ? 99 ASN B CB 1 ATOM 7935 C CG . ASN B 2 99 ? -26.078 5.895 27.993 1.00 147.10 ? 99 ASN B CG 1 ATOM 7936 O OD1 . ASN B 2 99 ? -27.079 5.832 27.279 1.00 148.90 ? 99 ASN B OD1 1 ATOM 7937 N ND2 . ASN B 2 99 ? -25.928 5.150 29.085 1.00 177.44 ? 99 ASN B ND2 1 ATOM 7938 N N . PHE B 2 100 ? -21.957 5.481 26.964 1.00 78.71 ? 100 PHE B N 1 ATOM 7939 C CA . PHE B 2 100 ? -20.995 4.448 27.328 1.00 78.70 ? 100 PHE B CA 1 ATOM 7940 C C . PHE B 2 100 ? -20.296 4.801 28.640 1.00 79.29 ? 100 PHE B C 1 ATOM 7941 O O . PHE B 2 100 ? -20.572 5.839 29.239 1.00 83.97 ? 100 PHE B O 1 ATOM 7942 C CB . PHE B 2 100 ? -19.970 4.249 26.208 1.00 78.39 ? 100 PHE B CB 1 ATOM 7943 C CG . PHE B 2 100 ? -19.224 5.499 25.831 1.00 78.81 ? 100 PHE B CG 1 ATOM 7944 C CD1 . PHE B 2 100 ? -18.022 5.814 26.441 1.00 96.86 ? 100 PHE B CD1 1 ATOM 7945 C CD2 . PHE B 2 100 ? -19.720 6.353 24.859 1.00 96.09 ? 100 PHE B CD2 1 ATOM 7946 C CE1 . PHE B 2 100 ? -17.331 6.960 26.096 1.00 99.74 ? 100 PHE B CE1 1 ATOM 7947 C CE2 . PHE B 2 100 ? -19.034 7.502 24.509 1.00 96.30 ? 100 PHE B CE2 1 ATOM 7948 C CZ . PHE B 2 100 ? -17.838 7.805 25.128 1.00 82.19 ? 100 PHE B CZ 1 ATOM 7949 N N . SER B 2 101 ? -19.393 3.933 29.083 1.00 87.38 ? 101 SER B N 1 ATOM 7950 C CA . SER B 2 101 ? -18.714 4.129 30.360 1.00 80.41 ? 101 SER B CA 1 ATOM 7951 C C . SER B 2 101 ? -17.208 3.923 30.249 1.00 82.53 ? 101 SER B C 1 ATOM 7952 O O . SER B 2 101 ? -16.727 3.255 29.334 1.00 99.35 ? 101 SER B O 1 ATOM 7953 C CB . SER B 2 101 ? -19.289 3.184 31.417 1.00 93.50 ? 101 SER B CB 1 ATOM 7954 O OG . SER B 2 101 ? -18.581 3.297 32.639 1.00 105.76 ? 101 SER B OG 1 ATOM 7955 N N . ILE B 2 102 ? -16.469 4.506 31.187 1.00 75.98 ? 102 ILE B N 1 ATOM 7956 C CA . ILE B 2 102 ? -15.018 4.367 31.227 1.00 85.49 ? 102 ILE B CA 1 ATOM 7957 C C . ILE B 2 102 ? -14.521 4.278 32.672 1.00 78.73 ? 102 ILE B C 1 ATOM 7958 O O . ILE B 2 102 ? -14.959 5.035 33.538 1.00 76.17 ? 102 ILE B O 1 ATOM 7959 C CB . ILE B 2 102 ? -14.322 5.546 30.502 1.00 80.96 ? 102 ILE B CB 1 ATOM 7960 C CG1 . ILE B 2 102 ? -12.802 5.472 30.670 1.00 89.65 ? 102 ILE B CG1 1 ATOM 7961 C CG2 . ILE B 2 102 ? -14.848 6.881 31.006 1.00 84.93 ? 102 ILE B CG2 1 ATOM 7962 C CD1 . ILE B 2 102 ? -12.067 6.657 30.078 1.00 99.74 ? 102 ILE B CD1 1 ATOM 7963 N N . GLN B 2 103 ? -13.618 3.336 32.929 1.00 83.05 ? 103 GLN B N 1 ATOM 7964 C CA . GLN B 2 103 ? -13.010 3.200 34.249 1.00 79.49 ? 103 GLN B CA 1 ATOM 7965 C C . GLN B 2 103 ? -11.581 3.731 34.241 1.00 78.51 ? 103 GLN B C 1 ATOM 7966 O O . GLN B 2 103 ? -10.831 3.505 33.291 1.00 78.13 ? 103 GLN B O 1 ATOM 7967 C CB . GLN B 2 103 ? -13.021 1.741 34.713 1.00 82.62 ? 103 GLN B CB 1 ATOM 7968 C CG . GLN B 2 103 ? -14.347 1.269 35.289 1.00 110.62 ? 103 GLN B CG 1 ATOM 7969 C CD . GLN B 2 103 ? -15.422 1.101 34.235 1.00 130.44 ? 103 GLN B CD 1 ATOM 7970 O OE1 . GLN B 2 103 ? -15.143 1.126 33.036 1.00 141.85 ? 103 GLN B OE1 1 ATOM 7971 N NE2 . GLN B 2 103 ? -16.662 0.929 34.678 1.00 125.92 ? 103 GLN B NE2 1 ATOM 7972 N N . VAL B 2 104 ? -11.213 4.441 35.302 1.00 78.39 ? 104 VAL B N 1 ATOM 7973 C CA . VAL B 2 104 ? -9.867 4.990 35.432 1.00 78.31 ? 104 VAL B CA 1 ATOM 7974 C C . VAL B 2 104 ? -9.272 4.651 36.796 1.00 80.20 ? 104 VAL B C 1 ATOM 7975 O O . VAL B 2 104 ? -9.889 4.896 37.832 1.00 81.11 ? 104 VAL B O 1 ATOM 7976 C CB . VAL B 2 104 ? -9.854 6.521 35.242 1.00 74.83 ? 104 VAL B CB 1 ATOM 7977 C CG1 . VAL B 2 104 ? -8.463 7.077 35.505 1.00 75.91 ? 104 VAL B CG1 1 ATOM 7978 C CG2 . VAL B 2 104 ? -10.317 6.892 33.842 1.00 74.65 ? 104 VAL B CG2 1 ATOM 7979 N N . ARG B 2 105 ? -8.070 4.087 36.788 1.00 98.27 ? 105 ARG B N 1 ATOM 7980 C CA . ARG B 2 105 ? -7.381 3.724 38.020 1.00 101.67 ? 105 ARG B CA 1 ATOM 7981 C C . ARG B 2 105 ? -5.927 4.179 37.989 1.00 91.98 ? 105 ARG B C 1 ATOM 7982 O O . ARG B 2 105 ? -5.239 4.012 36.984 1.00 88.42 ? 105 ARG B O 1 ATOM 7983 C CB . ARG B 2 105 ? -7.449 2.210 38.245 1.00 87.87 ? 105 ARG B CB 1 ATOM 7984 C CG . ARG B 2 105 ? -6.596 1.698 39.398 1.00 91.39 ? 105 ARG B CG 1 ATOM 7985 C CD . ARG B 2 105 ? -6.567 0.178 39.425 1.00 103.94 ? 105 ARG B CD 1 ATOM 7986 N NE . ARG B 2 105 ? -7.898 -0.388 39.618 1.00 107.90 ? 105 ARG B NE 1 ATOM 7987 C CZ . ARG B 2 105 ? -8.205 -1.664 39.410 1.00 97.81 ? 105 ARG B CZ 1 ATOM 7988 N NH1 . ARG B 2 105 ? -7.275 -2.512 38.991 1.00 99.81 ? 105 ARG B NH1 1 ATOM 7989 N NH2 . ARG B 2 105 ? -9.444 -2.092 39.613 1.00 98.35 ? 105 ARG B NH2 1 ATOM 7990 N N . GLN B 2 106 ? -5.460 4.755 39.090 1.00 85.28 ? 106 GLN B N 1 ATOM 7991 C CA . GLN B 2 106 ? -4.049 5.086 39.213 1.00 92.63 ? 106 GLN B CA 1 ATOM 7992 C C . GLN B 2 106 ? -3.341 3.921 39.883 1.00 96.58 ? 106 GLN B C 1 ATOM 7993 O O . GLN B 2 106 ? -3.539 3.658 41.066 1.00 92.73 ? 106 GLN B O 1 ATOM 7994 C CB . GLN B 2 106 ? -3.856 6.375 40.012 1.00 97.35 ? 106 GLN B CB 1 ATOM 7995 C CG . GLN B 2 106 ? -4.319 7.624 39.286 1.00 101.60 ? 106 GLN B CG 1 ATOM 7996 C CD . GLN B 2 106 ? -4.563 8.784 40.226 1.00 111.77 ? 106 GLN B CD 1 ATOM 7997 O OE1 . GLN B 2 106 ? -4.994 8.593 41.364 1.00 128.29 ? 106 GLN B OE1 1 ATOM 7998 N NE2 . GLN B 2 106 ? -4.291 9.997 39.757 1.00 87.49 ? 106 GLN B NE2 1 ATOM 7999 N N . VAL B 2 107 ? -2.510 3.225 39.117 1.00 91.09 ? 107 VAL B N 1 ATOM 8000 C CA . VAL B 2 107 ? -1.888 2.001 39.599 1.00 99.99 ? 107 VAL B CA 1 ATOM 8001 C C . VAL B 2 107 ? -0.735 2.301 40.548 1.00 111.54 ? 107 VAL B C 1 ATOM 8002 O O . VAL B 2 107 ? -0.045 3.312 40.410 1.00 109.05 ? 107 VAL B O 1 ATOM 8003 C CB . VAL B 2 107 ? -1.384 1.129 38.430 1.00 107.74 ? 107 VAL B CB 1 ATOM 8004 C CG1 . VAL B 2 107 ? -2.538 0.769 37.512 1.00 119.73 ? 107 VAL B CG1 1 ATOM 8005 C CG2 . VAL B 2 107 ? -0.305 1.851 37.649 1.00 105.34 ? 107 VAL B CG2 1 ATOM 8006 N N . GLU B 2 108 ? -0.547 1.426 41.529 1.00 102.18 ? 108 GLU B N 1 ATOM 8007 C CA . GLU B 2 108 ? 0.557 1.560 42.467 1.00 115.45 ? 108 GLU B CA 1 ATOM 8008 C C . GLU B 2 108 ? 1.862 1.167 41.787 1.00 125.89 ? 108 GLU B C 1 ATOM 8009 O O . GLU B 2 108 ? 1.850 0.464 40.775 1.00 125.20 ? 108 GLU B O 1 ATOM 8010 C CB . GLU B 2 108 ? 0.316 0.704 43.712 1.00 109.99 ? 108 GLU B CB 1 ATOM 8011 C CG . GLU B 2 108 ? -0.989 1.016 44.430 1.00 109.12 ? 108 GLU B CG 1 ATOM 8012 C CD . GLU B 2 108 ? -1.198 0.158 45.662 1.00 153.26 ? 108 GLU B CD 1 ATOM 8013 O OE1 . GLU B 2 108 ? -0.225 -0.480 46.119 1.00 170.72 ? 108 GLU B OE1 1 ATOM 8014 O OE2 . GLU B 2 108 ? -2.337 0.117 46.173 1.00 142.03 ? 108 GLU B OE2 1 ATOM 8015 N N . ASP B 2 109 ? 2.977 1.638 42.342 1.00 130.38 ? 109 ASP B N 1 ATOM 8016 C CA . ASP B 2 109 ? 4.308 1.357 41.806 1.00 124.88 ? 109 ASP B CA 1 ATOM 8017 C C . ASP B 2 109 ? 4.434 1.832 40.358 1.00 117.35 ? 109 ASP B C 1 ATOM 8018 O O . ASP B 2 109 ? 5.007 1.143 39.514 1.00 122.10 ? 109 ASP B O 1 ATOM 8019 C CB . ASP B 2 109 ? 4.625 -0.139 41.908 1.00 115.62 ? 109 ASP B CB 1 ATOM 8020 C CG . ASP B 2 109 ? 6.113 -0.428 41.865 1.00 136.01 ? 109 ASP B CG 1 ATOM 8021 O OD1 . ASP B 2 109 ? 6.895 0.496 41.556 1.00 117.76 ? 109 ASP B OD1 1 ATOM 8022 O OD2 . ASP B 2 109 ? 6.502 -1.584 42.134 1.00 151.87 ? 109 ASP B OD2 1 ATOM 8023 N N . TYR B 2 110 ? 3.891 3.013 40.078 1.00 102.18 ? 110 TYR B N 1 ATOM 8024 C CA . TYR B 2 110 ? 3.976 3.595 38.744 1.00 109.24 ? 110 TYR B CA 1 ATOM 8025 C C . TYR B 2 110 ? 5.284 4.363 38.596 1.00 112.86 ? 110 TYR B C 1 ATOM 8026 O O . TYR B 2 110 ? 5.604 5.209 39.432 1.00 106.20 ? 110 TYR B O 1 ATOM 8027 C CB . TYR B 2 110 ? 2.779 4.512 38.482 1.00 95.20 ? 110 TYR B CB 1 ATOM 8028 C CG . TYR B 2 110 ? 2.506 4.782 37.018 1.00 90.51 ? 110 TYR B CG 1 ATOM 8029 C CD1 . TYR B 2 110 ? 2.161 3.751 36.155 1.00 91.31 ? 110 TYR B CD1 1 ATOM 8030 C CD2 . TYR B 2 110 ? 2.573 6.071 36.504 1.00 114.37 ? 110 TYR B CD2 1 ATOM 8031 C CE1 . TYR B 2 110 ? 1.903 3.991 34.820 1.00 88.88 ? 110 TYR B CE1 1 ATOM 8032 C CE2 . TYR B 2 110 ? 2.316 6.320 35.168 1.00 117.33 ? 110 TYR B CE2 1 ATOM 8033 C CZ . TYR B 2 110 ? 1.981 5.275 34.332 1.00 112.34 ? 110 TYR B CZ 1 ATOM 8034 O OH . TYR B 2 110 ? 1.722 5.511 33.001 1.00 125.99 ? 110 TYR B OH 1 ATOM 8035 N N . PRO B 2 111 ? 6.046 4.069 37.530 1.00 110.32 ? 111 PRO B N 1 ATOM 8036 C CA . PRO B 2 111 ? 7.356 4.686 37.287 1.00 109.59 ? 111 PRO B CA 1 ATOM 8037 C C . PRO B 2 111 ? 7.280 6.210 37.226 1.00 102.73 ? 111 PRO B C 1 ATOM 8038 O O . PRO B 2 111 ? 6.343 6.762 36.648 1.00 95.82 ? 111 PRO B O 1 ATOM 8039 C CB . PRO B 2 111 ? 7.777 4.101 35.933 1.00 100.13 ? 111 PRO B CB 1 ATOM 8040 C CG . PRO B 2 111 ? 6.511 3.625 35.303 1.00 98.07 ? 111 PRO B CG 1 ATOM 8041 C CD . PRO B 2 111 ? 5.656 3.163 36.437 1.00 104.82 ? 111 PRO B CD 1 ATOM 8042 N N . VAL B 2 112 ? 8.260 6.877 37.826 1.00 106.77 ? 112 VAL B N 1 ATOM 8043 C CA . VAL B 2 112 ? 8.245 8.331 37.935 1.00 93.15 ? 112 VAL B CA 1 ATOM 8044 C C . VAL B 2 112 ? 9.470 8.969 37.284 1.00 93.80 ? 112 VAL B C 1 ATOM 8045 O O . VAL B 2 112 ? 10.601 8.530 37.500 1.00 99.21 ? 112 VAL B O 1 ATOM 8046 C CB . VAL B 2 112 ? 8.175 8.776 39.413 1.00 94.51 ? 112 VAL B CB 1 ATOM 8047 C CG1 . VAL B 2 112 ? 8.247 10.291 39.525 1.00 126.41 ? 112 VAL B CG1 1 ATOM 8048 C CG2 . VAL B 2 112 ? 6.906 8.251 40.068 1.00 94.63 ? 112 VAL B CG2 1 ATOM 8049 N N . ASP B 2 113 ? 9.238 9.999 36.476 1.00 92.04 ? 113 ASP B N 1 ATOM 8050 C CA . ASP B 2 113 ? 10.321 10.803 35.924 1.00 90.07 ? 113 ASP B CA 1 ATOM 8051 C C . ASP B 2 113 ? 10.351 12.169 36.601 1.00 100.96 ? 113 ASP B C 1 ATOM 8052 O O . ASP B 2 113 ? 9.318 12.823 36.736 1.00 112.17 ? 113 ASP B O 1 ATOM 8053 C CB . ASP B 2 113 ? 10.168 10.967 34.410 1.00 86.19 ? 113 ASP B CB 1 ATOM 8054 C CG . ASP B 2 113 ? 10.371 9.669 33.656 1.00 95.20 ? 113 ASP B CG 1 ATOM 8055 O OD1 . ASP B 2 113 ? 9.860 9.555 32.522 1.00 87.48 ? 113 ASP B OD1 1 ATOM 8056 O OD2 . ASP B 2 113 ? 11.040 8.762 34.195 1.00 123.98 ? 113 ASP B OD2 1 ATOM 8057 N N . ILE B 2 114 ? 11.534 12.592 37.034 1.00 105.82 ? 114 ILE B N 1 ATOM 8058 C CA . ILE B 2 114 ? 11.684 13.890 37.683 1.00 95.66 ? 114 ILE B CA 1 ATOM 8059 C C . ILE B 2 114 ? 12.808 14.701 37.049 1.00 91.23 ? 114 ILE B C 1 ATOM 8060 O O . ILE B 2 114 ? 13.967 14.291 37.067 1.00 97.08 ? 114 ILE B O 1 ATOM 8061 C CB . ILE B 2 114 ? 11.958 13.747 39.193 1.00 96.16 ? 114 ILE B CB 1 ATOM 8062 C CG1 . ILE B 2 114 ? 10.768 13.088 39.894 1.00 106.14 ? 114 ILE B CG1 1 ATOM 8063 C CG2 . ILE B 2 114 ? 12.247 15.105 39.811 1.00 89.04 ? 114 ILE B CG2 1 ATOM 8064 C CD1 . ILE B 2 114 ? 10.921 12.979 41.396 1.00 99.72 ? 114 ILE B CD1 1 ATOM 8065 N N . TYR B 2 115 ? 12.457 15.852 36.486 1.00 84.63 ? 115 TYR B N 1 ATOM 8066 C CA . TYR B 2 115 ? 13.448 16.745 35.901 1.00 84.42 ? 115 TYR B CA 1 ATOM 8067 C C . TYR B 2 115 ? 13.493 18.056 36.679 1.00 91.77 ? 115 TYR B C 1 ATOM 8068 O O . TYR B 2 115 ? 12.484 18.749 36.804 1.00 102.98 ? 115 TYR B O 1 ATOM 8069 C CB . TYR B 2 115 ? 13.142 17.004 34.425 1.00 83.59 ? 115 TYR B CB 1 ATOM 8070 C CG . TYR B 2 115 ? 14.257 17.704 33.681 1.00 87.28 ? 115 TYR B CG 1 ATOM 8071 C CD1 . TYR B 2 115 ? 15.371 17.002 33.239 1.00 112.63 ? 115 TYR B CD1 1 ATOM 8072 C CD2 . TYR B 2 115 ? 14.196 19.065 33.418 1.00 84.34 ? 115 TYR B CD2 1 ATOM 8073 C CE1 . TYR B 2 115 ? 16.391 17.635 32.556 1.00 111.93 ? 115 TYR B CE1 1 ATOM 8074 C CE2 . TYR B 2 115 ? 15.212 19.710 32.736 1.00 85.02 ? 115 TYR B CE2 1 ATOM 8075 C CZ . TYR B 2 115 ? 16.307 18.989 32.308 1.00 103.38 ? 115 TYR B CZ 1 ATOM 8076 O OH . TYR B 2 115 ? 17.321 19.623 31.629 1.00 104.37 ? 115 TYR B OH 1 ATOM 8077 N N . TYR B 2 116 ? 14.668 18.387 37.204 1.00 87.75 ? 116 TYR B N 1 ATOM 8078 C CA . TYR B 2 116 ? 14.831 19.576 38.034 1.00 88.99 ? 116 TYR B CA 1 ATOM 8079 C C . TYR B 2 116 ? 15.221 20.792 37.201 1.00 100.58 ? 116 TYR B C 1 ATOM 8080 O O . TYR B 2 116 ? 16.154 20.734 36.402 1.00 117.07 ? 116 TYR B O 1 ATOM 8081 C CB . TYR B 2 116 ? 15.885 19.329 39.116 1.00 98.79 ? 116 TYR B CB 1 ATOM 8082 C CG . TYR B 2 116 ? 15.417 19.617 40.525 1.00 108.04 ? 116 TYR B CG 1 ATOM 8083 C CD1 . TYR B 2 116 ? 15.084 18.584 41.391 1.00 110.50 ? 116 TYR B CD1 1 ATOM 8084 C CD2 . TYR B 2 116 ? 15.316 20.921 40.992 1.00 109.89 ? 116 TYR B CD2 1 ATOM 8085 C CE1 . TYR B 2 116 ? 14.657 18.841 42.680 1.00 111.64 ? 116 TYR B CE1 1 ATOM 8086 C CE2 . TYR B 2 116 ? 14.892 21.188 42.280 1.00 115.27 ? 116 TYR B CE2 1 ATOM 8087 C CZ . TYR B 2 116 ? 14.564 20.144 43.120 1.00 116.53 ? 116 TYR B CZ 1 ATOM 8088 O OH . TYR B 2 116 ? 14.141 20.403 44.404 1.00 106.69 ? 116 TYR B OH 1 ATOM 8089 N N . LEU B 2 117 ? 14.500 21.892 37.386 1.00 104.07 ? 117 LEU B N 1 ATOM 8090 C CA . LEU B 2 117 ? 14.870 23.154 36.758 1.00 87.43 ? 117 LEU B CA 1 ATOM 8091 C C . LEU B 2 117 ? 15.397 24.119 37.808 1.00 89.09 ? 117 LEU B C 1 ATOM 8092 O O . LEU B 2 117 ? 14.648 24.602 38.658 1.00 87.34 ? 117 LEU B O 1 ATOM 8093 C CB . LEU B 2 117 ? 13.684 23.765 36.014 1.00 84.39 ? 117 LEU B CB 1 ATOM 8094 C CG . LEU B 2 117 ? 13.394 23.175 34.633 1.00 97.72 ? 117 LEU B CG 1 ATOM 8095 C CD1 . LEU B 2 117 ? 12.271 23.939 33.953 1.00 89.29 ? 117 LEU B CD1 1 ATOM 8096 C CD2 . LEU B 2 117 ? 14.649 23.181 33.771 1.00 101.20 ? 117 LEU B CD2 1 ATOM 8097 N N . MET B 2 118 ? 16.694 24.396 37.739 1.00 99.24 ? 118 MET B N 1 ATOM 8098 C CA . MET B 2 118 ? 17.366 25.183 38.763 1.00 95.57 ? 118 MET B CA 1 ATOM 8099 C C . MET B 2 118 ? 17.616 26.618 38.313 1.00 90.82 ? 118 MET B C 1 ATOM 8100 O O . MET B 2 118 ? 17.992 26.866 37.167 1.00 90.07 ? 118 MET B O 1 ATOM 8101 C CB . MET B 2 118 ? 18.690 24.517 39.146 1.00 90.49 ? 118 MET B CB 1 ATOM 8102 C CG . MET B 2 118 ? 18.552 23.052 39.532 1.00 106.17 ? 118 MET B CG 1 ATOM 8103 S SD . MET B 2 118 ? 20.138 22.212 39.709 1.00 138.39 ? 118 MET B SD 1 ATOM 8104 C CE . MET B 2 118 ? 19.599 20.552 40.115 1.00 135.26 ? 118 MET B CE 1 ATOM 8105 N N . ASP B 2 119 ? 17.405 27.560 39.225 1.00 89.33 ? 119 ASP B N 1 ATOM 8106 C CA . ASP B 2 119 ? 17.709 28.958 38.960 1.00 89.56 ? 119 ASP B CA 1 ATOM 8107 C C . ASP B 2 119 ? 19.120 29.250 39.448 1.00 91.76 ? 119 ASP B C 1 ATOM 8108 O O . ASP B 2 119 ? 19.389 29.220 40.646 1.00 92.11 ? 119 ASP B O 1 ATOM 8109 C CB . ASP B 2 119 ? 16.692 29.873 39.647 1.00 93.20 ? 119 ASP B CB 1 ATOM 8110 C CG . ASP B 2 119 ? 16.926 31.340 39.344 1.00 104.62 ? 119 ASP B CG 1 ATOM 8111 O OD1 . ASP B 2 119 ? 16.464 32.190 40.134 1.00 97.98 ? 119 ASP B OD1 1 ATOM 8112 O OD2 . ASP B 2 119 ? 17.570 31.645 38.319 1.00 129.00 ? 119 ASP B OD2 1 ATOM 8113 N N . LEU B 2 120 ? 20.027 29.506 38.512 1.00 98.73 ? 120 LEU B N 1 ATOM 8114 C CA . LEU B 2 120 ? 21.431 29.717 38.850 1.00 109.15 ? 120 LEU B CA 1 ATOM 8115 C C . LEU B 2 120 ? 21.806 31.193 38.969 1.00 96.84 ? 120 LEU B C 1 ATOM 8116 O O . LEU B 2 120 ? 22.979 31.525 39.131 1.00 100.25 ? 120 LEU B O 1 ATOM 8117 C CB . LEU B 2 120 ? 22.333 29.023 37.829 1.00 114.20 ? 120 LEU B CB 1 ATOM 8118 C CG . LEU B 2 120 ? 22.286 27.492 37.888 1.00 96.49 ? 120 LEU B CG 1 ATOM 8119 C CD1 . LEU B 2 120 ? 23.500 26.888 37.197 1.00 112.98 ? 120 LEU B CD1 1 ATOM 8120 C CD2 . LEU B 2 120 ? 22.178 27.000 39.326 1.00 94.65 ? 120 LEU B CD2 1 ATOM 8121 N N . SER B 2 121 ? 20.814 32.073 38.873 1.00 94.86 ? 121 SER B N 1 ATOM 8122 C CA . SER B 2 121 ? 21.045 33.507 39.027 1.00 95.80 ? 121 SER B CA 1 ATOM 8123 C C . SER B 2 121 ? 21.546 33.822 40.435 1.00 97.15 ? 121 SER B C 1 ATOM 8124 O O . SER B 2 121 ? 21.325 33.045 41.365 1.00 100.86 ? 121 SER B O 1 ATOM 8125 C CB . SER B 2 121 ? 19.770 34.293 38.726 1.00 93.35 ? 121 SER B CB 1 ATOM 8126 O OG . SER B 2 121 ? 18.710 33.889 39.574 1.00 91.31 ? 121 SER B OG 1 ATOM 8127 N N . TYR B 2 122 ? 22.220 34.961 40.582 1.00 98.73 ? 122 TYR B N 1 ATOM 8128 C CA . TYR B 2 122 ? 22.934 35.303 41.813 1.00 100.45 ? 122 TYR B CA 1 ATOM 8129 C C . TYR B 2 122 ? 22.047 35.344 43.053 1.00 98.72 ? 122 TYR B C 1 ATOM 8130 O O . TYR B 2 122 ? 22.523 35.134 44.169 1.00 112.61 ? 122 TYR B O 1 ATOM 8131 C CB . TYR B 2 122 ? 23.643 36.650 41.655 1.00 113.94 ? 122 TYR B CB 1 ATOM 8132 C CG . TYR B 2 122 ? 24.722 36.884 42.688 1.00 125.90 ? 122 TYR B CG 1 ATOM 8133 C CD1 . TYR B 2 122 ? 26.006 36.391 42.499 1.00 120.12 ? 122 TYR B CD1 1 ATOM 8134 C CD2 . TYR B 2 122 ? 24.457 37.592 43.854 1.00 123.81 ? 122 TYR B CD2 1 ATOM 8135 C CE1 . TYR B 2 122 ? 26.996 36.597 43.440 1.00 110.24 ? 122 TYR B CE1 1 ATOM 8136 C CE2 . TYR B 2 122 ? 25.443 37.802 44.802 1.00 124.64 ? 122 TYR B CE2 1 ATOM 8137 C CZ . TYR B 2 122 ? 26.711 37.303 44.588 1.00 118.99 ? 122 TYR B CZ 1 ATOM 8138 O OH . TYR B 2 122 ? 27.697 37.509 45.526 1.00 139.64 ? 122 TYR B OH 1 ATOM 8139 N N . SER B 2 123 ? 20.761 35.613 42.855 1.00 94.92 ? 123 SER B N 1 ATOM 8140 C CA . SER B 2 123 ? 19.810 35.646 43.959 1.00 94.90 ? 123 SER B CA 1 ATOM 8141 C C . SER B 2 123 ? 19.690 34.281 44.633 1.00 102.55 ? 123 SER B C 1 ATOM 8142 O O . SER B 2 123 ? 19.275 34.180 45.787 1.00 88.97 ? 123 SER B O 1 ATOM 8143 C CB . SER B 2 123 ? 18.438 36.106 43.464 1.00 92.66 ? 123 SER B CB 1 ATOM 8144 O OG . SER B 2 123 ? 17.951 35.241 42.454 1.00 90.37 ? 123 SER B OG 1 ATOM 8145 N N . MET B 2 124 ? 20.057 33.235 43.899 1.00 107.86 ? 124 MET B N 1 ATOM 8146 C CA . MET B 2 124 ? 19.935 31.864 44.381 1.00 109.51 ? 124 MET B CA 1 ATOM 8147 C C . MET B 2 124 ? 21.221 31.341 45.013 1.00 121.70 ? 124 MET B C 1 ATOM 8148 O O . MET B 2 124 ? 21.290 30.177 45.407 1.00 131.85 ? 124 MET B O 1 ATOM 8149 C CB . MET B 2 124 ? 19.512 30.944 43.238 1.00 100.73 ? 124 MET B CB 1 ATOM 8150 C CG . MET B 2 124 ? 18.076 31.136 42.781 1.00 95.46 ? 124 MET B CG 1 ATOM 8151 S SD . MET B 2 124 ? 16.900 30.180 43.756 1.00 115.82 ? 124 MET B SD 1 ATOM 8152 C CE . MET B 2 124 ? 17.424 28.510 43.376 1.00 110.61 ? 124 MET B CE 1 ATOM 8153 N N . LYS B 2 125 ? 22.236 32.196 45.097 1.00 118.72 ? 125 LYS B N 1 ATOM 8154 C CA . LYS B 2 125 ? 23.502 31.829 45.727 1.00 113.14 ? 125 LYS B CA 1 ATOM 8155 C C . LYS B 2 125 ? 23.280 31.406 47.176 1.00 114.26 ? 125 LYS B C 1 ATOM 8156 O O . LYS B 2 125 ? 23.968 30.527 47.697 1.00 109.33 ? 125 LYS B O 1 ATOM 8157 C CB . LYS B 2 125 ? 24.487 32.996 45.660 1.00 106.15 ? 125 LYS B CB 1 ATOM 8158 C CG . LYS B 2 125 ? 25.881 32.675 46.178 1.00 129.92 ? 125 LYS B CG 1 ATOM 8159 C CD . LYS B 2 125 ? 26.767 33.911 46.154 1.00 137.91 ? 125 LYS B CD 1 ATOM 8160 C CE . LYS B 2 125 ? 28.178 33.591 46.617 1.00 131.05 ? 125 LYS B CE 1 ATOM 8161 N NZ . LYS B 2 125 ? 28.875 32.674 45.674 1.00 133.02 ? 125 LYS B NZ 1 ATOM 8162 N N . ASP B 2 126 ? 22.303 32.042 47.812 1.00 125.40 ? 126 ASP B N 1 ATOM 8163 C CA . ASP B 2 126 ? 21.934 31.743 49.188 1.00 112.31 ? 126 ASP B CA 1 ATOM 8164 C C . ASP B 2 126 ? 21.122 30.454 49.295 1.00 113.20 ? 126 ASP B C 1 ATOM 8165 O O . ASP B 2 126 ? 21.144 29.780 50.323 1.00 125.53 ? 126 ASP B O 1 ATOM 8166 C CB . ASP B 2 126 ? 21.136 32.908 49.778 1.00 111.12 ? 126 ASP B CB 1 ATOM 8167 C CG . ASP B 2 126 ? 19.951 33.299 48.910 1.00 153.97 ? 126 ASP B CG 1 ATOM 8168 O OD1 . ASP B 2 126 ? 20.017 33.097 47.678 1.00 162.11 ? 126 ASP B OD1 1 ATOM 8169 O OD2 . ASP B 2 126 ? 18.951 33.809 49.455 1.00 163.41 ? 126 ASP B OD2 1 ATOM 8170 N N . ASP B 2 127 ? 20.406 30.121 48.225 1.00 101.93 ? 127 ASP B N 1 ATOM 8171 C CA . ASP B 2 127 ? 19.458 29.009 48.243 1.00 111.83 ? 127 ASP B CA 1 ATOM 8172 C C . ASP B 2 127 ? 20.035 27.694 47.718 1.00 115.14 ? 127 ASP B C 1 ATOM 8173 O O . ASP B 2 127 ? 19.316 26.703 47.598 1.00 112.63 ? 127 ASP B O 1 ATOM 8174 C CB . ASP B 2 127 ? 18.212 29.380 47.437 1.00 119.15 ? 127 ASP B CB 1 ATOM 8175 C CG . ASP B 2 127 ? 17.617 30.706 47.867 1.00 122.89 ? 127 ASP B CG 1 ATOM 8176 O OD1 . ASP B 2 127 ? 17.918 31.733 47.222 1.00 115.27 ? 127 ASP B OD1 1 ATOM 8177 O OD2 . ASP B 2 127 ? 16.852 30.725 48.855 1.00 138.85 ? 127 ASP B OD2 1 ATOM 8178 N N . LEU B 2 128 ? 21.326 27.687 47.402 1.00 122.38 ? 128 LEU B N 1 ATOM 8179 C CA . LEU B 2 128 ? 21.976 26.505 46.835 1.00 123.80 ? 128 LEU B CA 1 ATOM 8180 C C . LEU B 2 128 ? 22.157 25.376 47.851 1.00 126.19 ? 128 LEU B C 1 ATOM 8181 O O . LEU B 2 128 ? 22.583 24.275 47.499 1.00 114.53 ? 128 LEU B O 1 ATOM 8182 C CB . LEU B 2 128 ? 23.333 26.887 46.241 1.00 134.00 ? 128 LEU B CB 1 ATOM 8183 C CG . LEU B 2 128 ? 23.483 26.725 44.728 1.00 122.19 ? 128 LEU B CG 1 ATOM 8184 C CD1 . LEU B 2 128 ? 22.345 27.420 43.999 1.00 98.37 ? 128 LEU B CD1 1 ATOM 8185 C CD2 . LEU B 2 128 ? 24.827 27.265 44.267 1.00 129.22 ? 128 LEU B CD2 1 ATOM 8186 N N . TRP B 2 129 ? 21.838 25.659 49.110 1.00 135.77 ? 129 TRP B N 1 ATOM 8187 C CA . TRP B 2 129 ? 21.962 24.683 50.188 1.00 133.47 ? 129 TRP B CA 1 ATOM 8188 C C . TRP B 2 129 ? 21.071 23.460 49.972 1.00 120.34 ? 129 TRP B C 1 ATOM 8189 O O . TRP B 2 129 ? 21.445 22.340 50.321 1.00 126.24 ? 129 TRP B O 1 ATOM 8190 C CB . TRP B 2 129 ? 21.620 25.338 51.529 1.00 130.72 ? 129 TRP B CB 1 ATOM 8191 C CG . TRP B 2 129 ? 20.245 25.930 51.549 1.00 142.89 ? 129 TRP B CG 1 ATOM 8192 C CD1 . TRP B 2 129 ? 19.889 27.185 51.161 1.00 161.73 ? 129 TRP B CD1 1 ATOM 8193 C CD2 . TRP B 2 129 ? 19.040 25.280 51.965 1.00 151.66 ? 129 TRP B CD2 1 ATOM 8194 N NE1 . TRP B 2 129 ? 18.535 27.364 51.314 1.00 157.78 ? 129 TRP B NE1 1 ATOM 8195 C CE2 . TRP B 2 129 ? 17.991 26.208 51.806 1.00 155.15 ? 129 TRP B CE2 1 ATOM 8196 C CE3 . TRP B 2 129 ? 18.745 24.007 52.458 1.00 165.72 ? 129 TRP B CE3 1 ATOM 8197 C CZ2 . TRP B 2 129 ? 16.671 25.902 52.123 1.00 154.66 ? 129 TRP B CZ2 1 ATOM 8198 C CZ3 . TRP B 2 129 ? 17.436 23.707 52.772 1.00 160.22 ? 129 TRP B CZ3 1 ATOM 8199 C CH2 . TRP B 2 129 ? 16.415 24.648 52.603 1.00 153.16 ? 129 TRP B CH2 1 ATOM 8200 N N . SER B 2 130 ? 19.896 23.680 49.393 1.00 114.98 ? 130 SER B N 1 ATOM 8201 C CA . SER B 2 130 ? 18.909 22.617 49.231 1.00 144.54 ? 130 SER B CA 1 ATOM 8202 C C . SER B 2 130 ? 19.175 21.756 48.000 1.00 142.98 ? 130 SER B C 1 ATOM 8203 O O . SER B 2 130 ? 18.596 20.680 47.849 1.00 112.39 ? 130 SER B O 1 ATOM 8204 C CB . SER B 2 130 ? 17.501 23.212 49.156 1.00 133.84 ? 130 SER B CB 1 ATOM 8205 O OG . SER B 2 130 ? 17.398 24.149 48.097 1.00 111.21 ? 130 SER B OG 1 ATOM 8206 N N . ILE B 2 131 ? 20.051 22.231 47.121 1.00 150.75 ? 131 ILE B N 1 ATOM 8207 C CA . ILE B 2 131 ? 20.354 21.505 45.894 1.00 137.93 ? 131 ILE B CA 1 ATOM 8208 C C . ILE B 2 131 ? 21.447 20.459 46.127 1.00 142.56 ? 131 ILE B C 1 ATOM 8209 O O . ILE B 2 131 ? 21.637 19.554 45.313 1.00 139.44 ? 131 ILE B O 1 ATOM 8210 C CB . ILE B 2 131 ? 20.770 22.469 44.761 1.00 144.09 ? 131 ILE B CB 1 ATOM 8211 C CG1 . ILE B 2 131 ? 20.222 21.976 43.422 1.00 133.21 ? 131 ILE B CG1 1 ATOM 8212 C CG2 . ILE B 2 131 ? 22.282 22.663 44.727 1.00 158.37 ? 131 ILE B CG2 1 ATOM 8213 C CD1 . ILE B 2 131 ? 18.720 21.778 43.420 1.00 137.18 ? 131 ILE B CD1 1 ATOM 8214 N N . GLN B 2 132 ? 22.147 20.577 47.252 1.00 136.69 ? 132 GLN B N 1 ATOM 8215 C CA . GLN B 2 132 ? 23.122 19.573 47.670 1.00 127.46 ? 132 GLN B CA 1 ATOM 8216 C C . GLN B 2 132 ? 22.370 18.297 48.017 1.00 128.21 ? 132 GLN B C 1 ATOM 8217 O O . GLN B 2 132 ? 21.157 18.350 48.230 1.00 125.27 ? 132 GLN B O 1 ATOM 8218 C CB . GLN B 2 132 ? 23.941 20.068 48.862 1.00 133.00 ? 132 GLN B CB 1 ATOM 8219 C CG . GLN B 2 132 ? 24.504 21.469 48.685 1.00 143.86 ? 132 GLN B CG 1 ATOM 8220 C CD . GLN B 2 132 ? 25.429 21.583 47.489 1.00 153.36 ? 132 GLN B CD 1 ATOM 8221 O OE1 . GLN B 2 132 ? 25.145 22.310 46.537 1.00 151.91 ? 132 GLN B OE1 1 ATOM 8222 N NE2 . GLN B 2 132 ? 26.548 20.869 47.536 1.00 156.25 ? 132 GLN B NE2 1 ATOM 8223 N N . ASN B 2 133 ? 23.070 17.162 48.078 1.00 133.20 ? 133 ASN B N 1 ATOM 8224 C CA . ASN B 2 133 ? 22.388 15.877 48.236 1.00 151.52 ? 133 ASN B CA 1 ATOM 8225 C C . ASN B 2 133 ? 21.420 15.694 47.073 1.00 157.99 ? 133 ASN B C 1 ATOM 8226 O O . ASN B 2 133 ? 21.857 15.387 45.962 1.00 173.32 ? 133 ASN B O 1 ATOM 8227 C CB . ASN B 2 133 ? 21.686 15.767 49.592 1.00 156.00 ? 133 ASN B CB 1 ATOM 8228 C CG . ASN B 2 133 ? 22.668 15.734 50.750 1.00 163.88 ? 133 ASN B CG 1 ATOM 8229 O OD1 . ASN B 2 133 ? 23.673 16.446 50.746 1.00 145.86 ? 133 ASN B OD1 1 ATOM 8230 N ND2 . ASN B 2 133 ? 22.391 14.895 51.739 1.00 166.50 ? 133 ASN B ND2 1 ATOM 8231 N N . LEU B 2 134 ? 20.121 15.845 47.329 1.00 148.76 ? 134 LEU B N 1 ATOM 8232 C CA . LEU B 2 134 ? 19.098 15.644 46.299 1.00 143.73 ? 134 LEU B CA 1 ATOM 8233 C C . LEU B 2 134 ? 19.077 14.188 45.848 1.00 141.65 ? 134 LEU B C 1 ATOM 8234 O O . LEU B 2 134 ? 18.609 13.346 46.595 1.00 149.26 ? 134 LEU B O 1 ATOM 8235 C CB . LEU B 2 134 ? 19.310 16.589 45.109 1.00 114.88 ? 134 LEU B CB 1 ATOM 8236 C CG . LEU B 2 134 ? 18.066 16.916 44.281 1.00 117.25 ? 134 LEU B CG 1 ATOM 8237 C CD1 . LEU B 2 134 ? 16.923 17.347 45.187 1.00 112.03 ? 134 LEU B CD1 1 ATOM 8238 C CD2 . LEU B 2 134 ? 18.372 18.000 43.260 1.00 112.96 ? 134 LEU B CD2 1 ATOM 8239 N N . GLY B 2 135 ? 19.535 13.887 44.636 1.00 133.58 ? 135 GLY B N 1 ATOM 8240 C CA . GLY B 2 135 ? 19.312 12.577 44.036 1.00 121.89 ? 135 GLY B CA 1 ATOM 8241 C C . GLY B 2 135 ? 19.525 11.363 44.932 1.00 145.63 ? 135 GLY B C 1 ATOM 8242 O O . GLY B 2 135 ? 18.883 10.331 44.734 1.00 155.04 ? 135 GLY B O 1 ATOM 8243 N N . THR B 2 136 ? 20.418 11.474 45.912 1.00 145.70 ? 136 THR B N 1 ATOM 8244 C CA . THR B 2 136 ? 20.486 10.482 46.983 1.00 153.56 ? 136 THR B CA 1 ATOM 8245 C C . THR B 2 136 ? 19.257 10.592 47.886 1.00 153.00 ? 136 THR B C 1 ATOM 8246 O O . THR B 2 136 ? 18.574 9.602 48.152 1.00 139.36 ? 136 THR B O 1 ATOM 8247 C CB . THR B 2 136 ? 21.757 10.641 47.839 1.00 161.26 ? 136 THR B CB 1 ATOM 8248 O OG1 . THR B 2 136 ? 22.912 10.345 47.045 1.00 156.51 ? 136 THR B OG1 1 ATOM 8249 C CG2 . THR B 2 136 ? 21.714 9.697 49.034 1.00 151.76 ? 136 THR B CG2 1 ATOM 8250 N N . LYS B 2 137 ? 18.988 11.808 48.356 1.00 169.04 ? 137 LYS B N 1 ATOM 8251 C CA . LYS B 2 137 ? 17.801 12.098 49.157 1.00 174.52 ? 137 LYS B CA 1 ATOM 8252 C C . LYS B 2 137 ? 16.523 11.879 48.348 1.00 161.95 ? 137 LYS B C 1 ATOM 8253 O O . LYS B 2 137 ? 15.502 11.470 48.892 1.00 153.24 ? 137 LYS B O 1 ATOM 8254 C CB . LYS B 2 137 ? 17.840 13.538 49.668 1.00 179.98 ? 137 LYS B CB 1 ATOM 8255 C CG . LYS B 2 137 ? 18.701 13.775 50.893 1.00 188.89 ? 137 LYS B CG 1 ATOM 8256 C CD . LYS B 2 137 ? 18.577 15.224 51.345 1.00 188.68 ? 137 LYS B CD 1 ATOM 8257 C CE . LYS B 2 137 ? 19.339 15.483 52.632 1.00 189.36 ? 137 LYS B CE 1 ATOM 8258 N NZ . LYS B 2 137 ? 19.314 16.926 52.997 1.00 185.87 ? 137 LYS B NZ 1 ATOM 8259 N N . LEU B 2 138 ? 16.583 12.167 47.049 1.00 123.73 ? 138 LEU B N 1 ATOM 8260 C CA . LEU B 2 138 ? 15.437 11.962 46.164 1.00 118.70 ? 138 LEU B CA 1 ATOM 8261 C C . LEU B 2 138 ? 15.022 10.498 46.141 1.00 148.65 ? 138 LEU B C 1 ATOM 8262 O O . LEU B 2 138 ? 13.852 10.172 45.935 1.00 160.74 ? 138 LEU B O 1 ATOM 8263 C CB . LEU B 2 138 ? 15.751 12.432 44.743 1.00 114.44 ? 138 LEU B CB 1 ATOM 8264 C CG . LEU B 2 138 ? 15.625 13.925 44.440 1.00 132.35 ? 138 LEU B CG 1 ATOM 8265 C CD1 . LEU B 2 138 ? 15.926 14.195 42.973 1.00 107.82 ? 138 LEU B CD1 1 ATOM 8266 C CD2 . LEU B 2 138 ? 14.238 14.425 44.804 1.00 135.81 ? 138 LEU B CD2 1 ATOM 8267 N N . ALA B 2 139 ? 15.994 9.620 46.353 1.00 140.45 ? 139 ALA B N 1 ATOM 8268 C CA . ALA B 2 139 ? 15.732 8.193 46.423 1.00 129.93 ? 139 ALA B CA 1 ATOM 8269 C C . ALA B 2 139 ? 15.149 7.814 47.780 1.00 136.54 ? 139 ALA B C 1 ATOM 8270 O O . ALA B 2 139 ? 14.255 6.976 47.859 1.00 140.05 ? 139 ALA B O 1 ATOM 8271 C CB . ALA B 2 139 ? 17.004 7.404 46.151 1.00 160.01 ? 139 ALA B CB 1 ATOM 8272 N N . THR B 2 140 ? 15.645 8.441 48.844 1.00 144.00 ? 140 THR B N 1 ATOM 8273 C CA . THR B 2 140 ? 15.231 8.084 50.201 1.00 162.91 ? 140 THR B CA 1 ATOM 8274 C C . THR B 2 140 ? 13.779 8.478 50.479 1.00 157.37 ? 140 THR B C 1 ATOM 8275 O O . THR B 2 140 ? 13.186 8.036 51.465 1.00 155.11 ? 140 THR B O 1 ATOM 8276 C CB . THR B 2 140 ? 16.150 8.729 51.267 1.00 164.25 ? 140 THR B CB 1 ATOM 8277 O OG1 . THR B 2 140 ? 16.210 7.884 52.423 1.00 161.85 ? 140 THR B OG1 1 ATOM 8278 C CG2 . THR B 2 140 ? 15.644 10.108 51.677 1.00 149.40 ? 140 THR B CG2 1 ATOM 8279 N N . GLN B 2 141 ? 13.211 9.304 49.606 1.00 130.32 ? 141 GLN B N 1 ATOM 8280 C CA . GLN B 2 141 ? 11.802 9.667 49.705 1.00 141.68 ? 141 GLN B CA 1 ATOM 8281 C C . GLN B 2 141 ? 10.954 8.835 48.742 1.00 145.75 ? 141 GLN B C 1 ATOM 8282 O O . GLN B 2 141 ? 10.081 8.082 49.167 1.00 149.57 ? 141 GLN B O 1 ATOM 8283 C CB . GLN B 2 141 ? 11.598 11.167 49.447 1.00 140.04 ? 141 GLN B CB 1 ATOM 8284 C CG . GLN B 2 141 ? 12.421 11.744 48.307 1.00 154.34 ? 141 GLN B CG 1 ATOM 8285 C CD . GLN B 2 141 ? 12.040 13.172 47.962 1.00 148.92 ? 141 GLN B CD 1 ATOM 8286 O OE1 . GLN B 2 141 ? 12.890 14.062 47.930 1.00 147.55 ? 141 GLN B OE1 1 ATOM 8287 N NE2 . GLN B 2 141 ? 10.759 13.395 47.692 1.00 130.75 ? 141 GLN B NE2 1 ATOM 8288 N N . MET B 2 142 ? 11.217 8.972 47.447 1.00 126.28 ? 142 MET B N 1 ATOM 8289 C CA . MET B 2 142 ? 10.393 8.357 46.411 1.00 116.36 ? 142 MET B CA 1 ATOM 8290 C C . MET B 2 142 ? 10.444 6.827 46.390 1.00 133.08 ? 142 MET B C 1 ATOM 8291 O O . MET B 2 142 ? 9.656 6.194 45.687 1.00 118.17 ? 142 MET B O 1 ATOM 8292 C CB . MET B 2 142 ? 10.803 8.893 45.037 1.00 112.18 ? 142 MET B CB 1 ATOM 8293 C CG . MET B 2 142 ? 10.549 10.380 44.847 1.00 107.59 ? 142 MET B CG 1 ATOM 8294 S SD . MET B 2 142 ? 8.795 10.793 44.785 1.00 154.73 ? 142 MET B SD 1 ATOM 8295 C CE . MET B 2 142 ? 8.294 9.925 43.301 1.00 100.95 ? 142 MET B CE 1 ATOM 8296 N N . ARG B 2 143 ? 11.362 6.237 47.151 1.00 146.92 ? 143 ARG B N 1 ATOM 8297 C CA . ARG B 2 143 ? 11.498 4.781 47.196 1.00 130.47 ? 143 ARG B CA 1 ATOM 8298 C C . ARG B 2 143 ? 10.219 4.114 47.693 1.00 135.18 ? 143 ARG B C 1 ATOM 8299 O O . ARG B 2 143 ? 9.880 3.010 47.266 1.00 149.46 ? 143 ARG B O 1 ATOM 8300 C CB . ARG B 2 143 ? 12.675 4.373 48.086 1.00 137.25 ? 143 ARG B CB 1 ATOM 8301 C CG . ARG B 2 143 ? 12.922 2.872 48.158 1.00 153.02 ? 143 ARG B CG 1 ATOM 8302 C CD . ARG B 2 143 ? 14.197 2.543 48.924 1.00 160.99 ? 143 ARG B CD 1 ATOM 8303 N NE . ARG B 2 143 ? 15.399 2.950 48.198 1.00 164.94 ? 143 ARG B NE 1 ATOM 8304 C CZ . ARG B 2 143 ? 16.104 4.042 48.466 1.00 167.02 ? 143 ARG B CZ 1 ATOM 8305 N NH1 . ARG B 2 143 ? 15.736 4.847 49.453 1.00 168.55 ? 143 ARG B NH1 1 ATOM 8306 N NH2 . ARG B 2 143 ? 17.184 4.327 47.751 1.00 164.33 ? 143 ARG B NH2 1 ATOM 8307 N N . LYS B 2 144 ? 9.511 4.791 48.590 1.00 140.58 ? 144 LYS B N 1 ATOM 8308 C CA . LYS B 2 144 ? 8.286 4.244 49.159 1.00 152.50 ? 144 LYS B CA 1 ATOM 8309 C C . LYS B 2 144 ? 7.185 4.115 48.102 1.00 145.02 ? 144 LYS B C 1 ATOM 8310 O O . LYS B 2 144 ? 6.505 3.092 48.031 1.00 157.36 ? 144 LYS B O 1 ATOM 8311 C CB . LYS B 2 144 ? 7.807 5.110 50.334 1.00 160.54 ? 144 LYS B CB 1 ATOM 8312 C CG . LYS B 2 144 ? 7.497 6.559 49.976 1.00 160.47 ? 144 LYS B CG 1 ATOM 8313 C CD . LYS B 2 144 ? 7.145 7.401 51.191 1.00 168.40 ? 144 LYS B CD 1 ATOM 8314 C CE . LYS B 2 144 ? 8.390 7.844 51.942 1.00 174.95 ? 144 LYS B CE 1 ATOM 8315 N NZ . LYS B 2 144 ? 8.073 8.867 52.975 1.00 174.09 ? 144 LYS B NZ 1 ATOM 8316 N N . LEU B 2 145 ? 7.014 5.151 47.286 1.00 125.85 ? 145 LEU B N 1 ATOM 8317 C CA . LEU B 2 145 ? 5.941 5.180 46.299 1.00 125.52 ? 145 LEU B CA 1 ATOM 8318 C C . LEU B 2 145 ? 6.298 4.553 44.952 1.00 122.80 ? 145 LEU B C 1 ATOM 8319 O O . LEU B 2 145 ? 5.408 4.223 44.168 1.00 120.52 ? 145 LEU B O 1 ATOM 8320 C CB . LEU B 2 145 ? 5.490 6.627 46.071 1.00 116.41 ? 145 LEU B CB 1 ATOM 8321 C CG . LEU B 2 145 ? 4.247 7.127 46.811 1.00 131.46 ? 145 LEU B CG 1 ATOM 8322 C CD1 . LEU B 2 145 ? 4.319 6.816 48.297 1.00 141.81 ? 145 LEU B CD1 1 ATOM 8323 C CD2 . LEU B 2 145 ? 4.066 8.622 46.587 1.00 104.65 ? 145 LEU B CD2 1 ATOM 8324 N N . THR B 2 146 ? 7.589 4.385 44.675 1.00 123.69 ? 146 THR B N 1 ATOM 8325 C CA . THR B 2 146 ? 8.006 4.009 43.325 1.00 116.41 ? 146 THR B CA 1 ATOM 8326 C C . THR B 2 146 ? 9.329 3.237 43.272 1.00 139.96 ? 146 THR B C 1 ATOM 8327 O O . THR B 2 146 ? 10.232 3.468 44.074 1.00 145.97 ? 146 THR B O 1 ATOM 8328 C CB . THR B 2 146 ? 8.128 5.276 42.432 1.00 129.63 ? 146 THR B CB 1 ATOM 8329 O OG1 . THR B 2 146 ? 6.904 6.019 42.483 1.00 169.23 ? 146 THR B OG1 1 ATOM 8330 C CG2 . THR B 2 146 ? 8.425 4.919 40.983 1.00 107.69 ? 146 THR B CG2 1 ATOM 8331 N N . SER B 2 147 ? 9.422 2.318 42.314 1.00 142.85 ? 147 SER B N 1 ATOM 8332 C CA . SER B 2 147 ? 10.685 1.708 41.918 1.00 134.43 ? 147 SER B CA 1 ATOM 8333 C C . SER B 2 147 ? 10.890 2.028 40.441 1.00 140.31 ? 147 SER B C 1 ATOM 8334 O O . SER B 2 147 ? 9.932 2.392 39.756 1.00 123.21 ? 147 SER B O 1 ATOM 8335 C CB . SER B 2 147 ? 10.684 0.199 42.165 1.00 128.93 ? 147 SER B CB 1 ATOM 8336 O OG . SER B 2 147 ? 9.722 -0.452 41.355 1.00 126.78 ? 147 SER B OG 1 ATOM 8337 N N . ASN B 2 148 ? 12.124 1.899 39.957 1.00 159.44 ? 148 ASN B N 1 ATOM 8338 C CA . ASN B 2 148 ? 12.491 2.351 38.613 1.00 163.48 ? 148 ASN B CA 1 ATOM 8339 C C . ASN B 2 148 ? 12.243 3.854 38.469 1.00 151.53 ? 148 ASN B C 1 ATOM 8340 O O . ASN B 2 148 ? 11.574 4.305 37.539 1.00 139.04 ? 148 ASN B O 1 ATOM 8341 C CB . ASN B 2 148 ? 11.721 1.569 37.538 1.00 159.22 ? 148 ASN B CB 1 ATOM 8342 C CG . ASN B 2 148 ? 12.308 1.740 36.145 1.00 154.09 ? 148 ASN B CG 1 ATOM 8343 O OD1 . ASN B 2 148 ? 13.113 2.638 35.896 1.00 133.44 ? 148 ASN B OD1 1 ATOM 8344 N ND2 . ASN B 2 148 ? 11.896 0.875 35.225 1.00 156.86 ? 148 ASN B ND2 1 ATOM 8345 N N . LEU B 2 149 ? 12.776 4.617 39.418 1.00 148.20 ? 149 LEU B N 1 ATOM 8346 C CA . LEU B 2 149 ? 12.729 6.075 39.370 1.00 123.95 ? 149 LEU B CA 1 ATOM 8347 C C . LEU B 2 149 ? 13.846 6.610 38.477 1.00 111.16 ? 149 LEU B C 1 ATOM 8348 O O . LEU B 2 149 ? 14.936 6.039 38.427 1.00 122.66 ? 149 LEU B O 1 ATOM 8349 C CB . LEU B 2 149 ? 12.843 6.660 40.782 1.00 112.78 ? 149 LEU B CB 1 ATOM 8350 C CG . LEU B 2 149 ? 12.971 8.177 40.938 1.00 109.35 ? 149 LEU B CG 1 ATOM 8351 C CD1 . LEU B 2 149 ? 11.700 8.877 40.494 1.00 127.25 ? 149 LEU B CD1 1 ATOM 8352 C CD2 . LEU B 2 149 ? 13.314 8.547 42.374 1.00 112.33 ? 149 LEU B CD2 1 ATOM 8353 N N . ARG B 2 150 ? 13.572 7.702 37.770 1.00 106.28 ? 150 ARG B N 1 ATOM 8354 C CA . ARG B 2 150 ? 14.556 8.313 36.880 1.00 105.74 ? 150 ARG B CA 1 ATOM 8355 C C . ARG B 2 150 ? 14.607 9.827 37.070 1.00 118.04 ? 150 ARG B C 1 ATOM 8356 O O . ARG B 2 150 ? 13.588 10.508 36.957 1.00 139.80 ? 150 ARG B O 1 ATOM 8357 C CB . ARG B 2 150 ? 14.238 7.976 35.422 1.00 106.84 ? 150 ARG B CB 1 ATOM 8358 C CG . ARG B 2 150 ? 14.393 6.503 35.078 1.00 123.48 ? 150 ARG B CG 1 ATOM 8359 C CD . ARG B 2 150 ? 15.681 6.245 34.316 1.00 144.74 ? 150 ARG B CD 1 ATOM 8360 N NE . ARG B 2 150 ? 15.625 6.770 32.954 1.00 156.25 ? 150 ARG B NE 1 ATOM 8361 C CZ . ARG B 2 150 ? 15.295 6.049 31.888 1.00 155.70 ? 150 ARG B CZ 1 ATOM 8362 N NH1 . ARG B 2 150 ? 14.996 4.764 32.022 1.00 145.79 ? 150 ARG B NH1 1 ATOM 8363 N NH2 . ARG B 2 150 ? 15.267 6.610 30.687 1.00 148.33 ? 150 ARG B NH2 1 ATOM 8364 N N . ILE B 2 151 ? 15.796 10.347 37.358 1.00 115.38 ? 151 ILE B N 1 ATOM 8365 C CA . ILE B 2 151 ? 15.962 11.777 37.601 1.00 119.74 ? 151 ILE B CA 1 ATOM 8366 C C . ILE B 2 151 ? 16.982 12.418 36.663 1.00 110.21 ? 151 ILE B C 1 ATOM 8367 O O . ILE B 2 151 ? 17.620 11.739 35.861 1.00 124.58 ? 151 ILE B O 1 ATOM 8368 C CB . ILE B 2 151 ? 16.397 12.048 39.051 1.00 104.28 ? 151 ILE B CB 1 ATOM 8369 C CG1 . ILE B 2 151 ? 17.740 11.374 39.332 1.00 110.16 ? 151 ILE B CG1 1 ATOM 8370 C CG2 . ILE B 2 151 ? 15.335 11.560 40.026 1.00 114.24 ? 151 ILE B CG2 1 ATOM 8371 C CD1 . ILE B 2 151 ? 18.244 11.580 40.739 1.00 113.80 ? 151 ILE B CD1 1 ATOM 8372 N N . GLY B 2 152 ? 17.139 13.732 36.793 1.00 99.60 ? 152 GLY B N 1 ATOM 8373 C CA . GLY B 2 152 ? 18.004 14.515 35.928 1.00 111.01 ? 152 GLY B CA 1 ATOM 8374 C C . GLY B 2 152 ? 17.644 15.980 36.088 1.00 94.29 ? 152 GLY B C 1 ATOM 8375 O O . GLY B 2 152 ? 16.664 16.299 36.760 1.00 92.04 ? 152 GLY B O 1 ATOM 8376 N N . PHE B 2 153 ? 18.418 16.876 35.483 1.00 100.66 ? 153 PHE B N 1 ATOM 8377 C CA . PHE B 2 153 ? 18.145 18.299 35.649 1.00 102.95 ? 153 PHE B CA 1 ATOM 8378 C C . PHE B 2 153 ? 18.709 19.188 34.545 1.00 99.84 ? 153 PHE B C 1 ATOM 8379 O O . PHE B 2 153 ? 19.376 18.723 33.620 1.00 100.96 ? 153 PHE B O 1 ATOM 8380 C CB . PHE B 2 153 ? 18.682 18.775 37.004 1.00 98.64 ? 153 PHE B CB 1 ATOM 8381 C CG . PHE B 2 153 ? 20.183 18.840 37.083 1.00 101.26 ? 153 PHE B CG 1 ATOM 8382 C CD1 . PHE B 2 153 ? 20.848 20.045 36.903 1.00 108.68 ? 153 PHE B CD1 1 ATOM 8383 C CD2 . PHE B 2 153 ? 20.929 17.706 37.352 1.00 108.43 ? 153 PHE B CD2 1 ATOM 8384 C CE1 . PHE B 2 153 ? 22.226 20.113 36.983 1.00 124.74 ? 153 PHE B CE1 1 ATOM 8385 C CE2 . PHE B 2 153 ? 22.309 17.767 37.430 1.00 119.16 ? 153 PHE B CE2 1 ATOM 8386 C CZ . PHE B 2 153 ? 22.957 18.973 37.246 1.00 133.42 ? 153 PHE B CZ 1 ATOM 8387 N N . GLY B 2 154 ? 18.421 20.480 34.669 1.00 94.29 ? 154 GLY B N 1 ATOM 8388 C CA . GLY B 2 154 ? 18.913 21.502 33.764 1.00 94.07 ? 154 GLY B CA 1 ATOM 8389 C C . GLY B 2 154 ? 18.885 22.830 34.498 1.00 97.10 ? 154 GLY B C 1 ATOM 8390 O O . GLY B 2 154 ? 18.342 22.914 35.599 1.00 90.20 ? 154 GLY B O 1 ATOM 8391 N N . ALA B 2 155 ? 19.462 23.869 33.904 1.00 93.50 ? 155 ALA B N 1 ATOM 8392 C CA . ALA B 2 155 ? 19.555 25.157 34.585 1.00 89.03 ? 155 ALA B CA 1 ATOM 8393 C C . ALA B 2 155 ? 19.158 26.328 33.690 1.00 89.06 ? 155 ALA B C 1 ATOM 8394 O O . ALA B 2 155 ? 19.298 26.268 32.469 1.00 86.47 ? 155 ALA B O 1 ATOM 8395 C CB . ALA B 2 155 ? 20.962 25.362 35.118 1.00 97.07 ? 155 ALA B CB 1 ATOM 8396 N N . PHE B 2 156 ? 18.664 27.393 34.315 1.00 94.73 ? 156 PHE B N 1 ATOM 8397 C CA . PHE B 2 156 ? 18.328 28.624 33.608 1.00 88.27 ? 156 PHE B CA 1 ATOM 8398 C C . PHE B 2 156 ? 18.815 29.833 34.397 1.00 90.31 ? 156 PHE B C 1 ATOM 8399 O O . PHE B 2 156 ? 18.967 29.765 35.617 1.00 90.40 ? 156 PHE B O 1 ATOM 8400 C CB . PHE B 2 156 ? 16.818 28.727 33.373 1.00 86.03 ? 156 PHE B CB 1 ATOM 8401 C CG . PHE B 2 156 ? 16.014 28.852 34.639 1.00 86.26 ? 156 PHE B CG 1 ATOM 8402 C CD1 . PHE B 2 156 ? 15.722 30.097 35.179 1.00 86.38 ? 156 PHE B CD1 1 ATOM 8403 C CD2 . PHE B 2 156 ? 15.547 27.721 35.288 1.00 87.15 ? 156 PHE B CD2 1 ATOM 8404 C CE1 . PHE B 2 156 ? 14.988 30.208 36.344 1.00 84.22 ? 156 PHE B CE1 1 ATOM 8405 C CE2 . PHE B 2 156 ? 14.810 27.826 36.451 1.00 92.32 ? 156 PHE B CE2 1 ATOM 8406 C CZ . PHE B 2 156 ? 14.528 29.071 36.980 1.00 83.55 ? 156 PHE B CZ 1 ATOM 8407 N N . VAL B 2 157 ? 19.058 30.938 33.701 1.00 95.24 ? 157 VAL B N 1 ATOM 8408 C CA . VAL B 2 157 ? 19.354 32.199 34.368 1.00 91.16 ? 157 VAL B CA 1 ATOM 8409 C C . VAL B 2 157 ? 18.407 33.279 33.863 1.00 89.79 ? 157 VAL B C 1 ATOM 8410 O O . VAL B 2 157 ? 17.536 33.733 34.598 1.00 90.37 ? 157 VAL B O 1 ATOM 8411 C CB . VAL B 2 157 ? 20.809 32.652 34.147 1.00 92.27 ? 157 VAL B CB 1 ATOM 8412 C CG1 . VAL B 2 157 ? 21.073 33.945 34.899 1.00 101.62 ? 157 VAL B CG1 1 ATOM 8413 C CG2 . VAL B 2 157 ? 21.778 31.572 34.598 1.00 93.23 ? 157 VAL B CG2 1 ATOM 8414 N N . ASP B 2 158 ? 18.580 33.667 32.602 1.00 87.88 ? 158 ASP B N 1 ATOM 8415 C CA . ASP B 2 158 ? 17.726 34.647 31.932 1.00 85.47 ? 158 ASP B CA 1 ATOM 8416 C C . ASP B 2 158 ? 18.229 34.794 30.503 1.00 82.34 ? 158 ASP B C 1 ATOM 8417 O O . ASP B 2 158 ? 19.261 34.226 30.151 1.00 82.57 ? 158 ASP B O 1 ATOM 8418 C CB . ASP B 2 158 ? 17.740 36.000 32.651 1.00 87.28 ? 158 ASP B CB 1 ATOM 8419 C CG . ASP B 2 158 ? 16.463 36.792 32.436 1.00 83.26 ? 158 ASP B CG 1 ATOM 8420 O OD1 . ASP B 2 158 ? 15.865 36.684 31.344 1.00 78.69 ? 158 ASP B OD1 1 ATOM 8421 O OD2 . ASP B 2 158 ? 16.057 37.524 33.365 1.00 82.03 ? 158 ASP B OD2 1 ATOM 8422 N N . LYS B 2 159 ? 17.510 35.554 29.682 1.00 77.87 ? 159 LYS B N 1 ATOM 8423 C CA . LYS B 2 159 ? 17.920 35.761 28.296 1.00 72.62 ? 159 LYS B CA 1 ATOM 8424 C C . LYS B 2 159 ? 19.262 36.488 28.220 1.00 77.03 ? 159 LYS B C 1 ATOM 8425 O O . LYS B 2 159 ? 19.387 37.622 28.683 1.00 76.16 ? 159 LYS B O 1 ATOM 8426 C CB . LYS B 2 159 ? 16.851 36.542 27.529 1.00 69.43 ? 159 LYS B CB 1 ATOM 8427 C CG . LYS B 2 159 ? 15.555 35.774 27.318 1.00 79.18 ? 159 LYS B CG 1 ATOM 8428 C CD . LYS B 2 159 ? 14.598 36.525 26.405 1.00 74.64 ? 159 LYS B CD 1 ATOM 8429 C CE . LYS B 2 159 ? 13.358 35.695 26.107 1.00 70.68 ? 159 LYS B CE 1 ATOM 8430 N NZ . LYS B 2 159 ? 13.699 34.384 25.489 1.00 80.54 ? 159 LYS B NZ 1 ATOM 8431 N N . PRO B 2 160 ? 20.271 35.832 27.625 1.00 79.79 ? 160 PRO B N 1 ATOM 8432 C CA . PRO B 2 160 ? 21.636 36.365 27.538 1.00 75.58 ? 160 PRO B CA 1 ATOM 8433 C C . PRO B 2 160 ? 21.738 37.546 26.579 1.00 88.42 ? 160 PRO B C 1 ATOM 8434 O O . PRO B 2 160 ? 22.470 37.481 25.592 1.00 120.54 ? 160 PRO B O 1 ATOM 8435 C CB . PRO B 2 160 ? 22.441 35.171 27.022 1.00 74.51 ? 160 PRO B CB 1 ATOM 8436 C CG . PRO B 2 160 ? 21.459 34.391 26.223 1.00 73.77 ? 160 PRO B CG 1 ATOM 8437 C CD . PRO B 2 160 ? 20.144 34.533 26.941 1.00 85.62 ? 160 PRO B CD 1 ATOM 8438 N N . VAL B 2 161 ? 21.005 38.614 26.877 1.00 78.22 ? 161 VAL B N 1 ATOM 8439 C CA . VAL B 2 161 ? 20.971 39.792 26.024 1.00 68.31 ? 161 VAL B CA 1 ATOM 8440 C C . VAL B 2 161 ? 20.554 41.016 26.837 1.00 69.65 ? 161 VAL B C 1 ATOM 8441 O O . VAL B 2 161 ? 20.030 40.887 27.943 1.00 69.93 ? 161 VAL B O 1 ATOM 8442 C CB . VAL B 2 161 ? 20.006 39.595 24.832 1.00 63.71 ? 161 VAL B CB 1 ATOM 8443 C CG1 . VAL B 2 161 ? 18.580 39.956 25.229 1.00 53.58 ? 161 VAL B CG1 1 ATOM 8444 C CG2 . VAL B 2 161 ? 20.457 40.419 23.636 1.00 101.47 ? 161 VAL B CG2 1 ATOM 8445 N N . SER B 2 162 ? 20.801 42.201 26.291 1.00 63.24 ? 162 SER B N 1 ATOM 8446 C CA . SER B 2 162 ? 20.430 43.451 26.944 1.00 63.36 ? 162 SER B CA 1 ATOM 8447 C C . SER B 2 162 ? 18.909 43.625 27.032 1.00 62.60 ? 162 SER B C 1 ATOM 8448 O O . SER B 2 162 ? 18.177 43.155 26.161 1.00 80.86 ? 162 SER B O 1 ATOM 8449 C CB . SER B 2 162 ? 21.059 44.629 26.186 1.00 86.87 ? 162 SER B CB 1 ATOM 8450 O OG . SER B 2 162 ? 20.779 45.872 26.808 1.00 89.63 ? 162 SER B OG 1 ATOM 8451 N N . PRO B 2 163 ? 18.432 44.314 28.085 1.00 57.41 ? 163 PRO B N 1 ATOM 8452 C CA . PRO B 2 163 ? 19.242 44.690 29.247 1.00 78.47 ? 163 PRO B CA 1 ATOM 8453 C C . PRO B 2 163 ? 19.183 43.684 30.393 1.00 75.06 ? 163 PRO B C 1 ATOM 8454 O O . PRO B 2 163 ? 19.063 44.103 31.543 1.00 84.77 ? 163 PRO B O 1 ATOM 8455 C CB . PRO B 2 163 ? 18.603 46.007 29.677 1.00 95.87 ? 163 PRO B CB 1 ATOM 8456 C CG . PRO B 2 163 ? 17.141 45.787 29.383 1.00 71.49 ? 163 PRO B CG 1 ATOM 8457 C CD . PRO B 2 163 ? 17.076 44.887 28.160 1.00 50.27 ? 163 PRO B CD 1 ATOM 8458 N N . TYR B 2 164 ? 19.266 42.393 30.095 1.00 78.43 ? 164 TYR B N 1 ATOM 8459 C CA . TYR B 2 164 ? 19.355 41.377 31.139 1.00 83.25 ? 164 TYR B CA 1 ATOM 8460 C C . TYR B 2 164 ? 20.798 41.108 31.553 1.00 88.57 ? 164 TYR B C 1 ATOM 8461 O O . TYR B 2 164 ? 21.109 40.967 32.736 1.00 92.42 ? 164 TYR B O 1 ATOM 8462 C CB . TYR B 2 164 ? 18.668 40.092 30.679 1.00 83.39 ? 164 TYR B CB 1 ATOM 8463 C CG . TYR B 2 164 ? 17.276 40.342 30.147 1.00 72.12 ? 164 TYR B CG 1 ATOM 8464 C CD1 . TYR B 2 164 ? 16.984 40.170 28.802 1.00 64.62 ? 164 TYR B CD1 1 ATOM 8465 C CD2 . TYR B 2 164 ? 16.259 40.782 30.987 1.00 69.13 ? 164 TYR B CD2 1 ATOM 8466 C CE1 . TYR B 2 164 ? 15.714 40.408 28.311 1.00 65.16 ? 164 TYR B CE1 1 ATOM 8467 C CE2 . TYR B 2 164 ? 14.988 41.025 30.505 1.00 59.79 ? 164 TYR B CE2 1 ATOM 8468 C CZ . TYR B 2 164 ? 14.721 40.837 29.165 1.00 62.43 ? 164 TYR B CZ 1 ATOM 8469 O OH . TYR B 2 164 ? 13.454 41.076 28.682 1.00 72.38 ? 164 TYR B OH 1 ATOM 8470 N N . MET B 2 165 ? 21.670 41.046 30.552 1.00 86.37 ? 165 MET B N 1 ATOM 8471 C CA . MET B 2 165 ? 23.052 40.611 30.721 1.00 89.61 ? 165 MET B CA 1 ATOM 8472 C C . MET B 2 165 ? 23.996 41.784 30.938 1.00 103.75 ? 165 MET B C 1 ATOM 8473 O O . MET B 2 165 ? 23.798 42.855 30.364 1.00 113.49 ? 165 MET B O 1 ATOM 8474 C CB . MET B 2 165 ? 23.490 39.810 29.492 1.00 85.29 ? 165 MET B CB 1 ATOM 8475 C CG . MET B 2 165 ? 24.898 39.245 29.556 1.00 94.71 ? 165 MET B CG 1 ATOM 8476 S SD . MET B 2 165 ? 25.258 38.219 28.119 1.00 101.23 ? 165 MET B SD 1 ATOM 8477 C CE . MET B 2 165 ? 24.883 39.360 26.790 1.00 117.31 ? 165 MET B CE 1 ATOM 8478 N N . TYR B 2 166 ? 25.024 41.594 31.763 1.00 103.50 ? 166 TYR B N 1 ATOM 8479 C CA . TYR B 2 166 ? 26.027 42.637 31.902 1.00 98.00 ? 166 TYR B CA 1 ATOM 8480 C C . TYR B 2 166 ? 26.960 42.556 30.706 1.00 95.80 ? 166 TYR B C 1 ATOM 8481 O O . TYR B 2 166 ? 27.729 41.605 30.571 1.00 95.57 ? 166 TYR B O 1 ATOM 8482 C CB . TYR B 2 166 ? 26.826 42.466 33.199 1.00 101.25 ? 166 TYR B CB 1 ATOM 8483 C CG . TYR B 2 166 ? 26.062 42.744 34.472 1.00 101.90 ? 166 TYR B CG 1 ATOM 8484 C CD1 . TYR B 2 166 ? 26.338 43.871 35.232 1.00 105.06 ? 166 TYR B CD1 1 ATOM 8485 C CD2 . TYR B 2 166 ? 25.077 41.875 34.923 1.00 101.33 ? 166 TYR B CD2 1 ATOM 8486 C CE1 . TYR B 2 166 ? 25.648 44.133 36.397 1.00 102.73 ? 166 TYR B CE1 1 ATOM 8487 C CE2 . TYR B 2 166 ? 24.382 42.130 36.090 1.00 101.69 ? 166 TYR B CE2 1 ATOM 8488 C CZ . TYR B 2 166 ? 24.673 43.260 36.823 1.00 102.36 ? 166 TYR B CZ 1 ATOM 8489 O OH . TYR B 2 166 ? 23.985 43.520 37.985 1.00 109.74 ? 166 TYR B OH 1 ATOM 8490 N N . ILE B 2 167 ? 26.887 43.558 29.838 1.00 102.38 ? 167 ILE B N 1 ATOM 8491 C CA . ILE B 2 167 ? 27.800 43.668 28.707 1.00 100.34 ? 167 ILE B CA 1 ATOM 8492 C C . ILE B 2 167 ? 28.878 44.733 28.894 1.00 109.89 ? 167 ILE B C 1 ATOM 8493 O O . ILE B 2 167 ? 29.773 44.865 28.059 1.00 112.62 ? 167 ILE B O 1 ATOM 8494 C CB . ILE B 2 167 ? 27.025 43.979 27.417 1.00 86.91 ? 167 ILE B CB 1 ATOM 8495 C CG1 . ILE B 2 167 ? 26.219 45.267 27.591 1.00 86.93 ? 167 ILE B CG1 1 ATOM 8496 C CG2 . ILE B 2 167 ? 26.107 42.823 27.060 1.00 77.04 ? 167 ILE B CG2 1 ATOM 8497 C CD1 . ILE B 2 167 ? 25.280 45.566 26.445 1.00 94.89 ? 167 ILE B CD1 1 ATOM 8498 N N . SER B 2 168 ? 28.788 45.490 29.985 1.00 120.23 ? 168 SER B N 1 ATOM 8499 C CA . SER B 2 168 ? 29.448 46.793 30.044 1.00 115.32 ? 168 SER B CA 1 ATOM 8500 C C . SER B 2 168 ? 30.991 46.757 29.994 1.00 105.55 ? 168 SER B C 1 ATOM 8501 O O . SER B 2 168 ? 31.571 47.315 29.064 1.00 122.82 ? 168 SER B O 1 ATOM 8502 C CB . SER B 2 168 ? 28.948 47.558 31.276 1.00 142.14 ? 168 SER B CB 1 ATOM 8503 O OG . SER B 2 168 ? 28.460 46.673 32.270 1.00 150.64 ? 168 SER B OG 1 ATOM 8504 N N . PRO B 2 169 ? 31.673 46.117 30.968 1.00 104.24 ? 169 PRO B N 1 ATOM 8505 C CA . PRO B 2 169 ? 33.069 45.865 30.592 1.00 101.38 ? 169 PRO B CA 1 ATOM 8506 C C . PRO B 2 169 ? 33.182 44.626 29.712 1.00 98.55 ? 169 PRO B C 1 ATOM 8507 O O . PRO B 2 169 ? 32.274 43.796 29.726 1.00 114.76 ? 169 PRO B O 1 ATOM 8508 C CB . PRO B 2 169 ? 33.774 45.649 31.938 1.00 103.53 ? 169 PRO B CB 1 ATOM 8509 C CG . PRO B 2 169 ? 32.837 46.183 32.964 1.00 105.31 ? 169 PRO B CG 1 ATOM 8510 C CD . PRO B 2 169 ? 31.478 45.913 32.413 1.00 104.82 ? 169 PRO B CD 1 ATOM 8511 N N . PRO B 2 170 ? 34.276 44.503 28.948 1.00 108.96 ? 170 PRO B N 1 ATOM 8512 C CA . PRO B 2 170 ? 34.521 43.228 28.267 1.00 111.52 ? 170 PRO B CA 1 ATOM 8513 C C . PRO B 2 170 ? 34.763 42.107 29.276 1.00 111.60 ? 170 PRO B C 1 ATOM 8514 O O . PRO B 2 170 ? 34.500 40.942 28.979 1.00 108.89 ? 170 PRO B O 1 ATOM 8515 C CB . PRO B 2 170 ? 35.776 43.506 27.432 1.00 114.41 ? 170 PRO B CB 1 ATOM 8516 C CG . PRO B 2 170 ? 36.428 44.675 28.095 1.00 138.64 ? 170 PRO B CG 1 ATOM 8517 C CD . PRO B 2 170 ? 35.306 45.507 28.636 1.00 112.20 ? 170 PRO B CD 1 ATOM 8518 N N . GLU B 2 171 ? 35.249 42.467 30.461 1.00 119.41 ? 171 GLU B N 1 ATOM 8519 C CA . GLU B 2 171 ? 35.497 41.494 31.518 1.00 121.89 ? 171 GLU B CA 1 ATOM 8520 C C . GLU B 2 171 ? 34.200 41.051 32.195 1.00 120.19 ? 171 GLU B C 1 ATOM 8521 O O . GLU B 2 171 ? 34.194 40.087 32.961 1.00 131.90 ? 171 GLU B O 1 ATOM 8522 C CB . GLU B 2 171 ? 36.463 42.062 32.563 1.00 121.62 ? 171 GLU B CB 1 ATOM 8523 C CG . GLU B 2 171 ? 37.877 42.309 32.052 1.00 145.35 ? 171 GLU B CG 1 ATOM 8524 C CD . GLU B 2 171 ? 38.015 43.631 31.320 1.00 159.27 ? 171 GLU B CD 1 ATOM 8525 O OE1 . GLU B 2 171 ? 37.042 44.413 31.317 1.00 164.38 ? 171 GLU B OE1 1 ATOM 8526 O OE2 . GLU B 2 171 ? 39.096 43.887 30.751 1.00 166.49 ? 171 GLU B OE2 1 ATOM 8527 N N . ALA B 2 172 ? 33.107 41.755 31.916 1.00 107.02 ? 172 ALA B N 1 ATOM 8528 C CA . ALA B 2 172 ? 31.801 41.359 32.434 1.00 110.94 ? 172 ALA B CA 1 ATOM 8529 C C . ALA B 2 172 ? 31.317 40.106 31.718 1.00 104.19 ? 172 ALA B C 1 ATOM 8530 O O . ALA B 2 172 ? 30.561 39.311 32.274 1.00 95.36 ? 172 ALA B O 1 ATOM 8531 C CB . ALA B 2 172 ? 30.795 42.481 32.279 1.00 121.47 ? 172 ALA B CB 1 ATOM 8532 N N . LEU B 2 173 ? 31.748 39.943 30.473 1.00 111.70 ? 173 LEU B N 1 ATOM 8533 C CA . LEU B 2 173 ? 31.522 38.698 29.757 1.00 131.05 ? 173 LEU B CA 1 ATOM 8534 C C . LEU B 2 173 ? 32.548 37.684 30.241 1.00 147.41 ? 173 LEU B C 1 ATOM 8535 O O . LEU B 2 173 ? 33.708 38.038 30.468 1.00 145.66 ? 173 LEU B O 1 ATOM 8536 C CB . LEU B 2 173 ? 31.616 38.908 28.246 1.00 135.78 ? 173 LEU B CB 1 ATOM 8537 C CG . LEU B 2 173 ? 30.544 39.822 27.646 1.00 126.61 ? 173 LEU B CG 1 ATOM 8538 C CD1 . LEU B 2 173 ? 30.747 39.990 26.148 1.00 132.86 ? 173 LEU B CD1 1 ATOM 8539 C CD2 . LEU B 2 173 ? 29.151 39.284 27.945 1.00 114.43 ? 173 LEU B CD2 1 ATOM 8540 N N . GLU B 2 174 ? 32.093 36.445 30.440 1.00 131.74 ? 174 GLU B N 1 ATOM 8541 C CA . GLU B 2 174 ? 32.881 35.337 30.999 1.00 146.75 ? 174 GLU B CA 1 ATOM 8542 C C . GLU B 2 174 ? 33.061 35.514 32.513 1.00 140.66 ? 174 GLU B C 1 ATOM 8543 O O . GLU B 2 174 ? 33.363 34.561 33.232 1.00 139.51 ? 174 GLU B O 1 ATOM 8544 C CB . GLU B 2 174 ? 34.241 35.214 30.284 1.00 149.60 ? 174 GLU B CB 1 ATOM 8545 C CG . GLU B 2 174 ? 35.220 34.199 30.865 1.00 154.26 ? 174 GLU B CG 1 ATOM 8546 C CD . GLU B 2 174 ? 34.883 32.766 30.494 1.00 165.06 ? 174 GLU B CD 1 ATOM 8547 O OE1 . GLU B 2 174 ? 35.597 31.852 30.958 1.00 164.34 ? 174 GLU B OE1 1 ATOM 8548 O OE2 . GLU B 2 174 ? 33.913 32.553 29.737 1.00 164.48 ? 174 GLU B OE2 1 ATOM 8549 N N . ASN B 2 175 ? 32.838 36.733 32.995 1.00 130.26 ? 175 ASN B N 1 ATOM 8550 C CA . ASN B 2 175 ? 32.835 37.019 34.426 1.00 116.90 ? 175 ASN B CA 1 ATOM 8551 C C . ASN B 2 175 ? 31.809 38.095 34.783 1.00 114.66 ? 175 ASN B C 1 ATOM 8552 O O . ASN B 2 175 ? 32.172 39.260 34.952 1.00 117.12 ? 175 ASN B O 1 ATOM 8553 C CB . ASN B 2 175 ? 34.227 37.442 34.894 1.00 127.03 ? 175 ASN B CB 1 ATOM 8554 C CG . ASN B 2 175 ? 34.331 37.530 36.404 1.00 148.49 ? 175 ASN B CG 1 ATOM 8555 O OD1 . ASN B 2 175 ? 33.520 36.953 37.129 1.00 130.03 ? 175 ASN B OD1 1 ATOM 8556 N ND2 . ASN B 2 175 ? 35.332 38.258 36.887 1.00 163.53 ? 175 ASN B ND2 1 ATOM 8557 N N . PRO B 2 176 ? 30.523 37.713 34.881 1.00 110.33 ? 176 PRO B N 1 ATOM 8558 C CA . PRO B 2 176 ? 29.429 38.640 35.201 1.00 95.67 ? 176 PRO B CA 1 ATOM 8559 C C . PRO B 2 176 ? 29.680 39.462 36.462 1.00 96.74 ? 176 PRO B C 1 ATOM 8560 O O . PRO B 2 176 ? 29.110 40.542 36.609 1.00 94.71 ? 176 PRO B O 1 ATOM 8561 C CB . PRO B 2 176 ? 28.234 37.708 35.390 1.00 94.92 ? 176 PRO B CB 1 ATOM 8562 C CG . PRO B 2 176 ? 28.532 36.566 34.501 1.00 103.06 ? 176 PRO B CG 1 ATOM 8563 C CD . PRO B 2 176 ? 30.019 36.356 34.610 1.00 116.61 ? 176 PRO B CD 1 ATOM 8564 N N . CYS B 2 177 ? 30.520 38.956 37.357 1.00 99.98 ? 177 CYS B N 1 ATOM 8565 C CA . CYS B 2 177 ? 30.940 39.743 38.504 1.00 111.17 ? 177 CYS B CA 1 ATOM 8566 C C . CYS B 2 177 ? 32.342 40.299 38.273 1.00 137.05 ? 177 CYS B C 1 ATOM 8567 O O . CYS B 2 177 ? 33.331 39.570 38.318 1.00 162.86 ? 177 CYS B O 1 ATOM 8568 C CB . CYS B 2 177 ? 30.902 38.905 39.784 1.00 105.58 ? 177 CYS B CB 1 ATOM 8569 S SG . CYS B 2 177 ? 29.245 38.388 40.290 1.00 140.24 ? 177 CYS B SG 1 ATOM 8570 N N . TYR B 2 178 ? 32.408 41.601 38.026 1.00 117.32 ? 178 TYR B N 1 ATOM 8571 C CA . TYR B 2 178 ? 33.670 42.318 37.903 1.00 114.68 ? 178 TYR B CA 1 ATOM 8572 C C . TYR B 2 178 ? 33.647 43.410 38.954 1.00 149.87 ? 178 TYR B C 1 ATOM 8573 O O . TYR B 2 178 ? 34.489 43.452 39.851 1.00 164.55 ? 178 TYR B O 1 ATOM 8574 C CB . TYR B 2 178 ? 33.859 42.897 36.501 1.00 113.10 ? 178 TYR B CB 1 ATOM 8575 C CG . TYR B 2 178 ? 35.262 43.402 36.239 1.00 144.00 ? 178 TYR B CG 1 ATOM 8576 C CD1 . TYR B 2 178 ? 36.323 42.515 36.102 1.00 151.33 ? 178 TYR B CD1 1 ATOM 8577 C CD2 . TYR B 2 178 ? 35.525 44.761 36.126 1.00 140.23 ? 178 TYR B CD2 1 ATOM 8578 C CE1 . TYR B 2 178 ? 37.608 42.968 35.863 1.00 154.92 ? 178 TYR B CE1 1 ATOM 8579 C CE2 . TYR B 2 178 ? 36.808 45.223 35.886 1.00 144.89 ? 178 TYR B CE2 1 ATOM 8580 C CZ . TYR B 2 178 ? 37.845 44.321 35.755 1.00 149.22 ? 178 TYR B CZ 1 ATOM 8581 O OH . TYR B 2 178 ? 39.123 44.774 35.517 1.00 141.34 ? 178 TYR B OH 1 ATOM 8582 N N . ASP B 2 179 ? 32.672 44.304 38.821 1.00 148.50 ? 179 ASP B N 1 ATOM 8583 C CA . ASP B 2 179 ? 32.292 45.184 39.914 1.00 139.08 ? 179 ASP B CA 1 ATOM 8584 C C . ASP B 2 179 ? 31.874 44.315 41.096 1.00 139.00 ? 179 ASP B C 1 ATOM 8585 O O . ASP B 2 179 ? 31.379 43.202 40.903 1.00 124.05 ? 179 ASP B O 1 ATOM 8586 C CB . ASP B 2 179 ? 31.163 46.124 39.491 1.00 131.96 ? 179 ASP B CB 1 ATOM 8587 C CG . ASP B 2 179 ? 30.141 45.442 38.601 1.00 145.00 ? 179 ASP B CG 1 ATOM 8588 O OD1 . ASP B 2 179 ? 29.113 44.964 39.125 1.00 139.87 ? 179 ASP B OD1 1 ATOM 8589 O OD2 . ASP B 2 179 ? 30.366 45.386 37.373 1.00 149.62 ? 179 ASP B OD2 1 ATOM 8590 N N . MET B 2 180 ? 32.099 44.830 42.306 1.00 146.93 ? 180 MET B N 1 ATOM 8591 C CA . MET B 2 180 ? 31.940 44.094 43.569 1.00 154.83 ? 180 MET B CA 1 ATOM 8592 C C . MET B 2 180 ? 33.031 43.033 43.748 1.00 157.02 ? 180 MET B C 1 ATOM 8593 O O . MET B 2 180 ? 33.101 42.379 44.788 1.00 159.35 ? 180 MET B O 1 ATOM 8594 C CB . MET B 2 180 ? 30.551 43.446 43.682 1.00 145.87 ? 180 MET B CB 1 ATOM 8595 C CG . MET B 2 180 ? 29.398 44.428 43.847 1.00 145.94 ? 180 MET B CG 1 ATOM 8596 S SD . MET B 2 180 ? 28.859 45.179 42.299 1.00 204.57 ? 180 MET B SD 1 ATOM 8597 C CE . MET B 2 180 ? 27.474 46.163 42.865 1.00 142.31 ? 180 MET B CE 1 ATOM 8598 N N . LYS B 2 181 ? 33.865 42.865 42.723 1.00 156.67 ? 181 LYS B N 1 ATOM 8599 C CA . LYS B 2 181 ? 35.084 42.057 42.796 1.00 158.61 ? 181 LYS B CA 1 ATOM 8600 C C . LYS B 2 181 ? 34.878 40.632 43.312 1.00 160.38 ? 181 LYS B C 1 ATOM 8601 O O . LYS B 2 181 ? 35.312 40.292 44.413 1.00 172.87 ? 181 LYS B O 1 ATOM 8602 C CB . LYS B 2 181 ? 36.123 42.768 43.669 1.00 147.18 ? 181 LYS B CB 1 ATOM 8603 C CG . LYS B 2 181 ? 36.592 44.097 43.098 1.00 147.81 ? 181 LYS B CG 1 ATOM 8604 C CD . LYS B 2 181 ? 37.679 44.720 43.955 1.00 161.71 ? 181 LYS B CD 1 ATOM 8605 C CE . LYS B 2 181 ? 38.177 46.021 43.347 1.00 154.69 ? 181 LYS B CE 1 ATOM 8606 N NZ . LYS B 2 181 ? 39.261 46.634 44.162 1.00 164.37 ? 181 LYS B NZ 1 ATOM 8607 N N . THR B 2 182 ? 34.219 39.805 42.508 1.00 136.31 ? 182 THR B N 1 ATOM 8608 C CA . THR B 2 182 ? 34.046 38.392 42.826 1.00 138.29 ? 182 THR B CA 1 ATOM 8609 C C . THR B 2 182 ? 34.075 37.586 41.530 1.00 148.63 ? 182 THR B C 1 ATOM 8610 O O . THR B 2 182 ? 34.390 38.127 40.472 1.00 154.22 ? 182 THR B O 1 ATOM 8611 C CB . THR B 2 182 ? 32.730 38.130 43.584 1.00 145.16 ? 182 THR B CB 1 ATOM 8612 O OG1 . THR B 2 182 ? 32.308 39.330 44.244 1.00 147.88 ? 182 THR B OG1 1 ATOM 8613 C CG2 . THR B 2 182 ? 32.915 37.025 44.618 1.00 153.25 ? 182 THR B CG2 1 ATOM 8614 N N . THR B 2 183 ? 33.757 36.297 41.606 1.00 150.14 ? 183 THR B N 1 ATOM 8615 C CA . THR B 2 183 ? 33.748 35.462 40.410 1.00 135.00 ? 183 THR B CA 1 ATOM 8616 C C . THR B 2 183 ? 32.412 34.759 40.200 1.00 137.48 ? 183 THR B C 1 ATOM 8617 O O . THR B 2 183 ? 32.020 33.890 40.979 1.00 137.43 ? 183 THR B O 1 ATOM 8618 C CB . THR B 2 183 ? 34.860 34.401 40.458 1.00 137.16 ? 183 THR B CB 1 ATOM 8619 O OG1 . THR B 2 183 ? 36.139 35.047 40.490 1.00 146.04 ? 183 THR B OG1 1 ATOM 8620 C CG2 . THR B 2 183 ? 34.785 33.498 39.234 1.00 127.11 ? 183 THR B CG2 1 ATOM 8621 N N . CYS B 2 184 ? 31.719 35.149 39.136 1.00 135.75 ? 184 CYS B N 1 ATOM 8622 C CA . CYS B 2 184 ? 30.499 34.477 38.710 1.00 107.47 ? 184 CYS B CA 1 ATOM 8623 C C . CYS B 2 184 ? 30.783 33.663 37.455 1.00 106.87 ? 184 CYS B C 1 ATOM 8624 O O . CYS B 2 184 ? 31.924 33.587 37.003 1.00 131.78 ? 184 CYS B O 1 ATOM 8625 C CB . CYS B 2 184 ? 29.379 35.488 38.455 1.00 104.00 ? 184 CYS B CB 1 ATOM 8626 S SG . CYS B 2 184 ? 28.875 36.427 39.916 1.00 167.78 ? 184 CYS B SG 1 ATOM 8627 N N . LEU B 2 185 ? 29.746 33.052 36.895 1.00 105.34 ? 185 LEU B N 1 ATOM 8628 C CA . LEU B 2 185 ? 29.882 32.334 35.635 1.00 105.60 ? 185 LEU B CA 1 ATOM 8629 C C . LEU B 2 185 ? 29.018 33.018 34.582 1.00 102.77 ? 185 LEU B C 1 ATOM 8630 O O . LEU B 2 185 ? 27.952 33.538 34.908 1.00 105.98 ? 185 LEU B O 1 ATOM 8631 C CB . LEU B 2 185 ? 29.480 30.862 35.792 1.00 112.49 ? 185 LEU B CB 1 ATOM 8632 C CG . LEU B 2 185 ? 30.500 29.877 36.376 1.00 135.99 ? 185 LEU B CG 1 ATOM 8633 C CD1 . LEU B 2 185 ? 30.811 30.180 37.836 1.00 148.17 ? 185 LEU B CD1 1 ATOM 8634 C CD2 . LEU B 2 185 ? 30.010 28.443 36.217 1.00 129.83 ? 185 LEU B CD2 1 ATOM 8635 N N . PRO B 2 186 ? 29.476 33.019 33.317 1.00 101.64 ? 186 PRO B N 1 ATOM 8636 C CA . PRO B 2 186 ? 28.744 33.658 32.216 1.00 100.24 ? 186 PRO B CA 1 ATOM 8637 C C . PRO B 2 186 ? 27.307 33.160 32.113 1.00 97.50 ? 186 PRO B C 1 ATOM 8638 O O . PRO B 2 186 ? 27.070 31.953 32.147 1.00 113.69 ? 186 PRO B O 1 ATOM 8639 C CB . PRO B 2 186 ? 29.554 33.263 30.972 1.00 103.73 ? 186 PRO B CB 1 ATOM 8640 C CG . PRO B 2 186 ? 30.448 32.142 31.414 1.00 110.37 ? 186 PRO B CG 1 ATOM 8641 C CD . PRO B 2 186 ? 30.732 32.410 32.853 1.00 104.65 ? 186 PRO B CD 1 ATOM 8642 N N . MET B 2 187 ? 26.363 34.087 31.992 1.00 92.50 ? 187 MET B N 1 ATOM 8643 C CA . MET B 2 187 ? 24.950 33.737 32.051 1.00 93.94 ? 187 MET B CA 1 ATOM 8644 C C . MET B 2 187 ? 24.474 33.007 30.801 1.00 90.87 ? 187 MET B C 1 ATOM 8645 O O . MET B 2 187 ? 25.090 33.088 29.737 1.00 92.36 ? 187 MET B O 1 ATOM 8646 C CB . MET B 2 187 ? 24.098 34.985 32.277 1.00 85.16 ? 187 MET B CB 1 ATOM 8647 C CG . MET B 2 187 ? 23.827 35.794 31.026 1.00 82.45 ? 187 MET B CG 1 ATOM 8648 S SD . MET B 2 187 ? 22.570 37.044 31.328 1.00 92.41 ? 187 MET B SD 1 ATOM 8649 C CE . MET B 2 187 ? 21.228 36.027 31.920 1.00 76.21 ? 187 MET B CE 1 ATOM 8650 N N . PHE B 2 188 ? 23.365 32.292 30.954 1.00 89.27 ? 188 PHE B N 1 ATOM 8651 C CA . PHE B 2 188 ? 22.798 31.467 29.897 1.00 93.00 ? 188 PHE B CA 1 ATOM 8652 C C . PHE B 2 188 ? 21.281 31.424 30.044 1.00 102.78 ? 188 PHE B C 1 ATOM 8653 O O . PHE B 2 188 ? 20.767 31.440 31.162 1.00 101.60 ? 188 PHE B O 1 ATOM 8654 C CB . PHE B 2 188 ? 23.386 30.055 29.952 1.00 95.92 ? 188 PHE B CB 1 ATOM 8655 C CG . PHE B 2 188 ? 23.449 29.480 31.343 1.00 97.67 ? 188 PHE B CG 1 ATOM 8656 C CD1 . PHE B 2 188 ? 22.356 28.827 31.888 1.00 95.45 ? 188 PHE B CD1 1 ATOM 8657 C CD2 . PHE B 2 188 ? 24.601 29.597 32.106 1.00 108.84 ? 188 PHE B CD2 1 ATOM 8658 C CE1 . PHE B 2 188 ? 22.409 28.302 33.166 1.00 97.56 ? 188 PHE B CE1 1 ATOM 8659 C CE2 . PHE B 2 188 ? 24.661 29.072 33.385 1.00 112.80 ? 188 PHE B CE2 1 ATOM 8660 C CZ . PHE B 2 188 ? 23.563 28.425 33.915 1.00 102.40 ? 188 PHE B CZ 1 ATOM 8661 N N . GLY B 2 189 ? 20.562 31.383 28.926 1.00 101.69 ? 189 GLY B N 1 ATOM 8662 C CA . GLY B 2 189 ? 19.113 31.328 28.984 1.00 106.41 ? 189 GLY B CA 1 ATOM 8663 C C . GLY B 2 189 ? 18.617 30.027 29.583 1.00 87.24 ? 189 GLY B C 1 ATOM 8664 O O . GLY B 2 189 ? 17.926 30.024 30.602 1.00 77.96 ? 189 GLY B O 1 ATOM 8665 N N . TYR B 2 190 ? 18.978 28.918 28.947 1.00 83.92 ? 190 TYR B N 1 ATOM 8666 C CA . TYR B 2 190 ? 18.716 27.590 29.490 1.00 84.68 ? 190 TYR B CA 1 ATOM 8667 C C . TYR B 2 190 ? 19.742 26.593 28.970 1.00 90.47 ? 190 TYR B C 1 ATOM 8668 O O . TYR B 2 190 ? 20.151 26.664 27.811 1.00 92.69 ? 190 TYR B O 1 ATOM 8669 C CB . TYR B 2 190 ? 17.300 27.129 29.136 1.00 80.57 ? 190 TYR B CB 1 ATOM 8670 C CG . TYR B 2 190 ? 17.054 25.652 29.361 1.00 98.18 ? 190 TYR B CG 1 ATOM 8671 C CD1 . TYR B 2 190 ? 16.969 25.127 30.645 1.00 97.52 ? 190 TYR B CD1 1 ATOM 8672 C CD2 . TYR B 2 190 ? 16.901 24.783 28.289 1.00 104.78 ? 190 TYR B CD2 1 ATOM 8673 C CE1 . TYR B 2 190 ? 16.742 23.778 30.852 1.00 87.86 ? 190 TYR B CE1 1 ATOM 8674 C CE2 . TYR B 2 190 ? 16.674 23.434 28.486 1.00 84.12 ? 190 TYR B CE2 1 ATOM 8675 C CZ . TYR B 2 190 ? 16.595 22.937 29.770 1.00 88.38 ? 190 TYR B CZ 1 ATOM 8676 O OH . TYR B 2 190 ? 16.368 21.594 29.970 1.00 94.77 ? 190 TYR B OH 1 ATOM 8677 N N . LYS B 2 191 ? 20.151 25.657 29.819 1.00 93.03 ? 191 LYS B N 1 ATOM 8678 C CA . LYS B 2 191 ? 21.031 24.587 29.369 1.00 100.83 ? 191 LYS B CA 1 ATOM 8679 C C . LYS B 2 191 ? 20.678 23.258 30.027 1.00 101.56 ? 191 LYS B C 1 ATOM 8680 O O . LYS B 2 191 ? 20.415 23.186 31.228 1.00 98.46 ? 191 LYS B O 1 ATOM 8681 C CB . LYS B 2 191 ? 22.502 24.939 29.624 1.00 104.81 ? 191 LYS B CB 1 ATOM 8682 C CG . LYS B 2 191 ? 22.906 25.077 31.084 1.00 106.73 ? 191 LYS B CG 1 ATOM 8683 C CD . LYS B 2 191 ? 24.401 25.352 31.197 1.00 111.97 ? 191 LYS B CD 1 ATOM 8684 C CE . LYS B 2 191 ? 24.853 25.462 32.645 1.00 114.82 ? 191 LYS B CE 1 ATOM 8685 N NZ . LYS B 2 191 ? 24.683 24.186 33.392 1.00 118.20 ? 191 LYS B NZ 1 ATOM 8686 N N . HIS B 2 192 ? 20.662 22.206 29.215 1.00 97.47 ? 192 HIS B N 1 ATOM 8687 C CA . HIS B 2 192 ? 20.386 20.862 29.697 1.00 97.07 ? 192 HIS B CA 1 ATOM 8688 C C . HIS B 2 192 ? 21.671 20.210 30.187 1.00 101.32 ? 192 HIS B C 1 ATOM 8689 O O . HIS B 2 192 ? 22.612 20.019 29.418 1.00 105.79 ? 192 HIS B O 1 ATOM 8690 C CB . HIS B 2 192 ? 19.744 20.021 28.593 1.00 97.58 ? 192 HIS B CB 1 ATOM 8691 C CG . HIS B 2 192 ? 19.550 18.585 28.962 1.00 107.10 ? 192 HIS B CG 1 ATOM 8692 N ND1 . HIS B 2 192 ? 18.749 18.189 30.011 1.00 112.55 ? 192 HIS B ND1 1 ATOM 8693 C CD2 . HIS B 2 192 ? 20.050 17.450 28.419 1.00 106.04 ? 192 HIS B CD2 1 ATOM 8694 C CE1 . HIS B 2 192 ? 18.765 16.871 30.099 1.00 125.03 ? 192 HIS B CE1 1 ATOM 8695 N NE2 . HIS B 2 192 ? 19.547 16.398 29.145 1.00 118.54 ? 192 HIS B NE2 1 ATOM 8696 N N . VAL B 2 193 ? 21.705 19.868 31.470 1.00 100.98 ? 193 VAL B N 1 ATOM 8697 C CA . VAL B 2 193 ? 22.909 19.321 32.080 1.00 107.40 ? 193 VAL B CA 1 ATOM 8698 C C . VAL B 2 193 ? 22.916 17.797 32.054 1.00 120.96 ? 193 VAL B C 1 ATOM 8699 O O . VAL B 2 193 ? 23.697 17.184 31.328 1.00 128.29 ? 193 VAL B O 1 ATOM 8700 C CB . VAL B 2 193 ? 23.066 19.799 33.534 1.00 103.98 ? 193 VAL B CB 1 ATOM 8701 C CG1 . VAL B 2 193 ? 24.425 19.392 34.079 1.00 118.54 ? 193 VAL B CG1 1 ATOM 8702 C CG2 . VAL B 2 193 ? 22.886 21.305 33.616 1.00 103.59 ? 193 VAL B CG2 1 ATOM 8703 N N . LEU B 2 194 ? 22.040 17.190 32.849 1.00 123.94 ? 194 LEU B N 1 ATOM 8704 C CA . LEU B 2 194 ? 21.987 15.737 32.948 1.00 127.38 ? 194 LEU B CA 1 ATOM 8705 C C . LEU B 2 194 ? 20.651 15.180 32.468 1.00 116.69 ? 194 LEU B C 1 ATOM 8706 O O . LEU B 2 194 ? 19.596 15.520 33.003 1.00 98.17 ? 194 LEU B O 1 ATOM 8707 C CB . LEU B 2 194 ? 22.251 15.294 34.389 1.00 118.72 ? 194 LEU B CB 1 ATOM 8708 C CG . LEU B 2 194 ? 22.251 13.787 34.644 1.00 129.52 ? 194 LEU B CG 1 ATOM 8709 C CD1 . LEU B 2 194 ? 23.257 13.096 33.738 1.00 140.85 ? 194 LEU B CD1 1 ATOM 8710 C CD2 . LEU B 2 194 ? 22.546 13.489 36.105 1.00 136.31 ? 194 LEU B CD2 1 ATOM 8711 N N . THR B 2 195 ? 20.707 14.318 31.457 1.00 116.70 ? 195 THR B N 1 ATOM 8712 C CA . THR B 2 195 ? 19.511 13.664 30.939 1.00 111.27 ? 195 THR B CA 1 ATOM 8713 C C . THR B 2 195 ? 18.993 12.650 31.949 1.00 124.56 ? 195 THR B C 1 ATOM 8714 O O . THR B 2 195 ? 19.734 12.219 32.835 1.00 119.81 ? 195 THR B O 1 ATOM 8715 C CB . THR B 2 195 ? 19.778 12.968 29.592 1.00 108.03 ? 195 THR B CB 1 ATOM 8716 O OG1 . THR B 2 195 ? 18.540 12.510 29.035 1.00 107.30 ? 195 THR B OG1 1 ATOM 8717 C CG2 . THR B 2 195 ? 20.719 11.789 29.776 1.00 136.85 ? 195 THR B CG2 1 ATOM 8718 N N . LEU B 2 196 ? 17.721 12.280 31.824 1.00 131.31 ? 196 LEU B N 1 ATOM 8719 C CA . LEU B 2 196 ? 17.099 11.374 32.784 1.00 117.72 ? 196 LEU B CA 1 ATOM 8720 C C . LEU B 2 196 ? 17.804 10.022 32.808 1.00 112.85 ? 196 LEU B C 1 ATOM 8721 O O . LEU B 2 196 ? 17.926 9.354 31.781 1.00 115.93 ? 196 LEU B O 1 ATOM 8722 C CB . LEU B 2 196 ? 15.613 11.186 32.465 1.00 109.32 ? 196 LEU B CB 1 ATOM 8723 C CG . LEU B 2 196 ? 14.699 12.397 32.681 1.00 103.39 ? 196 LEU B CG 1 ATOM 8724 C CD1 . LEU B 2 196 ? 13.289 12.099 32.197 1.00 99.04 ? 196 LEU B CD1 1 ATOM 8725 C CD2 . LEU B 2 196 ? 14.685 12.817 34.141 1.00 97.96 ? 196 LEU B CD2 1 ATOM 8726 N N . THR B 2 197 ? 18.258 9.628 33.993 1.00 115.09 ? 197 THR B N 1 ATOM 8727 C CA . THR B 2 197 ? 18.984 8.375 34.182 1.00 130.23 ? 197 THR B CA 1 ATOM 8728 C C . THR B 2 197 ? 18.608 7.740 35.515 1.00 130.77 ? 197 THR B C 1 ATOM 8729 O O . THR B 2 197 ? 18.046 8.400 36.389 1.00 120.44 ? 197 THR B O 1 ATOM 8730 C CB . THR B 2 197 ? 20.517 8.577 34.143 1.00 142.47 ? 197 THR B CB 1 ATOM 8731 O OG1 . THR B 2 197 ? 20.891 9.619 35.054 1.00 152.76 ? 197 THR B OG1 1 ATOM 8732 C CG2 . THR B 2 197 ? 20.989 8.938 32.741 1.00 142.21 ? 197 THR B CG2 1 ATOM 8733 N N . ASP B 2 198 ? 18.927 6.459 35.667 1.00 129.97 ? 198 ASP B N 1 ATOM 8734 C CA . ASP B 2 198 ? 18.615 5.729 36.891 1.00 135.10 ? 198 ASP B CA 1 ATOM 8735 C C . ASP B 2 198 ? 19.765 5.804 37.891 1.00 148.88 ? 198 ASP B C 1 ATOM 8736 O O . ASP B 2 198 ? 19.707 5.202 38.964 1.00 154.78 ? 198 ASP B O 1 ATOM 8737 C CB . ASP B 2 198 ? 18.290 4.268 36.575 1.00 145.28 ? 198 ASP B CB 1 ATOM 8738 C CG . ASP B 2 198 ? 19.438 3.548 35.894 1.00 153.86 ? 198 ASP B CG 1 ATOM 8739 O OD1 . ASP B 2 198 ? 20.155 4.190 35.098 1.00 158.16 ? 198 ASP B OD1 1 ATOM 8740 O OD2 . ASP B 2 198 ? 19.627 2.340 36.155 1.00 155.10 ? 198 ASP B OD2 1 ATOM 8741 N N . GLN B 2 199 ? 20.806 6.550 37.535 1.00 146.33 ? 199 GLN B N 1 ATOM 8742 C CA . GLN B 2 199 ? 21.989 6.667 38.380 1.00 142.09 ? 199 GLN B CA 1 ATOM 8743 C C . GLN B 2 199 ? 21.932 7.916 39.253 1.00 137.16 ? 199 GLN B C 1 ATOM 8744 O O . GLN B 2 199 ? 22.025 9.037 38.753 1.00 140.26 ? 199 GLN B O 1 ATOM 8745 C CB . GLN B 2 199 ? 23.251 6.692 37.517 1.00 143.62 ? 199 GLN B CB 1 ATOM 8746 C CG . GLN B 2 199 ? 23.380 5.514 36.568 1.00 155.90 ? 199 GLN B CG 1 ATOM 8747 C CD . GLN B 2 199 ? 24.203 5.847 35.339 1.00 160.26 ? 199 GLN B CD 1 ATOM 8748 O OE1 . GLN B 2 199 ? 24.190 6.980 34.858 1.00 154.12 ? 199 GLN B OE1 1 ATOM 8749 N NE2 . GLN B 2 199 ? 24.926 4.859 34.824 1.00 153.62 ? 199 GLN B NE2 1 ATOM 8750 N N . VAL B 2 200 ? 21.780 7.717 40.558 1.00 140.60 ? 200 VAL B N 1 ATOM 8751 C CA . VAL B 2 200 ? 21.779 8.829 41.502 1.00 137.25 ? 200 VAL B CA 1 ATOM 8752 C C . VAL B 2 200 ? 23.203 9.206 41.894 1.00 145.15 ? 200 VAL B C 1 ATOM 8753 O O . VAL B 2 200 ? 23.446 10.294 42.415 1.00 148.04 ? 200 VAL B O 1 ATOM 8754 C CB . VAL B 2 200 ? 20.970 8.496 42.771 1.00 135.28 ? 200 VAL B CB 1 ATOM 8755 C CG1 . VAL B 2 200 ? 19.541 8.124 42.406 1.00 129.39 ? 200 VAL B CG1 1 ATOM 8756 C CG2 . VAL B 2 200 ? 21.635 7.371 43.550 1.00 154.83 ? 200 VAL B CG2 1 ATOM 8757 N N . THR B 2 201 ? 24.142 8.299 41.634 1.00 148.35 ? 201 THR B N 1 ATOM 8758 C CA . THR B 2 201 ? 25.545 8.531 41.953 1.00 150.40 ? 201 THR B CA 1 ATOM 8759 C C . THR B 2 201 ? 26.127 9.599 41.039 1.00 160.58 ? 201 THR B C 1 ATOM 8760 O O . THR B 2 201 ? 26.843 10.494 41.488 1.00 171.78 ? 201 THR B O 1 ATOM 8761 C CB . THR B 2 201 ? 26.376 7.244 41.828 1.00 154.38 ? 201 THR B CB 1 ATOM 8762 O OG1 . THR B 2 201 ? 26.310 6.759 40.481 1.00 154.33 ? 201 THR B OG1 1 ATOM 8763 C CG2 . THR B 2 201 ? 25.849 6.175 42.773 1.00 183.31 ? 201 THR B CG2 1 ATOM 8764 N N . ARG B 2 202 ? 25.815 9.494 39.752 1.00 152.94 ? 202 ARG B N 1 ATOM 8765 C CA . ARG B 2 202 ? 26.243 10.489 38.779 1.00 153.27 ? 202 ARG B CA 1 ATOM 8766 C C . ARG B 2 202 ? 25.552 11.821 39.040 1.00 145.25 ? 202 ARG B C 1 ATOM 8767 O O . ARG B 2 202 ? 26.152 12.884 38.883 1.00 147.87 ? 202 ARG B O 1 ATOM 8768 C CB . ARG B 2 202 ? 25.951 10.009 37.355 1.00 157.28 ? 202 ARG B CB 1 ATOM 8769 C CG . ARG B 2 202 ? 26.206 11.056 36.282 1.00 165.14 ? 202 ARG B CG 1 ATOM 8770 C CD . ARG B 2 202 ? 26.021 10.482 34.887 1.00 164.81 ? 202 ARG B CD 1 ATOM 8771 N NE . ARG B 2 202 ? 26.185 11.505 33.859 1.00 164.85 ? 202 ARG B NE 1 ATOM 8772 C CZ . ARG B 2 202 ? 27.359 11.898 33.374 1.00 166.07 ? 202 ARG B CZ 1 ATOM 8773 N NH1 . ARG B 2 202 ? 28.480 11.355 33.826 1.00 169.66 ? 202 ARG B NH1 1 ATOM 8774 N NH2 . ARG B 2 202 ? 27.411 12.837 32.439 1.00 154.13 ? 202 ARG B NH2 1 ATOM 8775 N N . PHE B 2 203 ? 24.290 11.751 39.452 1.00 127.39 ? 203 PHE B N 1 ATOM 8776 C CA . PHE B 2 203 ? 23.474 12.939 39.679 1.00 124.45 ? 203 PHE B CA 1 ATOM 8777 C C . PHE B 2 203 ? 24.082 13.874 40.722 1.00 137.17 ? 203 PHE B C 1 ATOM 8778 O O . PHE B 2 203 ? 24.237 15.070 40.475 1.00 118.01 ? 203 PHE B O 1 ATOM 8779 C CB . PHE B 2 203 ? 22.061 12.532 40.105 1.00 127.01 ? 203 PHE B CB 1 ATOM 8780 C CG . PHE B 2 203 ? 21.121 13.691 40.279 1.00 118.98 ? 203 PHE B CG 1 ATOM 8781 C CD1 . PHE B 2 203 ? 20.382 14.166 39.208 1.00 107.57 ? 203 PHE B CD1 1 ATOM 8782 C CD2 . PHE B 2 203 ? 20.968 14.299 41.513 1.00 111.66 ? 203 PHE B CD2 1 ATOM 8783 C CE1 . PHE B 2 203 ? 19.514 15.228 39.366 1.00 102.47 ? 203 PHE B CE1 1 ATOM 8784 C CE2 . PHE B 2 203 ? 20.102 15.360 41.676 1.00 106.60 ? 203 PHE B CE2 1 ATOM 8785 C CZ . PHE B 2 203 ? 19.374 15.826 40.602 1.00 101.99 ? 203 PHE B CZ 1 ATOM 8786 N N . ASN B 2 204 ? 24.414 13.325 41.887 1.00 142.27 ? 204 ASN B N 1 ATOM 8787 C CA . ASN B 2 204 ? 24.977 14.115 42.978 1.00 139.98 ? 204 ASN B CA 1 ATOM 8788 C C . ASN B 2 204 ? 26.310 14.761 42.608 1.00 143.79 ? 204 ASN B C 1 ATOM 8789 O O . ASN B 2 204 ? 26.601 15.883 43.021 1.00 144.21 ? 204 ASN B O 1 ATOM 8790 C CB . ASN B 2 204 ? 25.157 13.247 44.226 1.00 132.99 ? 204 ASN B CB 1 ATOM 8791 C CG . ASN B 2 204 ? 23.853 12.646 44.713 1.00 134.53 ? 204 ASN B CG 1 ATOM 8792 O OD1 . ASN B 2 204 ? 23.778 11.452 45.003 1.00 143.65 ? 204 ASN B OD1 1 ATOM 8793 N ND2 . ASN B 2 204 ? 22.817 13.472 44.805 1.00 135.76 ? 204 ASN B ND2 1 ATOM 8794 N N . GLU B 2 205 ? 27.112 14.045 41.826 1.00 142.36 ? 205 GLU B N 1 ATOM 8795 C CA . GLU B 2 205 ? 28.429 14.529 41.420 1.00 146.37 ? 205 GLU B CA 1 ATOM 8796 C C . GLU B 2 205 ? 28.327 15.594 40.329 1.00 141.75 ? 205 GLU B C 1 ATOM 8797 O O . GLU B 2 205 ? 29.312 16.258 40.004 1.00 149.91 ? 205 GLU B O 1 ATOM 8798 C CB . GLU B 2 205 ? 29.297 13.363 40.943 1.00 144.23 ? 205 GLU B CB 1 ATOM 8799 C CG . GLU B 2 205 ? 29.521 12.290 41.999 1.00 153.51 ? 205 GLU B CG 1 ATOM 8800 C CD . GLU B 2 205 ? 30.291 11.096 41.469 1.00 177.21 ? 205 GLU B CD 1 ATOM 8801 O OE1 . GLU B 2 205 ? 30.529 10.147 42.247 1.00 180.91 ? 205 GLU B OE1 1 ATOM 8802 O OE2 . GLU B 2 205 ? 30.658 11.105 40.274 1.00 186.37 ? 205 GLU B OE2 1 ATOM 8803 N N . GLU B 2 206 ? 27.132 15.749 39.769 1.00 125.94 ? 206 GLU B N 1 ATOM 8804 C CA . GLU B 2 206 ? 26.874 16.782 38.772 1.00 140.91 ? 206 GLU B CA 1 ATOM 8805 C C . GLU B 2 206 ? 26.453 18.081 39.449 1.00 135.56 ? 206 GLU B C 1 ATOM 8806 O O . GLU B 2 206 ? 27.112 19.109 39.301 1.00 140.54 ? 206 GLU B O 1 ATOM 8807 C CB . GLU B 2 206 ? 25.800 16.329 37.778 1.00 135.21 ? 206 GLU B CB 1 ATOM 8808 C CG . GLU B 2 206 ? 26.254 15.241 36.819 1.00 151.71 ? 206 GLU B CG 1 ATOM 8809 C CD . GLU B 2 206 ? 27.436 15.664 35.968 1.00 149.84 ? 206 GLU B CD 1 ATOM 8810 O OE1 . GLU B 2 206 ? 28.279 14.798 35.649 1.00 134.91 ? 206 GLU B OE1 1 ATOM 8811 O OE2 . GLU B 2 206 ? 27.521 16.858 35.611 1.00 154.37 ? 206 GLU B OE2 1 ATOM 8812 N N . VAL B 2 207 ? 25.338 18.019 40.172 1.00 127.54 ? 207 VAL B N 1 ATOM 8813 C CA . VAL B 2 207 ? 24.784 19.165 40.891 1.00 114.84 ? 207 VAL B CA 1 ATOM 8814 C C . VAL B 2 207 ? 25.824 19.897 41.744 1.00 120.86 ? 207 VAL B C 1 ATOM 8815 O O . VAL B 2 207 ? 25.811 21.126 41.832 1.00 119.77 ? 207 VAL B O 1 ATOM 8816 C CB . VAL B 2 207 ? 23.619 18.729 41.797 1.00 125.38 ? 207 VAL B CB 1 ATOM 8817 C CG1 . VAL B 2 207 ? 22.975 19.934 42.445 1.00 114.14 ? 207 VAL B CG1 1 ATOM 8818 C CG2 . VAL B 2 207 ? 22.592 17.947 40.997 1.00 129.88 ? 207 VAL B CG2 1 ATOM 8819 N N . LYS B 2 208 ? 26.720 19.137 42.365 1.00 137.84 ? 208 LYS B N 1 ATOM 8820 C CA . LYS B 2 208 ? 27.790 19.706 43.180 1.00 128.21 ? 208 LYS B CA 1 ATOM 8821 C C . LYS B 2 208 ? 28.671 20.661 42.371 1.00 124.90 ? 208 LYS B C 1 ATOM 8822 O O . LYS B 2 208 ? 29.158 21.665 42.892 1.00 132.19 ? 208 LYS B O 1 ATOM 8823 C CB . LYS B 2 208 ? 28.643 18.589 43.786 1.00 132.44 ? 208 LYS B CB 1 ATOM 8824 C CG . LYS B 2 208 ? 29.805 19.072 44.641 1.00 157.45 ? 208 LYS B CG 1 ATOM 8825 C CD . LYS B 2 208 ? 29.320 19.847 45.856 1.00 163.96 ? 208 LYS B CD 1 ATOM 8826 C CE . LYS B 2 208 ? 30.484 20.291 46.728 1.00 157.02 ? 208 LYS B CE 1 ATOM 8827 N NZ . LYS B 2 208 ? 30.023 21.047 47.925 1.00 148.21 ? 208 LYS B NZ 1 ATOM 8828 N N . LYS B 2 209 ? 28.862 20.344 41.094 1.00 123.79 ? 209 LYS B N 1 ATOM 8829 C CA . LYS B 2 209 ? 29.689 21.159 40.211 1.00 128.78 ? 209 LYS B CA 1 ATOM 8830 C C . LYS B 2 209 ? 29.027 22.489 39.857 1.00 125.35 ? 209 LYS B C 1 ATOM 8831 O O . LYS B 2 209 ? 29.707 23.452 39.505 1.00 139.68 ? 209 LYS B O 1 ATOM 8832 C CB . LYS B 2 209 ? 30.013 20.393 38.925 1.00 124.86 ? 209 LYS B CB 1 ATOM 8833 C CG . LYS B 2 209 ? 30.812 19.116 39.131 1.00 137.64 ? 209 LYS B CG 1 ATOM 8834 C CD . LYS B 2 209 ? 30.941 18.337 37.830 1.00 138.99 ? 209 LYS B CD 1 ATOM 8835 C CE . LYS B 2 209 ? 31.574 19.181 36.733 1.00 139.06 ? 209 LYS B CE 1 ATOM 8836 N NZ . LYS B 2 209 ? 32.960 19.604 37.077 1.00 160.99 ? 209 LYS B NZ 1 ATOM 8837 N N . GLN B 2 210 ? 27.701 22.534 39.948 1.00 116.67 ? 210 GLN B N 1 ATOM 8838 C CA . GLN B 2 210 ? 26.938 23.709 39.532 1.00 117.23 ? 210 GLN B CA 1 ATOM 8839 C C . GLN B 2 210 ? 27.277 24.942 40.361 1.00 117.97 ? 210 GLN B C 1 ATOM 8840 O O . GLN B 2 210 ? 27.415 24.866 41.582 1.00 115.35 ? 210 GLN B O 1 ATOM 8841 C CB . GLN B 2 210 ? 25.437 23.424 39.612 1.00 111.00 ? 210 GLN B CB 1 ATOM 8842 C CG . GLN B 2 210 ? 24.987 22.264 38.743 1.00 113.07 ? 210 GLN B CG 1 ATOM 8843 C CD . GLN B 2 210 ? 25.337 22.464 37.282 1.00 113.41 ? 210 GLN B CD 1 ATOM 8844 O OE1 . GLN B 2 210 ? 25.118 23.537 36.719 1.00 110.47 ? 210 GLN B OE1 1 ATOM 8845 N NE2 . GLN B 2 210 ? 25.892 21.430 36.661 1.00 110.84 ? 210 GLN B NE2 1 ATOM 8846 N N . SER B 2 211 ? 27.409 26.079 39.685 1.00 118.93 ? 211 SER B N 1 ATOM 8847 C CA . SER B 2 211 ? 27.768 27.328 40.345 1.00 120.32 ? 211 SER B CA 1 ATOM 8848 C C . SER B 2 211 ? 26.798 28.449 39.980 1.00 117.76 ? 211 SER B C 1 ATOM 8849 O O . SER B 2 211 ? 26.015 28.324 39.038 1.00 111.82 ? 211 SER B O 1 ATOM 8850 C CB . SER B 2 211 ? 29.199 27.729 39.984 1.00 121.69 ? 211 SER B CB 1 ATOM 8851 O OG . SER B 2 211 ? 30.123 26.737 40.403 1.00 146.24 ? 211 SER B OG 1 ATOM 8852 N N . VAL B 2 212 ? 26.853 29.538 40.739 1.00 134.83 ? 212 VAL B N 1 ATOM 8853 C CA . VAL B 2 212 ? 25.926 30.648 40.561 1.00 112.55 ? 212 VAL B CA 1 ATOM 8854 C C . VAL B 2 212 ? 26.362 31.599 39.446 1.00 107.76 ? 212 VAL B C 1 ATOM 8855 O O . VAL B 2 212 ? 27.555 31.825 39.242 1.00 119.90 ? 212 VAL B O 1 ATOM 8856 C CB . VAL B 2 212 ? 25.771 31.452 41.866 1.00 119.34 ? 212 VAL B CB 1 ATOM 8857 C CG1 . VAL B 2 212 ? 24.370 32.018 41.973 1.00 111.50 ? 212 VAL B CG1 1 ATOM 8858 C CG2 . VAL B 2 212 ? 26.075 30.573 43.068 1.00 149.19 ? 212 VAL B CG2 1 ATOM 8859 N N . SER B 2 213 ? 25.386 32.149 38.730 1.00 103.54 ? 213 SER B N 1 ATOM 8860 C CA . SER B 2 213 ? 25.646 33.152 37.701 1.00 99.91 ? 213 SER B CA 1 ATOM 8861 C C . SER B 2 213 ? 24.948 34.458 38.069 1.00 100.59 ? 213 SER B C 1 ATOM 8862 O O . SER B 2 213 ? 24.333 34.552 39.127 1.00 110.25 ? 213 SER B O 1 ATOM 8863 C CB . SER B 2 213 ? 25.180 32.660 36.331 1.00 97.27 ? 213 SER B CB 1 ATOM 8864 O OG . SER B 2 213 ? 25.586 33.551 35.307 1.00 94.79 ? 213 SER B OG 1 ATOM 8865 N N . ARG B 2 214 ? 25.040 35.466 37.205 1.00 96.48 ? 214 ARG B N 1 ATOM 8866 C CA . ARG B 2 214 ? 24.438 36.764 37.509 1.00 91.44 ? 214 ARG B CA 1 ATOM 8867 C C . ARG B 2 214 ? 23.831 37.462 36.291 1.00 86.69 ? 214 ARG B C 1 ATOM 8868 O O . ARG B 2 214 ? 24.445 37.522 35.225 1.00 95.29 ? 214 ARG B O 1 ATOM 8869 C CB . ARG B 2 214 ? 25.480 37.685 38.150 1.00 102.00 ? 214 ARG B CB 1 ATOM 8870 C CG . ARG B 2 214 ? 24.941 39.047 38.569 1.00 95.70 ? 214 ARG B CG 1 ATOM 8871 C CD . ARG B 2 214 ? 26.075 40.010 38.891 1.00 95.08 ? 214 ARG B CD 1 ATOM 8872 N NE . ARG B 2 214 ? 25.591 41.270 39.450 1.00 94.94 ? 214 ARG B NE 1 ATOM 8873 C CZ . ARG B 2 214 ? 26.372 42.307 39.736 1.00 107.25 ? 214 ARG B CZ 1 ATOM 8874 N NH1 . ARG B 2 214 ? 27.677 42.238 39.511 1.00 121.20 ? 214 ARG B NH1 1 ATOM 8875 N NH2 . ARG B 2 214 ? 25.850 43.415 40.245 1.00 123.50 ? 214 ARG B NH2 1 ATOM 8876 N N . ASN B 2 215 ? 22.622 37.993 36.466 1.00 83.32 ? 215 ASN B N 1 ATOM 8877 C CA . ASN B 2 215 ? 22.021 38.899 35.492 1.00 79.39 ? 215 ASN B CA 1 ATOM 8878 C C . ASN B 2 215 ? 21.583 40.176 36.202 1.00 78.56 ? 215 ASN B C 1 ATOM 8879 O O . ASN B 2 215 ? 21.719 40.284 37.419 1.00 81.10 ? 215 ASN B O 1 ATOM 8880 C CB . ASN B 2 215 ? 20.838 38.240 34.773 1.00 76.35 ? 215 ASN B CB 1 ATOM 8881 C CG . ASN B 2 215 ? 19.605 38.122 35.651 1.00 77.72 ? 215 ASN B CG 1 ATOM 8882 O OD1 . ASN B 2 215 ? 18.541 38.649 35.320 1.00 79.31 ? 215 ASN B OD1 1 ATOM 8883 N ND2 . ASN B 2 215 ? 19.740 37.420 36.770 1.00 81.31 ? 215 ASN B ND2 1 ATOM 8884 N N . ARG B 2 216 ? 21.076 41.150 35.454 1.00 75.11 ? 216 ARG B N 1 ATOM 8885 C CA . ARG B 2 216 ? 20.742 42.442 36.054 1.00 73.33 ? 216 ARG B CA 1 ATOM 8886 C C . ARG B 2 216 ? 19.372 42.519 36.733 1.00 71.51 ? 216 ARG B C 1 ATOM 8887 O O . ARG B 2 216 ? 19.256 43.068 37.828 1.00 79.63 ? 216 ARG B O 1 ATOM 8888 C CB . ARG B 2 216 ? 20.841 43.551 35.007 1.00 77.43 ? 216 ARG B CB 1 ATOM 8889 C CG . ARG B 2 216 ? 20.609 44.932 35.591 1.00 74.91 ? 216 ARG B CG 1 ATOM 8890 C CD . ARG B 2 216 ? 21.043 46.026 34.643 1.00 77.80 ? 216 ARG B CD 1 ATOM 8891 N NE . ARG B 2 216 ? 22.491 46.215 34.632 1.00 95.29 ? 216 ARG B NE 1 ATOM 8892 C CZ . ARG B 2 216 ? 23.304 45.727 33.702 1.00 92.75 ? 216 ARG B CZ 1 ATOM 8893 N NH1 . ARG B 2 216 ? 22.814 45.017 32.696 1.00 74.05 ? 216 ARG B NH1 1 ATOM 8894 N NH2 . ARG B 2 216 ? 24.607 45.961 33.771 1.00 83.52 ? 216 ARG B NH2 1 ATOM 8895 N N . ASP B 2 217 ? 18.339 41.973 36.097 1.00 72.71 ? 217 ASP B N 1 ATOM 8896 C CA . ASP B 2 217 ? 16.970 42.217 36.559 1.00 68.81 ? 217 ASP B CA 1 ATOM 8897 C C . ASP B 2 217 ? 16.348 41.029 37.292 1.00 70.78 ? 217 ASP B C 1 ATOM 8898 O O . ASP B 2 217 ? 16.571 39.870 36.932 1.00 81.84 ? 217 ASP B O 1 ATOM 8899 C CB . ASP B 2 217 ? 16.080 42.623 35.383 1.00 68.69 ? 217 ASP B CB 1 ATOM 8900 C CG . ASP B 2 217 ? 15.785 41.471 34.447 1.00 96.74 ? 217 ASP B CG 1 ATOM 8901 O OD1 . ASP B 2 217 ? 16.549 40.482 34.448 1.00 127.04 ? 217 ASP B OD1 1 ATOM 8902 O OD2 . ASP B 2 217 ? 14.786 41.555 33.703 1.00 96.45 ? 217 ASP B OD2 1 ATOM 8903 N N . ALA B 2 218 ? 15.548 41.344 38.309 1.00 74.35 ? 218 ALA B N 1 ATOM 8904 C CA . ALA B 2 218 ? 15.016 40.352 39.242 1.00 83.27 ? 218 ALA B CA 1 ATOM 8905 C C . ALA B 2 218 ? 14.170 39.239 38.604 1.00 78.04 ? 218 ALA B C 1 ATOM 8906 O O . ALA B 2 218 ? 14.385 38.068 38.916 1.00 85.95 ? 218 ALA B O 1 ATOM 8907 C CB . ALA B 2 218 ? 14.213 41.052 40.341 1.00 69.73 ? 218 ALA B CB 1 ATOM 8908 N N . PRO B 2 219 ? 13.191 39.582 37.740 1.00 62.48 ? 219 PRO B N 1 ATOM 8909 C CA . PRO B 2 219 ? 12.507 38.450 37.104 1.00 73.20 ? 219 PRO B CA 1 ATOM 8910 C C . PRO B 2 219 ? 13.478 37.651 36.240 1.00 78.53 ? 219 PRO B C 1 ATOM 8911 O O . PRO B 2 219 ? 14.171 38.228 35.403 1.00 66.92 ? 219 PRO B O 1 ATOM 8912 C CB . PRO B 2 219 ? 11.416 39.117 36.260 1.00 84.82 ? 219 PRO B CB 1 ATOM 8913 C CG . PRO B 2 219 ? 11.862 40.525 36.087 1.00 80.13 ? 219 PRO B CG 1 ATOM 8914 C CD . PRO B 2 219 ? 12.622 40.874 37.321 1.00 79.00 ? 219 PRO B CD 1 ATOM 8915 N N . GLU B 2 220 ? 13.536 36.341 36.458 1.00 77.66 ? 220 GLU B N 1 ATOM 8916 C CA . GLU B 2 220 ? 14.579 35.528 35.842 1.00 78.46 ? 220 GLU B CA 1 ATOM 8917 C C . GLU B 2 220 ? 14.160 34.770 34.581 1.00 75.85 ? 220 GLU B C 1 ATOM 8918 O O . GLU B 2 220 ? 14.993 34.143 33.933 1.00 91.01 ? 220 GLU B O 1 ATOM 8919 C CB . GLU B 2 220 ? 15.129 34.544 36.878 1.00 70.40 ? 220 GLU B CB 1 ATOM 8920 C CG . GLU B 2 220 ? 16.574 34.813 37.284 1.00 74.06 ? 220 GLU B CG 1 ATOM 8921 C CD . GLU B 2 220 ? 16.854 36.276 37.587 1.00 86.32 ? 220 GLU B CD 1 ATOM 8922 O OE1 . GLU B 2 220 ? 16.783 36.658 38.772 1.00 95.79 ? 220 GLU B OE1 1 ATOM 8923 O OE2 . GLU B 2 220 ? 17.161 37.042 36.645 1.00 102.36 ? 220 GLU B OE2 1 ATOM 8924 N N . GLY B 2 221 ? 12.885 34.845 34.217 1.00 66.92 ? 221 GLY B N 1 ATOM 8925 C CA . GLY B 2 221 ? 12.412 34.195 33.006 1.00 105.67 ? 221 GLY B CA 1 ATOM 8926 C C . GLY B 2 221 ? 12.691 32.703 32.937 1.00 105.18 ? 221 GLY B C 1 ATOM 8927 O O . GLY B 2 221 ? 13.318 32.223 31.992 1.00 64.23 ? 221 GLY B O 1 ATOM 8928 N N . GLY B 2 222 ? 12.230 31.964 33.941 1.00 94.67 ? 222 GLY B N 1 ATOM 8929 C CA . GLY B 2 222 ? 12.429 30.527 33.972 1.00 83.43 ? 222 GLY B CA 1 ATOM 8930 C C . GLY B 2 222 ? 11.430 29.795 33.099 1.00 91.53 ? 222 GLY B C 1 ATOM 8931 O O . GLY B 2 222 ? 11.547 28.590 32.877 1.00 91.67 ? 222 GLY B O 1 ATOM 8932 N N . PHE B 2 223 ? 10.443 30.535 32.604 1.00 95.29 ? 223 PHE B N 1 ATOM 8933 C CA . PHE B 2 223 ? 9.391 29.970 31.768 1.00 75.69 ? 223 PHE B CA 1 ATOM 8934 C C . PHE B 2 223 ? 9.930 29.466 30.432 1.00 67.05 ? 223 PHE B C 1 ATOM 8935 O O . PHE B 2 223 ? 9.354 28.563 29.827 1.00 68.91 ? 223 PHE B O 1 ATOM 8936 C CB . PHE B 2 223 ? 8.286 31.002 31.536 1.00 86.86 ? 223 PHE B CB 1 ATOM 8937 C CG . PHE B 2 223 ? 7.392 31.210 32.727 1.00 80.01 ? 223 PHE B CG 1 ATOM 8938 C CD1 . PHE B 2 223 ? 7.506 30.397 33.844 1.00 74.74 ? 223 PHE B CD1 1 ATOM 8939 C CD2 . PHE B 2 223 ? 6.430 32.206 32.725 1.00 64.21 ? 223 PHE B CD2 1 ATOM 8940 C CE1 . PHE B 2 223 ? 6.685 30.581 34.940 1.00 69.31 ? 223 PHE B CE1 1 ATOM 8941 C CE2 . PHE B 2 223 ? 5.605 32.394 33.818 1.00 57.42 ? 223 PHE B CE2 1 ATOM 8942 C CZ . PHE B 2 223 ? 5.733 31.580 34.927 1.00 61.92 ? 223 PHE B CZ 1 ATOM 8943 N N . ASP B 2 224 ? 11.031 30.055 29.974 1.00 62.90 ? 224 ASP B N 1 ATOM 8944 C CA . ASP B 2 224 ? 11.715 29.565 28.783 1.00 70.50 ? 224 ASP B CA 1 ATOM 8945 C C . ASP B 2 224 ? 12.205 28.139 29.008 1.00 88.83 ? 224 ASP B C 1 ATOM 8946 O O . ASP B 2 224 ? 12.090 27.282 28.131 1.00 80.72 ? 224 ASP B O 1 ATOM 8947 C CB . ASP B 2 224 ? 12.891 30.473 28.411 1.00 80.99 ? 224 ASP B CB 1 ATOM 8948 C CG . ASP B 2 224 ? 12.480 31.628 27.517 1.00 79.52 ? 224 ASP B CG 1 ATOM 8949 O OD1 . ASP B 2 224 ? 11.471 31.496 26.795 1.00 65.45 ? 224 ASP B OD1 1 ATOM 8950 O OD2 . ASP B 2 224 ? 13.178 32.664 27.527 1.00 102.27 ? 224 ASP B OD2 1 ATOM 8951 N N . ALA B 2 225 ? 12.748 27.899 30.198 1.00 90.88 ? 225 ALA B N 1 ATOM 8952 C CA . ALA B 2 225 ? 13.276 26.590 30.563 1.00 88.91 ? 225 ALA B CA 1 ATOM 8953 C C . ALA B 2 225 ? 12.167 25.550 30.675 1.00 75.32 ? 225 ALA B C 1 ATOM 8954 O O . ALA B 2 225 ? 12.327 24.415 30.228 1.00 88.84 ? 225 ALA B O 1 ATOM 8955 C CB . ALA B 2 225 ? 14.048 26.682 31.870 1.00 93.33 ? 225 ALA B CB 1 ATOM 8956 N N . ILE B 2 226 ? 11.047 25.945 31.276 1.00 64.83 ? 226 ILE B N 1 ATOM 8957 C CA . ILE B 2 226 ? 9.892 25.064 31.424 1.00 67.92 ? 226 ILE B CA 1 ATOM 8958 C C . ILE B 2 226 ? 9.381 24.602 30.063 1.00 81.78 ? 226 ILE B C 1 ATOM 8959 O O . ILE B 2 226 ? 9.038 23.432 29.879 1.00 104.13 ? 226 ILE B O 1 ATOM 8960 C CB . ILE B 2 226 ? 8.749 25.760 32.197 1.00 62.94 ? 226 ILE B CB 1 ATOM 8961 C CG1 . ILE B 2 226 ? 9.124 25.921 33.671 1.00 62.93 ? 226 ILE B CG1 1 ATOM 8962 C CG2 . ILE B 2 226 ? 7.455 24.973 32.081 1.00 64.84 ? 226 ILE B CG2 1 ATOM 8963 C CD1 . ILE B 2 226 ? 8.011 26.491 34.527 1.00 62.76 ? 226 ILE B CD1 1 ATOM 8964 N N . MET B 2 227 ? 9.349 25.526 29.109 1.00 67.34 ? 227 MET B N 1 ATOM 8965 C CA . MET B 2 227 ? 8.894 25.226 27.757 1.00 73.30 ? 227 MET B CA 1 ATOM 8966 C C . MET B 2 227 ? 9.776 24.180 27.080 1.00 77.59 ? 227 MET B C 1 ATOM 8967 O O . MET B 2 227 ? 9.282 23.170 26.581 1.00 92.11 ? 227 MET B O 1 ATOM 8968 C CB . MET B 2 227 ? 8.856 26.502 26.913 1.00 90.06 ? 227 MET B CB 1 ATOM 8969 C CG . MET B 2 227 ? 8.496 26.269 25.457 1.00 91.23 ? 227 MET B CG 1 ATOM 8970 S SD . MET B 2 227 ? 6.879 25.500 25.259 1.00 84.33 ? 227 MET B SD 1 ATOM 8971 C CE . MET B 2 227 ? 5.823 26.737 26.007 1.00 66.57 ? 227 MET B CE 1 ATOM 8972 N N . GLN B 2 228 ? 11.083 24.426 27.077 1.00 79.24 ? 228 GLN B N 1 ATOM 8973 C CA . GLN B 2 228 ? 12.028 23.553 26.389 1.00 80.97 ? 228 GLN B CA 1 ATOM 8974 C C . GLN B 2 228 ? 12.143 22.176 27.039 1.00 91.52 ? 228 GLN B C 1 ATOM 8975 O O . GLN B 2 228 ? 12.330 21.173 26.349 1.00 78.48 ? 228 GLN B O 1 ATOM 8976 C CB . GLN B 2 228 ? 13.404 24.216 26.324 1.00 76.44 ? 228 GLN B CB 1 ATOM 8977 C CG . GLN B 2 228 ? 13.428 25.478 25.476 1.00 76.60 ? 228 GLN B CG 1 ATOM 8978 C CD . GLN B 2 228 ? 12.899 25.245 24.071 1.00 82.82 ? 228 GLN B CD 1 ATOM 8979 O OE1 . GLN B 2 228 ? 13.202 24.231 23.441 1.00 81.04 ? 228 GLN B OE1 1 ATOM 8980 N NE2 . GLN B 2 228 ? 12.100 26.184 23.577 1.00 93.85 ? 228 GLN B NE2 1 ATOM 8981 N N . ALA B 2 229 ? 12.030 22.128 28.362 1.00 88.18 ? 229 ALA B N 1 ATOM 8982 C CA . ALA B 2 229 ? 12.089 20.860 29.081 1.00 77.93 ? 229 ALA B CA 1 ATOM 8983 C C . ALA B 2 229 ? 10.867 20.005 28.759 1.00 89.98 ? 229 ALA B C 1 ATOM 8984 O O . ALA B 2 229 ? 10.879 18.788 28.942 1.00 103.16 ? 229 ALA B O 1 ATOM 8985 C CB . ALA B 2 229 ? 12.193 21.101 30.578 1.00 73.62 ? 229 ALA B CB 1 ATOM 8986 N N . THR B 2 230 ? 9.816 20.657 28.275 1.00 89.37 ? 230 THR B N 1 ATOM 8987 C CA . THR B 2 230 ? 8.574 19.982 27.921 1.00 88.11 ? 230 THR B CA 1 ATOM 8988 C C . THR B 2 230 ? 8.595 19.503 26.470 1.00 85.77 ? 230 THR B C 1 ATOM 8989 O O . THR B 2 230 ? 8.523 18.304 26.200 1.00 94.71 ? 230 THR B O 1 ATOM 8990 C CB . THR B 2 230 ? 7.357 20.902 28.138 1.00 92.38 ? 230 THR B CB 1 ATOM 8991 O OG1 . THR B 2 230 ? 7.317 21.334 29.504 1.00 74.93 ? 230 THR B OG1 1 ATOM 8992 C CG2 . THR B 2 230 ? 6.067 20.172 27.805 1.00 95.44 ? 230 THR B CG2 1 ATOM 8993 N N . VAL B 2 231 ? 8.693 20.452 25.544 1.00 89.65 ? 231 VAL B N 1 ATOM 8994 C CA . VAL B 2 231 ? 8.585 20.165 24.117 1.00 95.52 ? 231 VAL B CA 1 ATOM 8995 C C . VAL B 2 231 ? 9.735 19.331 23.555 1.00 91.01 ? 231 VAL B C 1 ATOM 8996 O O . VAL B 2 231 ? 9.611 18.752 22.476 1.00 116.34 ? 231 VAL B O 1 ATOM 8997 C CB . VAL B 2 231 ? 8.492 21.466 23.299 1.00 103.07 ? 231 VAL B CB 1 ATOM 8998 C CG1 . VAL B 2 231 ? 7.246 22.242 23.689 1.00 100.74 ? 231 VAL B CG1 1 ATOM 8999 C CG2 . VAL B 2 231 ? 9.742 22.310 23.503 1.00 96.57 ? 231 VAL B CG2 1 ATOM 9000 N N . CYS B 2 232 ? 10.853 19.260 24.273 1.00 83.37 ? 232 CYS B N 1 ATOM 9001 C CA . CYS B 2 232 ? 11.954 18.419 23.820 1.00 99.38 ? 232 CYS B CA 1 ATOM 9002 C C . CYS B 2 232 ? 11.951 17.116 24.606 1.00 110.57 ? 232 CYS B C 1 ATOM 9003 O O . CYS B 2 232 ? 12.320 17.079 25.779 1.00 129.79 ? 232 CYS B O 1 ATOM 9004 C CB . CYS B 2 232 ? 13.294 19.142 23.975 1.00 121.24 ? 232 CYS B CB 1 ATOM 9005 S SG . CYS B 2 232 ? 13.430 20.688 23.041 1.00 92.89 ? 232 CYS B SG 1 ATOM 9006 N N . ASP B 2 233 ? 11.529 16.047 23.939 1.00 105.82 ? 233 ASP B N 1 ATOM 9007 C CA . ASP B 2 233 ? 11.395 14.740 24.568 1.00 107.56 ? 233 ASP B CA 1 ATOM 9008 C C . ASP B 2 233 ? 12.710 13.963 24.614 1.00 117.89 ? 233 ASP B C 1 ATOM 9009 O O . ASP B 2 233 ? 13.042 13.346 25.626 1.00 128.19 ? 233 ASP B O 1 ATOM 9010 C CB . ASP B 2 233 ? 10.329 13.919 23.837 1.00 126.74 ? 233 ASP B CB 1 ATOM 9011 C CG . ASP B 2 233 ? 9.024 14.678 23.669 1.00 130.72 ? 233 ASP B CG 1 ATOM 9012 O OD1 . ASP B 2 233 ? 8.721 15.543 24.517 1.00 98.82 ? 233 ASP B OD1 1 ATOM 9013 O OD2 . ASP B 2 233 ? 8.299 14.408 22.688 1.00 155.05 ? 233 ASP B OD2 1 ATOM 9014 N N . GLU B 2 234 ? 13.455 13.998 23.514 1.00 126.74 ? 234 GLU B N 1 ATOM 9015 C CA . GLU B 2 234 ? 14.658 13.179 23.371 1.00 124.02 ? 234 GLU B CA 1 ATOM 9016 C C . GLU B 2 234 ? 15.818 13.697 24.217 1.00 127.08 ? 234 GLU B C 1 ATOM 9017 O O . GLU B 2 234 ? 16.620 12.913 24.724 1.00 140.59 ? 234 GLU B O 1 ATOM 9018 C CB . GLU B 2 234 ? 15.079 13.094 21.896 1.00 128.33 ? 234 GLU B CB 1 ATOM 9019 C CG . GLU B 2 234 ? 15.557 14.403 21.272 1.00 157.17 ? 234 GLU B CG 1 ATOM 9020 C CD . GLU B 2 234 ? 14.439 15.410 21.074 1.00 155.76 ? 234 GLU B CD 1 ATOM 9021 O OE1 . GLU B 2 234 ? 13.262 14.994 21.048 1.00 169.55 ? 234 GLU B OE1 1 ATOM 9022 O OE2 . GLU B 2 234 ? 14.737 16.616 20.950 1.00 121.15 ? 234 GLU B OE2 1 ATOM 9023 N N . LYS B 2 235 ? 15.905 15.015 24.367 1.00 114.49 ? 235 LYS B N 1 ATOM 9024 C CA . LYS B 2 235 ? 16.963 15.624 25.165 1.00 111.13 ? 235 LYS B CA 1 ATOM 9025 C C . LYS B 2 235 ? 16.766 15.329 26.645 1.00 105.33 ? 235 LYS B C 1 ATOM 9026 O O . LYS B 2 235 ? 17.678 14.849 27.320 1.00 108.64 ? 235 LYS B O 1 ATOM 9027 C CB . LYS B 2 235 ? 17.011 17.135 24.934 1.00 109.40 ? 235 LYS B CB 1 ATOM 9028 C CG . LYS B 2 235 ? 17.646 17.541 23.616 1.00 111.14 ? 235 LYS B CG 1 ATOM 9029 C CD . LYS B 2 235 ? 19.123 17.189 23.592 1.00 115.45 ? 235 LYS B CD 1 ATOM 9030 C CE . LYS B 2 235 ? 19.761 17.572 22.268 1.00 120.00 ? 235 LYS B CE 1 ATOM 9031 N NZ . LYS B 2 235 ? 21.215 17.254 22.248 1.00 124.97 ? 235 LYS B NZ 1 ATOM 9032 N N . ILE B 2 236 ? 15.570 15.621 27.143 1.00 100.86 ? 236 ILE B N 1 ATOM 9033 C CA . ILE B 2 236 ? 15.249 15.384 28.543 1.00 103.51 ? 236 ILE B CA 1 ATOM 9034 C C . ILE B 2 236 ? 15.208 13.888 28.838 1.00 106.78 ? 236 ILE B C 1 ATOM 9035 O O . ILE B 2 236 ? 15.710 13.438 29.867 1.00 106.78 ? 236 ILE B O 1 ATOM 9036 C CB . ILE B 2 236 ? 13.906 16.025 28.932 1.00 103.46 ? 236 ILE B CB 1 ATOM 9037 C CG1 . ILE B 2 236 ? 13.896 17.508 28.557 1.00 93.01 ? 236 ILE B CG1 1 ATOM 9038 C CG2 . ILE B 2 236 ? 13.637 15.840 30.417 1.00 97.43 ? 236 ILE B CG2 1 ATOM 9039 C CD1 . ILE B 2 236 ? 15.038 18.302 29.153 1.00 100.35 ? 236 ILE B CD1 1 ATOM 9040 N N . GLY B 2 237 ? 14.631 13.117 27.921 1.00 99.84 ? 237 GLY B N 1 ATOM 9041 C CA . GLY B 2 237 ? 14.556 11.677 28.087 1.00 115.98 ? 237 GLY B CA 1 ATOM 9042 C C . GLY B 2 237 ? 13.294 11.182 28.769 1.00 131.80 ? 237 GLY B C 1 ATOM 9043 O O . GLY B 2 237 ? 13.306 10.124 29.399 1.00 138.81 ? 237 GLY B O 1 ATOM 9044 N N . TRP B 2 238 ? 12.215 11.956 28.665 1.00 131.63 ? 238 TRP B N 1 ATOM 9045 C CA . TRP B 2 238 ? 10.928 11.570 29.240 1.00 101.04 ? 238 TRP B CA 1 ATOM 9046 C C . TRP B 2 238 ? 10.496 10.185 28.764 1.00 106.30 ? 238 TRP B C 1 ATOM 9047 O O . TRP B 2 238 ? 10.621 9.858 27.584 1.00 109.14 ? 238 TRP B O 1 ATOM 9048 C CB . TRP B 2 238 ? 9.841 12.591 28.886 1.00 101.10 ? 238 TRP B CB 1 ATOM 9049 C CG . TRP B 2 238 ? 10.025 13.951 29.492 1.00 103.20 ? 238 TRP B CG 1 ATOM 9050 C CD1 . TRP B 2 238 ? 10.345 15.103 28.835 1.00 95.90 ? 238 TRP B CD1 1 ATOM 9051 C CD2 . TRP B 2 238 ? 9.886 14.303 30.875 1.00 101.34 ? 238 TRP B CD2 1 ATOM 9052 N NE1 . TRP B 2 238 ? 10.416 16.150 29.722 1.00 90.13 ? 238 TRP B NE1 1 ATOM 9053 C CE2 . TRP B 2 238 ? 10.141 15.685 30.982 1.00 87.39 ? 238 TRP B CE2 1 ATOM 9054 C CE3 . TRP B 2 238 ? 9.576 13.584 32.034 1.00 109.36 ? 238 TRP B CE3 1 ATOM 9055 C CZ2 . TRP B 2 238 ? 10.094 16.362 32.199 1.00 84.68 ? 238 TRP B CZ2 1 ATOM 9056 C CZ3 . TRP B 2 238 ? 9.528 14.259 33.241 1.00 89.96 ? 238 TRP B CZ3 1 ATOM 9057 C CH2 . TRP B 2 238 ? 9.787 15.633 33.314 1.00 85.93 ? 238 TRP B CH2 1 ATOM 9058 N N . ARG B 2 239 ? 9.992 9.376 29.690 1.00 116.35 ? 239 ARG B N 1 ATOM 9059 C CA . ARG B 2 239 ? 9.503 8.044 29.356 1.00 118.98 ? 239 ARG B CA 1 ATOM 9060 C C . ARG B 2 239 ? 7.983 8.017 29.293 1.00 113.81 ? 239 ARG B C 1 ATOM 9061 O O . ARG B 2 239 ? 7.309 8.465 30.220 1.00 111.41 ? 239 ARG B O 1 ATOM 9062 C CB . ARG B 2 239 ? 9.988 7.013 30.377 1.00 120.94 ? 239 ARG B CB 1 ATOM 9063 C CG . ARG B 2 239 ? 11.494 6.856 30.461 1.00 128.22 ? 239 ARG B CG 1 ATOM 9064 C CD . ARG B 2 239 ? 11.862 5.839 31.529 1.00 121.65 ? 239 ARG B CD 1 ATOM 9065 N NE . ARG B 2 239 ? 11.367 6.235 32.845 1.00 118.99 ? 239 ARG B NE 1 ATOM 9066 C CZ . ARG B 2 239 ? 11.351 5.440 33.910 1.00 127.63 ? 239 ARG B CZ 1 ATOM 9067 N NH1 . ARG B 2 239 ? 11.801 4.196 33.820 1.00 134.21 ? 239 ARG B NH1 1 ATOM 9068 N NH2 . ARG B 2 239 ? 10.882 5.889 35.066 1.00 121.84 ? 239 ARG B NH2 1 ATOM 9069 N N . ASN B 2 240 ? 7.446 7.495 28.196 1.00 117.24 ? 240 ASN B N 1 ATOM 9070 C CA . ASN B 2 240 ? 6.013 7.252 28.109 1.00 123.43 ? 240 ASN B CA 1 ATOM 9071 C C . ASN B 2 240 ? 5.629 6.151 29.090 1.00 135.29 ? 240 ASN B C 1 ATOM 9072 O O . ASN B 2 240 ? 6.466 5.323 29.454 1.00 148.71 ? 240 ASN B O 1 ATOM 9073 C CB . ASN B 2 240 ? 5.605 6.882 26.682 1.00 124.24 ? 240 ASN B CB 1 ATOM 9074 C CG . ASN B 2 240 ? 6.464 5.779 26.097 1.00 143.40 ? 240 ASN B CG 1 ATOM 9075 O OD1 . ASN B 2 240 ? 7.645 5.655 26.425 1.00 152.81 ? 240 ASN B OD1 1 ATOM 9076 N ND2 . ASN B 2 240 ? 5.876 4.973 25.221 1.00 152.37 ? 240 ASN B ND2 1 ATOM 9077 N N . ASP B 2 241 ? 4.368 6.155 29.516 1.00 134.93 ? 241 ASP B N 1 ATOM 9078 C CA . ASP B 2 241 ? 3.886 5.263 30.570 1.00 142.45 ? 241 ASP B CA 1 ATOM 9079 C C . ASP B 2 241 ? 4.684 5.456 31.856 1.00 130.22 ? 241 ASP B C 1 ATOM 9080 O O . ASP B 2 241 ? 5.120 4.491 32.485 1.00 126.67 ? 241 ASP B O 1 ATOM 9081 C CB . ASP B 2 241 ? 3.941 3.800 30.124 1.00 141.87 ? 241 ASP B CB 1 ATOM 9082 C CG . ASP B 2 241 ? 2.936 3.488 29.037 1.00 150.34 ? 241 ASP B CG 1 ATOM 9083 O OD1 . ASP B 2 241 ? 3.237 3.753 27.854 1.00 136.49 ? 241 ASP B OD1 1 ATOM 9084 O OD2 . ASP B 2 241 ? 1.843 2.978 29.365 1.00 160.00 ? 241 ASP B OD2 1 ATOM 9085 N N . ALA B 2 242 ? 4.871 6.716 32.234 1.00 118.09 ? 242 ALA B N 1 ATOM 9086 C CA . ALA B 2 242 ? 5.546 7.067 33.477 1.00 115.65 ? 242 ALA B CA 1 ATOM 9087 C C . ALA B 2 242 ? 5.051 8.421 33.969 1.00 110.85 ? 242 ALA B C 1 ATOM 9088 O O . ALA B 2 242 ? 4.607 9.249 33.175 1.00 113.34 ? 242 ALA B O 1 ATOM 9089 C CB . ALA B 2 242 ? 7.052 7.086 33.284 1.00 114.87 ? 242 ALA B CB 1 ATOM 9090 N N . SER B 2 243 ? 5.128 8.647 35.276 1.00 109.84 ? 243 SER B N 1 ATOM 9091 C CA . SER B 2 243 ? 4.706 9.923 35.839 1.00 105.82 ? 243 SER B CA 1 ATOM 9092 C C . SER B 2 243 ? 5.754 10.993 35.566 1.00 105.34 ? 243 SER B C 1 ATOM 9093 O O . SER B 2 243 ? 6.914 10.853 35.954 1.00 116.11 ? 243 SER B O 1 ATOM 9094 C CB . SER B 2 243 ? 4.452 9.798 37.342 1.00 106.88 ? 243 SER B CB 1 ATOM 9095 O OG . SER B 2 243 ? 3.323 8.982 37.599 1.00 118.37 ? 243 SER B OG 1 ATOM 9096 N N . HIS B 2 244 ? 5.337 12.063 34.898 1.00 98.20 ? 244 HIS B N 1 ATOM 9097 C CA . HIS B 2 244 ? 6.253 13.131 34.517 1.00 94.21 ? 244 HIS B CA 1 ATOM 9098 C C . HIS B 2 244 ? 6.171 14.300 35.490 1.00 90.93 ? 244 HIS B C 1 ATOM 9099 O O . HIS B 2 244 ? 5.148 14.978 35.577 1.00 110.45 ? 244 HIS B O 1 ATOM 9100 C CB . HIS B 2 244 ? 5.954 13.607 33.096 1.00 98.20 ? 244 HIS B CB 1 ATOM 9101 C CG . HIS B 2 244 ? 5.993 12.514 32.074 1.00 96.76 ? 244 HIS B CG 1 ATOM 9102 N ND1 . HIS B 2 244 ? 5.292 12.579 30.889 1.00 109.50 ? 244 HIS B ND1 1 ATOM 9103 C CD2 . HIS B 2 244 ? 6.651 11.332 32.058 1.00 100.26 ? 244 HIS B CD2 1 ATOM 9104 C CE1 . HIS B 2 244 ? 5.515 11.482 30.188 1.00 101.65 ? 244 HIS B CE1 1 ATOM 9105 N NE2 . HIS B 2 244 ? 6.336 10.708 30.874 1.00 103.23 ? 244 HIS B NE2 1 ATOM 9106 N N . LEU B 2 245 ? 7.256 14.530 36.218 1.00 89.95 ? 245 LEU B N 1 ATOM 9107 C CA . LEU B 2 245 ? 7.301 15.599 37.204 1.00 87.47 ? 245 LEU B CA 1 ATOM 9108 C C . LEU B 2 245 ? 8.384 16.617 36.867 1.00 98.93 ? 245 LEU B C 1 ATOM 9109 O O . LEU B 2 245 ? 9.570 16.290 36.840 1.00 112.17 ? 245 LEU B O 1 ATOM 9110 C CB . LEU B 2 245 ? 7.537 15.025 38.604 1.00 89.95 ? 245 LEU B CB 1 ATOM 9111 C CG . LEU B 2 245 ? 6.508 14.019 39.119 1.00 93.60 ? 245 LEU B CG 1 ATOM 9112 C CD1 . LEU B 2 245 ? 6.824 13.606 40.550 1.00 96.04 ? 245 LEU B CD1 1 ATOM 9113 C CD2 . LEU B 2 245 ? 5.104 14.593 39.021 1.00 92.87 ? 245 LEU B CD2 1 ATOM 9114 N N . LEU B 2 246 ? 7.970 17.851 36.603 1.00 99.86 ? 246 LEU B N 1 ATOM 9115 C CA . LEU B 2 246 ? 8.913 18.937 36.363 1.00 88.68 ? 246 LEU B CA 1 ATOM 9116 C C . LEU B 2 246 ? 8.898 19.892 37.550 1.00 86.59 ? 246 LEU B C 1 ATOM 9117 O O . LEU B 2 246 ? 7.926 20.617 37.763 1.00 101.35 ? 246 LEU B O 1 ATOM 9118 C CB . LEU B 2 246 ? 8.571 19.678 35.068 1.00 76.57 ? 246 LEU B CB 1 ATOM 9119 C CG . LEU B 2 246 ? 9.559 20.745 34.589 1.00 73.14 ? 246 LEU B CG 1 ATOM 9120 C CD1 . LEU B 2 246 ? 10.911 20.124 34.286 1.00 74.66 ? 246 LEU B CD1 1 ATOM 9121 C CD2 . LEU B 2 246 ? 9.020 21.475 33.367 1.00 80.24 ? 246 LEU B CD2 1 ATOM 9122 N N . VAL B 2 247 ? 9.981 19.888 38.321 1.00 77.56 ? 247 VAL B N 1 ATOM 9123 C CA . VAL B 2 247 ? 10.063 20.705 39.525 1.00 95.11 ? 247 VAL B CA 1 ATOM 9124 C C . VAL B 2 247 ? 10.845 21.991 39.262 1.00 96.64 ? 247 VAL B C 1 ATOM 9125 O O . VAL B 2 247 ? 11.959 21.965 38.736 1.00 96.16 ? 247 VAL B O 1 ATOM 9126 C CB . VAL B 2 247 ? 10.706 19.919 40.689 1.00 91.88 ? 247 VAL B CB 1 ATOM 9127 C CG1 . VAL B 2 247 ? 11.865 19.077 40.187 1.00 102.49 ? 247 VAL B CG1 1 ATOM 9128 C CG2 . VAL B 2 247 ? 11.145 20.859 41.802 1.00 115.65 ? 247 VAL B CG2 1 ATOM 9129 N N . PHE B 2 248 ? 10.242 23.115 39.634 1.00 92.48 ? 248 PHE B N 1 ATOM 9130 C CA . PHE B 2 248 ? 10.763 24.434 39.304 1.00 75.61 ? 248 PHE B CA 1 ATOM 9131 C C . PHE B 2 248 ? 11.186 25.197 40.560 1.00 81.14 ? 248 PHE B C 1 ATOM 9132 O O . PHE B 2 248 ? 10.386 25.387 41.476 1.00 102.80 ? 248 PHE B O 1 ATOM 9133 C CB . PHE B 2 248 ? 9.703 25.219 38.528 1.00 67.78 ? 248 PHE B CB 1 ATOM 9134 C CG . PHE B 2 248 ? 10.163 26.560 38.038 1.00 78.00 ? 248 PHE B CG 1 ATOM 9135 C CD1 . PHE B 2 248 ? 10.836 26.678 36.836 1.00 79.27 ? 248 PHE B CD1 1 ATOM 9136 C CD2 . PHE B 2 248 ? 9.900 27.705 38.768 1.00 88.16 ? 248 PHE B CD2 1 ATOM 9137 C CE1 . PHE B 2 248 ? 11.253 27.911 36.376 1.00 68.88 ? 248 PHE B CE1 1 ATOM 9138 C CE2 . PHE B 2 248 ? 10.314 28.941 38.316 1.00 71.52 ? 248 PHE B CE2 1 ATOM 9139 C CZ . PHE B 2 248 ? 10.991 29.044 37.119 1.00 75.48 ? 248 PHE B CZ 1 ATOM 9140 N N . THR B 2 249 ? 12.442 25.635 40.597 1.00 72.87 ? 249 THR B N 1 ATOM 9141 C CA . THR B 2 249 ? 12.967 26.354 41.756 1.00 84.63 ? 249 THR B CA 1 ATOM 9142 C C . THR B 2 249 ? 13.503 27.736 41.390 1.00 80.33 ? 249 THR B C 1 ATOM 9143 O O . THR B 2 249 ? 14.272 27.880 40.440 1.00 88.54 ? 249 THR B O 1 ATOM 9144 C CB . THR B 2 249 ? 14.087 25.554 42.453 1.00 95.01 ? 249 THR B CB 1 ATOM 9145 O OG1 . THR B 2 249 ? 15.081 25.178 41.492 1.00 112.42 ? 249 THR B OG1 1 ATOM 9146 C CG2 . THR B 2 249 ? 13.522 24.305 43.107 1.00 78.54 ? 249 THR B CG2 1 ATOM 9147 N N . THR B 2 250 ? 13.192 28.768 42.191 1.00 70.79 ? 250 THR B N 1 ATOM 9148 C CA . THR B 2 250 ? 13.714 30.135 41.967 1.00 77.84 ? 250 THR B CA 1 ATOM 9149 C C . THR B 2 250 ? 13.750 31.081 43.176 1.00 89.73 ? 250 THR B C 1 ATOM 9150 O O . THR B 2 250 ? 13.057 30.821 44.134 1.00 72.48 ? 250 THR B O 1 ATOM 9151 C CB . THR B 2 250 ? 12.876 30.886 40.956 1.00 74.29 ? 250 THR B CB 1 ATOM 9152 O OG1 . THR B 2 250 ? 13.443 32.183 40.776 1.00 79.14 ? 250 THR B OG1 1 ATOM 9153 C CG2 . THR B 2 250 ? 11.527 31.075 41.501 1.00 65.59 ? 250 THR B CG2 1 ATOM 9154 N N . ASP B 2 251 ? 14.514 32.197 43.117 1.00 109.81 ? 251 ASP B N 1 ATOM 9155 C CA . ASP B 2 251 ? 14.586 33.081 44.277 1.00 93.38 ? 251 ASP B CA 1 ATOM 9156 C C . ASP B 2 251 ? 13.550 34.201 44.202 1.00 94.54 ? 251 ASP B C 1 ATOM 9157 O O . ASP B 2 251 ? 12.922 34.550 45.202 1.00 93.60 ? 251 ASP B O 1 ATOM 9158 C CB . ASP B 2 251 ? 15.992 33.685 44.394 1.00 95.07 ? 251 ASP B CB 1 ATOM 9159 C CG . ASP B 2 251 ? 16.404 33.949 45.834 1.00 137.85 ? 251 ASP B CG 1 ATOM 9160 O OD1 . ASP B 2 251 ? 17.052 34.987 46.090 1.00 143.48 ? 251 ASP B OD1 1 ATOM 9161 O OD2 . ASP B 2 251 ? 16.102 33.112 46.711 1.00 159.52 ? 251 ASP B OD2 1 ATOM 9162 N N . ALA B 2 252 ? 13.290 34.668 42.996 1.00 90.96 ? 252 ALA B N 1 ATOM 9163 C CA . ALA B 2 252 ? 12.321 35.721 42.838 1.00 105.92 ? 252 ALA B CA 1 ATOM 9164 C C . ALA B 2 252 ? 11.392 35.514 41.685 1.00 94.62 ? 252 ALA B C 1 ATOM 9165 O O . ALA B 2 252 ? 11.350 34.476 41.060 1.00 89.69 ? 252 ALA B O 1 ATOM 9166 C CB . ALA B 2 252 ? 13.016 37.059 42.699 1.00 108.60 ? 252 ALA B CB 1 ATOM 9167 N N . LYS B 2 253 ? 10.641 36.552 41.415 1.00 88.43 ? 253 LYS B N 1 ATOM 9168 C CA . LYS B 2 253 ? 9.579 36.486 40.415 1.00 88.66 ? 253 LYS B CA 1 ATOM 9169 C C . LYS B 2 253 ? 10.134 36.168 39.028 1.00 77.20 ? 253 LYS B C 1 ATOM 9170 O O . LYS B 2 253 ? 11.339 35.988 38.859 1.00 75.06 ? 253 LYS B O 1 ATOM 9171 C CB . LYS B 2 253 ? 8.793 37.800 40.381 1.00 95.89 ? 253 LYS B CB 1 ATOM 9172 C CG . LYS B 2 253 ? 9.617 39.048 40.655 1.00 85.69 ? 253 LYS B CG 1 ATOM 9173 C CD . LYS B 2 253 ? 8.724 40.281 40.673 1.00 93.44 ? 253 LYS B CD 1 ATOM 9174 C CE . LYS B 2 253 ? 9.410 41.472 41.326 1.00 89.57 ? 253 LYS B CE 1 ATOM 9175 N NZ . LYS B 2 253 ? 10.589 41.948 40.555 1.00 68.05 ? 253 LYS B NZ 1 ATOM 9176 N N . THR B 2 254 ? 9.251 36.096 38.037 1.00 75.34 ? 254 THR B N 1 ATOM 9177 C CA . THR B 2 254 ? 9.640 35.604 36.719 1.00 71.46 ? 254 THR B CA 1 ATOM 9178 C C . THR B 2 254 ? 9.204 36.507 35.573 1.00 73.14 ? 254 THR B C 1 ATOM 9179 O O . THR B 2 254 ? 8.285 37.314 35.715 1.00 98.41 ? 254 THR B O 1 ATOM 9180 C CB . THR B 2 254 ? 9.065 34.196 36.466 1.00 70.26 ? 254 THR B CB 1 ATOM 9181 O OG1 . THR B 2 254 ? 9.308 33.816 35.107 1.00 62.54 ? 254 THR B OG1 1 ATOM 9182 C CG2 . THR B 2 254 ? 7.566 34.178 36.727 1.00 57.08 ? 254 THR B CG2 1 ATOM 9183 N N . HIS B 2 255 ? 9.882 36.366 34.438 1.00 65.27 ? 255 HIS B N 1 ATOM 9184 C CA . HIS B 2 255 ? 9.471 37.039 33.214 1.00 77.38 ? 255 HIS B CA 1 ATOM 9185 C C . HIS B 2 255 ? 8.292 36.304 32.593 1.00 78.74 ? 255 HIS B C 1 ATOM 9186 O O . HIS B 2 255 ? 8.305 35.080 32.471 1.00 88.63 ? 255 HIS B O 1 ATOM 9187 C CB . HIS B 2 255 ? 10.622 37.116 32.206 1.00 70.47 ? 255 HIS B CB 1 ATOM 9188 C CG . HIS B 2 255 ? 11.576 38.241 32.456 1.00 70.31 ? 255 HIS B CG 1 ATOM 9189 N ND1 . HIS B 2 255 ? 11.175 39.557 32.515 1.00 83.82 ? 255 HIS B ND1 1 ATOM 9190 C CD2 . HIS B 2 255 ? 12.917 38.247 32.643 1.00 67.48 ? 255 HIS B CD2 1 ATOM 9191 C CE1 . HIS B 2 255 ? 12.226 40.327 32.736 1.00 100.40 ? 255 HIS B CE1 1 ATOM 9192 N NE2 . HIS B 2 255 ? 13.295 39.556 32.821 1.00 80.92 ? 255 HIS B NE2 1 ATOM 9193 N N . ILE B 2 256 ? 7.270 37.059 32.211 1.00 70.61 ? 256 ILE B N 1 ATOM 9194 C CA . ILE B 2 256 ? 6.138 36.504 31.487 1.00 60.60 ? 256 ILE B CA 1 ATOM 9195 C C . ILE B 2 256 ? 6.273 36.874 30.015 1.00 75.19 ? 256 ILE B C 1 ATOM 9196 O O . ILE B 2 256 ? 7.257 37.494 29.617 1.00 56.22 ? 256 ILE B O 1 ATOM 9197 C CB . ILE B 2 256 ? 4.800 37.019 32.043 1.00 58.57 ? 256 ILE B CB 1 ATOM 9198 C CG1 . ILE B 2 256 ? 4.690 38.531 31.846 1.00 55.20 ? 256 ILE B CG1 1 ATOM 9199 C CG2 . ILE B 2 256 ? 4.672 36.666 33.517 1.00 56.09 ? 256 ILE B CG2 1 ATOM 9200 C CD1 . ILE B 2 256 ? 3.462 39.143 32.477 1.00 69.29 ? 256 ILE B CD1 1 ATOM 9201 N N . ALA B 2 257 ? 5.291 36.495 29.206 1.00 76.87 ? 257 ALA B N 1 ATOM 9202 C CA . ALA B 2 257 ? 5.319 36.838 27.790 1.00 60.14 ? 257 ALA B CA 1 ATOM 9203 C C . ALA B 2 257 ? 5.188 38.348 27.598 1.00 69.39 ? 257 ALA B C 1 ATOM 9204 O O . ALA B 2 257 ? 4.703 39.050 28.488 1.00 82.10 ? 257 ALA B O 1 ATOM 9205 C CB . ALA B 2 257 ? 4.220 36.106 27.044 1.00 64.73 ? 257 ALA B CB 1 ATOM 9206 N N . LEU B 2 258 ? 5.650 38.823 26.441 1.00 70.57 ? 258 LEU B N 1 ATOM 9207 C CA . LEU B 2 258 ? 5.627 40.238 26.046 1.00 63.34 ? 258 LEU B CA 1 ATOM 9208 C C . LEU B 2 258 ? 6.639 41.098 26.808 1.00 65.63 ? 258 LEU B C 1 ATOM 9209 O O . LEU B 2 258 ? 6.817 42.275 26.494 1.00 63.46 ? 258 LEU B O 1 ATOM 9210 C CB . LEU B 2 258 ? 4.220 40.829 26.197 1.00 64.29 ? 258 LEU B CB 1 ATOM 9211 C CG . LEU B 2 258 ? 3.155 40.280 25.244 1.00 68.71 ? 258 LEU B CG 1 ATOM 9212 C CD1 . LEU B 2 258 ? 1.817 40.966 25.479 1.00 75.86 ? 258 LEU B CD1 1 ATOM 9213 C CD2 . LEU B 2 258 ? 3.596 40.438 23.796 1.00 76.60 ? 258 LEU B CD2 1 ATOM 9214 N N . ASP B 2 259 ? 7.308 40.512 27.797 1.00 65.90 ? 259 ASP B N 1 ATOM 9215 C CA . ASP B 2 259 ? 8.375 41.211 28.508 1.00 55.57 ? 259 ASP B CA 1 ATOM 9216 C C . ASP B 2 259 ? 9.593 41.400 27.611 1.00 55.63 ? 259 ASP B C 1 ATOM 9217 O O . ASP B 2 259 ? 10.355 42.354 27.770 1.00 61.29 ? 259 ASP B O 1 ATOM 9218 C CB . ASP B 2 259 ? 8.777 40.453 29.775 1.00 58.79 ? 259 ASP B CB 1 ATOM 9219 C CG . ASP B 2 259 ? 7.836 40.707 30.933 1.00 80.13 ? 259 ASP B CG 1 ATOM 9220 O OD1 . ASP B 2 259 ? 7.059 41.681 30.864 1.00 103.88 ? 259 ASP B OD1 1 ATOM 9221 O OD2 . ASP B 2 259 ? 7.882 39.941 31.920 1.00 87.61 ? 259 ASP B OD2 1 ATOM 9222 N N . GLY B 2 260 ? 9.765 40.485 26.663 1.00 57.69 ? 260 GLY B N 1 ATOM 9223 C CA . GLY B 2 260 ? 10.932 40.477 25.802 1.00 58.17 ? 260 GLY B CA 1 ATOM 9224 C C . GLY B 2 260 ? 11.008 41.617 24.803 1.00 58.10 ? 260 GLY B C 1 ATOM 9225 O O . GLY B 2 260 ? 12.020 41.776 24.121 1.00 58.38 ? 260 GLY B O 1 ATOM 9226 N N . ARG B 2 261 ? 9.946 42.412 24.709 1.00 61.05 ? 261 ARG B N 1 ATOM 9227 C CA . ARG B 2 261 ? 9.920 43.529 23.770 1.00 64.95 ? 261 ARG B CA 1 ATOM 9228 C C . ARG B 2 261 ? 10.945 44.593 24.162 1.00 66.24 ? 261 ARG B C 1 ATOM 9229 O O . ARG B 2 261 ? 11.493 45.284 23.304 1.00 62.10 ? 261 ARG B O 1 ATOM 9230 C CB . ARG B 2 261 ? 8.518 44.139 23.690 1.00 59.82 ? 261 ARG B CB 1 ATOM 9231 C CG . ARG B 2 261 ? 8.380 45.227 22.637 1.00 60.97 ? 261 ARG B CG 1 ATOM 9232 C CD . ARG B 2 261 ? 6.960 45.761 22.551 1.00 63.66 ? 261 ARG B CD 1 ATOM 9233 N NE . ARG B 2 261 ? 6.881 46.926 21.674 1.00 88.86 ? 261 ARG B NE 1 ATOM 9234 C CZ . ARG B 2 261 ? 5.759 47.583 21.399 1.00 91.82 ? 261 ARG B CZ 1 ATOM 9235 N NH1 . ARG B 2 261 ? 4.610 47.188 21.929 1.00 102.05 ? 261 ARG B NH1 1 ATOM 9236 N NH2 . ARG B 2 261 ? 5.786 48.634 20.591 1.00 76.17 ? 261 ARG B NH2 1 ATOM 9237 N N . LEU B 2 262 ? 11.205 44.709 25.461 1.00 71.67 ? 262 LEU B N 1 ATOM 9238 C CA . LEU B 2 262 ? 12.220 45.630 25.965 1.00 52.85 ? 262 LEU B CA 1 ATOM 9239 C C . LEU B 2 262 ? 13.601 45.246 25.444 1.00 60.92 ? 262 LEU B C 1 ATOM 9240 O O . LEU B 2 262 ? 14.457 46.103 25.227 1.00 80.28 ? 262 LEU B O 1 ATOM 9241 C CB . LEU B 2 262 ? 12.223 45.652 27.495 1.00 50.78 ? 262 LEU B CB 1 ATOM 9242 C CG . LEU B 2 262 ? 11.284 46.621 28.219 1.00 61.93 ? 262 LEU B CG 1 ATOM 9243 C CD1 . LEU B 2 262 ? 9.826 46.368 27.869 1.00 70.82 ? 262 LEU B CD1 1 ATOM 9244 C CD2 . LEU B 2 262 ? 11.494 46.535 29.723 1.00 88.48 ? 262 LEU B CD2 1 ATOM 9245 N N . ALA B 2 263 ? 13.807 43.950 25.242 1.00 64.48 ? 263 ALA B N 1 ATOM 9246 C CA . ALA B 2 263 ? 15.065 43.446 24.711 1.00 55.50 ? 263 ALA B CA 1 ATOM 9247 C C . ALA B 2 263 ? 15.057 43.511 23.192 1.00 58.14 ? 263 ALA B C 1 ATOM 9248 O O . ALA B 2 263 ? 16.021 43.119 22.536 1.00 58.83 ? 263 ALA B O 1 ATOM 9249 C CB . ALA B 2 263 ? 15.311 42.021 25.182 1.00 57.09 ? 263 ALA B CB 1 ATOM 9250 N N . GLY B 2 264 ? 13.956 44.003 22.637 1.00 75.83 ? 264 GLY B N 1 ATOM 9251 C CA . GLY B 2 264 ? 13.806 44.089 21.199 1.00 92.34 ? 264 GLY B CA 1 ATOM 9252 C C . GLY B 2 264 ? 13.443 42.744 20.606 1.00 67.27 ? 264 GLY B C 1 ATOM 9253 O O . GLY B 2 264 ? 13.812 42.434 19.473 1.00 80.43 ? 264 GLY B O 1 ATOM 9254 N N . ILE B 2 265 ? 12.719 41.939 21.376 1.00 62.22 ? 265 ILE B N 1 ATOM 9255 C CA . ILE B 2 265 ? 12.295 40.631 20.902 1.00 65.34 ? 265 ILE B CA 1 ATOM 9256 C C . ILE B 2 265 ? 10.781 40.594 20.716 1.00 67.11 ? 265 ILE B C 1 ATOM 9257 O O . ILE B 2 265 ? 10.024 40.528 21.686 1.00 65.49 ? 265 ILE B O 1 ATOM 9258 C CB . ILE B 2 265 ? 12.717 39.528 21.882 1.00 65.45 ? 265 ILE B CB 1 ATOM 9259 C CG1 . ILE B 2 265 ? 14.208 39.646 22.210 1.00 66.74 ? 265 ILE B CG1 1 ATOM 9260 C CG2 . ILE B 2 265 ? 12.401 38.175 21.306 1.00 70.94 ? 265 ILE B CG2 1 ATOM 9261 C CD1 . ILE B 2 265 ? 14.663 38.735 23.332 1.00 66.84 ? 265 ILE B CD1 1 ATOM 9262 N N . VAL B 2 266 ? 10.351 40.635 19.459 1.00 69.91 ? 266 VAL B N 1 ATOM 9263 C CA . VAL B 2 266 ? 8.932 40.666 19.123 1.00 73.52 ? 266 VAL B CA 1 ATOM 9264 C C . VAL B 2 266 ? 8.345 39.327 18.676 1.00 83.18 ? 266 VAL B C 1 ATOM 9265 O O . VAL B 2 266 ? 7.145 39.236 18.416 1.00 100.07 ? 266 VAL B O 1 ATOM 9266 C CB . VAL B 2 266 ? 8.667 41.697 18.017 1.00 83.13 ? 266 VAL B CB 1 ATOM 9267 C CG1 . VAL B 2 266 ? 8.847 43.103 18.561 1.00 71.46 ? 266 VAL B CG1 1 ATOM 9268 C CG2 . VAL B 2 266 ? 9.594 41.451 16.842 1.00 111.05 ? 266 VAL B CG2 1 ATOM 9269 N N . GLN B 2 267 ? 9.176 38.295 18.579 1.00 77.24 ? 267 GLN B N 1 ATOM 9270 C CA . GLN B 2 267 ? 8.713 37.014 18.047 1.00 80.89 ? 267 GLN B CA 1 ATOM 9271 C C . GLN B 2 267 ? 8.181 36.099 19.146 1.00 77.57 ? 267 GLN B C 1 ATOM 9272 O O . GLN B 2 267 ? 8.909 35.749 20.074 1.00 76.09 ? 267 GLN B O 1 ATOM 9273 C CB . GLN B 2 267 ? 9.834 36.307 17.279 1.00 89.38 ? 267 GLN B CB 1 ATOM 9274 C CG . GLN B 2 267 ? 9.360 35.094 16.483 1.00 93.35 ? 267 GLN B CG 1 ATOM 9275 C CD . GLN B 2 267 ? 10.485 34.382 15.754 1.00 100.21 ? 267 GLN B CD 1 ATOM 9276 O OE1 . GLN B 2 267 ? 11.653 34.498 16.126 1.00 118.76 ? 267 GLN B OE1 1 ATOM 9277 N NE2 . GLN B 2 267 ? 10.137 33.639 14.710 1.00 93.32 ? 267 GLN B NE2 1 ATOM 9278 N N . PRO B 2 268 ? 6.902 35.708 19.037 1.00 78.49 ? 268 PRO B N 1 ATOM 9279 C CA . PRO B 2 268 ? 6.243 34.834 20.014 1.00 77.02 ? 268 PRO B CA 1 ATOM 9280 C C . PRO B 2 268 ? 6.833 33.428 20.026 1.00 76.61 ? 268 PRO B C 1 ATOM 9281 O O . PRO B 2 268 ? 7.315 32.956 18.996 1.00 78.35 ? 268 PRO B O 1 ATOM 9282 C CB . PRO B 2 268 ? 4.785 34.799 19.535 1.00 79.26 ? 268 PRO B CB 1 ATOM 9283 C CG . PRO B 2 268 ? 4.640 35.973 18.623 1.00 81.96 ? 268 PRO B CG 1 ATOM 9284 C CD . PRO B 2 268 ? 5.976 36.139 17.977 1.00 81.71 ? 268 PRO B CD 1 ATOM 9285 N N . ASN B 2 269 ? 6.793 32.774 21.182 1.00 74.56 ? 269 ASN B N 1 ATOM 9286 C CA . ASN B 2 269 ? 7.282 31.407 21.313 1.00 74.07 ? 269 ASN B CA 1 ATOM 9287 C C . ASN B 2 269 ? 6.493 30.447 20.427 1.00 80.12 ? 269 ASN B C 1 ATOM 9288 O O . ASN B 2 269 ? 5.262 30.437 20.455 1.00 86.49 ? 269 ASN B O 1 ATOM 9289 C CB . ASN B 2 269 ? 7.209 30.956 22.773 1.00 71.19 ? 269 ASN B CB 1 ATOM 9290 C CG . ASN B 2 269 ? 8.124 29.784 23.068 1.00 96.29 ? 269 ASN B CG 1 ATOM 9291 O OD1 . ASN B 2 269 ? 7.867 28.658 22.645 1.00 117.71 ? 269 ASN B OD1 1 ATOM 9292 N ND2 . ASN B 2 269 ? 9.197 30.046 23.807 1.00 101.02 ? 269 ASN B ND2 1 ATOM 9293 N N . ASP B 2 270 ? 7.202 29.644 19.640 1.00 78.05 ? 270 ASP B N 1 ATOM 9294 C CA . ASP B 2 270 ? 6.555 28.708 18.726 1.00 79.93 ? 270 ASP B CA 1 ATOM 9295 C C . ASP B 2 270 ? 6.276 27.360 19.386 1.00 87.52 ? 270 ASP B C 1 ATOM 9296 O O . ASP B 2 270 ? 5.584 26.514 18.821 1.00 101.25 ? 270 ASP B O 1 ATOM 9297 C CB . ASP B 2 270 ? 7.405 28.511 17.469 1.00 82.04 ? 270 ASP B CB 1 ATOM 9298 C CG . ASP B 2 270 ? 8.847 28.157 17.785 1.00 85.12 ? 270 ASP B CG 1 ATOM 9299 O OD1 . ASP B 2 270 ? 9.156 27.866 18.960 1.00 92.48 ? 270 ASP B OD1 1 ATOM 9300 O OD2 . ASP B 2 270 ? 9.674 28.163 16.849 1.00 84.32 ? 270 ASP B OD2 1 ATOM 9301 N N . GLY B 2 271 ? 6.822 27.165 20.582 1.00 77.62 ? 271 GLY B N 1 ATOM 9302 C CA . GLY B 2 271 ? 6.618 25.932 21.319 1.00 78.01 ? 271 GLY B CA 1 ATOM 9303 C C . GLY B 2 271 ? 7.272 24.731 20.663 1.00 90.80 ? 271 GLY B C 1 ATOM 9304 O O . GLY B 2 271 ? 6.801 23.603 20.806 1.00 104.04 ? 271 GLY B O 1 ATOM 9305 N N . GLN B 2 272 ? 8.355 24.971 19.933 1.00 82.79 ? 272 GLN B N 1 ATOM 9306 C CA . GLN B 2 272 ? 9.109 23.889 19.313 1.00 90.17 ? 272 GLN B CA 1 ATOM 9307 C C . GLN B 2 272 ? 10.356 23.580 20.133 1.00 108.69 ? 272 GLN B C 1 ATOM 9308 O O . GLN B 2 272 ? 10.636 24.258 21.122 1.00 100.05 ? 272 GLN B O 1 ATOM 9309 C CB . GLN B 2 272 ? 9.491 24.253 17.877 1.00 85.99 ? 272 GLN B CB 1 ATOM 9310 C CG . GLN B 2 272 ? 8.339 24.798 17.040 1.00 86.14 ? 272 GLN B CG 1 ATOM 9311 C CD . GLN B 2 272 ? 7.271 23.761 16.748 1.00 141.45 ? 272 GLN B CD 1 ATOM 9312 O OE1 . GLN B 2 272 ? 7.498 22.558 16.884 1.00 153.39 ? 272 GLN B OE1 1 ATOM 9313 N NE2 . GLN B 2 272 ? 6.094 24.225 16.340 1.00 158.94 ? 272 GLN B NE2 1 ATOM 9314 N N . CYS B 2 273 ? 11.112 22.566 19.723 1.00 117.64 ? 273 CYS B N 1 ATOM 9315 C CA . CYS B 2 273 ? 12.343 22.227 20.428 1.00 109.09 ? 273 CYS B CA 1 ATOM 9316 C C . CYS B 2 273 ? 13.543 22.883 19.758 1.00 110.51 ? 273 CYS B C 1 ATOM 9317 O O . CYS B 2 273 ? 13.962 22.479 18.673 1.00 128.95 ? 273 CYS B O 1 ATOM 9318 C CB . CYS B 2 273 ? 12.531 20.709 20.480 1.00 120.97 ? 273 CYS B CB 1 ATOM 9319 S SG . CYS B 2 273 ? 14.101 20.171 21.195 1.00 156.02 ? 273 CYS B SG 1 ATOM 9320 N N . HIS B 2 274 ? 14.089 23.901 20.414 1.00 105.00 ? 274 HIS B N 1 ATOM 9321 C CA . HIS B 2 274 ? 15.234 24.634 19.888 1.00 112.22 ? 274 HIS B CA 1 ATOM 9322 C C . HIS B 2 274 ? 16.563 24.224 20.522 1.00 120.52 ? 274 HIS B C 1 ATOM 9323 O O . HIS B 2 274 ? 17.609 24.789 20.201 1.00 130.77 ? 274 HIS B O 1 ATOM 9324 C CB . HIS B 2 274 ? 14.999 26.135 20.049 1.00 105.56 ? 274 HIS B CB 1 ATOM 9325 C CG . HIS B 2 274 ? 13.826 26.640 19.267 1.00 111.59 ? 274 HIS B CG 1 ATOM 9326 N ND1 . HIS B 2 274 ? 13.757 26.554 17.893 1.00 107.98 ? 274 HIS B ND1 1 ATOM 9327 C CD2 . HIS B 2 274 ? 12.673 27.226 19.666 1.00 122.75 ? 274 HIS B CD2 1 ATOM 9328 C CE1 . HIS B 2 274 ? 12.613 27.070 17.479 1.00 121.88 ? 274 HIS B CE1 1 ATOM 9329 N NE2 . HIS B 2 274 ? 11.937 27.485 18.535 1.00 131.51 ? 274 HIS B NE2 1 ATOM 9330 N N . VAL B 2 275 ? 16.522 23.247 21.423 1.00 120.09 ? 275 VAL B N 1 ATOM 9331 C CA . VAL B 2 275 ? 17.734 22.785 22.094 1.00 109.49 ? 275 VAL B CA 1 ATOM 9332 C C . VAL B 2 275 ? 18.544 21.875 21.174 1.00 114.94 ? 275 VAL B C 1 ATOM 9333 O O . VAL B 2 275 ? 18.053 20.843 20.715 1.00 119.14 ? 275 VAL B O 1 ATOM 9334 C CB . VAL B 2 275 ? 17.410 22.031 23.398 1.00 92.25 ? 275 VAL B CB 1 ATOM 9335 C CG1 . VAL B 2 275 ? 18.688 21.558 24.069 1.00 94.54 ? 275 VAL B CG1 1 ATOM 9336 C CG2 . VAL B 2 275 ? 16.613 22.919 24.338 1.00 87.52 ? 275 VAL B CG2 1 ATOM 9337 N N . GLY B 2 276 ? 19.788 22.263 20.911 1.00 112.48 ? 276 GLY B N 1 ATOM 9338 C CA . GLY B 2 276 ? 20.636 21.535 19.984 1.00 112.55 ? 276 GLY B CA 1 ATOM 9339 C C . GLY B 2 276 ? 21.629 20.608 20.657 1.00 120.63 ? 276 GLY B C 1 ATOM 9340 O O . GLY B 2 276 ? 21.492 20.284 21.837 1.00 112.05 ? 276 GLY B O 1 ATOM 9341 N N . SER B 2 277 ? 22.638 20.187 19.900 1.00 127.28 ? 277 SER B N 1 ATOM 9342 C CA . SER B 2 277 ? 23.651 19.265 20.403 1.00 120.78 ? 277 SER B CA 1 ATOM 9343 C C . SER B 2 277 ? 24.573 19.932 21.419 1.00 116.57 ? 277 SER B C 1 ATOM 9344 O O . SER B 2 277 ? 25.306 19.256 22.141 1.00 121.82 ? 277 SER B O 1 ATOM 9345 C CB . SER B 2 277 ? 24.475 18.697 19.246 1.00 124.15 ? 277 SER B CB 1 ATOM 9346 O OG . SER B 2 277 ? 25.105 19.733 18.514 1.00 132.62 ? 277 SER B OG 1 ATOM 9347 N N . ASP B 2 278 ? 24.536 21.260 21.471 1.00 111.78 ? 278 ASP B N 1 ATOM 9348 C CA . ASP B 2 278 ? 25.330 22.007 22.439 1.00 114.28 ? 278 ASP B CA 1 ATOM 9349 C C . ASP B 2 278 ? 24.583 22.125 23.764 1.00 116.44 ? 278 ASP B C 1 ATOM 9350 O O . ASP B 2 278 ? 25.082 22.725 24.717 1.00 112.67 ? 278 ASP B O 1 ATOM 9351 C CB . ASP B 2 278 ? 25.676 23.396 21.899 1.00 128.90 ? 278 ASP B CB 1 ATOM 9352 C CG . ASP B 2 278 ? 24.446 24.230 21.603 1.00 142.78 ? 278 ASP B CG 1 ATOM 9353 O OD1 . ASP B 2 278 ? 23.412 23.650 21.211 1.00 154.59 ? 278 ASP B OD1 1 ATOM 9354 O OD2 . ASP B 2 278 ? 24.513 25.468 21.762 1.00 132.97 ? 278 ASP B OD2 1 ATOM 9355 N N . ASN B 2 279 ? 23.384 21.548 23.804 1.00 118.59 ? 279 ASN B N 1 ATOM 9356 C CA . ASN B 2 279 ? 22.545 21.529 25.000 1.00 112.98 ? 279 ASN B CA 1 ATOM 9357 C C . ASN B 2 279 ? 22.234 22.921 25.544 1.00 111.09 ? 279 ASN B C 1 ATOM 9358 O O . ASN B 2 279 ? 22.177 23.122 26.756 1.00 117.96 ? 279 ASN B O 1 ATOM 9359 C CB . ASN B 2 279 ? 23.199 20.680 26.094 1.00 107.98 ? 279 ASN B CB 1 ATOM 9360 C CG . ASN B 2 279 ? 23.227 19.205 25.745 1.00 108.44 ? 279 ASN B CG 1 ATOM 9361 O OD1 . ASN B 2 279 ? 23.124 18.830 24.577 1.00 116.40 ? 279 ASN B OD1 1 ATOM 9362 N ND2 . ASN B 2 279 ? 23.362 18.359 26.760 1.00 113.95 ? 279 ASN B ND2 1 ATOM 9363 N N . HIS B 2 280 ? 22.032 23.876 24.643 1.00 104.55 ? 280 HIS B N 1 ATOM 9364 C CA . HIS B 2 280 ? 21.617 25.220 25.030 1.00 103.33 ? 280 HIS B CA 1 ATOM 9365 C C . HIS B 2 280 ? 20.347 25.619 24.289 1.00 99.84 ? 280 HIS B C 1 ATOM 9366 O O . HIS B 2 280 ? 20.063 25.101 23.208 1.00 117.76 ? 280 HIS B O 1 ATOM 9367 C CB . HIS B 2 280 ? 22.727 26.237 24.753 1.00 120.51 ? 280 HIS B CB 1 ATOM 9368 C CG . HIS B 2 280 ? 23.878 26.154 25.707 1.00 131.35 ? 280 HIS B CG 1 ATOM 9369 N ND1 . HIS B 2 280 ? 23.803 26.611 27.005 1.00 113.90 ? 280 HIS B ND1 1 ATOM 9370 C CD2 . HIS B 2 280 ? 25.133 25.673 25.549 1.00 142.55 ? 280 HIS B CD2 1 ATOM 9371 C CE1 . HIS B 2 280 ? 24.961 26.412 27.608 1.00 115.80 ? 280 HIS B CE1 1 ATOM 9372 N NE2 . HIS B 2 280 ? 25.786 25.844 26.746 1.00 137.31 ? 280 HIS B NE2 1 ATOM 9373 N N . TYR B 2 281 ? 19.589 26.543 24.869 1.00 92.70 ? 281 TYR B N 1 ATOM 9374 C CA . TYR B 2 281 ? 18.404 27.063 24.205 1.00 88.44 ? 281 TYR B CA 1 ATOM 9375 C C . TYR B 2 281 ? 18.869 28.088 23.176 1.00 89.01 ? 281 TYR B C 1 ATOM 9376 O O . TYR B 2 281 ? 19.434 29.122 23.530 1.00 89.25 ? 281 TYR B O 1 ATOM 9377 C CB . TYR B 2 281 ? 17.446 27.685 25.227 1.00 83.45 ? 281 TYR B CB 1 ATOM 9378 C CG . TYR B 2 281 ? 16.148 28.228 24.662 1.00 80.38 ? 281 TYR B CG 1 ATOM 9379 C CD1 . TYR B 2 281 ? 15.646 27.784 23.445 1.00 90.67 ? 281 TYR B CD1 1 ATOM 9380 C CD2 . TYR B 2 281 ? 15.427 29.195 25.353 1.00 79.84 ? 281 TYR B CD2 1 ATOM 9381 C CE1 . TYR B 2 281 ? 14.462 28.287 22.935 1.00 90.46 ? 281 TYR B CE1 1 ATOM 9382 C CE2 . TYR B 2 281 ? 14.246 29.701 24.852 1.00 73.77 ? 281 TYR B CE2 1 ATOM 9383 C CZ . TYR B 2 281 ? 13.767 29.245 23.643 1.00 84.87 ? 281 TYR B CZ 1 ATOM 9384 O OH . TYR B 2 281 ? 12.589 29.750 23.142 1.00 100.02 ? 281 TYR B OH 1 ATOM 9385 N N . SER B 2 282 ? 18.621 27.797 21.903 1.00 89.42 ? 282 SER B N 1 ATOM 9386 C CA . SER B 2 282 ? 19.157 28.603 20.811 1.00 90.83 ? 282 SER B CA 1 ATOM 9387 C C . SER B 2 282 ? 18.328 29.853 20.538 1.00 95.06 ? 282 SER B C 1 ATOM 9388 O O . SER B 2 282 ? 18.863 30.897 20.161 1.00 112.05 ? 282 SER B O 1 ATOM 9389 C CB . SER B 2 282 ? 19.260 27.763 19.537 1.00 92.92 ? 282 SER B CB 1 ATOM 9390 O OG . SER B 2 282 ? 17.986 27.294 19.129 1.00 91.26 ? 282 SER B OG 1 ATOM 9391 N N . ALA B 2 283 ? 17.021 29.741 20.740 1.00 84.30 ? 283 ALA B N 1 ATOM 9392 C CA . ALA B 2 283 ? 16.094 30.817 20.408 1.00 84.50 ? 283 ALA B CA 1 ATOM 9393 C C . ALA B 2 283 ? 15.910 31.778 21.577 1.00 87.59 ? 283 ALA B C 1 ATOM 9394 O O . ALA B 2 283 ? 15.073 32.680 21.519 1.00 95.12 ? 283 ALA B O 1 ATOM 9395 C CB . ALA B 2 283 ? 14.757 30.244 19.977 1.00 88.34 ? 283 ALA B CB 1 ATOM 9396 N N . SER B 2 284 ? 16.685 31.564 22.637 1.00 91.69 ? 284 SER B N 1 ATOM 9397 C CA . SER B 2 284 ? 16.604 32.377 23.847 1.00 84.64 ? 284 SER B CA 1 ATOM 9398 C C . SER B 2 284 ? 16.706 33.872 23.551 1.00 81.43 ? 284 SER B C 1 ATOM 9399 O O . SER B 2 284 ? 15.933 34.671 24.078 1.00 75.27 ? 284 SER B O 1 ATOM 9400 C CB . SER B 2 284 ? 17.703 31.966 24.830 1.00 79.13 ? 284 SER B CB 1 ATOM 9401 O OG . SER B 2 284 ? 17.556 32.636 26.070 1.00 91.15 ? 284 SER B OG 1 ATOM 9402 N N . THR B 2 285 ? 17.665 34.241 22.708 1.00 92.45 ? 285 THR B N 1 ATOM 9403 C CA . THR B 2 285 ? 17.835 35.633 22.311 1.00 83.73 ? 285 THR B CA 1 ATOM 9404 C C . THR B 2 285 ? 16.855 36.052 21.217 1.00 79.22 ? 285 THR B C 1 ATOM 9405 O O . THR B 2 285 ? 16.473 37.218 21.136 1.00 89.96 ? 285 THR B O 1 ATOM 9406 C CB . THR B 2 285 ? 19.267 35.906 21.809 1.00 77.91 ? 285 THR B CB 1 ATOM 9407 O OG1 . THR B 2 285 ? 19.510 35.152 20.615 1.00 82.08 ? 285 THR B OG1 1 ATOM 9408 C CG2 . THR B 2 285 ? 20.289 35.522 22.866 1.00 79.44 ? 285 THR B CG2 1 ATOM 9409 N N . THR B 2 286 ? 16.455 35.105 20.372 1.00 80.05 ? 286 THR B N 1 ATOM 9410 C CA . THR B 2 286 ? 15.671 35.440 19.183 1.00 75.76 ? 286 THR B CA 1 ATOM 9411 C C . THR B 2 286 ? 14.148 35.368 19.340 1.00 81.02 ? 286 THR B C 1 ATOM 9412 O O . THR B 2 286 ? 13.423 35.830 18.459 1.00 75.30 ? 286 THR B O 1 ATOM 9413 C CB . THR B 2 286 ? 16.058 34.530 17.999 1.00 79.19 ? 286 THR B CB 1 ATOM 9414 O OG1 . THR B 2 286 ? 15.610 33.193 18.249 1.00 87.78 ? 286 THR B OG1 1 ATOM 9415 C CG2 . THR B 2 286 ? 17.563 34.531 17.799 1.00 82.32 ? 286 THR B CG2 1 ATOM 9416 N N . MET B 2 287 ? 13.650 34.808 20.439 1.00 75.41 ? 287 MET B N 1 ATOM 9417 C CA . MET B 2 287 ? 12.199 34.750 20.624 1.00 73.34 ? 287 MET B CA 1 ATOM 9418 C C . MET B 2 287 ? 11.769 34.952 22.075 1.00 69.96 ? 287 MET B C 1 ATOM 9419 O O . MET B 2 287 ? 12.536 34.727 23.011 1.00 68.83 ? 287 MET B O 1 ATOM 9420 C CB . MET B 2 287 ? 11.635 33.432 20.093 1.00 83.17 ? 287 MET B CB 1 ATOM 9421 C CG . MET B 2 287 ? 11.900 32.223 20.961 1.00 98.66 ? 287 MET B CG 1 ATOM 9422 S SD . MET B 2 287 ? 10.893 30.825 20.436 1.00 111.49 ? 287 MET B SD 1 ATOM 9423 C CE . MET B 2 287 ? 11.166 30.859 18.665 1.00 78.54 ? 287 MET B CE 1 ATOM 9424 N N . ASP B 2 288 ? 10.521 35.381 22.233 1.00 69.15 ? 288 ASP B N 1 ATOM 9425 C CA . ASP B 2 288 ? 9.978 35.844 23.506 1.00 67.02 ? 288 ASP B CA 1 ATOM 9426 C C . ASP B 2 288 ? 9.682 34.720 24.497 1.00 74.94 ? 288 ASP B C 1 ATOM 9427 O O . ASP B 2 288 ? 9.574 33.552 24.120 1.00 105.09 ? 288 ASP B O 1 ATOM 9428 C CB . ASP B 2 288 ? 8.700 36.645 23.249 1.00 73.95 ? 288 ASP B CB 1 ATOM 9429 C CG . ASP B 2 288 ? 8.347 37.574 24.393 1.00 82.81 ? 288 ASP B CG 1 ATOM 9430 O OD1 . ASP B 2 288 ? 8.863 37.375 25.513 1.00 81.13 ? 288 ASP B OD1 1 ATOM 9431 O OD2 . ASP B 2 288 ? 7.548 38.506 24.169 1.00 74.66 ? 288 ASP B OD2 1 ATOM 9432 N N . TYR B 2 289 ? 9.567 35.090 25.771 1.00 63.20 ? 289 TYR B N 1 ATOM 9433 C CA . TYR B 2 289 ? 9.097 34.180 26.809 1.00 61.40 ? 289 TYR B CA 1 ATOM 9434 C C . TYR B 2 289 ? 7.707 33.651 26.461 1.00 62.06 ? 289 TYR B C 1 ATOM 9435 O O . TYR B 2 289 ? 6.889 34.376 25.894 1.00 63.28 ? 289 TYR B O 1 ATOM 9436 C CB . TYR B 2 289 ? 9.058 34.877 28.172 1.00 59.08 ? 289 TYR B CB 1 ATOM 9437 C CG . TYR B 2 289 ? 10.353 35.544 28.580 1.00 75.73 ? 289 TYR B CG 1 ATOM 9438 C CD1 . TYR B 2 289 ? 10.569 36.894 28.332 1.00 81.96 ? 289 TYR B CD1 1 ATOM 9439 C CD2 . TYR B 2 289 ? 11.356 34.829 29.222 1.00 87.81 ? 289 TYR B CD2 1 ATOM 9440 C CE1 . TYR B 2 289 ? 11.748 37.512 28.707 1.00 67.21 ? 289 TYR B CE1 1 ATOM 9441 C CE2 . TYR B 2 289 ? 12.539 35.437 29.600 1.00 86.74 ? 289 TYR B CE2 1 ATOM 9442 C CZ . TYR B 2 289 ? 12.729 36.778 29.341 1.00 75.72 ? 289 TYR B CZ 1 ATOM 9443 O OH . TYR B 2 289 ? 13.904 37.387 29.715 1.00 60.56 ? 289 TYR B OH 1 ATOM 9444 N N . PRO B 2 290 ? 7.434 32.383 26.801 1.00 65.36 ? 290 PRO B N 1 ATOM 9445 C CA . PRO B 2 290 ? 6.138 31.781 26.475 1.00 70.40 ? 290 PRO B CA 1 ATOM 9446 C C . PRO B 2 290 ? 5.004 32.278 27.368 1.00 69.20 ? 290 PRO B C 1 ATOM 9447 O O . PRO B 2 290 ? 5.216 32.539 28.553 1.00 65.48 ? 290 PRO B O 1 ATOM 9448 C CB . PRO B 2 290 ? 6.389 30.289 26.696 1.00 62.82 ? 290 PRO B CB 1 ATOM 9449 C CG . PRO B 2 290 ? 7.442 30.247 27.745 1.00 66.43 ? 290 PRO B CG 1 ATOM 9450 C CD . PRO B 2 290 ? 8.329 31.434 27.487 1.00 76.55 ? 290 PRO B CD 1 ATOM 9451 N N . SER B 2 291 ? 3.812 32.409 26.794 1.00 63.27 ? 291 SER B N 1 ATOM 9452 C CA . SER B 2 291 ? 2.627 32.779 27.557 1.00 63.90 ? 291 SER B CA 1 ATOM 9453 C C . SER B 2 291 ? 2.141 31.596 28.385 1.00 82.27 ? 291 SER B C 1 ATOM 9454 O O . SER B 2 291 ? 2.485 30.450 28.097 1.00 68.22 ? 291 SER B O 1 ATOM 9455 C CB . SER B 2 291 ? 1.516 33.270 26.627 1.00 66.69 ? 291 SER B CB 1 ATOM 9456 O OG . SER B 2 291 ? 1.109 32.247 25.735 1.00 75.70 ? 291 SER B OG 1 ATOM 9457 N N . LEU B 2 292 ? 1.353 31.880 29.419 1.00 87.27 ? 292 LEU B N 1 ATOM 9458 C CA . LEU B 2 292 ? 0.801 30.834 30.274 1.00 76.41 ? 292 LEU B CA 1 ATOM 9459 C C . LEU B 2 292 ? -0.061 29.855 29.484 1.00 88.03 ? 292 LEU B C 1 ATOM 9460 O O . LEU B 2 292 ? -0.035 28.651 29.735 1.00 72.67 ? 292 LEU B O 1 ATOM 9461 C CB . LEU B 2 292 ? -0.019 31.445 31.412 1.00 67.22 ? 292 LEU B CB 1 ATOM 9462 C CG . LEU B 2 292 ? 0.753 32.231 32.470 1.00 64.62 ? 292 LEU B CG 1 ATOM 9463 C CD1 . LEU B 2 292 ? -0.163 32.614 33.621 1.00 66.41 ? 292 LEU B CD1 1 ATOM 9464 C CD2 . LEU B 2 292 ? 1.942 31.428 32.971 1.00 62.64 ? 292 LEU B CD2 1 ATOM 9465 N N . GLY B 2 293 ? -0.817 30.379 28.526 1.00 96.58 ? 293 GLY B N 1 ATOM 9466 C CA . GLY B 2 293 ? -1.688 29.557 27.707 1.00 90.22 ? 293 GLY B CA 1 ATOM 9467 C C . GLY B 2 293 ? -0.929 28.544 26.872 1.00 84.28 ? 293 GLY B C 1 ATOM 9468 O O . GLY B 2 293 ? -1.326 27.382 26.780 1.00 101.30 ? 293 GLY B O 1 ATOM 9469 N N . LEU B 2 294 ? 0.170 28.983 26.267 1.00 77.01 ? 294 LEU B N 1 ATOM 9470 C CA . LEU B 2 294 ? 0.974 28.111 25.417 1.00 77.12 ? 294 LEU B CA 1 ATOM 9471 C C . LEU B 2 294 ? 1.642 27.002 26.222 1.00 75.18 ? 294 LEU B C 1 ATOM 9472 O O . LEU B 2 294 ? 1.639 25.841 25.812 1.00 99.94 ? 294 LEU B O 1 ATOM 9473 C CB . LEU B 2 294 ? 2.036 28.916 24.668 1.00 75.66 ? 294 LEU B CB 1 ATOM 9474 C CG . LEU B 2 294 ? 2.908 28.101 23.710 1.00 75.64 ? 294 LEU B CG 1 ATOM 9475 C CD1 . LEU B 2 294 ? 2.076 27.594 22.541 1.00 81.67 ? 294 LEU B CD1 1 ATOM 9476 C CD2 . LEU B 2 294 ? 4.098 28.915 23.221 1.00 79.03 ? 294 LEU B CD2 1 ATOM 9477 N N . MET B 2 295 ? 2.215 27.361 27.365 1.00 69.57 ? 295 MET B N 1 ATOM 9478 C CA . MET B 2 295 ? 2.899 26.382 28.201 1.00 87.77 ? 295 MET B CA 1 ATOM 9479 C C . MET B 2 295 ? 1.898 25.491 28.928 1.00 91.22 ? 295 MET B C 1 ATOM 9480 O O . MET B 2 295 ? 2.243 24.401 29.371 1.00 114.24 ? 295 MET B O 1 ATOM 9481 C CB . MET B 2 295 ? 3.833 27.078 29.198 1.00 100.47 ? 295 MET B CB 1 ATOM 9482 C CG . MET B 2 295 ? 3.152 28.067 30.126 1.00 115.58 ? 295 MET B CG 1 ATOM 9483 S SD . MET B 2 295 ? 4.310 29.259 30.830 1.00 101.72 ? 295 MET B SD 1 ATOM 9484 C CE . MET B 2 295 ? 5.512 28.169 31.591 1.00 64.37 ? 295 MET B CE 1 ATOM 9485 N N . THR B 2 296 ? 0.655 25.954 29.042 1.00 98.11 ? 296 THR B N 1 ATOM 9486 C CA . THR B 2 296 ? -0.421 25.108 29.547 1.00 81.14 ? 296 THR B CA 1 ATOM 9487 C C . THR B 2 296 ? -0.745 24.030 28.518 1.00 73.53 ? 296 THR B C 1 ATOM 9488 O O . THR B 2 296 ? -0.878 22.852 28.853 1.00 82.67 ? 296 THR B O 1 ATOM 9489 C CB . THR B 2 296 ? -1.696 25.923 29.866 1.00 74.54 ? 296 THR B CB 1 ATOM 9490 O OG1 . THR B 2 296 ? -1.586 26.490 31.177 1.00 77.47 ? 296 THR B OG1 1 ATOM 9491 C CG2 . THR B 2 296 ? -2.934 25.041 29.817 1.00 77.82 ? 296 THR B CG2 1 ATOM 9492 N N . GLU B 2 297 ? -0.853 24.450 27.261 1.00 76.51 ? 297 GLU B N 1 ATOM 9493 C CA . GLU B 2 297 ? -1.165 23.547 26.160 1.00 79.29 ? 297 GLU B CA 1 ATOM 9494 C C . GLU B 2 297 ? -0.115 22.453 26.006 1.00 90.15 ? 297 GLU B C 1 ATOM 9495 O O . GLU B 2 297 ? -0.448 21.276 25.877 1.00 102.63 ? 297 GLU B O 1 ATOM 9496 C CB . GLU B 2 297 ? -1.291 24.333 24.854 1.00 83.34 ? 297 GLU B CB 1 ATOM 9497 C CG . GLU B 2 297 ? -1.585 23.475 23.636 1.00 98.69 ? 297 GLU B CG 1 ATOM 9498 C CD . GLU B 2 297 ? -1.505 24.256 22.339 1.00 115.47 ? 297 GLU B CD 1 ATOM 9499 O OE1 . GLU B 2 297 ? -0.477 24.929 22.109 1.00 94.27 ? 297 GLU B OE1 1 ATOM 9500 O OE2 . GLU B 2 297 ? -2.472 24.202 21.550 1.00 137.38 ? 297 GLU B OE2 1 ATOM 9501 N N . LYS B 2 298 ? 1.154 22.849 26.026 1.00 96.47 ? 298 LYS B N 1 ATOM 9502 C CA . LYS B 2 298 ? 2.255 21.916 25.806 1.00 96.32 ? 298 LYS B CA 1 ATOM 9503 C C . LYS B 2 298 ? 2.485 20.981 26.992 1.00 102.08 ? 298 LYS B C 1 ATOM 9504 O O . LYS B 2 298 ? 2.863 19.825 26.807 1.00 114.27 ? 298 LYS B O 1 ATOM 9505 C CB . LYS B 2 298 ? 3.541 22.682 25.486 1.00 71.33 ? 298 LYS B CB 1 ATOM 9506 C CG . LYS B 2 298 ? 3.605 23.212 24.061 1.00 70.99 ? 298 LYS B CG 1 ATOM 9507 C CD . LYS B 2 298 ? 3.497 22.074 23.056 1.00 82.95 ? 298 LYS B CD 1 ATOM 9508 C CE . LYS B 2 298 ? 3.571 22.577 21.623 1.00 99.08 ? 298 LYS B CE 1 ATOM 9509 N NZ . LYS B 2 298 ? 2.424 23.457 21.276 1.00 110.01 ? 298 LYS B NZ 1 ATOM 9510 N N . LEU B 2 299 ? 2.262 21.478 28.206 1.00 74.92 ? 299 LEU B N 1 ATOM 9511 C CA . LEU B 2 299 ? 2.384 20.640 29.397 1.00 96.11 ? 299 LEU B CA 1 ATOM 9512 C C . LEU B 2 299 ? 1.332 19.537 29.385 1.00 93.38 ? 299 LEU B C 1 ATOM 9513 O O . LEU B 2 299 ? 1.601 18.401 29.776 1.00 85.49 ? 299 LEU B O 1 ATOM 9514 C CB . LEU B 2 299 ? 2.252 21.475 30.675 1.00 75.25 ? 299 LEU B CB 1 ATOM 9515 C CG . LEU B 2 299 ? 3.503 22.191 31.193 1.00 72.20 ? 299 LEU B CG 1 ATOM 9516 C CD1 . LEU B 2 299 ? 3.191 22.962 32.468 1.00 70.99 ? 299 LEU B CD1 1 ATOM 9517 C CD2 . LEU B 2 299 ? 4.638 21.207 31.422 1.00 112.79 ? 299 LEU B CD2 1 ATOM 9518 N N . SER B 2 300 ? 0.132 19.882 28.928 1.00 82.09 ? 300 SER B N 1 ATOM 9519 C CA . SER B 2 300 ? -0.975 18.935 28.876 1.00 86.52 ? 300 SER B CA 1 ATOM 9520 C C . SER B 2 300 ? -0.760 17.872 27.801 1.00 100.10 ? 300 SER B C 1 ATOM 9521 O O . SER B 2 300 ? -1.092 16.704 27.998 1.00 108.96 ? 300 SER B O 1 ATOM 9522 C CB . SER B 2 300 ? -2.292 19.674 28.626 1.00 94.79 ? 300 SER B CB 1 ATOM 9523 O OG . SER B 2 300 ? -3.377 18.766 28.545 1.00 127.96 ? 300 SER B OG 1 ATOM 9524 N N . GLN B 2 301 ? -0.203 18.286 26.667 1.00 95.36 ? 301 GLN B N 1 ATOM 9525 C CA . GLN B 2 301 ? 0.030 17.377 25.549 1.00 107.82 ? 301 GLN B CA 1 ATOM 9526 C C . GLN B 2 301 ? 1.111 16.348 25.861 1.00 109.12 ? 301 GLN B C 1 ATOM 9527 O O . GLN B 2 301 ? 1.006 15.186 25.466 1.00 98.30 ? 301 GLN B O 1 ATOM 9528 C CB . GLN B 2 301 ? 0.412 18.162 24.291 1.00 105.07 ? 301 GLN B CB 1 ATOM 9529 C CG . GLN B 2 301 ? -0.726 18.961 23.682 1.00 124.40 ? 301 GLN B CG 1 ATOM 9530 C CD . GLN B 2 301 ? -0.305 19.697 22.426 1.00 132.33 ? 301 GLN B CD 1 ATOM 9531 O OE1 . GLN B 2 301 ? 0.837 19.583 21.980 1.00 139.29 ? 301 GLN B OE1 1 ATOM 9532 N NE2 . GLN B 2 301 ? -1.226 20.459 21.847 1.00 126.84 ? 301 GLN B NE2 1 ATOM 9533 N N . LYS B 2 302 ? 2.149 16.778 26.571 1.00 107.91 ? 302 LYS B N 1 ATOM 9534 C CA . LYS B 2 302 ? 3.271 15.905 26.893 1.00 99.01 ? 302 LYS B CA 1 ATOM 9535 C C . LYS B 2 302 ? 3.046 15.156 28.203 1.00 104.45 ? 302 LYS B C 1 ATOM 9536 O O . LYS B 2 302 ? 3.917 14.409 28.652 1.00 118.92 ? 302 LYS B O 1 ATOM 9537 C CB . LYS B 2 302 ? 4.570 16.710 26.971 1.00 89.49 ? 302 LYS B CB 1 ATOM 9538 C CG . LYS B 2 302 ? 4.963 17.396 25.673 1.00 87.12 ? 302 LYS B CG 1 ATOM 9539 C CD . LYS B 2 302 ? 5.274 16.387 24.580 1.00 91.40 ? 302 LYS B CD 1 ATOM 9540 C CE . LYS B 2 302 ? 5.746 17.077 23.310 1.00 112.55 ? 302 LYS B CE 1 ATOM 9541 N NZ . LYS B 2 302 ? 6.128 16.098 22.256 1.00 127.29 ? 302 LYS B NZ 1 ATOM 9542 N N . ASN B 2 303 ? 1.876 15.364 28.803 1.00 96.42 ? 303 ASN B N 1 ATOM 9543 C CA . ASN B 2 303 ? 1.509 14.736 30.072 1.00 99.65 ? 303 ASN B CA 1 ATOM 9544 C C . ASN B 2 303 ? 2.539 14.987 31.169 1.00 99.55 ? 303 ASN B C 1 ATOM 9545 O O . ASN B 2 303 ? 2.965 14.063 31.860 1.00 122.60 ? 303 ASN B O 1 ATOM 9546 C CB . ASN B 2 303 ? 1.304 13.230 29.884 1.00 106.18 ? 303 ASN B CB 1 ATOM 9547 C CG . ASN B 2 303 ? 0.111 12.909 29.006 1.00 108.26 ? 303 ASN B CG 1 ATOM 9548 O OD1 . ASN B 2 303 ? -0.953 13.514 29.136 1.00 106.72 ? 303 ASN B OD1 1 ATOM 9549 N ND2 . ASN B 2 303 ? 0.284 11.954 28.098 1.00 112.21 ? 303 ASN B ND2 1 ATOM 9550 N N . ILE B 2 304 ? 2.933 16.249 31.322 1.00 99.64 ? 304 ILE B N 1 ATOM 9551 C CA . ILE B 2 304 ? 3.936 16.625 32.310 1.00 103.30 ? 304 ILE B CA 1 ATOM 9552 C C . ILE B 2 304 ? 3.336 17.475 33.424 1.00 89.81 ? 304 ILE B C 1 ATOM 9553 O O . ILE B 2 304 ? 2.720 18.507 33.165 1.00 86.14 ? 304 ILE B O 1 ATOM 9554 C CB . ILE B 2 304 ? 5.099 17.399 31.663 1.00 106.95 ? 304 ILE B CB 1 ATOM 9555 C CG1 . ILE B 2 304 ? 5.782 16.541 30.598 1.00 123.79 ? 304 ILE B CG1 1 ATOM 9556 C CG2 . ILE B 2 304 ? 6.100 17.843 32.720 1.00 98.72 ? 304 ILE B CG2 1 ATOM 9557 C CD1 . ILE B 2 304 ? 6.960 17.215 29.932 1.00 124.86 ? 304 ILE B CD1 1 ATOM 9558 N N . ASN B 2 305 ? 3.521 17.033 34.663 1.00 92.80 ? 305 ASN B N 1 ATOM 9559 C CA . ASN B 2 305 ? 3.059 17.788 35.819 1.00 91.67 ? 305 ASN B CA 1 ATOM 9560 C C . ASN B 2 305 ? 4.122 18.769 36.306 1.00 106.60 ? 305 ASN B C 1 ATOM 9561 O O . ASN B 2 305 ? 5.227 18.369 36.670 1.00 108.31 ? 305 ASN B O 1 ATOM 9562 C CB . ASN B 2 305 ? 2.657 16.839 36.949 1.00 97.38 ? 305 ASN B CB 1 ATOM 9563 C CG . ASN B 2 305 ? 1.425 16.022 36.614 1.00 109.90 ? 305 ASN B CG 1 ATOM 9564 O OD1 . ASN B 2 305 ? 1.519 14.844 36.266 1.00 130.77 ? 305 ASN B OD1 1 ATOM 9565 N ND2 . ASN B 2 305 ? 0.258 16.647 36.715 1.00 112.35 ? 305 ASN B ND2 1 ATOM 9566 N N . LEU B 2 306 ? 3.784 20.055 36.304 1.00 99.83 ? 306 LEU B N 1 ATOM 9567 C CA . LEU B 2 306 ? 4.712 21.091 36.741 1.00 80.20 ? 306 LEU B CA 1 ATOM 9568 C C . LEU B 2 306 ? 4.617 21.309 38.246 1.00 88.87 ? 306 LEU B C 1 ATOM 9569 O O . LEU B 2 306 ? 3.523 21.378 38.805 1.00 97.15 ? 306 LEU B O 1 ATOM 9570 C CB . LEU B 2 306 ? 4.443 22.403 35.999 1.00 87.56 ? 306 LEU B CB 1 ATOM 9571 C CG . LEU B 2 306 ? 5.308 23.606 36.383 1.00 71.54 ? 306 LEU B CG 1 ATOM 9572 C CD1 . LEU B 2 306 ? 6.776 23.317 36.113 1.00 71.29 ? 306 LEU B CD1 1 ATOM 9573 C CD2 . LEU B 2 306 ? 4.857 24.854 35.639 1.00 67.47 ? 306 LEU B CD2 1 ATOM 9574 N N . ILE B 2 307 ? 5.770 21.411 38.899 1.00 102.72 ? 307 ILE B N 1 ATOM 9575 C CA . ILE B 2 307 ? 5.817 21.631 40.340 1.00 96.40 ? 307 ILE B CA 1 ATOM 9576 C C . ILE B 2 307 ? 6.637 22.869 40.680 1.00 93.65 ? 307 ILE B C 1 ATOM 9577 O O . ILE B 2 307 ? 7.794 22.986 40.280 1.00 79.32 ? 307 ILE B O 1 ATOM 9578 C CB . ILE B 2 307 ? 6.413 20.418 41.079 1.00 90.25 ? 307 ILE B CB 1 ATOM 9579 C CG1 . ILE B 2 307 ? 5.561 19.171 40.831 1.00 101.94 ? 307 ILE B CG1 1 ATOM 9580 C CG2 . ILE B 2 307 ? 6.519 20.701 42.568 1.00 92.89 ? 307 ILE B CG2 1 ATOM 9581 C CD1 . ILE B 2 307 ? 6.074 17.931 41.528 1.00 108.87 ? 307 ILE B CD1 1 ATOM 9582 N N . PHE B 2 308 ? 6.031 23.795 41.415 1.00 97.36 ? 308 PHE B N 1 ATOM 9583 C CA . PHE B 2 308 ? 6.733 24.993 41.852 1.00 82.74 ? 308 PHE B CA 1 ATOM 9584 C C . PHE B 2 308 ? 7.300 24.829 43.257 1.00 94.12 ? 308 PHE B C 1 ATOM 9585 O O . PHE B 2 308 ? 6.552 24.742 44.230 1.00 101.19 ? 308 PHE B O 1 ATOM 9586 C CB . PHE B 2 308 ? 5.806 26.211 41.812 1.00 78.03 ? 308 PHE B CB 1 ATOM 9587 C CG . PHE B 2 308 ? 5.506 26.704 40.427 1.00 89.58 ? 308 PHE B CG 1 ATOM 9588 C CD1 . PHE B 2 308 ? 6.434 27.464 39.735 1.00 97.26 ? 308 PHE B CD1 1 ATOM 9589 C CD2 . PHE B 2 308 ? 4.293 26.422 39.824 1.00 111.48 ? 308 PHE B CD2 1 ATOM 9590 C CE1 . PHE B 2 308 ? 6.164 27.925 38.462 1.00 94.41 ? 308 PHE B CE1 1 ATOM 9591 C CE2 . PHE B 2 308 ? 4.014 26.881 38.551 1.00 103.34 ? 308 PHE B CE2 1 ATOM 9592 C CZ . PHE B 2 308 ? 4.951 27.635 37.870 1.00 83.03 ? 308 PHE B CZ 1 ATOM 9593 N N . ALA B 2 309 ? 8.623 24.790 43.358 1.00 93.51 ? 309 ALA B N 1 ATOM 9594 C CA . ALA B 2 309 ? 9.282 24.817 44.655 1.00 92.48 ? 309 ALA B CA 1 ATOM 9595 C C . ALA B 2 309 ? 9.990 26.153 44.803 1.00 104.01 ? 309 ALA B C 1 ATOM 9596 O O . ALA B 2 309 ? 11.011 26.392 44.166 1.00 116.30 ? 309 ALA B O 1 ATOM 9597 C CB . ALA B 2 309 ? 10.261 23.665 44.791 1.00 88.67 ? 309 ALA B CB 1 ATOM 9598 N N . VAL B 2 310 ? 9.455 27.020 45.656 1.00 102.99 ? 310 VAL B N 1 ATOM 9599 C CA . VAL B 2 310 ? 9.924 28.398 45.711 1.00 94.66 ? 310 VAL B CA 1 ATOM 9600 C C . VAL B 2 310 ? 10.150 28.893 47.136 1.00 100.79 ? 310 VAL B C 1 ATOM 9601 O O . VAL B 2 310 ? 9.659 28.302 48.098 1.00 100.80 ? 310 VAL B O 1 ATOM 9602 C CB . VAL B 2 310 ? 8.931 29.343 45.010 1.00 91.36 ? 310 VAL B CB 1 ATOM 9603 C CG1 . VAL B 2 310 ? 8.985 29.150 43.503 1.00 85.74 ? 310 VAL B CG1 1 ATOM 9604 C CG2 . VAL B 2 310 ? 7.526 29.103 45.527 1.00 88.80 ? 310 VAL B CG2 1 ATOM 9605 N N . THR B 2 311 ? 10.894 29.988 47.258 1.00 105.77 ? 311 THR B N 1 ATOM 9606 C CA . THR B 2 311 ? 11.215 30.568 48.557 1.00 111.21 ? 311 THR B CA 1 ATOM 9607 C C . THR B 2 311 ? 9.982 31.198 49.203 1.00 107.86 ? 311 THR B C 1 ATOM 9608 O O . THR B 2 311 ? 9.008 31.516 48.523 1.00 103.09 ? 311 THR B O 1 ATOM 9609 C CB . THR B 2 311 ? 12.331 31.623 48.443 1.00 117.80 ? 311 THR B CB 1 ATOM 9610 O OG1 . THR B 2 311 ? 11.931 32.654 47.532 1.00 129.72 ? 311 THR B OG1 1 ATOM 9611 C CG2 . THR B 2 311 ? 13.619 30.985 47.943 1.00 121.10 ? 311 THR B CG2 1 ATOM 9612 N N . GLU B 2 312 ? 10.042 31.376 50.520 1.00 110.13 ? 312 GLU B N 1 ATOM 9613 C CA . GLU B 2 312 ? 8.894 31.817 51.310 1.00 111.93 ? 312 GLU B CA 1 ATOM 9614 C C . GLU B 2 312 ? 8.396 33.212 50.928 1.00 121.59 ? 312 GLU B C 1 ATOM 9615 O O . GLU B 2 312 ? 7.238 33.551 51.166 1.00 126.96 ? 312 GLU B O 1 ATOM 9616 C CB . GLU B 2 312 ? 9.246 31.785 52.801 1.00 116.99 ? 312 GLU B CB 1 ATOM 9617 C CG . GLU B 2 312 ? 8.165 31.191 53.692 1.00 135.10 ? 312 GLU B CG 1 ATOM 9618 C CD . GLU B 2 312 ? 6.927 32.062 53.778 1.00 142.66 ? 312 GLU B CD 1 ATOM 9619 O OE1 . GLU B 2 312 ? 5.807 31.518 53.668 1.00 146.30 ? 312 GLU B OE1 1 ATOM 9620 O OE2 . GLU B 2 312 ? 7.071 33.289 53.961 1.00 138.28 ? 312 GLU B OE2 1 ATOM 9621 N N . ASN B 2 313 ? 9.271 34.020 50.340 1.00 118.25 ? 313 ASN B N 1 ATOM 9622 C CA . ASN B 2 313 ? 8.895 35.372 49.952 1.00 96.31 ? 313 ASN B CA 1 ATOM 9623 C C . ASN B 2 313 ? 8.041 35.390 48.685 1.00 92.44 ? 313 ASN B C 1 ATOM 9624 O O . ASN B 2 313 ? 7.045 36.110 48.607 1.00 103.70 ? 313 ASN B O 1 ATOM 9625 C CB . ASN B 2 313 ? 10.142 36.240 49.761 1.00 92.50 ? 313 ASN B CB 1 ATOM 9626 C CG . ASN B 2 313 ? 11.057 35.720 48.670 1.00 97.70 ? 313 ASN B CG 1 ATOM 9627 O OD1 . ASN B 2 313 ? 11.860 34.817 48.895 1.00 107.24 ? 313 ASN B OD1 1 ATOM 9628 N ND2 . ASN B 2 313 ? 10.939 36.293 47.476 1.00 94.34 ? 313 ASN B ND2 1 ATOM 9629 N N . VAL B 2 314 ? 8.431 34.590 47.700 1.00 92.74 ? 314 VAL B N 1 ATOM 9630 C CA . VAL B 2 314 ? 7.773 34.586 46.400 1.00 89.32 ? 314 VAL B CA 1 ATOM 9631 C C . VAL B 2 314 ? 6.731 33.466 46.277 1.00 95.25 ? 314 VAL B C 1 ATOM 9632 O O . VAL B 2 314 ? 6.093 33.308 45.234 1.00 85.95 ? 314 VAL B O 1 ATOM 9633 C CB . VAL B 2 314 ? 8.819 34.466 45.266 1.00 90.09 ? 314 VAL B CB 1 ATOM 9634 C CG1 . VAL B 2 314 ? 9.208 33.011 45.039 1.00 95.19 ? 314 VAL B CG1 1 ATOM 9635 C CG2 . VAL B 2 314 ? 8.307 35.106 43.984 1.00 100.11 ? 314 VAL B CG2 1 ATOM 9636 N N . VAL B 2 315 ? 6.551 32.700 47.351 1.00 99.54 ? 315 VAL B N 1 ATOM 9637 C CA . VAL B 2 315 ? 5.661 31.538 47.318 1.00 96.08 ? 315 VAL B CA 1 ATOM 9638 C C . VAL B 2 315 ? 4.199 31.931 47.088 1.00 104.69 ? 315 VAL B C 1 ATOM 9639 O O . VAL B 2 315 ? 3.446 31.193 46.452 1.00 105.82 ? 315 VAL B O 1 ATOM 9640 C CB . VAL B 2 315 ? 5.779 30.699 48.620 1.00 121.18 ? 315 VAL B CB 1 ATOM 9641 C CG1 . VAL B 2 315 ? 5.283 31.480 49.825 1.00 127.59 ? 315 VAL B CG1 1 ATOM 9642 C CG2 . VAL B 2 315 ? 5.022 29.384 48.484 1.00 111.96 ? 315 VAL B CG2 1 ATOM 9643 N N . ASN B 2 316 ? 3.805 33.099 47.587 1.00 105.90 ? 316 ASN B N 1 ATOM 9644 C CA . ASN B 2 316 ? 2.439 33.575 47.419 1.00 97.77 ? 316 ASN B CA 1 ATOM 9645 C C . ASN B 2 316 ? 2.154 33.940 45.965 1.00 101.77 ? 316 ASN B C 1 ATOM 9646 O O . ASN B 2 316 ? 1.033 33.785 45.481 1.00 105.65 ? 316 ASN B O 1 ATOM 9647 C CB . ASN B 2 316 ? 2.180 34.777 48.330 1.00 86.11 ? 316 ASN B CB 1 ATOM 9648 C CG . ASN B 2 316 ? 1.076 34.519 49.337 1.00 95.54 ? 316 ASN B CG 1 ATOM 9649 O OD1 . ASN B 2 316 ? -0.078 34.886 49.115 1.00 121.67 ? 316 ASN B OD1 1 ATOM 9650 N ND2 . ASN B 2 316 ? 1.425 33.885 50.451 1.00 109.42 ? 316 ASN B ND2 1 ATOM 9651 N N . LEU B 2 317 ? 3.183 34.420 45.273 1.00 87.81 ? 317 LEU B N 1 ATOM 9652 C CA . LEU B 2 317 ? 3.071 34.768 43.862 1.00 83.06 ? 317 LEU B CA 1 ATOM 9653 C C . LEU B 2 317 ? 2.816 33.542 42.993 1.00 79.14 ? 317 LEU B C 1 ATOM 9654 O O . LEU B 2 317 ? 1.865 33.509 42.213 1.00 95.37 ? 317 LEU B O 1 ATOM 9655 C CB . LEU B 2 317 ? 4.339 35.479 43.384 1.00 86.93 ? 317 LEU B CB 1 ATOM 9656 C CG . LEU B 2 317 ? 4.432 35.713 41.874 1.00 69.67 ? 317 LEU B CG 1 ATOM 9657 C CD1 . LEU B 2 317 ? 3.360 36.687 41.408 1.00 71.60 ? 317 LEU B CD1 1 ATOM 9658 C CD2 . LEU B 2 317 ? 5.814 36.203 41.485 1.00 66.41 ? 317 LEU B CD2 1 ATOM 9659 N N . TYR B 2 318 ? 3.672 32.535 43.135 1.00 79.43 ? 318 TYR B N 1 ATOM 9660 C CA . TYR B 2 318 ? 3.605 31.346 42.292 1.00 77.81 ? 318 TYR B CA 1 ATOM 9661 C C . TYR B 2 318 ? 2.394 30.472 42.608 1.00 79.06 ? 318 TYR B C 1 ATOM 9662 O O . TYR B 2 318 ? 1.959 29.683 41.769 1.00 80.47 ? 318 TYR B O 1 ATOM 9663 C CB . TYR B 2 318 ? 4.892 30.532 42.420 1.00 78.60 ? 318 TYR B CB 1 ATOM 9664 C CG . TYR B 2 318 ? 6.056 31.143 41.676 1.00 78.94 ? 318 TYR B CG 1 ATOM 9665 C CD1 . TYR B 2 318 ? 6.928 32.020 42.305 1.00 82.09 ? 318 TYR B CD1 1 ATOM 9666 C CD2 . TYR B 2 318 ? 6.273 30.854 40.335 1.00 78.65 ? 318 TYR B CD2 1 ATOM 9667 C CE1 . TYR B 2 318 ? 7.990 32.584 41.621 1.00 81.56 ? 318 TYR B CE1 1 ATOM 9668 C CE2 . TYR B 2 318 ? 7.332 31.412 39.644 1.00 83.62 ? 318 TYR B CE2 1 ATOM 9669 C CZ . TYR B 2 318 ? 8.187 32.278 40.293 1.00 86.06 ? 318 TYR B CZ 1 ATOM 9670 O OH . TYR B 2 318 ? 9.242 32.840 39.611 1.00 80.41 ? 318 TYR B OH 1 ATOM 9671 N N . GLN B 2 319 ? 1.858 30.610 43.817 1.00 85.63 ? 319 GLN B N 1 ATOM 9672 C CA . GLN B 2 319 ? 0.600 29.959 44.160 1.00 101.50 ? 319 GLN B CA 1 ATOM 9673 C C . GLN B 2 319 ? -0.509 30.522 43.285 1.00 95.76 ? 319 GLN B C 1 ATOM 9674 O O . GLN B 2 319 ? -1.283 29.779 42.682 1.00 106.69 ? 319 GLN B O 1 ATOM 9675 C CB . GLN B 2 319 ? 0.260 30.151 45.641 1.00 90.52 ? 319 GLN B CB 1 ATOM 9676 C CG . GLN B 2 319 ? 0.915 29.148 46.576 1.00 96.00 ? 319 GLN B CG 1 ATOM 9677 C CD . GLN B 2 319 ? 0.336 29.196 47.978 1.00 119.21 ? 319 GLN B CD 1 ATOM 9678 O OE1 . GLN B 2 319 ? -0.641 29.900 48.234 1.00 138.81 ? 319 GLN B OE1 1 ATOM 9679 N NE2 . GLN B 2 319 ? 0.935 28.443 48.894 1.00 123.13 ? 319 GLN B NE2 1 ATOM 9680 N N . ASN B 2 320 ? -0.571 31.847 43.218 1.00 92.24 ? 320 ASN B N 1 ATOM 9681 C CA . ASN B 2 320 ? -1.547 32.531 42.383 1.00 82.92 ? 320 ASN B CA 1 ATOM 9682 C C . ASN B 2 320 ? -1.265 32.303 40.901 1.00 76.42 ? 320 ASN B C 1 ATOM 9683 O O . ASN B 2 320 ? -2.182 32.303 40.077 1.00 86.34 ? 320 ASN B O 1 ATOM 9684 C CB . ASN B 2 320 ? -1.559 34.025 42.709 1.00 73.43 ? 320 ASN B CB 1 ATOM 9685 C CG . ASN B 2 320 ? -2.415 34.346 43.918 1.00 97.33 ? 320 ASN B CG 1 ATOM 9686 O OD1 . ASN B 2 320 ? -2.980 33.451 44.545 1.00 114.01 ? 320 ASN B OD1 1 ATOM 9687 N ND2 . ASN B 2 320 ? -2.514 35.626 44.254 1.00 129.17 ? 320 ASN B ND2 1 ATOM 9688 N N . TYR B 2 321 ? 0.009 32.107 40.573 1.00 81.21 ? 321 TYR B N 1 ATOM 9689 C CA . TYR B 2 321 ? 0.412 31.755 39.216 1.00 80.11 ? 321 TYR B CA 1 ATOM 9690 C C . TYR B 2 321 ? -0.090 30.363 38.851 1.00 71.75 ? 321 TYR B C 1 ATOM 9691 O O . TYR B 2 321 ? -0.531 30.124 37.727 1.00 92.17 ? 321 TYR B O 1 ATOM 9692 C CB . TYR B 2 321 ? 1.936 31.815 39.070 1.00 94.79 ? 321 TYR B CB 1 ATOM 9693 C CG . TYR B 2 321 ? 2.463 33.106 38.483 1.00 89.09 ? 321 TYR B CG 1 ATOM 9694 C CD1 . TYR B 2 321 ? 1.745 33.799 37.518 1.00 76.26 ? 321 TYR B CD1 1 ATOM 9695 C CD2 . TYR B 2 321 ? 3.683 33.630 38.893 1.00 101.88 ? 321 TYR B CD2 1 ATOM 9696 C CE1 . TYR B 2 321 ? 2.225 34.979 36.980 1.00 93.15 ? 321 TYR B CE1 1 ATOM 9697 C CE2 . TYR B 2 321 ? 4.172 34.808 38.359 1.00 91.89 ? 321 TYR B CE2 1 ATOM 9698 C CZ . TYR B 2 321 ? 3.438 35.478 37.403 1.00 87.95 ? 321 TYR B CZ 1 ATOM 9699 O OH . TYR B 2 321 ? 3.918 36.651 36.868 1.00 86.09 ? 321 TYR B OH 1 ATOM 9700 N N . SER B 2 322 ? -0.023 29.450 39.816 1.00 80.09 ? 322 SER B N 1 ATOM 9701 C CA . SER B 2 322 ? -0.408 28.059 39.599 1.00 90.89 ? 322 SER B CA 1 ATOM 9702 C C . SER B 2 322 ? -1.905 27.900 39.360 1.00 90.24 ? 322 SER B C 1 ATOM 9703 O O . SER B 2 322 ? -2.336 26.961 38.694 1.00 95.65 ? 322 SER B O 1 ATOM 9704 C CB . SER B 2 322 ? 0.015 27.201 40.792 1.00 84.07 ? 322 SER B CB 1 ATOM 9705 O OG . SER B 2 322 ? -0.579 27.671 41.990 1.00 109.99 ? 322 SER B OG 1 ATOM 9706 N N . GLU B 2 323 ? -2.693 28.818 39.910 1.00 89.96 ? 323 GLU B N 1 ATOM 9707 C CA . GLU B 2 323 ? -4.143 28.767 39.757 1.00 87.71 ? 323 GLU B CA 1 ATOM 9708 C C . GLU B 2 323 ? -4.553 28.968 38.301 1.00 84.12 ? 323 GLU B C 1 ATOM 9709 O O . GLU B 2 323 ? -5.648 28.577 37.896 1.00 79.78 ? 323 GLU B O 1 ATOM 9710 C CB . GLU B 2 323 ? -4.814 29.818 40.644 1.00 80.64 ? 323 GLU B CB 1 ATOM 9711 C CG . GLU B 2 323 ? -4.555 29.636 42.131 1.00 108.52 ? 323 GLU B CG 1 ATOM 9712 C CD . GLU B 2 323 ? -5.319 30.629 42.985 1.00 140.97 ? 323 GLU B CD 1 ATOM 9713 O OE1 . GLU B 2 323 ? -6.303 31.212 42.482 1.00 155.35 ? 323 GLU B OE1 1 ATOM 9714 O OE2 . GLU B 2 323 ? -4.935 30.829 44.156 1.00 142.80 ? 323 GLU B OE2 1 ATOM 9715 N N . LEU B 2 324 ? -3.669 29.579 37.519 1.00 87.71 ? 324 LEU B N 1 ATOM 9716 C CA . LEU B 2 324 ? -3.921 29.792 36.100 1.00 92.57 ? 324 LEU B CA 1 ATOM 9717 C C . LEU B 2 324 ? -3.403 28.622 35.267 1.00 82.04 ? 324 LEU B C 1 ATOM 9718 O O . LEU B 2 324 ? -3.686 28.522 34.073 1.00 96.43 ? 324 LEU B O 1 ATOM 9719 C CB . LEU B 2 324 ? -3.280 31.102 35.636 1.00 72.97 ? 324 LEU B CB 1 ATOM 9720 C CG . LEU B 2 324 ? -3.886 32.386 36.209 1.00 73.95 ? 324 LEU B CG 1 ATOM 9721 C CD1 . LEU B 2 324 ? -3.106 33.607 35.751 1.00 97.72 ? 324 LEU B CD1 1 ATOM 9722 C CD2 . LEU B 2 324 ? -5.347 32.505 35.810 1.00 75.48 ? 324 LEU B CD2 1 ATOM 9723 N N . ILE B 2 325 ? -2.646 27.737 35.906 1.00 71.88 ? 325 ILE B N 1 ATOM 9724 C CA . ILE B 2 325 ? -2.129 26.544 35.245 1.00 77.79 ? 325 ILE B CA 1 ATOM 9725 C C . ILE B 2 325 ? -2.536 25.302 36.034 1.00 84.21 ? 325 ILE B C 1 ATOM 9726 O O . ILE B 2 325 ? -1.795 24.850 36.907 1.00 111.09 ? 325 ILE B O 1 ATOM 9727 C CB . ILE B 2 325 ? -0.590 26.584 35.100 1.00 92.03 ? 325 ILE B CB 1 ATOM 9728 C CG1 . ILE B 2 325 ? -0.126 27.959 34.609 1.00 81.83 ? 325 ILE B CG1 1 ATOM 9729 C CG2 . ILE B 2 325 ? -0.106 25.487 34.159 1.00 97.80 ? 325 ILE B CG2 1 ATOM 9730 C CD1 . ILE B 2 325 ? 1.380 28.097 34.507 1.00 79.59 ? 325 ILE B CD1 1 ATOM 9731 N N . PRO B 2 326 ? -3.725 24.754 35.732 1.00 81.08 ? 326 PRO B N 1 ATOM 9732 C CA . PRO B 2 326 ? -4.293 23.597 36.436 1.00 97.64 ? 326 PRO B CA 1 ATOM 9733 C C . PRO B 2 326 ? -3.363 22.387 36.450 1.00 108.50 ? 326 PRO B C 1 ATOM 9734 O O . PRO B 2 326 ? -2.625 22.167 35.490 1.00 123.45 ? 326 PRO B O 1 ATOM 9735 C CB . PRO B 2 326 ? -5.563 23.289 35.635 1.00 106.24 ? 326 PRO B CB 1 ATOM 9736 C CG . PRO B 2 326 ? -5.923 24.579 34.990 1.00 91.03 ? 326 PRO B CG 1 ATOM 9737 C CD . PRO B 2 326 ? -4.621 25.246 34.671 1.00 79.33 ? 326 PRO B CD 1 ATOM 9738 N N . GLY B 2 327 ? -3.402 21.615 37.532 1.00 96.82 ? 327 GLY B N 1 ATOM 9739 C CA . GLY B 2 327 ? -2.573 20.432 37.654 1.00 124.37 ? 327 GLY B CA 1 ATOM 9740 C C . GLY B 2 327 ? -1.203 20.722 38.237 1.00 129.77 ? 327 GLY B C 1 ATOM 9741 O O . GLY B 2 327 ? -0.398 19.810 38.431 1.00 133.51 ? 327 GLY B O 1 ATOM 9742 N N . THR B 2 328 ? -0.936 21.993 38.520 1.00 94.70 ? 328 THR B N 1 ATOM 9743 C CA . THR B 2 328 ? 0.346 22.394 39.087 1.00 99.73 ? 328 THR B CA 1 ATOM 9744 C C . THR B 2 328 ? 0.199 22.799 40.549 1.00 105.61 ? 328 THR B C 1 ATOM 9745 O O . THR B 2 328 ? -0.734 23.513 40.915 1.00 104.65 ? 328 THR B O 1 ATOM 9746 C CB . THR B 2 328 ? 0.976 23.560 38.303 1.00 90.25 ? 328 THR B CB 1 ATOM 9747 O OG1 . THR B 2 328 ? 0.199 24.749 38.497 1.00 99.60 ? 328 THR B OG1 1 ATOM 9748 C CG2 . THR B 2 328 ? 1.035 23.232 36.823 1.00 89.36 ? 328 THR B CG2 1 ATOM 9749 N N . THR B 2 329 ? 1.129 22.338 41.381 1.00 98.38 ? 329 THR B N 1 ATOM 9750 C CA . THR B 2 329 ? 1.098 22.633 42.809 1.00 90.72 ? 329 THR B CA 1 ATOM 9751 C C . THR B 2 329 ? 2.359 23.371 43.252 1.00 88.35 ? 329 THR B C 1 ATOM 9752 O O . THR B 2 329 ? 3.403 23.282 42.606 1.00 86.02 ? 329 THR B O 1 ATOM 9753 C CB . THR B 2 329 ? 0.941 21.348 43.643 1.00 97.15 ? 329 THR B CB 1 ATOM 9754 O OG1 . THR B 2 329 ? 1.097 21.657 45.034 1.00 112.59 ? 329 THR B OG1 1 ATOM 9755 C CG2 . THR B 2 329 ? 1.984 20.320 43.239 1.00 98.53 ? 329 THR B CG2 1 ATOM 9756 N N . VAL B 2 330 ? 2.250 24.101 44.357 1.00 89.36 ? 330 VAL B N 1 ATOM 9757 C CA . VAL B 2 330 ? 3.355 24.908 44.865 1.00 87.50 ? 330 VAL B CA 1 ATOM 9758 C C . VAL B 2 330 ? 3.723 24.477 46.283 1.00 92.72 ? 330 VAL B C 1 ATOM 9759 O O . VAL B 2 330 ? 2.873 23.988 47.026 1.00 97.29 ? 330 VAL B O 1 ATOM 9760 C CB . VAL B 2 330 ? 3.004 26.412 44.859 1.00 86.29 ? 330 VAL B CB 1 ATOM 9761 C CG1 . VAL B 2 330 ? 4.248 27.262 45.067 1.00 86.25 ? 330 VAL B CG1 1 ATOM 9762 C CG2 . VAL B 2 330 ? 2.328 26.789 43.552 1.00 80.14 ? 330 VAL B CG2 1 ATOM 9763 N N . GLY B 2 331 ? 4.987 24.660 46.654 1.00 92.48 ? 331 GLY B N 1 ATOM 9764 C CA . GLY B 2 331 ? 5.443 24.322 47.989 1.00 113.09 ? 331 GLY B CA 1 ATOM 9765 C C . GLY B 2 331 ? 6.585 25.208 48.449 1.00 96.18 ? 331 GLY B C 1 ATOM 9766 O O . GLY B 2 331 ? 7.291 25.801 47.634 1.00 91.81 ? 331 GLY B O 1 ATOM 9767 N N . VAL B 2 332 ? 6.769 25.287 49.762 1.00 100.74 ? 332 VAL B N 1 ATOM 9768 C CA . VAL B 2 332 ? 7.728 26.212 50.353 1.00 100.34 ? 332 VAL B CA 1 ATOM 9769 C C . VAL B 2 332 ? 9.131 25.620 50.449 1.00 115.86 ? 332 VAL B C 1 ATOM 9770 O O . VAL B 2 332 ? 9.318 24.522 50.975 1.00 134.60 ? 332 VAL B O 1 ATOM 9771 C CB . VAL B 2 332 ? 7.274 26.653 51.761 1.00 118.20 ? 332 VAL B CB 1 ATOM 9772 C CG1 . VAL B 2 332 ? 8.298 27.584 52.390 1.00 120.58 ? 332 VAL B CG1 1 ATOM 9773 C CG2 . VAL B 2 332 ? 5.912 27.324 51.687 1.00 125.96 ? 332 VAL B CG2 1 ATOM 9774 N N . LEU B 2 333 ? 10.112 26.353 49.932 1.00 118.11 ? 333 LEU B N 1 ATOM 9775 C CA . LEU B 2 333 ? 11.509 25.951 50.037 1.00 110.07 ? 333 LEU B CA 1 ATOM 9776 C C . LEU B 2 333 ? 12.204 26.783 51.112 1.00 116.04 ? 333 LEU B C 1 ATOM 9777 O O . LEU B 2 333 ? 12.451 27.974 50.921 1.00 124.43 ? 333 LEU B O 1 ATOM 9778 C CB . LEU B 2 333 ? 12.216 26.116 48.689 1.00 106.00 ? 333 LEU B CB 1 ATOM 9779 C CG . LEU B 2 333 ? 13.422 25.224 48.389 1.00 105.38 ? 333 LEU B CG 1 ATOM 9780 C CD1 . LEU B 2 333 ? 12.971 23.807 48.067 1.00 119.78 ? 333 LEU B CD1 1 ATOM 9781 C CD2 . LEU B 2 333 ? 14.244 25.801 47.248 1.00 105.14 ? 333 LEU B CD2 1 ATOM 9782 N N . SER B 2 334 ? 12.515 26.154 52.242 1.00 122.99 ? 334 SER B N 1 ATOM 9783 C CA . SER B 2 334 ? 13.143 26.857 53.357 1.00 140.87 ? 334 SER B CA 1 ATOM 9784 C C . SER B 2 334 ? 13.870 25.898 54.295 1.00 142.34 ? 334 SER B C 1 ATOM 9785 O O . SER B 2 334 ? 13.602 24.696 54.300 1.00 134.56 ? 334 SER B O 1 ATOM 9786 C CB . SER B 2 334 ? 12.098 27.660 54.138 1.00 142.77 ? 334 SER B CB 1 ATOM 9787 O OG . SER B 2 334 ? 11.056 26.823 54.605 1.00 132.86 ? 334 SER B OG 1 ATOM 9788 N N . MET B 2 335 ? 14.789 26.440 55.090 1.00 140.11 ? 335 MET B N 1 ATOM 9789 C CA . MET B 2 335 ? 15.567 25.633 56.023 1.00 150.85 ? 335 MET B CA 1 ATOM 9790 C C . MET B 2 335 ? 14.712 25.140 57.183 1.00 162.42 ? 335 MET B C 1 ATOM 9791 O O . MET B 2 335 ? 14.959 24.063 57.728 1.00 165.79 ? 335 MET B O 1 ATOM 9792 C CB . MET B 2 335 ? 16.768 26.421 56.546 1.00 148.15 ? 335 MET B CB 1 ATOM 9793 C CG . MET B 2 335 ? 17.932 26.475 55.570 1.00 136.14 ? 335 MET B CG 1 ATOM 9794 S SD . MET B 2 335 ? 19.343 27.403 56.199 1.00 183.79 ? 335 MET B SD 1 ATOM 9795 C CE . MET B 2 335 ? 19.613 26.589 57.772 1.00 143.60 ? 335 MET B CE 1 ATOM 9796 N N . ASP B 2 336 ? 13.711 25.924 57.568 1.00 162.19 ? 336 ASP B N 1 ATOM 9797 C CA . ASP B 2 336 ? 12.727 25.433 58.521 1.00 173.91 ? 336 ASP B CA 1 ATOM 9798 C C . ASP B 2 336 ? 11.466 25.065 57.755 1.00 170.53 ? 336 ASP B C 1 ATOM 9799 O O . ASP B 2 336 ? 10.686 25.934 57.360 1.00 155.29 ? 336 ASP B O 1 ATOM 9800 C CB . ASP B 2 336 ? 12.424 26.481 59.594 1.00 167.65 ? 336 ASP B CB 1 ATOM 9801 C CG . ASP B 2 336 ? 11.738 25.890 60.813 1.00 167.71 ? 336 ASP B CG 1 ATOM 9802 O OD1 . ASP B 2 336 ? 12.025 26.353 61.938 1.00 166.56 ? 336 ASP B OD1 1 ATOM 9803 O OD2 . ASP B 2 336 ? 10.914 24.963 60.655 1.00 158.90 ? 336 ASP B OD2 1 ATOM 9804 N N . SER B 2 337 ? 11.274 23.759 57.589 1.00 178.68 ? 337 SER B N 1 ATOM 9805 C CA . SER B 2 337 ? 10.202 23.183 56.783 1.00 168.53 ? 337 SER B CA 1 ATOM 9806 C C . SER B 2 337 ? 10.418 21.679 56.715 1.00 179.67 ? 337 SER B C 1 ATOM 9807 O O . SER B 2 337 ? 11.403 21.162 57.243 1.00 166.17 ? 337 SER B O 1 ATOM 9808 C CB . SER B 2 337 ? 10.165 23.771 55.368 1.00 162.85 ? 337 SER B CB 1 ATOM 9809 O OG . SER B 2 337 ? 9.630 25.084 55.365 1.00 173.28 ? 337 SER B OG 1 ATOM 9810 N N . SER B 2 338 ? 9.499 20.980 56.062 1.00 193.05 ? 338 SER B N 1 ATOM 9811 C CA . SER B 2 338 ? 9.719 19.584 55.707 1.00 191.80 ? 338 SER B CA 1 ATOM 9812 C C . SER B 2 338 ? 10.713 19.501 54.542 1.00 177.98 ? 338 SER B C 1 ATOM 9813 O O . SER B 2 338 ? 11.143 18.416 54.146 1.00 179.41 ? 338 SER B O 1 ATOM 9814 C CB . SER B 2 338 ? 8.395 18.907 55.353 1.00 186.09 ? 338 SER B CB 1 ATOM 9815 O OG . SER B 2 338 ? 7.484 18.970 56.436 1.00 183.58 ? 338 SER B OG 1 ATOM 9816 N N . ASN B 2 339 ? 11.064 20.671 54.013 1.00 156.91 ? 339 ASN B N 1 ATOM 9817 C CA . ASN B 2 339 ? 12.050 20.850 52.948 1.00 157.63 ? 339 ASN B CA 1 ATOM 9818 C C . ASN B 2 339 ? 11.772 20.047 51.679 1.00 176.08 ? 339 ASN B C 1 ATOM 9819 O O . ASN B 2 339 ? 10.621 19.827 51.327 1.00 191.94 ? 339 ASN B O 1 ATOM 9820 C CB . ASN B 2 339 ? 13.446 20.498 53.474 1.00 170.63 ? 339 ASN B CB 1 ATOM 9821 C CG . ASN B 2 339 ? 14.552 21.234 52.745 1.00 173.48 ? 339 ASN B CG 1 ATOM 9822 O OD1 . ASN B 2 339 ? 14.331 21.820 51.684 1.00 165.26 ? 339 ASN B OD1 1 ATOM 9823 N ND2 . ASN B 2 339 ? 15.754 21.194 53.305 1.00 159.23 ? 339 ASN B ND2 1 ATOM 9824 N N . VAL B 2 340 ? 12.836 19.560 51.044 1.00 184.58 ? 340 VAL B N 1 ATOM 9825 C CA . VAL B 2 340 ? 12.776 19.037 49.679 1.00 176.42 ? 340 VAL B CA 1 ATOM 9826 C C . VAL B 2 340 ? 12.289 17.590 49.638 1.00 168.20 ? 340 VAL B C 1 ATOM 9827 O O . VAL B 2 340 ? 11.784 17.114 48.620 1.00 168.10 ? 340 VAL B O 1 ATOM 9828 C CB . VAL B 2 340 ? 14.165 19.167 48.987 1.00 134.03 ? 340 VAL B CB 1 ATOM 9829 C CG1 . VAL B 2 340 ? 14.740 17.808 48.616 1.00 135.86 ? 340 VAL B CG1 1 ATOM 9830 C CG2 . VAL B 2 340 ? 14.075 20.070 47.763 1.00 114.48 ? 340 VAL B CG2 1 ATOM 9831 N N . LEU B 2 341 ? 12.392 16.912 50.772 1.00 150.67 ? 341 LEU B N 1 ATOM 9832 C CA . LEU B 2 341 ? 12.045 15.503 50.848 1.00 165.84 ? 341 LEU B CA 1 ATOM 9833 C C . LEU B 2 341 ? 10.533 15.301 50.769 1.00 177.67 ? 341 LEU B C 1 ATOM 9834 O O . LEU B 2 341 ? 10.024 14.688 49.828 1.00 181.29 ? 341 LEU B O 1 ATOM 9835 C CB . LEU B 2 341 ? 12.604 14.903 52.135 1.00 171.91 ? 341 LEU B CB 1 ATOM 9836 C CG . LEU B 2 341 ? 14.122 15.062 52.242 1.00 183.41 ? 341 LEU B CG 1 ATOM 9837 C CD1 . LEU B 2 341 ? 14.660 14.480 53.541 1.00 192.18 ? 341 LEU B CD1 1 ATOM 9838 C CD2 . LEU B 2 341 ? 14.790 14.423 51.040 1.00 187.79 ? 341 LEU B CD2 1 ATOM 9839 N N . GLN B 2 342 ? 9.820 15.812 51.766 1.00 180.57 ? 342 GLN B N 1 ATOM 9840 C CA . GLN B 2 342 ? 8.364 15.766 51.771 1.00 174.71 ? 342 GLN B CA 1 ATOM 9841 C C . GLN B 2 342 ? 7.767 16.528 50.591 1.00 165.38 ? 342 GLN B C 1 ATOM 9842 O O . GLN B 2 342 ? 6.838 16.046 49.941 1.00 170.40 ? 342 GLN B O 1 ATOM 9843 C CB . GLN B 2 342 ? 7.820 16.335 53.081 1.00 173.41 ? 342 GLN B CB 1 ATOM 9844 C CG . GLN B 2 342 ? 7.474 15.304 54.156 1.00 160.04 ? 342 GLN B CG 1 ATOM 9845 C CD . GLN B 2 342 ? 7.883 13.885 53.794 1.00 165.73 ? 342 GLN B CD 1 ATOM 9846 O OE1 . GLN B 2 342 ? 9.046 13.506 53.935 1.00 169.06 ? 342 GLN B OE1 1 ATOM 9847 N NE2 . GLN B 2 342 ? 6.922 13.090 53.332 1.00 175.07 ? 342 GLN B NE2 1 ATOM 9848 N N . LEU B 2 343 ? 8.311 17.713 50.322 1.00 140.00 ? 343 LEU B N 1 ATOM 9849 C CA . LEU B 2 343 ? 7.771 18.629 49.314 1.00 134.44 ? 343 LEU B CA 1 ATOM 9850 C C . LEU B 2 343 ? 7.487 17.977 47.973 1.00 127.72 ? 343 LEU B C 1 ATOM 9851 O O . LEU B 2 343 ? 6.413 18.149 47.411 1.00 125.52 ? 343 LEU B O 1 ATOM 9852 C CB . LEU B 2 343 ? 8.737 19.797 49.108 1.00 137.48 ? 343 LEU B CB 1 ATOM 9853 C CG . LEU B 2 343 ? 8.738 20.583 47.796 1.00 140.72 ? 343 LEU B CG 1 ATOM 9854 C CD1 . LEU B 2 343 ? 7.519 21.462 47.686 1.00 154.56 ? 343 LEU B CD1 1 ATOM 9855 C CD2 . LEU B 2 343 ? 10.004 21.415 47.702 1.00 134.30 ? 343 LEU B CD2 1 ATOM 9856 N N . ILE B 2 344 ? 8.454 17.232 47.459 1.00 127.37 ? 344 ILE B N 1 ATOM 9857 C CA . ILE B 2 344 ? 8.257 16.551 46.184 1.00 122.98 ? 344 ILE B CA 1 ATOM 9858 C C . ILE B 2 344 ? 7.255 15.408 46.347 1.00 123.37 ? 344 ILE B C 1 ATOM 9859 O O . ILE B 2 344 ? 6.348 15.234 45.529 1.00 118.92 ? 344 ILE B O 1 ATOM 9860 C CB . ILE B 2 344 ? 9.584 16.027 45.615 1.00 123.85 ? 344 ILE B CB 1 ATOM 9861 C CG1 . ILE B 2 344 ? 10.277 17.132 44.798 1.00 122.12 ? 344 ILE B CG1 1 ATOM 9862 C CG2 . ILE B 2 344 ? 9.362 14.791 44.763 1.00 121.77 ? 344 ILE B CG2 1 ATOM 9863 C CD1 . ILE B 2 344 ? 11.406 16.640 43.924 1.00 123.20 ? 344 ILE B CD1 1 ATOM 9864 N N . VAL B 2 345 ? 7.414 14.638 47.417 1.00 133.39 ? 345 VAL B N 1 ATOM 9865 C CA . VAL B 2 345 ? 6.506 13.533 47.698 1.00 127.93 ? 345 VAL B CA 1 ATOM 9866 C C . VAL B 2 345 ? 5.073 14.025 47.922 1.00 126.19 ? 345 VAL B C 1 ATOM 9867 O O . VAL B 2 345 ? 4.123 13.477 47.359 1.00 126.17 ? 345 VAL B O 1 ATOM 9868 C CB . VAL B 2 345 ? 6.977 12.727 48.929 1.00 135.31 ? 345 VAL B CB 1 ATOM 9869 C CG1 . VAL B 2 345 ? 5.816 12.000 49.572 1.00 145.79 ? 345 VAL B CG1 1 ATOM 9870 C CG2 . VAL B 2 345 ? 8.073 11.743 48.538 1.00 135.95 ? 345 VAL B CG2 1 ATOM 9871 N N . ASP B 2 346 ? 4.925 15.065 48.737 1.00 129.74 ? 346 ASP B N 1 ATOM 9872 C CA . ASP B 2 346 ? 3.608 15.625 49.019 1.00 130.16 ? 346 ASP B CA 1 ATOM 9873 C C . ASP B 2 346 ? 2.975 16.184 47.753 1.00 122.97 ? 346 ASP B C 1 ATOM 9874 O O . ASP B 2 346 ? 1.760 16.114 47.574 1.00 121.74 ? 346 ASP B O 1 ATOM 9875 C CB . ASP B 2 346 ? 3.703 16.716 50.086 1.00 143.48 ? 346 ASP B CB 1 ATOM 9876 C CG . ASP B 2 346 ? 4.350 16.224 51.363 1.00 159.31 ? 346 ASP B CG 1 ATOM 9877 O OD1 . ASP B 2 346 ? 4.413 14.993 51.565 1.00 157.73 ? 346 ASP B OD1 1 ATOM 9878 O OD2 . ASP B 2 346 ? 4.805 17.068 52.162 1.00 168.95 ? 346 ASP B OD2 1 ATOM 9879 N N . ALA B 2 347 ? 3.807 16.733 46.874 1.00 120.18 ? 347 ALA B N 1 ATOM 9880 C CA . ALA B 2 347 ? 3.331 17.285 45.614 1.00 113.88 ? 347 ALA B CA 1 ATOM 9881 C C . ALA B 2 347 ? 2.833 16.182 44.691 1.00 109.74 ? 347 ALA B C 1 ATOM 9882 O O . ALA B 2 347 ? 1.730 16.260 44.151 1.00 106.02 ? 347 ALA B O 1 ATOM 9883 C CB . ALA B 2 347 ? 4.430 18.083 44.934 1.00 121.14 ? 347 ALA B CB 1 ATOM 9884 N N . TYR B 2 348 ? 3.659 15.156 44.513 1.00 112.32 ? 348 TYR B N 1 ATOM 9885 C CA . TYR B 2 348 ? 3.305 14.012 43.681 1.00 106.71 ? 348 TYR B CA 1 ATOM 9886 C C . TYR B 2 348 ? 2.058 13.312 44.210 1.00 106.16 ? 348 TYR B C 1 ATOM 9887 O O . TYR B 2 348 ? 1.224 12.843 43.438 1.00 102.15 ? 348 TYR B O 1 ATOM 9888 C CB . TYR B 2 348 ? 4.470 13.027 43.605 1.00 109.08 ? 348 TYR B CB 1 ATOM 9889 C CG . TYR B 2 348 ? 4.145 11.746 42.873 1.00 106.81 ? 348 TYR B CG 1 ATOM 9890 C CD1 . TYR B 2 348 ? 3.892 11.749 41.507 1.00 104.23 ? 348 TYR B CD1 1 ATOM 9891 C CD2 . TYR B 2 348 ? 4.099 10.532 43.545 1.00 108.87 ? 348 TYR B CD2 1 ATOM 9892 C CE1 . TYR B 2 348 ? 3.597 10.580 40.833 1.00 102.27 ? 348 TYR B CE1 1 ATOM 9893 C CE2 . TYR B 2 348 ? 3.806 9.357 42.878 1.00 116.72 ? 348 TYR B CE2 1 ATOM 9894 C CZ . TYR B 2 348 ? 3.556 9.386 41.524 1.00 113.98 ? 348 TYR B CZ 1 ATOM 9895 O OH . TYR B 2 348 ? 3.265 8.219 40.858 1.00 112.32 ? 348 TYR B OH 1 ATOM 9896 N N . GLY B 2 349 ? 1.939 13.244 45.532 1.00 111.03 ? 349 GLY B N 1 ATOM 9897 C CA . GLY B 2 349 ? 0.769 12.663 46.162 1.00 111.80 ? 349 GLY B CA 1 ATOM 9898 C C . GLY B 2 349 ? -0.461 13.521 45.934 1.00 109.78 ? 349 GLY B C 1 ATOM 9899 O O . GLY B 2 349 ? -1.563 13.007 45.744 1.00 108.57 ? 349 GLY B O 1 ATOM 9900 N N . LYS B 2 350 ? -0.266 14.835 45.948 1.00 111.73 ? 350 LYS B N 1 ATOM 9901 C CA . LYS B 2 350 ? -1.353 15.777 45.711 1.00 112.07 ? 350 LYS B CA 1 ATOM 9902 C C . LYS B 2 350 ? -1.773 15.763 44.243 1.00 106.33 ? 350 LYS B C 1 ATOM 9903 O O . LYS B 2 350 ? -2.939 15.981 43.919 1.00 105.31 ? 350 LYS B O 1 ATOM 9904 C CB . LYS B 2 350 ? -0.938 17.188 46.135 1.00 112.31 ? 350 LYS B CB 1 ATOM 9905 C CG . LYS B 2 350 ? -2.069 18.203 46.135 1.00 112.29 ? 350 LYS B CG 1 ATOM 9906 C CD . LYS B 2 350 ? -1.616 19.529 46.727 1.00 118.08 ? 350 LYS B CD 1 ATOM 9907 C CE . LYS B 2 350 ? -2.772 20.513 46.826 1.00 125.12 ? 350 LYS B CE 1 ATOM 9908 N NZ . LYS B 2 350 ? -2.365 21.795 47.466 1.00 129.13 ? 350 LYS B NZ 1 ATOM 9909 N N . ILE B 2 351 ? -0.813 15.499 43.362 1.00 113.02 ? 351 ILE B N 1 ATOM 9910 C CA . ILE B 2 351 ? -1.077 15.421 41.928 1.00 101.09 ? 351 ILE B CA 1 ATOM 9911 C C . ILE B 2 351 ? -1.852 14.147 41.589 1.00 95.47 ? 351 ILE B C 1 ATOM 9912 O O . ILE B 2 351 ? -2.731 14.149 40.725 1.00 100.30 ? 351 ILE B O 1 ATOM 9913 C CB . ILE B 2 351 ? 0.237 15.473 41.117 1.00 93.93 ? 351 ILE B CB 1 ATOM 9914 C CG1 . ILE B 2 351 ? 0.846 16.875 41.185 1.00 99.11 ? 351 ILE B CG1 1 ATOM 9915 C CG2 . ILE B 2 351 ? 0.002 15.086 39.668 1.00 96.59 ? 351 ILE B CG2 1 ATOM 9916 C CD1 . ILE B 2 351 ? 2.210 16.984 40.544 1.00 115.37 ? 351 ILE B CD1 1 ATOM 9917 N N . ARG B 2 352 ? -1.540 13.068 42.299 1.00 94.40 ? 352 ARG B N 1 ATOM 9918 C CA . ARG B 2 352 ? -2.202 11.786 42.084 1.00 92.78 ? 352 ARG B CA 1 ATOM 9919 C C . ARG B 2 352 ? -3.470 11.674 42.922 1.00 95.04 ? 352 ARG B C 1 ATOM 9920 O O . ARG B 2 352 ? -4.121 10.632 42.944 1.00 92.57 ? 352 ARG B O 1 ATOM 9921 C CB . ARG B 2 352 ? -1.258 10.627 42.412 1.00 103.69 ? 352 ARG B CB 1 ATOM 9922 C CG . ARG B 2 352 ? -0.162 10.387 41.384 1.00 112.60 ? 352 ARG B CG 1 ATOM 9923 C CD . ARG B 2 352 ? -0.742 9.959 40.046 1.00 120.96 ? 352 ARG B CD 1 ATOM 9924 N NE . ARG B 2 352 ? -0.773 11.056 39.082 1.00 135.97 ? 352 ARG B NE 1 ATOM 9925 C CZ . ARG B 2 352 ? 0.150 11.250 38.146 1.00 138.14 ? 352 ARG B CZ 1 ATOM 9926 N NH1 . ARG B 2 352 ? 0.046 12.273 37.310 1.00 130.13 ? 352 ARG B NH1 1 ATOM 9927 N NH2 . ARG B 2 352 ? 1.176 10.417 38.044 1.00 138.10 ? 352 ARG B NH2 1 ATOM 9928 N N . SER B 2 353 ? -3.813 12.752 43.618 1.00 103.78 ? 353 SER B N 1 ATOM 9929 C CA . SER B 2 353 ? -4.992 12.759 44.476 1.00 112.12 ? 353 SER B CA 1 ATOM 9930 C C . SER B 2 353 ? -6.241 13.217 43.729 1.00 120.09 ? 353 SER B C 1 ATOM 9931 O O . SER B 2 353 ? -7.316 13.337 44.318 1.00 126.86 ? 353 SER B O 1 ATOM 9932 C CB . SER B 2 353 ? -4.757 13.654 45.694 1.00 107.33 ? 353 SER B CB 1 ATOM 9933 O OG . SER B 2 353 ? -4.585 15.005 45.304 1.00 106.95 ? 353 SER B OG 1 ATOM 9934 N N . LYS B 2 354 ? -6.096 13.469 42.433 1.00 120.11 ? 354 LYS B N 1 ATOM 9935 C CA . LYS B 2 354 ? -7.195 13.999 41.633 1.00 108.33 ? 354 LYS B CA 1 ATOM 9936 C C . LYS B 2 354 ? -7.265 13.342 40.256 1.00 108.55 ? 354 LYS B C 1 ATOM 9937 O O . LYS B 2 354 ? -6.237 13.032 39.652 1.00 117.02 ? 354 LYS B O 1 ATOM 9938 C CB . LYS B 2 354 ? -7.048 15.517 41.487 1.00 95.81 ? 354 LYS B CB 1 ATOM 9939 C CG . LYS B 2 354 ? -8.219 16.209 40.813 1.00 98.24 ? 354 LYS B CG 1 ATOM 9940 C CD . LYS B 2 354 ? -8.000 17.712 40.749 1.00 117.15 ? 354 LYS B CD 1 ATOM 9941 C CE . LYS B 2 354 ? -9.179 18.412 40.098 1.00 125.88 ? 354 LYS B CE 1 ATOM 9942 N NZ . LYS B 2 354 ? -9.400 17.939 38.705 1.00 126.20 ? 354 LYS B NZ 1 ATOM 9943 N N . VAL B 2 355 ? -8.483 13.123 39.769 1.00 83.82 ? 355 VAL B N 1 ATOM 9944 C CA . VAL B 2 355 ? -8.694 12.582 38.429 1.00 78.66 ? 355 VAL B CA 1 ATOM 9945 C C . VAL B 2 355 ? -9.735 13.389 37.658 1.00 98.72 ? 355 VAL B C 1 ATOM 9946 O O . VAL B 2 355 ? -10.897 13.459 38.057 1.00 117.67 ? 355 VAL B O 1 ATOM 9947 C CB . VAL B 2 355 ? -9.139 11.105 38.476 1.00 78.27 ? 355 VAL B CB 1 ATOM 9948 C CG1 . VAL B 2 355 ? -9.624 10.651 37.106 1.00 79.14 ? 355 VAL B CG1 1 ATOM 9949 C CG2 . VAL B 2 355 ? -8.001 10.224 38.961 1.00 90.41 ? 355 VAL B CG2 1 ATOM 9950 N N . GLU B 2 356 ? -9.309 13.999 36.556 1.00 86.66 ? 356 GLU B N 1 ATOM 9951 C CA . GLU B 2 356 ? -10.214 14.738 35.678 1.00 83.77 ? 356 GLU B CA 1 ATOM 9952 C C . GLU B 2 356 ? -10.002 14.284 34.236 1.00 86.19 ? 356 GLU B C 1 ATOM 9953 O O . GLU B 2 356 ? -8.914 13.833 33.878 1.00 100.58 ? 356 GLU B O 1 ATOM 9954 C CB . GLU B 2 356 ? -9.994 16.247 35.812 1.00 90.07 ? 356 GLU B CB 1 ATOM 9955 C CG . GLU B 2 356 ? -11.055 17.099 35.125 1.00 113.62 ? 356 GLU B CG 1 ATOM 9956 C CD . GLU B 2 356 ? -10.857 18.583 35.359 1.00 123.40 ? 356 GLU B CD 1 ATOM 9957 O OE1 . GLU B 2 356 ? -9.875 18.953 36.037 1.00 129.85 ? 356 GLU B OE1 1 ATOM 9958 O OE2 . GLU B 2 356 ? -11.684 19.380 34.867 1.00 116.30 ? 356 GLU B OE2 1 ATOM 9959 N N . LEU B 2 357 ? -11.038 14.400 33.411 1.00 74.34 ? 357 LEU B N 1 ATOM 9960 C CA . LEU B 2 357 ? -10.984 13.862 32.056 1.00 74.04 ? 357 LEU B CA 1 ATOM 9961 C C . LEU B 2 357 ? -10.756 14.918 30.978 1.00 84.47 ? 357 LEU B C 1 ATOM 9962 O O . LEU B 2 357 ? -11.543 15.853 30.833 1.00 87.39 ? 357 LEU B O 1 ATOM 9963 C CB . LEU B 2 357 ? -12.270 13.094 31.745 1.00 82.83 ? 357 LEU B CB 1 ATOM 9964 C CG . LEU B 2 357 ? -12.503 11.827 32.567 1.00 82.62 ? 357 LEU B CG 1 ATOM 9965 C CD1 . LEU B 2 357 ? -13.778 11.129 32.120 1.00 83.68 ? 357 LEU B CD1 1 ATOM 9966 C CD2 . LEU B 2 357 ? -11.304 10.896 32.461 1.00 77.03 ? 357 LEU B CD2 1 ATOM 9967 N N . GLU B 2 358 ? -9.672 14.755 30.225 1.00 105.38 ? 358 GLU B N 1 ATOM 9968 C CA . GLU B 2 358 ? -9.412 15.584 29.053 1.00 90.84 ? 358 GLU B CA 1 ATOM 9969 C C . GLU B 2 358 ? -10.230 15.102 27.859 1.00 80.23 ? 358 GLU B C 1 ATOM 9970 O O . GLU B 2 358 ? -10.583 13.927 27.774 1.00 95.24 ? 358 GLU B O 1 ATOM 9971 C CB . GLU B 2 358 ? -7.925 15.573 28.692 1.00 103.85 ? 358 GLU B CB 1 ATOM 9972 C CG . GLU B 2 358 ? -7.003 16.156 29.744 1.00 122.71 ? 358 GLU B CG 1 ATOM 9973 C CD . GLU B 2 358 ? -5.552 16.162 29.300 1.00 135.79 ? 358 GLU B CD 1 ATOM 9974 O OE1 . GLU B 2 358 ? -4.660 16.210 30.173 1.00 134.70 ? 358 GLU B OE1 1 ATOM 9975 O OE2 . GLU B 2 358 ? -5.304 16.118 28.077 1.00 134.81 ? 358 GLU B OE2 1 ATOM 9976 N N . VAL B 2 359 ? -10.530 16.015 26.941 1.00 95.68 ? 359 VAL B N 1 ATOM 9977 C CA . VAL B 2 359 ? -11.197 15.659 25.694 1.00 86.68 ? 359 VAL B CA 1 ATOM 9978 C C . VAL B 2 359 ? -10.478 16.296 24.509 1.00 93.53 ? 359 VAL B C 1 ATOM 9979 O O . VAL B 2 359 ? -10.411 17.521 24.401 1.00 120.54 ? 359 VAL B O 1 ATOM 9980 C CB . VAL B 2 359 ? -12.674 16.099 25.684 1.00 86.00 ? 359 VAL B CB 1 ATOM 9981 C CG1 . VAL B 2 359 ? -13.316 15.759 24.348 1.00 83.91 ? 359 VAL B CG1 1 ATOM 9982 C CG2 . VAL B 2 359 ? -13.435 15.444 26.825 1.00 79.12 ? 359 VAL B CG2 1 ATOM 9983 N N . ARG B 2 360 ? -9.944 15.463 23.622 1.00 87.18 ? 360 ARG B N 1 ATOM 9984 C CA . ARG B 2 360 ? -9.180 15.954 22.479 1.00 90.77 ? 360 ARG B CA 1 ATOM 9985 C C . ARG B 2 360 ? -9.875 15.671 21.151 1.00 93.39 ? 360 ARG B C 1 ATOM 9986 O O . ARG B 2 360 ? -10.395 14.577 20.937 1.00 106.97 ? 360 ARG B O 1 ATOM 9987 C CB . ARG B 2 360 ? -7.781 15.334 22.467 1.00 91.88 ? 360 ARG B CB 1 ATOM 9988 C CG . ARG B 2 360 ? -6.905 15.730 23.646 1.00 92.42 ? 360 ARG B CG 1 ATOM 9989 C CD . ARG B 2 360 ? -5.550 15.038 23.581 1.00 107.22 ? 360 ARG B CD 1 ATOM 9990 N NE . ARG B 2 360 ? -4.693 15.389 24.710 1.00 124.84 ? 360 ARG B NE 1 ATOM 9991 C CZ . ARG B 2 360 ? -3.502 14.844 24.942 1.00 123.01 ? 360 ARG B CZ 1 ATOM 9992 N NH1 . ARG B 2 360 ? -3.024 13.916 24.124 1.00 107.83 ? 360 ARG B NH1 1 ATOM 9993 N NH2 . ARG B 2 360 ? -2.790 15.226 25.995 1.00 119.87 ? 360 ARG B NH2 1 ATOM 9994 N N . ASP B 2 361 ? -9.878 16.671 20.272 1.00 96.30 ? 361 ASP B N 1 ATOM 9995 C CA . ASP B 2 361 ? -10.372 16.538 18.900 1.00 99.60 ? 361 ASP B CA 1 ATOM 9996 C C . ASP B 2 361 ? -11.847 16.153 18.805 1.00 98.93 ? 361 ASP B C 1 ATOM 9997 O O . ASP B 2 361 ? -12.232 15.366 17.941 1.00 112.21 ? 361 ASP B O 1 ATOM 9998 C CB . ASP B 2 361 ? -9.531 15.511 18.133 1.00 104.82 ? 361 ASP B CB 1 ATOM 9999 C CG . ASP B 2 361 ? -8.064 15.889 18.074 1.00 132.61 ? 361 ASP B CG 1 ATOM 10000 O OD1 . ASP B 2 361 ? -7.299 15.445 18.957 1.00 142.80 ? 361 ASP B OD1 1 ATOM 10001 O OD2 . ASP B 2 361 ? -7.675 16.626 17.144 1.00 134.71 ? 361 ASP B OD2 1 ATOM 10002 N N . LEU B 2 362 ? -12.672 16.717 19.681 1.00 96.29 ? 362 LEU B N 1 ATOM 10003 C CA . LEU B 2 362 ? -14.107 16.452 19.651 1.00 95.76 ? 362 LEU B CA 1 ATOM 10004 C C . LEU B 2 362 ? -14.785 17.206 18.511 1.00 109.42 ? 362 LEU B C 1 ATOM 10005 O O . LEU B 2 362 ? -14.647 18.424 18.403 1.00 125.46 ? 362 LEU B O 1 ATOM 10006 C CB . LEU B 2 362 ? -14.753 16.829 20.985 1.00 92.34 ? 362 LEU B CB 1 ATOM 10007 C CG . LEU B 2 362 ? -16.266 16.623 21.094 1.00 94.34 ? 362 LEU B CG 1 ATOM 10008 C CD1 . LEU B 2 362 ? -16.619 15.144 21.086 1.00 105.49 ? 362 LEU B CD1 1 ATOM 10009 C CD2 . LEU B 2 362 ? -16.813 17.298 22.341 1.00 110.24 ? 362 LEU B CD2 1 ATOM 10010 N N . PRO B 2 363 ? -15.518 16.479 17.651 1.00 110.79 ? 363 PRO B N 1 ATOM 10011 C CA . PRO B 2 363 ? -16.272 17.065 16.535 1.00 110.43 ? 363 PRO B CA 1 ATOM 10012 C C . PRO B 2 363 ? -17.281 18.120 16.989 1.00 112.77 ? 363 PRO B C 1 ATOM 10013 O O . PRO B 2 363 ? -17.728 18.091 18.136 1.00 117.54 ? 363 PRO B O 1 ATOM 10014 C CB . PRO B 2 363 ? -16.983 15.857 15.923 1.00 122.61 ? 363 PRO B CB 1 ATOM 10015 C CG . PRO B 2 363 ? -16.107 14.703 16.262 1.00 123.35 ? 363 PRO B CG 1 ATOM 10016 C CD . PRO B 2 363 ? -15.563 15.006 17.627 1.00 116.57 ? 363 PRO B CD 1 ATOM 10017 N N . GLU B 2 364 ? -17.631 19.034 16.088 1.00 128.42 ? 364 GLU B N 1 ATOM 10018 C CA . GLU B 2 364 ? -18.485 20.176 16.416 1.00 130.82 ? 364 GLU B CA 1 ATOM 10019 C C . GLU B 2 364 ? -19.877 19.781 16.905 1.00 137.70 ? 364 GLU B C 1 ATOM 10020 O O . GLU B 2 364 ? -20.285 20.154 18.006 1.00 127.48 ? 364 GLU B O 1 ATOM 10021 C CB . GLU B 2 364 ? -18.625 21.093 15.197 1.00 119.05 ? 364 GLU B CB 1 ATOM 10022 C CG . GLU B 2 364 ? -17.310 21.621 14.638 1.00 154.32 ? 364 GLU B CG 1 ATOM 10023 C CD . GLU B 2 364 ? -16.787 22.836 15.387 1.00 176.19 ? 364 GLU B CD 1 ATOM 10024 O OE1 . GLU B 2 364 ? -16.031 23.624 14.780 1.00 177.47 ? 364 GLU B OE1 1 ATOM 10025 O OE2 . GLU B 2 364 ? -17.126 23.006 16.577 1.00 174.15 ? 364 GLU B OE2 1 ATOM 10026 N N . GLU B 2 365 ? -20.603 19.028 16.084 1.00 129.66 ? 365 GLU B N 1 ATOM 10027 C CA . GLU B 2 365 ? -21.984 18.673 16.391 1.00 125.42 ? 365 GLU B CA 1 ATOM 10028 C C . GLU B 2 365 ? -22.087 17.629 17.501 1.00 114.60 ? 365 GLU B C 1 ATOM 10029 O O . GLU B 2 365 ? -23.183 17.314 17.965 1.00 108.22 ? 365 GLU B O 1 ATOM 10030 C CB . GLU B 2 365 ? -22.696 18.167 15.132 1.00 128.81 ? 365 GLU B CB 1 ATOM 10031 C CG . GLU B 2 365 ? -22.880 19.224 14.050 1.00 148.30 ? 365 GLU B CG 1 ATOM 10032 C CD . GLU B 2 365 ? -23.615 18.694 12.832 1.00 169.58 ? 365 GLU B CD 1 ATOM 10033 O OE1 . GLU B 2 365 ? -23.784 17.460 12.729 1.00 176.50 ? 365 GLU B OE1 1 ATOM 10034 O OE2 . GLU B 2 365 ? -24.026 19.509 11.979 1.00 169.56 ? 365 GLU B OE2 1 ATOM 10035 N N . LEU B 2 366 ? -20.948 17.092 17.924 1.00 110.26 ? 366 LEU B N 1 ATOM 10036 C CA . LEU B 2 366 ? -20.935 16.078 18.972 1.00 109.36 ? 366 LEU B CA 1 ATOM 10037 C C . LEU B 2 366 ? -20.854 16.724 20.354 1.00 107.38 ? 366 LEU B C 1 ATOM 10038 O O . LEU B 2 366 ? -20.130 17.701 20.552 1.00 119.36 ? 366 LEU B O 1 ATOM 10039 C CB . LEU B 2 366 ? -19.772 15.107 18.766 1.00 102.58 ? 366 LEU B CB 1 ATOM 10040 C CG . LEU B 2 366 ? -20.014 13.671 19.231 1.00 102.00 ? 366 LEU B CG 1 ATOM 10041 C CD1 . LEU B 2 366 ? -21.265 13.107 18.571 1.00 106.54 ? 366 LEU B CD1 1 ATOM 10042 C CD2 . LEU B 2 366 ? -18.807 12.795 18.930 1.00 106.68 ? 366 LEU B CD2 1 ATOM 10043 N N . SER B 2 367 ? -21.604 16.173 21.303 1.00 96.36 ? 367 SER B N 1 ATOM 10044 C CA . SER B 2 367 ? -21.658 16.712 22.658 1.00 90.71 ? 367 SER B CA 1 ATOM 10045 C C . SER B 2 367 ? -21.512 15.600 23.693 1.00 93.78 ? 367 SER B C 1 ATOM 10046 O O . SER B 2 367 ? -21.974 14.480 23.478 1.00 105.92 ? 367 SER B O 1 ATOM 10047 C CB . SER B 2 367 ? -22.968 17.470 22.877 1.00 94.29 ? 367 SER B CB 1 ATOM 10048 O OG . SER B 2 367 ? -23.196 18.398 21.830 1.00 105.72 ? 367 SER B OG 1 ATOM 10049 N N . LEU B 2 368 ? -20.872 15.913 24.816 1.00 90.05 ? 368 LEU B N 1 ATOM 10050 C CA . LEU B 2 368 ? -20.615 14.911 25.846 1.00 84.99 ? 368 LEU B CA 1 ATOM 10051 C C . LEU B 2 368 ? -21.177 15.305 27.211 1.00 95.69 ? 368 LEU B C 1 ATOM 10052 O O . LEU B 2 368 ? -21.045 16.450 27.645 1.00 113.65 ? 368 LEU B O 1 ATOM 10053 C CB . LEU B 2 368 ? -19.112 14.648 25.965 1.00 80.64 ? 368 LEU B CB 1 ATOM 10054 C CG . LEU B 2 368 ? -18.421 14.024 24.750 1.00 82.04 ? 368 LEU B CG 1 ATOM 10055 C CD1 . LEU B 2 368 ? -16.965 13.708 25.059 1.00 81.64 ? 368 LEU B CD1 1 ATOM 10056 C CD2 . LEU B 2 368 ? -19.157 12.775 24.295 1.00 83.75 ? 368 LEU B CD2 1 ATOM 10057 N N . SER B 2 369 ? -21.805 14.342 27.879 1.00 94.88 ? 369 SER B N 1 ATOM 10058 C CA . SER B 2 369 ? -22.302 14.529 29.237 1.00 97.17 ? 369 SER B CA 1 ATOM 10059 C C . SER B 2 369 ? -21.585 13.559 30.169 1.00 97.10 ? 369 SER B C 1 ATOM 10060 O O . SER B 2 369 ? -21.311 12.423 29.789 1.00 96.66 ? 369 SER B O 1 ATOM 10061 C CB . SER B 2 369 ? -23.816 14.314 29.299 1.00 88.08 ? 369 SER B CB 1 ATOM 10062 O OG . SER B 2 369 ? -24.487 15.127 28.352 1.00 99.89 ? 369 SER B OG 1 ATOM 10063 N N . PHE B 2 370 ? -21.278 14.000 31.385 1.00 94.69 ? 370 PHE B N 1 ATOM 10064 C CA . PHE B 2 370 ? -20.503 13.170 32.302 1.00 85.83 ? 370 PHE B CA 1 ATOM 10065 C C . PHE B 2 370 ? -21.138 13.002 33.679 1.00 91.77 ? 370 PHE B C 1 ATOM 10066 O O . PHE B 2 370 ? -21.241 13.960 34.439 1.00 107.03 ? 370 PHE B O 1 ATOM 10067 C CB . PHE B 2 370 ? -19.096 13.750 32.477 1.00 86.17 ? 370 PHE B CB 1 ATOM 10068 C CG . PHE B 2 370 ? -18.267 13.735 31.223 1.00 94.14 ? 370 PHE B CG 1 ATOM 10069 C CD1 . PHE B 2 370 ? -18.347 14.772 30.308 1.00 86.80 ? 370 PHE B CD1 1 ATOM 10070 C CD2 . PHE B 2 370 ? -17.394 12.692 30.967 1.00 75.50 ? 370 PHE B CD2 1 ATOM 10071 C CE1 . PHE B 2 370 ? -17.580 14.763 29.158 1.00 86.09 ? 370 PHE B CE1 1 ATOM 10072 C CE2 . PHE B 2 370 ? -16.625 12.677 29.818 1.00 86.54 ? 370 PHE B CE2 1 ATOM 10073 C CZ . PHE B 2 370 ? -16.718 13.712 28.913 1.00 102.42 ? 370 PHE B CZ 1 ATOM 10074 N N . ASN B 2 371 ? -21.547 11.780 34.005 1.00 88.49 ? 371 ASN B N 1 ATOM 10075 C CA . ASN B 2 371 ? -21.845 11.434 35.389 1.00 90.92 ? 371 ASN B CA 1 ATOM 10076 C C . ASN B 2 371 ? -20.624 10.740 35.974 1.00 96.21 ? 371 ASN B C 1 ATOM 10077 O O . ASN B 2 371 ? -19.995 9.919 35.308 1.00 93.22 ? 371 ASN B O 1 ATOM 10078 C CB . ASN B 2 371 ? -23.078 10.533 35.502 1.00 97.18 ? 371 ASN B CB 1 ATOM 10079 C CG . ASN B 2 371 ? -24.353 11.217 35.050 1.00 97.35 ? 371 ASN B CG 1 ATOM 10080 O OD1 . ASN B 2 371 ? -24.406 12.440 34.916 1.00 99.29 ? 371 ASN B OD1 1 ATOM 10081 N ND2 . ASN B 2 371 ? -25.395 10.422 34.815 1.00 120.08 ? 371 ASN B ND2 1 ATOM 10082 N N . ALA B 2 372 ? -20.281 11.073 37.213 1.00 94.15 ? 372 ALA B N 1 ATOM 10083 C CA . ALA B 2 372 ? -19.073 10.528 37.820 1.00 90.41 ? 372 ALA B CA 1 ATOM 10084 C C . ALA B 2 372 ? -19.369 9.706 39.068 1.00 98.40 ? 372 ALA B C 1 ATOM 10085 O O . ALA B 2 372 ? -19.993 10.189 40.012 1.00 109.38 ? 372 ALA B O 1 ATOM 10086 C CB . ALA B 2 372 ? -18.102 11.646 38.152 1.00 87.61 ? 372 ALA B CB 1 ATOM 10087 N N . THR B 2 373 ? -18.912 8.459 39.060 1.00 98.25 ? 373 THR B N 1 ATOM 10088 C CA . THR B 2 373 ? -18.961 7.621 40.248 1.00 98.03 ? 373 THR B CA 1 ATOM 10089 C C . THR B 2 373 ? -17.573 7.543 40.871 1.00 96.14 ? 373 THR B C 1 ATOM 10090 O O . THR B 2 373 ? -16.666 6.922 40.317 1.00 90.36 ? 373 THR B O 1 ATOM 10091 C CB . THR B 2 373 ? -19.466 6.205 39.932 1.00 99.08 ? 373 THR B CB 1 ATOM 10092 O OG1 . THR B 2 373 ? -20.820 6.272 39.468 1.00 99.61 ? 373 THR B OG1 1 ATOM 10093 C CG2 . THR B 2 373 ? -19.407 5.334 41.176 1.00 104.17 ? 373 THR B CG2 1 ATOM 10094 N N . CYS B 2 374 ? -17.414 8.181 42.024 1.00 101.70 ? 374 CYS B N 1 ATOM 10095 C CA . CYS B 2 374 ? -16.124 8.222 42.699 1.00 101.84 ? 374 CYS B CA 1 ATOM 10096 C C . CYS B 2 374 ? -16.119 7.336 43.940 1.00 111.81 ? 374 CYS B C 1 ATOM 10097 O O . CYS B 2 374 ? -15.360 6.371 44.018 1.00 129.19 ? 374 CYS B O 1 ATOM 10098 C CB . CYS B 2 374 ? -15.757 9.661 43.072 1.00 124.41 ? 374 CYS B CB 1 ATOM 10099 S SG . CYS B 2 374 ? -15.539 10.772 41.657 1.00 120.80 ? 374 CYS B SG 1 ATOM 10100 N N . LEU B 2 375 ? -16.964 7.668 44.912 1.00 115.61 ? 375 LEU B N 1 ATOM 10101 C CA . LEU B 2 375 ? -16.980 6.941 46.176 1.00 116.86 ? 375 LEU B CA 1 ATOM 10102 C C . LEU B 2 375 ? -18.147 5.960 46.279 1.00 117.54 ? 375 LEU B C 1 ATOM 10103 O O . LEU B 2 375 ? -19.289 6.368 46.491 1.00 122.15 ? 375 LEU B O 1 ATOM 10104 C CB . LEU B 2 375 ? -17.034 7.937 47.337 1.00 122.13 ? 375 LEU B CB 1 ATOM 10105 C CG . LEU B 2 375 ? -17.082 7.398 48.764 1.00 125.48 ? 375 LEU B CG 1 ATOM 10106 C CD1 . LEU B 2 375 ? -15.808 6.641 49.099 1.00 140.03 ? 375 LEU B CD1 1 ATOM 10107 C CD2 . LEU B 2 375 ? -17.310 8.533 49.746 1.00 129.91 ? 375 LEU B CD2 1 ATOM 10108 N N . ASN B 2 376 ? -17.832 4.670 46.146 1.00 115.60 ? 376 ASN B N 1 ATOM 10109 C CA . ASN B 2 376 ? -18.776 3.555 46.309 1.00 113.52 ? 376 ASN B CA 1 ATOM 10110 C C . ASN B 2 376 ? -20.186 3.806 45.767 1.00 117.20 ? 376 ASN B C 1 ATOM 10111 O O . ASN B 2 376 ? -21.139 3.922 46.538 1.00 122.26 ? 376 ASN B O 1 ATOM 10112 C CB . ASN B 2 376 ? -18.860 3.118 47.782 1.00 116.38 ? 376 ASN B CB 1 ATOM 10113 C CG . ASN B 2 376 ? -19.053 4.276 48.739 1.00 122.34 ? 376 ASN B CG 1 ATOM 10114 O OD1 . ASN B 2 376 ? -18.195 4.546 49.578 1.00 122.46 ? 376 ASN B OD1 1 ATOM 10115 N ND2 . ASN B 2 376 ? -20.184 4.962 48.624 1.00 141.30 ? 376 ASN B ND2 1 ATOM 10116 N N . ASN B 2 377 ? -20.300 3.905 44.444 1.00 124.85 ? 377 ASN B N 1 ATOM 10117 C CA . ASN B 2 377 ? -21.590 4.021 43.761 1.00 128.74 ? 377 ASN B CA 1 ATOM 10118 C C . ASN B 2 377 ? -22.391 5.270 44.140 1.00 130.78 ? 377 ASN B C 1 ATOM 10119 O O . ASN B 2 377 ? -23.607 5.201 44.310 1.00 130.39 ? 377 ASN B O 1 ATOM 10120 C CB . ASN B 2 377 ? -22.444 2.777 44.029 1.00 125.22 ? 377 ASN B CB 1 ATOM 10121 C CG . ASN B 2 377 ? -21.642 1.490 43.961 1.00 125.72 ? 377 ASN B CG 1 ATOM 10122 O OD1 . ASN B 2 377 ? -20.695 1.374 43.184 1.00 133.17 ? 377 ASN B OD1 1 ATOM 10123 N ND2 . ASN B 2 377 ? -22.018 0.516 44.782 1.00 118.91 ? 377 ASN B ND2 1 ATOM 10124 N N . GLU B 2 378 ? -21.712 6.407 44.273 1.00 137.28 ? 378 GLU B N 1 ATOM 10125 C CA . GLU B 2 378 ? -22.383 7.656 44.633 1.00 134.65 ? 378 GLU B CA 1 ATOM 10126 C C . GLU B 2 378 ? -23.048 8.343 43.435 1.00 134.68 ? 378 GLU B C 1 ATOM 10127 O O . GLU B 2 378 ? -24.099 8.969 43.583 1.00 154.14 ? 378 GLU B O 1 ATOM 10128 C CB . GLU B 2 378 ? -21.400 8.617 45.307 1.00 149.34 ? 378 GLU B CB 1 ATOM 10129 C CG . GLU B 2 378 ? -20.181 8.974 44.478 1.00 148.90 ? 378 GLU B CG 1 ATOM 10130 C CD . GLU B 2 378 ? -19.294 9.985 45.173 1.00 162.95 ? 378 GLU B CD 1 ATOM 10131 O OE1 . GLU B 2 378 ? -19.463 10.185 46.394 1.00 174.52 ? 378 GLU B OE1 1 ATOM 10132 O OE2 . GLU B 2 378 ? -18.432 10.585 44.498 1.00 166.09 ? 378 GLU B OE2 1 ATOM 10133 N N . VAL B 2 379 ? -22.427 8.225 42.262 1.00 125.15 ? 379 VAL B N 1 ATOM 10134 C CA . VAL B 2 379 ? -22.971 8.765 41.010 1.00 120.06 ? 379 VAL B CA 1 ATOM 10135 C C . VAL B 2 379 ? -23.224 10.279 41.059 1.00 115.75 ? 379 VAL B C 1 ATOM 10136 O O . VAL B 2 379 ? -24.368 10.726 41.149 1.00 114.00 ? 379 VAL B O 1 ATOM 10137 C CB . VAL B 2 379 ? -24.283 8.046 40.607 1.00 116.35 ? 379 VAL B CB 1 ATOM 10138 C CG1 . VAL B 2 379 ? -24.655 8.378 39.167 1.00 107.89 ? 379 VAL B CG1 1 ATOM 10139 C CG2 . VAL B 2 379 ? -24.138 6.541 40.772 1.00 134.33 ? 379 VAL B CG2 1 ATOM 10140 N N . ILE B 2 380 ? -22.148 11.062 41.031 1.00 116.06 ? 380 ILE B N 1 ATOM 10141 C CA . ILE B 2 380 ? -22.259 12.517 40.951 1.00 108.39 ? 380 ILE B CA 1 ATOM 10142 C C . ILE B 2 380 ? -22.469 12.978 39.507 1.00 111.81 ? 380 ILE B C 1 ATOM 10143 O O . ILE B 2 380 ? -21.599 12.783 38.658 1.00 123.26 ? 380 ILE B O 1 ATOM 10144 C CB . ILE B 2 380 ? -21.010 13.215 41.522 1.00 108.59 ? 380 ILE B CB 1 ATOM 10145 C CG1 . ILE B 2 380 ? -20.850 12.895 43.010 1.00 116.19 ? 380 ILE B CG1 1 ATOM 10146 C CG2 . ILE B 2 380 ? -21.096 14.718 41.307 1.00 115.61 ? 380 ILE B CG2 1 ATOM 10147 C CD1 . ILE B 2 380 ? -19.652 13.562 43.653 1.00 118.77 ? 380 ILE B CD1 1 ATOM 10148 N N . PRO B 2 381 ? -23.630 13.592 39.229 1.00 115.22 ? 381 PRO B N 1 ATOM 10149 C CA . PRO B 2 381 ? -24.006 14.035 37.880 1.00 110.18 ? 381 PRO B CA 1 ATOM 10150 C C . PRO B 2 381 ? -23.273 15.294 37.420 1.00 107.69 ? 381 PRO B C 1 ATOM 10151 O O . PRO B 2 381 ? -22.976 16.169 38.234 1.00 125.80 ? 381 PRO B O 1 ATOM 10152 C CB . PRO B 2 381 ? -25.511 14.322 38.008 1.00 117.84 ? 381 PRO B CB 1 ATOM 10153 C CG . PRO B 2 381 ? -25.929 13.739 39.327 1.00 132.31 ? 381 PRO B CG 1 ATOM 10154 C CD . PRO B 2 381 ? -24.719 13.808 40.193 1.00 131.50 ? 381 PRO B CD 1 ATOM 10155 N N . GLY B 2 382 ? -22.993 15.374 36.123 1.00 89.41 ? 382 GLY B N 1 ATOM 10156 C CA . GLY B 2 382 ? -22.451 16.578 35.519 1.00 86.46 ? 382 GLY B CA 1 ATOM 10157 C C . GLY B 2 382 ? -20.994 16.876 35.820 1.00 87.57 ? 382 GLY B C 1 ATOM 10158 O O . GLY B 2 382 ? -20.525 17.986 35.566 1.00 121.36 ? 382 GLY B O 1 ATOM 10159 N N . LEU B 2 383 ? -20.266 15.896 36.344 1.00 86.97 ? 383 LEU B N 1 ATOM 10160 C CA . LEU B 2 383 ? -18.888 16.134 36.763 1.00 98.45 ? 383 LEU B CA 1 ATOM 10161 C C . LEU B 2 383 ? -17.889 15.179 36.111 1.00 92.43 ? 383 LEU B C 1 ATOM 10162 O O . LEU B 2 383 ? -18.127 13.976 36.021 1.00 82.48 ? 383 LEU B O 1 ATOM 10163 C CB . LEU B 2 383 ? -18.779 16.038 38.285 1.00 94.25 ? 383 LEU B CB 1 ATOM 10164 C CG . LEU B 2 383 ? -17.446 16.481 38.886 1.00 109.30 ? 383 LEU B CG 1 ATOM 10165 C CD1 . LEU B 2 383 ? -17.126 17.912 38.479 1.00 114.10 ? 383 LEU B CD1 1 ATOM 10166 C CD2 . LEU B 2 383 ? -17.476 16.343 40.398 1.00 120.54 ? 383 LEU B CD2 1 ATOM 10167 N N . LYS B 2 384 ? -16.779 15.735 35.636 1.00 93.63 ? 384 LYS B N 1 ATOM 10168 C CA . LYS B 2 384 ? -15.700 14.945 35.054 1.00 78.49 ? 384 LYS B CA 1 ATOM 10169 C C . LYS B 2 384 ? -14.568 14.689 36.045 1.00 91.17 ? 384 LYS B C 1 ATOM 10170 O O . LYS B 2 384 ? -13.569 14.054 35.702 1.00 91.52 ? 384 LYS B O 1 ATOM 10171 C CB . LYS B 2 384 ? -15.140 15.643 33.815 1.00 75.93 ? 384 LYS B CB 1 ATOM 10172 C CG . LYS B 2 384 ? -16.190 16.064 32.808 1.00 91.71 ? 384 LYS B CG 1 ATOM 10173 C CD . LYS B 2 384 ? -15.549 16.729 31.603 1.00 101.32 ? 384 LYS B CD 1 ATOM 10174 C CE . LYS B 2 384 ? -14.678 17.901 32.025 1.00 103.59 ? 384 LYS B CE 1 ATOM 10175 N NZ . LYS B 2 384 ? -15.460 18.927 32.765 1.00 99.04 ? 384 LYS B NZ 1 ATOM 10176 N N . SER B 2 385 ? -14.721 15.181 37.271 1.00 96.69 ? 385 SER B N 1 ATOM 10177 C CA . SER B 2 385 ? -13.612 15.204 38.220 1.00 85.92 ? 385 SER B CA 1 ATOM 10178 C C . SER B 2 385 ? -13.846 14.343 39.460 1.00 87.58 ? 385 SER B C 1 ATOM 10179 O O . SER B 2 385 ? -14.986 14.058 39.826 1.00 108.80 ? 385 SER B O 1 ATOM 10180 C CB . SER B 2 385 ? -13.327 16.644 38.651 1.00 111.49 ? 385 SER B CB 1 ATOM 10181 O OG . SER B 2 385 ? -13.199 17.498 37.527 1.00 118.41 ? 385 SER B OG 1 ATOM 10182 N N . CYS B 2 386 ? -12.752 13.931 40.096 1.00 87.62 ? 386 CYS B N 1 ATOM 10183 C CA . CYS B 2 386 ? -12.810 13.178 41.347 1.00 92.83 ? 386 CYS B CA 1 ATOM 10184 C C . CYS B 2 386 ? -11.781 13.700 42.352 1.00 96.97 ? 386 CYS B C 1 ATOM 10185 O O . CYS B 2 386 ? -10.588 13.774 42.055 1.00 93.17 ? 386 CYS B O 1 ATOM 10186 C CB . CYS B 2 386 ? -12.593 11.687 41.088 1.00 89.92 ? 386 CYS B CB 1 ATOM 10187 S SG . CYS B 2 386 ? -14.008 10.861 40.323 1.00 150.52 ? 386 CYS B SG 1 ATOM 10188 N N . MET B 2 387 ? -12.256 14.048 43.545 1.00 110.17 ? 387 MET B N 1 ATOM 10189 C CA . MET B 2 387 ? -11.437 14.711 44.557 1.00 113.79 ? 387 MET B CA 1 ATOM 10190 C C . MET B 2 387 ? -11.068 13.781 45.716 1.00 118.41 ? 387 MET B C 1 ATOM 10191 O O . MET B 2 387 ? -11.850 12.911 46.099 1.00 131.45 ? 387 MET B O 1 ATOM 10192 C CB . MET B 2 387 ? -12.180 15.947 45.087 1.00 116.76 ? 387 MET B CB 1 ATOM 10193 C CG . MET B 2 387 ? -11.485 16.699 46.213 1.00 120.70 ? 387 MET B CG 1 ATOM 10194 S SD . MET B 2 387 ? -10.013 17.588 45.673 1.00 176.71 ? 387 MET B SD 1 ATOM 10195 C CE . MET B 2 387 ? -9.506 18.362 47.207 1.00 135.77 ? 387 MET B CE 1 ATOM 10196 N N . GLY B 2 388 ? -9.869 13.971 46.264 1.00 118.62 ? 388 GLY B N 1 ATOM 10197 C CA . GLY B 2 388 ? -9.436 13.255 47.451 1.00 121.42 ? 388 GLY B CA 1 ATOM 10198 C C . GLY B 2 388 ? -9.161 11.781 47.230 1.00 115.16 ? 388 GLY B C 1 ATOM 10199 O O . GLY B 2 388 ? -9.668 10.932 47.962 1.00 116.59 ? 388 GLY B O 1 ATOM 10200 N N . LEU B 2 389 ? -8.348 11.475 46.226 1.00 108.12 ? 389 LEU B N 1 ATOM 10201 C CA . LEU B 2 389 ? -8.053 10.087 45.884 1.00 113.36 ? 389 LEU B CA 1 ATOM 10202 C C . LEU B 2 389 ? -6.681 9.643 46.383 1.00 117.55 ? 389 LEU B C 1 ATOM 10203 O O . LEU B 2 389 ? -5.741 10.434 46.440 1.00 105.98 ? 389 LEU B O 1 ATOM 10204 C CB . LEU B 2 389 ? -8.141 9.881 44.371 1.00 99.85 ? 389 LEU B CB 1 ATOM 10205 C CG . LEU B 2 389 ? -9.484 10.210 43.717 1.00 95.45 ? 389 LEU B CG 1 ATOM 10206 C CD1 . LEU B 2 389 ? -9.506 9.736 42.273 1.00 88.93 ? 389 LEU B CD1 1 ATOM 10207 C CD2 . LEU B 2 389 ? -10.633 9.601 44.504 1.00 108.86 ? 389 LEU B CD2 1 ATOM 10208 N N . LYS B 2 390 ? -6.578 8.374 46.761 1.00 123.15 ? 390 LYS B N 1 ATOM 10209 C CA . LYS B 2 390 ? -5.292 7.776 47.090 1.00 122.03 ? 390 LYS B CA 1 ATOM 10210 C C . LYS B 2 390 ? -4.693 7.146 45.838 1.00 122.62 ? 390 LYS B C 1 ATOM 10211 O O . LYS B 2 390 ? -5.213 7.323 44.736 1.00 126.49 ? 390 LYS B O 1 ATOM 10212 C CB . LYS B 2 390 ? -5.440 6.728 48.194 1.00 131.31 ? 390 LYS B CB 1 ATOM 10213 C CG . LYS B 2 390 ? -6.002 7.265 49.501 1.00 138.60 ? 390 LYS B CG 1 ATOM 10214 C CD . LYS B 2 390 ? -5.051 8.250 50.158 1.00 133.19 ? 390 LYS B CD 1 ATOM 10215 C CE . LYS B 2 390 ? -5.579 8.698 51.512 1.00 139.28 ? 390 LYS B CE 1 ATOM 10216 N NZ . LYS B 2 390 ? -5.775 7.548 52.440 1.00 140.95 ? 390 LYS B NZ 1 ATOM 10217 N N . ILE B 2 391 ? -3.600 6.411 46.007 1.00 121.21 ? 391 ILE B N 1 ATOM 10218 C CA . ILE B 2 391 ? -2.996 5.687 44.897 1.00 103.51 ? 391 ILE B CA 1 ATOM 10219 C C . ILE B 2 391 ? -3.449 4.230 44.933 1.00 101.99 ? 391 ILE B C 1 ATOM 10220 O O . ILE B 2 391 ? -3.295 3.549 45.946 1.00 125.78 ? 391 ILE B O 1 ATOM 10221 C CB . ILE B 2 391 ? -1.454 5.753 44.926 1.00 102.28 ? 391 ILE B CB 1 ATOM 10222 C CG1 . ILE B 2 391 ? -0.967 7.175 44.634 1.00 107.87 ? 391 ILE B CG1 1 ATOM 10223 C CG2 . ILE B 2 391 ? -0.859 4.785 43.916 1.00 97.11 ? 391 ILE B CG2 1 ATOM 10224 C CD1 . ILE B 2 391 ? -0.884 8.076 45.850 1.00 104.90 ? 391 ILE B CD1 1 ATOM 10225 N N . GLY B 2 392 ? -4.005 3.759 43.822 1.00 91.52 ? 392 GLY B N 1 ATOM 10226 C CA . GLY B 2 392 ? -4.574 2.426 43.762 1.00 103.11 ? 392 GLY B CA 1 ATOM 10227 C C . GLY B 2 392 ? -6.088 2.467 43.698 1.00 115.86 ? 392 GLY B C 1 ATOM 10228 O O . GLY B 2 392 ? -6.739 1.442 43.501 1.00 111.83 ? 392 GLY B O 1 ATOM 10229 N N . ASP B 2 393 ? -6.651 3.660 43.866 1.00 118.79 ? 393 ASP B N 1 ATOM 10230 C CA . ASP B 2 393 ? -8.095 3.839 43.796 1.00 113.90 ? 393 ASP B CA 1 ATOM 10231 C C . ASP B 2 393 ? -8.585 3.792 42.353 1.00 107.61 ? 393 ASP B C 1 ATOM 10232 O O . ASP B 2 393 ? -7.836 4.091 41.423 1.00 83.99 ? 393 ASP B O 1 ATOM 10233 C CB . ASP B 2 393 ? -8.507 5.161 44.449 1.00 117.60 ? 393 ASP B CB 1 ATOM 10234 C CG . ASP B 2 393 ? -8.191 5.201 45.932 1.00 138.17 ? 393 ASP B CG 1 ATOM 10235 O OD1 . ASP B 2 393 ? -7.282 4.464 46.368 1.00 148.84 ? 393 ASP B OD1 1 ATOM 10236 O OD2 . ASP B 2 393 ? -8.852 5.970 46.661 1.00 132.96 ? 393 ASP B OD2 1 ATOM 10237 N N . THR B 2 394 ? -9.846 3.415 42.175 1.00 119.74 ? 394 THR B N 1 ATOM 10238 C CA . THR B 2 394 ? -10.442 3.342 40.847 1.00 87.54 ? 394 THR B CA 1 ATOM 10239 C C . THR B 2 394 ? -11.746 4.133 40.799 1.00 82.65 ? 394 THR B C 1 ATOM 10240 O O . THR B 2 394 ? -12.571 4.038 41.707 1.00 85.57 ? 394 THR B O 1 ATOM 10241 C CB . THR B 2 394 ? -10.714 1.883 40.428 1.00 86.54 ? 394 THR B CB 1 ATOM 10242 O OG1 . THR B 2 394 ? -9.549 1.085 40.674 1.00 85.47 ? 394 THR B OG1 1 ATOM 10243 C CG2 . THR B 2 394 ? -11.078 1.808 38.952 1.00 78.56 ? 394 THR B CG2 1 ATOM 10244 N N . VAL B 2 395 ? -11.925 4.916 39.741 1.00 80.46 ? 395 VAL B N 1 ATOM 10245 C CA . VAL B 2 395 ? -13.147 5.694 39.567 1.00 81.16 ? 395 VAL B CA 1 ATOM 10246 C C . VAL B 2 395 ? -13.816 5.382 38.233 1.00 78.56 ? 395 VAL B C 1 ATOM 10247 O O . VAL B 2 395 ? -13.175 4.887 37.305 1.00 76.11 ? 395 VAL B O 1 ATOM 10248 C CB . VAL B 2 395 ? -12.874 7.208 39.652 1.00 85.40 ? 395 VAL B CB 1 ATOM 10249 C CG1 . VAL B 2 395 ? -12.535 7.606 41.081 1.00 86.52 ? 395 VAL B CG1 1 ATOM 10250 C CG2 . VAL B 2 395 ? -11.760 7.604 38.695 1.00 94.60 ? 395 VAL B CG2 1 ATOM 10251 N N . SER B 2 396 ? -15.109 5.674 38.146 1.00 90.94 ? 396 SER B N 1 ATOM 10252 C CA . SER B 2 396 ? -15.882 5.392 36.943 1.00 85.24 ? 396 SER B CA 1 ATOM 10253 C C . SER B 2 396 ? -16.549 6.644 36.387 1.00 93.33 ? 396 SER B C 1 ATOM 10254 O O . SER B 2 396 ? -16.940 7.539 37.137 1.00 81.33 ? 396 SER B O 1 ATOM 10255 C CB . SER B 2 396 ? -16.941 4.326 37.229 1.00 80.48 ? 396 SER B CB 1 ATOM 10256 O OG . SER B 2 396 ? -17.802 4.152 36.117 1.00 88.03 ? 396 SER B OG 1 ATOM 10257 N N . PHE B 2 397 ? -16.677 6.697 35.066 1.00 92.24 ? 397 PHE B N 1 ATOM 10258 C CA . PHE B 2 397 ? -17.373 7.793 34.402 1.00 75.27 ? 397 PHE B CA 1 ATOM 10259 C C . PHE B 2 397 ? -18.328 7.258 33.338 1.00 77.78 ? 397 PHE B C 1 ATOM 10260 O O . PHE B 2 397 ? -17.938 6.448 32.497 1.00 102.13 ? 397 PHE B O 1 ATOM 10261 C CB . PHE B 2 397 ? -16.379 8.766 33.762 1.00 73.04 ? 397 PHE B CB 1 ATOM 10262 C CG . PHE B 2 397 ? -15.469 9.449 34.746 1.00 78.95 ? 397 PHE B CG 1 ATOM 10263 C CD1 . PHE B 2 397 ? -14.199 8.955 34.998 1.00 82.35 ? 397 PHE B CD1 1 ATOM 10264 C CD2 . PHE B 2 397 ? -15.877 10.595 35.408 1.00 79.34 ? 397 PHE B CD2 1 ATOM 10265 C CE1 . PHE B 2 397 ? -13.358 9.584 35.897 1.00 79.37 ? 397 PHE B CE1 1 ATOM 10266 C CE2 . PHE B 2 397 ? -15.040 11.228 36.308 1.00 76.33 ? 397 PHE B CE2 1 ATOM 10267 C CZ . PHE B 2 397 ? -13.780 10.722 36.552 1.00 85.41 ? 397 PHE B CZ 1 ATOM 10268 N N . SER B 2 398 ? -19.579 7.706 33.380 1.00 78.38 ? 398 SER B N 1 ATOM 10269 C CA . SER B 2 398 ? -20.538 7.387 32.327 1.00 85.13 ? 398 SER B CA 1 ATOM 10270 C C . SER B 2 398 ? -20.667 8.580 31.391 1.00 86.57 ? 398 SER B C 1 ATOM 10271 O O . SER B 2 398 ? -20.834 9.714 31.840 1.00 77.18 ? 398 SER B O 1 ATOM 10272 C CB . SER B 2 398 ? -21.899 7.009 32.912 1.00 93.04 ? 398 SER B CB 1 ATOM 10273 O OG . SER B 2 398 ? -22.457 8.083 33.646 1.00 101.70 ? 398 SER B OG 1 ATOM 10274 N N . ILE B 2 399 ? -20.575 8.323 30.090 1.00 83.83 ? 399 ILE B N 1 ATOM 10275 C CA . ILE B 2 399 ? -20.533 9.397 29.103 1.00 76.84 ? 399 ILE B CA 1 ATOM 10276 C C . ILE B 2 399 ? -21.608 9.249 28.032 1.00 80.18 ? 399 ILE B C 1 ATOM 10277 O O . ILE B 2 399 ? -21.693 8.218 27.368 1.00 92.46 ? 399 ILE B O 1 ATOM 10278 C CB . ILE B 2 399 ? -19.159 9.460 28.411 1.00 91.39 ? 399 ILE B CB 1 ATOM 10279 C CG1 . ILE B 2 399 ? -18.037 9.431 29.449 1.00 93.16 ? 399 ILE B CG1 1 ATOM 10280 C CG2 . ILE B 2 399 ? -19.060 10.697 27.529 1.00 95.37 ? 399 ILE B CG2 1 ATOM 10281 C CD1 . ILE B 2 399 ? -16.664 9.248 28.858 1.00 98.05 ? 399 ILE B CD1 1 ATOM 10282 N N . GLU B 2 400 ? -22.421 10.288 27.864 1.00 93.97 ? 400 GLU B N 1 ATOM 10283 C CA . GLU B 2 400 ? -23.423 10.311 26.805 1.00 95.78 ? 400 GLU B CA 1 ATOM 10284 C C . GLU B 2 400 ? -22.908 11.096 25.606 1.00 87.88 ? 400 GLU B C 1 ATOM 10285 O O . GLU B 2 400 ? -22.470 12.237 25.745 1.00 92.32 ? 400 GLU B O 1 ATOM 10286 C CB . GLU B 2 400 ? -24.733 10.920 27.306 1.00 100.21 ? 400 GLU B CB 1 ATOM 10287 C CG . GLU B 2 400 ? -25.846 10.937 26.268 1.00 104.90 ? 400 GLU B CG 1 ATOM 10288 C CD . GLU B 2 400 ? -27.037 11.769 26.701 1.00 125.02 ? 400 GLU B CD 1 ATOM 10289 O OE1 . GLU B 2 400 ? -28.166 11.476 26.253 1.00 138.81 ? 400 GLU B OE1 1 ATOM 10290 O OE2 . GLU B 2 400 ? -26.844 12.723 27.486 1.00 123.95 ? 400 GLU B OE2 1 ATOM 10291 N N . ALA B 2 401 ? -22.959 10.482 24.429 1.00 87.83 ? 401 ALA B N 1 ATOM 10292 C CA . ALA B 2 401 ? -22.508 11.140 23.209 1.00 91.23 ? 401 ALA B CA 1 ATOM 10293 C C . ALA B 2 401 ? -23.695 11.565 22.352 1.00 95.65 ? 401 ALA B C 1 ATOM 10294 O O . ALA B 2 401 ? -24.391 10.726 21.784 1.00 98.84 ? 401 ALA B O 1 ATOM 10295 C CB . ALA B 2 401 ? -21.583 10.226 22.426 1.00 93.38 ? 401 ALA B CB 1 ATOM 10296 N N . LYS B 2 402 ? -23.912 12.873 22.257 1.00 95.93 ? 402 LYS B N 1 ATOM 10297 C CA . LYS B 2 402 ? -25.053 13.413 21.525 1.00 100.07 ? 402 LYS B CA 1 ATOM 10298 C C . LYS B 2 402 ? -24.619 14.097 20.234 1.00 103.78 ? 402 LYS B C 1 ATOM 10299 O O . LYS B 2 402 ? -23.683 14.895 20.231 1.00 106.02 ? 402 LYS B O 1 ATOM 10300 C CB . LYS B 2 402 ? -25.825 14.401 22.402 1.00 122.57 ? 402 LYS B CB 1 ATOM 10301 C CG . LYS B 2 402 ? -27.043 15.022 21.736 1.00 139.97 ? 402 LYS B CG 1 ATOM 10302 C CD . LYS B 2 402 ? -28.149 14.000 21.538 1.00 136.61 ? 402 LYS B CD 1 ATOM 10303 C CE . LYS B 2 402 ? -29.434 14.659 21.067 1.00 144.09 ? 402 LYS B CE 1 ATOM 10304 N NZ . LYS B 2 402 ? -29.257 15.359 19.766 1.00 152.51 ? 402 LYS B NZ 1 ATOM 10305 N N . VAL B 2 403 ? -25.304 13.783 19.139 1.00 109.51 ? 403 VAL B N 1 ATOM 10306 C CA . VAL B 2 403 ? -25.043 14.437 17.863 1.00 120.35 ? 403 VAL B CA 1 ATOM 10307 C C . VAL B 2 403 ? -26.283 15.201 17.394 1.00 120.72 ? 403 VAL B C 1 ATOM 10308 O O . VAL B 2 403 ? -27.411 14.728 17.539 1.00 128.08 ? 403 VAL B O 1 ATOM 10309 C CB . VAL B 2 403 ? -24.605 13.419 16.780 1.00 119.86 ? 403 VAL B CB 1 ATOM 10310 C CG1 . VAL B 2 403 ? -25.660 12.338 16.586 1.00 126.72 ? 403 VAL B CG1 1 ATOM 10311 C CG2 . VAL B 2 403 ? -24.303 14.127 15.465 1.00 121.50 ? 403 VAL B CG2 1 ATOM 10312 N N . ARG B 2 404 ? -26.067 16.397 16.853 1.00 115.29 ? 404 ARG B N 1 ATOM 10313 C CA . ARG B 2 404 ? -27.157 17.217 16.342 1.00 117.42 ? 404 ARG B CA 1 ATOM 10314 C C . ARG B 2 404 ? -27.154 17.213 14.817 1.00 121.69 ? 404 ARG B C 1 ATOM 10315 O O . ARG B 2 404 ? -26.255 17.773 14.191 1.00 123.17 ? 404 ARG B O 1 ATOM 10316 C CB . ARG B 2 404 ? -27.039 18.646 16.873 1.00 113.95 ? 404 ARG B CB 1 ATOM 10317 C CG . ARG B 2 404 ? -28.041 19.625 16.287 1.00 131.71 ? 404 ARG B CG 1 ATOM 10318 C CD . ARG B 2 404 ? -27.661 21.044 16.662 1.00 147.85 ? 404 ARG B CD 1 ATOM 10319 N NE . ARG B 2 404 ? -26.260 21.313 16.351 1.00 153.19 ? 404 ARG B NE 1 ATOM 10320 C CZ . ARG B 2 404 ? -25.611 22.415 16.713 1.00 159.18 ? 404 ARG B CZ 1 ATOM 10321 N NH1 . ARG B 2 404 ? -26.236 23.357 17.404 1.00 151.03 ? 404 ARG B NH1 1 ATOM 10322 N NH2 . ARG B 2 404 ? -24.336 22.573 16.385 1.00 166.11 ? 404 ARG B NH2 1 ATOM 10323 N N . GLY B 2 405 ? -28.165 16.585 14.226 1.00 126.16 ? 405 GLY B N 1 ATOM 10324 C CA . GLY B 2 405 ? -28.211 16.408 12.785 1.00 134.11 ? 405 GLY B CA 1 ATOM 10325 C C . GLY B 2 405 ? -27.098 15.479 12.339 1.00 138.17 ? 405 GLY B C 1 ATOM 10326 O O . GLY B 2 405 ? -26.612 14.669 13.127 1.00 142.08 ? 405 GLY B O 1 ATOM 10327 N N . CYS B 2 406 ? -26.691 15.588 11.078 1.00 139.21 ? 406 CYS B N 1 ATOM 10328 C CA . CYS B 2 406 ? -25.552 14.819 10.596 1.00 133.65 ? 406 CYS B CA 1 ATOM 10329 C C . CYS B 2 406 ? -24.612 15.691 9.768 1.00 139.19 ? 406 CYS B C 1 ATOM 10330 O O . CYS B 2 406 ? -25.061 16.491 8.947 1.00 151.09 ? 406 CYS B O 1 ATOM 10331 C CB . CYS B 2 406 ? -26.030 13.621 9.770 1.00 145.59 ? 406 CYS B CB 1 ATOM 10332 S SG . CYS B 2 406 ? -24.710 12.648 9.007 1.00 222.90 ? 406 CYS B SG 1 ATOM 10333 N N . PRO B 2 407 ? -23.298 15.529 9.982 1.00 136.73 ? 407 PRO B N 1 ATOM 10334 C CA . PRO B 2 407 ? -22.250 16.255 9.253 1.00 152.02 ? 407 PRO B CA 1 ATOM 10335 C C . PRO B 2 407 ? -22.075 15.785 7.810 1.00 158.21 ? 407 PRO B C 1 ATOM 10336 O O . PRO B 2 407 ? -21.634 16.564 6.963 1.00 155.31 ? 407 PRO B O 1 ATOM 10337 C CB . PRO B 2 407 ? -20.983 15.959 10.068 1.00 138.45 ? 407 PRO B CB 1 ATOM 10338 C CG . PRO B 2 407 ? -21.468 15.453 11.392 1.00 126.24 ? 407 PRO B CG 1 ATOM 10339 C CD . PRO B 2 407 ? -22.739 14.737 11.089 1.00 128.55 ? 407 PRO B CD 1 ATOM 10340 N N . GLN B 2 408 ? -22.406 14.520 7.559 1.00 154.80 ? 408 GLN B N 1 ATOM 10341 C CA . GLN B 2 408 ? -22.127 13.842 6.291 1.00 160.86 ? 408 GLN B CA 1 ATOM 10342 C C . GLN B 2 408 ? -20.615 13.816 6.032 1.00 171.70 ? 408 GLN B C 1 ATOM 10343 O O . GLN B 2 408 ? -20.158 13.685 4.896 1.00 171.91 ? 408 GLN B O 1 ATOM 10344 C CB . GLN B 2 408 ? -22.883 14.508 5.131 1.00 159.67 ? 408 GLN B CB 1 ATOM 10345 C CG . GLN B 2 408 ? -22.979 13.668 3.858 1.00 162.81 ? 408 GLN B CG 1 ATOM 10346 C CD . GLN B 2 408 ? -23.331 12.217 4.133 1.00 166.60 ? 408 GLN B CD 1 ATOM 10347 O OE1 . GLN B 2 408 ? -24.311 11.921 4.817 1.00 168.04 ? 408 GLN B OE1 1 ATOM 10348 N NE2 . GLN B 2 408 ? -22.526 11.303 3.602 1.00 164.13 ? 408 GLN B NE2 1 ATOM 10349 N N . GLU B 2 409 ? -19.844 13.942 7.108 1.00 169.85 ? 409 GLU B N 1 ATOM 10350 C CA . GLU B 2 409 ? -18.410 13.688 7.069 1.00 159.21 ? 409 GLU B CA 1 ATOM 10351 C C . GLU B 2 409 ? -18.191 12.183 7.156 1.00 162.99 ? 409 GLU B C 1 ATOM 10352 O O . GLU B 2 409 ? -19.054 11.459 7.653 1.00 158.98 ? 409 GLU B O 1 ATOM 10353 C CB . GLU B 2 409 ? -17.688 14.418 8.202 1.00 137.46 ? 409 GLU B CB 1 ATOM 10354 C CG . GLU B 2 409 ? -18.052 13.931 9.594 1.00 135.72 ? 409 GLU B CG 1 ATOM 10355 C CD . GLU B 2 409 ? -17.510 14.834 10.684 1.00 147.01 ? 409 GLU B CD 1 ATOM 10356 O OE1 . GLU B 2 409 ? -17.032 15.941 10.357 1.00 163.12 ? 409 GLU B OE1 1 ATOM 10357 O OE2 . GLU B 2 409 ? -17.561 14.439 11.868 1.00 140.65 ? 409 GLU B OE2 1 ATOM 10358 N N . LYS B 2 410 ? -17.049 11.705 6.674 1.00 159.80 ? 410 LYS B N 1 ATOM 10359 C CA . LYS B 2 410 ? -16.822 10.267 6.611 1.00 154.09 ? 410 LYS B CA 1 ATOM 10360 C C . LYS B 2 410 ? -16.540 9.681 7.992 1.00 147.35 ? 410 LYS B C 1 ATOM 10361 O O . LYS B 2 410 ? -17.390 8.996 8.560 1.00 150.61 ? 410 LYS B O 1 ATOM 10362 C CB . LYS B 2 410 ? -15.666 9.952 5.659 1.00 158.95 ? 410 LYS B CB 1 ATOM 10363 C CG . LYS B 2 410 ? -15.809 10.591 4.287 1.00 169.60 ? 410 LYS B CG 1 ATOM 10364 C CD . LYS B 2 410 ? -14.670 10.185 3.369 1.00 173.95 ? 410 LYS B CD 1 ATOM 10365 C CE . LYS B 2 410 ? -14.723 8.701 3.054 1.00 169.87 ? 410 LYS B CE 1 ATOM 10366 N NZ . LYS B 2 410 ? -15.994 8.332 2.371 1.00 170.99 ? 410 LYS B NZ 1 ATOM 10367 N N . GLU B 2 411 ? -15.360 9.964 8.538 1.00 135.53 ? 411 GLU B N 1 ATOM 10368 C CA . GLU B 2 411 ? -14.997 9.476 9.867 1.00 131.73 ? 411 GLU B CA 1 ATOM 10369 C C . GLU B 2 411 ? -14.086 10.446 10.613 1.00 128.31 ? 411 GLU B C 1 ATOM 10370 O O . GLU B 2 411 ? -13.186 11.045 10.024 1.00 135.89 ? 411 GLU B O 1 ATOM 10371 C CB . GLU B 2 411 ? -14.310 8.108 9.777 1.00 152.97 ? 411 GLU B CB 1 ATOM 10372 C CG . GLU B 2 411 ? -15.241 6.941 9.481 1.00 171.14 ? 411 GLU B CG 1 ATOM 10373 C CD . GLU B 2 411 ? -14.596 5.595 9.750 1.00 180.21 ? 411 GLU B CD 1 ATOM 10374 O OE1 . GLU B 2 411 ? -13.490 5.566 10.329 1.00 186.25 ? 411 GLU B OE1 1 ATOM 10375 O OE2 . GLU B 2 411 ? -15.199 4.563 9.383 1.00 178.53 ? 411 GLU B OE2 1 ATOM 10376 N N . LYS B 2 412 ? -14.323 10.584 11.914 1.00 125.81 ? 412 LYS B N 1 ATOM 10377 C CA . LYS B 2 412 ? -13.448 11.355 12.793 1.00 121.88 ? 412 LYS B CA 1 ATOM 10378 C C . LYS B 2 412 ? -13.331 10.664 14.146 1.00 119.58 ? 412 LYS B C 1 ATOM 10379 O O . LYS B 2 412 ? -14.318 10.160 14.682 1.00 119.36 ? 412 LYS B O 1 ATOM 10380 C CB . LYS B 2 412 ? -13.963 12.787 12.973 1.00 125.73 ? 412 LYS B CB 1 ATOM 10381 C CG . LYS B 2 412 ? -13.861 13.650 11.725 1.00 139.89 ? 412 LYS B CG 1 ATOM 10382 C CD . LYS B 2 412 ? -14.324 15.071 11.983 1.00 145.72 ? 412 LYS B CD 1 ATOM 10383 C CE . LYS B 2 412 ? -13.353 15.825 12.873 1.00 150.23 ? 412 LYS B CE 1 ATOM 10384 N NZ . LYS B 2 412 ? -13.752 17.252 13.021 1.00 134.90 ? 412 LYS B NZ 1 ATOM 10385 N N . SER B 2 413 ? -12.122 10.640 14.694 1.00 117.53 ? 413 SER B N 1 ATOM 10386 C CA . SER B 2 413 ? -11.876 9.978 15.968 1.00 114.34 ? 413 SER B CA 1 ATOM 10387 C C . SER B 2 413 ? -11.375 10.971 17.011 1.00 110.37 ? 413 SER B C 1 ATOM 10388 O O . SER B 2 413 ? -10.468 11.758 16.739 1.00 123.10 ? 413 SER B O 1 ATOM 10389 C CB . SER B 2 413 ? -10.866 8.842 15.791 1.00 116.80 ? 413 SER B CB 1 ATOM 10390 O OG . SER B 2 413 ? -11.290 7.940 14.785 1.00 132.91 ? 413 SER B OG 1 ATOM 10391 N N . PHE B 2 414 ? -11.964 10.937 18.203 1.00 105.82 ? 414 PHE B N 1 ATOM 10392 C CA . PHE B 2 414 ? -11.508 11.806 19.281 1.00 100.25 ? 414 PHE B CA 1 ATOM 10393 C C . PHE B 2 414 ? -10.988 11.001 20.468 1.00 97.28 ? 414 PHE B C 1 ATOM 10394 O O . PHE B 2 414 ? -11.025 9.771 20.462 1.00 98.19 ? 414 PHE B O 1 ATOM 10395 C CB . PHE B 2 414 ? -12.626 12.762 19.718 1.00 97.28 ? 414 PHE B CB 1 ATOM 10396 C CG . PHE B 2 414 ? -13.795 12.091 20.382 1.00 95.83 ? 414 PHE B CG 1 ATOM 10397 C CD1 . PHE B 2 414 ? -13.847 11.964 21.761 1.00 102.58 ? 414 PHE B CD1 1 ATOM 10398 C CD2 . PHE B 2 414 ? -14.858 11.618 19.631 1.00 99.42 ? 414 PHE B CD2 1 ATOM 10399 C CE1 . PHE B 2 414 ? -14.924 11.359 22.376 1.00 105.21 ? 414 PHE B CE1 1 ATOM 10400 C CE2 . PHE B 2 414 ? -15.940 11.015 20.242 1.00 97.54 ? 414 PHE B CE2 1 ATOM 10401 C CZ . PHE B 2 414 ? -15.973 10.885 21.616 1.00 93.02 ? 414 PHE B CZ 1 ATOM 10402 N N . THR B 2 415 ? -10.507 11.706 21.486 1.00 92.78 ? 415 THR B N 1 ATOM 10403 C CA . THR B 2 415 ? -9.827 11.061 22.602 1.00 90.19 ? 415 THR B CA 1 ATOM 10404 C C . THR B 2 415 ? -10.380 11.509 23.951 1.00 85.22 ? 415 THR B C 1 ATOM 10405 O O . THR B 2 415 ? -10.644 12.692 24.164 1.00 97.25 ? 415 THR B O 1 ATOM 10406 C CB . THR B 2 415 ? -8.309 11.350 22.564 1.00 91.46 ? 415 THR B CB 1 ATOM 10407 O OG1 . THR B 2 415 ? -7.788 11.020 21.271 1.00 102.37 ? 415 THR B OG1 1 ATOM 10408 C CG2 . THR B 2 415 ? -7.578 10.540 23.623 1.00 91.06 ? 415 THR B CG2 1 ATOM 10409 N N . ILE B 2 416 ? -10.562 10.553 24.856 1.00 83.15 ? 416 ILE B N 1 ATOM 10410 C CA . ILE B 2 416 ? -10.933 10.852 26.233 1.00 79.17 ? 416 ILE B CA 1 ATOM 10411 C C . ILE B 2 416 ? -9.827 10.367 27.166 1.00 82.53 ? 416 ILE B C 1 ATOM 10412 O O . ILE B 2 416 ? -9.472 9.189 27.163 1.00 93.63 ? 416 ILE B O 1 ATOM 10413 C CB . ILE B 2 416 ? -12.273 10.207 26.614 1.00 77.56 ? 416 ILE B CB 1 ATOM 10414 C CG1 . ILE B 2 416 ? -13.377 10.712 25.683 1.00 80.79 ? 416 ILE B CG1 1 ATOM 10415 C CG2 . ILE B 2 416 ? -12.613 10.509 28.064 1.00 74.87 ? 416 ILE B CG2 1 ATOM 10416 C CD1 . ILE B 2 416 ? -14.729 10.097 25.944 1.00 96.11 ? 416 ILE B CD1 1 ATOM 10417 N N . LYS B 2 417 ? -9.286 11.283 27.963 1.00 77.98 ? 417 LYS B N 1 ATOM 10418 C CA . LYS B 2 417 ? -8.063 11.021 28.711 1.00 78.36 ? 417 LYS B CA 1 ATOM 10419 C C . LYS B 2 417 ? -8.111 11.510 30.150 1.00 88.79 ? 417 LYS B C 1 ATOM 10420 O O . LYS B 2 417 ? -8.662 12.570 30.426 1.00 111.92 ? 417 LYS B O 1 ATOM 10421 C CB . LYS B 2 417 ? -6.878 11.686 28.008 1.00 91.47 ? 417 LYS B CB 1 ATOM 10422 C CG . LYS B 2 417 ? -5.913 10.731 27.344 1.00 107.13 ? 417 LYS B CG 1 ATOM 10423 C CD . LYS B 2 417 ? -4.821 11.485 26.603 1.00 97.58 ? 417 LYS B CD 1 ATOM 10424 C CE . LYS B 2 417 ? -4.188 12.550 27.485 1.00 107.99 ? 417 LYS B CE 1 ATOM 10425 N NZ . LYS B 2 417 ? -3.635 11.984 28.744 1.00 117.54 ? 417 LYS B NZ 1 ATOM 10426 N N . PRO B 2 418 ? -7.516 10.740 31.073 1.00 96.80 ? 418 PRO B N 1 ATOM 10427 C CA . PRO B 2 418 ? -7.231 11.283 32.403 1.00 96.44 ? 418 PRO B CA 1 ATOM 10428 C C . PRO B 2 418 ? -6.082 12.283 32.305 1.00 96.13 ? 418 PRO B C 1 ATOM 10429 O O . PRO B 2 418 ? -5.153 12.051 31.531 1.00 95.45 ? 418 PRO B O 1 ATOM 10430 C CB . PRO B 2 418 ? -6.839 10.046 33.216 1.00 79.68 ? 418 PRO B CB 1 ATOM 10431 C CG . PRO B 2 418 ? -6.320 9.084 32.202 1.00 83.21 ? 418 PRO B CG 1 ATOM 10432 C CD . PRO B 2 418 ? -7.127 9.324 30.954 1.00 89.72 ? 418 PRO B CD 1 ATOM 10433 N N . VAL B 2 419 ? -6.148 13.377 33.057 1.00 86.87 ? 419 VAL B N 1 ATOM 10434 C CA . VAL B 2 419 ? -5.146 14.433 32.944 1.00 84.77 ? 419 VAL B CA 1 ATOM 10435 C C . VAL B 2 419 ? -3.755 13.942 33.338 1.00 86.70 ? 419 VAL B C 1 ATOM 10436 O O . VAL B 2 419 ? -3.560 13.397 34.425 1.00 92.25 ? 419 VAL B O 1 ATOM 10437 C CB . VAL B 2 419 ? -5.511 15.656 33.813 1.00 89.16 ? 419 VAL B CB 1 ATOM 10438 C CG1 . VAL B 2 419 ? -4.409 16.704 33.749 1.00 102.49 ? 419 VAL B CG1 1 ATOM 10439 C CG2 . VAL B 2 419 ? -6.835 16.250 33.365 1.00 84.51 ? 419 VAL B CG2 1 ATOM 10440 N N . GLY B 2 420 ? -2.794 14.136 32.441 1.00 97.34 ? 420 GLY B N 1 ATOM 10441 C CA . GLY B 2 420 ? -1.408 13.795 32.712 1.00 108.92 ? 420 GLY B CA 1 ATOM 10442 C C . GLY B 2 420 ? -1.097 12.311 32.683 1.00 91.88 ? 420 GLY B C 1 ATOM 10443 O O . GLY B 2 420 ? -0.205 11.848 33.394 1.00 95.85 ? 420 GLY B O 1 ATOM 10444 N N . PHE B 2 421 ? -1.826 11.561 31.862 1.00 98.33 ? 421 PHE B N 1 ATOM 10445 C CA . PHE B 2 421 ? -1.590 10.126 31.724 1.00 91.23 ? 421 PHE B CA 1 ATOM 10446 C C . PHE B 2 421 ? -1.607 9.688 30.262 1.00 89.71 ? 421 PHE B C 1 ATOM 10447 O O . PHE B 2 421 ? -2.368 10.217 29.453 1.00 94.51 ? 421 PHE B O 1 ATOM 10448 C CB . PHE B 2 421 ? -2.628 9.334 32.522 1.00 94.57 ? 421 PHE B CB 1 ATOM 10449 C CG . PHE B 2 421 ? -2.250 9.112 33.960 1.00 118.80 ? 421 PHE B CG 1 ATOM 10450 C CD1 . PHE B 2 421 ? -0.921 8.988 34.331 1.00 106.59 ? 421 PHE B CD1 1 ATOM 10451 C CD2 . PHE B 2 421 ? -3.223 9.023 34.940 1.00 122.85 ? 421 PHE B CD2 1 ATOM 10452 C CE1 . PHE B 2 421 ? -0.571 8.783 35.653 1.00 94.89 ? 421 PHE B CE1 1 ATOM 10453 C CE2 . PHE B 2 421 ? -2.879 8.819 36.263 1.00 130.17 ? 421 PHE B CE2 1 ATOM 10454 C CZ . PHE B 2 421 ? -1.552 8.698 36.620 1.00 120.04 ? 421 PHE B CZ 1 ATOM 10455 N N . LYS B 2 422 ? -0.765 8.714 29.932 1.00 92.56 ? 422 LYS B N 1 ATOM 10456 C CA . LYS B 2 422 ? -0.645 8.233 28.561 1.00 95.16 ? 422 LYS B CA 1 ATOM 10457 C C . LYS B 2 422 ? -1.847 7.387 28.151 1.00 99.95 ? 422 LYS B C 1 ATOM 10458 O O . LYS B 2 422 ? -2.257 7.397 26.989 1.00 107.06 ? 422 LYS B O 1 ATOM 10459 C CB . LYS B 2 422 ? 0.647 7.428 28.395 1.00 102.00 ? 422 LYS B CB 1 ATOM 10460 C CG . LYS B 2 422 ? 0.939 7.006 26.965 1.00 116.03 ? 422 LYS B CG 1 ATOM 10461 C CD . LYS B 2 422 ? 1.068 8.214 26.053 1.00 120.64 ? 422 LYS B CD 1 ATOM 10462 C CE . LYS B 2 422 ? 1.354 7.795 24.620 1.00 124.09 ? 422 LYS B CE 1 ATOM 10463 N NZ . LYS B 2 422 ? 1.481 8.967 23.710 1.00 139.60 ? 422 LYS B NZ 1 ATOM 10464 N N . ASP B 2 423 ? -2.408 6.658 29.112 1.00 96.20 ? 423 ASP B N 1 ATOM 10465 C CA . ASP B 2 423 ? -3.566 5.805 28.863 1.00 103.32 ? 423 ASP B CA 1 ATOM 10466 C C . ASP B 2 423 ? -4.762 6.624 28.390 1.00 87.94 ? 423 ASP B C 1 ATOM 10467 O O . ASP B 2 423 ? -5.127 7.621 29.012 1.00 84.44 ? 423 ASP B O 1 ATOM 10468 C CB . ASP B 2 423 ? -3.929 5.017 30.122 1.00 117.51 ? 423 ASP B CB 1 ATOM 10469 C CG . ASP B 2 423 ? -2.841 4.044 30.531 1.00 115.72 ? 423 ASP B CG 1 ATOM 10470 O OD1 . ASP B 2 423 ? -2.863 2.894 30.045 1.00 103.87 ? 423 ASP B OD1 1 ATOM 10471 O OD2 . ASP B 2 423 ? -1.965 4.428 31.334 1.00 115.31 ? 423 ASP B OD2 1 ATOM 10472 N N . SER B 2 424 ? -5.371 6.196 27.289 1.00 98.04 ? 424 SER B N 1 ATOM 10473 C CA . SER B 2 424 ? -6.432 6.972 26.658 1.00 102.39 ? 424 SER B CA 1 ATOM 10474 C C . SER B 2 424 ? -7.599 6.119 26.175 1.00 112.91 ? 424 SER B C 1 ATOM 10475 O O . SER B 2 424 ? -7.428 4.951 25.824 1.00 110.98 ? 424 SER B O 1 ATOM 10476 C CB . SER B 2 424 ? -5.867 7.765 25.479 1.00 104.42 ? 424 SER B CB 1 ATOM 10477 O OG . SER B 2 424 ? -5.291 6.904 24.512 1.00 114.52 ? 424 SER B OG 1 ATOM 10478 N N . LEU B 2 425 ? -8.786 6.716 26.164 1.00 108.11 ? 425 LEU B N 1 ATOM 10479 C CA . LEU B 2 425 ? -9.954 6.103 25.549 1.00 81.73 ? 425 LEU B CA 1 ATOM 10480 C C . LEU B 2 425 ? -10.225 6.766 24.203 1.00 79.85 ? 425 LEU B C 1 ATOM 10481 O O . LEU B 2 425 ? -10.645 7.923 24.147 1.00 95.28 ? 425 LEU B O 1 ATOM 10482 C CB . LEU B 2 425 ? -11.180 6.222 26.458 1.00 86.36 ? 425 LEU B CB 1 ATOM 10483 C CG . LEU B 2 425 ? -12.526 5.792 25.862 1.00 89.78 ? 425 LEU B CG 1 ATOM 10484 C CD1 . LEU B 2 425 ? -12.586 4.288 25.664 1.00 88.05 ? 425 LEU B CD1 1 ATOM 10485 C CD2 . LEU B 2 425 ? -13.680 6.262 26.733 1.00 114.63 ? 425 LEU B CD2 1 ATOM 10486 N N . ILE B 2 426 ? -9.985 6.033 23.121 1.00 91.68 ? 426 ILE B N 1 ATOM 10487 C CA . ILE B 2 426 ? -10.172 6.572 21.779 1.00 89.52 ? 426 ILE B CA 1 ATOM 10488 C C . ILE B 2 426 ? -11.523 6.161 21.208 1.00 95.21 ? 426 ILE B C 1 ATOM 10489 O O . ILE B 2 426 ? -11.856 4.977 21.168 1.00 98.46 ? 426 ILE B O 1 ATOM 10490 C CB . ILE B 2 426 ? -9.052 6.111 20.825 1.00 86.58 ? 426 ILE B CB 1 ATOM 10491 C CG1 . ILE B 2 426 ? -7.692 6.612 21.318 1.00 92.80 ? 426 ILE B CG1 1 ATOM 10492 C CG2 . ILE B 2 426 ? -9.318 6.603 19.411 1.00 82.20 ? 426 ILE B CG2 1 ATOM 10493 C CD1 . ILE B 2 426 ? -6.530 6.188 20.447 1.00 108.97 ? 426 ILE B CD1 1 ATOM 10494 N N . VAL B 2 427 ? -12.302 7.144 20.768 1.00 83.03 ? 427 VAL B N 1 ATOM 10495 C CA . VAL B 2 427 ? -13.631 6.880 20.232 1.00 84.13 ? 427 VAL B CA 1 ATOM 10496 C C . VAL B 2 427 ? -13.715 7.208 18.746 1.00 81.85 ? 427 VAL B C 1 ATOM 10497 O O . VAL B 2 427 ? -13.614 8.368 18.349 1.00 79.69 ? 427 VAL B O 1 ATOM 10498 C CB . VAL B 2 427 ? -14.711 7.681 20.982 1.00 79.97 ? 427 VAL B CB 1 ATOM 10499 C CG1 . VAL B 2 427 ? -16.083 7.416 20.380 1.00 81.78 ? 427 VAL B CG1 1 ATOM 10500 C CG2 . VAL B 2 427 ? -14.698 7.334 22.461 1.00 89.09 ? 427 VAL B CG2 1 ATOM 10501 N N . GLN B 2 428 ? -13.894 6.174 17.931 1.00 85.17 ? 428 GLN B N 1 ATOM 10502 C CA . GLN B 2 428 ? -14.081 6.340 16.494 1.00 86.23 ? 428 GLN B CA 1 ATOM 10503 C C . GLN B 2 428 ? -15.540 6.667 16.198 1.00 88.34 ? 428 GLN B C 1 ATOM 10504 O O . GLN B 2 428 ? -16.439 5.927 16.595 1.00 110.24 ? 428 GLN B O 1 ATOM 10505 C CB . GLN B 2 428 ? -13.656 5.076 15.746 1.00 89.72 ? 428 GLN B CB 1 ATOM 10506 C CG . GLN B 2 428 ? -12.281 4.558 16.134 1.00 96.08 ? 428 GLN B CG 1 ATOM 10507 C CD . GLN B 2 428 ? -11.983 3.192 15.544 1.00 110.63 ? 428 GLN B CD 1 ATOM 10508 O OE1 . GLN B 2 428 ? -11.048 2.511 15.967 1.00 106.19 ? 428 GLN B OE1 1 ATOM 10509 N NE2 . GLN B 2 428 ? -12.779 2.785 14.561 1.00 103.59 ? 428 GLN B NE2 1 ATOM 10510 N N . VAL B 2 429 ? -15.778 7.774 15.502 1.00 86.05 ? 429 VAL B N 1 ATOM 10511 C CA . VAL B 2 429 ? -17.144 8.224 15.263 1.00 94.25 ? 429 VAL B CA 1 ATOM 10512 C C . VAL B 2 429 ? -17.557 8.096 13.801 1.00 113.06 ? 429 VAL B C 1 ATOM 10513 O O . VAL B 2 429 ? -16.855 8.558 12.901 1.00 122.83 ? 429 VAL B O 1 ATOM 10514 C CB . VAL B 2 429 ? -17.336 9.685 15.701 1.00 102.64 ? 429 VAL B CB 1 ATOM 10515 C CG1 . VAL B 2 429 ? -18.814 10.028 15.752 1.00 100.50 ? 429 VAL B CG1 1 ATOM 10516 C CG2 . VAL B 2 429 ? -16.694 9.913 17.054 1.00 125.63 ? 429 VAL B CG2 1 ATOM 10517 N N . THR B 2 430 ? -18.702 7.460 13.580 1.00 120.53 ? 430 THR B N 1 ATOM 10518 C CA . THR B 2 430 ? -19.299 7.370 12.255 1.00 107.78 ? 430 THR B CA 1 ATOM 10519 C C . THR B 2 430 ? -20.752 7.822 12.326 1.00 104.04 ? 430 THR B C 1 ATOM 10520 O O . THR B 2 430 ? -21.411 7.653 13.353 1.00 107.00 ? 430 THR B O 1 ATOM 10521 C CB . THR B 2 430 ? -19.232 5.938 11.685 1.00 113.13 ? 430 THR B CB 1 ATOM 10522 O OG1 . THR B 2 430 ? -19.967 5.048 12.534 1.00 130.86 ? 430 THR B OG1 1 ATOM 10523 C CG2 . THR B 2 430 ? -17.791 5.462 11.588 1.00 113.73 ? 430 THR B CG2 1 ATOM 10524 N N . PHE B 2 431 ? -21.248 8.404 11.240 1.00 111.94 ? 431 PHE B N 1 ATOM 10525 C CA . PHE B 2 431 ? -22.624 8.884 11.206 1.00 119.13 ? 431 PHE B CA 1 ATOM 10526 C C . PHE B 2 431 ? -23.428 8.199 10.107 1.00 122.31 ? 431 PHE B C 1 ATOM 10527 O O . PHE B 2 431 ? -23.057 8.247 8.934 1.00 133.45 ? 431 PHE B O 1 ATOM 10528 C CB . PHE B 2 431 ? -22.658 10.400 11.006 1.00 114.50 ? 431 PHE B CB 1 ATOM 10529 C CG . PHE B 2 431 ? -21.873 11.167 12.032 1.00 110.67 ? 431 PHE B CG 1 ATOM 10530 C CD1 . PHE B 2 431 ? -20.598 11.624 11.747 1.00 114.01 ? 431 PHE B CD1 1 ATOM 10531 C CD2 . PHE B 2 431 ? -22.411 11.431 13.281 1.00 102.16 ? 431 PHE B CD2 1 ATOM 10532 C CE1 . PHE B 2 431 ? -19.872 12.333 12.688 1.00 108.03 ? 431 PHE B CE1 1 ATOM 10533 C CE2 . PHE B 2 431 ? -21.690 12.136 14.225 1.00 92.05 ? 431 PHE B CE2 1 ATOM 10534 C CZ . PHE B 2 431 ? -20.420 12.589 13.927 1.00 95.84 ? 431 PHE B CZ 1 ATOM 10535 N N . ASP B 2 432 ? -24.530 7.563 10.491 1.00 115.06 ? 432 ASP B N 1 ATOM 10536 C CA . ASP B 2 432 ? -25.415 6.932 9.521 1.00 120.50 ? 432 ASP B CA 1 ATOM 10537 C C . ASP B 2 432 ? -26.534 7.883 9.123 1.00 130.22 ? 432 ASP B C 1 ATOM 10538 O O . ASP B 2 432 ? -27.419 8.188 9.920 1.00 132.43 ? 432 ASP B O 1 ATOM 10539 C CB . ASP B 2 432 ? -26.002 5.634 10.082 1.00 134.17 ? 432 ASP B CB 1 ATOM 10540 C CG . ASP B 2 432 ? -25.034 4.471 9.999 1.00 143.83 ? 432 ASP B CG 1 ATOM 10541 O OD1 . ASP B 2 432 ? -23.809 4.708 10.060 1.00 140.56 ? 432 ASP B OD1 1 ATOM 10542 O OD2 . ASP B 2 432 ? -25.500 3.319 9.870 1.00 146.45 ? 432 ASP B OD2 1 ATOM 10543 N N . CYS B 2 433 ? -26.485 8.344 7.878 1.00 136.72 ? 433 CYS B N 1 ATOM 10544 C CA . CYS B 2 433 ? -27.475 9.273 7.353 1.00 135.69 ? 433 CYS B CA 1 ATOM 10545 C C . CYS B 2 433 ? -28.022 8.759 6.029 1.00 151.18 ? 433 CYS B C 1 ATOM 10546 O O . CYS B 2 433 ? -29.213 8.475 5.904 1.00 162.97 ? 433 CYS B O 1 ATOM 10547 C CB . CYS B 2 433 ? -26.871 10.667 7.180 1.00 130.41 ? 433 CYS B CB 1 ATOM 10548 S SG . CYS B 2 433 ? -26.307 11.426 8.720 1.00 152.89 ? 433 CYS B SG 1 ATOM 10549 N N . ASP B 2 434 ? -27.141 8.659 5.040 1.00 155.16 ? 434 ASP B N 1 ATOM 10550 C CA . ASP B 2 434 ? -27.500 8.124 3.733 1.00 168.38 ? 434 ASP B CA 1 ATOM 10551 C C . ASP B 2 434 ? -27.978 6.681 3.847 1.00 169.10 ? 434 ASP B C 1 ATOM 10552 O O . ASP B 2 434 ? -27.332 5.851 4.487 1.00 161.98 ? 434 ASP B O 1 ATOM 10553 C CB . ASP B 2 434 ? -26.310 8.208 2.776 1.00 174.55 ? 434 ASP B CB 1 ATOM 10554 C CG . ASP B 2 434 ? -25.670 9.582 2.762 1.00 173.54 ? 434 ASP B CG 1 ATOM 10555 O OD1 . ASP B 2 434 ? -26.386 10.575 3.004 1.00 177.33 ? 434 ASP B OD1 1 ATOM 10556 O OD2 . ASP B 2 434 ? -24.449 9.668 2.510 1.00 171.19 ? 434 ASP B OD2 1 ATOM 10557 N N . CYS B 2 435 ? -29.113 6.390 3.222 1.00 165.98 ? 435 CYS B N 1 ATOM 10558 C CA . CYS B 2 435 ? -29.694 5.055 3.268 1.00 163.23 ? 435 CYS B CA 1 ATOM 10559 C C . CYS B 2 435 ? -28.910 4.068 2.411 1.00 162.48 ? 435 CYS B C 1 ATOM 10560 O O . CYS B 2 435 ? -28.150 4.462 1.527 1.00 162.16 ? 435 CYS B O 1 ATOM 10561 C CB . CYS B 2 435 ? -31.154 5.098 2.819 1.00 161.52 ? 435 CYS B CB 1 ATOM 10562 S SG . CYS B 2 435 ? -32.198 6.139 3.858 1.00 216.49 ? 435 CYS B SG 1 ATOM 10563 N N . ALA B 2 436 ? -29.097 2.781 2.685 1.00 159.40 ? 436 ALA B N 1 ATOM 10564 C CA . ALA B 2 436 ? -28.407 1.726 1.951 1.00 160.71 ? 436 ALA B CA 1 ATOM 10565 C C . ALA B 2 436 ? -28.907 1.610 0.513 1.00 176.09 ? 436 ALA B C 1 ATOM 10566 O O . ALA B 2 436 ? -28.317 0.901 -0.302 1.00 179.70 ? 436 ALA B O 1 ATOM 10567 C CB . ALA B 2 436 ? -28.565 0.396 2.671 1.00 155.75 ? 436 ALA B CB 1 ATOM 10568 N N . CYS B 2 437 ? -29.997 2.307 0.205 1.00 186.22 ? 437 CYS B N 1 ATOM 10569 C CA . CYS B 2 437 ? -30.561 2.290 -1.139 1.00 198.80 ? 437 CYS B CA 1 ATOM 10570 C C . CYS B 2 437 ? -29.962 3.398 -2.000 1.00 208.17 ? 437 CYS B C 1 ATOM 10571 O O . CYS B 2 437 ? -30.353 3.576 -3.154 1.00 218.72 ? 437 CYS B O 1 ATOM 10572 C CB . CYS B 2 437 ? -32.084 2.428 -1.087 1.00 195.60 ? 437 CYS B CB 1 ATOM 10573 S SG . CYS B 2 437 ? -32.670 4.052 -0.553 1.00 205.89 ? 437 CYS B SG 1 ATOM 10574 N N . GLN B 2 438 ? -29.017 4.141 -1.430 1.00 199.85 ? 438 GLN B N 1 ATOM 10575 C CA . GLN B 2 438 ? -28.342 5.217 -2.150 1.00 195.84 ? 438 GLN B CA 1 ATOM 10576 C C . GLN B 2 438 ? -27.663 4.670 -3.400 1.00 193.15 ? 438 GLN B C 1 ATOM 10577 O O . GLN B 2 438 ? -27.696 5.294 -4.461 1.00 196.81 ? 438 GLN B O 1 ATOM 10578 C CB . GLN B 2 438 ? -27.317 5.912 -1.253 1.00 201.99 ? 438 GLN B CB 1 ATOM 10579 C CG . GLN B 2 438 ? -26.935 7.309 -1.714 1.00 205.58 ? 438 GLN B CG 1 ATOM 10580 C CD . GLN B 2 438 ? -27.956 8.355 -1.307 1.00 204.84 ? 438 GLN B CD 1 ATOM 10581 O OE1 . GLN B 2 438 ? -28.593 8.241 -0.260 1.00 202.17 ? 438 GLN B OE1 1 ATOM 10582 N NE2 . GLN B 2 438 ? -28.118 9.380 -2.136 1.00 203.20 ? 438 GLN B NE2 1 ATOM 10583 N N . ALA B 2 439 ? -27.049 3.500 -3.264 1.00 194.77 ? 439 ALA B N 1 ATOM 10584 C CA . ALA B 2 439 ? -26.487 2.795 -4.408 1.00 195.82 ? 439 ALA B CA 1 ATOM 10585 C C . ALA B 2 439 ? -27.619 2.291 -5.294 1.00 200.70 ? 439 ALA B C 1 ATOM 10586 O O . ALA B 2 439 ? -28.661 1.865 -4.794 1.00 200.22 ? 439 ALA B O 1 ATOM 10587 C CB . ALA B 2 439 ? -25.604 1.647 -3.953 1.00 196.16 ? 439 ALA B CB 1 ATOM 10588 N N . GLN B 2 440 ? -27.402 2.343 -6.605 1.00 205.62 ? 440 GLN B N 1 ATOM 10589 C CA . GLN B 2 440 ? -28.439 2.049 -7.591 1.00 214.10 ? 440 GLN B CA 1 ATOM 10590 C C . GLN B 2 440 ? -29.690 2.886 -7.334 1.00 217.20 ? 440 GLN B C 1 ATOM 10591 O O . GLN B 2 440 ? -30.770 2.355 -7.071 1.00 217.48 ? 440 GLN B O 1 ATOM 10592 C CB . GLN B 2 440 ? -28.786 0.558 -7.591 1.00 217.97 ? 440 GLN B CB 1 ATOM 10593 C CG . GLN B 2 440 ? -28.073 -0.247 -8.667 1.00 223.62 ? 440 GLN B CG 1 ATOM 10594 C CD . GLN B 2 440 ? -28.658 -0.020 -10.048 1.00 228.87 ? 440 GLN B CD 1 ATOM 10595 O OE1 . GLN B 2 440 ? -29.802 -0.386 -10.318 1.00 231.00 ? 440 GLN B OE1 1 ATOM 10596 N NE2 . GLN B 2 440 ? -27.874 0.589 -10.931 1.00 228.97 ? 440 GLN B NE2 1 ATOM 10597 N N . ALA B 2 441 ? -29.523 4.201 -7.416 1.00 216.01 ? 441 ALA B N 1 ATOM 10598 C CA . ALA B 2 441 ? -30.631 5.145 -7.359 1.00 219.47 ? 441 ALA B CA 1 ATOM 10599 C C . ALA B 2 441 ? -31.052 5.482 -8.782 1.00 229.42 ? 441 ALA B C 1 ATOM 10600 O O . ALA B 2 441 ? -31.857 6.385 -9.004 1.00 232.52 ? 441 ALA B O 1 ATOM 10601 C CB . ALA B 2 441 ? -30.238 6.399 -6.598 1.00 211.56 ? 441 ALA B CB 1 ATOM 10602 N N . GLU B 2 442 ? -30.444 4.757 -9.722 1.00 235.77 ? 442 GLU B N 1 ATOM 10603 C CA . GLU B 2 442 ? -30.543 4.958 -11.170 1.00 240.22 ? 442 GLU B CA 1 ATOM 10604 C C . GLU B 2 442 ? -29.678 6.163 -11.548 1.00 242.86 ? 442 GLU B C 1 ATOM 10605 O O . GLU B 2 442 ? -29.529 7.095 -10.757 1.00 238.69 ? 442 GLU B O 1 ATOM 10606 C CB . GLU B 2 442 ? -32.005 5.141 -11.611 1.00 236.24 ? 442 GLU B CB 1 ATOM 10607 C CG . GLU B 2 442 ? -32.309 4.753 -13.049 1.00 236.56 ? 442 GLU B CG 1 ATOM 10608 C CD . GLU B 2 442 ? -33.720 4.229 -13.228 1.00 235.10 ? 442 GLU B CD 1 ATOM 10609 O OE1 . GLU B 2 442 ? -34.435 4.090 -12.215 1.00 228.90 ? 442 GLU B OE1 1 ATOM 10610 O OE2 . GLU B 2 442 ? -34.109 3.951 -14.382 1.00 238.50 ? 442 GLU B OE2 1 ATOM 10611 N N . PRO B 2 443 ? -29.102 6.150 -12.761 1.00 246.30 ? 443 PRO B N 1 ATOM 10612 C CA . PRO B 2 443 ? -28.217 7.247 -13.170 1.00 244.23 ? 443 PRO B CA 1 ATOM 10613 C C . PRO B 2 443 ? -28.920 8.583 -13.407 1.00 245.17 ? 443 PRO B C 1 ATOM 10614 O O . PRO B 2 443 ? -28.329 9.627 -13.133 1.00 241.46 ? 443 PRO B O 1 ATOM 10615 C CB . PRO B 2 443 ? -27.597 6.729 -14.477 1.00 244.80 ? 443 PRO B CB 1 ATOM 10616 C CG . PRO B 2 443 ? -28.494 5.623 -14.929 1.00 244.63 ? 443 PRO B CG 1 ATOM 10617 C CD . PRO B 2 443 ? -28.992 4.998 -13.672 1.00 244.26 ? 443 PRO B CD 1 ATOM 10618 N N . ASN B 2 444 ? -30.154 8.555 -13.903 1.00 247.48 ? 444 ASN B N 1 ATOM 10619 C CA . ASN B 2 444 ? -30.804 9.786 -14.342 1.00 243.31 ? 444 ASN B CA 1 ATOM 10620 C C . ASN B 2 444 ? -32.244 9.982 -13.870 1.00 241.06 ? 444 ASN B C 1 ATOM 10621 O O . ASN B 2 444 ? -32.767 9.217 -13.059 1.00 234.54 ? 444 ASN B O 1 ATOM 10622 C CB . ASN B 2 444 ? -30.761 9.873 -15.870 1.00 245.66 ? 444 ASN B CB 1 ATOM 10623 C CG . ASN B 2 444 ? -29.392 10.263 -16.391 1.00 242.63 ? 444 ASN B CG 1 ATOM 10624 O OD1 . ASN B 2 444 ? -28.647 10.985 -15.728 1.00 234.96 ? 444 ASN B OD1 1 ATOM 10625 N ND2 . ASN B 2 444 ? -29.054 9.790 -17.584 1.00 249.97 ? 444 ASN B ND2 1 ATOM 10626 N N . SER B 2 445 ? -32.867 11.031 -14.403 1.00 244.58 ? 445 SER B N 1 ATOM 10627 C CA . SER B 2 445 ? -34.181 11.508 -13.978 1.00 243.43 ? 445 SER B CA 1 ATOM 10628 C C . SER B 2 445 ? -35.357 10.645 -14.436 1.00 246.07 ? 445 SER B C 1 ATOM 10629 O O . SER B 2 445 ? -36.502 10.913 -14.075 1.00 248.84 ? 445 SER B O 1 ATOM 10630 C CB . SER B 2 445 ? -34.387 12.938 -14.480 1.00 243.51 ? 445 SER B CB 1 ATOM 10631 O OG . SER B 2 445 ? -34.222 13.014 -15.885 1.00 247.68 ? 445 SER B OG 1 ATOM 10632 N N . HIS B 2 446 ? -35.076 9.614 -15.224 1.00 242.74 ? 446 HIS B N 1 ATOM 10633 C CA . HIS B 2 446 ? -36.126 8.832 -15.874 1.00 245.68 ? 446 HIS B CA 1 ATOM 10634 C C . HIS B 2 446 ? -36.869 7.899 -14.917 1.00 240.15 ? 446 HIS B C 1 ATOM 10635 O O . HIS B 2 446 ? -36.740 8.022 -13.697 1.00 232.38 ? 446 HIS B O 1 ATOM 10636 C CB . HIS B 2 446 ? -35.536 8.016 -17.026 1.00 250.96 ? 446 HIS B CB 1 ATOM 10637 C CG . HIS B 2 446 ? -35.791 8.606 -18.378 1.00 252.79 ? 446 HIS B CG 1 ATOM 10638 N ND1 . HIS B 2 446 ? -36.820 8.183 -19.191 1.00 253.93 ? 446 HIS B ND1 1 ATOM 10639 C CD2 . HIS B 2 446 ? -35.152 9.586 -19.059 1.00 252.44 ? 446 HIS B CD2 1 ATOM 10640 C CE1 . HIS B 2 446 ? -36.804 8.876 -20.316 1.00 256.01 ? 446 HIS B CE1 1 ATOM 10641 N NE2 . HIS B 2 446 ? -35.802 9.735 -20.261 1.00 256.38 ? 446 HIS B NE2 1 ATOM 10642 N N . ARG B 2 447 ? -37.688 7.022 -15.507 1.00 243.02 ? 447 ARG B N 1 ATOM 10643 C CA . ARG B 2 447 ? -38.431 5.943 -14.835 1.00 237.85 ? 447 ARG B CA 1 ATOM 10644 C C . ARG B 2 447 ? -39.768 6.413 -14.249 1.00 235.52 ? 447 ARG B C 1 ATOM 10645 O O . ARG B 2 447 ? -40.548 5.602 -13.752 1.00 232.86 ? 447 ARG B O 1 ATOM 10646 C CB . ARG B 2 447 ? -37.575 5.282 -13.742 1.00 228.39 ? 447 ARG B CB 1 ATOM 10647 C CG . ARG B 2 447 ? -37.819 3.791 -13.545 1.00 226.97 ? 447 ARG B CG 1 ATOM 10648 C CD . ARG B 2 447 ? -38.751 3.522 -12.376 1.00 222.49 ? 447 ARG B CD 1 ATOM 10649 N NE . ARG B 2 447 ? -38.883 2.096 -12.095 1.00 220.04 ? 447 ARG B NE 1 ATOM 10650 C CZ . ARG B 2 447 ? -39.757 1.582 -11.236 1.00 212.35 ? 447 ARG B CZ 1 ATOM 10651 N NH1 . ARG B 2 447 ? -40.588 2.377 -10.576 1.00 203.86 ? 447 ARG B NH1 1 ATOM 10652 N NH2 . ARG B 2 447 ? -39.806 0.271 -11.042 1.00 216.66 ? 447 ARG B NH2 1 ATOM 10653 N N . CYS B 2 448 ? -40.051 7.709 -14.327 1.00 234.47 ? 448 CYS B N 1 ATOM 10654 C CA . CYS B 2 448 ? -41.337 8.215 -13.850 1.00 233.08 ? 448 CYS B CA 1 ATOM 10655 C C . CYS B 2 448 ? -42.304 8.463 -15.002 1.00 237.49 ? 448 CYS B C 1 ATOM 10656 O O . CYS B 2 448 ? -43.241 7.693 -15.216 1.00 238.50 ? 448 CYS B O 1 ATOM 10657 C CB . CYS B 2 448 ? -41.144 9.502 -13.047 1.00 226.77 ? 448 CYS B CB 1 ATOM 10658 S SG . CYS B 2 448 ? -41.307 9.288 -11.265 1.00 233.26 ? 448 CYS B SG 1 ATOM 10659 N N . ASN B 2 449 ? -42.069 9.541 -15.741 1.00 238.33 ? 449 ASN B N 1 ATOM 10660 C CA . ASN B 2 449 ? -42.848 9.847 -16.934 1.00 248.39 ? 449 ASN B CA 1 ATOM 10661 C C . ASN B 2 449 ? -41.906 10.110 -18.098 1.00 253.01 ? 449 ASN B C 1 ATOM 10662 O O . ASN B 2 449 ? -41.880 9.364 -19.077 1.00 257.57 ? 449 ASN B O 1 ATOM 10663 C CB . ASN B 2 449 ? -43.764 11.049 -16.699 1.00 250.39 ? 449 ASN B CB 1 ATOM 10664 C CG . ASN B 2 449 ? -44.649 11.355 -17.895 1.00 264.10 ? 449 ASN B CG 1 ATOM 10665 O OD1 . ASN B 2 449 ? -44.946 10.476 -18.704 1.00 265.35 ? 449 ASN B OD1 1 ATOM 10666 N ND2 . ASN B 2 449 ? -45.073 12.608 -18.012 1.00 269.77 ? 449 ASN B ND2 1 ATOM 10667 N N . ASN B 2 450 ? -41.133 11.184 -17.978 1.00 250.37 ? 450 ASN B N 1 ATOM 10668 C CA . ASN B 2 450 ? -40.084 11.491 -18.940 1.00 255.65 ? 450 ASN B CA 1 ATOM 10669 C C . ASN B 2 450 ? -38.751 11.766 -18.253 1.00 254.11 ? 450 ASN B C 1 ATOM 10670 O O . ASN B 2 450 ? -37.797 11.005 -18.403 1.00 256.83 ? 450 ASN B O 1 ATOM 10671 C CB . ASN B 2 450 ? -40.475 12.688 -19.805 1.00 256.79 ? 450 ASN B CB 1 ATOM 10672 C CG . ASN B 2 450 ? -39.344 13.147 -20.706 1.00 253.19 ? 450 ASN B CG 1 ATOM 10673 O OD1 . ASN B 2 450 ? -39.088 12.551 -21.753 1.00 254.24 ? 450 ASN B OD1 1 ATOM 10674 N ND2 . ASN B 2 450 ? -38.660 14.212 -20.302 1.00 249.72 ? 450 ASN B ND2 1 ATOM 10675 N N . GLY B 2 451 ? -38.695 12.854 -17.490 1.00 253.04 ? 451 GLY B N 1 ATOM 10676 C CA . GLY B 2 451 ? -37.448 13.294 -16.890 1.00 251.62 ? 451 GLY B CA 1 ATOM 10677 C C . GLY B 2 451 ? -37.600 14.517 -16.008 1.00 254.88 ? 451 GLY B C 1 ATOM 10678 O O . GLY B 2 451 ? -38.689 14.790 -15.499 1.00 254.96 ? 451 GLY B O 1 ATOM 10679 N N . ASN B 2 452 ? -36.485 15.223 -15.805 1.00 258.63 ? 452 ASN B N 1 ATOM 10680 C CA . ASN B 2 452 ? -36.406 16.449 -15.001 1.00 258.01 ? 452 ASN B CA 1 ATOM 10681 C C . ASN B 2 452 ? -36.531 16.182 -13.500 1.00 257.84 ? 452 ASN B C 1 ATOM 10682 O O . ASN B 2 452 ? -36.389 17.092 -12.685 1.00 257.35 ? 452 ASN B O 1 ATOM 10683 C CB . ASN B 2 452 ? -37.466 17.464 -15.442 1.00 258.66 ? 452 ASN B CB 1 ATOM 10684 C CG . ASN B 2 452 ? -37.412 17.754 -16.929 1.00 260.79 ? 452 ASN B CG 1 ATOM 10685 O OD1 . ASN B 2 452 ? -36.784 17.023 -17.694 1.00 260.45 ? 452 ASN B OD1 1 ATOM 10686 N ND2 . ASN B 2 452 ? -38.078 18.824 -17.348 1.00 262.99 ? 452 ASN B ND2 1 ATOM 10687 N N . GLY B 2 453 ? -36.798 14.929 -13.146 1.00 257.93 ? 453 GLY B N 1 ATOM 10688 C CA . GLY B 2 453 ? -36.896 14.516 -11.758 1.00 252.97 ? 453 GLY B CA 1 ATOM 10689 C C . GLY B 2 453 ? -35.636 13.825 -11.270 1.00 249.69 ? 453 GLY B C 1 ATOM 10690 O O . GLY B 2 453 ? -34.524 14.182 -11.655 1.00 248.66 ? 453 GLY B O 1 ATOM 10691 N N . THR B 2 454 ? -35.820 12.850 -10.387 1.00 247.73 ? 454 THR B N 1 ATOM 10692 C CA . THR B 2 454 ? -34.736 11.988 -9.926 1.00 241.64 ? 454 THR B CA 1 ATOM 10693 C C . THR B 2 454 ? -35.314 10.615 -9.610 1.00 238.15 ? 454 THR B C 1 ATOM 10694 O O . THR B 2 454 ? -36.447 10.327 -9.983 1.00 238.21 ? 454 THR B O 1 ATOM 10695 C CB . THR B 2 454 ? -34.029 12.560 -8.686 1.00 235.50 ? 454 THR B CB 1 ATOM 10696 O OG1 . THR B 2 454 ? -33.000 11.657 -8.262 1.00 232.38 ? 454 THR B OG1 1 ATOM 10697 C CG2 . THR B 2 454 ? -35.021 12.760 -7.551 1.00 232.11 ? 454 THR B CG2 1 ATOM 10698 N N . PHE B 2 455 ? -34.527 9.744 -8.988 1.00 233.49 ? 455 PHE B N 1 ATOM 10699 C CA . PHE B 2 455 ? -35.082 8.514 -8.429 1.00 232.14 ? 455 PHE B CA 1 ATOM 10700 C C . PHE B 2 455 ? -34.470 8.175 -7.069 1.00 233.30 ? 455 PHE B C 1 ATOM 10701 O O . PHE B 2 455 ? -33.269 7.918 -6.988 1.00 237.23 ? 455 PHE B O 1 ATOM 10702 C CB . PHE B 2 455 ? -34.876 7.353 -9.409 1.00 227.85 ? 455 PHE B CB 1 ATOM 10703 C CG . PHE B 2 455 ? -35.516 6.063 -8.973 1.00 222.62 ? 455 PHE B CG 1 ATOM 10704 C CD1 . PHE B 2 455 ? -36.855 5.817 -9.229 1.00 222.05 ? 455 PHE B CD1 1 ATOM 10705 C CD2 . PHE B 2 455 ? -34.774 5.090 -8.322 1.00 216.87 ? 455 PHE B CD2 1 ATOM 10706 C CE1 . PHE B 2 455 ? -37.445 4.630 -8.834 1.00 219.62 ? 455 PHE B CE1 1 ATOM 10707 C CE2 . PHE B 2 455 ? -35.358 3.902 -7.925 1.00 216.52 ? 455 PHE B CE2 1 ATOM 10708 C CZ . PHE B 2 455 ? -36.695 3.672 -8.182 1.00 217.17 ? 455 PHE B CZ 1 ATOM 10709 N N . GLU B 2 456 ? -35.269 8.168 -6.001 1.00 229.06 ? 456 GLU B N 1 ATOM 10710 C CA . GLU B 2 456 ? -34.783 7.553 -4.767 1.00 215.74 ? 456 GLU B CA 1 ATOM 10711 C C . GLU B 2 456 ? -35.770 6.578 -4.116 1.00 203.09 ? 456 GLU B C 1 ATOM 10712 O O . GLU B 2 456 ? -36.697 6.974 -3.408 1.00 201.62 ? 456 GLU B O 1 ATOM 10713 C CB . GLU B 2 456 ? -34.424 8.649 -3.760 1.00 206.65 ? 456 GLU B CB 1 ATOM 10714 C CG . GLU B 2 456 ? -33.691 8.157 -2.526 1.00 202.98 ? 456 GLU B CG 1 ATOM 10715 C CD . GLU B 2 456 ? -32.198 8.039 -2.748 1.00 200.54 ? 456 GLU B CD 1 ATOM 10716 O OE1 . GLU B 2 456 ? -31.724 8.446 -3.830 1.00 201.76 ? 456 GLU B OE1 1 ATOM 10717 O OE2 . GLU B 2 456 ? -31.498 7.544 -1.842 1.00 197.01 ? 456 GLU B OE2 1 ATOM 10718 N N . CYS B 2 457 ? -35.538 5.298 -4.380 1.00 191.97 ? 457 CYS B N 1 ATOM 10719 C CA . CYS B 2 457 ? -35.917 4.131 -3.578 1.00 188.01 ? 457 CYS B CA 1 ATOM 10720 C C . CYS B 2 457 ? -37.391 3.914 -3.209 1.00 188.84 ? 457 CYS B C 1 ATOM 10721 O O . CYS B 2 457 ? -37.834 2.767 -3.133 1.00 186.56 ? 457 CYS B O 1 ATOM 10722 C CB . CYS B 2 457 ? -35.122 4.155 -2.269 1.00 182.85 ? 457 CYS B CB 1 ATOM 10723 S SG . CYS B 2 457 ? -33.331 4.238 -2.466 1.00 223.27 ? 457 CYS B SG 1 ATOM 10724 N N . GLY B 2 458 ? -38.156 4.978 -2.980 1.00 188.96 ? 458 GLY B N 1 ATOM 10725 C CA . GLY B 2 458 ? -39.595 4.832 -2.830 1.00 189.27 ? 458 GLY B CA 1 ATOM 10726 C C . GLY B 2 458 ? -40.489 5.629 -3.756 1.00 181.85 ? 458 GLY B C 1 ATOM 10727 O O . GLY B 2 458 ? -41.665 5.315 -3.935 1.00 172.27 ? 458 GLY B O 1 ATOM 10728 N N . VAL B 2 459 ? -39.917 6.672 -4.347 1.00 190.08 ? 459 VAL B N 1 ATOM 10729 C CA . VAL B 2 459 ? -40.715 7.764 -4.898 1.00 201.19 ? 459 VAL B CA 1 ATOM 10730 C C . VAL B 2 459 ? -40.279 8.160 -6.296 1.00 209.97 ? 459 VAL B C 1 ATOM 10731 O O . VAL B 2 459 ? -41.065 8.086 -7.241 1.00 219.25 ? 459 VAL B O 1 ATOM 10732 C CB . VAL B 2 459 ? -40.658 9.023 -3.998 1.00 197.48 ? 459 VAL B CB 1 ATOM 10733 C CG1 . VAL B 2 459 ? -41.670 10.054 -4.470 1.00 200.67 ? 459 VAL B CG1 1 ATOM 10734 C CG2 . VAL B 2 459 ? -40.917 8.666 -2.541 1.00 187.63 ? 459 VAL B CG2 1 ATOM 10735 N N . CYS B 2 460 ? -39.022 8.606 -6.367 1.00 207.20 ? 460 CYS B N 1 ATOM 10736 C CA . CYS B 2 460 ? -38.369 9.261 -7.509 1.00 215.54 ? 460 CYS B CA 1 ATOM 10737 C C . CYS B 2 460 ? -38.612 10.767 -7.477 1.00 221.05 ? 460 CYS B C 1 ATOM 10738 O O . CYS B 2 460 ? -38.007 11.514 -8.243 1.00 221.74 ? 460 CYS B O 1 ATOM 10739 C CB . CYS B 2 460 ? -38.823 8.685 -8.856 1.00 226.44 ? 460 CYS B CB 1 ATOM 10740 S SG . CYS B 2 460 ? -40.065 9.680 -9.710 1.00 246.60 ? 460 CYS B SG 1 ATOM 10741 N N . ARG B 2 461 ? -39.475 11.206 -6.563 1.00 222.73 ? 461 ARG B N 1 ATOM 10742 C CA . ARG B 2 461 ? -39.796 12.622 -6.401 1.00 219.19 ? 461 ARG B CA 1 ATOM 10743 C C . ARG B 2 461 ? -40.169 13.230 -7.749 1.00 227.12 ? 461 ARG B C 1 ATOM 10744 O O . ARG B 2 461 ? -40.878 12.603 -8.538 1.00 235.88 ? 461 ARG B O 1 ATOM 10745 C CB . ARG B 2 461 ? -38.617 13.380 -5.775 1.00 211.26 ? 461 ARG B CB 1 ATOM 10746 C CG . ARG B 2 461 ? -37.818 12.566 -4.762 1.00 208.49 ? 461 ARG B CG 1 ATOM 10747 C CD . ARG B 2 461 ? -36.733 13.394 -4.087 1.00 202.37 ? 461 ARG B CD 1 ATOM 10748 N NE . ARG B 2 461 ? -37.215 14.030 -2.864 1.00 201.98 ? 461 ARG B NE 1 ATOM 10749 C CZ . ARG B 2 461 ? -36.451 14.728 -2.031 1.00 202.13 ? 461 ARG B CZ 1 ATOM 10750 N NH1 . ARG B 2 461 ? -35.160 14.888 -2.287 1.00 199.53 ? 461 ARG B NH1 1 ATOM 10751 N NH2 . ARG B 2 461 ? -36.979 15.268 -0.941 1.00 204.45 ? 461 ARG B NH2 1 ATOM 10752 N N . CYS B 2 462 ? -39.662 14.433 -8.007 1.00 224.32 ? 462 CYS B N 1 ATOM 10753 C CA . CYS B 2 462 ? -39.786 15.107 -9.300 1.00 230.46 ? 462 CYS B CA 1 ATOM 10754 C C . CYS B 2 462 ? -39.097 16.467 -9.246 1.00 230.07 ? 462 CYS B C 1 ATOM 10755 O O . CYS B 2 462 ? -38.611 16.884 -8.195 1.00 220.47 ? 462 CYS B O 1 ATOM 10756 C CB . CYS B 2 462 ? -41.249 15.278 -9.713 1.00 233.10 ? 462 CYS B CB 1 ATOM 10757 S SG . CYS B 2 462 ? -41.756 14.255 -11.121 1.00 234.68 ? 462 CYS B SG 1 ATOM 10758 N N . GLY B 2 463 ? -39.062 17.154 -10.382 1.00 211.85 ? 463 GLY B N 1 ATOM 10759 C CA . GLY B 2 463 ? -38.349 18.414 -10.487 1.00 214.71 ? 463 GLY B CA 1 ATOM 10760 C C . GLY B 2 463 ? -39.084 19.633 -9.962 1.00 207.85 ? 463 GLY B C 1 ATOM 10761 O O . GLY B 2 463 ? -40.023 19.514 -9.175 1.00 205.07 ? 463 GLY B O 1 ATOM 10762 N N . PRO B 2 464 ? -38.652 20.823 -10.409 1.00 204.17 ? 464 PRO B N 1 ATOM 10763 C CA . PRO B 2 464 ? -39.146 22.152 -10.029 1.00 208.49 ? 464 PRO B CA 1 ATOM 10764 C C . PRO B 2 464 ? -40.502 22.476 -10.649 1.00 209.52 ? 464 PRO B C 1 ATOM 10765 O O . PRO B 2 464 ? -40.548 23.088 -11.715 1.00 216.10 ? 464 PRO B O 1 ATOM 10766 C CB . PRO B 2 464 ? -38.069 23.103 -10.570 1.00 206.83 ? 464 PRO B CB 1 ATOM 10767 C CG . PRO B 2 464 ? -36.891 22.236 -10.894 1.00 201.60 ? 464 PRO B CG 1 ATOM 10768 C CD . PRO B 2 464 ? -37.477 20.923 -11.288 1.00 197.97 ? 464 PRO B CD 1 ATOM 10769 N N . GLY B 2 465 ? -41.585 22.079 -9.991 1.00 204.09 ? 465 GLY B N 1 ATOM 10770 C CA . GLY B 2 465 ? -42.904 22.263 -10.566 1.00 209.94 ? 465 GLY B CA 1 ATOM 10771 C C . GLY B 2 465 ? -43.581 21.008 -11.085 1.00 216.09 ? 465 GLY B C 1 ATOM 10772 O O . GLY B 2 465 ? -44.514 21.094 -11.879 1.00 215.49 ? 465 GLY B O 1 ATOM 10773 N N . TRP B 2 466 ? -43.098 19.842 -10.672 1.00 221.57 ? 466 TRP B N 1 ATOM 10774 C CA . TRP B 2 466 ? -43.836 18.605 -10.920 1.00 224.78 ? 466 TRP B CA 1 ATOM 10775 C C . TRP B 2 466 ? -44.262 17.939 -9.604 1.00 218.10 ? 466 TRP B C 1 ATOM 10776 O O . TRP B 2 466 ? -45.454 17.831 -9.326 1.00 218.23 ? 466 TRP B O 1 ATOM 10777 C CB . TRP B 2 466 ? -43.013 17.649 -11.781 1.00 227.10 ? 466 TRP B CB 1 ATOM 10778 C CG . TRP B 2 466 ? -43.657 17.387 -13.111 1.00 230.60 ? 466 TRP B CG 1 ATOM 10779 C CD1 . TRP B 2 466 ? -44.995 17.371 -13.379 1.00 227.89 ? 466 TRP B CD1 1 ATOM 10780 C CD2 . TRP B 2 466 ? -42.997 17.131 -14.357 1.00 231.30 ? 466 TRP B CD2 1 ATOM 10781 N NE1 . TRP B 2 466 ? -45.210 17.107 -14.709 1.00 226.20 ? 466 TRP B NE1 1 ATOM 10782 C CE2 . TRP B 2 466 ? -43.999 16.955 -15.333 1.00 229.40 ? 466 TRP B CE2 1 ATOM 10783 C CE3 . TRP B 2 466 ? -41.656 17.023 -14.742 1.00 230.05 ? 466 TRP B CE3 1 ATOM 10784 C CZ2 . TRP B 2 466 ? -43.706 16.680 -16.666 1.00 231.30 ? 466 TRP B CZ2 1 ATOM 10785 C CZ3 . TRP B 2 466 ? -41.367 16.751 -16.068 1.00 231.54 ? 466 TRP B CZ3 1 ATOM 10786 C CH2 . TRP B 2 466 ? -42.387 16.583 -17.014 1.00 232.69 ? 466 TRP B CH2 1 ATOM 10787 N N . LEU B 2 467 ? -43.288 17.485 -8.816 1.00 212.58 ? 467 LEU B N 1 ATOM 10788 C CA . LEU B 2 467 ? -43.488 17.034 -7.427 1.00 209.84 ? 467 LEU B CA 1 ATOM 10789 C C . LEU B 2 467 ? -44.748 16.192 -7.168 1.00 208.98 ? 467 LEU B C 1 ATOM 10790 O O . LEU B 2 467 ? -45.701 16.665 -6.550 1.00 216.23 ? 467 LEU B O 1 ATOM 10791 C CB . LEU B 2 467 ? -43.471 18.238 -6.470 1.00 210.46 ? 467 LEU B CB 1 ATOM 10792 C CG . LEU B 2 467 ? -44.301 19.504 -6.707 1.00 214.18 ? 467 LEU B CG 1 ATOM 10793 C CD1 . LEU B 2 467 ? -45.286 19.726 -5.571 1.00 214.55 ? 467 LEU B CD1 1 ATOM 10794 C CD2 . LEU B 2 467 ? -43.387 20.708 -6.869 1.00 215.86 ? 467 LEU B CD2 1 ATOM 10795 N N . GLY B 2 468 ? -44.748 14.947 -7.634 1.00 196.56 ? 468 GLY B N 1 ATOM 10796 C CA . GLY B 2 468 ? -45.895 14.072 -7.456 1.00 191.87 ? 468 GLY B CA 1 ATOM 10797 C C . GLY B 2 468 ? -45.504 12.610 -7.343 1.00 189.90 ? 468 GLY B C 1 ATOM 10798 O O . GLY B 2 468 ? -44.316 12.285 -7.396 1.00 191.15 ? 468 GLY B O 1 ATOM 10799 N N . SER B 2 469 ? -46.497 11.740 -7.148 1.00 188.08 ? 469 SER B N 1 ATOM 10800 C CA . SER B 2 469 ? -46.283 10.291 -7.128 1.00 182.58 ? 469 SER B CA 1 ATOM 10801 C C . SER B 2 469 ? -45.436 9.903 -8.330 1.00 181.06 ? 469 SER B C 1 ATOM 10802 O O . SER B 2 469 ? -44.280 9.502 -8.192 1.00 171.58 ? 469 SER B O 1 ATOM 10803 C CB . SER B 2 469 ? -47.618 9.543 -7.144 1.00 176.06 ? 469 SER B CB 1 ATOM 10804 O OG . SER B 2 469 ? -48.484 10.019 -6.129 1.00 172.38 ? 469 SER B OG 1 ATOM 10805 N N . GLN B 2 470 ? -46.028 10.024 -9.511 1.00 193.07 ? 470 GLN B N 1 ATOM 10806 C CA . GLN B 2 470 ? -45.255 10.246 -10.719 1.00 200.54 ? 470 GLN B CA 1 ATOM 10807 C C . GLN B 2 470 ? -45.448 11.723 -11.038 1.00 207.51 ? 470 GLN B C 1 ATOM 10808 O O . GLN B 2 470 ? -46.177 12.415 -10.327 1.00 211.95 ? 470 GLN B O 1 ATOM 10809 C CB . GLN B 2 470 ? -45.709 9.344 -11.870 1.00 203.67 ? 470 GLN B CB 1 ATOM 10810 C CG . GLN B 2 470 ? -44.728 8.222 -12.196 1.00 199.46 ? 470 GLN B CG 1 ATOM 10811 C CD . GLN B 2 470 ? -45.255 6.848 -11.824 1.00 193.30 ? 470 GLN B CD 1 ATOM 10812 O OE1 . GLN B 2 470 ? -46.462 6.606 -11.842 1.00 193.67 ? 470 GLN B OE1 1 ATOM 10813 N NE2 . GLN B 2 470 ? -44.346 5.939 -11.484 1.00 182.46 ? 470 GLN B NE2 1 ATOM 10814 N N . CYS B 2 471 ? -44.806 12.215 -12.090 1.00 210.74 ? 471 CYS B N 1 ATOM 10815 C CA . CYS B 2 471 ? -44.883 13.637 -12.411 1.00 216.68 ? 471 CYS B CA 1 ATOM 10816 C C . CYS B 2 471 ? -46.302 14.049 -12.804 1.00 212.63 ? 471 CYS B C 1 ATOM 10817 O O . CYS B 2 471 ? -46.900 13.448 -13.697 1.00 210.20 ? 471 CYS B O 1 ATOM 10818 C CB . CYS B 2 471 ? -43.897 13.975 -13.528 1.00 223.07 ? 471 CYS B CB 1 ATOM 10819 S SG . CYS B 2 471 ? -42.161 13.778 -13.055 1.00 274.11 ? 471 CYS B SG 1 ATOM 10820 N N . GLU B 2 472 ? -46.822 15.089 -12.150 1.00 215.46 ? 472 GLU B N 1 ATOM 10821 C CA . GLU B 2 472 ? -48.220 15.498 -12.316 1.00 220.30 ? 472 GLU B CA 1 ATOM 10822 C C . GLU B 2 472 ? -48.561 16.779 -11.543 1.00 227.76 ? 472 GLU B C 1 ATOM 10823 O O . GLU B 2 472 ? -47.820 17.189 -10.649 1.00 228.02 ? 472 GLU B O 1 ATOM 10824 C CB . GLU B 2 472 ? -49.156 14.373 -11.859 1.00 215.09 ? 472 GLU B CB 1 ATOM 10825 C CG . GLU B 2 472 ? -50.415 14.211 -12.696 1.00 219.19 ? 472 GLU B CG 1 ATOM 10826 C CD . GLU B 2 472 ? -50.167 13.454 -13.988 1.00 224.73 ? 472 GLU B CD 1 ATOM 10827 O OE1 . GLU B 2 472 ? -50.668 12.316 -14.113 1.00 224.00 ? 472 GLU B OE1 1 ATOM 10828 O OE2 . GLU B 2 472 ? -49.476 13.993 -14.877 1.00 230.24 ? 472 GLU B OE2 1 ATOM 10829 N N . CYS B 2 473 ? -49.690 17.392 -11.901 1.00 233.26 ? 473 CYS B N 1 ATOM 10830 C CA . CYS B 2 473 ? -50.203 18.614 -11.266 1.00 236.17 ? 473 CYS B CA 1 ATOM 10831 C C . CYS B 2 473 ? -49.171 19.741 -11.251 1.00 237.96 ? 473 CYS B C 1 ATOM 10832 O O . CYS B 2 473 ? -48.441 19.922 -12.227 1.00 237.40 ? 473 CYS B O 1 ATOM 10833 C CB . CYS B 2 473 ? -50.666 18.314 -9.837 1.00 232.48 ? 473 CYS B CB 1 ATOM 10834 S SG . CYS B 2 473 ? -51.436 19.713 -8.991 1.00 244.72 ? 473 CYS B SG 1 ATOM 10835 N N . SER B 2 474 ? -49.113 20.489 -10.146 1.00 239.97 ? 474 SER B N 1 ATOM 10836 C CA . SER B 2 474 ? -47.992 21.397 -9.892 1.00 236.70 ? 474 SER B CA 1 ATOM 10837 C C . SER B 2 474 ? -47.773 22.459 -10.974 1.00 233.55 ? 474 SER B C 1 ATOM 10838 O O . SER B 2 474 ? -46.973 22.231 -11.881 1.00 234.62 ? 474 SER B O 1 ATOM 10839 C CB . SER B 2 474 ? -46.708 20.600 -9.688 1.00 231.73 ? 474 SER B CB 1 ATOM 10840 O OG . SER B 2 474 ? -45.718 21.395 -9.061 1.00 226.65 ? 474 SER B OG 1 ATOM 10841 N N . GLU B 2 475 ? -48.520 23.568 -10.881 1.00 229.07 ? 475 GLU B N 1 ATOM 10842 C CA . GLU B 2 475 ? -48.583 24.677 -11.860 1.00 227.00 ? 475 GLU B CA 1 ATOM 10843 C C . GLU B 2 475 ? -49.707 24.459 -12.874 1.00 229.28 ? 475 GLU B C 1 ATOM 10844 O O . GLU B 2 475 ? -49.979 25.319 -13.713 1.00 229.95 ? 475 GLU B O 1 ATOM 10845 C CB . GLU B 2 475 ? -47.237 24.885 -12.584 1.00 223.64 ? 475 GLU B CB 1 ATOM 10846 C CG . GLU B 2 475 ? -47.129 26.115 -13.475 1.00 231.33 ? 475 GLU B CG 1 ATOM 10847 C CD . GLU B 2 475 ? -46.174 25.901 -14.635 1.00 232.05 ? 475 GLU B CD 1 ATOM 10848 O OE1 . GLU B 2 475 ? -45.532 24.829 -14.689 1.00 226.52 ? 475 GLU B OE1 1 ATOM 10849 O OE2 . GLU B 2 475 ? -46.067 26.799 -15.497 1.00 232.79 ? 475 GLU B OE2 1 ATOM 10850 N N . GLU B 2 476 ? -50.391 23.325 -12.779 1.00 230.57 ? 476 GLU B N 1 ATOM 10851 C CA . GLU B 2 476 ? -51.661 23.185 -13.479 1.00 234.09 ? 476 GLU B CA 1 ATOM 10852 C C . GLU B 2 476 ? -52.704 24.053 -12.781 1.00 229.49 ? 476 GLU B C 1 ATOM 10853 O O . GLU B 2 476 ? -52.418 24.682 -11.762 1.00 223.90 ? 476 GLU B O 1 ATOM 10854 C CB . GLU B 2 476 ? -52.129 21.729 -13.502 1.00 232.25 ? 476 GLU B CB 1 ATOM 10855 C CG . GLU B 2 476 ? -51.302 20.797 -14.363 1.00 234.57 ? 476 GLU B CG 1 ATOM 10856 C CD . GLU B 2 476 ? -51.882 19.396 -14.403 1.00 239.98 ? 476 GLU B CD 1 ATOM 10857 O OE1 . GLU B 2 476 ? -52.791 19.106 -13.595 1.00 240.45 ? 476 GLU B OE1 1 ATOM 10858 O OE2 . GLU B 2 476 ? -51.437 18.586 -15.243 1.00 244.95 ? 476 GLU B OE2 1 ATOM 10859 N N . ASP B 2 477 ? -53.918 24.082 -13.320 1.00 230.08 ? 477 ASP B N 1 ATOM 10860 C CA . ASP B 2 477 ? -55.026 24.694 -12.602 1.00 228.02 ? 477 ASP B CA 1 ATOM 10861 C C . ASP B 2 477 ? -55.735 23.595 -11.832 1.00 228.43 ? 477 ASP B C 1 ATOM 10862 O O . ASP B 2 477 ? -56.382 22.729 -12.422 1.00 227.79 ? 477 ASP B O 1 ATOM 10863 C CB . ASP B 2 477 ? -55.987 25.408 -13.554 1.00 228.08 ? 477 ASP B CB 1 ATOM 10864 C CG . ASP B 2 477 ? -55.505 26.792 -13.939 1.00 230.32 ? 477 ASP B CG 1 ATOM 10865 O OD1 . ASP B 2 477 ? -54.746 27.398 -13.153 1.00 234.27 ? 477 ASP B OD1 1 ATOM 10866 O OD2 . ASP B 2 477 ? -55.889 27.278 -15.024 1.00 228.62 ? 477 ASP B OD2 1 ATOM 10867 N N . TYR B 2 478 ? -55.614 23.631 -10.511 1.00 225.07 ? 478 TYR B N 1 ATOM 10868 C CA . TYR B 2 478 ? -56.078 22.520 -9.697 1.00 220.29 ? 478 TYR B CA 1 ATOM 10869 C C . TYR B 2 478 ? -57.527 22.688 -9.260 1.00 223.81 ? 478 TYR B C 1 ATOM 10870 O O . TYR B 2 478 ? -57.882 23.636 -8.559 1.00 224.80 ? 478 TYR B O 1 ATOM 10871 C CB . TYR B 2 478 ? -55.165 22.326 -8.477 1.00 215.83 ? 478 TYR B CB 1 ATOM 10872 C CG . TYR B 2 478 ? -55.103 23.496 -7.516 1.00 224.67 ? 478 TYR B CG 1 ATOM 10873 C CD1 . TYR B 2 478 ? -55.803 23.471 -6.316 1.00 226.05 ? 478 TYR B CD1 1 ATOM 10874 C CD2 . TYR B 2 478 ? -54.332 24.616 -7.800 1.00 228.27 ? 478 TYR B CD2 1 ATOM 10875 C CE1 . TYR B 2 478 ? -55.746 24.532 -5.432 1.00 226.33 ? 478 TYR B CE1 1 ATOM 10876 C CE2 . TYR B 2 478 ? -54.268 25.683 -6.921 1.00 227.12 ? 478 TYR B CE2 1 ATOM 10877 C CZ . TYR B 2 478 ? -54.977 25.635 -5.740 1.00 224.29 ? 478 TYR B CZ 1 ATOM 10878 O OH . TYR B 2 478 ? -54.918 26.694 -4.862 1.00 219.17 ? 478 TYR B OH 1 ATOM 10879 N N . ARG B 2 479 ? -58.362 21.758 -9.708 1.00 223.46 ? 479 ARG B N 1 ATOM 10880 C CA . ARG B 2 479 ? -59.717 21.622 -9.202 1.00 224.06 ? 479 ARG B CA 1 ATOM 10881 C C . ARG B 2 479 ? -59.630 21.128 -7.764 1.00 223.18 ? 479 ARG B C 1 ATOM 10882 O O . ARG B 2 479 ? -58.561 20.703 -7.325 1.00 212.85 ? 479 ARG B O 1 ATOM 10883 C CB . ARG B 2 479 ? -60.525 20.647 -10.063 1.00 219.41 ? 479 ARG B CB 1 ATOM 10884 C CG . ARG B 2 479 ? -60.636 21.032 -11.528 1.00 217.74 ? 479 ARG B CG 1 ATOM 10885 C CD . ARG B 2 479 ? -61.434 19.989 -12.295 1.00 217.33 ? 479 ARG B CD 1 ATOM 10886 N NE . ARG B 2 479 ? -61.591 20.335 -13.703 1.00 218.65 ? 479 ARG B NE 1 ATOM 10887 C CZ . ARG B 2 479 ? -62.253 19.592 -14.584 1.00 218.93 ? 479 ARG B CZ 1 ATOM 10888 N NH1 . ARG B 2 479 ? -62.822 18.457 -14.201 1.00 216.23 ? 479 ARG B NH1 1 ATOM 10889 N NH2 . ARG B 2 479 ? -62.348 19.984 -15.848 1.00 222.18 ? 479 ARG B NH2 1 ATOM 10890 N N . PRO B 2 480 ? -60.743 21.178 -7.016 1.00 227.79 ? 480 PRO B N 1 ATOM 10891 C CA . PRO B 2 480 ? -60.660 20.554 -5.692 1.00 224.13 ? 480 PRO B CA 1 ATOM 10892 C C . PRO B 2 480 ? -60.473 19.043 -5.813 1.00 231.38 ? 480 PRO B C 1 ATOM 10893 O O . PRO B 2 480 ? -61.408 18.277 -5.575 1.00 234.63 ? 480 PRO B O 1 ATOM 10894 C CB . PRO B 2 480 ? -62.009 20.897 -5.050 1.00 221.04 ? 480 PRO B CB 1 ATOM 10895 C CG . PRO B 2 480 ? -62.912 21.231 -6.196 1.00 223.43 ? 480 PRO B CG 1 ATOM 10896 C CD . PRO B 2 480 ? -62.028 21.867 -7.223 1.00 226.66 ? 480 PRO B CD 1 ATOM 10897 N N . SER B 2 481 ? -59.264 18.638 -6.199 1.00 231.06 ? 481 SER B N 1 ATOM 10898 C CA . SER B 2 481 ? -58.920 17.235 -6.397 1.00 227.38 ? 481 SER B CA 1 ATOM 10899 C C . SER B 2 481 ? -59.187 16.442 -5.132 1.00 220.29 ? 481 SER B C 1 ATOM 10900 O O . SER B 2 481 ? -59.779 15.363 -5.180 1.00 215.52 ? 481 SER B O 1 ATOM 10901 C CB . SER B 2 481 ? -57.454 17.095 -6.812 1.00 216.62 ? 481 SER B CB 1 ATOM 10902 O OG . SER B 2 481 ? -57.077 15.732 -6.914 1.00 213.44 ? 481 SER B OG 1 ATOM 10903 N N . GLN B 2 482 ? -58.768 17.008 -4.003 1.00 211.50 ? 482 GLN B N 1 ATOM 10904 C CA . GLN B 2 482 ? -59.003 16.423 -2.690 1.00 208.13 ? 482 GLN B CA 1 ATOM 10905 C C . GLN B 2 482 ? -58.494 17.332 -1.581 1.00 202.35 ? 482 GLN B C 1 ATOM 10906 O O . GLN B 2 482 ? -57.709 18.251 -1.813 1.00 192.66 ? 482 GLN B O 1 ATOM 10907 C CB . GLN B 2 482 ? -58.337 15.049 -2.569 1.00 207.50 ? 482 GLN B CB 1 ATOM 10908 C CG . GLN B 2 482 ? -59.324 13.905 -2.398 1.00 212.34 ? 482 GLN B CG 1 ATOM 10909 C CD . GLN B 2 482 ? -58.645 12.553 -2.311 1.00 210.91 ? 482 GLN B CD 1 ATOM 10910 O OE1 . GLN B 2 482 ? -57.458 12.461 -2.001 1.00 209.83 ? 482 GLN B OE1 1 ATOM 10911 N NE2 . GLN B 2 482 ? -59.397 11.495 -2.590 1.00 202.44 ? 482 GLN B NE2 1 ATOM 10912 N N . GLN B 2 483 ? -58.958 17.054 -0.371 1.00 205.70 ? 483 GLN B N 1 ATOM 10913 C CA . GLN B 2 483 ? -58.550 17.773 0.825 1.00 192.10 ? 483 GLN B CA 1 ATOM 10914 C C . GLN B 2 483 ? -57.353 17.082 1.455 1.00 185.06 ? 483 GLN B C 1 ATOM 10915 O O . GLN B 2 483 ? -56.926 17.446 2.552 1.00 182.02 ? 483 GLN B O 1 ATOM 10916 C CB . GLN B 2 483 ? -59.699 17.836 1.827 1.00 195.71 ? 483 GLN B CB 1 ATOM 10917 C CG . GLN B 2 483 ? -60.068 16.467 2.373 1.00 202.31 ? 483 GLN B CG 1 ATOM 10918 C CD . GLN B 2 483 ? -61.359 16.474 3.158 1.00 202.02 ? 483 GLN B CD 1 ATOM 10919 O OE1 . GLN B 2 483 ? -61.937 17.529 3.417 1.00 203.68 ? 483 GLN B OE1 1 ATOM 10920 N NE2 . GLN B 2 483 ? -61.823 15.290 3.539 1.00 201.34 ? 483 GLN B NE2 1 ATOM 10921 N N . ASP B 2 484 ? -56.823 16.083 0.751 1.00 192.40 ? 484 ASP B N 1 ATOM 10922 C CA . ASP B 2 484 ? -55.996 15.047 1.358 1.00 194.59 ? 484 ASP B CA 1 ATOM 10923 C C . ASP B 2 484 ? -54.821 15.607 2.148 1.00 178.70 ? 484 ASP B C 1 ATOM 10924 O O . ASP B 2 484 ? -53.948 16.283 1.603 1.00 178.90 ? 484 ASP B O 1 ATOM 10925 C CB . ASP B 2 484 ? -55.479 14.109 0.259 1.00 203.76 ? 484 ASP B CB 1 ATOM 10926 C CG . ASP B 2 484 ? -54.939 12.799 0.801 1.00 200.26 ? 484 ASP B CG 1 ATOM 10927 O OD1 . ASP B 2 484 ? -54.914 11.812 0.036 1.00 198.28 ? 484 ASP B OD1 1 ATOM 10928 O OD2 . ASP B 2 484 ? -54.542 12.745 1.982 1.00 196.88 ? 484 ASP B OD2 1 ATOM 10929 N N . GLU B 2 485 ? -54.822 15.284 3.441 1.00 174.95 ? 485 GLU B N 1 ATOM 10930 C CA . GLU B 2 485 ? -53.755 15.609 4.385 1.00 185.82 ? 485 GLU B CA 1 ATOM 10931 C C . GLU B 2 485 ? -53.195 17.024 4.229 1.00 189.92 ? 485 GLU B C 1 ATOM 10932 O O . GLU B 2 485 ? -51.995 17.240 4.396 1.00 187.44 ? 485 GLU B O 1 ATOM 10933 C CB . GLU B 2 485 ? -52.622 14.588 4.272 1.00 186.69 ? 485 GLU B CB 1 ATOM 10934 C CG . GLU B 2 485 ? -52.539 13.618 5.448 1.00 182.53 ? 485 GLU B CG 1 ATOM 10935 C CD . GLU B 2 485 ? -53.535 12.476 5.349 1.00 179.70 ? 485 GLU B CD 1 ATOM 10936 O OE1 . GLU B 2 485 ? -54.320 12.280 6.301 1.00 182.55 ? 485 GLU B OE1 1 ATOM 10937 O OE2 . GLU B 2 485 ? -53.520 11.765 4.323 1.00 170.04 ? 485 GLU B OE2 1 ATOM 10938 N N . CYS B 2 486 ? -54.060 17.981 3.906 1.00 184.02 ? 486 CYS B N 1 ATOM 10939 C CA . CYS B 2 486 ? -53.652 19.380 3.877 1.00 176.29 ? 486 CYS B CA 1 ATOM 10940 C C . CYS B 2 486 ? -53.953 20.019 5.227 1.00 175.90 ? 486 CYS B C 1 ATOM 10941 O O . CYS B 2 486 ? -53.525 21.135 5.517 1.00 194.00 ? 486 CYS B O 1 ATOM 10942 C CB . CYS B 2 486 ? -54.351 20.139 2.745 1.00 181.50 ? 486 CYS B CB 1 ATOM 10943 S SG . CYS B 2 486 ? -53.409 20.226 1.190 1.00 181.68 ? 486 CYS B SG 1 ATOM 10944 N N . SER B 2 487 ? -54.708 19.293 6.042 1.00 170.91 ? 487 SER B N 1 ATOM 10945 C CA . SER B 2 487 ? -54.955 19.667 7.426 1.00 167.01 ? 487 SER B CA 1 ATOM 10946 C C . SER B 2 487 ? -55.118 18.396 8.244 1.00 172.04 ? 487 SER B C 1 ATOM 10947 O O . SER B 2 487 ? -55.606 17.390 7.727 1.00 175.43 ? 487 SER B O 1 ATOM 10948 C CB . SER B 2 487 ? -56.197 20.547 7.543 1.00 170.47 ? 487 SER B CB 1 ATOM 10949 O OG . SER B 2 487 ? -57.362 19.841 7.156 1.00 174.02 ? 487 SER B OG 1 ATOM 10950 N N . PRO B 2 488 ? -54.716 18.422 9.522 1.00 176.87 ? 488 PRO B N 1 ATOM 10951 C CA . PRO B 2 488 ? -54.944 17.205 10.305 1.00 177.17 ? 488 PRO B CA 1 ATOM 10952 C C . PRO B 2 488 ? -56.362 17.143 10.869 1.00 181.18 ? 488 PRO B C 1 ATOM 10953 O O . PRO B 2 488 ? -56.536 16.825 12.046 1.00 177.69 ? 488 PRO B O 1 ATOM 10954 C CB . PRO B 2 488 ? -53.914 17.323 11.429 1.00 165.94 ? 488 PRO B CB 1 ATOM 10955 C CG . PRO B 2 488 ? -53.774 18.800 11.630 1.00 161.62 ? 488 PRO B CG 1 ATOM 10956 C CD . PRO B 2 488 ? -53.937 19.428 10.265 1.00 168.98 ? 488 PRO B CD 1 ATOM 10957 N N . ARG B 2 489 ? -57.344 17.414 10.008 1.00 182.50 ? 489 ARG B N 1 ATOM 10958 C CA . ARG B 2 489 ? -58.774 17.336 10.312 1.00 187.39 ? 489 ARG B CA 1 ATOM 10959 C C . ARG B 2 489 ? -59.572 17.840 9.113 1.00 193.88 ? 489 ARG B C 1 ATOM 10960 O O . ARG B 2 489 ? -58.999 18.299 8.126 1.00 196.76 ? 489 ARG B O 1 ATOM 10961 C CB . ARG B 2 489 ? -59.148 18.137 11.564 1.00 183.08 ? 489 ARG B CB 1 ATOM 10962 C CG . ARG B 2 489 ? -59.612 17.253 12.715 1.00 176.82 ? 489 ARG B CG 1 ATOM 10963 C CD . ARG B 2 489 ? -60.440 18.014 13.736 1.00 176.94 ? 489 ARG B CD 1 ATOM 10964 N NE . ARG B 2 489 ? -59.650 18.970 14.502 1.00 176.96 ? 489 ARG B NE 1 ATOM 10965 C CZ . ARG B 2 489 ? -60.079 19.569 15.608 1.00 172.37 ? 489 ARG B CZ 1 ATOM 10966 N NH1 . ARG B 2 489 ? -61.290 19.304 16.078 1.00 179.27 ? 489 ARG B NH1 1 ATOM 10967 N NH2 . ARG B 2 489 ? -59.296 20.428 16.247 1.00 157.43 ? 489 ARG B NH2 1 ATOM 10968 N N . GLU B 2 490 ? -60.895 17.752 9.204 1.00 193.77 ? 490 GLU B N 1 ATOM 10969 C CA . GLU B 2 490 ? -61.771 18.199 8.124 1.00 192.14 ? 490 GLU B CA 1 ATOM 10970 C C . GLU B 2 490 ? -61.922 19.718 8.080 1.00 187.27 ? 490 GLU B C 1 ATOM 10971 O O . GLU B 2 490 ? -61.478 20.367 7.133 1.00 185.17 ? 490 GLU B O 1 ATOM 10972 C CB . GLU B 2 490 ? -63.148 17.549 8.255 1.00 195.52 ? 490 GLU B CB 1 ATOM 10973 C CG . GLU B 2 490 ? -63.176 16.088 7.852 1.00 200.75 ? 490 GLU B CG 1 ATOM 10974 C CD . GLU B 2 490 ? -62.772 15.885 6.407 1.00 203.53 ? 490 GLU B CD 1 ATOM 10975 O OE1 . GLU B 2 490 ? -63.584 16.198 5.510 1.00 206.04 ? 490 GLU B OE1 1 ATOM 10976 O OE2 . GLU B 2 490 ? -61.638 15.421 6.164 1.00 202.51 ? 490 GLU B OE2 1 ATOM 10977 N N . GLY B 2 491 ? -62.552 20.278 9.109 1.00 189.78 ? 491 GLY B N 1 ATOM 10978 C CA . GLY B 2 491 ? -62.845 21.701 9.149 1.00 192.42 ? 491 GLY B CA 1 ATOM 10979 C C . GLY B 2 491 ? -61.623 22.586 9.303 1.00 197.84 ? 491 GLY B C 1 ATOM 10980 O O . GLY B 2 491 ? -61.704 23.802 9.126 1.00 194.42 ? 491 GLY B O 1 ATOM 10981 N N . GLN B 2 492 ? -60.492 21.976 9.640 1.00 204.07 ? 492 GLN B N 1 ATOM 10982 C CA . GLN B 2 492 ? -59.236 22.701 9.786 1.00 194.33 ? 492 GLN B CA 1 ATOM 10983 C C . GLN B 2 492 ? -58.849 23.356 8.459 1.00 193.79 ? 492 GLN B C 1 ATOM 10984 O O . GLN B 2 492 ? -59.033 22.763 7.395 1.00 199.80 ? 492 GLN B O 1 ATOM 10985 C CB . GLN B 2 492 ? -58.128 21.757 10.263 1.00 183.03 ? 492 GLN B CB 1 ATOM 10986 C CG . GLN B 2 492 ? -57.125 22.376 11.228 1.00 184.49 ? 492 GLN B CG 1 ATOM 10987 C CD . GLN B 2 492 ? -57.688 22.548 12.627 1.00 188.54 ? 492 GLN B CD 1 ATOM 10988 O OE1 . GLN B 2 492 ? -58.779 22.068 12.935 1.00 193.77 ? 492 GLN B OE1 1 ATOM 10989 N NE2 . GLN B 2 492 ? -56.940 23.233 13.485 1.00 180.60 ? 492 GLN B NE2 1 ATOM 10990 N N . PRO B 2 493 ? -58.317 24.587 8.520 1.00 187.40 ? 493 PRO B N 1 ATOM 10991 C CA . PRO B 2 493 ? -57.922 25.364 7.338 1.00 179.74 ? 493 PRO B CA 1 ATOM 10992 C C . PRO B 2 493 ? -56.818 24.706 6.511 1.00 179.02 ? 493 PRO B C 1 ATOM 10993 O O . PRO B 2 493 ? -56.409 23.580 6.786 1.00 188.62 ? 493 PRO B O 1 ATOM 10994 C CB . PRO B 2 493 ? -57.427 26.684 7.937 1.00 171.99 ? 493 PRO B CB 1 ATOM 10995 C CG . PRO B 2 493 ? -58.127 26.791 9.241 1.00 172.07 ? 493 PRO B CG 1 ATOM 10996 C CD . PRO B 2 493 ? -58.218 25.386 9.754 1.00 178.61 ? 493 PRO B CD 1 ATOM 10997 N N . VAL B 2 494 ? -56.334 25.429 5.507 1.00 174.51 ? 494 VAL B N 1 ATOM 10998 C CA . VAL B 2 494 ? -55.335 24.921 4.573 1.00 175.85 ? 494 VAL B CA 1 ATOM 10999 C C . VAL B 2 494 ? -53.999 24.746 5.313 1.00 176.89 ? 494 VAL B C 1 ATOM 11000 O O . VAL B 2 494 ? -53.937 25.015 6.514 1.00 184.26 ? 494 VAL B O 1 ATOM 11001 C CB . VAL B 2 494 ? -55.199 25.883 3.374 1.00 188.84 ? 494 VAL B CB 1 ATOM 11002 C CG1 . VAL B 2 494 ? -54.400 27.121 3.771 1.00 190.68 ? 494 VAL B CG1 1 ATOM 11003 C CG2 . VAL B 2 494 ? -54.611 25.181 2.160 1.00 190.33 ? 494 VAL B CG2 1 ATOM 11004 N N . CYS B 2 495 ? -52.934 24.307 4.638 1.00 171.83 ? 495 CYS B N 1 ATOM 11005 C CA . CYS B 2 495 ? -51.749 23.885 5.386 1.00 173.99 ? 495 CYS B CA 1 ATOM 11006 C C . CYS B 2 495 ? -51.096 25.070 6.079 1.00 157.86 ? 495 CYS B C 1 ATOM 11007 O O . CYS B 2 495 ? -50.507 25.925 5.426 1.00 155.69 ? 495 CYS B O 1 ATOM 11008 C CB . CYS B 2 495 ? -50.709 23.238 4.458 1.00 182.04 ? 495 CYS B CB 1 ATOM 11009 S SG . CYS B 2 495 ? -51.174 21.740 3.568 1.00 240.25 ? 495 CYS B SG 1 ATOM 11010 N N . SER B 2 496 ? -51.156 25.063 7.410 1.00 150.76 ? 496 SER B N 1 ATOM 11011 C CA . SER B 2 496 ? -50.508 26.056 8.266 1.00 145.54 ? 496 SER B CA 1 ATOM 11012 C C . SER B 2 496 ? -50.623 27.489 7.744 1.00 148.43 ? 496 SER B C 1 ATOM 11013 O O . SER B 2 496 ? -49.695 28.278 7.913 1.00 161.30 ? 496 SER B O 1 ATOM 11014 C CB . SER B 2 496 ? -49.035 25.696 8.452 1.00 158.25 ? 496 SER B CB 1 ATOM 11015 O OG . SER B 2 496 ? -48.891 24.308 8.698 1.00 138.03 ? 496 SER B OG 1 ATOM 11016 N N . GLN B 2 497 ? -51.762 27.827 7.140 1.00 147.65 ? 497 GLN B N 1 ATOM 11017 C CA . GLN B 2 497 ? -51.893 29.066 6.368 1.00 152.49 ? 497 GLN B CA 1 ATOM 11018 C C . GLN B 2 497 ? -50.755 29.165 5.347 1.00 158.54 ? 497 GLN B C 1 ATOM 11019 O O . GLN B 2 497 ? -50.678 28.348 4.432 1.00 156.27 ? 497 GLN B O 1 ATOM 11020 C CB . GLN B 2 497 ? -51.918 30.290 7.286 1.00 151.39 ? 497 GLN B CB 1 ATOM 11021 C CG . GLN B 2 497 ? -53.282 30.958 7.386 1.00 154.15 ? 497 GLN B CG 1 ATOM 11022 C CD . GLN B 2 497 ? -54.370 30.013 7.865 1.00 146.41 ? 497 GLN B CD 1 ATOM 11023 O OE1 . GLN B 2 497 ? -54.117 29.104 8.657 1.00 144.62 ? 497 GLN B OE1 1 ATOM 11024 N NE2 . GLN B 2 497 ? -55.589 30.224 7.384 1.00 149.94 ? 497 GLN B NE2 1 ATOM 11025 N N . ARG B 2 498 ? -49.916 30.190 5.486 1.00 171.23 ? 498 ARG B N 1 ATOM 11026 C CA . ARG B 2 498 ? -48.618 30.273 4.799 1.00 175.89 ? 498 ARG B CA 1 ATOM 11027 C C . ARG B 2 498 ? -48.610 29.818 3.337 1.00 190.79 ? 498 ARG B C 1 ATOM 11028 O O . ARG B 2 498 ? -48.039 28.776 3.022 1.00 180.89 ? 498 ARG B O 1 ATOM 11029 C CB . ARG B 2 498 ? -47.569 29.456 5.564 1.00 153.58 ? 498 ARG B CB 1 ATOM 11030 C CG . ARG B 2 498 ? -47.271 29.946 6.975 1.00 151.93 ? 498 ARG B CG 1 ATOM 11031 C CD . ARG B 2 498 ? -46.300 29.004 7.680 1.00 151.53 ? 498 ARG B CD 1 ATOM 11032 N NE . ARG B 2 498 ? -46.300 29.181 9.130 1.00 153.77 ? 498 ARG B NE 1 ATOM 11033 C CZ . ARG B 2 498 ? -45.487 28.537 9.961 1.00 147.94 ? 498 ARG B CZ 1 ATOM 11034 N NH1 . ARG B 2 498 ? -44.597 27.675 9.488 1.00 151.71 ? 498 ARG B NH1 1 ATOM 11035 N NH2 . ARG B 2 498 ? -45.559 28.757 11.268 1.00 142.32 ? 498 ARG B NH2 1 ATOM 11036 N N . GLY B 2 499 ? -49.249 30.577 2.452 1.00 200.33 ? 499 GLY B N 1 ATOM 11037 C CA . GLY B 2 499 ? -49.227 30.259 1.032 1.00 208.70 ? 499 GLY B CA 1 ATOM 11038 C C . GLY B 2 499 ? -50.003 29.008 0.658 1.00 215.42 ? 499 GLY B C 1 ATOM 11039 O O . GLY B 2 499 ? -49.748 28.395 -0.379 1.00 214.44 ? 499 GLY B O 1 ATOM 11040 N N . GLU B 2 500 ? -50.933 28.629 1.531 1.00 208.11 ? 500 GLU B N 1 ATOM 11041 C CA . GLU B 2 500 ? -51.907 27.540 1.344 1.00 192.61 ? 500 GLU B CA 1 ATOM 11042 C C . GLU B 2 500 ? -51.337 26.206 0.835 1.00 195.52 ? 500 GLU B C 1 ATOM 11043 O O . GLU B 2 500 ? -50.250 25.791 1.236 1.00 192.12 ? 500 GLU B O 1 ATOM 11044 C CB . GLU B 2 500 ? -53.067 27.991 0.426 1.00 194.05 ? 500 GLU B CB 1 ATOM 11045 C CG . GLU B 2 500 ? -52.726 28.479 -0.984 1.00 195.85 ? 500 GLU B CG 1 ATOM 11046 C CD . GLU B 2 500 ? -52.477 29.974 -1.041 1.00 195.56 ? 500 GLU B CD 1 ATOM 11047 O OE1 . GLU B 2 500 ? -52.904 30.684 -0.107 1.00 192.70 ? 500 GLU B OE1 1 ATOM 11048 O OE2 . GLU B 2 500 ? -51.847 30.437 -2.014 1.00 197.73 ? 500 GLU B OE2 1 ATOM 11049 N N . CYS B 2 501 ? -52.090 25.542 -0.040 1.00 209.20 ? 501 CYS B N 1 ATOM 11050 C CA . CYS B 2 501 ? -51.752 24.199 -0.512 1.00 210.36 ? 501 CYS B CA 1 ATOM 11051 C C . CYS B 2 501 ? -52.391 23.888 -1.863 1.00 210.69 ? 501 CYS B C 1 ATOM 11052 O O . CYS B 2 501 ? -53.429 24.453 -2.210 1.00 213.97 ? 501 CYS B O 1 ATOM 11053 C CB . CYS B 2 501 ? -52.188 23.158 0.524 1.00 210.31 ? 501 CYS B CB 1 ATOM 11054 S SG . CYS B 2 501 ? -52.458 21.477 -0.104 1.00 233.17 ? 501 CYS B SG 1 ATOM 11055 N N . LEU B 2 502 ? -51.769 22.992 -2.624 1.00 202.22 ? 502 LEU B N 1 ATOM 11056 C CA . LEU B 2 502 ? -52.375 22.497 -3.858 1.00 193.91 ? 502 LEU B CA 1 ATOM 11057 C C . LEU B 2 502 ? -52.030 21.033 -4.134 1.00 193.46 ? 502 LEU B C 1 ATOM 11058 O O . LEU B 2 502 ? -50.882 20.619 -3.967 1.00 195.72 ? 502 LEU B O 1 ATOM 11059 C CB . LEU B 2 502 ? -51.961 23.372 -5.048 1.00 195.77 ? 502 LEU B CB 1 ATOM 11060 C CG . LEU B 2 502 ? -50.522 23.891 -5.163 1.00 198.45 ? 502 LEU B CG 1 ATOM 11061 C CD1 . LEU B 2 502 ? -49.559 22.840 -5.698 1.00 199.11 ? 502 LEU B CD1 1 ATOM 11062 C CD2 . LEU B 2 502 ? -50.482 25.139 -6.033 1.00 199.21 ? 502 LEU B CD2 1 ATOM 11063 N N . CYS B 2 503 ? -53.043 20.263 -4.533 1.00 192.05 ? 503 CYS B N 1 ATOM 11064 C CA . CYS B 2 503 ? -52.889 18.899 -5.059 1.00 164.81 ? 503 CYS B CA 1 ATOM 11065 C C . CYS B 2 503 ? -51.885 18.032 -4.294 1.00 154.10 ? 503 CYS B C 1 ATOM 11066 O O . CYS B 2 503 ? -50.790 17.758 -4.787 1.00 166.45 ? 503 CYS B O 1 ATOM 11067 C CB . CYS B 2 503 ? -52.517 18.937 -6.551 1.00 156.26 ? 503 CYS B CB 1 ATOM 11068 S SG . CYS B 2 503 ? -51.011 19.836 -7.008 1.00 187.09 ? 503 CYS B SG 1 ATOM 11069 N N . GLY B 2 504 ? -52.257 17.590 -3.098 1.00 144.10 ? 504 GLY B N 1 ATOM 11070 C CA . GLY B 2 504 ? -51.317 16.875 -2.256 1.00 151.24 ? 504 GLY B CA 1 ATOM 11071 C C . GLY B 2 504 ? -50.272 17.799 -1.663 1.00 149.08 ? 504 GLY B C 1 ATOM 11072 O O . GLY B 2 504 ? -50.621 18.748 -0.959 1.00 142.02 ? 504 GLY B O 1 ATOM 11073 N N . GLN B 2 505 ? -49.000 17.507 -1.926 1.00 151.42 ? 505 GLN B N 1 ATOM 11074 C CA . GLN B 2 505 ? -47.880 18.204 -1.292 1.00 164.52 ? 505 GLN B CA 1 ATOM 11075 C C . GLN B 2 505 ? -48.022 19.723 -1.360 1.00 173.01 ? 505 GLN B C 1 ATOM 11076 O O . GLN B 2 505 ? -48.269 20.293 -2.423 1.00 174.34 ? 505 GLN B O 1 ATOM 11077 C CB . GLN B 2 505 ? -46.554 17.785 -1.938 1.00 170.52 ? 505 GLN B CB 1 ATOM 11078 C CG . GLN B 2 505 ? -46.261 16.291 -1.883 1.00 168.77 ? 505 GLN B CG 1 ATOM 11079 C CD . GLN B 2 505 ? -46.944 15.516 -2.994 1.00 170.90 ? 505 GLN B CD 1 ATOM 11080 O OE1 . GLN B 2 505 ? -47.618 16.093 -3.847 1.00 169.87 ? 505 GLN B OE1 1 ATOM 11081 N NE2 . GLN B 2 505 ? -46.771 14.199 -2.989 1.00 168.11 ? 505 GLN B NE2 1 ATOM 11082 N N . CYS B 2 506 ? -47.863 20.363 -0.206 1.00 172.07 ? 506 CYS B N 1 ATOM 11083 C CA . CYS B 2 506 ? -48.165 21.780 -0.052 1.00 165.77 ? 506 CYS B CA 1 ATOM 11084 C C . CYS B 2 506 ? -47.054 22.691 -0.561 1.00 171.05 ? 506 CYS B C 1 ATOM 11085 O O . CYS B 2 506 ? -45.872 22.444 -0.319 1.00 164.07 ? 506 CYS B O 1 ATOM 11086 C CB . CYS B 2 506 ? -48.442 22.103 1.422 1.00 151.88 ? 506 CYS B CB 1 ATOM 11087 S SG . CYS B 2 506 ? -49.784 21.158 2.199 1.00 176.52 ? 506 CYS B SG 1 ATOM 11088 N N . VAL B 2 507 ? -47.442 23.743 -1.276 1.00 180.18 ? 507 VAL B N 1 ATOM 11089 C CA . VAL B 2 507 ? -46.540 24.859 -1.523 1.00 177.88 ? 507 VAL B CA 1 ATOM 11090 C C . VAL B 2 507 ? -46.787 25.882 -0.422 1.00 170.25 ? 507 VAL B C 1 ATOM 11091 O O . VAL B 2 507 ? -47.915 26.325 -0.211 1.00 158.88 ? 507 VAL B O 1 ATOM 11092 C CB . VAL B 2 507 ? -46.742 25.496 -2.919 1.00 182.29 ? 507 VAL B CB 1 ATOM 11093 C CG1 . VAL B 2 507 ? -46.165 24.597 -4.003 1.00 183.53 ? 507 VAL B CG1 1 ATOM 11094 C CG2 . VAL B 2 507 ? -48.211 25.786 -3.183 1.00 185.79 ? 507 VAL B CG2 1 ATOM 11095 N N . CYS B 2 508 ? -45.738 26.240 0.305 1.00 172.39 ? 508 CYS B N 1 ATOM 11096 C CA . CYS B 2 508 ? -45.919 27.073 1.482 1.00 168.30 ? 508 CYS B CA 1 ATOM 11097 C C . CYS B 2 508 ? -45.123 28.366 1.430 1.00 176.47 ? 508 CYS B C 1 ATOM 11098 O O . CYS B 2 508 ? -45.691 29.458 1.414 1.00 175.68 ? 508 CYS B O 1 ATOM 11099 C CB . CYS B 2 508 ? -45.547 26.293 2.745 1.00 162.49 ? 508 CYS B CB 1 ATOM 11100 S SG . CYS B 2 508 ? -46.804 25.112 3.289 1.00 163.32 ? 508 CYS B SG 1 ATOM 11101 N N . HIS B 2 509 ? -43.804 28.233 1.407 1.00 185.48 ? 509 HIS B N 1 ATOM 11102 C CA . HIS B 2 509 ? -42.938 29.363 1.696 1.00 197.68 ? 509 HIS B CA 1 ATOM 11103 C C . HIS B 2 509 ? -42.800 30.408 0.594 1.00 200.22 ? 509 HIS B C 1 ATOM 11104 O O . HIS B 2 509 ? -43.273 30.245 -0.532 1.00 199.71 ? 509 HIS B O 1 ATOM 11105 C CB . HIS B 2 509 ? -41.536 28.842 2.033 1.00 198.05 ? 509 HIS B CB 1 ATOM 11106 C CG . HIS B 2 509 ? -40.843 28.187 0.876 1.00 207.80 ? 509 HIS B CG 1 ATOM 11107 N ND1 . HIS B 2 509 ? -41.504 27.807 -0.273 1.00 213.25 ? 509 HIS B ND1 1 ATOM 11108 C CD2 . HIS B 2 509 ? -39.545 27.849 0.690 1.00 203.96 ? 509 HIS B CD2 1 ATOM 11109 C CE1 . HIS B 2 509 ? -40.645 27.262 -1.115 1.00 213.24 ? 509 HIS B CE1 1 ATOM 11110 N NE2 . HIS B 2 509 ? -39.449 27.275 -0.556 1.00 212.77 ? 509 HIS B NE2 1 ATOM 11111 N N . SER B 2 510 ? -42.136 31.489 0.978 1.00 191.05 ? 510 SER B N 1 ATOM 11112 C CA . SER B 2 510 ? -41.477 32.449 0.102 1.00 196.80 ? 510 SER B CA 1 ATOM 11113 C C . SER B 2 510 ? -40.061 32.663 0.704 1.00 195.15 ? 510 SER B C 1 ATOM 11114 O O . SER B 2 510 ? -39.077 32.441 -0.001 1.00 199.78 ? 510 SER B O 1 ATOM 11115 C CB . SER B 2 510 ? -42.291 33.744 -0.078 1.00 193.68 ? 510 SER B CB 1 ATOM 11116 O OG . SER B 2 510 ? -41.629 34.652 -0.940 1.00 199.40 ? 510 SER B OG 1 ATOM 11117 N N . SER B 2 511 ? -39.929 33.086 1.976 1.00 195.01 ? 511 SER B N 1 ATOM 11118 C CA . SER B 2 511 ? -41.027 33.566 2.824 1.00 191.22 ? 511 SER B CA 1 ATOM 11119 C C . SER B 2 511 ? -40.772 34.908 3.493 1.00 201.74 ? 511 SER B C 1 ATOM 11120 O O . SER B 2 511 ? -41.162 35.958 2.984 1.00 206.95 ? 511 SER B O 1 ATOM 11121 C CB . SER B 2 511 ? -41.334 32.524 3.904 1.00 168.68 ? 511 SER B CB 1 ATOM 11122 O OG . SER B 2 511 ? -40.185 32.251 4.687 1.00 162.58 ? 511 SER B OG 1 ATOM 11123 N N . ASP B 2 512 ? -40.117 34.852 4.646 1.00 189.44 ? 512 ASP B N 1 ATOM 11124 C CA . ASP B 2 512 ? -39.712 36.044 5.372 1.00 190.21 ? 512 ASP B CA 1 ATOM 11125 C C . ASP B 2 512 ? -38.324 35.891 5.982 1.00 179.19 ? 512 ASP B C 1 ATOM 11126 O O . ASP B 2 512 ? -37.349 36.514 5.560 1.00 172.91 ? 512 ASP B O 1 ATOM 11127 C CB . ASP B 2 512 ? -40.739 36.358 6.460 1.00 195.03 ? 512 ASP B CB 1 ATOM 11128 C CG . ASP B 2 512 ? -41.440 35.112 6.970 1.00 184.48 ? 512 ASP B CG 1 ATOM 11129 O OD1 . ASP B 2 512 ? -42.611 35.216 7.393 1.00 181.38 ? 512 ASP B OD1 1 ATOM 11130 O OD2 . ASP B 2 512 ? -40.823 34.026 6.938 1.00 157.22 ? 512 ASP B OD2 1 ATOM 11131 N N . PHE B 2 513 ? -38.278 35.032 6.996 1.00 172.09 ? 513 PHE B N 1 ATOM 11132 C CA . PHE B 2 513 ? -37.118 34.824 7.852 1.00 162.42 ? 513 PHE B CA 1 ATOM 11133 C C . PHE B 2 513 ? -36.292 33.618 7.411 1.00 166.31 ? 513 PHE B C 1 ATOM 11134 O O . PHE B 2 513 ? -35.361 33.205 8.101 1.00 156.76 ? 513 PHE B O 1 ATOM 11135 C CB . PHE B 2 513 ? -37.571 34.669 9.306 1.00 157.55 ? 513 PHE B CB 1 ATOM 11136 C CG . PHE B 2 513 ? -38.524 35.745 9.758 1.00 168.44 ? 513 PHE B CG 1 ATOM 11137 C CD1 . PHE B 2 513 ? -39.583 35.446 10.599 1.00 168.30 ? 513 PHE B CD1 1 ATOM 11138 C CD2 . PHE B 2 513 ? -38.360 37.056 9.338 1.00 171.44 ? 513 PHE B CD2 1 ATOM 11139 C CE1 . PHE B 2 513 ? -40.461 36.432 11.010 1.00 164.86 ? 513 PHE B CE1 1 ATOM 11140 C CE2 . PHE B 2 513 ? -39.235 38.046 9.746 1.00 165.08 ? 513 PHE B CE2 1 ATOM 11141 C CZ . PHE B 2 513 ? -40.286 37.735 10.584 1.00 162.28 ? 513 PHE B CZ 1 ATOM 11142 N N . GLY B 2 514 ? -36.639 33.061 6.255 1.00 189.82 ? 514 GLY B N 1 ATOM 11143 C CA . GLY B 2 514 ? -36.077 31.805 5.792 1.00 185.93 ? 514 GLY B CA 1 ATOM 11144 C C . GLY B 2 514 ? -37.075 30.661 5.765 1.00 182.26 ? 514 GLY B C 1 ATOM 11145 O O . GLY B 2 514 ? -38.245 30.837 6.109 1.00 182.20 ? 514 GLY B O 1 ATOM 11146 N N . LYS B 2 515 ? -36.596 29.484 5.366 1.00 185.69 ? 515 LYS B N 1 ATOM 11147 C CA . LYS B 2 515 ? -37.453 28.399 4.883 1.00 190.92 ? 515 LYS B CA 1 ATOM 11148 C C . LYS B 2 515 ? -38.571 27.958 5.829 1.00 184.91 ? 515 LYS B C 1 ATOM 11149 O O . LYS B 2 515 ? -38.408 27.929 7.051 1.00 179.06 ? 515 LYS B O 1 ATOM 11150 C CB . LYS B 2 515 ? -36.595 27.178 4.529 1.00 183.89 ? 515 LYS B CB 1 ATOM 11151 C CG . LYS B 2 515 ? -35.985 26.455 5.722 1.00 172.85 ? 515 LYS B CG 1 ATOM 11152 C CD . LYS B 2 515 ? -35.421 25.103 5.310 1.00 176.39 ? 515 LYS B CD 1 ATOM 11153 C CE . LYS B 2 515 ? -34.999 24.283 6.518 1.00 175.18 ? 515 LYS B CE 1 ATOM 11154 N NZ . LYS B 2 515 ? -34.521 22.928 6.129 1.00 179.16 ? 515 LYS B NZ 1 ATOM 11155 N N . ILE B 2 516 ? -39.715 27.633 5.233 1.00 175.54 ? 516 ILE B N 1 ATOM 11156 C CA . ILE B 2 516 ? -40.840 27.038 5.941 1.00 162.47 ? 516 ILE B CA 1 ATOM 11157 C C . ILE B 2 516 ? -41.067 25.624 5.416 1.00 163.31 ? 516 ILE B C 1 ATOM 11158 O O . ILE B 2 516 ? -41.468 25.440 4.266 1.00 178.39 ? 516 ILE B O 1 ATOM 11159 C CB . ILE B 2 516 ? -42.128 27.867 5.770 1.00 161.01 ? 516 ILE B CB 1 ATOM 11160 C CG1 . ILE B 2 516 ? -41.941 29.271 6.348 1.00 161.39 ? 516 ILE B CG1 1 ATOM 11161 C CG2 . ILE B 2 516 ? -43.305 27.166 6.430 1.00 158.61 ? 516 ILE B CG2 1 ATOM 11162 C CD1 . ILE B 2 516 ? -43.147 30.169 6.172 1.00 172.71 ? 516 ILE B CD1 1 ATOM 11163 N N . THR B 2 517 ? -40.805 24.628 6.256 1.00 159.78 ? 517 THR B N 1 ATOM 11164 C CA . THR B 2 517 ? -40.861 23.235 5.826 1.00 159.78 ? 517 THR B CA 1 ATOM 11165 C C . THR B 2 517 ? -41.904 22.420 6.583 1.00 156.15 ? 517 THR B C 1 ATOM 11166 O O . THR B 2 517 ? -42.289 22.766 7.698 1.00 152.89 ? 517 THR B O 1 ATOM 11167 C CB . THR B 2 517 ? -39.495 22.546 5.995 1.00 164.93 ? 517 THR B CB 1 ATOM 11168 O OG1 . THR B 2 517 ? -39.620 21.152 5.690 1.00 172.41 ? 517 THR B OG1 1 ATOM 11169 C CG2 . THR B 2 517 ? -38.996 22.702 7.424 1.00 161.08 ? 517 THR B CG2 1 ATOM 11170 N N . GLY B 2 518 ? -42.372 21.346 5.955 1.00 157.06 ? 518 GLY B N 1 ATOM 11171 C CA . GLY B 2 518 ? -43.262 20.403 6.606 1.00 151.48 ? 518 GLY B CA 1 ATOM 11172 C C . GLY B 2 518 ? -44.195 19.722 5.626 1.00 147.17 ? 518 GLY B C 1 ATOM 11173 O O . GLY B 2 518 ? -44.190 20.030 4.434 1.00 150.44 ? 518 GLY B O 1 ATOM 11174 N N . LYS B 2 519 ? -45.001 18.792 6.128 1.00 142.07 ? 519 LYS B N 1 ATOM 11175 C CA . LYS B 2 519 ? -46.063 18.200 5.327 1.00 139.45 ? 519 LYS B CA 1 ATOM 11176 C C . LYS B 2 519 ? -47.189 19.214 5.205 1.00 140.36 ? 519 LYS B C 1 ATOM 11177 O O . LYS B 2 519 ? -47.691 19.488 4.115 1.00 141.35 ? 519 LYS B O 1 ATOM 11178 C CB . LYS B 2 519 ? -46.572 16.904 5.958 1.00 133.36 ? 519 LYS B CB 1 ATOM 11179 C CG . LYS B 2 519 ? -47.474 16.087 5.052 1.00 131.75 ? 519 LYS B CG 1 ATOM 11180 C CD . LYS B 2 519 ? -48.124 14.940 5.808 1.00 128.29 ? 519 LYS B CD 1 ATOM 11181 C CE . LYS B 2 519 ? -48.735 13.936 4.848 1.00 137.20 ? 519 LYS B CE 1 ATOM 11182 N NZ . LYS B 2 519 ? -49.466 14.615 3.746 1.00 144.03 ? 519 LYS B NZ 1 ATOM 11183 N N . TYR B 2 520 ? -47.575 19.766 6.350 1.00 144.30 ? 520 TYR B N 1 ATOM 11184 C CA . TYR B 2 520 ? -48.545 20.848 6.412 1.00 149.74 ? 520 TYR B CA 1 ATOM 11185 C C . TYR B 2 520 ? -47.806 22.179 6.462 1.00 153.14 ? 520 TYR B C 1 ATOM 11186 O O . TYR B 2 520 ? -48.421 23.235 6.598 1.00 146.23 ? 520 TYR B O 1 ATOM 11187 C CB . TYR B 2 520 ? -49.454 20.696 7.636 1.00 149.95 ? 520 TYR B CB 1 ATOM 11188 C CG . TYR B 2 520 ? -50.060 19.319 7.795 1.00 153.43 ? 520 TYR B CG 1 ATOM 11189 C CD1 . TYR B 2 520 ? -49.370 18.306 8.451 1.00 148.57 ? 520 TYR B CD1 1 ATOM 11190 C CD2 . TYR B 2 520 ? -51.323 19.033 7.296 1.00 157.46 ? 520 TYR B CD2 1 ATOM 11191 C CE1 . TYR B 2 520 ? -49.919 17.046 8.600 1.00 150.53 ? 520 TYR B CE1 1 ATOM 11192 C CE2 . TYR B 2 520 ? -51.880 17.777 7.442 1.00 150.84 ? 520 TYR B CE2 1 ATOM 11193 C CZ . TYR B 2 520 ? -51.175 16.788 8.093 1.00 148.05 ? 520 TYR B CZ 1 ATOM 11194 O OH . TYR B 2 520 ? -51.727 15.537 8.239 1.00 141.00 ? 520 TYR B OH 1 ATOM 11195 N N . CYS B 2 521 ? -46.479 22.106 6.362 1.00 165.60 ? 521 CYS B N 1 ATOM 11196 C CA . CYS B 2 521 ? -45.600 23.263 6.528 1.00 160.51 ? 521 CYS B CA 1 ATOM 11197 C C . CYS B 2 521 ? -45.817 23.902 7.897 1.00 150.74 ? 521 CYS B C 1 ATOM 11198 O O . CYS B 2 521 ? -45.805 25.125 8.035 1.00 156.50 ? 521 CYS B O 1 ATOM 11199 C CB . CYS B 2 521 ? -45.823 24.290 5.412 1.00 163.26 ? 521 CYS B CB 1 ATOM 11200 S SG . CYS B 2 521 ? -45.436 23.684 3.752 1.00 155.05 ? 521 CYS B SG 1 ATOM 11201 N N . GLU B 2 522 ? -46.012 23.056 8.905 1.00 146.78 ? 522 GLU B N 1 ATOM 11202 C CA . GLU B 2 522 ? -46.292 23.514 10.262 1.00 146.56 ? 522 GLU B CA 1 ATOM 11203 C C . GLU B 2 522 ? -45.023 23.870 11.025 1.00 146.14 ? 522 GLU B C 1 ATOM 11204 O O . GLU B 2 522 ? -45.079 24.537 12.057 1.00 145.58 ? 522 GLU B O 1 ATOM 11205 C CB . GLU B 2 522 ? -47.076 22.448 11.033 1.00 153.29 ? 522 GLU B CB 1 ATOM 11206 C CG . GLU B 2 522 ? -46.275 21.196 11.382 1.00 158.61 ? 522 GLU B CG 1 ATOM 11207 C CD . GLU B 2 522 ? -46.099 20.250 10.205 1.00 150.50 ? 522 GLU B CD 1 ATOM 11208 O OE1 . GLU B 2 522 ? -46.553 20.582 9.091 1.00 152.07 ? 522 GLU B OE1 1 ATOM 11209 O OE2 . GLU B 2 522 ? -45.506 19.167 10.397 1.00 139.45 ? 522 GLU B OE2 1 ATOM 11210 N N . CYS B 2 523 ? -43.880 23.419 10.518 1.00 147.71 ? 523 CYS B N 1 ATOM 11211 C CA . CYS B 2 523 ? -42.606 23.694 11.171 1.00 151.23 ? 523 CYS B CA 1 ATOM 11212 C C . CYS B 2 523 ? -42.141 25.115 10.878 1.00 162.37 ? 523 CYS B C 1 ATOM 11213 O O . CYS B 2 523 ? -42.107 25.545 9.724 1.00 160.63 ? 523 CYS B O 1 ATOM 11214 C CB . CYS B 2 523 ? -41.543 22.687 10.729 1.00 154.06 ? 523 CYS B CB 1 ATOM 11215 S SG . CYS B 2 523 ? -41.906 20.973 11.171 1.00 167.69 ? 523 CYS B SG 1 ATOM 11216 N N . ASP B 2 524 ? -41.782 25.836 11.934 1.00 170.16 ? 524 ASP B N 1 ATOM 11217 C CA . ASP B 2 524 ? -41.347 27.221 11.815 1.00 166.93 ? 524 ASP B CA 1 ATOM 11218 C C . ASP B 2 524 ? -39.926 27.318 11.274 1.00 157.95 ? 524 ASP B C 1 ATOM 11219 O O . ASP B 2 524 ? -39.706 27.890 10.207 1.00 160.34 ? 524 ASP B O 1 ATOM 11220 C CB . ASP B 2 524 ? -41.437 27.930 13.169 1.00 164.69 ? 524 ASP B CB 1 ATOM 11221 C CG . ASP B 2 524 ? -42.852 27.975 13.710 1.00 173.54 ? 524 ASP B CG 1 ATOM 11222 O OD1 . ASP B 2 524 ? -43.226 27.060 14.474 1.00 172.09 ? 524 ASP B OD1 1 ATOM 11223 O OD2 . ASP B 2 524 ? -43.590 28.925 13.371 1.00 174.07 ? 524 ASP B OD2 1 ATOM 11224 N N . ASP B 2 525 ? -38.982 26.772 12.042 1.00 155.36 ? 525 ASP B N 1 ATOM 11225 C CA . ASP B 2 525 ? -37.537 26.834 11.782 1.00 159.12 ? 525 ASP B CA 1 ATOM 11226 C C . ASP B 2 525 ? -36.977 28.221 12.109 1.00 153.16 ? 525 ASP B C 1 ATOM 11227 O O . ASP B 2 525 ? -35.762 28.413 12.154 1.00 152.40 ? 525 ASP B O 1 ATOM 11228 C CB . ASP B 2 525 ? -37.204 26.443 10.335 1.00 177.42 ? 525 ASP B CB 1 ATOM 11229 C CG . ASP B 2 525 ? -35.715 26.246 10.109 1.00 170.79 ? 525 ASP B CG 1 ATOM 11230 O OD1 . ASP B 2 525 ? -35.216 25.130 10.362 1.00 170.74 ? 525 ASP B OD1 1 ATOM 11231 O OD2 . ASP B 2 525 ? -35.044 27.208 9.676 1.00 162.50 ? 525 ASP B OD2 1 ATOM 11232 N N . PHE B 2 526 ? -37.863 29.183 12.350 1.00 152.43 ? 526 PHE B N 1 ATOM 11233 C CA . PHE B 2 526 ? -37.449 30.472 12.892 1.00 149.89 ? 526 PHE B CA 1 ATOM 11234 C C . PHE B 2 526 ? -38.147 30.741 14.224 1.00 149.45 ? 526 PHE B C 1 ATOM 11235 O O . PHE B 2 526 ? -37.481 30.894 15.244 1.00 147.54 ? 526 PHE B O 1 ATOM 11236 C CB . PHE B 2 526 ? -37.688 31.626 11.902 1.00 150.20 ? 526 PHE B CB 1 ATOM 11237 C CG . PHE B 2 526 ? -38.976 31.536 11.127 1.00 154.44 ? 526 PHE B CG 1 ATOM 11238 C CD1 . PHE B 2 526 ? -40.122 32.167 11.581 1.00 154.87 ? 526 PHE B CD1 1 ATOM 11239 C CD2 . PHE B 2 526 ? -39.023 30.863 9.919 1.00 157.86 ? 526 PHE B CD2 1 ATOM 11240 C CE1 . PHE B 2 526 ? -41.300 32.098 10.862 1.00 159.97 ? 526 PHE B CE1 1 ATOM 11241 C CE2 . PHE B 2 526 ? -40.197 30.791 9.194 1.00 169.50 ? 526 PHE B CE2 1 ATOM 11242 C CZ . PHE B 2 526 ? -41.337 31.409 9.666 1.00 172.51 ? 526 PHE B CZ 1 ATOM 11243 N N . SER B 2 527 ? -39.476 30.805 14.219 1.00 153.73 ? 527 SER B N 1 ATOM 11244 C CA . SER B 2 527 ? -40.225 31.115 15.434 1.00 160.32 ? 527 SER B CA 1 ATOM 11245 C C . SER B 2 527 ? -39.887 30.145 16.565 1.00 154.11 ? 527 SER B C 1 ATOM 11246 O O . SER B 2 527 ? -40.027 28.930 16.423 1.00 158.87 ? 527 SER B O 1 ATOM 11247 C CB . SER B 2 527 ? -41.729 31.092 15.154 1.00 175.16 ? 527 SER B CB 1 ATOM 11248 O OG . SER B 2 527 ? -42.081 32.054 14.174 1.00 186.10 ? 527 SER B OG 1 ATOM 11249 N N . CYS B 2 528 ? -39.446 30.705 17.686 1.00 153.90 ? 528 CYS B N 1 ATOM 11250 C CA . CYS B 2 528 ? -38.998 29.926 18.836 1.00 147.68 ? 528 CYS B CA 1 ATOM 11251 C C . CYS B 2 528 ? -39.050 30.758 20.110 1.00 156.28 ? 528 CYS B C 1 ATOM 11252 O O . CYS B 2 528 ? -39.162 31.983 20.057 1.00 183.28 ? 528 CYS B O 1 ATOM 11253 C CB . CYS B 2 528 ? -37.579 29.398 18.617 1.00 144.55 ? 528 CYS B CB 1 ATOM 11254 S SG . CYS B 2 528 ? -37.490 27.717 17.961 1.00 142.58 ? 528 CYS B SG 1 ATOM 11255 N N . VAL B 2 529 ? -38.972 30.087 21.254 1.00 143.36 ? 529 VAL B N 1 ATOM 11256 C CA . VAL B 2 529 ? -38.931 30.772 22.541 1.00 144.92 ? 529 VAL B CA 1 ATOM 11257 C C . VAL B 2 529 ? -37.643 31.579 22.698 1.00 149.02 ? 529 VAL B C 1 ATOM 11258 O O . VAL B 2 529 ? -36.621 31.263 22.089 1.00 138.35 ? 529 VAL B O 1 ATOM 11259 C CB . VAL B 2 529 ? -39.050 29.780 23.712 1.00 134.15 ? 529 VAL B CB 1 ATOM 11260 C CG1 . VAL B 2 529 ? -40.456 29.204 23.779 1.00 135.31 ? 529 VAL B CG1 1 ATOM 11261 C CG2 . VAL B 2 529 ? -38.017 28.673 23.576 1.00 129.33 ? 529 VAL B CG2 1 ATOM 11262 N N . ARG B 2 530 ? -37.704 32.621 23.519 1.00 150.33 ? 530 ARG B N 1 ATOM 11263 C CA . ARG B 2 530 ? -36.557 33.487 23.760 1.00 140.22 ? 530 ARG B CA 1 ATOM 11264 C C . ARG B 2 530 ? -36.346 33.701 25.256 1.00 140.72 ? 530 ARG B C 1 ATOM 11265 O O . ARG B 2 530 ? -37.309 33.873 26.003 1.00 147.66 ? 530 ARG B O 1 ATOM 11266 C CB . ARG B 2 530 ? -36.745 34.836 23.061 1.00 148.12 ? 530 ARG B CB 1 ATOM 11267 C CG . ARG B 2 530 ? -36.846 34.755 21.546 1.00 150.52 ? 530 ARG B CG 1 ATOM 11268 C CD . ARG B 2 530 ? -37.224 36.103 20.949 1.00 162.52 ? 530 ARG B CD 1 ATOM 11269 N NE . ARG B 2 530 ? -37.187 36.092 19.490 1.00 159.17 ? 530 ARG B NE 1 ATOM 11270 C CZ . ARG B 2 530 ? -36.165 36.530 18.764 1.00 153.53 ? 530 ARG B CZ 1 ATOM 11271 N NH1 . ARG B 2 530 ? -35.087 37.022 19.360 1.00 147.80 ? 530 ARG B NH1 1 ATOM 11272 N NH2 . ARG B 2 530 ? -36.220 36.480 17.440 1.00 154.45 ? 530 ARG B NH2 1 ATOM 11273 N N . TYR B 2 531 ? -35.090 33.692 25.693 1.00 139.43 ? 531 TYR B N 1 ATOM 11274 C CA . TYR B 2 531 ? -34.790 33.934 27.099 1.00 145.47 ? 531 TYR B CA 1 ATOM 11275 C C . TYR B 2 531 ? -34.756 35.432 27.384 1.00 168.90 ? 531 TYR B C 1 ATOM 11276 O O . TYR B 2 531 ? -35.683 35.975 27.986 1.00 186.27 ? 531 TYR B O 1 ATOM 11277 C CB . TYR B 2 531 ? -33.460 33.283 27.486 1.00 129.05 ? 531 TYR B CB 1 ATOM 11278 C CG . TYR B 2 531 ? -32.950 33.690 28.850 1.00 121.83 ? 531 TYR B CG 1 ATOM 11279 C CD1 . TYR B 2 531 ? -33.699 33.446 29.994 1.00 129.92 ? 531 TYR B CD1 1 ATOM 11280 C CD2 . TYR B 2 531 ? -31.717 34.313 28.995 1.00 117.69 ? 531 TYR B CD2 1 ATOM 11281 C CE1 . TYR B 2 531 ? -33.237 33.817 31.243 1.00 136.97 ? 531 TYR B CE1 1 ATOM 11282 C CE2 . TYR B 2 531 ? -31.246 34.686 30.239 1.00 129.39 ? 531 TYR B CE2 1 ATOM 11283 C CZ . TYR B 2 531 ? -32.009 34.436 31.359 1.00 130.12 ? 531 TYR B CZ 1 ATOM 11284 O OH . TYR B 2 531 ? -31.542 34.806 32.600 1.00 123.22 ? 531 TYR B OH 1 ATOM 11285 N N . LYS B 2 532 ? -33.690 36.097 26.952 1.00 155.05 ? 532 LYS B N 1 ATOM 11286 C CA . LYS B 2 532 ? -33.653 37.554 26.971 1.00 134.95 ? 532 LYS B CA 1 ATOM 11287 C C . LYS B 2 532 ? -33.198 38.109 25.629 1.00 137.54 ? 532 LYS B C 1 ATOM 11288 O O . LYS B 2 532 ? -32.030 37.980 25.263 1.00 128.01 ? 532 LYS B O 1 ATOM 11289 C CB . LYS B 2 532 ? -32.723 38.052 28.078 1.00 123.67 ? 532 LYS B CB 1 ATOM 11290 C CG . LYS B 2 532 ? -33.308 37.974 29.474 1.00 127.83 ? 532 LYS B CG 1 ATOM 11291 C CD . LYS B 2 532 ? -32.284 38.393 30.513 1.00 138.17 ? 532 LYS B CD 1 ATOM 11292 C CE . LYS B 2 532 ? -32.958 38.938 31.759 1.00 155.31 ? 532 LYS B CE 1 ATOM 11293 N NZ . LYS B 2 532 ? -33.676 40.212 31.474 1.00 153.20 ? 532 LYS B NZ 1 ATOM 11294 N N . GLY B 2 533 ? -34.117 38.731 24.897 1.00 154.28 ? 533 GLY B N 1 ATOM 11295 C CA . GLY B 2 533 ? -33.767 39.470 23.697 1.00 165.48 ? 533 GLY B CA 1 ATOM 11296 C C . GLY B 2 533 ? -33.282 38.621 22.534 1.00 144.23 ? 533 GLY B C 1 ATOM 11297 O O . GLY B 2 533 ? -33.090 39.127 21.429 1.00 154.70 ? 533 GLY B O 1 ATOM 11298 N N . GLU B 2 534 ? -33.089 37.328 22.777 1.00 133.93 ? 534 GLU B N 1 ATOM 11299 C CA . GLU B 2 534 ? -32.400 36.470 21.820 1.00 139.63 ? 534 GLU B CA 1 ATOM 11300 C C . GLU B 2 534 ? -33.057 35.099 21.711 1.00 144.08 ? 534 GLU B C 1 ATOM 11301 O O . GLU B 2 534 ? -33.486 34.522 22.709 1.00 143.39 ? 534 GLU B O 1 ATOM 11302 C CB . GLU B 2 534 ? -30.930 36.325 22.223 1.00 134.17 ? 534 GLU B CB 1 ATOM 11303 C CG . GLU B 2 534 ? -29.977 36.040 21.075 1.00 134.91 ? 534 GLU B CG 1 ATOM 11304 C CD . GLU B 2 534 ? -28.524 36.241 21.469 1.00 144.03 ? 534 GLU B CD 1 ATOM 11305 O OE1 . GLU B 2 534 ? -28.261 36.499 22.664 1.00 143.52 ? 534 GLU B OE1 1 ATOM 11306 O OE2 . GLU B 2 534 ? -27.646 36.148 20.586 1.00 149.75 ? 534 GLU B OE2 1 ATOM 11307 N N . MET B 2 535 ? -33.123 34.579 20.489 1.00 149.08 ? 535 MET B N 1 ATOM 11308 C CA . MET B 2 535 ? -33.761 33.294 20.231 1.00 148.20 ? 535 MET B CA 1 ATOM 11309 C C . MET B 2 535 ? -32.884 32.132 20.680 1.00 139.94 ? 535 MET B C 1 ATOM 11310 O O . MET B 2 535 ? -31.740 32.002 20.239 1.00 128.23 ? 535 MET B O 1 ATOM 11311 C CB . MET B 2 535 ? -34.087 33.159 18.745 1.00 152.17 ? 535 MET B CB 1 ATOM 11312 C CG . MET B 2 535 ? -34.786 31.869 18.369 1.00 140.76 ? 535 MET B CG 1 ATOM 11313 S SD . MET B 2 535 ? -34.833 31.677 16.581 1.00 140.42 ? 535 MET B SD 1 ATOM 11314 C CE . MET B 2 535 ? -35.514 33.263 16.098 1.00 158.63 ? 535 MET B CE 1 ATOM 11315 N N . CYS B 2 536 ? -33.435 31.295 21.558 1.00 127.53 ? 536 CYS B N 1 ATOM 11316 C CA . CYS B 2 536 ? -32.715 30.166 22.145 1.00 120.63 ? 536 CYS B CA 1 ATOM 11317 C C . CYS B 2 536 ? -31.418 30.612 22.815 1.00 114.54 ? 536 CYS B C 1 ATOM 11318 O O . CYS B 2 536 ? -30.447 29.853 22.866 1.00 120.73 ? 536 CYS B O 1 ATOM 11319 C CB . CYS B 2 536 ? -32.420 29.099 21.086 1.00 121.88 ? 536 CYS B CB 1 ATOM 11320 S SG . CYS B 2 536 ? -33.880 28.241 20.458 1.00 133.55 ? 536 CYS B SG 1 ATOM 11321 N N . SER B 2 537 ? -31.412 31.856 23.297 1.00 113.99 ? 537 SER B N 1 ATOM 11322 C CA . SER B 2 537 ? -30.264 32.465 23.973 1.00 108.78 ? 537 SER B CA 1 ATOM 11323 C C . SER B 2 537 ? -29.070 32.660 23.033 1.00 106.10 ? 537 SER B C 1 ATOM 11324 O O . SER B 2 537 ? -28.044 33.215 23.430 1.00 102.01 ? 537 SER B O 1 ATOM 11325 C CB . SER B 2 537 ? -29.847 31.635 25.191 1.00 104.02 ? 537 SER B CB 1 ATOM 11326 O OG . SER B 2 537 ? -30.928 31.489 26.098 1.00 105.17 ? 537 SER B OG 1 ATOM 11327 N N . GLY B 2 538 ? -29.208 32.202 21.792 1.00 114.11 ? 538 GLY B N 1 ATOM 11328 C CA . GLY B 2 538 ? -28.122 32.235 20.829 1.00 111.63 ? 538 GLY B CA 1 ATOM 11329 C C . GLY B 2 538 ? -27.267 30.992 20.967 1.00 111.15 ? 538 GLY B C 1 ATOM 11330 O O . GLY B 2 538 ? -26.322 30.778 20.208 1.00 114.49 ? 538 GLY B O 1 ATOM 11331 N N . HIS B 2 539 ? -27.606 30.176 21.959 1.00 108.76 ? 539 HIS B N 1 ATOM 11332 C CA . HIS B 2 539 ? -26.856 28.969 22.277 1.00 106.42 ? 539 HIS B CA 1 ATOM 11333 C C . HIS B 2 539 ? -27.451 27.700 21.665 1.00 111.01 ? 539 HIS B C 1 ATOM 11334 O O . HIS B 2 539 ? -26.999 26.598 21.970 1.00 110.21 ? 539 HIS B O 1 ATOM 11335 C CB . HIS B 2 539 ? -26.744 28.817 23.795 1.00 100.58 ? 539 HIS B CB 1 ATOM 11336 C CG . HIS B 2 539 ? -26.046 29.963 24.460 1.00 103.29 ? 539 HIS B CG 1 ATOM 11337 N ND1 . HIS B 2 539 ? -24.786 30.381 24.091 1.00 99.52 ? 539 HIS B ND1 1 ATOM 11338 C CD2 . HIS B 2 539 ? -26.435 30.781 25.466 1.00 109.66 ? 539 HIS B CD2 1 ATOM 11339 C CE1 . HIS B 2 539 ? -24.428 31.408 24.840 1.00 98.88 ? 539 HIS B CE1 1 ATOM 11340 N NE2 . HIS B 2 539 ? -25.411 31.670 25.685 1.00 109.82 ? 539 HIS B NE2 1 ATOM 11341 N N . GLY B 2 540 ? -28.477 27.841 20.831 1.00 115.69 ? 540 GLY B N 1 ATOM 11342 C CA . GLY B 2 540 ? -29.078 26.675 20.209 1.00 120.31 ? 540 GLY B CA 1 ATOM 11343 C C . GLY B 2 540 ? -29.753 26.909 18.871 1.00 127.60 ? 540 GLY B C 1 ATOM 11344 O O . GLY B 2 540 ? -30.175 28.021 18.556 1.00 128.05 ? 540 GLY B O 1 ATOM 11345 N N . GLN B 2 541 ? -29.854 25.842 18.082 1.00 136.86 ? 541 GLN B N 1 ATOM 11346 C CA . GLN B 2 541 ? -30.532 25.884 16.790 1.00 143.96 ? 541 GLN B CA 1 ATOM 11347 C C . GLN B 2 541 ? -32.037 25.700 16.956 1.00 145.73 ? 541 GLN B C 1 ATOM 11348 O O . GLN B 2 541 ? -32.488 24.981 17.848 1.00 154.42 ? 541 GLN B O 1 ATOM 11349 C CB . GLN B 2 541 ? -29.978 24.809 15.852 1.00 148.84 ? 541 GLN B CB 1 ATOM 11350 C CG . GLN B 2 541 ? -28.512 24.981 15.491 1.00 157.44 ? 541 GLN B CG 1 ATOM 11351 C CD . GLN B 2 541 ? -28.021 23.916 14.527 1.00 166.24 ? 541 GLN B CD 1 ATOM 11352 O OE1 . GLN B 2 541 ? -28.784 23.047 14.105 1.00 167.53 ? 541 GLN B OE1 1 ATOM 11353 N NE2 . GLN B 2 541 ? -26.742 23.978 14.175 1.00 173.03 ? 541 GLN B NE2 1 ATOM 11354 N N . CYS B 2 542 ? -32.810 26.351 16.094 1.00 144.11 ? 542 CYS B N 1 ATOM 11355 C CA . CYS B 2 542 ? -34.262 26.230 16.132 1.00 142.96 ? 542 CYS B CA 1 ATOM 11356 C C . CYS B 2 542 ? -34.765 25.301 15.031 1.00 150.02 ? 542 CYS B C 1 ATOM 11357 O O . CYS B 2 542 ? -34.684 25.627 13.846 1.00 154.21 ? 542 CYS B O 1 ATOM 11358 C CB . CYS B 2 542 ? -34.918 27.606 16.000 1.00 143.84 ? 542 CYS B CB 1 ATOM 11359 S SG . CYS B 2 542 ? -36.723 27.582 16.086 1.00 146.85 ? 542 CYS B SG 1 ATOM 11360 N N . SER B 2 543 ? -35.282 24.143 15.428 1.00 152.51 ? 543 SER B N 1 ATOM 11361 C CA . SER B 2 543 ? -35.804 23.169 14.475 1.00 149.04 ? 543 SER B CA 1 ATOM 11362 C C . SER B 2 543 ? -37.283 22.889 14.717 1.00 145.13 ? 543 SER B C 1 ATOM 11363 O O . SER B 2 543 ? -37.651 22.310 15.739 1.00 138.99 ? 543 SER B O 1 ATOM 11364 C CB . SER B 2 543 ? -35.009 21.864 14.551 1.00 148.72 ? 543 SER B CB 1 ATOM 11365 O OG . SER B 2 543 ? -35.537 20.893 13.665 1.00 154.22 ? 543 SER B OG 1 ATOM 11366 N N . CYS B 2 544 ? -38.115 23.301 13.764 1.00 147.98 ? 544 CYS B N 1 ATOM 11367 C CA . CYS B 2 544 ? -39.561 23.084 13.813 1.00 149.84 ? 544 CYS B CA 1 ATOM 11368 C C . CYS B 2 544 ? -40.177 23.617 15.106 1.00 142.42 ? 544 CYS B C 1 ATOM 11369 O O . CYS B 2 544 ? -41.030 22.968 15.714 1.00 137.46 ? 544 CYS B O 1 ATOM 11370 C CB . CYS B 2 544 ? -39.884 21.595 13.649 1.00 149.24 ? 544 CYS B CB 1 ATOM 11371 S SG . CYS B 2 544 ? -41.592 21.238 13.160 1.00 193.87 ? 544 CYS B SG 1 ATOM 11372 N N . GLY B 2 545 ? -39.738 24.799 15.522 1.00 143.70 ? 545 GLY B N 1 ATOM 11373 C CA . GLY B 2 545 ? -40.265 25.432 16.717 1.00 141.61 ? 545 GLY B CA 1 ATOM 11374 C C . GLY B 2 545 ? -39.722 24.841 18.005 1.00 136.60 ? 545 GLY B C 1 ATOM 11375 O O . GLY B 2 545 ? -40.285 25.052 19.079 1.00 134.03 ? 545 GLY B O 1 ATOM 11376 N N . ASP B 2 546 ? -38.623 24.100 17.898 1.00 135.43 ? 546 ASP B N 1 ATOM 11377 C CA . ASP B 2 546 ? -37.992 23.496 19.066 1.00 129.78 ? 546 ASP B CA 1 ATOM 11378 C C . ASP B 2 546 ? -36.503 23.823 19.104 1.00 129.28 ? 546 ASP B C 1 ATOM 11379 O O . ASP B 2 546 ? -35.846 23.883 18.065 1.00 133.68 ? 546 ASP B O 1 ATOM 11380 C CB . ASP B 2 546 ? -38.209 21.982 19.072 1.00 132.25 ? 546 ASP B CB 1 ATOM 11381 C CG . ASP B 2 546 ? -39.661 21.604 19.298 1.00 153.06 ? 546 ASP B CG 1 ATOM 11382 O OD1 . ASP B 2 546 ? -40.159 20.695 18.600 1.00 157.84 ? 546 ASP B OD1 1 ATOM 11383 O OD2 . ASP B 2 546 ? -40.305 22.216 20.176 1.00 162.49 ? 546 ASP B OD2 1 ATOM 11384 N N . CYS B 2 547 ? -35.976 24.034 20.305 1.00 124.21 ? 547 CYS B N 1 ATOM 11385 C CA . CYS B 2 547 ? -34.582 24.427 20.465 1.00 122.35 ? 547 CYS B CA 1 ATOM 11386 C C . CYS B 2 547 ? -33.654 23.227 20.598 1.00 119.02 ? 547 CYS B C 1 ATOM 11387 O O . CYS B 2 547 ? -33.769 22.441 21.540 1.00 114.69 ? 547 CYS B O 1 ATOM 11388 C CB . CYS B 2 547 ? -34.421 25.340 21.683 1.00 118.54 ? 547 CYS B CB 1 ATOM 11389 S SG . CYS B 2 547 ? -35.117 26.994 21.480 1.00 146.61 ? 547 CYS B SG 1 ATOM 11390 N N . LEU B 2 548 ? -32.735 23.094 19.648 1.00 123.21 ? 548 LEU B N 1 ATOM 11391 C CA . LEU B 2 548 ? -31.688 22.087 19.731 1.00 122.21 ? 548 LEU B CA 1 ATOM 11392 C C . LEU B 2 548 ? -30.403 22.768 20.182 1.00 120.98 ? 548 LEU B C 1 ATOM 11393 O O . LEU B 2 548 ? -29.800 23.536 19.433 1.00 126.35 ? 548 LEU B O 1 ATOM 11394 C CB . LEU B 2 548 ? -31.495 21.383 18.387 1.00 130.42 ? 548 LEU B CB 1 ATOM 11395 C CG . LEU B 2 548 ? -32.746 20.749 17.773 1.00 131.71 ? 548 LEU B CG 1 ATOM 11396 C CD1 . LEU B 2 548 ? -32.404 19.984 16.501 1.00 140.29 ? 548 LEU B CD1 1 ATOM 11397 C CD2 . LEU B 2 548 ? -33.445 19.845 18.778 1.00 123.39 ? 548 LEU B CD2 1 ATOM 11398 N N . CYS B 2 549 ? -29.989 22.479 21.411 1.00 114.26 ? 549 CYS B N 1 ATOM 11399 C CA . CYS B 2 549 ? -28.915 23.226 22.054 1.00 110.66 ? 549 CYS B CA 1 ATOM 11400 C C . CYS B 2 549 ? -27.529 22.881 21.523 1.00 116.35 ? 549 CYS B C 1 ATOM 11401 O O . CYS B 2 549 ? -27.254 21.739 21.155 1.00 120.36 ? 549 CYS B O 1 ATOM 11402 C CB . CYS B 2 549 ? -28.949 22.996 23.567 1.00 101.88 ? 549 CYS B CB 1 ATOM 11403 S SG . CYS B 2 549 ? -30.449 23.582 24.383 1.00 153.93 ? 549 CYS B SG 1 ATOM 11404 N N . ASP B 2 550 ? -26.661 23.886 21.493 1.00 109.83 ? 550 ASP B N 1 ATOM 11405 C CA . ASP B 2 550 ? -25.251 23.681 21.195 1.00 109.32 ? 550 ASP B CA 1 ATOM 11406 C C . ASP B 2 550 ? -24.601 22.958 22.366 1.00 102.51 ? 550 ASP B C 1 ATOM 11407 O O . ASP B 2 550 ? -25.171 22.899 23.456 1.00 102.98 ? 550 ASP B O 1 ATOM 11408 C CB . ASP B 2 550 ? -24.543 25.009 20.922 1.00 113.79 ? 550 ASP B CB 1 ATOM 11409 C CG . ASP B 2 550 ? -25.100 25.730 19.709 1.00 118.88 ? 550 ASP B CG 1 ATOM 11410 O OD1 . ASP B 2 550 ? -25.479 25.048 18.735 1.00 139.10 ? 550 ASP B OD1 1 ATOM 11411 O OD2 . ASP B 2 550 ? -25.162 26.978 19.730 1.00 100.79 ? 550 ASP B OD2 1 ATOM 11412 N N . SER B 2 551 ? -23.425 22.385 22.131 1.00 101.40 ? 551 SER B N 1 ATOM 11413 C CA . SER B 2 551 ? -22.694 21.666 23.169 1.00 100.83 ? 551 SER B CA 1 ATOM 11414 C C . SER B 2 551 ? -22.466 22.546 24.395 1.00 100.60 ? 551 SER B C 1 ATOM 11415 O O . SER B 2 551 ? -22.331 23.764 24.271 1.00 117.83 ? 551 SER B O 1 ATOM 11416 C CB . SER B 2 551 ? -21.355 21.166 22.626 1.00 99.37 ? 551 SER B CB 1 ATOM 11417 O OG . SER B 2 551 ? -21.529 20.493 21.392 1.00 104.04 ? 551 SER B OG 1 ATOM 11418 N N . ASP B 2 552 ? -22.464 21.911 25.568 1.00 101.19 ? 552 ASP B N 1 ATOM 11419 C CA . ASP B 2 552 ? -22.266 22.567 26.867 1.00 100.37 ? 552 ASP B CA 1 ATOM 11420 C C . ASP B 2 552 ? -23.477 23.395 27.306 1.00 101.26 ? 552 ASP B C 1 ATOM 11421 O O . ASP B 2 552 ? -23.473 23.978 28.391 1.00 101.88 ? 552 ASP B O 1 ATOM 11422 C CB . ASP B 2 552 ? -21.007 23.442 26.856 1.00 98.05 ? 552 ASP B CB 1 ATOM 11423 C CG . ASP B 2 552 ? -19.740 22.635 26.663 1.00 101.98 ? 552 ASP B CG 1 ATOM 11424 O OD1 . ASP B 2 552 ? -19.269 22.529 25.512 1.00 103.94 ? 552 ASP B OD1 1 ATOM 11425 O OD2 . ASP B 2 552 ? -19.220 22.099 27.664 1.00 119.00 ? 552 ASP B OD2 1 ATOM 11426 N N . TRP B 2 553 ? -24.505 23.451 26.466 1.00 102.62 ? 553 TRP B N 1 ATOM 11427 C CA . TRP B 2 553 ? -25.745 24.135 26.823 1.00 103.66 ? 553 TRP B CA 1 ATOM 11428 C C . TRP B 2 553 ? -26.937 23.176 26.863 1.00 104.70 ? 553 TRP B C 1 ATOM 11429 O O . TRP B 2 553 ? -27.062 22.289 26.019 1.00 104.84 ? 553 TRP B O 1 ATOM 11430 C CB . TRP B 2 553 ? -26.027 25.275 25.842 1.00 108.56 ? 553 TRP B CB 1 ATOM 11431 C CG . TRP B 2 553 ? -25.003 26.363 25.880 1.00 101.01 ? 553 TRP B CG 1 ATOM 11432 C CD1 . TRP B 2 553 ? -23.970 26.548 25.007 1.00 101.77 ? 553 TRP B CD1 1 ATOM 11433 C CD2 . TRP B 2 553 ? -24.907 27.419 26.844 1.00 99.49 ? 553 TRP B CD2 1 ATOM 11434 N NE1 . TRP B 2 553 ? -23.239 27.655 25.367 1.00 96.14 ? 553 TRP B NE1 1 ATOM 11435 C CE2 . TRP B 2 553 ? -23.794 28.207 26.492 1.00 95.69 ? 553 TRP B CE2 1 ATOM 11436 C CE3 . TRP B 2 553 ? -25.656 27.774 27.970 1.00 103.09 ? 553 TRP B CE3 1 ATOM 11437 C CZ2 . TRP B 2 553 ? -23.411 29.327 27.226 1.00 91.54 ? 553 TRP B CZ2 1 ATOM 11438 C CZ3 . TRP B 2 553 ? -25.275 28.886 28.696 1.00 96.84 ? 553 TRP B CZ3 1 ATOM 11439 C CH2 . TRP B 2 553 ? -24.164 29.650 28.322 1.00 91.87 ? 553 TRP B CH2 1 ATOM 11440 N N . THR B 2 554 ? -27.803 23.357 27.857 1.00 104.91 ? 554 THR B N 1 ATOM 11441 C CA . THR B 2 554 ? -29.020 22.560 27.987 1.00 105.17 ? 554 THR B CA 1 ATOM 11442 C C . THR B 2 554 ? -30.200 23.444 28.375 1.00 104.07 ? 554 THR B C 1 ATOM 11443 O O . THR B 2 554 ? -30.049 24.653 28.547 1.00 111.01 ? 554 THR B O 1 ATOM 11444 C CB . THR B 2 554 ? -28.872 21.442 29.041 1.00 105.35 ? 554 THR B CB 1 ATOM 11445 O OG1 . THR B 2 554 ? -28.455 22.009 30.289 1.00 105.26 ? 554 THR B OG1 1 ATOM 11446 C CG2 . THR B 2 554 ? -27.853 20.407 28.593 1.00 105.94 ? 554 THR B CG2 1 ATOM 11447 N N . GLY B 2 555 ? -31.374 22.836 28.519 1.00 103.14 ? 555 GLY B N 1 ATOM 11448 C CA . GLY B 2 555 ? -32.562 23.560 28.931 1.00 100.84 ? 555 GLY B CA 1 ATOM 11449 C C . GLY B 2 555 ? -33.525 23.847 27.794 1.00 99.38 ? 555 GLY B C 1 ATOM 11450 O O . GLY B 2 555 ? -33.158 23.781 26.622 1.00 100.45 ? 555 GLY B O 1 ATOM 11451 N N . TYR B 2 556 ? -34.766 24.164 28.150 1.00 97.35 ? 556 TYR B N 1 ATOM 11452 C CA . TYR B 2 556 ? -35.797 24.485 27.170 1.00 95.71 ? 556 TYR B CA 1 ATOM 11453 C C . TYR B 2 556 ? -35.436 25.750 26.395 1.00 95.71 ? 556 TYR B C 1 ATOM 11454 O O . TYR B 2 556 ? -35.637 25.825 25.183 1.00 95.45 ? 556 TYR B O 1 ATOM 11455 C CB . TYR B 2 556 ? -37.154 24.651 27.860 1.00 98.99 ? 556 TYR B CB 1 ATOM 11456 C CG . TYR B 2 556 ? -38.324 24.827 26.916 1.00 126.91 ? 556 TYR B CG 1 ATOM 11457 C CD1 . TYR B 2 556 ? -38.707 26.089 26.478 1.00 115.13 ? 556 TYR B CD1 1 ATOM 11458 C CD2 . TYR B 2 556 ? -39.056 23.732 26.473 1.00 136.76 ? 556 TYR B CD2 1 ATOM 11459 C CE1 . TYR B 2 556 ? -39.777 26.256 25.621 1.00 109.47 ? 556 TYR B CE1 1 ATOM 11460 C CE2 . TYR B 2 556 ? -40.130 23.890 25.614 1.00 137.19 ? 556 TYR B CE2 1 ATOM 11461 C CZ . TYR B 2 556 ? -40.485 25.154 25.192 1.00 136.62 ? 556 TYR B CZ 1 ATOM 11462 O OH . TYR B 2 556 ? -41.552 25.319 24.338 1.00 152.59 ? 556 TYR B OH 1 ATOM 11463 N N . TYR B 2 557 ? -34.904 26.740 27.105 1.00 113.24 ? 557 TYR B N 1 ATOM 11464 C CA . TYR B 2 557 ? -34.495 28.000 26.493 1.00 105.25 ? 557 TYR B CA 1 ATOM 11465 C C . TYR B 2 557 ? -33.015 27.983 26.129 1.00 103.38 ? 557 TYR B C 1 ATOM 11466 O O . TYR B 2 557 ? -32.484 28.964 25.605 1.00 115.01 ? 557 TYR B O 1 ATOM 11467 C CB . TYR B 2 557 ? -34.783 29.173 27.433 1.00 97.19 ? 557 TYR B CB 1 ATOM 11468 C CG . TYR B 2 557 ? -36.226 29.281 27.869 1.00 114.67 ? 557 TYR B CG 1 ATOM 11469 C CD1 . TYR B 2 557 ? -37.160 29.948 27.087 1.00 116.69 ? 557 TYR B CD1 1 ATOM 11470 C CD2 . TYR B 2 557 ? -36.654 28.719 29.065 1.00 120.94 ? 557 TYR B CD2 1 ATOM 11471 C CE1 . TYR B 2 557 ? -38.481 30.048 27.483 1.00 117.75 ? 557 TYR B CE1 1 ATOM 11472 C CE2 . TYR B 2 557 ? -37.972 28.815 29.469 1.00 118.30 ? 557 TYR B CE2 1 ATOM 11473 C CZ . TYR B 2 557 ? -38.881 29.481 28.675 1.00 122.67 ? 557 TYR B CZ 1 ATOM 11474 O OH . TYR B 2 557 ? -40.194 29.578 29.075 1.00 131.38 ? 557 TYR B OH 1 ATOM 11475 N N . CYS B 2 558 ? -32.359 26.861 26.422 1.00 102.44 ? 558 CYS B N 1 ATOM 11476 C CA . CYS B 2 558 ? -30.922 26.689 26.205 1.00 101.70 ? 558 CYS B CA 1 ATOM 11477 C C . CYS B 2 558 ? -30.083 27.723 26.958 1.00 100.85 ? 558 CYS B C 1 ATOM 11478 O O . CYS B 2 558 ? -28.990 28.079 26.519 1.00 101.05 ? 558 CYS B O 1 ATOM 11479 C CB . CYS B 2 558 ? -30.590 26.741 24.710 1.00 101.53 ? 558 CYS B CB 1 ATOM 11480 S SG . CYS B 2 558 ? -31.227 25.349 23.751 1.00 160.77 ? 558 CYS B SG 1 ATOM 11481 N N . ASN B 2 559 ? -30.598 28.205 28.087 1.00 98.48 ? 559 ASN B N 1 ATOM 11482 C CA . ASN B 2 559 ? -29.853 29.142 28.925 1.00 95.92 ? 559 ASN B CA 1 ATOM 11483 C C . ASN B 2 559 ? -29.139 28.459 30.095 1.00 113.83 ? 559 ASN B C 1 ATOM 11484 O O . ASN B 2 559 ? -28.510 29.123 30.920 1.00 119.66 ? 559 ASN B O 1 ATOM 11485 C CB . ASN B 2 559 ? -30.779 30.248 29.443 1.00 91.98 ? 559 ASN B CB 1 ATOM 11486 C CG . ASN B 2 559 ? -31.893 29.722 30.333 1.00 115.05 ? 559 ASN B CG 1 ATOM 11487 O OD1 . ASN B 2 559 ? -32.200 28.532 30.329 1.00 125.54 ? 559 ASN B OD1 1 ATOM 11488 N ND2 . ASN B 2 559 ? -32.508 30.621 31.097 1.00 130.41 ? 559 ASN B ND2 1 ATOM 11489 N N . CYS B 2 560 ? -29.235 27.134 30.163 1.00 113.07 ? 560 CYS B N 1 ATOM 11490 C CA . CYS B 2 560 ? -28.612 26.370 31.245 1.00 100.10 ? 560 CYS B CA 1 ATOM 11491 C C . CYS B 2 560 ? -27.250 25.807 30.831 1.00 102.14 ? 560 CYS B C 1 ATOM 11492 O O . CYS B 2 560 ? -27.048 25.425 29.678 1.00 102.71 ? 560 CYS B O 1 ATOM 11493 C CB . CYS B 2 560 ? -29.531 25.236 31.696 1.00 100.48 ? 560 CYS B CB 1 ATOM 11494 S SG . CYS B 2 560 ? -28.961 24.366 33.175 1.00 152.82 ? 560 CYS B SG 1 ATOM 11495 N N . THR B 2 561 ? -26.318 25.759 31.778 1.00 101.73 ? 561 THR B N 1 ATOM 11496 C CA . THR B 2 561 ? -24.937 25.386 31.477 1.00 100.89 ? 561 THR B CA 1 ATOM 11497 C C . THR B 2 561 ? -24.533 24.043 32.088 1.00 102.12 ? 561 THR B C 1 ATOM 11498 O O . THR B 2 561 ? -25.079 23.623 33.108 1.00 115.42 ? 561 THR B O 1 ATOM 11499 C CB . THR B 2 561 ? -23.959 26.466 31.973 1.00 96.35 ? 561 THR B CB 1 ATOM 11500 O OG1 . THR B 2 561 ? -24.618 27.738 31.998 1.00 121.70 ? 561 THR B OG1 1 ATOM 11501 C CG2 . THR B 2 561 ? -22.744 26.546 31.061 1.00 93.20 ? 561 THR B CG2 1 ATOM 11502 N N . THR B 2 562 ? -23.582 23.371 31.444 1.00 101.30 ? 562 THR B N 1 ATOM 11503 C CA . THR B 2 562 ? -23.040 22.108 31.940 1.00 101.86 ? 562 THR B CA 1 ATOM 11504 C C . THR B 2 562 ? -21.799 22.350 32.803 1.00 98.29 ? 562 THR B C 1 ATOM 11505 O O . THR B 2 562 ? -21.238 21.417 33.378 1.00 98.34 ? 562 THR B O 1 ATOM 11506 C CB . THR B 2 562 ? -22.668 21.157 30.780 1.00 103.10 ? 562 THR B CB 1 ATOM 11507 O OG1 . THR B 2 562 ? -23.558 21.365 29.678 1.00 102.84 ? 562 THR B OG1 1 ATOM 11508 C CG2 . THR B 2 562 ? -22.738 19.699 31.223 1.00 139.11 ? 562 THR B CG2 1 ATOM 11509 N N . ARG B 2 563 ? -21.378 23.608 32.886 1.00 95.24 ? 563 ARG B N 1 ATOM 11510 C CA . ARG B 2 563 ? -20.152 23.971 33.596 1.00 94.29 ? 563 ARG B CA 1 ATOM 11511 C C . ARG B 2 563 ? -20.280 23.856 35.114 1.00 90.95 ? 563 ARG B C 1 ATOM 11512 O O . ARG B 2 563 ? -21.150 24.477 35.722 1.00 90.78 ? 563 ARG B O 1 ATOM 11513 C CB . ARG B 2 563 ? -19.737 25.399 33.233 1.00 90.38 ? 563 ARG B CB 1 ATOM 11514 C CG . ARG B 2 563 ? -19.283 25.584 31.795 1.00 106.35 ? 563 ARG B CG 1 ATOM 11515 C CD . ARG B 2 563 ? -19.118 27.060 31.460 1.00 107.69 ? 563 ARG B CD 1 ATOM 11516 N NE . ARG B 2 563 ? -18.207 27.736 32.379 1.00 99.96 ? 563 ARG B NE 1 ATOM 11517 C CZ . ARG B 2 563 ? -17.891 29.025 32.303 1.00 85.91 ? 563 ARG B CZ 1 ATOM 11518 N NH1 . ARG B 2 563 ? -18.413 29.782 31.348 1.00 84.86 ? 563 ARG B NH1 1 ATOM 11519 N NH2 . ARG B 2 563 ? -17.052 29.557 33.182 1.00 78.21 ? 563 ARG B NH2 1 ATOM 11520 N N . THR B 2 564 ? -19.411 23.049 35.716 1.00 98.45 ? 564 THR B N 1 ATOM 11521 C CA . THR B 2 564 ? -19.308 22.967 37.171 1.00 100.95 ? 564 THR B CA 1 ATOM 11522 C C . THR B 2 564 ? -18.150 23.797 37.720 1.00 94.31 ? 564 THR B C 1 ATOM 11523 O O . THR B 2 564 ? -17.959 23.876 38.934 1.00 89.89 ? 564 THR B O 1 ATOM 11524 C CB . THR B 2 564 ? -19.126 21.514 37.639 1.00 100.35 ? 564 THR B CB 1 ATOM 11525 O OG1 . THR B 2 564 ? -17.943 20.965 37.046 1.00 106.15 ? 564 THR B OG1 1 ATOM 11526 C CG2 . THR B 2 564 ? -20.327 20.673 37.244 1.00 95.65 ? 564 THR B CG2 1 ATOM 11527 N N . ASP B 2 565 ? -17.381 24.410 36.826 1.00 96.37 ? 565 ASP B N 1 ATOM 11528 C CA . ASP B 2 565 ? -16.142 25.078 37.218 1.00 96.44 ? 565 ASP B CA 1 ATOM 11529 C C . ASP B 2 565 ? -16.400 26.332 38.047 1.00 89.76 ? 565 ASP B C 1 ATOM 11530 O O . ASP B 2 565 ? -15.598 26.688 38.910 1.00 97.99 ? 565 ASP B O 1 ATOM 11531 C CB . ASP B 2 565 ? -15.308 25.427 35.981 1.00 102.17 ? 565 ASP B CB 1 ATOM 11532 C CG . ASP B 2 565 ? -15.969 26.474 35.106 1.00 102.68 ? 565 ASP B CG 1 ATOM 11533 O OD1 . ASP B 2 565 ? -16.757 26.097 34.213 1.00 118.49 ? 565 ASP B OD1 1 ATOM 11534 O OD2 . ASP B 2 565 ? -15.695 27.676 35.309 1.00 87.18 ? 565 ASP B OD2 1 ATOM 11535 N N . THR B 2 566 ? -17.521 26.996 37.787 1.00 88.28 ? 566 THR B N 1 ATOM 11536 C CA . THR B 2 566 ? -17.883 28.196 38.532 1.00 82.55 ? 566 THR B CA 1 ATOM 11537 C C . THR B 2 566 ? -18.529 27.826 39.864 1.00 77.81 ? 566 THR B C 1 ATOM 11538 O O . THR B 2 566 ? -18.788 28.690 40.700 1.00 77.14 ? 566 THR B O 1 ATOM 11539 C CB . THR B 2 566 ? -18.843 29.096 37.732 1.00 80.70 ? 566 THR B CB 1 ATOM 11540 O OG1 . THR B 2 566 ? -20.050 28.378 37.446 1.00 100.49 ? 566 THR B OG1 1 ATOM 11541 C CG2 . THR B 2 566 ? -18.200 29.541 36.427 1.00 75.64 ? 566 THR B CG2 1 ATOM 11542 N N . CYS B 2 567 ? -18.794 26.536 40.047 1.00 82.70 ? 567 CYS B N 1 ATOM 11543 C CA . CYS B 2 567 ? -19.378 26.034 41.285 1.00 89.29 ? 567 CYS B CA 1 ATOM 11544 C C . CYS B 2 567 ? -18.311 25.507 42.242 1.00 107.30 ? 567 CYS B C 1 ATOM 11545 O O . CYS B 2 567 ? -18.623 25.056 43.345 1.00 128.10 ? 567 CYS B O 1 ATOM 11546 C CB . CYS B 2 567 ? -20.396 24.932 40.986 1.00 82.78 ? 567 CYS B CB 1 ATOM 11547 S SG . CYS B 2 567 ? -21.820 25.454 40.005 1.00 129.28 ? 567 CYS B SG 1 ATOM 11548 N N . MET B 2 568 ? -17.054 25.565 41.815 1.00 105.76 ? 568 MET B N 1 ATOM 11549 C CA . MET B 2 568 ? -15.954 24.992 42.586 1.00 108.13 ? 568 MET B CA 1 ATOM 11550 C C . MET B 2 568 ? -15.467 25.930 43.688 1.00 104.75 ? 568 MET B C 1 ATOM 11551 O O . MET B 2 568 ? -15.053 27.058 43.421 1.00 94.64 ? 568 MET B O 1 ATOM 11552 C CB . MET B 2 568 ? -14.791 24.630 41.658 1.00 121.39 ? 568 MET B CB 1 ATOM 11553 C CG . MET B 2 568 ? -15.150 23.614 40.584 1.00 133.74 ? 568 MET B CG 1 ATOM 11554 S SD . MET B 2 568 ? -15.531 21.982 41.249 1.00 136.65 ? 568 MET B SD 1 ATOM 11555 C CE . MET B 2 568 ? -13.890 21.406 41.674 1.00 126.02 ? 568 MET B CE 1 ATOM 11556 N N . SER B 2 569 ? -15.522 25.448 44.926 1.00 120.94 ? 569 SER B N 1 ATOM 11557 C CA . SER B 2 569 ? -15.052 26.206 46.081 1.00 108.69 ? 569 SER B CA 1 ATOM 11558 C C . SER B 2 569 ? -13.529 26.261 46.138 1.00 111.59 ? 569 SER B C 1 ATOM 11559 O O . SER B 2 569 ? -12.847 25.463 45.495 1.00 119.37 ? 569 SER B O 1 ATOM 11560 C CB . SER B 2 569 ? -15.601 25.602 47.375 1.00 109.05 ? 569 SER B CB 1 ATOM 11561 O OG . SER B 2 569 ? -15.099 26.286 48.510 1.00 106.09 ? 569 SER B OG 1 ATOM 11562 N N . SER B 2 570 ? -13.006 27.215 46.903 1.00 122.68 ? 570 SER B N 1 ATOM 11563 C CA . SER B 2 570 ? -11.564 27.372 47.073 1.00 123.36 ? 570 SER B CA 1 ATOM 11564 C C . SER B 2 570 ? -10.914 26.118 47.658 1.00 112.46 ? 570 SER B C 1 ATOM 11565 O O . SER B 2 570 ? -9.757 25.817 47.366 1.00 99.39 ? 570 SER B O 1 ATOM 11566 C CB . SER B 2 570 ? -11.262 28.576 47.969 1.00 132.17 ? 570 SER B CB 1 ATOM 11567 O OG . SER B 2 570 ? -11.797 29.768 47.421 1.00 129.30 ? 570 SER B OG 1 ATOM 11568 N N . ASN B 2 571 ? -11.664 25.391 48.482 1.00 114.36 ? 571 ASN B N 1 ATOM 11569 C CA . ASN B 2 571 ? -11.166 24.157 49.080 1.00 120.87 ? 571 ASN B CA 1 ATOM 11570 C C . ASN B 2 571 ? -11.054 23.031 48.056 1.00 131.99 ? 571 ASN B C 1 ATOM 11571 O O . ASN B 2 571 ? -10.348 22.046 48.276 1.00 135.79 ? 571 ASN B O 1 ATOM 11572 C CB . ASN B 2 571 ? -12.064 23.728 50.246 1.00 126.63 ? 571 ASN B CB 1 ATOM 11573 C CG . ASN B 2 571 ? -13.531 23.630 49.856 1.00 133.37 ? 571 ASN B CG 1 ATOM 11574 O OD1 . ASN B 2 571 ? -13.873 23.147 48.775 1.00 135.11 ? 571 ASN B OD1 1 ATOM 11575 N ND2 . ASN B 2 571 ? -14.406 24.092 50.741 1.00 129.72 ? 571 ASN B ND2 1 ATOM 11576 N N . GLY B 2 572 ? -11.755 23.185 46.938 1.00 136.53 ? 572 GLY B N 1 ATOM 11577 C CA . GLY B 2 572 ? -11.707 22.212 45.862 1.00 136.39 ? 572 GLY B CA 1 ATOM 11578 C C . GLY B 2 572 ? -12.950 21.349 45.761 1.00 129.18 ? 572 GLY B C 1 ATOM 11579 O O . GLY B 2 572 ? -13.198 20.729 44.728 1.00 140.93 ? 572 GLY B O 1 ATOM 11580 N N . LEU B 2 573 ? -13.732 21.304 46.834 1.00 110.13 ? 573 LEU B N 1 ATOM 11581 C CA . LEU B 2 573 ? -14.965 20.527 46.838 1.00 120.08 ? 573 LEU B CA 1 ATOM 11582 C C . LEU B 2 573 ? -16.104 21.324 46.206 1.00 122.52 ? 573 LEU B C 1 ATOM 11583 O O . LEU B 2 573 ? -16.184 22.541 46.373 1.00 112.20 ? 573 LEU B O 1 ATOM 11584 C CB . LEU B 2 573 ? -15.332 20.107 48.263 1.00 122.94 ? 573 LEU B CB 1 ATOM 11585 C CG . LEU B 2 573 ? -16.463 19.085 48.385 1.00 128.15 ? 573 LEU B CG 1 ATOM 11586 C CD1 . LEU B 2 573 ? -16.132 17.832 47.588 1.00 123.98 ? 573 LEU B CD1 1 ATOM 11587 C CD2 . LEU B 2 573 ? -16.725 18.741 49.842 1.00 121.38 ? 573 LEU B CD2 1 ATOM 11588 N N . LEU B 2 574 ? -16.979 20.636 45.478 1.00 117.60 ? 574 LEU B N 1 ATOM 11589 C CA . LEU B 2 574 ? -18.095 21.291 44.800 1.00 105.10 ? 574 LEU B CA 1 ATOM 11590 C C . LEU B 2 574 ? -19.070 21.919 45.793 1.00 109.77 ? 574 LEU B C 1 ATOM 11591 O O . LEU B 2 574 ? -19.560 21.250 46.703 1.00 128.60 ? 574 LEU B O 1 ATOM 11592 C CB . LEU B 2 574 ? -18.836 20.294 43.909 1.00 116.46 ? 574 LEU B CB 1 ATOM 11593 C CG . LEU B 2 574 ? -19.923 20.867 42.996 1.00 107.35 ? 574 LEU B CG 1 ATOM 11594 C CD1 . LEU B 2 574 ? -19.300 21.596 41.815 1.00 127.61 ? 574 LEU B CD1 1 ATOM 11595 C CD2 . LEU B 2 574 ? -20.866 19.772 42.521 1.00 95.15 ? 574 LEU B CD2 1 ATOM 11596 N N . CYS B 2 575 ? -19.337 23.210 45.604 1.00 97.12 ? 575 CYS B N 1 ATOM 11597 C CA . CYS B 2 575 ? -20.266 23.973 46.441 1.00 89.36 ? 575 CYS B CA 1 ATOM 11598 C C . CYS B 2 575 ? -19.947 23.878 47.932 1.00 85.13 ? 575 CYS B C 1 ATOM 11599 O O . CYS B 2 575 ? -20.848 23.935 48.770 1.00 84.20 ? 575 CYS B O 1 ATOM 11600 C CB . CYS B 2 575 ? -21.706 23.514 46.191 1.00 84.64 ? 575 CYS B CB 1 ATOM 11601 S SG . CYS B 2 575 ? -22.339 23.933 44.550 1.00 118.28 ? 575 CYS B SG 1 ATOM 11602 N N . SER B 2 576 ? -18.662 23.722 48.246 1.00 87.29 ? 576 SER B N 1 ATOM 11603 C CA . SER B 2 576 ? -18.174 23.634 49.622 1.00 99.24 ? 576 SER B CA 1 ATOM 11604 C C . SER B 2 576 ? -18.825 22.480 50.384 1.00 111.30 ? 576 SER B C 1 ATOM 11605 O O . SER B 2 576 ? -18.865 22.483 51.615 1.00 125.99 ? 576 SER B O 1 ATOM 11606 C CB . SER B 2 576 ? -18.418 24.953 50.364 1.00 85.22 ? 576 SER B CB 1 ATOM 11607 O OG . SER B 2 576 ? -17.955 26.058 49.607 1.00 85.49 ? 576 SER B OG 1 ATOM 11608 N N . GLY B 2 577 ? -19.328 21.495 49.646 1.00 106.20 ? 577 GLY B N 1 ATOM 11609 C CA . GLY B 2 577 ? -20.021 20.366 50.240 1.00 98.07 ? 577 GLY B CA 1 ATOM 11610 C C . GLY B 2 577 ? -21.392 20.731 50.782 1.00 87.57 ? 577 GLY B C 1 ATOM 11611 O O . GLY B 2 577 ? -22.147 19.864 51.220 1.00 96.49 ? 577 GLY B O 1 ATOM 11612 N N . ARG B 2 578 ? -21.710 22.022 50.750 1.00 86.26 ? 578 ARG B N 1 ATOM 11613 C CA . ARG B 2 578 ? -22.922 22.541 51.371 1.00 87.18 ? 578 ARG B CA 1 ATOM 11614 C C . ARG B 2 578 ? -24.090 22.711 50.401 1.00 88.41 ? 578 ARG B C 1 ATOM 11615 O O . ARG B 2 578 ? -25.158 23.178 50.794 1.00 88.62 ? 578 ARG B O 1 ATOM 11616 C CB . ARG B 2 578 ? -22.626 23.882 52.051 1.00 86.13 ? 578 ARG B CB 1 ATOM 11617 C CG . ARG B 2 578 ? -21.677 23.788 53.238 1.00 86.12 ? 578 ARG B CG 1 ATOM 11618 C CD . ARG B 2 578 ? -21.811 25.001 54.149 1.00 87.02 ? 578 ARG B CD 1 ATOM 11619 N NE . ARG B 2 578 ? -20.693 25.935 54.028 1.00 87.87 ? 578 ARG B NE 1 ATOM 11620 C CZ . ARG B 2 578 ? -19.707 26.038 54.913 1.00 89.97 ? 578 ARG B CZ 1 ATOM 11621 N NH1 . ARG B 2 578 ? -19.697 25.264 55.990 1.00 104.78 ? 578 ARG B NH1 1 ATOM 11622 N NH2 . ARG B 2 578 ? -18.731 26.917 54.726 1.00 91.22 ? 578 ARG B NH2 1 ATOM 11623 N N . GLY B 2 579 ? -23.895 22.343 49.139 1.00 97.56 ? 579 GLY B N 1 ATOM 11624 C CA . GLY B 2 579 ? -24.944 22.524 48.152 1.00 104.57 ? 579 GLY B CA 1 ATOM 11625 C C . GLY B 2 579 ? -24.768 21.747 46.863 1.00 99.84 ? 579 GLY B C 1 ATOM 11626 O O . GLY B 2 579 ? -23.825 20.970 46.711 1.00 104.57 ? 579 GLY B O 1 ATOM 11627 N N . LYS B 2 580 ? -25.692 21.963 45.932 1.00 99.01 ? 580 LYS B N 1 ATOM 11628 C CA . LYS B 2 580 ? -25.658 21.296 44.637 1.00 108.61 ? 580 LYS B CA 1 ATOM 11629 C C . LYS B 2 580 ? -25.481 22.304 43.509 1.00 105.61 ? 580 LYS B C 1 ATOM 11630 O O . LYS B 2 580 ? -26.057 23.391 43.540 1.00 101.37 ? 580 LYS B O 1 ATOM 11631 C CB . LYS B 2 580 ? -26.934 20.481 44.417 1.00 113.01 ? 580 LYS B CB 1 ATOM 11632 C CG . LYS B 2 580 ? -27.194 19.447 45.495 1.00 122.47 ? 580 LYS B CG 1 ATOM 11633 C CD . LYS B 2 580 ? -26.021 18.493 45.629 1.00 132.62 ? 580 LYS B CD 1 ATOM 11634 C CE . LYS B 2 580 ? -26.237 17.514 46.769 1.00 124.77 ? 580 LYS B CE 1 ATOM 11635 N NZ . LYS B 2 580 ? -25.060 16.622 46.958 1.00 107.54 ? 580 LYS B NZ 1 ATOM 11636 N N . CYS B 2 581 ? -24.685 21.935 42.512 1.00 101.04 ? 581 CYS B N 1 ATOM 11637 C CA . CYS B 2 581 ? -24.403 22.820 41.390 1.00 96.68 ? 581 CYS B CA 1 ATOM 11638 C C . CYS B 2 581 ? -25.400 22.624 40.253 1.00 98.77 ? 581 CYS B C 1 ATOM 11639 O O . CYS B 2 581 ? -25.494 21.540 39.677 1.00 102.09 ? 581 CYS B O 1 ATOM 11640 C CB . CYS B 2 581 ? -22.978 22.593 40.882 1.00 94.70 ? 581 CYS B CB 1 ATOM 11641 S SG . CYS B 2 581 ? -22.517 23.622 39.470 1.00 121.01 ? 581 CYS B SG 1 ATOM 11642 N N . GLU B 2 582 ? -26.143 23.681 39.936 1.00 96.37 ? 582 GLU B N 1 ATOM 11643 C CA . GLU B 2 582 ? -27.133 23.633 38.865 1.00 98.00 ? 582 GLU B CA 1 ATOM 11644 C C . GLU B 2 582 ? -27.044 24.870 37.972 1.00 95.24 ? 582 GLU B C 1 ATOM 11645 O O . GLU B 2 582 ? -27.115 26.001 38.456 1.00 90.62 ? 582 GLU B O 1 ATOM 11646 C CB . GLU B 2 582 ? -28.543 23.495 39.445 1.00 111.69 ? 582 GLU B CB 1 ATOM 11647 C CG . GLU B 2 582 ? -28.804 22.156 40.125 1.00 135.48 ? 582 GLU B CG 1 ATOM 11648 C CD . GLU B 2 582 ? -30.225 22.017 40.638 1.00 148.89 ? 582 GLU B CD 1 ATOM 11649 O OE1 . GLU B 2 582 ? -30.966 23.023 40.633 1.00 140.82 ? 582 GLU B OE1 1 ATOM 11650 O OE2 . GLU B 2 582 ? -30.603 20.898 41.047 1.00 148.92 ? 582 GLU B OE2 1 ATOM 11651 N N . CYS B 2 583 ? -26.887 24.636 36.671 1.00 102.19 ? 583 CYS B N 1 ATOM 11652 C CA . CYS B 2 583 ? -26.748 25.697 35.672 1.00 96.79 ? 583 CYS B CA 1 ATOM 11653 C C . CYS B 2 583 ? -25.583 26.636 35.977 1.00 93.06 ? 583 CYS B C 1 ATOM 11654 O O . CYS B 2 583 ? -25.696 27.853 35.826 1.00 104.75 ? 583 CYS B O 1 ATOM 11655 C CB . CYS B 2 583 ? -28.048 26.498 35.551 1.00 93.66 ? 583 CYS B CB 1 ATOM 11656 S SG . CYS B 2 583 ? -29.387 25.618 34.716 1.00 112.95 ? 583 CYS B SG 1 ATOM 11657 N N . GLY B 2 584 ? -24.464 26.061 36.405 1.00 92.86 ? 584 GLY B N 1 ATOM 11658 C CA . GLY B 2 584 ? -23.256 26.825 36.652 1.00 86.92 ? 584 GLY B CA 1 ATOM 11659 C C . GLY B 2 584 ? -23.295 27.686 37.899 1.00 84.73 ? 584 GLY B C 1 ATOM 11660 O O . GLY B 2 584 ? -22.417 28.523 38.109 1.00 92.96 ? 584 GLY B O 1 ATOM 11661 N N . SER B 2 585 ? -24.312 27.485 38.732 1.00 84.43 ? 585 SER B N 1 ATOM 11662 C CA . SER B 2 585 ? -24.448 28.251 39.966 1.00 81.20 ? 585 SER B CA 1 ATOM 11663 C C . SER B 2 585 ? -24.890 27.359 41.120 1.00 81.73 ? 585 SER B C 1 ATOM 11664 O O . SER B 2 585 ? -25.863 26.615 41.001 1.00 87.63 ? 585 SER B O 1 ATOM 11665 C CB . SER B 2 585 ? -25.440 29.401 39.778 1.00 80.76 ? 585 SER B CB 1 ATOM 11666 O OG . SER B 2 585 ? -24.981 30.319 38.802 1.00 96.77 ? 585 SER B OG 1 ATOM 11667 N N . CYS B 2 586 ? -24.172 27.437 42.236 1.00 80.55 ? 586 CYS B N 1 ATOM 11668 C CA . CYS B 2 586 ? -24.493 26.631 43.408 1.00 82.04 ? 586 CYS B CA 1 ATOM 11669 C C . CYS B 2 586 ? -25.814 27.050 44.040 1.00 84.34 ? 586 CYS B C 1 ATOM 11670 O O . CYS B 2 586 ? -26.074 28.237 44.234 1.00 80.09 ? 586 CYS B O 1 ATOM 11671 C CB . CYS B 2 586 ? -23.379 26.722 44.454 1.00 80.39 ? 586 CYS B CB 1 ATOM 11672 S SG . CYS B 2 586 ? -21.863 25.841 44.037 1.00 142.46 ? 586 CYS B SG 1 ATOM 11673 N N . VAL B 2 587 ? -26.646 26.062 44.351 1.00 84.36 ? 587 VAL B N 1 ATOM 11674 C CA . VAL B 2 587 ? -27.857 26.293 45.124 1.00 84.47 ? 587 VAL B CA 1 ATOM 11675 C C . VAL B 2 587 ? -27.663 25.676 46.504 1.00 88.98 ? 587 VAL B C 1 ATOM 11676 O O . VAL B 2 587 ? -27.607 24.456 46.643 1.00 96.55 ? 587 VAL B O 1 ATOM 11677 C CB . VAL B 2 587 ? -29.098 25.696 44.439 1.00 85.91 ? 587 VAL B CB 1 ATOM 11678 C CG1 . VAL B 2 587 ? -30.350 26.015 45.237 1.00 85.22 ? 587 VAL B CG1 1 ATOM 11679 C CG2 . VAL B 2 587 ? -29.220 26.226 43.019 1.00 88.18 ? 587 VAL B CG2 1 ATOM 11680 N N . CYS B 2 588 ? -27.556 26.526 47.520 1.00 92.61 ? 588 CYS B N 1 ATOM 11681 C CA . CYS B 2 588 ? -27.161 26.081 48.852 1.00 104.34 ? 588 CYS B CA 1 ATOM 11682 C C . CYS B 2 588 ? -28.284 25.388 49.619 1.00 118.71 ? 588 CYS B C 1 ATOM 11683 O O . CYS B 2 588 ? -29.379 25.932 49.763 1.00 121.19 ? 588 CYS B O 1 ATOM 11684 C CB . CYS B 2 588 ? -26.647 27.268 49.672 1.00 86.31 ? 588 CYS B CB 1 ATOM 11685 S SG . CYS B 2 588 ? -25.256 28.153 48.929 1.00 157.36 ? 588 CYS B SG 1 ATOM 11686 N N . ILE B 2 589 ? -28.002 24.183 50.107 1.00 104.87 ? 589 ILE B N 1 ATOM 11687 C CA . ILE B 2 589 ? -28.890 23.507 51.046 1.00 102.41 ? 589 ILE B CA 1 ATOM 11688 C C . ILE B 2 589 ? -28.099 23.081 52.285 1.00 113.17 ? 589 ILE B C 1 ATOM 11689 O O . ILE B 2 589 ? -27.273 22.170 52.229 1.00 123.79 ? 589 ILE B O 1 ATOM 11690 C CB . ILE B 2 589 ? -29.590 22.277 50.409 1.00 104.02 ? 589 ILE B CB 1 ATOM 11691 C CG1 . ILE B 2 589 ? -28.605 21.435 49.586 1.00 99.32 ? 589 ILE B CG1 1 ATOM 11692 C CG2 . ILE B 2 589 ? -30.768 22.722 49.550 1.00 104.14 ? 589 ILE B CG2 1 ATOM 11693 C CD1 . ILE B 2 589 ? -28.591 21.740 48.098 1.00 107.27 ? 589 ILE B CD1 1 ATOM 11694 N N . GLN B 2 590 ? -28.397 23.734 53.405 1.00 113.82 ? 590 GLN B N 1 ATOM 11695 C CA . GLN B 2 590 ? -27.631 23.620 54.647 1.00 110.78 ? 590 GLN B CA 1 ATOM 11696 C C . GLN B 2 590 ? -28.282 24.530 55.690 1.00 115.87 ? 590 GLN B C 1 ATOM 11697 O O . GLN B 2 590 ? -29.157 25.326 55.348 1.00 109.38 ? 590 GLN B O 1 ATOM 11698 C CB . GLN B 2 590 ? -26.159 24.006 54.425 1.00 94.61 ? 590 GLN B CB 1 ATOM 11699 C CG . GLN B 2 590 ? -25.184 22.829 54.397 1.00 100.99 ? 590 GLN B CG 1 ATOM 11700 C CD . GLN B 2 590 ? -24.466 22.617 55.718 1.00 125.20 ? 590 GLN B CD 1 ATOM 11701 O OE1 . GLN B 2 590 ? -23.786 23.513 56.219 1.00 112.80 ? 590 GLN B OE1 1 ATOM 11702 N NE2 . GLN B 2 590 ? -24.619 21.429 56.292 1.00 148.55 ? 590 GLN B NE2 1 ATOM 11703 N N . PRO B 2 591 ? -27.868 24.423 56.964 1.00 129.01 ? 591 PRO B N 1 ATOM 11704 C CA . PRO B 2 591 ? -28.423 25.344 57.963 1.00 135.05 ? 591 PRO B CA 1 ATOM 11705 C C . PRO B 2 591 ? -27.965 26.791 57.771 1.00 122.26 ? 591 PRO B C 1 ATOM 11706 O O . PRO B 2 591 ? -27.065 27.257 58.470 1.00 133.53 ? 591 PRO B O 1 ATOM 11707 C CB . PRO B 2 591 ? -27.900 24.780 59.293 1.00 149.01 ? 591 PRO B CB 1 ATOM 11708 C CG . PRO B 2 591 ? -26.748 23.906 58.922 1.00 141.98 ? 591 PRO B CG 1 ATOM 11709 C CD . PRO B 2 591 ? -27.123 23.324 57.600 1.00 131.74 ? 591 PRO B CD 1 ATOM 11710 N N . GLY B 2 592 ? -28.588 27.486 56.823 1.00 110.07 ? 592 GLY B N 1 ATOM 11711 C CA . GLY B 2 592 ? -28.323 28.895 56.597 1.00 120.04 ? 592 GLY B CA 1 ATOM 11712 C C . GLY B 2 592 ? -26.957 29.228 56.029 1.00 109.53 ? 592 GLY B C 1 ATOM 11713 O O . GLY B 2 592 ? -26.204 30.005 56.616 1.00 107.95 ? 592 GLY B O 1 ATOM 11714 N N . SER B 2 593 ? -26.633 28.641 54.882 1.00 95.12 ? 593 SER B N 1 ATOM 11715 C CA . SER B 2 593 ? -25.387 28.956 54.193 1.00 88.39 ? 593 SER B CA 1 ATOM 11716 C C . SER B 2 593 ? -25.663 29.707 52.892 1.00 86.68 ? 593 SER B C 1 ATOM 11717 O O . SER B 2 593 ? -26.712 29.527 52.273 1.00 93.84 ? 593 SER B O 1 ATOM 11718 C CB . SER B 2 593 ? -24.588 27.683 53.909 1.00 96.26 ? 593 SER B CB 1 ATOM 11719 O OG . SER B 2 593 ? -25.306 26.810 53.056 1.00 99.66 ? 593 SER B OG 1 ATOM 11720 N N . TYR B 2 594 ? -24.721 30.551 52.485 1.00 86.49 ? 594 TYR B N 1 ATOM 11721 C CA . TYR B 2 594 ? -24.877 31.330 51.263 1.00 85.99 ? 594 TYR B CA 1 ATOM 11722 C C . TYR B 2 594 ? -23.534 31.630 50.603 1.00 87.09 ? 594 TYR B C 1 ATOM 11723 O O . TYR B 2 594 ? -22.488 31.160 51.054 1.00 88.29 ? 594 TYR B O 1 ATOM 11724 C CB . TYR B 2 594 ? -25.625 32.634 51.553 1.00 86.21 ? 594 TYR B CB 1 ATOM 11725 C CG . TYR B 2 594 ? -25.010 33.470 52.650 1.00 87.64 ? 594 TYR B CG 1 ATOM 11726 C CD1 . TYR B 2 594 ? -24.067 34.446 52.360 1.00 89.73 ? 594 TYR B CD1 1 ATOM 11727 C CD2 . TYR B 2 594 ? -25.372 33.284 53.977 1.00 87.23 ? 594 TYR B CD2 1 ATOM 11728 C CE1 . TYR B 2 594 ? -23.502 35.212 53.360 1.00 90.36 ? 594 TYR B CE1 1 ATOM 11729 C CE2 . TYR B 2 594 ? -24.812 34.044 54.982 1.00 87.77 ? 594 TYR B CE2 1 ATOM 11730 C CZ . TYR B 2 594 ? -23.878 35.007 54.669 1.00 89.12 ? 594 TYR B CZ 1 ATOM 11731 O OH . TYR B 2 594 ? -23.317 35.769 55.667 1.00 89.12 ? 594 TYR B OH 1 ATOM 11732 N N . GLY B 2 595 ? -23.572 32.420 49.536 1.00 86.58 ? 595 GLY B N 1 ATOM 11733 C CA . GLY B 2 595 ? -22.386 32.711 48.752 1.00 87.31 ? 595 GLY B CA 1 ATOM 11734 C C . GLY B 2 595 ? -22.422 31.991 47.418 1.00 86.39 ? 595 GLY B C 1 ATOM 11735 O O . GLY B 2 595 ? -23.245 31.098 47.213 1.00 96.19 ? 595 GLY B O 1 ATOM 11736 N N . ASP B 2 596 ? -21.532 32.382 46.510 1.00 84.87 ? 596 ASP B N 1 ATOM 11737 C CA . ASP B 2 596 ? -21.461 31.776 45.183 1.00 82.18 ? 596 ASP B CA 1 ATOM 11738 C C . ASP B 2 596 ? -21.141 30.286 45.260 1.00 87.97 ? 596 ASP B C 1 ATOM 11739 O O . ASP B 2 596 ? -21.844 29.461 44.682 1.00 118.05 ? 596 ASP B O 1 ATOM 11740 C CB . ASP B 2 596 ? -20.414 32.488 44.323 1.00 99.37 ? 596 ASP B CB 1 ATOM 11741 C CG . ASP B 2 596 ? -20.742 33.949 44.092 1.00 107.39 ? 596 ASP B CG 1 ATOM 11742 O OD1 . ASP B 2 596 ? -21.934 34.314 44.162 1.00 118.70 ? 596 ASP B OD1 1 ATOM 11743 O OD2 . ASP B 2 596 ? -19.804 34.735 43.835 1.00 100.98 ? 596 ASP B OD2 1 ATOM 11744 N N . THR B 2 597 ? -20.068 29.954 45.970 1.00 91.01 ? 597 THR B N 1 ATOM 11745 C CA . THR B 2 597 ? -19.658 28.566 46.158 1.00 86.42 ? 597 THR B CA 1 ATOM 11746 C C . THR B 2 597 ? -20.199 27.987 47.463 1.00 91.90 ? 597 THR B C 1 ATOM 11747 O O . THR B 2 597 ? -19.822 26.883 47.856 1.00 113.57 ? 597 THR B O 1 ATOM 11748 C CB . THR B 2 597 ? -18.126 28.421 46.142 1.00 88.38 ? 597 THR B CB 1 ATOM 11749 O OG1 . THR B 2 597 ? -17.554 29.245 47.165 1.00 119.67 ? 597 THR B OG1 1 ATOM 11750 C CG2 . THR B 2 597 ? -17.568 28.835 44.791 1.00 95.65 ? 597 THR B CG2 1 ATOM 11751 N N . CYS B 2 598 ? -21.050 28.759 48.138 1.00 83.09 ? 598 CYS B N 1 ATOM 11752 C CA . CYS B 2 598 ? -21.603 28.402 49.447 1.00 84.10 ? 598 CYS B CA 1 ATOM 11753 C C . CYS B 2 598 ? -20.496 28.323 50.492 1.00 86.12 ? 598 CYS B C 1 ATOM 11754 O O . CYS B 2 598 ? -20.527 27.476 51.386 1.00 86.39 ? 598 CYS B O 1 ATOM 11755 C CB . CYS B 2 598 ? -22.375 27.079 49.386 1.00 82.99 ? 598 CYS B CB 1 ATOM 11756 S SG . CYS B 2 598 ? -23.720 27.053 48.183 1.00 113.65 ? 598 CYS B SG 1 ATOM 11757 N N . GLU B 2 599 ? -19.521 29.217 50.368 1.00 88.04 ? 599 GLU B N 1 ATOM 11758 C CA . GLU B 2 599 ? -18.393 29.273 51.290 1.00 90.55 ? 599 GLU B CA 1 ATOM 11759 C C . GLU B 2 599 ? -18.762 29.971 52.596 1.00 92.17 ? 599 GLU B C 1 ATOM 11760 O O . GLU B 2 599 ? -18.124 29.753 53.626 1.00 94.97 ? 599 GLU B O 1 ATOM 11761 C CB . GLU B 2 599 ? -17.204 29.984 50.634 1.00 92.46 ? 599 GLU B CB 1 ATOM 11762 C CG . GLU B 2 599 ? -17.401 31.480 50.393 1.00 94.70 ? 599 GLU B CG 1 ATOM 11763 C CD . GLU B 2 599 ? -18.322 31.783 49.224 1.00 97.82 ? 599 GLU B CD 1 ATOM 11764 O OE1 . GLU B 2 599 ? -18.642 32.972 49.009 1.00 96.01 ? 599 GLU B OE1 1 ATOM 11765 O OE2 . GLU B 2 599 ? -18.724 30.836 48.515 1.00 111.16 ? 599 GLU B OE2 1 ATOM 11766 N N . LYS B 2 600 ? -19.795 30.807 52.551 1.00 92.07 ? 600 LYS B N 1 ATOM 11767 C CA . LYS B 2 600 ? -20.196 31.592 53.714 1.00 93.16 ? 600 LYS B CA 1 ATOM 11768 C C . LYS B 2 600 ? -21.299 30.919 54.525 1.00 91.68 ? 600 LYS B C 1 ATOM 11769 O O . LYS B 2 600 ? -22.422 30.751 54.049 1.00 89.72 ? 600 LYS B O 1 ATOM 11770 C CB . LYS B 2 600 ? -20.660 32.985 53.283 1.00 93.65 ? 600 LYS B CB 1 ATOM 11771 C CG . LYS B 2 600 ? -19.575 33.836 52.650 1.00 95.40 ? 600 LYS B CG 1 ATOM 11772 C CD . LYS B 2 600 ? -20.092 35.224 52.315 1.00 106.49 ? 600 LYS B CD 1 ATOM 11773 C CE . LYS B 2 600 ? -18.988 36.093 51.736 1.00 120.70 ? 600 LYS B CE 1 ATOM 11774 N NZ . LYS B 2 600 ? -19.465 37.466 51.419 1.00 123.28 ? 600 LYS B NZ 1 ATOM 11775 N N . CYS B 2 601 ? -20.968 30.534 55.752 1.00 91.96 ? 601 CYS B N 1 ATOM 11776 C CA . CYS B 2 601 ? -21.955 29.997 56.682 1.00 89.89 ? 601 CYS B CA 1 ATOM 11777 C C . CYS B 2 601 ? -21.665 30.477 58.105 1.00 93.97 ? 601 CYS B C 1 ATOM 11778 O O . CYS B 2 601 ? -21.103 29.731 58.909 1.00 99.58 ? 601 CYS B O 1 ATOM 11779 C CB . CYS B 2 601 ? -21.975 28.469 56.626 1.00 89.47 ? 601 CYS B CB 1 ATOM 11780 S SG . CYS B 2 601 ? -23.356 27.712 57.506 1.00 101.28 ? 601 CYS B SG 1 ATOM 11781 N N . PRO B 2 602 ? -22.040 31.731 58.413 1.00 89.27 ? 602 PRO B N 1 ATOM 11782 C CA . PRO B 2 602 ? -21.768 32.361 59.710 1.00 88.09 ? 602 PRO B CA 1 ATOM 11783 C C . PRO B 2 602 ? -22.285 31.543 60.885 1.00 87.27 ? 602 PRO B C 1 ATOM 11784 O O . PRO B 2 602 ? -21.568 31.375 61.872 1.00 88.42 ? 602 PRO B O 1 ATOM 11785 C CB . PRO B 2 602 ? -22.510 33.696 59.615 1.00 87.71 ? 602 PRO B CB 1 ATOM 11786 C CG . PRO B 2 602 ? -22.593 33.975 58.165 1.00 94.54 ? 602 PRO B CG 1 ATOM 11787 C CD . PRO B 2 602 ? -22.768 32.638 57.510 1.00 98.90 ? 602 PRO B CD 1 ATOM 11788 N N . THR B 2 603 ? -23.512 31.043 60.784 1.00 94.58 ? 603 THR B N 1 ATOM 11789 C CA . THR B 2 603 ? -24.034 30.160 61.814 1.00 86.31 ? 603 THR B CA 1 ATOM 11790 C C . THR B 2 603 ? -24.030 28.724 61.309 1.00 103.78 ? 603 THR B C 1 ATOM 11791 O O . THR B 2 603 ? -24.857 28.337 60.484 1.00 144.05 ? 603 THR B O 1 ATOM 11792 C CB . THR B 2 603 ? -25.462 30.553 62.236 1.00 88.79 ? 603 THR B CB 1 ATOM 11793 O OG1 . THR B 2 603 ? -26.379 30.248 61.179 1.00 86.99 ? 603 THR B OG1 1 ATOM 11794 C CG2 . THR B 2 603 ? -25.535 32.038 62.559 1.00 106.75 ? 603 THR B CG2 1 ATOM 11795 N N . CYS B 2 604 ? -23.082 27.944 61.816 1.00 103.63 ? 604 CYS B N 1 ATOM 11796 C CA . CYS B 2 604 ? -22.965 26.529 61.497 1.00 98.00 ? 604 CYS B CA 1 ATOM 11797 C C . CYS B 2 604 ? -22.372 25.799 62.691 1.00 95.78 ? 604 CYS B C 1 ATOM 11798 O O . CYS B 2 604 ? -21.708 26.421 63.521 1.00 98.41 ? 604 CYS B O 1 ATOM 11799 C CB . CYS B 2 604 ? -22.100 26.314 60.252 1.00 98.66 ? 604 CYS B CB 1 ATOM 11800 S SG . CYS B 2 604 ? -23.032 26.116 58.719 1.00 185.75 ? 604 CYS B SG 1 ATOM 11801 N N . PRO B 2 605 ? -22.620 24.483 62.794 1.00 88.76 ? 605 PRO B N 1 ATOM 11802 C CA . PRO B 2 605 ? -21.893 23.702 63.799 1.00 87.60 ? 605 PRO B CA 1 ATOM 11803 C C . PRO B 2 605 ? -20.392 23.888 63.602 1.00 89.72 ? 605 PRO B C 1 ATOM 11804 O O . PRO B 2 605 ? -19.897 23.711 62.489 1.00 103.14 ? 605 PRO B O 1 ATOM 11805 C CB . PRO B 2 605 ? -22.325 22.265 63.510 1.00 121.40 ? 605 PRO B CB 1 ATOM 11806 C CG . PRO B 2 605 ? -23.671 22.404 62.877 1.00 109.05 ? 605 PRO B CG 1 ATOM 11807 C CD . PRO B 2 605 ? -23.618 23.673 62.074 1.00 96.59 ? 605 PRO B CD 1 ATOM 11808 N N . ASP B 2 606 ? -19.681 24.240 64.667 1.00 90.31 ? 606 ASP B N 1 ATOM 11809 C CA . ASP B 2 606 ? -18.304 24.696 64.530 1.00 107.87 ? 606 ASP B CA 1 ATOM 11810 C C . ASP B 2 606 ? -17.280 23.602 64.791 1.00 122.03 ? 606 ASP B C 1 ATOM 11811 O O . ASP B 2 606 ? -17.481 22.749 65.656 1.00 136.45 ? 606 ASP B O 1 ATOM 11812 C CB . ASP B 2 606 ? -18.038 25.868 65.480 1.00 123.95 ? 606 ASP B CB 1 ATOM 11813 C CG . ASP B 2 606 ? -17.875 25.426 66.924 1.00 145.36 ? 606 ASP B CG 1 ATOM 11814 O OD1 . ASP B 2 606 ? -16.898 25.857 67.573 1.00 158.16 ? 606 ASP B OD1 1 ATOM 11815 O OD2 . ASP B 2 606 ? -18.721 24.645 67.411 1.00 143.51 ? 606 ASP B OD2 1 ATOM 11816 N N . ALA B 2 607 ? -16.196 23.629 64.016 1.00 117.35 ? 607 ALA B N 1 ATOM 11817 C CA . ALA B 2 607 ? -14.972 22.914 64.362 1.00 118.61 ? 607 ALA B CA 1 ATOM 11818 C C . ALA B 2 607 ? -15.200 21.442 64.683 1.00 106.70 ? 607 ALA B C 1 ATOM 11819 O O . ALA B 2 607 ? -15.561 20.645 63.814 1.00 95.12 ? 607 ALA B O 1 ATOM 11820 C CB . ALA B 2 607 ? -14.282 23.603 65.533 1.00 117.78 ? 607 ALA B CB 1 ATOM 11821 N N . CYS B 2 608 ? -14.966 21.108 65.949 1.00 95.66 ? 608 CYS B N 1 ATOM 11822 C CA . CYS B 2 608 ? -15.005 19.743 66.458 1.00 126.26 ? 608 CYS B CA 1 ATOM 11823 C C . CYS B 2 608 ? -16.220 18.936 66.008 1.00 116.93 ? 608 CYS B C 1 ATOM 11824 O O . CYS B 2 608 ? -16.092 17.756 65.702 1.00 142.72 ? 608 CYS B O 1 ATOM 11825 C CB . CYS B 2 608 ? -14.957 19.767 67.989 1.00 141.78 ? 608 CYS B CB 1 ATOM 11826 S SG . CYS B 2 608 ? -14.844 21.427 68.704 1.00 169.60 ? 608 CYS B SG 1 ATOM 11827 N N . THR B 2 609 ? -17.388 19.573 65.968 1.00 90.05 ? 609 THR B N 1 ATOM 11828 C CA . THR B 2 609 ? -18.626 18.897 65.581 1.00 94.55 ? 609 THR B CA 1 ATOM 11829 C C . THR B 2 609 ? -18.503 18.189 64.232 1.00 94.95 ? 609 THR B C 1 ATOM 11830 O O . THR B 2 609 ? -19.019 17.086 64.050 1.00 94.42 ? 609 THR B O 1 ATOM 11831 C CB . THR B 2 609 ? -19.804 19.885 65.510 1.00 90.42 ? 609 THR B CB 1 ATOM 11832 O OG1 . THR B 2 609 ? -19.520 20.895 64.534 1.00 111.93 ? 609 THR B OG1 1 ATOM 11833 C CG2 . THR B 2 609 ? -20.035 20.543 66.865 1.00 86.32 ? 609 THR B CG2 1 ATOM 11834 N N . PHE B 2 610 ? -17.817 18.831 63.292 1.00 100.89 ? 610 PHE B N 1 ATOM 11835 C CA . PHE B 2 610 ? -17.572 18.237 61.983 1.00 106.78 ? 610 PHE B CA 1 ATOM 11836 C C . PHE B 2 610 ? -16.425 17.233 62.025 1.00 106.45 ? 610 PHE B C 1 ATOM 11837 O O . PHE B 2 610 ? -16.431 16.241 61.298 1.00 89.43 ? 610 PHE B O 1 ATOM 11838 C CB . PHE B 2 610 ? -17.275 19.325 60.948 1.00 124.43 ? 610 PHE B CB 1 ATOM 11839 C CG . PHE B 2 610 ? -18.491 19.809 60.210 1.00 128.03 ? 610 PHE B CG 1 ATOM 11840 C CD1 . PHE B 2 610 ? -19.263 20.843 60.715 1.00 127.14 ? 610 PHE B CD1 1 ATOM 11841 C CD2 . PHE B 2 610 ? -18.861 19.230 59.008 1.00 126.34 ? 610 PHE B CD2 1 ATOM 11842 C CE1 . PHE B 2 610 ? -20.382 21.288 60.034 1.00 127.97 ? 610 PHE B CE1 1 ATOM 11843 C CE2 . PHE B 2 610 ? -19.976 19.671 58.323 1.00 134.10 ? 610 PHE B CE2 1 ATOM 11844 C CZ . PHE B 2 610 ? -20.738 20.701 58.836 1.00 134.52 ? 610 PHE B CZ 1 ATOM 11845 N N . LYS B 2 611 ? -15.440 17.494 62.878 1.00 113.00 ? 611 LYS B N 1 ATOM 11846 C CA . LYS B 2 611 ? -14.268 16.631 62.964 1.00 94.58 ? 611 LYS B CA 1 ATOM 11847 C C . LYS B 2 611 ? -14.427 15.569 64.048 1.00 91.53 ? 611 LYS B C 1 ATOM 11848 O O . LYS B 2 611 ? -13.544 14.735 64.244 1.00 92.99 ? 611 LYS B O 1 ATOM 11849 C CB . LYS B 2 611 ? -13.010 17.463 63.216 1.00 93.04 ? 611 LYS B CB 1 ATOM 11850 C CG . LYS B 2 611 ? -12.718 18.471 62.114 1.00 106.28 ? 611 LYS B CG 1 ATOM 11851 C CD . LYS B 2 611 ? -11.405 19.198 62.347 1.00 110.35 ? 611 LYS B CD 1 ATOM 11852 C CE . LYS B 2 611 ? -11.123 20.185 61.226 1.00 108.45 ? 611 LYS B CE 1 ATOM 11853 N NZ . LYS B 2 611 ? -11.066 19.514 59.897 1.00 97.07 ? 611 LYS B NZ 1 ATOM 11854 N N . LYS B 2 612 ? -15.555 15.605 64.750 1.00 101.83 ? 612 LYS B N 1 ATOM 11855 C CA . LYS B 2 612 ? -15.875 14.584 65.743 1.00 87.99 ? 612 LYS B CA 1 ATOM 11856 C C . LYS B 2 612 ? -16.115 13.246 65.060 1.00 87.12 ? 612 LYS B C 1 ATOM 11857 O O . LYS B 2 612 ? -15.663 12.203 65.530 1.00 86.90 ? 612 LYS B O 1 ATOM 11858 C CB . LYS B 2 612 ? -17.104 14.994 66.557 1.00 89.38 ? 612 LYS B CB 1 ATOM 11859 C CG . LYS B 2 612 ? -17.660 13.910 67.461 1.00 104.64 ? 612 LYS B CG 1 ATOM 11860 C CD . LYS B 2 612 ? -18.850 14.430 68.250 1.00 121.23 ? 612 LYS B CD 1 ATOM 11861 C CE . LYS B 2 612 ? -19.892 15.047 67.331 1.00 123.77 ? 612 LYS B CE 1 ATOM 11862 N NZ . LYS B 2 612 ? -20.989 15.702 68.096 1.00 117.74 ? 612 LYS B NZ 1 ATOM 11863 N N . GLU B 2 613 ? -16.829 13.293 63.940 1.00 87.29 ? 613 GLU B N 1 ATOM 11864 C CA . GLU B 2 613 ? -17.112 12.104 63.149 1.00 89.80 ? 613 GLU B CA 1 ATOM 11865 C C . GLU B 2 613 ? -15.835 11.516 62.560 1.00 95.02 ? 613 GLU B C 1 ATOM 11866 O O . GLU B 2 613 ? -15.745 10.310 62.327 1.00 108.66 ? 613 GLU B O 1 ATOM 11867 C CB . GLU B 2 613 ? -18.105 12.435 62.032 1.00 107.05 ? 613 GLU B CB 1 ATOM 11868 C CG . GLU B 2 613 ? -19.443 12.955 62.529 1.00 129.41 ? 613 GLU B CG 1 ATOM 11869 C CD . GLU B 2 613 ? -20.227 11.909 63.298 1.00 151.64 ? 613 GLU B CD 1 ATOM 11870 O OE1 . GLU B 2 613 ? -20.033 10.703 63.030 1.00 150.75 ? 613 GLU B OE1 1 ATOM 11871 O OE2 . GLU B 2 613 ? -21.034 12.290 64.171 1.00 163.48 ? 613 GLU B OE2 1 ATOM 11872 N N . CYS B 2 614 ? -14.849 12.376 62.323 1.00 103.56 ? 614 CYS B N 1 ATOM 11873 C CA . CYS B 2 614 ? -13.580 11.945 61.751 1.00 100.03 ? 614 CYS B CA 1 ATOM 11874 C C . CYS B 2 614 ? -12.750 11.136 62.742 1.00 89.47 ? 614 CYS B C 1 ATOM 11875 O O . CYS B 2 614 ? -12.164 10.119 62.378 1.00 96.93 ? 614 CYS B O 1 ATOM 11876 C CB . CYS B 2 614 ? -12.775 13.151 61.260 1.00 87.06 ? 614 CYS B CB 1 ATOM 11877 S SG . CYS B 2 614 ? -13.288 13.788 59.647 1.00 181.61 ? 614 CYS B SG 1 ATOM 11878 N N . VAL B 2 615 ? -12.697 11.586 63.992 1.00 87.04 ? 615 VAL B N 1 ATOM 11879 C CA . VAL B 2 615 ? -11.924 10.881 65.009 1.00 86.84 ? 615 VAL B CA 1 ATOM 11880 C C . VAL B 2 615 ? -12.677 9.656 65.515 1.00 87.93 ? 615 VAL B C 1 ATOM 11881 O O . VAL B 2 615 ? -12.090 8.765 66.125 1.00 120.14 ? 615 VAL B O 1 ATOM 11882 C CB . VAL B 2 615 ? -11.578 11.791 66.210 1.00 88.36 ? 615 VAL B CB 1 ATOM 11883 C CG1 . VAL B 2 615 ? -10.907 13.070 65.734 1.00 88.72 ? 615 VAL B CG1 1 ATOM 11884 C CG2 . VAL B 2 615 ? -12.822 12.106 67.024 1.00 95.63 ? 615 VAL B CG2 1 ATOM 11885 N N . GLU B 2 616 ? -13.981 9.618 65.260 1.00 86.45 ? 616 GLU B N 1 ATOM 11886 C CA . GLU B 2 616 ? -14.810 8.509 65.715 1.00 86.74 ? 616 GLU B CA 1 ATOM 11887 C C . GLU B 2 616 ? -14.686 7.298 64.793 1.00 87.12 ? 616 GLU B C 1 ATOM 11888 O O . GLU B 2 616 ? -14.598 6.161 65.256 1.00 97.39 ? 616 GLU B O 1 ATOM 11889 C CB . GLU B 2 616 ? -16.272 8.948 65.819 1.00 87.39 ? 616 GLU B CB 1 ATOM 11890 C CG . GLU B 2 616 ? -17.028 8.327 66.983 1.00 96.81 ? 616 GLU B CG 1 ATOM 11891 C CD . GLU B 2 616 ? -16.459 8.725 68.335 1.00 110.28 ? 616 GLU B CD 1 ATOM 11892 O OE1 . GLU B 2 616 ? -16.678 7.982 69.315 1.00 122.12 ? 616 GLU B OE1 1 ATOM 11893 O OE2 . GLU B 2 616 ? -15.799 9.782 68.422 1.00 94.24 ? 616 GLU B OE2 1 ATOM 11894 N N . CYS B 2 617 ? -14.678 7.549 63.488 1.00 87.53 ? 617 CYS B N 1 ATOM 11895 C CA . CYS B 2 617 ? -14.563 6.479 62.502 1.00 90.91 ? 617 CYS B CA 1 ATOM 11896 C C . CYS B 2 617 ? -13.118 6.014 62.335 1.00 88.08 ? 617 CYS B C 1 ATOM 11897 O O . CYS B 2 617 ? -12.858 4.832 62.114 1.00 91.91 ? 617 CYS B O 1 ATOM 11898 C CB . CYS B 2 617 ? -15.122 6.932 61.153 1.00 92.42 ? 617 CYS B CB 1 ATOM 11899 S SG . CYS B 2 617 ? -14.103 8.150 60.291 1.00 129.76 ? 617 CYS B SG 1 ATOM 11900 N N . LYS B 2 618 ? -12.184 6.954 62.437 1.00 87.31 ? 618 LYS B N 1 ATOM 11901 C CA . LYS B 2 618 ? -10.765 6.649 62.287 1.00 87.79 ? 618 LYS B CA 1 ATOM 11902 C C . LYS B 2 618 ? -10.188 5.997 63.537 1.00 89.56 ? 618 LYS B C 1 ATOM 11903 O O . LYS B 2 618 ? -9.787 4.834 63.512 1.00 114.35 ? 618 LYS B O 1 ATOM 11904 C CB . LYS B 2 618 ? -9.976 7.919 61.958 1.00 88.37 ? 618 LYS B CB 1 ATOM 11905 C CG . LYS B 2 618 ? -10.012 8.327 60.495 1.00 88.87 ? 618 LYS B CG 1 ATOM 11906 C CD . LYS B 2 618 ? -9.152 7.403 59.653 1.00 107.76 ? 618 LYS B CD 1 ATOM 11907 C CE . LYS B 2 618 ? -9.044 7.894 58.221 1.00 124.58 ? 618 LYS B CE 1 ATOM 11908 N NZ . LYS B 2 618 ? -8.113 7.051 57.421 1.00 122.51 ? 618 LYS B NZ 1 ATOM 11909 N N . LYS B 2 619 ? -10.149 6.755 64.629 1.00 87.27 ? 619 LYS B N 1 ATOM 11910 C CA . LYS B 2 619 ? -9.514 6.296 65.861 1.00 87.84 ? 619 LYS B CA 1 ATOM 11911 C C . LYS B 2 619 ? -10.355 5.281 66.631 1.00 96.99 ? 619 LYS B C 1 ATOM 11912 O O . LYS B 2 619 ? -9.831 4.274 67.100 1.00 123.91 ? 619 LYS B O 1 ATOM 11913 C CB . LYS B 2 619 ? -9.189 7.488 66.765 1.00 88.00 ? 619 LYS B CB 1 ATOM 11914 C CG . LYS B 2 619 ? -7.884 8.192 66.418 1.00 94.74 ? 619 LYS B CG 1 ATOM 11915 C CD . LYS B 2 619 ? -6.691 7.283 66.678 1.00 106.38 ? 619 LYS B CD 1 ATOM 11916 C CE . LYS B 2 619 ? -5.381 7.918 66.233 1.00 99.11 ? 619 LYS B CE 1 ATOM 11917 N NZ . LYS B 2 619 ? -5.243 7.945 64.750 1.00 105.49 ? 619 LYS B NZ 1 ATOM 11918 N N . PHE B 2 620 ? -11.647 5.548 66.784 1.00 86.47 ? 620 PHE B N 1 ATOM 11919 C CA . PHE B 2 620 ? -12.502 4.650 67.555 1.00 86.27 ? 620 PHE B CA 1 ATOM 11920 C C . PHE B 2 620 ? -13.294 3.659 66.704 1.00 87.35 ? 620 PHE B C 1 ATOM 11921 O O . PHE B 2 620 ? -14.008 2.816 67.249 1.00 87.97 ? 620 PHE B O 1 ATOM 11922 C CB . PHE B 2 620 ? -13.460 5.460 68.429 1.00 86.12 ? 620 PHE B CB 1 ATOM 11923 C CG . PHE B 2 620 ? -12.800 6.079 69.625 1.00 85.78 ? 620 PHE B CG 1 ATOM 11924 C CD1 . PHE B 2 620 ? -12.334 7.382 69.579 1.00 86.07 ? 620 PHE B CD1 1 ATOM 11925 C CD2 . PHE B 2 620 ? -12.635 5.353 70.793 1.00 86.04 ? 620 PHE B CD2 1 ATOM 11926 C CE1 . PHE B 2 620 ? -11.722 7.952 70.678 1.00 90.71 ? 620 PHE B CE1 1 ATOM 11927 C CE2 . PHE B 2 620 ? -12.025 5.917 71.895 1.00 88.02 ? 620 PHE B CE2 1 ATOM 11928 C CZ . PHE B 2 620 ? -11.567 7.219 71.837 1.00 92.01 ? 620 PHE B CZ 1 ATOM 11929 N N . ASP B 2 621 ? -13.161 3.757 65.381 1.00 88.32 ? 621 ASP B N 1 ATOM 11930 C CA . ASP B 2 621 ? -13.865 2.868 64.454 1.00 89.90 ? 621 ASP B CA 1 ATOM 11931 C C . ASP B 2 621 ? -15.363 2.867 64.750 1.00 91.58 ? 621 ASP B C 1 ATOM 11932 O O . ASP B 2 621 ? -15.977 1.812 64.904 1.00 107.04 ? 621 ASP B O 1 ATOM 11933 C CB . ASP B 2 621 ? -13.293 1.447 64.540 1.00 109.88 ? 621 ASP B CB 1 ATOM 11934 C CG . ASP B 2 621 ? -13.721 0.567 63.379 1.00 130.37 ? 621 ASP B CG 1 ATOM 11935 O OD1 . ASP B 2 621 ? -14.620 -0.279 63.569 1.00 120.13 ? 621 ASP B OD1 1 ATOM 11936 O OD2 . ASP B 2 621 ? -13.153 0.718 62.277 1.00 145.86 ? 621 ASP B OD2 1 ATOM 11937 N N . ARG B 2 622 ? -15.946 4.059 64.843 1.00 103.89 ? 622 ARG B N 1 ATOM 11938 C CA . ARG B 2 622 ? -17.305 4.190 65.357 1.00 96.96 ? 622 ARG B CA 1 ATOM 11939 C C . ARG B 2 622 ? -18.248 5.007 64.465 1.00 109.56 ? 622 ARG B C 1 ATOM 11940 O O . ARG B 2 622 ? -17.902 5.396 63.352 1.00 111.02 ? 622 ARG B O 1 ATOM 11941 C CB . ARG B 2 622 ? -17.276 4.798 66.759 1.00 112.72 ? 622 ARG B CB 1 ATOM 11942 C CG . ARG B 2 622 ? -18.123 4.042 67.773 1.00 106.24 ? 622 ARG B CG 1 ATOM 11943 C CD . ARG B 2 622 ? -17.257 3.268 68.753 1.00 118.26 ? 622 ARG B CD 1 ATOM 11944 N NE . ARG B 2 622 ? -16.513 4.163 69.631 1.00 132.35 ? 622 ARG B NE 1 ATOM 11945 C CZ . ARG B 2 622 ? -16.936 4.556 70.828 1.00 112.74 ? 622 ARG B CZ 1 ATOM 11946 N NH1 . ARG B 2 622 ? -18.101 4.126 71.295 1.00 95.40 ? 622 ARG B NH1 1 ATOM 11947 N NH2 . ARG B 2 622 ? -16.195 5.375 71.561 1.00 104.62 ? 622 ARG B NH2 1 ATOM 11948 N N . GLY B 2 623 ? -19.434 5.275 65.002 1.00 121.74 ? 623 GLY B N 1 ATOM 11949 C CA . GLY B 2 623 ? -20.608 5.669 64.242 1.00 120.26 ? 623 GLY B CA 1 ATOM 11950 C C . GLY B 2 623 ? -20.623 6.768 63.193 1.00 126.67 ? 623 GLY B C 1 ATOM 11951 O O . GLY B 2 623 ? -19.947 7.793 63.296 1.00 140.48 ? 623 GLY B O 1 ATOM 11952 N N . ALA B 2 624 ? -21.409 6.483 62.156 1.00 118.84 ? 624 ALA B N 1 ATOM 11953 C CA . ALA B 2 624 ? -21.948 7.429 61.174 1.00 108.22 ? 624 ALA B CA 1 ATOM 11954 C C . ALA B 2 624 ? -20.991 7.920 60.085 1.00 107.12 ? 624 ALA B C 1 ATOM 11955 O O . ALA B 2 624 ? -21.452 8.391 59.046 1.00 121.96 ? 624 ALA B O 1 ATOM 11956 C CB . ALA B 2 624 ? -22.541 8.637 61.903 1.00 101.88 ? 624 ALA B CB 1 ATOM 11957 N N . LEU B 2 625 ? -19.682 7.827 60.288 1.00 117.22 ? 625 LEU B N 1 ATOM 11958 C CA . LEU B 2 625 ? -18.780 7.869 59.142 1.00 115.31 ? 625 LEU B CA 1 ATOM 11959 C C . LEU B 2 625 ? -18.267 6.468 58.832 1.00 109.52 ? 625 LEU B C 1 ATOM 11960 O O . LEU B 2 625 ? -17.610 6.239 57.816 1.00 96.10 ? 625 LEU B O 1 ATOM 11961 C CB . LEU B 2 625 ? -17.622 8.837 59.385 1.00 119.95 ? 625 LEU B CB 1 ATOM 11962 C CG . LEU B 2 625 ? -17.647 10.059 58.461 1.00 92.85 ? 625 LEU B CG 1 ATOM 11963 C CD1 . LEU B 2 625 ? -18.972 10.798 58.592 1.00 91.61 ? 625 LEU B CD1 1 ATOM 11964 C CD2 . LEU B 2 625 ? -16.481 10.992 58.740 1.00 88.60 ? 625 LEU B CD2 1 ATOM 11965 N N . HIS B 2 626 ? -18.578 5.537 59.727 1.00 117.27 ? 626 HIS B N 1 ATOM 11966 C CA . HIS B 2 626 ? -18.207 4.136 59.568 1.00 108.49 ? 626 HIS B CA 1 ATOM 11967 C C . HIS B 2 626 ? -19.222 3.397 58.709 1.00 109.30 ? 626 HIS B C 1 ATOM 11968 O O . HIS B 2 626 ? -18.875 2.506 57.935 1.00 128.65 ? 626 HIS B O 1 ATOM 11969 C CB . HIS B 2 626 ? -18.083 3.465 60.937 1.00 113.87 ? 626 HIS B CB 1 ATOM 11970 C CG . HIS B 2 626 ? -17.555 2.066 60.884 1.00 102.07 ? 626 HIS B CG 1 ATOM 11971 N ND1 . HIS B 2 626 ? -16.316 1.757 60.368 1.00 118.80 ? 626 HIS B ND1 1 ATOM 11972 C CD2 . HIS B 2 626 ? -18.097 0.893 61.291 1.00 103.43 ? 626 HIS B CD2 1 ATOM 11973 C CE1 . HIS B 2 626 ? -16.118 0.453 60.454 1.00 139.58 ? 626 HIS B CE1 1 ATOM 11974 N NE2 . HIS B 2 626 ? -17.184 -0.093 61.011 1.00 128.57 ? 626 HIS B NE2 1 ATOM 11975 N N . ASP B 2 627 ? -20.484 3.787 58.858 1.00 104.80 ? 627 ASP B N 1 ATOM 11976 C CA . ASP B 2 627 ? -21.601 3.064 58.264 1.00 108.27 ? 627 ASP B CA 1 ATOM 11977 C C . ASP B 2 627 ? -21.700 3.261 56.753 1.00 111.06 ? 627 ASP B C 1 ATOM 11978 O O . ASP B 2 627 ? -22.085 2.345 56.027 1.00 118.13 ? 627 ASP B O 1 ATOM 11979 C CB . ASP B 2 627 ? -22.908 3.492 58.934 1.00 110.71 ? 627 ASP B CB 1 ATOM 11980 C CG . ASP B 2 627 ? -22.798 3.541 60.449 1.00 113.26 ? 627 ASP B CG 1 ATOM 11981 O OD1 . ASP B 2 627 ? -21.897 2.876 61.002 1.00 116.78 ? 627 ASP B OD1 1 ATOM 11982 O OD2 . ASP B 2 627 ? -23.611 4.245 61.083 1.00 110.74 ? 627 ASP B OD2 1 ATOM 11983 N N . GLU B 2 628 ? -21.355 4.456 56.283 1.00 107.29 ? 628 GLU B N 1 ATOM 11984 C CA . GLU B 2 628 ? -21.436 4.763 54.858 1.00 108.18 ? 628 GLU B CA 1 ATOM 11985 C C . GLU B 2 628 ? -20.120 4.487 54.137 1.00 107.20 ? 628 GLU B C 1 ATOM 11986 O O . GLU B 2 628 ? -20.010 4.718 52.932 1.00 122.41 ? 628 GLU B O 1 ATOM 11987 C CB . GLU B 2 628 ? -21.845 6.223 54.644 1.00 111.12 ? 628 GLU B CB 1 ATOM 11988 C CG . GLU B 2 628 ? -23.284 6.551 55.024 1.00 129.53 ? 628 GLU B CG 1 ATOM 11989 C CD . GLU B 2 628 ? -23.445 6.906 56.491 1.00 133.48 ? 628 GLU B CD 1 ATOM 11990 O OE1 . GLU B 2 628 ? -22.690 6.366 57.327 1.00 135.93 ? 628 GLU B OE1 1 ATOM 11991 O OE2 . GLU B 2 628 ? -24.326 7.733 56.807 1.00 119.29 ? 628 GLU B OE2 1 ATOM 11992 N N . ASN B 2 629 ? -19.127 4.005 54.884 1.00 104.55 ? 629 ASN B N 1 ATOM 11993 C CA . ASN B 2 629 ? -17.804 3.686 54.345 1.00 102.93 ? 629 ASN B CA 1 ATOM 11994 C C . ASN B 2 629 ? -17.134 4.907 53.711 1.00 108.97 ? 629 ASN B C 1 ATOM 11995 O O . ASN B 2 629 ? -16.292 4.780 52.821 1.00 110.16 ? 629 ASN B O 1 ATOM 11996 C CB . ASN B 2 629 ? -17.902 2.543 53.326 1.00 110.73 ? 629 ASN B CB 1 ATOM 11997 C CG . ASN B 2 629 ? -16.562 1.884 53.048 1.00 128.02 ? 629 ASN B CG 1 ATOM 11998 O OD1 . ASN B 2 629 ? -15.703 1.804 53.926 1.00 137.97 ? 629 ASN B OD1 1 ATOM 11999 N ND2 . ASN B 2 629 ? -16.376 1.419 51.819 1.00 124.97 ? 629 ASN B ND2 1 ATOM 12000 N N . THR B 2 630 ? -17.517 6.091 54.176 1.00 121.31 ? 630 THR B N 1 ATOM 12001 C CA . THR B 2 630 ? -16.965 7.340 53.663 1.00 106.21 ? 630 THR B CA 1 ATOM 12002 C C . THR B 2 630 ? -15.817 7.849 54.530 1.00 112.75 ? 630 THR B C 1 ATOM 12003 O O . THR B 2 630 ? -15.256 8.912 54.268 1.00 116.95 ? 630 THR B O 1 ATOM 12004 C CB . THR B 2 630 ? -18.042 8.438 53.575 1.00 99.96 ? 630 THR B CB 1 ATOM 12005 O OG1 . THR B 2 630 ? -18.466 8.802 54.894 1.00 113.33 ? 630 THR B OG1 1 ATOM 12006 C CG2 . THR B 2 630 ? -19.240 7.948 52.778 1.00 101.40 ? 630 THR B CG2 1 ATOM 12007 N N . CYS B 2 631 ? -15.477 7.085 55.564 1.00 120.62 ? 631 CYS B N 1 ATOM 12008 C CA . CYS B 2 631 ? -14.468 7.501 56.536 1.00 119.72 ? 631 CYS B CA 1 ATOM 12009 C C . CYS B 2 631 ? -13.093 7.710 55.907 1.00 115.52 ? 631 CYS B C 1 ATOM 12010 O O . CYS B 2 631 ? -12.472 8.757 56.090 1.00 120.36 ? 631 CYS B O 1 ATOM 12011 C CB . CYS B 2 631 ? -14.369 6.472 57.664 1.00 119.51 ? 631 CYS B CB 1 ATOM 12012 S SG . CYS B 2 631 ? -13.194 6.904 58.969 1.00 162.29 ? 631 CYS B SG 1 ATOM 12013 N N . ASN B 2 632 ? -12.624 6.712 55.164 1.00 115.98 ? 632 ASN B N 1 ATOM 12014 C CA . ASN B 2 632 ? -11.300 6.766 54.553 1.00 120.15 ? 632 ASN B CA 1 ATOM 12015 C C . ASN B 2 632 ? -11.223 7.814 53.448 1.00 126.43 ? 632 ASN B C 1 ATOM 12016 O O . ASN B 2 632 ? -10.137 8.238 53.053 1.00 130.53 ? 632 ASN B O 1 ATOM 12017 C CB . ASN B 2 632 ? -10.915 5.393 53.997 1.00 134.11 ? 632 ASN B CB 1 ATOM 12018 C CG . ASN B 2 632 ? -9.416 5.228 53.835 1.00 154.12 ? 632 ASN B CG 1 ATOM 12019 O OD1 . ASN B 2 632 ? -8.842 5.610 52.815 1.00 166.45 ? 632 ASN B OD1 1 ATOM 12020 N ND2 . ASN B 2 632 ? -8.773 4.654 54.846 1.00 157.01 ? 632 ASN B ND2 1 ATOM 12021 N N . ARG B 2 633 ? -12.385 8.227 52.955 1.00 128.83 ? 633 ARG B N 1 ATOM 12022 C CA . ARG B 2 633 ? -12.465 9.229 51.898 1.00 136.85 ? 633 ARG B CA 1 ATOM 12023 C C . ARG B 2 633 ? -12.668 10.629 52.468 1.00 135.00 ? 633 ARG B C 1 ATOM 12024 O O . ARG B 2 633 ? -11.819 11.504 52.300 1.00 135.80 ? 633 ARG B O 1 ATOM 12025 C CB . ARG B 2 633 ? -13.598 8.891 50.928 1.00 145.25 ? 633 ARG B CB 1 ATOM 12026 C CG . ARG B 2 633 ? -13.800 9.913 49.820 1.00 143.96 ? 633 ARG B CG 1 ATOM 12027 C CD . ARG B 2 633 ? -12.585 9.999 48.912 1.00 144.23 ? 633 ARG B CD 1 ATOM 12028 N NE . ARG B 2 633 ? -12.303 8.729 48.248 1.00 135.15 ? 633 ARG B NE 1 ATOM 12029 C CZ . ARG B 2 633 ? -12.812 8.371 47.074 1.00 131.51 ? 633 ARG B CZ 1 ATOM 12030 N NH1 . ARG B 2 633 ? -13.634 9.187 46.427 1.00 136.38 ? 633 ARG B NH1 1 ATOM 12031 N NH2 . ARG B 2 633 ? -12.501 7.195 46.545 1.00 123.79 ? 633 ARG B NH2 1 ATOM 12032 N N . TYR B 2 634 ? -13.799 10.834 53.138 1.00 135.08 ? 634 TYR B N 1 ATOM 12033 C CA . TYR B 2 634 ? -14.171 12.157 53.629 1.00 126.80 ? 634 TYR B CA 1 ATOM 12034 C C . TYR B 2 634 ? -13.216 12.701 54.690 1.00 120.82 ? 634 TYR B C 1 ATOM 12035 O O . TYR B 2 634 ? -13.110 13.916 54.860 1.00 132.80 ? 634 TYR B O 1 ATOM 12036 C CB . TYR B 2 634 ? -15.600 12.138 54.179 1.00 124.28 ? 634 TYR B CB 1 ATOM 12037 C CG . TYR B 2 634 ? -16.666 12.141 53.106 1.00 131.48 ? 634 TYR B CG 1 ATOM 12038 C CD1 . TYR B 2 634 ? -16.329 12.272 51.764 1.00 138.33 ? 634 TYR B CD1 1 ATOM 12039 C CD2 . TYR B 2 634 ? -18.010 12.026 53.435 1.00 142.90 ? 634 TYR B CD2 1 ATOM 12040 C CE1 . TYR B 2 634 ? -17.300 12.278 50.780 1.00 144.33 ? 634 TYR B CE1 1 ATOM 12041 C CE2 . TYR B 2 634 ? -18.989 12.032 52.458 1.00 141.91 ? 634 TYR B CE2 1 ATOM 12042 C CZ . TYR B 2 634 ? -18.629 12.158 51.133 1.00 142.78 ? 634 TYR B CZ 1 ATOM 12043 O OH . TYR B 2 634 ? -19.600 12.165 50.158 1.00 147.69 ? 634 TYR B OH 1 ATOM 12044 N N . CYS B 2 635 ? -12.527 11.820 55.408 1.00 117.54 ? 635 CYS B N 1 ATOM 12045 C CA . CYS B 2 635 ? -11.492 12.286 56.321 1.00 118.09 ? 635 CYS B CA 1 ATOM 12046 C C . CYS B 2 635 ? -10.114 12.056 55.715 1.00 118.09 ? 635 CYS B C 1 ATOM 12047 O O . CYS B 2 635 ? -9.620 10.929 55.675 1.00 119.44 ? 635 CYS B O 1 ATOM 12048 C CB . CYS B 2 635 ? -11.600 11.579 57.675 1.00 106.53 ? 635 CYS B CB 1 ATOM 12049 S SG . CYS B 2 635 ? -13.052 12.030 58.655 1.00 109.05 ? 635 CYS B SG 1 ATOM 12050 N N . ARG B 2 636 ? -9.501 13.136 55.242 1.00 126.40 ? 636 ARG B N 1 ATOM 12051 C CA . ARG B 2 636 ? -8.137 13.092 54.732 1.00 133.84 ? 636 ARG B CA 1 ATOM 12052 C C . ARG B 2 636 ? -7.132 13.623 55.748 1.00 127.10 ? 636 ARG B C 1 ATOM 12053 O O . ARG B 2 636 ? -5.925 13.609 55.506 1.00 133.16 ? 636 ARG B O 1 ATOM 12054 C CB . ARG B 2 636 ? -8.035 13.878 53.424 1.00 145.83 ? 636 ARG B CB 1 ATOM 12055 C CG . ARG B 2 636 ? -8.811 13.251 52.278 1.00 146.22 ? 636 ARG B CG 1 ATOM 12056 C CD . ARG B 2 636 ? -8.639 14.042 50.994 1.00 152.23 ? 636 ARG B CD 1 ATOM 12057 N NE . ARG B 2 636 ? -9.182 15.392 51.108 1.00 163.60 ? 636 ARG B NE 1 ATOM 12058 C CZ . ARG B 2 636 ? -10.440 15.716 50.826 1.00 165.87 ? 636 ARG B CZ 1 ATOM 12059 N NH1 . ARG B 2 636 ? -11.289 14.787 50.412 1.00 165.65 ? 636 ARG B NH1 1 ATOM 12060 N NH2 . ARG B 2 636 ? -10.848 16.970 50.958 1.00 165.75 ? 636 ARG B NH2 1 ATOM 12061 N N . ASP B 2 637 ? -7.636 14.093 56.884 1.00 123.86 ? 637 ASP B N 1 ATOM 12062 C CA . ASP B 2 637 ? -6.791 14.716 57.895 1.00 121.86 ? 637 ASP B CA 1 ATOM 12063 C C . ASP B 2 637 ? -5.890 13.691 58.571 1.00 119.72 ? 637 ASP B C 1 ATOM 12064 O O . ASP B 2 637 ? -6.226 12.509 58.647 1.00 120.47 ? 637 ASP B O 1 ATOM 12065 C CB . ASP B 2 637 ? -7.647 15.437 58.940 1.00 132.20 ? 637 ASP B CB 1 ATOM 12066 C CG . ASP B 2 637 ? -8.536 16.503 58.330 1.00 150.17 ? 637 ASP B CG 1 ATOM 12067 O OD1 . ASP B 2 637 ? -9.706 16.194 58.015 1.00 160.31 ? 637 ASP B OD1 1 ATOM 12068 O OD2 . ASP B 2 637 ? -8.067 17.649 58.164 1.00 148.42 ? 637 ASP B OD2 1 ATOM 12069 N N . GLU B 2 638 ? -4.743 14.149 59.061 1.00 122.68 ? 638 GLU B N 1 ATOM 12070 C CA . GLU B 2 638 ? -3.796 13.261 59.718 1.00 123.04 ? 638 GLU B CA 1 ATOM 12071 C C . GLU B 2 638 ? -4.043 13.267 61.222 1.00 115.86 ? 638 GLU B C 1 ATOM 12072 O O . GLU B 2 638 ? -3.805 14.270 61.895 1.00 129.34 ? 638 GLU B O 1 ATOM 12073 C CB . GLU B 2 638 ? -2.359 13.682 59.397 1.00 135.27 ? 638 GLU B CB 1 ATOM 12074 C CG . GLU B 2 638 ? -1.341 12.550 59.449 1.00 153.36 ? 638 GLU B CG 1 ATOM 12075 C CD . GLU B 2 638 ? -0.878 12.236 60.857 1.00 160.55 ? 638 GLU B CD 1 ATOM 12076 O OE1 . GLU B 2 638 ? -0.946 13.136 61.720 1.00 177.30 ? 638 GLU B OE1 1 ATOM 12077 O OE2 . GLU B 2 638 ? -0.445 11.090 61.100 1.00 138.60 ? 638 GLU B OE2 1 ATOM 12078 N N . ILE B 2 639 ? -4.521 12.142 61.742 1.00 108.04 ? 639 ILE B N 1 ATOM 12079 C CA . ILE B 2 639 ? -4.856 12.035 63.156 1.00 101.57 ? 639 ILE B CA 1 ATOM 12080 C C . ILE B 2 639 ? -3.761 11.303 63.924 1.00 108.34 ? 639 ILE B C 1 ATOM 12081 O O . ILE B 2 639 ? -3.340 10.212 63.540 1.00 127.88 ? 639 ILE B O 1 ATOM 12082 C CB . ILE B 2 639 ? -6.201 11.308 63.361 1.00 94.17 ? 639 ILE B CB 1 ATOM 12083 C CG1 . ILE B 2 639 ? -7.306 11.996 62.557 1.00 93.67 ? 639 ILE B CG1 1 ATOM 12084 C CG2 . ILE B 2 639 ? -6.564 11.258 64.839 1.00 89.42 ? 639 ILE B CG2 1 ATOM 12085 C CD1 . ILE B 2 639 ? -8.664 11.348 62.710 1.00 97.94 ? 639 ILE B CD1 1 ATOM 12086 N N . GLU B 2 640 ? -3.303 11.916 65.010 1.00 104.10 ? 640 GLU B N 1 ATOM 12087 C CA . GLU B 2 640 ? -2.227 11.349 65.813 1.00 106.75 ? 640 GLU B CA 1 ATOM 12088 C C . GLU B 2 640 ? -2.567 11.382 67.298 1.00 102.07 ? 640 GLU B C 1 ATOM 12089 O O . GLU B 2 640 ? -3.028 12.398 67.817 1.00 101.75 ? 640 GLU B O 1 ATOM 12090 C CB . GLU B 2 640 ? -0.919 12.101 65.557 1.00 118.04 ? 640 GLU B CB 1 ATOM 12091 C CG . GLU B 2 640 ? 0.241 11.654 66.429 1.00 127.17 ? 640 GLU B CG 1 ATOM 12092 C CD . GLU B 2 640 ? 1.473 12.512 66.232 1.00 143.68 ? 640 GLU B CD 1 ATOM 12093 O OE1 . GLU B 2 640 ? 1.456 13.380 65.333 1.00 145.41 ? 640 GLU B OE1 1 ATOM 12094 O OE2 . GLU B 2 640 ? 2.458 12.323 66.976 1.00 154.89 ? 640 GLU B OE2 1 ATOM 12095 N N . SER B 2 641 ? -2.337 10.263 67.975 1.00 99.46 ? 641 SER B N 1 ATOM 12096 C CA . SER B 2 641 ? -2.585 10.171 69.406 1.00 99.21 ? 641 SER B CA 1 ATOM 12097 C C . SER B 2 641 ? -1.475 10.861 70.193 1.00 114.06 ? 641 SER B C 1 ATOM 12098 O O . SER B 2 641 ? -0.300 10.527 70.049 1.00 137.71 ? 641 SER B O 1 ATOM 12099 C CB . SER B 2 641 ? -2.710 8.708 69.832 1.00 105.00 ? 641 SER B CB 1 ATOM 12100 O OG . SER B 2 641 ? -3.800 8.075 69.184 1.00 96.84 ? 641 SER B OG 1 ATOM 12101 N N . VAL B 2 642 ? -1.858 11.818 71.031 1.00 113.78 ? 642 VAL B N 1 ATOM 12102 C CA . VAL B 2 642 ? -0.895 12.585 71.813 1.00 113.16 ? 642 VAL B CA 1 ATOM 12103 C C . VAL B 2 642 ? -1.028 12.184 73.282 1.00 111.86 ? 642 VAL B C 1 ATOM 12104 O O . VAL B 2 642 ? -2.097 11.752 73.715 1.00 104.77 ? 642 VAL B O 1 ATOM 12105 C CB . VAL B 2 642 ? -1.102 14.109 71.627 1.00 117.56 ? 642 VAL B CB 1 ATOM 12106 C CG1 . VAL B 2 642 ? -2.400 14.565 72.275 1.00 124.96 ? 642 VAL B CG1 1 ATOM 12107 C CG2 . VAL B 2 642 ? 0.087 14.891 72.172 1.00 129.86 ? 642 VAL B CG2 1 ATOM 12108 N N . LYS B 2 643 ? 0.055 12.306 74.045 1.00 122.19 ? 643 LYS B N 1 ATOM 12109 C CA . LYS B 2 643 ? 0.101 11.704 75.374 1.00 139.14 ? 643 LYS B CA 1 ATOM 12110 C C . LYS B 2 643 ? -0.348 12.643 76.490 1.00 142.11 ? 643 LYS B C 1 ATOM 12111 O O . LYS B 2 643 ? 0.354 13.590 76.847 1.00 148.46 ? 643 LYS B O 1 ATOM 12112 C CB . LYS B 2 643 ? 1.522 11.212 75.668 1.00 143.43 ? 643 LYS B CB 1 ATOM 12113 C CG . LYS B 2 643 ? 1.757 10.779 77.107 1.00 147.70 ? 643 LYS B CG 1 ATOM 12114 C CD . LYS B 2 643 ? 3.240 10.597 77.391 1.00 156.23 ? 643 LYS B CD 1 ATOM 12115 C CE . LYS B 2 643 ? 4.006 11.895 77.181 1.00 163.62 ? 643 LYS B CE 1 ATOM 12116 N NZ . LYS B 2 643 ? 3.529 12.982 78.081 1.00 159.02 ? 643 LYS B NZ 1 ATOM 12117 N N . GLU B 2 644 ? -1.537 12.357 77.017 1.00 142.01 ? 644 GLU B N 1 ATOM 12118 C CA . GLU B 2 644 ? -2.063 12.920 78.262 1.00 149.44 ? 644 GLU B CA 1 ATOM 12119 C C . GLU B 2 644 ? -1.880 14.424 78.432 1.00 157.26 ? 644 GLU B C 1 ATOM 12120 O O . GLU B 2 644 ? -1.793 14.905 79.564 1.00 164.70 ? 644 GLU B O 1 ATOM 12121 C CB . GLU B 2 644 ? -1.427 12.208 79.458 1.00 159.19 ? 644 GLU B CB 1 ATOM 12122 C CG . GLU B 2 644 ? -1.795 10.741 79.571 1.00 157.50 ? 644 GLU B CG 1 ATOM 12123 C CD . GLU B 2 644 ? -1.287 10.112 80.851 1.00 164.69 ? 644 GLU B CD 1 ATOM 12124 O OE1 . GLU B 2 644 ? -0.746 10.848 81.704 1.00 161.11 ? 644 GLU B OE1 1 ATOM 12125 O OE2 . GLU B 2 644 ? -1.429 8.881 81.007 1.00 170.70 ? 644 GLU B OE2 1 ATOM 12126 N N . LEU B 2 645 ? -1.874 15.156 77.321 1.00 157.47 ? 645 LEU B N 1 ATOM 12127 C CA . LEU B 2 645 ? -1.664 16.601 77.342 1.00 162.19 ? 645 LEU B CA 1 ATOM 12128 C C . LEU B 2 645 ? -1.642 17.176 75.932 1.00 151.17 ? 645 LEU B C 1 ATOM 12129 O O . LEU B 2 645 ? -1.423 16.457 74.957 1.00 141.73 ? 645 LEU B O 1 ATOM 12130 C CB . LEU B 2 645 ? -0.349 16.951 78.053 1.00 170.74 ? 645 LEU B CB 1 ATOM 12131 C CG . LEU B 2 645 ? -0.187 18.359 78.629 1.00 173.56 ? 645 LEU B CG 1 ATOM 12132 C CD1 . LEU B 2 645 ? 0.341 18.289 80.051 1.00 171.77 ? 645 LEU B CD1 1 ATOM 12133 C CD2 . LEU B 2 645 ? 0.741 19.189 77.758 1.00 177.90 ? 645 LEU B CD2 1 ATOM 12134 N N . LYS B 2 646 ? -1.869 18.481 75.838 1.00 143.42 ? 646 LYS B N 1 ATOM 12135 C CA . LYS B 2 646 ? -1.633 19.226 74.612 1.00 140.23 ? 646 LYS B CA 1 ATOM 12136 C C . LYS B 2 646 ? -0.873 20.497 74.970 1.00 157.02 ? 646 LYS B C 1 ATOM 12137 O O . LYS B 2 646 ? -1.393 21.349 75.690 1.00 172.45 ? 646 LYS B O 1 ATOM 12138 C CB . LYS B 2 646 ? -2.949 19.553 73.905 1.00 128.80 ? 646 LYS B CB 1 ATOM 12139 C CG . LYS B 2 646 ? -3.733 18.329 73.459 1.00 117.94 ? 646 LYS B CG 1 ATOM 12140 C CD . LYS B 2 646 ? -5.119 18.705 72.961 1.00 118.87 ? 646 LYS B CD 1 ATOM 12141 C CE . LYS B 2 646 ? -5.925 19.398 74.047 1.00 140.33 ? 646 LYS B CE 1 ATOM 12142 N NZ . LYS B 2 646 ? -7.290 19.776 73.582 1.00 154.17 ? 646 LYS B NZ 1 ATOM 12143 N N . ASP B 2 647 ? 0.358 20.613 74.479 1.00 167.87 ? 647 ASP B N 1 ATOM 12144 C CA . ASP B 2 647 ? 1.200 21.763 74.793 1.00 184.20 ? 647 ASP B CA 1 ATOM 12145 C C . ASP B 2 647 ? 0.535 23.047 74.325 1.00 180.22 ? 647 ASP B C 1 ATOM 12146 O O . ASP B 2 647 ? -0.126 23.060 73.286 1.00 169.33 ? 647 ASP B O 1 ATOM 12147 C CB . ASP B 2 647 ? 2.577 21.628 74.140 1.00 198.54 ? 647 ASP B CB 1 ATOM 12148 C CG . ASP B 2 647 ? 3.227 20.288 74.420 1.00 208.25 ? 647 ASP B CG 1 ATOM 12149 O OD1 . ASP B 2 647 ? 2.496 19.281 74.518 1.00 212.27 ? 647 ASP B OD1 1 ATOM 12150 O OD2 . ASP B 2 647 ? 4.469 20.243 74.540 1.00 213.25 ? 647 ASP B OD2 1 ATOM 12151 N N . THR B 2 648 ? 0.693 24.126 75.085 1.00 185.41 ? 648 THR B N 1 ATOM 12152 C CA . THR B 2 648 ? 0.173 25.400 74.616 1.00 188.15 ? 648 THR B CA 1 ATOM 12153 C C . THR B 2 648 ? 1.047 25.829 73.444 1.00 195.09 ? 648 THR B C 1 ATOM 12154 O O . THR B 2 648 ? 2.252 26.039 73.585 1.00 199.10 ? 648 THR B O 1 ATOM 12155 C CB . THR B 2 648 ? 0.161 26.471 75.728 1.00 188.24 ? 648 THR B CB 1 ATOM 12156 O OG1 . THR B 2 648 ? 0.080 27.775 75.140 1.00 191.51 ? 648 THR B OG1 1 ATOM 12157 C CG2 . THR B 2 648 ? 1.417 26.380 76.585 1.00 188.97 ? 648 THR B CG2 1 ATOM 12158 N N . GLY B 2 649 ? 0.419 25.950 72.283 1.00 194.28 ? 649 GLY B N 1 ATOM 12159 C CA . GLY B 2 649 ? 1.131 26.188 71.043 1.00 195.48 ? 649 GLY B CA 1 ATOM 12160 C C . GLY B 2 649 ? 0.892 27.551 70.438 1.00 199.60 ? 649 GLY B C 1 ATOM 12161 O O . GLY B 2 649 ? 0.580 28.522 71.128 1.00 200.19 ? 649 GLY B O 1 ATOM 12162 N N . LYS B 2 650 ? 1.044 27.606 69.119 1.00 198.80 ? 650 LYS B N 1 ATOM 12163 C CA . LYS B 2 650 ? 0.592 28.737 68.325 1.00 195.23 ? 650 LYS B CA 1 ATOM 12164 C C . LYS B 2 650 ? -0.925 28.641 68.210 1.00 186.85 ? 650 LYS B C 1 ATOM 12165 O O . LYS B 2 650 ? -1.545 27.828 68.897 1.00 173.63 ? 650 LYS B O 1 ATOM 12166 C CB . LYS B 2 650 ? 1.256 28.738 66.948 1.00 193.71 ? 650 LYS B CB 1 ATOM 12167 C CG . LYS B 2 650 ? 2.771 28.895 66.988 1.00 198.75 ? 650 LYS B CG 1 ATOM 12168 C CD . LYS B 2 650 ? 3.481 27.727 66.313 1.00 197.98 ? 650 LYS B CD 1 ATOM 12169 C CE . LYS B 2 650 ? 3.333 26.442 67.113 1.00 196.07 ? 650 LYS B CE 1 ATOM 12170 N NZ . LYS B 2 650 ? 3.910 26.569 68.481 1.00 197.83 ? 650 LYS B NZ 1 ATOM 12171 N N . ASP B 2 651 ? -1.529 29.470 67.363 1.00 190.53 ? 651 ASP B N 1 ATOM 12172 C CA . ASP B 2 651 ? -2.987 29.512 67.272 1.00 180.01 ? 651 ASP B CA 1 ATOM 12173 C C . ASP B 2 651 ? -3.573 28.134 66.965 1.00 155.44 ? 651 ASP B C 1 ATOM 12174 O O . ASP B 2 651 ? -3.225 27.497 65.970 1.00 146.54 ? 651 ASP B O 1 ATOM 12175 C CB . ASP B 2 651 ? -3.427 30.525 66.211 1.00 193.32 ? 651 ASP B CB 1 ATOM 12176 C CG . ASP B 2 651 ? -2.847 30.229 64.843 1.00 200.98 ? 651 ASP B CG 1 ATOM 12177 O OD1 . ASP B 2 651 ? -3.541 30.477 63.835 1.00 204.18 ? 651 ASP B OD1 1 ATOM 12178 O OD2 . ASP B 2 651 ? -1.696 29.745 64.773 1.00 204.97 ? 651 ASP B OD2 1 ATOM 12179 N N . ALA B 2 652 ? -4.463 27.685 67.844 1.00 159.91 ? 652 ALA B N 1 ATOM 12180 C CA . ALA B 2 652 ? -5.084 26.372 67.733 1.00 151.75 ? 652 ALA B CA 1 ATOM 12181 C C . ALA B 2 652 ? -6.382 26.347 68.531 1.00 149.78 ? 652 ALA B C 1 ATOM 12182 O O . ALA B 2 652 ? -6.602 27.197 69.393 1.00 167.76 ? 652 ALA B O 1 ATOM 12183 C CB . ALA B 2 652 ? -4.137 25.285 68.214 1.00 133.75 ? 652 ALA B CB 1 ATOM 12184 N N . VAL B 2 653 ? -7.237 25.372 68.249 1.00 121.23 ? 653 VAL B N 1 ATOM 12185 C CA . VAL B 2 653 ? -8.526 25.289 68.922 1.00 130.37 ? 653 VAL B CA 1 ATOM 12186 C C . VAL B 2 653 ? -8.767 23.916 69.543 1.00 136.87 ? 653 VAL B C 1 ATOM 12187 O O . VAL B 2 653 ? -8.702 22.890 68.864 1.00 125.24 ? 653 VAL B O 1 ATOM 12188 C CB . VAL B 2 653 ? -9.679 25.624 67.951 1.00 125.30 ? 653 VAL B CB 1 ATOM 12189 C CG1 . VAL B 2 653 ? -9.410 25.034 66.575 1.00 112.71 ? 653 VAL B CG1 1 ATOM 12190 C CG2 . VAL B 2 653 ? -11.017 25.153 68.511 1.00 111.91 ? 653 VAL B CG2 1 ATOM 12191 N N . ASN B 2 654 ? -9.034 23.909 70.845 1.00 147.44 ? 654 ASN B N 1 ATOM 12192 C CA . ASN B 2 654 ? -9.352 22.680 71.560 1.00 132.20 ? 654 ASN B CA 1 ATOM 12193 C C . ASN B 2 654 ? -10.806 22.276 71.344 1.00 106.81 ? 654 ASN B C 1 ATOM 12194 O O . ASN B 2 654 ? -11.683 23.131 71.209 1.00 106.77 ? 654 ASN B O 1 ATOM 12195 C CB . ASN B 2 654 ? -9.069 22.840 73.055 1.00 144.92 ? 654 ASN B CB 1 ATOM 12196 C CG . ASN B 2 654 ? -7.599 23.077 73.350 1.00 150.01 ? 654 ASN B CG 1 ATOM 12197 O OD1 . ASN B 2 654 ? -6.821 23.411 72.458 1.00 167.21 ? 654 ASN B OD1 1 ATOM 12198 N ND2 . ASN B 2 654 ? -7.214 22.905 74.610 1.00 134.57 ? 654 ASN B ND2 1 ATOM 12199 N N . CYS B 2 655 ? -11.060 20.973 71.309 1.00 98.22 ? 655 CYS B N 1 ATOM 12200 C CA . CYS B 2 655 ? -12.418 20.470 71.152 1.00 108.21 ? 655 CYS B CA 1 ATOM 12201 C C . CYS B 2 655 ? -12.690 19.310 72.102 1.00 100.67 ? 655 CYS B C 1 ATOM 12202 O O . CYS B 2 655 ? -11.780 18.571 72.476 1.00 92.84 ? 655 CYS B O 1 ATOM 12203 C CB . CYS B 2 655 ? -12.671 20.040 69.706 1.00 100.67 ? 655 CYS B CB 1 ATOM 12204 S SG . CYS B 2 655 ? -12.820 21.412 68.536 1.00 184.00 ? 655 CYS B SG 1 ATOM 12205 N N . THR B 2 656 ? -13.952 19.158 72.484 1.00 108.92 ? 656 THR B N 1 ATOM 12206 C CA . THR B 2 656 ? -14.346 18.166 73.475 1.00 91.86 ? 656 THR B CA 1 ATOM 12207 C C . THR B 2 656 ? -15.712 17.587 73.109 1.00 94.66 ? 656 THR B C 1 ATOM 12208 O O . THR B 2 656 ? -16.485 18.232 72.401 1.00 115.48 ? 656 THR B O 1 ATOM 12209 C CB . THR B 2 656 ? -14.388 18.788 74.890 1.00 101.93 ? 656 THR B CB 1 ATOM 12210 O OG1 . THR B 2 656 ? -13.218 19.589 75.099 1.00 104.09 ? 656 THR B OG1 1 ATOM 12211 C CG2 . THR B 2 656 ? -14.449 17.716 75.962 1.00 106.23 ? 656 THR B CG2 1 ATOM 12212 N N . TYR B 2 657 ? -16.003 16.381 73.595 1.00 88.89 ? 657 TYR B N 1 ATOM 12213 C CA . TYR B 2 657 ? -17.290 15.726 73.362 1.00 88.25 ? 657 TYR B CA 1 ATOM 12214 C C . TYR B 2 657 ? -17.391 14.404 74.115 1.00 86.77 ? 657 TYR B C 1 ATOM 12215 O O . TYR B 2 657 ? -16.386 13.851 74.561 1.00 85.95 ? 657 TYR B O 1 ATOM 12216 C CB . TYR B 2 657 ? -17.518 15.471 71.866 1.00 87.23 ? 657 TYR B CB 1 ATOM 12217 C CG . TYR B 2 657 ? -16.706 14.327 71.297 1.00 84.72 ? 657 TYR B CG 1 ATOM 12218 C CD1 . TYR B 2 657 ? -17.272 13.070 71.121 1.00 91.76 ? 657 TYR B CD1 1 ATOM 12219 C CD2 . TYR B 2 657 ? -15.378 14.505 70.931 1.00 95.93 ? 657 TYR B CD2 1 ATOM 12220 C CE1 . TYR B 2 657 ? -16.537 12.022 70.601 1.00 91.85 ? 657 TYR B CE1 1 ATOM 12221 C CE2 . TYR B 2 657 ? -14.636 13.462 70.409 1.00 84.47 ? 657 TYR B CE2 1 ATOM 12222 C CZ . TYR B 2 657 ? -15.219 12.224 70.246 1.00 87.44 ? 657 TYR B CZ 1 ATOM 12223 O OH . TYR B 2 657 ? -14.484 11.183 69.727 1.00 93.26 ? 657 TYR B OH 1 ATOM 12224 N N . LYS B 2 658 ? -18.614 13.901 74.243 1.00 95.94 ? 658 LYS B N 1 ATOM 12225 C CA . LYS B 2 658 ? -18.851 12.589 74.831 1.00 92.68 ? 658 LYS B CA 1 ATOM 12226 C C . LYS B 2 658 ? -19.134 11.567 73.740 1.00 92.74 ? 658 LYS B C 1 ATOM 12227 O O . LYS B 2 658 ? -19.937 11.816 72.840 1.00 100.80 ? 658 LYS B O 1 ATOM 12228 C CB . LYS B 2 658 ? -20.020 12.633 75.816 1.00 94.13 ? 658 LYS B CB 1 ATOM 12229 C CG . LYS B 2 658 ? -19.616 12.722 77.277 1.00 96.71 ? 658 LYS B CG 1 ATOM 12230 C CD . LYS B 2 658 ? -20.809 12.452 78.181 1.00 114.78 ? 658 LYS B CD 1 ATOM 12231 C CE . LYS B 2 658 ? -20.407 12.396 79.647 1.00 134.35 ? 658 LYS B CE 1 ATOM 12232 N NZ . LYS B 2 658 ? -21.555 12.013 80.516 1.00 135.60 ? 658 LYS B NZ 1 ATOM 12233 N N . ASN B 2 659 ? -18.471 10.417 73.816 1.00 89.87 ? 659 ASN B N 1 ATOM 12234 C CA . ASN B 2 659 ? -18.729 9.339 72.872 1.00 96.59 ? 659 ASN B CA 1 ATOM 12235 C C . ASN B 2 659 ? -19.860 8.445 73.364 1.00 93.57 ? 659 ASN B C 1 ATOM 12236 O O . ASN B 2 659 ? -20.496 8.737 74.377 1.00 95.60 ? 659 ASN B O 1 ATOM 12237 C CB . ASN B 2 659 ? -17.461 8.514 72.627 1.00 114.86 ? 659 ASN B CB 1 ATOM 12238 C CG . ASN B 2 659 ? -16.806 8.041 73.914 1.00 108.54 ? 659 ASN B CG 1 ATOM 12239 O OD1 . ASN B 2 659 ? -17.377 8.159 75.000 1.00 109.79 ? 659 ASN B OD1 1 ATOM 12240 N ND2 . ASN B 2 659 ? -15.600 7.497 73.796 1.00 84.65 ? 659 ASN B ND2 1 ATOM 12241 N N . GLU B 2 660 ? -20.103 7.354 72.646 1.00 94.06 ? 660 GLU B N 1 ATOM 12242 C CA . GLU B 2 660 ? -21.164 6.417 72.997 1.00 96.43 ? 660 GLU B CA 1 ATOM 12243 C C . GLU B 2 660 ? -20.894 5.743 74.340 1.00 97.91 ? 660 GLU B C 1 ATOM 12244 O O . GLU B 2 660 ? -21.802 5.204 74.972 1.00 107.57 ? 660 GLU B O 1 ATOM 12245 C CB . GLU B 2 660 ? -21.317 5.358 71.903 1.00 96.00 ? 660 GLU B CB 1 ATOM 12246 C CG . GLU B 2 660 ? -21.466 5.936 70.506 1.00 117.40 ? 660 GLU B CG 1 ATOM 12247 C CD . GLU B 2 660 ? -21.354 4.880 69.424 1.00 140.66 ? 660 GLU B CD 1 ATOM 12248 O OE1 . GLU B 2 660 ? -21.268 3.681 69.766 1.00 155.64 ? 660 GLU B OE1 1 ATOM 12249 O OE2 . GLU B 2 660 ? -21.348 5.249 68.230 1.00 136.14 ? 660 GLU B OE2 1 ATOM 12250 N N . ASP B 2 661 ? -19.636 5.782 74.767 1.00 101.69 ? 661 ASP B N 1 ATOM 12251 C CA . ASP B 2 661 ? -19.204 5.131 75.997 1.00 99.57 ? 661 ASP B CA 1 ATOM 12252 C C . ASP B 2 661 ? -19.249 6.078 77.192 1.00 105.99 ? 661 ASP B C 1 ATOM 12253 O O . ASP B 2 661 ? -18.790 5.730 78.282 1.00 114.87 ? 661 ASP B O 1 ATOM 12254 C CB . ASP B 2 661 ? -17.794 4.565 75.825 1.00 100.44 ? 661 ASP B CB 1 ATOM 12255 C CG . ASP B 2 661 ? -17.695 3.607 74.655 1.00 108.91 ? 661 ASP B CG 1 ATOM 12256 O OD1 . ASP B 2 661 ? -18.715 2.967 74.325 1.00 114.97 ? 661 ASP B OD1 1 ATOM 12257 O OD2 . ASP B 2 661 ? -16.600 3.496 74.063 1.00 107.39 ? 661 ASP B OD2 1 ATOM 12258 N N . ASP B 2 662 ? -19.777 7.279 76.966 1.00 107.73 ? 662 ASP B N 1 ATOM 12259 C CA . ASP B 2 662 ? -19.910 8.308 77.998 1.00 110.76 ? 662 ASP B CA 1 ATOM 12260 C C . ASP B 2 662 ? -18.553 8.766 78.524 1.00 100.19 ? 662 ASP B C 1 ATOM 12261 O O . ASP B 2 662 ? -18.421 9.136 79.691 1.00 102.34 ? 662 ASP B O 1 ATOM 12262 C CB . ASP B 2 662 ? -20.776 7.810 79.160 1.00 121.49 ? 662 ASP B CB 1 ATOM 12263 C CG . ASP B 2 662 ? -22.151 7.351 78.713 1.00 139.61 ? 662 ASP B CG 1 ATOM 12264 O OD1 . ASP B 2 662 ? -22.269 6.824 77.587 1.00 136.87 ? 662 ASP B OD1 1 ATOM 12265 O OD2 . ASP B 2 662 ? -23.113 7.519 79.491 1.00 144.57 ? 662 ASP B OD2 1 ATOM 12266 N N . CYS B 2 663 ? -17.547 8.745 77.656 1.00 100.31 ? 663 CYS B N 1 ATOM 12267 C CA . CYS B 2 663 ? -16.216 9.212 78.022 1.00 94.55 ? 663 CYS B CA 1 ATOM 12268 C C . CYS B 2 663 ? -15.928 10.564 77.379 1.00 93.75 ? 663 CYS B C 1 ATOM 12269 O O . CYS B 2 663 ? -16.386 10.847 76.273 1.00 102.09 ? 663 CYS B O 1 ATOM 12270 C CB . CYS B 2 663 ? -15.152 8.193 77.613 1.00 95.94 ? 663 CYS B CB 1 ATOM 12271 S SG . CYS B 2 663 ? -15.202 6.644 78.547 1.00 119.58 ? 663 CYS B SG 1 ATOM 12272 N N . VAL B 2 664 ? -15.164 11.395 78.081 1.00 98.65 ? 664 VAL B N 1 ATOM 12273 C CA . VAL B 2 664 ? -14.835 12.730 77.596 1.00 99.05 ? 664 VAL B CA 1 ATOM 12274 C C . VAL B 2 664 ? -13.550 12.714 76.772 1.00 94.79 ? 664 VAL B C 1 ATOM 12275 O O . VAL B 2 664 ? -12.471 12.417 77.287 1.00 89.62 ? 664 VAL B O 1 ATOM 12276 C CB . VAL B 2 664 ? -14.686 13.728 78.764 1.00 92.74 ? 664 VAL B CB 1 ATOM 12277 C CG1 . VAL B 2 664 ? -14.070 15.028 78.283 1.00 92.83 ? 664 VAL B CG1 1 ATOM 12278 C CG2 . VAL B 2 664 ? -16.034 13.977 79.425 1.00 95.87 ? 664 VAL B CG2 1 ATOM 12279 N N . VAL B 2 665 ? -13.677 13.034 75.488 1.00 88.16 ? 665 VAL B N 1 ATOM 12280 C CA . VAL B 2 665 ? -12.539 13.034 74.574 1.00 86.86 ? 665 VAL B CA 1 ATOM 12281 C C . VAL B 2 665 ? -12.124 14.456 74.215 1.00 100.58 ? 665 VAL B C 1 ATOM 12282 O O . VAL B 2 665 ? -12.944 15.254 73.764 1.00 87.41 ? 665 VAL B O 1 ATOM 12283 C CB . VAL B 2 665 ? -12.854 12.263 73.277 1.00 83.21 ? 665 VAL B CB 1 ATOM 12284 C CG1 . VAL B 2 665 ? -11.666 12.312 72.327 1.00 82.99 ? 665 VAL B CG1 1 ATOM 12285 C CG2 . VAL B 2 665 ? -13.233 10.826 73.591 1.00 82.42 ? 665 VAL B CG2 1 ATOM 12286 N N . ARG B 2 666 ? -10.848 14.766 74.415 1.00 120.09 ? 666 ARG B N 1 ATOM 12287 C CA . ARG B 2 666 ? -10.329 16.091 74.102 1.00 111.15 ? 666 ARG B CA 1 ATOM 12288 C C . ARG B 2 666 ? -9.354 16.020 72.934 1.00 97.48 ? 666 ARG B C 1 ATOM 12289 O O . ARG B 2 666 ? -8.495 15.140 72.889 1.00 88.78 ? 666 ARG B O 1 ATOM 12290 C CB . ARG B 2 666 ? -9.643 16.704 75.325 1.00 121.89 ? 666 ARG B CB 1 ATOM 12291 C CG . ARG B 2 666 ? -10.269 16.298 76.650 1.00 124.93 ? 666 ARG B CG 1 ATOM 12292 C CD . ARG B 2 666 ? -9.718 17.121 77.802 1.00 119.09 ? 666 ARG B CD 1 ATOM 12293 N NE . ARG B 2 666 ? -10.261 18.477 77.805 1.00 129.07 ? 666 ARG B NE 1 ATOM 12294 C CZ . ARG B 2 666 ? -11.339 18.847 78.489 1.00 126.23 ? 666 ARG B CZ 1 ATOM 12295 N NH1 . ARG B 2 666 ? -11.990 17.961 79.232 1.00 121.78 ? 666 ARG B NH1 1 ATOM 12296 N NH2 . ARG B 2 666 ? -11.764 20.101 78.434 1.00 120.11 ? 666 ARG B NH2 1 ATOM 12297 N N . PHE B 2 667 ? -9.490 16.941 71.985 1.00 101.95 ? 667 PHE B N 1 ATOM 12298 C CA . PHE B 2 667 ? -8.584 16.976 70.844 1.00 92.86 ? 667 PHE B CA 1 ATOM 12299 C C . PHE B 2 667 ? -8.460 18.377 70.257 1.00 93.20 ? 667 PHE B C 1 ATOM 12300 O O . PHE B 2 667 ? -9.336 19.221 70.441 1.00 136.11 ? 667 PHE B O 1 ATOM 12301 C CB . PHE B 2 667 ? -9.044 15.992 69.762 1.00 97.53 ? 667 PHE B CB 1 ATOM 12302 C CG . PHE B 2 667 ? -10.293 16.413 69.037 1.00 87.71 ? 667 PHE B CG 1 ATOM 12303 C CD1 . PHE B 2 667 ? -10.214 17.090 67.830 1.00 88.93 ? 667 PHE B CD1 1 ATOM 12304 C CD2 . PHE B 2 667 ? -11.543 16.116 69.551 1.00 105.10 ? 667 PHE B CD2 1 ATOM 12305 C CE1 . PHE B 2 667 ? -11.356 17.475 67.156 1.00 113.17 ? 667 PHE B CE1 1 ATOM 12306 C CE2 . PHE B 2 667 ? -12.691 16.497 68.881 1.00 118.52 ? 667 PHE B CE2 1 ATOM 12307 C CZ . PHE B 2 667 ? -12.597 17.176 67.681 1.00 109.77 ? 667 PHE B CZ 1 ATOM 12308 N N . GLN B 2 668 ? -7.362 18.613 69.548 1.00 94.85 ? 668 GLN B N 1 ATOM 12309 C CA . GLN B 2 668 ? -7.125 19.894 68.894 1.00 100.56 ? 668 GLN B CA 1 ATOM 12310 C C . GLN B 2 668 ? -6.621 19.681 67.474 1.00 102.53 ? 668 GLN B C 1 ATOM 12311 O O . GLN B 2 668 ? -6.117 18.609 67.140 1.00 104.21 ? 668 GLN B O 1 ATOM 12312 C CB . GLN B 2 668 ? -6.115 20.729 69.685 1.00 109.17 ? 668 GLN B CB 1 ATOM 12313 C CG . GLN B 2 668 ? -4.708 20.152 69.679 1.00 130.20 ? 668 GLN B CG 1 ATOM 12314 C CD . GLN B 2 668 ? -3.715 21.015 70.433 1.00 133.29 ? 668 GLN B CD 1 ATOM 12315 O OE1 . GLN B 2 668 ? -4.035 22.128 70.852 1.00 130.97 ? 668 GLN B OE1 1 ATOM 12316 N NE2 . GLN B 2 668 ? -2.501 20.506 70.609 1.00 134.85 ? 668 GLN B NE2 1 ATOM 12317 N N . TYR B 2 669 ? -6.761 20.704 66.639 1.00 107.56 ? 669 TYR B N 1 ATOM 12318 C CA . TYR B 2 669 ? -6.245 20.649 65.278 1.00 119.59 ? 669 TYR B CA 1 ATOM 12319 C C . TYR B 2 669 ? -5.620 21.982 64.885 1.00 124.48 ? 669 TYR B C 1 ATOM 12320 O O . TYR B 2 669 ? -6.181 23.045 65.152 1.00 130.28 ? 669 TYR B O 1 ATOM 12321 C CB . TYR B 2 669 ? -7.352 20.263 64.290 1.00 107.71 ? 669 TYR B CB 1 ATOM 12322 C CG . TYR B 2 669 ? -8.474 21.273 64.162 1.00 121.70 ? 669 TYR B CG 1 ATOM 12323 C CD1 . TYR B 2 669 ? -8.456 22.237 63.160 1.00 139.94 ? 669 TYR B CD1 1 ATOM 12324 C CD2 . TYR B 2 669 ? -9.556 21.254 65.033 1.00 124.31 ? 669 TYR B CD2 1 ATOM 12325 C CE1 . TYR B 2 669 ? -9.479 23.158 63.036 1.00 144.55 ? 669 TYR B CE1 1 ATOM 12326 C CE2 . TYR B 2 669 ? -10.585 22.172 64.915 1.00 133.14 ? 669 TYR B CE2 1 ATOM 12327 C CZ . TYR B 2 669 ? -10.541 23.121 63.914 1.00 138.46 ? 669 TYR B CZ 1 ATOM 12328 O OH . TYR B 2 669 ? -11.560 24.038 63.793 1.00 141.31 ? 669 TYR B OH 1 ATOM 12329 N N . TYR B 2 670 ? -4.450 21.922 64.258 1.00 126.69 ? 670 TYR B N 1 ATOM 12330 C CA . TYR B 2 670 ? -3.770 23.128 63.807 1.00 136.89 ? 670 TYR B CA 1 ATOM 12331 C C . TYR B 2 670 ? -4.468 23.700 62.579 1.00 142.56 ? 670 TYR B C 1 ATOM 12332 O O . TYR B 2 670 ? -4.950 22.957 61.724 1.00 132.10 ? 670 TYR B O 1 ATOM 12333 C CB . TYR B 2 670 ? -2.298 22.837 63.510 1.00 151.17 ? 670 TYR B CB 1 ATOM 12334 C CG . TYR B 2 670 ? -1.465 22.653 64.759 1.00 166.17 ? 670 TYR B CG 1 ATOM 12335 C CD1 . TYR B 2 670 ? -1.868 23.203 65.970 1.00 172.33 ? 670 TYR B CD1 1 ATOM 12336 C CD2 . TYR B 2 670 ? -0.278 21.931 64.730 1.00 174.97 ? 670 TYR B CD2 1 ATOM 12337 C CE1 . TYR B 2 670 ? -1.114 23.042 67.115 1.00 176.93 ? 670 TYR B CE1 1 ATOM 12338 C CE2 . TYR B 2 670 ? 0.484 21.764 65.874 1.00 182.66 ? 670 TYR B CE2 1 ATOM 12339 C CZ . TYR B 2 670 ? 0.061 22.321 67.062 1.00 184.63 ? 670 TYR B CZ 1 ATOM 12340 O OH . TYR B 2 670 ? 0.812 22.160 68.204 1.00 189.95 ? 670 TYR B OH 1 ATOM 12341 N N . GLU B 2 671 ? -4.511 25.026 62.495 1.00 157.83 ? 671 GLU B N 1 ATOM 12342 C CA . GLU B 2 671 ? -5.287 25.703 61.461 1.00 167.16 ? 671 GLU B CA 1 ATOM 12343 C C . GLU B 2 671 ? -4.616 25.600 60.099 1.00 168.56 ? 671 GLU B C 1 ATOM 12344 O O . GLU B 2 671 ? -5.091 24.889 59.214 1.00 159.68 ? 671 GLU B O 1 ATOM 12345 C CB . GLU B 2 671 ? -5.488 27.174 61.834 1.00 175.21 ? 671 GLU B CB 1 ATOM 12346 C CG . GLU B 2 671 ? -6.236 27.996 60.795 1.00 179.03 ? 671 GLU B CG 1 ATOM 12347 C CD . GLU B 2 671 ? -7.734 27.774 60.839 1.00 186.43 ? 671 GLU B CD 1 ATOM 12348 O OE1 . GLU B 2 671 ? -8.212 27.100 61.777 1.00 182.46 ? 671 GLU B OE1 1 ATOM 12349 O OE2 . GLU B 2 671 ? -8.437 28.278 59.937 1.00 192.50 ? 671 GLU B OE2 1 ATOM 12350 N N . ASP B 2 672 ? -3.510 26.318 59.935 0.50 168.46 ? 672 ASP B N 1 ATOM 12351 C CA . ASP B 2 672 ? -2.733 26.245 58.706 0.50 169.21 ? 672 ASP B CA 1 ATOM 12352 C C . ASP B 2 672 ? -1.240 26.195 59.000 0.50 174.77 ? 672 ASP B C 1 ATOM 12353 O O . ASP B 2 672 ? -0.683 27.125 59.585 0.50 182.98 ? 672 ASP B O 1 ATOM 12354 C CB . ASP B 2 672 ? -3.051 27.436 57.799 1.00 178.46 ? 672 ASP B CB 1 ATOM 12355 C CG . ASP B 2 672 ? -2.049 27.592 56.669 1.00 186.08 ? 672 ASP B CG 1 ATOM 12356 O OD1 . ASP B 2 672 ? -1.173 28.476 56.772 1.00 183.81 ? 672 ASP B OD1 1 ATOM 12357 O OD2 . ASP B 2 672 ? -2.135 26.831 55.683 1.00 185.90 ? 672 ASP B OD2 1 ATOM 12358 N N . SER B 2 673 ? -0.595 25.107 58.596 1.00 173.99 ? 673 SER B N 1 ATOM 12359 C CA . SER B 2 673 ? 0.855 25.009 58.683 1.00 187.50 ? 673 SER B CA 1 ATOM 12360 C C . SER B 2 673 ? 1.426 24.902 57.276 1.00 201.63 ? 673 SER B C 1 ATOM 12361 O O . SER B 2 673 ? 1.957 25.870 56.733 1.00 203.68 ? 673 SER B O 1 ATOM 12362 C CB . SER B 2 673 ? 1.268 23.806 59.533 1.00 177.93 ? 673 SER B CB 1 ATOM 12363 O OG . SER B 2 673 ? 2.676 23.704 59.628 1.00 185.26 ? 673 SER B OG 1 ATOM 12364 N N . SER B 2 674 ? 1.312 23.714 56.693 1.00 203.03 ? 674 SER B N 1 ATOM 12365 C CA . SER B 2 674 ? 1.519 23.537 55.263 1.00 199.20 ? 674 SER B CA 1 ATOM 12366 C C . SER B 2 674 ? 0.164 23.496 54.571 1.00 186.05 ? 674 SER B C 1 ATOM 12367 O O . SER B 2 674 ? 0.074 23.344 53.353 1.00 181.05 ? 674 SER B O 1 ATOM 12368 C CB . SER B 2 674 ? 2.309 22.260 54.976 1.00 194.90 ? 674 SER B CB 1 ATOM 12369 O OG . SER B 2 674 ? 2.485 22.075 53.581 1.00 195.14 ? 674 SER B OG 1 ATOM 12370 N N . GLY B 2 675 ? -0.890 23.638 55.368 1.00 178.50 ? 675 GLY B N 1 ATOM 12371 C CA . GLY B 2 675 ? -2.242 23.395 54.907 1.00 176.54 ? 675 GLY B CA 1 ATOM 12372 C C . GLY B 2 675 ? -2.615 21.969 55.262 1.00 178.02 ? 675 GLY B C 1 ATOM 12373 O O . GLY B 2 675 ? -3.640 21.447 54.825 1.00 179.70 ? 675 GLY B O 1 ATOM 12374 N N . LYS B 2 676 ? -1.759 21.341 56.066 1.00 173.80 ? 676 LYS B N 1 ATOM 12375 C CA . LYS B 2 676 ? -1.924 19.946 56.459 1.00 165.90 ? 676 LYS B CA 1 ATOM 12376 C C . LYS B 2 676 ? -3.162 19.715 57.319 1.00 166.12 ? 676 LYS B C 1 ATOM 12377 O O . LYS B 2 676 ? -3.885 18.736 57.120 1.00 168.90 ? 676 LYS B O 1 ATOM 12378 C CB . LYS B 2 676 ? -0.683 19.459 57.213 1.00 167.10 ? 676 LYS B CB 1 ATOM 12379 C CG . LYS B 2 676 ? 0.533 19.202 56.334 1.00 173.57 ? 676 LYS B CG 1 ATOM 12380 C CD . LYS B 2 676 ? 1.709 18.707 57.164 1.00 179.60 ? 676 LYS B CD 1 ATOM 12381 C CE . LYS B 2 676 ? 2.816 18.143 56.287 1.00 185.09 ? 676 LYS B CE 1 ATOM 12382 N NZ . LYS B 2 676 ? 3.349 19.148 55.327 1.00 186.87 ? 676 LYS B NZ 1 ATOM 12383 N N . SER B 2 677 ? -3.393 20.617 58.272 1.00 163.59 ? 677 SER B N 1 ATOM 12384 C CA . SER B 2 677 ? -4.496 20.496 59.225 1.00 159.52 ? 677 SER B CA 1 ATOM 12385 C C . SER B 2 677 ? -4.414 19.177 59.989 1.00 153.53 ? 677 SER B C 1 ATOM 12386 O O . SER B 2 677 ? -5.239 18.284 59.799 1.00 159.88 ? 677 SER B O 1 ATOM 12387 C CB . SER B 2 677 ? -5.847 20.618 58.513 1.00 154.90 ? 677 SER B CB 1 ATOM 12388 O OG . SER B 2 677 ? -5.939 21.838 57.799 1.00 168.52 ? 677 SER B OG 1 ATOM 12389 N N . ILE B 2 678 ? -3.408 19.065 60.850 1.00 138.13 ? 678 ILE B N 1 ATOM 12390 C CA . ILE B 2 678 ? -3.149 17.827 61.576 1.00 131.68 ? 678 ILE B CA 1 ATOM 12391 C C . ILE B 2 678 ? -3.989 17.727 62.852 1.00 121.28 ? 678 ILE B C 1 ATOM 12392 O O . ILE B 2 678 ? -4.177 18.713 63.566 1.00 120.39 ? 678 ILE B O 1 ATOM 12393 C CB . ILE B 2 678 ? -1.644 17.696 61.922 1.00 147.39 ? 678 ILE B CB 1 ATOM 12394 C CG1 . ILE B 2 678 ? -1.356 16.371 62.634 1.00 151.93 ? 678 ILE B CG1 1 ATOM 12395 C CG2 . ILE B 2 678 ? -1.168 18.884 62.750 1.00 146.02 ? 678 ILE B CG2 1 ATOM 12396 C CD1 . ILE B 2 678 ? 0.114 16.123 62.889 1.00 157.80 ? 678 ILE B CD1 1 ATOM 12397 N N . LEU B 2 679 ? -4.505 16.531 63.120 1.00 118.94 ? 679 LEU B N 1 ATOM 12398 C CA . LEU B 2 679 ? -5.332 16.290 64.298 1.00 108.31 ? 679 LEU B CA 1 ATOM 12399 C C . LEU B 2 679 ? -4.521 15.707 65.452 1.00 105.92 ? 679 LEU B C 1 ATOM 12400 O O . LEU B 2 679 ? -3.736 14.778 65.262 1.00 108.32 ? 679 LEU B O 1 ATOM 12401 C CB . LEU B 2 679 ? -6.491 15.350 63.953 1.00 100.81 ? 679 LEU B CB 1 ATOM 12402 C CG . LEU B 2 679 ? -7.839 15.969 63.570 1.00 106.34 ? 679 LEU B CG 1 ATOM 12403 C CD1 . LEU B 2 679 ? -8.433 16.716 64.752 1.00 113.59 ? 679 LEU B CD1 1 ATOM 12404 C CD2 . LEU B 2 679 ? -7.710 16.885 62.362 1.00 126.22 ? 679 LEU B CD2 1 ATOM 12405 N N . TYR B 2 680 ? -4.717 16.260 66.644 1.00 104.19 ? 680 TYR B N 1 ATOM 12406 C CA . TYR B 2 680 ? -4.088 15.737 67.852 1.00 105.38 ? 680 TYR B CA 1 ATOM 12407 C C . TYR B 2 680 ? -5.146 15.291 68.853 1.00 97.27 ? 680 TYR B C 1 ATOM 12408 O O . TYR B 2 680 ? -5.859 16.118 69.417 1.00 103.24 ? 680 TYR B O 1 ATOM 12409 C CB . TYR B 2 680 ? -3.177 16.789 68.492 1.00 129.12 ? 680 TYR B CB 1 ATOM 12410 C CG . TYR B 2 680 ? -1.839 16.952 67.809 1.00 132.90 ? 680 TYR B CG 1 ATOM 12411 C CD1 . TYR B 2 680 ? -1.287 15.917 67.066 1.00 134.78 ? 680 TYR B CD1 1 ATOM 12412 C CD2 . TYR B 2 680 ? -1.126 18.138 67.912 1.00 137.14 ? 680 TYR B CD2 1 ATOM 12413 C CE1 . TYR B 2 680 ? -0.064 16.061 66.443 1.00 141.84 ? 680 TYR B CE1 1 ATOM 12414 C CE2 . TYR B 2 680 ? 0.099 18.292 67.290 1.00 148.88 ? 680 TYR B CE2 1 ATOM 12415 C CZ . TYR B 2 680 ? 0.625 17.249 66.557 1.00 152.32 ? 680 TYR B CZ 1 ATOM 12416 O OH . TYR B 2 680 ? 1.844 17.392 65.936 1.00 167.30 ? 680 TYR B OH 1 ATOM 12417 N N . VAL B 2 681 ? -5.235 13.984 69.079 1.00 103.12 ? 681 VAL B N 1 ATOM 12418 C CA . VAL B 2 681 ? -6.210 13.432 70.012 1.00 90.67 ? 681 VAL B CA 1 ATOM 12419 C C . VAL B 2 681 ? -5.531 12.976 71.297 1.00 90.02 ? 681 VAL B C 1 ATOM 12420 O O . VAL B 2 681 ? -4.555 12.227 71.260 1.00 114.50 ? 681 VAL B O 1 ATOM 12421 C CB . VAL B 2 681 ? -6.974 12.245 69.394 1.00 85.27 ? 681 VAL B CB 1 ATOM 12422 C CG1 . VAL B 2 681 ? -7.893 11.605 70.425 1.00 84.25 ? 681 VAL B CG1 1 ATOM 12423 C CG2 . VAL B 2 681 ? -7.766 12.701 68.179 1.00 92.69 ? 681 VAL B CG2 1 ATOM 12424 N N . VAL B 2 682 ? -6.050 13.431 72.432 1.00 90.06 ? 682 VAL B N 1 ATOM 12425 C CA . VAL B 2 682 ? -5.482 13.069 73.722 1.00 94.15 ? 682 VAL B CA 1 ATOM 12426 C C . VAL B 2 682 ? -5.798 11.619 74.068 1.00 105.18 ? 682 VAL B C 1 ATOM 12427 O O . VAL B 2 682 ? -6.960 11.213 74.083 1.00 108.65 ? 682 VAL B O 1 ATOM 12428 C CB . VAL B 2 682 ? -6.006 13.983 74.847 1.00 99.90 ? 682 VAL B CB 1 ATOM 12429 C CG1 . VAL B 2 682 ? -5.391 13.593 76.182 1.00 98.35 ? 682 VAL B CG1 1 ATOM 12430 C CG2 . VAL B 2 682 ? -5.710 15.439 74.528 1.00 99.36 ? 682 VAL B CG2 1 ATOM 12431 N N . GLU B 2 683 ? -4.754 10.839 74.336 1.00 110.90 ? 683 GLU B N 1 ATOM 12432 C CA . GLU B 2 683 ? -4.923 9.468 74.796 1.00 92.11 ? 683 GLU B CA 1 ATOM 12433 C C . GLU B 2 683 ? -5.499 9.469 76.204 1.00 109.07 ? 683 GLU B C 1 ATOM 12434 O O . GLU B 2 683 ? -5.412 10.472 76.914 1.00 145.59 ? 683 GLU B O 1 ATOM 12435 C CB . GLU B 2 683 ? -3.593 8.714 74.763 1.00 100.17 ? 683 GLU B CB 1 ATOM 12436 C CG . GLU B 2 683 ? -3.088 8.393 73.367 1.00 152.03 ? 683 GLU B CG 1 ATOM 12437 C CD . GLU B 2 683 ? -3.326 6.945 72.974 1.00 182.97 ? 683 GLU B CD 1 ATOM 12438 O OE1 . GLU B 2 683 ? -4.272 6.329 73.508 1.00 210.78 ? 683 GLU B OE1 1 ATOM 12439 O OE2 . GLU B 2 683 ? -2.561 6.421 72.138 1.00 158.70 ? 683 GLU B OE2 1 ATOM 12440 N N . GLU B 2 684 ? -6.089 8.345 76.598 1.00 92.66 ? 684 GLU B N 1 ATOM 12441 C CA . GLU B 2 684 ? -6.736 8.214 77.902 1.00 116.52 ? 684 GLU B CA 1 ATOM 12442 C C . GLU B 2 684 ? -7.823 9.265 78.133 1.00 98.23 ? 684 GLU B C 1 ATOM 12443 O O . GLU B 2 684 ? -7.645 10.172 78.946 1.00 94.78 ? 684 GLU B O 1 ATOM 12444 C CB . GLU B 2 684 ? -5.699 8.296 79.027 1.00 112.83 ? 684 GLU B CB 1 ATOM 12445 C CG . GLU B 2 684 ? -4.673 7.176 79.027 1.00 132.79 ? 684 GLU B CG 1 ATOM 12446 C CD . GLU B 2 684 ? -5.171 5.922 79.721 1.00 146.46 ? 684 GLU B CD 1 ATOM 12447 O OE1 . GLU B 2 684 ? -6.400 5.773 79.887 1.00 145.23 ? 684 GLU B OE1 1 ATOM 12448 O OE2 . GLU B 2 684 ? -4.328 5.085 80.108 1.00 154.83 ? 684 GLU B OE2 1 ATOM 12449 N N . PRO B 2 685 ? -8.949 9.153 77.409 1.00 89.63 ? 685 PRO B N 1 ATOM 12450 C CA . PRO B 2 685 ? -10.096 10.028 77.665 1.00 91.64 ? 685 PRO B CA 1 ATOM 12451 C C . PRO B 2 685 ? -10.619 9.868 79.089 1.00 93.24 ? 685 PRO B C 1 ATOM 12452 O O . PRO B 2 685 ? -10.443 8.808 79.691 1.00 110.05 ? 685 PRO B O 1 ATOM 12453 C CB . PRO B 2 685 ? -11.136 9.552 76.646 1.00 100.06 ? 685 PRO B CB 1 ATOM 12454 C CG . PRO B 2 685 ? -10.341 8.912 75.566 1.00 85.77 ? 685 PRO B CG 1 ATOM 12455 C CD . PRO B 2 685 ? -9.189 8.261 76.262 1.00 87.94 ? 685 PRO B CD 1 ATOM 12456 N N . GLU B 2 686 ? -11.253 10.908 79.619 1.00 95.14 ? 686 GLU B N 1 ATOM 12457 C CA . GLU B 2 686 ? -11.777 10.860 80.977 1.00 104.18 ? 686 GLU B CA 1 ATOM 12458 C C . GLU B 2 686 ? -13.011 9.967 81.050 1.00 105.68 ? 686 GLU B C 1 ATOM 12459 O O . GLU B 2 686 ? -13.982 10.168 80.321 1.00 106.63 ? 686 GLU B O 1 ATOM 12460 C CB . GLU B 2 686 ? -12.110 12.268 81.475 1.00 111.39 ? 686 GLU B CB 1 ATOM 12461 C CG . GLU B 2 686 ? -10.938 13.235 81.422 1.00 127.49 ? 686 GLU B CG 1 ATOM 12462 C CD . GLU B 2 686 ? -11.255 14.574 82.057 1.00 150.92 ? 686 GLU B CD 1 ATOM 12463 O OE1 . GLU B 2 686 ? -11.868 14.587 83.146 1.00 162.09 ? 686 GLU B OE1 1 ATOM 12464 O OE2 . GLU B 2 686 ? -10.897 15.615 81.467 1.00 151.95 ? 686 GLU B OE2 1 ATOM 12465 N N . CYS B 2 687 ? -12.961 8.979 81.937 1.00 105.65 ? 687 CYS B N 1 ATOM 12466 C CA . CYS B 2 687 ? -14.054 8.029 82.104 1.00 107.72 ? 687 CYS B CA 1 ATOM 12467 C C . CYS B 2 687 ? -14.440 7.919 83.576 1.00 115.50 ? 687 CYS B C 1 ATOM 12468 O O . CYS B 2 687 ? -13.642 8.256 84.450 1.00 119.65 ? 687 CYS B O 1 ATOM 12469 C CB . CYS B 2 687 ? -13.657 6.660 81.543 1.00 105.04 ? 687 CYS B CB 1 ATOM 12470 S SG . CYS B 2 687 ? -13.557 6.594 79.740 1.00 120.83 ? 687 CYS B SG 1 ATOM 12471 N N . PRO B 2 688 ? -15.670 7.452 83.859 1.00 117.99 ? 688 PRO B N 1 ATOM 12472 C CA . PRO B 2 688 ? -16.107 7.318 85.254 1.00 124.76 ? 688 PRO B CA 1 ATOM 12473 C C . PRO B 2 688 ? -15.289 6.300 86.047 1.00 139.15 ? 688 PRO B C 1 ATOM 12474 O O . PRO B 2 688 ? -14.396 5.653 85.498 1.00 148.34 ? 688 PRO B O 1 ATOM 12475 C CB . PRO B 2 688 ? -17.566 6.858 85.123 1.00 123.38 ? 688 PRO B CB 1 ATOM 12476 C CG . PRO B 2 688 ? -17.666 6.281 83.749 1.00 118.93 ? 688 PRO B CG 1 ATOM 12477 C CD . PRO B 2 688 ? -16.747 7.111 82.915 1.00 114.99 ? 688 PRO B CD 1 ATOM 12478 N N . LYS B 2 689 ? -15.606 6.155 87.330 1.00 145.22 ? 689 LYS B N 1 ATOM 12479 C CA . LYS B 2 689 ? -14.838 5.286 88.213 1.00 154.37 ? 689 LYS B CA 1 ATOM 12480 C C . LYS B 2 689 ? -15.680 4.125 88.731 1.00 159.39 ? 689 LYS B C 1 ATOM 12481 O O . LYS B 2 689 ? -16.904 4.221 88.815 1.00 164.10 ? 689 LYS B O 1 ATOM 12482 C CB . LYS B 2 689 ? -14.275 6.089 89.388 1.00 157.60 ? 689 LYS B CB 1 ATOM 12483 C CG . LYS B 2 689 ? -13.576 7.377 88.980 1.00 151.19 ? 689 LYS B CG 1 ATOM 12484 C CD . LYS B 2 689 ? -12.412 7.107 88.040 1.00 155.11 ? 689 LYS B CD 1 ATOM 12485 C CE . LYS B 2 689 ? -11.325 6.289 88.720 1.00 162.27 ? 689 LYS B CE 1 ATOM 12486 N NZ . LYS B 2 689 ? -10.181 6.020 87.806 1.00 156.65 ? 689 LYS B NZ 1 ATOM 12487 N N . GLY B 2 690 ? -15.015 3.027 89.077 1.00 154.43 ? 690 GLY B N 1 ATOM 12488 C CA . GLY B 2 690 ? -15.695 1.852 89.589 1.00 155.41 ? 690 GLY B CA 1 ATOM 12489 C C . GLY B 2 690 ? -15.197 1.444 90.961 1.00 160.04 ? 690 GLY B C 1 ATOM 12490 O O . GLY B 2 690 ? -15.490 2.102 91.960 1.00 159.93 ? 690 GLY B O 1 ATOM 12491 N N . VAL C 3 74 ? 18.891 41.659 53.186 1.00 147.81 ? 1490 VAL C N 1 ATOM 12492 C CA . VAL C 3 74 ? 17.747 42.394 53.712 1.00 146.02 ? 1490 VAL C CA 1 ATOM 12493 C C . VAL C 3 74 ? 17.287 43.480 52.743 1.00 133.33 ? 1490 VAL C C 1 ATOM 12494 O O . VAL C 3 74 ? 16.089 43.669 52.533 1.00 115.56 ? 1490 VAL C O 1 ATOM 12495 C CB . VAL C 3 74 ? 18.066 43.031 55.083 1.00 142.64 ? 1490 VAL C CB 1 ATOM 12496 C CG1 . VAL C 3 74 ? 17.912 42.005 56.196 1.00 126.98 ? 1490 VAL C CG1 1 ATOM 12497 C CG2 . VAL C 3 74 ? 19.468 43.626 55.088 1.00 135.60 ? 1490 VAL C CG2 1 ATOM 12498 N N . ILE C 3 75 ? 18.244 44.192 52.157 1.00 137.00 ? 1491 ILE C N 1 ATOM 12499 C CA . ILE C 3 75 ? 17.935 45.232 51.183 1.00 141.24 ? 1491 ILE C CA 1 ATOM 12500 C C . ILE C 3 75 ? 18.834 45.129 49.956 1.00 132.64 ? 1491 ILE C C 1 ATOM 12501 O O . ILE C 3 75 ? 20.059 45.227 50.060 1.00 154.14 ? 1491 ILE C O 1 ATOM 12502 C CB . ILE C 3 75 ? 18.075 46.643 51.788 1.00 160.85 ? 1491 ILE C CB 1 ATOM 12503 C CG1 . ILE C 3 75 ? 16.964 46.897 52.809 1.00 165.71 ? 1491 ILE C CG1 1 ATOM 12504 C CG2 . ILE C 3 75 ? 18.024 47.697 50.693 1.00 162.79 ? 1491 ILE C CG2 1 ATOM 12505 C CD1 . ILE C 3 75 ? 16.957 48.303 53.364 1.00 158.53 ? 1491 ILE C CD1 1 ATOM 12506 N N . ALA C 3 76 ? 18.200 44.953 48.800 1.00 217.57 ? 1492 ALA C N 1 ATOM 12507 C CA . ALA C 3 76 ? 18.881 44.825 47.516 1.00 160.67 ? 1492 ALA C CA 1 ATOM 12508 C C . ALA C 3 76 ? 17.839 44.722 46.409 1.00 137.80 ? 1492 ALA C C 1 ATOM 12509 O O . ALA C 3 76 ? 16.671 44.440 46.674 1.00 128.48 ? 1492 ALA C O 1 ATOM 12510 C CB . ALA C 3 76 ? 19.798 43.606 47.499 1.00 138.06 ? 1492 ALA C CB 1 ATOM 12511 N N . ARG C 3 77 ? 18.262 44.944 45.169 1.00 121.25 ? 1493 ARG C N 1 ATOM 12512 C CA . ARG C 3 77 ? 17.339 44.903 44.040 1.00 106.76 ? 1493 ARG C CA 1 ATOM 12513 C C . ARG C 3 77 ? 18.027 44.442 42.759 1.00 108.62 ? 1493 ARG C C 1 ATOM 12514 O O . ARG C 3 77 ? 19.254 44.467 42.655 1.00 110.15 ? 1493 ARG C O 1 ATOM 12515 C CB . ARG C 3 77 ? 16.689 46.274 43.837 1.00 102.55 ? 1493 ARG C CB 1 ATOM 12516 C CG . ARG C 3 77 ? 17.575 47.450 44.206 1.00 110.52 ? 1493 ARG C CG 1 ATOM 12517 C CD . ARG C 3 77 ? 16.765 48.525 44.915 1.00 120.00 ? 1493 ARG C CD 1 ATOM 12518 N NE . ARG C 3 77 ? 15.596 48.928 44.139 1.00 110.30 ? 1493 ARG C NE 1 ATOM 12519 C CZ . ARG C 3 77 ? 15.509 50.064 43.455 1.00 110.55 ? 1493 ARG C CZ 1 ATOM 12520 N NH1 . ARG C 3 77 ? 16.521 50.921 43.454 1.00 112.70 ? 1493 ARG C NH1 1 ATOM 12521 N NH2 . ARG C 3 77 ? 14.407 50.346 42.773 1.00 122.89 ? 1493 ARG C NH2 1 ATOM 12522 N N . GLY C 3 78 ? 17.226 44.024 41.783 1.00 104.46 ? 1494 GLY C N 1 ATOM 12523 C CA . GLY C 3 78 ? 17.749 43.367 40.601 1.00 97.63 ? 1494 GLY C CA 1 ATOM 12524 C C . GLY C 3 78 ? 18.097 41.946 40.988 1.00 102.96 ? 1494 GLY C C 1 ATOM 12525 O O . GLY C 3 78 ? 17.453 41.372 41.865 1.00 90.60 ? 1494 GLY C O 1 ATOM 12526 N N . ASP C 3 79 ? 19.114 41.371 40.358 1.00 116.06 ? 1495 ASP C N 1 ATOM 12527 C CA . ASP C 3 79 ? 19.584 40.064 40.788 1.00 88.65 ? 1495 ASP C CA 1 ATOM 12528 C C . ASP C 3 79 ? 20.846 40.244 41.621 1.00 107.53 ? 1495 ASP C C 1 ATOM 12529 O O . ASP C 3 79 ? 21.931 40.487 41.087 1.00 137.00 ? 1495 ASP C O 1 ATOM 12530 C CB . ASP C 3 79 ? 19.843 39.157 39.583 1.00 86.69 ? 1495 ASP C CB 1 ATOM 12531 C CG . ASP C 3 79 ? 20.524 37.856 39.960 1.00 91.02 ? 1495 ASP C CG 1 ATOM 12532 O OD1 . ASP C 3 79 ? 20.255 37.328 41.058 1.00 109.72 ? 1495 ASP C OD1 1 ATOM 12533 O OD2 . ASP C 3 79 ? 21.330 37.359 39.146 1.00 90.35 ? 1495 ASP C OD2 1 ATOM 12534 N N . TRP C 3 80 ? 20.678 40.083 42.931 1.00 97.02 ? 1496 TRP C N 1 ATOM 12535 C CA . TRP C 3 80 ? 21.713 40.336 43.926 1.00 116.56 ? 1496 TRP C CA 1 ATOM 12536 C C . TRP C 3 80 ? 21.107 40.153 45.314 1.00 140.03 ? 1496 TRP C C 1 ATOM 12537 O O . TRP C 3 80 ? 19.885 40.204 45.466 1.00 141.35 ? 1496 TRP C O 1 ATOM 12538 C CB . TRP C 3 80 ? 22.284 41.751 43.781 1.00 126.50 ? 1496 TRP C CB 1 ATOM 12539 C CG . TRP C 3 80 ? 23.540 41.990 44.557 1.00 135.40 ? 1496 TRP C CG 1 ATOM 12540 C CD1 . TRP C 3 80 ? 23.644 42.531 45.805 1.00 134.80 ? 1496 TRP C CD1 1 ATOM 12541 C CD2 . TRP C 3 80 ? 24.877 41.703 44.132 1.00 145.32 ? 1496 TRP C CD2 1 ATOM 12542 N NE1 . TRP C 3 80 ? 24.961 42.593 46.186 1.00 146.11 ? 1496 TRP C NE1 1 ATOM 12543 C CE2 . TRP C 3 80 ? 25.739 42.091 45.176 1.00 153.63 ? 1496 TRP C CE2 1 ATOM 12544 C CE3 . TRP C 3 80 ? 25.428 41.151 42.972 1.00 146.09 ? 1496 TRP C CE3 1 ATOM 12545 C CZ2 . TRP C 3 80 ? 27.121 41.947 45.095 1.00 154.95 ? 1496 TRP C CZ2 1 ATOM 12546 C CZ3 . TRP C 3 80 ? 26.801 41.009 42.892 1.00 145.91 ? 1496 TRP C CZ3 1 ATOM 12547 C CH2 . TRP C 3 80 ? 27.631 41.405 43.947 1.00 146.37 ? 1496 TRP C CH2 1 ATOM 12548 N N . ASN C 3 81 ? 21.958 39.965 46.319 1.00 154.14 ? 1497 ASN C N 1 ATOM 12549 C CA . ASN C 3 81 ? 21.523 39.889 47.714 1.00 149.53 ? 1497 ASN C CA 1 ATOM 12550 C C . ASN C 3 81 ? 22.710 39.873 48.671 1.00 147.03 ? 1497 ASN C C 1 ATOM 12551 O O . ASN C 3 81 ? 23.819 40.266 48.307 1.00 142.60 ? 1497 ASN C O 1 ATOM 12552 C CB . ASN C 3 81 ? 20.645 38.656 47.952 1.00 146.00 ? 1497 ASN C CB 1 ATOM 12553 C CG . ASN C 3 81 ? 21.206 37.406 47.307 1.00 155.75 ? 1497 ASN C CG 1 ATOM 12554 O OD1 . ASN C 3 81 ? 22.373 37.362 46.919 1.00 166.37 ? 1497 ASN C OD1 1 ATOM 12555 N ND2 . ASN C 3 81 ? 20.372 36.379 47.187 1.00 144.47 ? 1497 ASN C ND2 1 HETATM 12556 C C1 . NAG D 4 . ? 22.075 44.914 7.582 1.00 69.95 ? 1001 NAG A C1 1 HETATM 12557 C C2 . NAG D 4 . ? 21.260 43.634 7.448 1.00 86.75 ? 1001 NAG A C2 1 HETATM 12558 C C3 . NAG D 4 . ? 21.844 42.541 8.345 1.00 99.73 ? 1001 NAG A C3 1 HETATM 12559 C C4 . NAG D 4 . ? 23.352 42.402 8.156 1.00 101.56 ? 1001 NAG A C4 1 HETATM 12560 C C5 . NAG D 4 . ? 24.044 43.767 8.174 1.00 81.92 ? 1001 NAG A C5 1 HETATM 12561 C C6 . NAG D 4 . ? 25.503 43.707 7.782 1.00 89.20 ? 1001 NAG A C6 1 HETATM 12562 C C7 . NAG D 4 . ? 18.954 44.289 6.900 1.00 87.61 ? 1001 NAG A C7 1 HETATM 12563 C C8 . NAG D 4 . ? 17.565 44.483 7.429 1.00 75.51 ? 1001 NAG A C8 1 HETATM 12564 N N2 . NAG D 4 . ? 19.865 43.873 7.786 1.00 80.78 ? 1001 NAG A N2 1 HETATM 12565 O O3 . NAG D 4 . ? 21.205 41.303 8.055 1.00 90.24 ? 1001 NAG A O3 1 HETATM 12566 O O4 . NAG D 4 . ? 23.866 41.633 9.238 1.00 126.96 ? 1001 NAG A O4 1 HETATM 12567 O O5 . NAG D 4 . ? 23.410 44.655 7.245 1.00 76.37 ? 1001 NAG A O5 1 HETATM 12568 O O6 . NAG D 4 . ? 25.940 44.937 7.220 1.00 110.45 ? 1001 NAG A O6 1 HETATM 12569 O O7 . NAG D 4 . ? 19.239 44.499 5.725 1.00 108.16 ? 1001 NAG A O7 1 HETATM 12570 C C1 . NAG E 4 . ? 24.661 40.511 8.813 1.00 139.40 ? 1002 NAG A C1 1 HETATM 12571 C C2 . NAG E 4 . ? 25.331 39.924 10.051 1.00 151.93 ? 1002 NAG A C2 1 HETATM 12572 C C3 . NAG E 4 . ? 26.223 38.752 9.659 1.00 162.12 ? 1002 NAG A C3 1 HETATM 12573 C C4 . NAG E 4 . ? 25.427 37.729 8.859 1.00 168.87 ? 1002 NAG A C4 1 HETATM 12574 C C5 . NAG E 4 . ? 24.741 38.406 7.675 1.00 154.26 ? 1002 NAG A C5 1 HETATM 12575 C C6 . NAG E 4 . ? 23.836 37.474 6.903 1.00 143.85 ? 1002 NAG A C6 1 HETATM 12576 C C7 . NAG E 4 . ? 25.789 41.353 11.998 1.00 172.65 ? 1002 NAG A C7 1 HETATM 12577 C C8 . NAG E 4 . ? 24.587 40.715 12.631 1.00 170.53 ? 1002 NAG A C8 1 HETATM 12578 N N2 . NAG E 4 . ? 26.095 40.936 10.765 1.00 158.54 ? 1002 NAG A N2 1 HETATM 12579 O O3 . NAG E 4 . ? 26.755 38.154 10.836 1.00 164.84 ? 1002 NAG A O3 1 HETATM 12580 O O4 . NAG E 4 . ? 26.290 36.702 8.383 1.00 182.59 ? 1002 NAG A O4 1 HETATM 12581 O O5 . NAG E 4 . ? 23.921 39.491 8.138 1.00 148.00 ? 1002 NAG A O5 1 HETATM 12582 O O6 . NAG E 4 . ? 22.580 38.079 6.629 1.00 142.92 ? 1002 NAG A O6 1 HETATM 12583 O O7 . NAG E 4 . ? 26.451 42.207 12.578 1.00 180.10 ? 1002 NAG A O7 1 HETATM 12584 C C1 . BMA F 5 . ? 26.101 35.528 9.195 1.00 189.94 ? 1003 BMA A C1 1 HETATM 12585 C C2 . BMA F 5 . ? 26.210 34.275 8.327 1.00 186.52 ? 1003 BMA A C2 1 HETATM 12586 C C3 . BMA F 5 . ? 26.014 33.029 9.197 1.00 194.19 ? 1003 BMA A C3 1 HETATM 12587 C C4 . BMA F 5 . ? 26.904 33.072 10.455 1.00 193.90 ? 1003 BMA A C4 1 HETATM 12588 C C5 . BMA F 5 . ? 26.718 34.404 11.203 1.00 191.07 ? 1003 BMA A C5 1 HETATM 12589 C C6 . BMA F 5 . ? 27.651 34.547 12.391 1.00 180.54 ? 1003 BMA A C6 1 HETATM 12590 O O2 . BMA F 5 . ? 27.508 34.176 7.760 1.00 176.92 ? 1003 BMA A O2 1 HETATM 12591 O O3 . BMA F 5 . ? 26.264 31.824 8.473 1.00 198.60 ? 1003 BMA A O3 1 HETATM 12592 O O4 . BMA F 5 . ? 26.575 31.996 11.319 1.00 193.46 ? 1003 BMA A O4 1 HETATM 12593 O O5 . BMA F 5 . ? 26.988 35.481 10.292 1.00 196.95 ? 1003 BMA A O5 1 HETATM 12594 O O6 . BMA F 5 . ? 27.474 35.844 12.944 1.00 175.99 ? 1003 BMA A O6 1 HETATM 12595 C C1 . MAN G 6 . ? 25.375 31.737 7.343 1.00 203.88 ? 1004 MAN A C1 1 HETATM 12596 C C2 . MAN G 6 . ? 24.551 30.434 7.425 1.00 203.74 ? 1004 MAN A C2 1 HETATM 12597 C C3 . MAN G 6 . ? 25.393 29.233 6.981 1.00 203.71 ? 1004 MAN A C3 1 HETATM 12598 C C4 . MAN G 6 . ? 26.102 29.520 5.647 1.00 202.08 ? 1004 MAN A C4 1 HETATM 12599 C C5 . MAN G 6 . ? 26.940 30.794 5.785 1.00 202.99 ? 1004 MAN A C5 1 HETATM 12600 C C6 . MAN G 6 . ? 27.668 31.169 4.508 1.00 199.27 ? 1004 MAN A C6 1 HETATM 12601 O O2 . MAN G 6 . ? 23.435 30.469 6.533 1.00 198.45 ? 1004 MAN A O2 1 HETATM 12602 O O3 . MAN G 6 . ? 24.608 28.051 6.873 1.00 201.84 ? 1004 MAN A O3 1 HETATM 12603 O O4 . MAN G 6 . ? 26.945 28.433 5.302 1.00 197.55 ? 1004 MAN A O4 1 HETATM 12604 O O5 . MAN G 6 . ? 26.058 31.883 6.122 1.00 205.90 ? 1004 MAN A O5 1 HETATM 12605 O O6 . MAN G 6 . ? 26.713 31.677 3.582 1.00 198.10 ? 1004 MAN A O6 1 HETATM 12606 C C1 . NAG H 4 . ? -1.489 69.325 41.308 1.00 111.42 ? 1005 NAG A C1 1 HETATM 12607 C C2 . NAG H 4 . ? -1.426 69.941 42.707 1.00 132.02 ? 1005 NAG A C2 1 HETATM 12608 C C3 . NAG H 4 . ? -2.354 71.151 42.794 1.00 149.64 ? 1005 NAG A C3 1 HETATM 12609 C C4 . NAG H 4 . ? -3.786 70.749 42.467 1.00 141.22 ? 1005 NAG A C4 1 HETATM 12610 C C5 . NAG H 4 . ? -3.817 69.892 41.205 1.00 126.87 ? 1005 NAG A C5 1 HETATM 12611 C C6 . NAG H 4 . ? -4.837 70.362 40.195 1.00 133.03 ? 1005 NAG A C6 1 HETATM 12612 C C7 . NAG H 4 . ? -1.435 69.099 45.015 1.00 162.58 ? 1005 NAG A C7 1 HETATM 12613 C C8 . NAG H 4 . ? -1.869 67.992 45.927 1.00 166.70 ? 1005 NAG A C8 1 HETATM 12614 N N2 . NAG H 4 . ? -1.768 68.961 43.726 1.00 148.23 ? 1005 NAG A N2 1 HETATM 12615 O O3 . NAG H 4 . ? -1.909 72.154 41.887 1.00 162.61 ? 1005 NAG A O3 1 HETATM 12616 O O4 . NAG H 4 . ? -4.346 70.009 43.547 1.00 146.89 ? 1005 NAG A O4 1 HETATM 12617 O O5 . NAG H 4 . ? -2.538 69.944 40.557 1.00 114.20 ? 1005 NAG A O5 1 HETATM 12618 O O6 . NAG H 4 . ? -5.136 69.345 39.248 1.00 133.37 ? 1005 NAG A O6 1 HETATM 12619 O O7 . NAG H 4 . ? -0.811 70.073 45.425 1.00 164.95 ? 1005 NAG A O7 1 HETATM 12620 C C1 . NAG I 4 . ? -5.025 70.914 44.435 1.00 163.18 ? 1006 NAG A C1 1 HETATM 12621 C C2 . NAG I 4 . ? -6.531 70.659 44.378 1.00 173.45 ? 1006 NAG A C2 1 HETATM 12622 C C3 . NAG I 4 . ? -7.263 71.603 45.328 1.00 177.05 ? 1006 NAG A C3 1 HETATM 12623 C C4 . NAG I 4 . ? -6.677 71.504 46.731 1.00 179.15 ? 1006 NAG A C4 1 HETATM 12624 C C5 . NAG I 4 . ? -5.167 71.724 46.687 1.00 174.43 ? 1006 NAG A C5 1 HETATM 12625 C C6 . NAG I 4 . ? -4.501 71.525 48.028 1.00 172.02 ? 1006 NAG A C6 1 HETATM 12626 C C7 . NAG I 4 . ? -7.804 69.895 42.417 1.00 167.27 ? 1006 NAG A C7 1 HETATM 12627 C C8 . NAG I 4 . ? -8.134 68.674 43.222 1.00 153.08 ? 1006 NAG A C8 1 HETATM 12628 N N2 . NAG I 4 . ? -7.035 70.809 43.021 1.00 174.96 ? 1006 NAG A N2 1 HETATM 12629 O O3 . NAG I 4 . ? -8.645 71.270 45.354 1.00 175.91 ? 1006 NAG A O3 1 HETATM 12630 O O4 . NAG I 4 . ? -7.271 72.482 47.577 1.00 180.61 ? 1006 NAG A O4 1 HETATM 12631 O O5 . NAG I 4 . ? -4.567 70.784 45.783 1.00 169.83 ? 1006 NAG A O5 1 HETATM 12632 O O6 . NAG I 4 . ? -3.087 71.630 47.929 1.00 173.75 ? 1006 NAG A O6 1 HETATM 12633 O O7 . NAG I 4 . ? -8.214 70.049 41.271 1.00 169.98 ? 1006 NAG A O7 1 HETATM 12634 C C1 . NAG J 4 . ? -2.447 54.481 41.673 1.00 52.47 ? 1007 NAG A C1 1 HETATM 12635 C C2 . NAG J 4 . ? -2.604 55.436 42.851 1.00 58.46 ? 1007 NAG A C2 1 HETATM 12636 C C3 . NAG J 4 . ? -1.247 56.011 43.249 1.00 65.04 ? 1007 NAG A C3 1 HETATM 12637 C C4 . NAG J 4 . ? -0.231 54.896 43.471 1.00 60.74 ? 1007 NAG A C4 1 HETATM 12638 C C5 . NAG J 4 . ? -0.205 53.948 42.275 1.00 67.58 ? 1007 NAG A C5 1 HETATM 12639 C C6 . NAG J 4 . ? 0.669 52.735 42.500 1.00 82.26 ? 1007 NAG A C6 1 HETATM 12640 C C7 . NAG J 4 . ? -4.842 56.441 42.801 1.00 90.22 ? 1007 NAG A C7 1 HETATM 12641 C C8 . NAG J 4 . ? -5.656 57.635 42.401 1.00 106.09 ? 1007 NAG A C8 1 HETATM 12642 N N2 . NAG J 4 . ? -3.535 56.507 42.531 1.00 69.13 ? 1007 NAG A N2 1 HETATM 12643 O O3 . NAG J 4 . ? -1.390 56.779 44.439 1.00 101.09 ? 1007 NAG A O3 1 HETATM 12644 O O4 . NAG J 4 . ? 1.064 55.467 43.620 1.00 79.85 ? 1007 NAG A O4 1 HETATM 12645 O O5 . NAG J 4 . ? -1.527 53.457 42.011 1.00 66.08 ? 1007 NAG A O5 1 HETATM 12646 O O6 . NAG J 4 . ? 0.101 51.860 43.465 1.00 90.38 ? 1007 NAG A O6 1 HETATM 12647 O O7 . NAG J 4 . ? -5.346 55.463 43.344 1.00 95.78 ? 1007 NAG A O7 1 HETATM 12648 C C1 . NAG K 4 . ? 1.559 55.254 44.952 1.00 76.18 ? 1008 NAG A C1 1 HETATM 12649 C C2 . NAG K 4 . ? 3.059 55.538 44.937 1.00 70.47 ? 1008 NAG A C2 1 HETATM 12650 C C3 . NAG K 4 . ? 3.642 55.383 46.338 1.00 90.86 ? 1008 NAG A C3 1 HETATM 12651 C C4 . NAG K 4 . ? 2.869 56.248 47.326 1.00 107.69 ? 1008 NAG A C4 1 HETATM 12652 C C5 . NAG K 4 . ? 1.382 55.915 47.252 1.00 101.91 ? 1008 NAG A C5 1 HETATM 12653 C C6 . NAG K 4 . ? 0.530 56.798 48.134 1.00 109.64 ? 1008 NAG A C6 1 HETATM 12654 C C7 . NAG K 4 . ? 3.920 54.976 42.708 1.00 66.10 ? 1008 NAG A C7 1 HETATM 12655 C C8 . NAG K 4 . ? 4.649 53.960 41.881 1.00 67.07 ? 1008 NAG A C8 1 HETATM 12656 N N2 . NAG K 4 . ? 3.746 54.666 43.997 1.00 66.91 ? 1008 NAG A N2 1 HETATM 12657 O O3 . NAG K 4 . ? 5.013 55.763 46.326 1.00 89.90 ? 1008 NAG A O3 1 HETATM 12658 O O4 . NAG K 4 . ? 3.352 56.037 48.648 1.00 133.32 ? 1008 NAG A O4 1 HETATM 12659 O O5 . NAG K 4 . ? 0.917 56.103 45.907 1.00 93.52 ? 1008 NAG A O5 1 HETATM 12660 O O6 . NAG K 4 . ? 0.415 58.109 47.599 1.00 109.34 ? 1008 NAG A O6 1 HETATM 12661 O O7 . NAG K 4 . ? 3.506 56.028 42.230 1.00 74.92 ? 1008 NAG A O7 1 HETATM 12662 C C1 . BMA L 5 . ? 4.029 57.243 49.056 1.00 142.78 ? 1009 BMA A C1 1 HETATM 12663 C C2 . BMA L 5 . ? 3.829 57.476 50.549 1.00 145.52 ? 1009 BMA A C2 1 HETATM 12664 C C3 . BMA L 5 . ? 4.495 58.794 50.934 1.00 149.02 ? 1009 BMA A C3 1 HETATM 12665 C C4 . BMA L 5 . ? 5.966 58.831 50.464 1.00 148.63 ? 1009 BMA A C4 1 HETATM 12666 C C5 . BMA L 5 . ? 6.048 58.516 48.951 1.00 144.32 ? 1009 BMA A C5 1 HETATM 12667 C C6 . BMA L 5 . ? 7.471 58.398 48.417 1.00 152.60 ? 1009 BMA A C6 1 HETATM 12668 O O2 . BMA L 5 . ? 4.470 56.458 51.306 1.00 135.01 ? 1009 BMA A O2 1 HETATM 12669 O O3 . BMA L 5 . ? 4.402 59.043 52.336 1.00 154.87 ? 1009 BMA A O3 1 HETATM 12670 O O4 . BMA L 5 . ? 6.521 60.111 50.712 1.00 153.75 ? 1009 BMA A O4 1 HETATM 12671 O O5 . BMA L 5 . ? 5.394 57.255 48.707 1.00 143.40 ? 1009 BMA A O5 1 HETATM 12672 O O6 . BMA L 5 . ? 8.325 59.311 49.103 1.00 155.39 ? 1009 BMA A O6 1 HETATM 12673 C C1 . MAN M 6 . ? 3.065 59.495 52.631 1.00 155.74 ? 1010 MAN A C1 1 HETATM 12674 C C2 . MAN M 6 . ? 3.119 60.724 53.566 1.00 157.46 ? 1010 MAN A C2 1 HETATM 12675 C C3 . MAN M 6 . ? 3.348 60.291 55.020 1.00 157.11 ? 1010 MAN A C3 1 HETATM 12676 C C4 . MAN M 6 . ? 2.397 59.152 55.420 1.00 161.19 ? 1010 MAN A C4 1 HETATM 12677 C C5 . MAN M 6 . ? 2.558 57.990 54.435 1.00 145.26 ? 1010 MAN A C5 1 HETATM 12678 C C6 . MAN M 6 . ? 1.644 56.819 54.740 1.00 131.92 ? 1010 MAN A C6 1 HETATM 12679 O O2 . MAN M 6 . ? 1.877 61.432 53.564 1.00 167.70 ? 1010 MAN A O2 1 HETATM 12680 O O3 . MAN M 6 . ? 3.211 61.384 55.924 1.00 154.68 ? 1010 MAN A O3 1 HETATM 12681 O O4 . MAN M 6 . ? 2.697 58.705 56.732 1.00 169.31 ? 1010 MAN A O4 1 HETATM 12682 O O5 . MAN M 6 . ? 2.235 58.464 53.117 1.00 143.39 ? 1010 MAN A O5 1 HETATM 12683 O O6 . MAN M 6 . ? 2.099 56.207 55.942 1.00 126.76 ? 1010 MAN A O6 1 HETATM 12684 C C1 . BMA N 5 . ? 9.480 58.585 49.568 1.00 154.01 ? 1011 BMA A C1 1 HETATM 12685 C C2 . BMA N 5 . ? 10.235 57.959 48.408 1.00 153.84 ? 1011 BMA A C2 1 HETATM 12686 C C3 . BMA N 5 . ? 11.353 57.053 48.948 1.00 146.27 ? 1011 BMA A C3 1 HETATM 12687 C C4 . BMA N 5 . ? 11.581 57.158 50.499 1.00 190.09 ? 1011 BMA A C4 1 HETATM 12688 C C5 . BMA N 5 . ? 11.311 58.596 51.102 1.00 160.77 ? 1011 BMA A C5 1 HETATM 12689 C C6 . BMA N 5 . ? 12.579 59.420 51.264 1.00 165.63 ? 1011 BMA A C6 1 HETATM 12690 O O2 . BMA N 5 . ? 10.863 58.960 47.619 1.00 150.16 ? 1011 BMA A O2 1 HETATM 12691 O O3 . BMA N 5 . ? 12.580 57.257 48.251 1.00 136.40 ? 1011 BMA A O3 1 HETATM 12692 O O4 . BMA N 5 . ? 10.795 56.160 51.166 1.00 183.67 ? 1011 BMA A O4 1 HETATM 12693 O O5 . BMA N 5 . ? 10.361 59.361 50.320 1.00 151.39 ? 1011 BMA A O5 1 HETATM 12694 O O6 . BMA N 5 . ? 13.179 59.571 49.983 1.00 164.31 ? 1011 BMA A O6 1 HETATM 12695 C C1 . MAN O 6 . ? 10.879 56.299 52.598 1.00 182.39 ? 1012 MAN A C1 1 HETATM 12696 C C2 . MAN O 6 . ? 12.176 55.642 53.109 1.00 181.36 ? 1012 MAN A C2 1 HETATM 12697 C C3 . MAN O 6 . ? 12.037 54.118 53.107 1.00 173.36 ? 1012 MAN A C3 1 HETATM 12698 C C4 . MAN O 6 . ? 10.737 53.681 53.798 1.00 171.26 ? 1012 MAN A C4 1 HETATM 12699 C C5 . MAN O 6 . ? 9.543 54.377 53.136 1.00 172.27 ? 1012 MAN A C5 1 HETATM 12700 C C6 . MAN O 6 . ? 8.222 54.037 53.797 1.00 158.25 ? 1012 MAN A C6 1 HETATM 12701 O O2 . MAN O 6 . ? 12.438 56.003 54.467 1.00 179.90 ? 1012 MAN A O2 1 HETATM 12702 O O3 . MAN O 6 . ? 13.154 53.486 53.722 1.00 161.28 ? 1012 MAN A O3 1 HETATM 12703 O O4 . MAN O 6 . ? 10.579 52.275 53.688 1.00 167.69 ? 1012 MAN A O4 1 HETATM 12704 O O5 . MAN O 6 . ? 9.728 55.806 53.234 1.00 182.32 ? 1012 MAN A O5 1 HETATM 12705 O O6 . MAN O 6 . ? 7.176 54.340 52.882 1.00 147.28 ? 1012 MAN A O6 1 HETATM 12706 C C1 . NAG P 4 . ? -62.345 51.069 -10.299 1.00 97.22 ? 1013 NAG A C1 1 HETATM 12707 C C2 . NAG P 4 . ? -62.588 52.089 -9.188 1.00 116.46 ? 1013 NAG A C2 1 HETATM 12708 C C3 . NAG P 4 . ? -61.948 53.428 -9.550 1.00 105.72 ? 1013 NAG A C3 1 HETATM 12709 C C4 . NAG P 4 . ? -60.483 53.242 -9.933 1.00 115.78 ? 1013 NAG A C4 1 HETATM 12710 C C5 . NAG P 4 . ? -60.341 52.149 -10.988 1.00 118.21 ? 1013 NAG A C5 1 HETATM 12711 C C6 . NAG P 4 . ? -58.903 51.810 -11.307 1.00 127.32 ? 1013 NAG A C6 1 HETATM 12712 C C7 . NAG P 4 . ? -64.505 52.740 -7.793 1.00 158.53 ? 1013 NAG A C7 1 HETATM 12713 C C8 . NAG P 4 . ? -65.999 52.842 -7.711 1.00 158.09 ? 1013 NAG A C8 1 HETATM 12714 N N2 . NAG P 4 . ? -64.013 52.255 -8.937 1.00 140.22 ? 1013 NAG A N2 1 HETATM 12715 O O3 . NAG P 4 . ? -62.046 54.321 -8.447 1.00 86.84 ? 1013 NAG A O3 1 HETATM 12716 O O4 . NAG P 4 . ? -59.975 54.456 -10.471 1.00 138.64 ? 1013 NAG A O4 1 HETATM 12717 O O5 . NAG P 4 . ? -60.955 50.939 -10.526 1.00 114.66 ? 1013 NAG A O5 1 HETATM 12718 O O6 . NAG P 4 . ? -58.791 50.515 -11.880 1.00 142.62 ? 1013 NAG A O6 1 HETATM 12719 O O7 . NAG P 4 . ? -63.779 53.085 -6.865 1.00 166.13 ? 1013 NAG A O7 1 HETATM 12720 C C1 . NAG Q 4 . ? -58.900 54.936 -9.647 1.00 161.10 ? 1014 NAG A C1 1 HETATM 12721 C C2 . NAG Q 4 . ? -57.911 55.691 -10.531 1.00 156.74 ? 1014 NAG A C2 1 HETATM 12722 C C3 . NAG Q 4 . ? -56.773 56.265 -9.688 1.00 164.93 ? 1014 NAG A C3 1 HETATM 12723 C C4 . NAG Q 4 . ? -57.323 57.073 -8.520 1.00 178.06 ? 1014 NAG A C4 1 HETATM 12724 C C5 . NAG Q 4 . ? -58.329 56.234 -7.734 1.00 176.27 ? 1014 NAG A C5 1 HETATM 12725 C C6 . NAG Q 4 . ? -59.010 56.991 -6.616 1.00 180.02 ? 1014 NAG A C6 1 HETATM 12726 C C7 . NAG Q 4 . ? -57.166 55.232 -12.828 1.00 132.38 ? 1014 NAG A C7 1 HETATM 12727 C C8 . NAG Q 4 . ? -56.622 54.199 -13.768 1.00 127.16 ? 1014 NAG A C8 1 HETATM 12728 N N2 . NAG Q 4 . ? -57.386 54.823 -11.573 1.00 145.14 ? 1014 NAG A N2 1 HETATM 12729 O O3 . NAG Q 4 . ? -55.949 57.087 -10.506 1.00 166.95 ? 1014 NAG A O3 1 HETATM 12730 O O4 . NAG Q 4 . ? -56.249 57.467 -7.671 1.00 190.58 ? 1014 NAG A O4 1 HETATM 12731 O O5 . NAG Q 4 . ? -59.368 55.789 -8.617 1.00 176.30 ? 1014 NAG A O5 1 HETATM 12732 O O6 . NAG Q 4 . ? -60.423 56.987 -6.773 1.00 185.61 ? 1014 NAG A O6 1 HETATM 12733 O O7 . NAG Q 4 . ? -57.396 56.382 -13.186 1.00 127.19 ? 1014 NAG A O7 1 HETATM 12734 C C1 . BMA R 5 . ? -56.288 58.894 -7.457 1.00 187.64 ? 1015 BMA A C1 1 HETATM 12735 C C2 . BMA R 5 . ? -55.030 59.371 -6.760 1.00 191.79 ? 1015 BMA A C2 1 HETATM 12736 C C3 . BMA R 5 . ? -55.287 60.812 -6.317 1.00 203.37 ? 1015 BMA A C3 1 HETATM 12737 C C4 . BMA R 5 . ? -55.678 61.687 -7.531 1.00 221.66 ? 1015 BMA A C4 1 HETATM 12738 C C5 . BMA R 5 . ? -56.844 61.041 -8.331 1.00 180.24 ? 1015 BMA A C5 1 HETATM 12739 C C6 . BMA R 5 . ? -57.117 61.746 -9.649 1.00 173.66 ? 1015 BMA A C6 1 HETATM 12740 O O2 . BMA R 5 . ? -53.951 59.405 -7.685 1.00 184.82 ? 1015 BMA A O2 1 HETATM 12741 O O3 . BMA R 5 . ? -54.189 61.419 -5.599 1.00 202.02 ? 1015 BMA A O3 1 HETATM 12742 O O4 . BMA R 5 . ? -56.065 62.979 -7.093 1.00 228.49 ? 1015 BMA A O4 1 HETATM 12743 O O5 . BMA R 5 . ? -56.534 59.657 -8.618 1.00 183.85 ? 1015 BMA A O5 1 HETATM 12744 O O6 . BMA R 5 . ? -57.260 63.137 -9.390 1.00 169.61 ? 1015 BMA A O6 1 HETATM 12745 C C1 . MAN S 6 . ? -53.443 60.466 -4.813 1.00 193.49 ? 1016 MAN A C1 1 HETATM 12746 C C2 . MAN S 6 . ? -53.986 60.388 -3.366 1.00 186.91 ? 1016 MAN A C2 1 HETATM 12747 C C3 . MAN S 6 . ? -53.483 61.568 -2.521 1.00 188.64 ? 1016 MAN A C3 1 HETATM 12748 C C4 . MAN S 6 . ? -51.977 61.800 -2.718 1.00 194.45 ? 1016 MAN A C4 1 HETATM 12749 C C5 . MAN S 6 . ? -51.679 61.950 -4.211 1.00 191.26 ? 1016 MAN A C5 1 HETATM 12750 C C6 . MAN S 6 . ? -50.214 62.191 -4.509 1.00 181.00 ? 1016 MAN A C6 1 HETATM 12751 O O2 . MAN S 6 . ? -53.512 59.214 -2.702 1.00 180.42 ? 1016 MAN A O2 1 HETATM 12752 O O3 . MAN S 6 . ? -53.769 61.381 -1.138 1.00 182.35 ? 1016 MAN A O3 1 HETATM 12753 O O4 . MAN S 6 . ? -51.573 62.976 -2.035 1.00 200.27 ? 1016 MAN A O4 1 HETATM 12754 O O5 . MAN S 6 . ? -52.069 60.734 -4.870 1.00 195.08 ? 1016 MAN A O5 1 HETATM 12755 O O6 . MAN S 6 . ? -49.978 63.593 -4.442 1.00 172.80 ? 1016 MAN A O6 1 HETATM 12756 C C1 . NAG T 4 . ? -30.111 49.349 -17.536 1.00 143.39 ? 1017 NAG A C1 1 HETATM 12757 C C2 . NAG T 4 . ? -30.881 48.901 -18.781 1.00 169.53 ? 1017 NAG A C2 1 HETATM 12758 C C3 . NAG T 4 . ? -30.304 47.594 -19.321 1.00 173.41 ? 1017 NAG A C3 1 HETATM 12759 C C4 . NAG T 4 . ? -28.802 47.723 -19.538 1.00 167.85 ? 1017 NAG A C4 1 HETATM 12760 C C5 . NAG T 4 . ? -28.130 48.199 -18.255 1.00 162.70 ? 1017 NAG A C5 1 HETATM 12761 C C6 . NAG T 4 . ? -26.650 48.451 -18.423 1.00 163.19 ? 1017 NAG A C6 1 HETATM 12762 C C7 . NAG T 4 . ? -33.251 48.859 -19.425 1.00 187.34 ? 1017 NAG A C7 1 HETATM 12763 C C8 . NAG T 4 . ? -34.660 48.676 -18.947 1.00 181.27 ? 1017 NAG A C8 1 HETATM 12764 N N2 . NAG T 4 . ? -32.298 48.752 -18.493 1.00 183.95 ? 1017 NAG A N2 1 HETATM 12765 O O3 . NAG T 4 . ? -30.942 47.261 -20.548 1.00 176.18 ? 1017 NAG A O3 1 HETATM 12766 O O4 . NAG T 4 . ? -28.254 46.466 -19.920 1.00 163.40 ? 1017 NAG A O4 1 HETATM 12767 O O5 . NAG T 4 . ? -28.716 49.440 -17.839 1.00 154.29 ? 1017 NAG A O5 1 HETATM 12768 O O6 . NAG T 4 . ? -26.023 47.405 -19.154 1.00 157.15 ? 1017 NAG A O6 1 HETATM 12769 O O7 . NAG T 4 . ? -32.988 49.092 -20.600 1.00 187.61 ? 1017 NAG A O7 1 HETATM 12770 C C1 . NAG U 4 . ? -35.277 42.291 2.001 1.00 128.96 ? 1018 NAG A C1 1 HETATM 12771 C C2 . NAG U 4 . ? -34.402 41.079 1.692 1.00 150.06 ? 1018 NAG A C2 1 HETATM 12772 C C3 . NAG U 4 . ? -33.158 41.090 2.574 1.00 162.60 ? 1018 NAG A C3 1 HETATM 12773 C C4 . NAG U 4 . ? -33.557 41.069 4.045 1.00 160.50 ? 1018 NAG A C4 1 HETATM 12774 C C5 . NAG U 4 . ? -34.632 42.120 4.308 1.00 151.89 ? 1018 NAG A C5 1 HETATM 12775 C C6 . NAG U 4 . ? -34.304 43.024 5.474 1.00 151.36 ? 1018 NAG A C6 1 HETATM 12776 C C7 . NAG U 4 . ? -35.986 39.355 0.953 1.00 156.27 ? 1018 NAG A C7 1 HETATM 12777 C C8 . NAG U 4 . ? -36.669 38.068 1.307 1.00 163.63 ? 1018 NAG A C8 1 HETATM 12778 N N2 . NAG U 4 . ? -35.145 39.842 1.871 1.00 152.25 ? 1018 NAG A N2 1 HETATM 12779 O O3 . NAG U 4 . ? -32.388 42.253 2.294 1.00 163.74 ? 1018 NAG A O3 1 HETATM 12780 O O4 . NAG U 4 . ? -34.062 39.784 4.389 1.00 160.81 ? 1018 NAG A O4 1 HETATM 12781 O O5 . NAG U 4 . ? -34.772 42.967 3.158 1.00 150.96 ? 1018 NAG A O5 1 HETATM 12782 O O6 . NAG U 4 . ? -34.931 44.292 5.339 1.00 157.08 ? 1018 NAG A O6 1 HETATM 12783 O O7 . NAG U 4 . ? -36.187 39.926 -0.114 1.00 152.08 ? 1018 NAG A O7 1 HETATM 12784 C C1 . NAG V 4 . ? -33.435 39.298 5.594 1.00 154.40 ? 1019 NAG A C1 1 HETATM 12785 C C2 . NAG V 4 . ? -31.922 39.178 5.411 1.00 150.90 ? 1019 NAG A C2 1 HETATM 12786 C C3 . NAG V 4 . ? -31.277 38.636 6.684 1.00 146.40 ? 1019 NAG A C3 1 HETATM 12787 C C4 . NAG V 4 . ? -31.692 39.472 7.889 1.00 146.33 ? 1019 NAG A C4 1 HETATM 12788 C C5 . NAG V 4 . ? -33.213 39.575 7.958 1.00 145.14 ? 1019 NAG A C5 1 HETATM 12789 C C6 . NAG V 4 . ? -33.698 40.484 9.064 1.00 134.33 ? 1019 NAG A C6 1 HETATM 12790 C C7 . NAG V 4 . ? -30.657 38.638 3.377 1.00 140.98 ? 1019 NAG A C7 1 HETATM 12791 C C8 . NAG V 4 . ? -30.459 37.651 2.266 1.00 130.43 ? 1019 NAG A C8 1 HETATM 12792 N N2 . NAG V 4 . ? -31.599 38.331 4.273 1.00 145.08 ? 1019 NAG A N2 1 HETATM 12793 O O3 . NAG V 4 . ? -29.861 38.655 6.543 1.00 145.24 ? 1019 NAG A O3 1 HETATM 12794 O O4 . NAG V 4 . ? -31.206 38.877 9.086 1.00 150.68 ? 1019 NAG A O4 1 HETATM 12795 O O5 . NAG V 4 . ? -33.717 40.115 6.728 1.00 149.39 ? 1019 NAG A O5 1 HETATM 12796 O O6 . NAG V 4 . ? -35.051 40.869 8.862 1.00 119.74 ? 1019 NAG A O6 1 HETATM 12797 O O7 . NAG V 4 . ? -29.993 39.667 3.458 1.00 151.07 ? 1019 NAG A O7 1 HETATM 12798 C C1 . NAG W 4 . ? -43.482 58.703 15.622 1.00 156.40 ? 1020 NAG A C1 1 HETATM 12799 C C2 . NAG W 4 . ? -42.536 59.614 14.836 1.00 180.58 ? 1020 NAG A C2 1 HETATM 12800 C C3 . NAG W 4 . ? -43.067 59.833 13.421 1.00 184.91 ? 1020 NAG A C3 1 HETATM 12801 C C4 . NAG W 4 . ? -44.433 60.506 13.462 1.00 184.33 ? 1020 NAG A C4 1 HETATM 12802 C C5 . NAG W 4 . ? -45.289 59.896 14.569 1.00 185.45 ? 1020 NAG A C5 1 HETATM 12803 C C6 . NAG W 4 . ? -46.720 59.653 14.147 1.00 184.98 ? 1020 NAG A C6 1 HETATM 12804 C C7 . NAG W 4 . ? -41.224 61.225 16.148 1.00 182.27 ? 1020 NAG A C7 1 HETATM 12805 C C8 . NAG W 4 . ? -41.214 62.577 16.797 1.00 173.68 ? 1020 NAG A C8 1 HETATM 12806 N N2 . NAG W 4 . ? -42.353 60.887 15.518 1.00 188.44 ? 1020 NAG A N2 1 HETATM 12807 O O3 . NAG W 4 . ? -43.160 58.581 12.751 1.00 183.64 ? 1020 NAG A O3 1 HETATM 12808 O O4 . NAG W 4 . ? -44.283 61.901 13.700 1.00 178.44 ? 1020 NAG A O4 1 HETATM 12809 O O5 . NAG W 4 . ? -44.747 58.623 14.949 1.00 176.67 ? 1020 NAG A O5 1 HETATM 12810 O O6 . NAG W 4 . ? -47.377 58.763 15.039 1.00 179.93 ? 1020 NAG A O6 1 HETATM 12811 O O7 . NAG W 4 . ? -40.254 60.476 16.192 1.00 183.35 ? 1020 NAG A O7 1 HETATM 12812 C C1 . NAG X 4 . ? -24.544 53.955 62.631 1.00 92.64 ? 1021 NAG A C1 1 HETATM 12813 C C2 . NAG X 4 . ? -25.585 54.368 61.591 1.00 110.30 ? 1021 NAG A C2 1 HETATM 12814 C C3 . NAG X 4 . ? -24.942 55.239 60.515 1.00 114.32 ? 1021 NAG A C3 1 HETATM 12815 C C4 . NAG X 4 . ? -24.210 56.414 61.148 1.00 132.72 ? 1021 NAG A C4 1 HETATM 12816 C C5 . NAG X 4 . ? -23.221 55.909 62.194 1.00 129.29 ? 1021 NAG A C5 1 HETATM 12817 C C6 . NAG X 4 . ? -22.529 57.023 62.944 1.00 129.70 ? 1021 NAG A C6 1 HETATM 12818 C C7 . NAG X 4 . ? -27.352 52.668 61.458 1.00 117.98 ? 1021 NAG A C7 1 HETATM 12819 C C8 . NAG X 4 . ? -27.862 51.468 60.719 1.00 105.94 ? 1021 NAG A C8 1 HETATM 12820 N N2 . NAG X 4 . ? -26.218 53.204 60.994 1.00 124.88 ? 1021 NAG A N2 1 HETATM 12821 O O3 . NAG X 4 . ? -25.947 55.713 59.625 1.00 113.67 ? 1021 NAG A O3 1 HETATM 12822 O O4 . NAG X 4 . ? -23.508 57.148 60.151 1.00 144.24 ? 1021 NAG A O4 1 HETATM 12823 O O5 . NAG X 4 . ? -23.915 55.120 63.172 1.00 119.39 ? 1021 NAG A O5 1 HETATM 12824 O O6 . NAG X 4 . ? -23.461 57.972 63.445 1.00 123.93 ? 1021 NAG A O6 1 HETATM 12825 O O7 . NAG X 4 . ? -27.940 53.131 62.431 1.00 126.46 ? 1021 NAG A O7 1 HETATM 12826 C C1 . NAG Y 4 . ? -41.442 32.786 62.792 1.00 107.21 ? 1022 NAG A C1 1 HETATM 12827 C C2 . NAG Y 4 . ? -42.752 32.667 62.007 1.00 123.85 ? 1022 NAG A C2 1 HETATM 12828 C C3 . NAG Y 4 . ? -42.514 31.938 60.685 1.00 140.85 ? 1022 NAG A C3 1 HETATM 12829 C C4 . NAG Y 4 . ? -41.994 30.528 60.936 1.00 146.99 ? 1022 NAG A C4 1 HETATM 12830 C C5 . NAG Y 4 . ? -40.984 30.535 62.081 1.00 133.69 ? 1022 NAG A C5 1 HETATM 12831 C C6 . NAG Y 4 . ? -39.785 29.652 61.824 1.00 124.71 ? 1022 NAG A C6 1 HETATM 12832 C C7 . NAG Y 4 . ? -44.425 32.568 63.803 1.00 144.35 ? 1022 NAG A C7 1 HETATM 12833 C C8 . NAG Y 4 . ? -45.446 31.719 64.497 1.00 148.28 ? 1022 NAG A C8 1 HETATM 12834 N N2 . NAG Y 4 . ? -43.775 31.990 62.788 1.00 125.87 ? 1022 NAG A N2 1 HETATM 12835 O O3 . NAG Y 4 . ? -41.579 32.670 59.901 1.00 146.54 ? 1022 NAG A O3 1 HETATM 12836 O O4 . NAG Y 4 . ? -43.075 29.657 61.251 1.00 163.61 ? 1022 NAG A O4 1 HETATM 12837 O O5 . NAG Y 4 . ? -40.481 31.865 62.267 1.00 128.46 ? 1022 NAG A O5 1 HETATM 12838 O O6 . NAG Y 4 . ? -38.692 30.006 62.661 1.00 121.13 ? 1022 NAG A O6 1 HETATM 12839 O O7 . NAG Y 4 . ? -44.199 33.725 64.146 1.00 152.68 ? 1022 NAG A O7 1 HETATM 12840 C C1 . NAG Z 4 . ? -42.848 28.382 60.612 1.00 178.27 ? 1023 NAG A C1 1 HETATM 12841 C C2 . NAG Z 4 . ? -42.869 27.253 61.648 1.00 180.49 ? 1023 NAG A C2 1 HETATM 12842 C C3 . NAG Z 4 . ? -44.174 26.466 61.552 1.00 183.48 ? 1023 NAG A C3 1 HETATM 12843 C C4 . NAG Z 4 . ? -45.331 27.396 61.219 1.00 181.02 ? 1023 NAG A C4 1 HETATM 12844 C C5 . NAG Z 4 . ? -45.134 27.985 59.825 1.00 178.76 ? 1023 NAG A C5 1 HETATM 12845 C C6 . NAG Z 4 . ? -45.693 29.381 59.676 1.00 172.53 ? 1023 NAG A C6 1 HETATM 12846 C C7 . NAG Z 4 . ? -40.857 26.102 62.465 1.00 150.97 ? 1023 NAG A C7 1 HETATM 12847 C C8 . NAG Z 4 . ? -41.124 26.769 63.781 1.00 144.17 ? 1023 NAG A C8 1 HETATM 12848 N N2 . NAG Z 4 . ? -41.726 26.371 61.483 1.00 164.45 ? 1023 NAG A N2 1 HETATM 12849 O O3 . NAG Z 4 . ? -44.419 25.808 62.790 1.00 179.33 ? 1023 NAG A O3 1 HETATM 12850 O O4 . NAG Z 4 . ? -46.559 26.678 61.255 1.00 179.41 ? 1023 NAG A O4 1 HETATM 12851 O O5 . NAG Z 4 . ? -43.735 28.050 59.503 1.00 183.68 ? 1023 NAG A O5 1 HETATM 12852 O O6 . NAG Z 4 . ? -45.847 29.736 58.309 1.00 166.69 ? 1023 NAG A O6 1 HETATM 12853 O O7 . NAG Z 4 . ? -39.899 25.353 62.297 1.00 154.14 ? 1023 NAG A O7 1 HETATM 12854 C C1 . NAG AA 4 . ? -29.178 21.663 75.913 1.00 86.26 ? 1024 NAG A C1 1 HETATM 12855 C C2 . NAG AA 4 . ? -29.271 21.038 74.521 1.00 120.07 ? 1024 NAG A C2 1 HETATM 12856 C C3 . NAG AA 4 . ? -30.689 21.181 73.970 1.00 125.11 ? 1024 NAG A C3 1 HETATM 12857 C C4 . NAG AA 4 . ? -31.700 20.615 74.959 1.00 128.56 ? 1024 NAG A C4 1 HETATM 12858 C C5 . NAG AA 4 . ? -31.509 21.274 76.323 1.00 119.45 ? 1024 NAG A C5 1 HETATM 12859 C C6 . NAG AA 4 . ? -32.407 20.702 77.394 1.00 130.63 ? 1024 NAG A C6 1 HETATM 12860 C C7 . NAG AA 4 . ? -27.400 20.926 72.936 1.00 130.51 ? 1024 NAG A C7 1 HETATM 12861 C C8 . NAG AA 4 . ? -26.482 21.709 72.046 1.00 130.34 ? 1024 NAG A C8 1 HETATM 12862 N N2 . NAG AA 4 . ? -28.306 21.638 73.614 1.00 132.48 ? 1024 NAG A N2 1 HETATM 12863 O O3 . NAG AA 4 . ? -30.782 20.503 72.722 1.00 127.27 ? 1024 NAG A O3 1 HETATM 12864 O O4 . NAG AA 4 . ? -33.029 20.837 74.498 1.00 145.14 ? 1024 NAG A O4 1 HETATM 12865 O O5 . NAG AA 4 . ? -30.159 21.076 76.769 1.00 110.23 ? 1024 NAG A O5 1 HETATM 12866 O O6 . NAG AA 4 . ? -32.222 21.367 78.635 1.00 138.42 ? 1024 NAG A O6 1 HETATM 12867 O O7 . NAG AA 4 . ? -27.325 19.705 73.036 1.00 119.64 ? 1024 NAG A O7 1 HETATM 12868 C C1 . NAG BA 4 . ? -33.560 19.591 73.993 1.00 170.61 ? 1025 NAG A C1 1 HETATM 12869 C C2 . NAG BA 4 . ? -34.390 18.855 75.062 1.00 192.64 ? 1025 NAG A C2 1 HETATM 12870 C C3 . NAG BA 4 . ? -35.696 19.601 75.359 1.00 205.45 ? 1025 NAG A C3 1 HETATM 12871 C C4 . NAG BA 4 . ? -36.288 20.228 74.101 1.00 209.07 ? 1025 NAG A C4 1 HETATM 12872 C C5 . NAG BA 4 . ? -35.755 19.537 72.851 1.00 196.86 ? 1025 NAG A C5 1 HETATM 12873 C C6 . NAG BA 4 . ? -36.357 20.076 71.574 1.00 196.85 ? 1025 NAG A C6 1 HETATM 12874 C C7 . NAG BA 4 . ? -34.868 16.510 75.612 1.00 189.64 ? 1025 NAG A C7 1 HETATM 12875 C C8 . NAG BA 4 . ? -35.114 15.135 75.068 1.00 186.94 ? 1025 NAG A C8 1 HETATM 12876 N N2 . NAG BA 4 . ? -34.645 17.467 74.705 1.00 193.38 ? 1025 NAG A N2 1 HETATM 12877 O O3 . NAG BA 4 . ? -35.441 20.610 76.331 1.00 202.42 ? 1025 NAG A O3 1 HETATM 12878 O O4 . NAG BA 4 . ? -37.706 20.095 74.112 1.00 217.35 ? 1025 NAG A O4 1 HETATM 12879 O O5 . NAG BA 4 . ? -34.334 19.715 72.750 1.00 179.85 ? 1025 NAG A O5 1 HETATM 12880 O O6 . NAG BA 4 . ? -37.284 19.159 71.009 1.00 192.29 ? 1025 NAG A O6 1 HETATM 12881 O O7 . NAG BA 4 . ? -34.870 16.743 76.817 1.00 188.46 ? 1025 NAG A O7 1 HETATM 12882 C C1 . BMA CA 5 . ? -38.302 20.969 75.092 1.00 217.26 ? 1026 BMA A C1 1 HETATM 12883 C C2 . BMA CA 5 . ? -39.417 21.845 74.413 1.00 182.52 ? 1026 BMA A C2 1 HETATM 12884 C C3 . BMA CA 5 . ? -40.875 21.543 74.888 1.00 190.93 ? 1026 BMA A C3 1 HETATM 12885 C C4 . BMA CA 5 . ? -40.979 20.720 76.190 1.00 189.39 ? 1026 BMA A C4 1 HETATM 12886 C C5 . BMA CA 5 . ? -39.720 20.894 77.012 1.00 195.73 ? 1026 BMA A C5 1 HETATM 12887 C C6 . BMA CA 5 . ? -39.800 20.210 78.365 1.00 180.99 ? 1026 BMA A C6 1 HETATM 12888 O O2 . BMA CA 5 . ? -39.407 21.657 73.004 1.00 179.91 ? 1026 BMA A O2 1 HETATM 12889 O O3 . BMA CA 5 . ? -41.647 20.930 73.856 1.00 189.67 ? 1026 BMA A O3 1 HETATM 12890 O O4 . BMA CA 5 . ? -42.105 21.143 76.946 1.00 179.68 ? 1026 BMA A O4 1 HETATM 12891 O O5 . BMA CA 5 . ? -38.694 20.269 76.265 1.00 211.77 ? 1026 BMA A O5 1 HETATM 12892 O O6 . BMA CA 5 . ? -40.961 20.683 79.033 1.00 173.31 ? 1026 BMA A O6 1 HETATM 12893 MN MN . MN DA 7 . ? -6.366 67.557 32.201 1.00 141.49 ? 1027 MN A MN 1 HETATM 12894 MN MN . MN EA 7 . ? -17.024 59.520 26.348 1.00 123.53 ? 1028 MN A MN 1 HETATM 12895 MN MN . MN FA 7 . ? -18.890 56.225 13.632 1.00 131.63 ? 1029 MN A MN 1 HETATM 12896 MN MN . MN GA 7 . ? -10.635 59.100 3.510 1.00 123.80 ? 1030 MN A MN 1 HETATM 12897 MN MN . MN HA 7 . ? -69.279 46.554 4.750 1.00 111.07 ? 1031 MN A MN 1 HETATM 12898 C C1 . NAG IA 4 . ? -26.952 4.226 29.493 1.00 123.69 ? 701 NAG B C1 1 HETATM 12899 C C2 . NAG IA 4 . ? -26.881 2.865 28.791 1.00 151.97 ? 701 NAG B C2 1 HETATM 12900 C C3 . NAG IA 4 . ? -26.729 1.745 29.813 1.00 150.14 ? 701 NAG B C3 1 HETATM 12901 C C4 . NAG IA 4 . ? -25.650 2.103 30.825 1.00 160.96 ? 701 NAG B C4 1 HETATM 12902 C C5 . NAG IA 4 . ? -26.084 3.325 31.627 1.00 162.49 ? 701 NAG B C5 1 HETATM 12903 C C6 . NAG IA 4 . ? -24.963 4.308 31.882 1.00 174.72 ? 701 NAG B C6 1 HETATM 12904 C C7 . NAG IA 4 . ? -28.058 2.840 26.638 1.00 180.04 ? 701 NAG B C7 1 HETATM 12905 C C8 . NAG IA 4 . ? -29.354 2.565 25.938 1.00 177.99 ? 701 NAG B C8 1 HETATM 12906 N N2 . NAG IA 4 . ? -28.055 2.644 27.960 1.00 172.39 ? 701 NAG B N2 1 HETATM 12907 O O3 . NAG IA 4 . ? -26.389 0.536 29.146 1.00 143.62 ? 701 NAG B O3 1 HETATM 12908 O O4 . NAG IA 4 . ? -25.438 1.011 31.712 1.00 165.98 ? 701 NAG B O4 1 HETATM 12909 O O5 . NAG IA 4 . ? -27.132 4.032 30.940 1.00 141.01 ? 701 NAG B O5 1 HETATM 12910 O O6 . NAG IA 4 . ? -23.898 3.707 32.606 1.00 172.66 ? 701 NAG B O6 1 HETATM 12911 O O7 . NAG IA 4 . ? -27.060 3.220 26.033 1.00 179.02 ? 701 NAG B O7 1 HETATM 12912 C C1 . NAG JA 4 . ? -3.317 36.017 45.382 1.00 95.38 ? 702 NAG B C1 1 HETATM 12913 C C2 . NAG JA 4 . ? -3.001 37.428 45.896 1.00 112.57 ? 702 NAG B C2 1 HETATM 12914 C C3 . NAG JA 4 . ? -3.978 37.827 47.004 1.00 124.72 ? 702 NAG B C3 1 HETATM 12915 C C4 . NAG JA 4 . ? -5.418 37.625 46.555 1.00 132.69 ? 702 NAG B C4 1 HETATM 12916 C C5 . NAG JA 4 . ? -5.608 36.196 46.066 1.00 130.16 ? 702 NAG B C5 1 HETATM 12917 C C6 . NAG JA 4 . ? -6.992 35.931 45.522 1.00 140.39 ? 702 NAG B C6 1 HETATM 12918 C C7 . NAG JA 4 . ? -0.561 37.519 45.573 1.00 128.56 ? 702 NAG B C7 1 HETATM 12919 C C8 . NAG JA 4 . ? 0.771 37.619 46.254 1.00 129.66 ? 702 NAG B C8 1 HETATM 12920 N N2 . NAG JA 4 . ? -1.631 37.516 46.377 1.00 123.18 ? 702 NAG B N2 1 HETATM 12921 O O3 . NAG JA 4 . ? -3.767 39.190 47.354 1.00 131.97 ? 702 NAG B O3 1 HETATM 12922 O O4 . NAG JA 4 . ? -6.309 37.875 47.637 1.00 150.65 ? 702 NAG B O4 1 HETATM 12923 O O5 . NAG JA 4 . ? -4.688 35.940 44.997 1.00 121.27 ? 702 NAG B O5 1 HETATM 12924 O O6 . NAG JA 4 . ? -6.985 34.858 44.589 1.00 144.85 ? 702 NAG B O6 1 HETATM 12925 O O7 . NAG JA 4 . ? -0.663 37.439 44.354 1.00 127.74 ? 702 NAG B O7 1 HETATM 12926 C C1 . NAG KA 4 . ? -26.670 10.935 34.378 1.00 94.52 ? 703 NAG B C1 1 HETATM 12927 C C2 . NAG KA 4 . ? -27.070 10.365 33.022 1.00 117.53 ? 703 NAG B C2 1 HETATM 12928 C C3 . NAG KA 4 . ? -28.387 10.982 32.559 1.00 123.77 ? 703 NAG B C3 1 HETATM 12929 C C4 . NAG KA 4 . ? -29.459 10.813 33.632 1.00 129.04 ? 703 NAG B C4 1 HETATM 12930 C C5 . NAG KA 4 . ? -28.946 11.342 34.971 1.00 118.08 ? 703 NAG B C5 1 HETATM 12931 C C6 . NAG KA 4 . ? -29.905 11.095 36.112 1.00 116.89 ? 703 NAG B C6 1 HETATM 12932 C C7 . NAG KA 4 . ? -25.022 9.721 31.833 1.00 129.31 ? 703 NAG B C7 1 HETATM 12933 C C8 . NAG KA 4 . ? -24.031 10.102 30.776 1.00 132.39 ? 703 NAG B C8 1 HETATM 12934 N N2 . NAG KA 4 . ? -26.025 10.582 32.034 1.00 121.90 ? 703 NAG B N2 1 HETATM 12935 O O3 . NAG KA 4 . ? -28.788 10.360 31.343 1.00 128.35 ? 703 NAG B O3 1 HETATM 12936 O O4 . NAG KA 4 . ? -30.631 11.543 33.287 1.00 149.66 ? 703 NAG B O4 1 HETATM 12937 O O5 . NAG KA 4 . ? -27.711 10.699 35.319 1.00 115.91 ? 703 NAG B O5 1 HETATM 12938 O O6 . NAG KA 4 . ? -31.144 11.758 35.903 1.00 124.34 ? 703 NAG B O6 1 HETATM 12939 O O7 . NAG KA 4 . ? -24.919 8.682 32.477 1.00 131.60 ? 703 NAG B O7 1 HETATM 12940 C C1 . NAG LA 4 . ? -31.585 10.736 32.557 1.00 163.99 ? 704 NAG B C1 1 HETATM 12941 C C2 . NAG LA 4 . ? -32.502 9.920 33.475 1.00 169.65 ? 704 NAG B C2 1 HETATM 12942 C C3 . NAG LA 4 . ? -33.955 10.081 33.045 1.00 166.79 ? 704 NAG B C3 1 HETATM 12943 C C4 . NAG LA 4 . ? -34.336 11.553 33.041 1.00 171.14 ? 704 NAG B C4 1 HETATM 12944 C C5 . NAG LA 4 . ? -33.435 12.321 32.079 1.00 166.46 ? 704 NAG B C5 1 HETATM 12945 C C6 . NAG LA 4 . ? -32.773 13.528 32.705 1.00 148.33 ? 704 NAG B C6 1 HETATM 12946 C C7 . NAG LA 4 . ? -32.045 7.767 34.579 1.00 174.76 ? 704 NAG B C7 1 HETATM 12947 C C8 . NAG LA 4 . ? -32.377 8.456 35.870 1.00 167.92 ? 704 NAG B C8 1 HETATM 12948 N N2 . NAG LA 4 . ? -32.122 8.516 33.473 1.00 175.23 ? 704 NAG B N2 1 HETATM 12949 O O3 . NAG LA 4 . ? -34.801 9.362 33.936 1.00 160.60 ? 704 NAG B O3 1 HETATM 12950 O O4 . NAG LA 4 . ? -35.692 11.706 32.639 1.00 172.30 ? 704 NAG B O4 1 HETATM 12951 O O5 . NAG LA 4 . ? -32.394 11.468 31.567 1.00 168.51 ? 704 NAG B O5 1 HETATM 12952 O O6 . NAG LA 4 . ? -33.051 13.609 34.097 1.00 126.59 ? 704 NAG B O6 1 HETATM 12953 O O7 . NAG LA 4 . ? -31.722 6.584 34.540 1.00 177.08 ? 704 NAG B O7 1 HETATM 12954 C C1 . NAG MA 4 . ? -33.579 30.307 32.001 1.00 85.96 ? 705 NAG B C1 1 HETATM 12955 C C2 . NAG MA 4 . ? -33.191 30.628 33.439 1.00 98.35 ? 705 NAG B C2 1 HETATM 12956 C C3 . NAG MA 4 . ? -34.328 30.265 34.390 1.00 108.58 ? 705 NAG B C3 1 HETATM 12957 C C4 . NAG MA 4 . ? -35.638 30.907 33.945 1.00 104.25 ? 705 NAG B C4 1 HETATM 12958 C C5 . NAG MA 4 . ? -35.909 30.596 32.472 1.00 97.37 ? 705 NAG B C5 1 HETATM 12959 C C6 . NAG MA 4 . ? -37.106 31.333 31.916 1.00 102.94 ? 705 NAG B C6 1 HETATM 12960 C C7 . NAG MA 4 . ? -30.754 30.474 33.691 1.00 115.45 ? 705 NAG B C7 1 HETATM 12961 C C8 . NAG MA 4 . ? -29.606 29.616 34.127 1.00 128.60 ? 705 NAG B C8 1 HETATM 12962 N N2 . NAG MA 4 . ? -31.970 29.934 33.815 1.00 103.87 ? 705 NAG B N2 1 HETATM 12963 O O3 . NAG MA 4 . ? -33.990 30.705 35.700 1.00 125.21 ? 705 NAG B O3 1 HETATM 12964 O O4 . NAG MA 4 . ? -36.702 30.396 34.743 1.00 119.18 ? 705 NAG B O4 1 HETATM 12965 O O5 . NAG MA 4 . ? -34.782 30.984 31.670 1.00 97.13 ? 705 NAG B O5 1 HETATM 12966 O O6 . NAG MA 4 . ? -36.721 32.266 30.915 1.00 110.51 ? 705 NAG B O6 1 HETATM 12967 O O7 . NAG MA 4 . ? -30.588 31.605 33.243 1.00 119.98 ? 705 NAG B O7 1 HETATM 12968 C C1 . NAG NA 4 . ? -37.476 31.455 35.359 1.00 115.17 ? 706 NAG B C1 1 HETATM 12969 C C2 . NAG NA 4 . ? -38.970 31.109 35.322 1.00 109.27 ? 706 NAG B C2 1 HETATM 12970 C C3 . NAG NA 4 . ? -39.575 31.203 36.719 1.00 112.34 ? 706 NAG B C3 1 HETATM 12971 C C4 . NAG NA 4 . ? -38.747 30.385 37.699 1.00 126.72 ? 706 NAG B C4 1 HETATM 12972 C C5 . NAG NA 4 . ? -37.330 30.946 37.780 1.00 128.02 ? 706 NAG B C5 1 HETATM 12973 C C6 . NAG NA 4 . ? -36.261 29.881 37.697 1.00 120.88 ? 706 NAG B C6 1 HETATM 12974 C C7 . NAG NA 4 . ? -40.319 31.501 33.310 1.00 114.74 ? 706 NAG B C7 1 HETATM 12975 C C8 . NAG NA 4 . ? -41.007 32.525 32.459 1.00 118.28 ? 706 NAG B C8 1 HETATM 12976 N N2 . NAG NA 4 . ? -39.687 31.966 34.393 1.00 113.70 ? 706 NAG B N2 1 HETATM 12977 O O3 . NAG NA 4 . ? -40.912 30.716 36.683 1.00 114.10 ? 706 NAG B O3 1 HETATM 12978 O O4 . NAG NA 4 . ? -39.337 30.365 38.996 1.00 129.61 ? 706 NAG B O4 1 HETATM 12979 O O5 . NAG NA 4 . ? -37.094 31.883 36.713 1.00 117.08 ? 706 NAG B O5 1 HETATM 12980 O O6 . NAG NA 4 . ? -36.787 28.594 37.990 1.00 116.50 ? 706 NAG B O6 1 HETATM 12981 O O7 . NAG NA 4 . ? -40.332 30.307 33.028 1.00 110.83 ? 706 NAG B O7 1 HETATM 12982 C C1 . BMA OA 5 . ? -39.741 31.672 39.456 1.00 127.87 ? 707 BMA B C1 1 HETATM 12983 C C2 . BMA OA 5 . ? -41.149 31.557 40.106 1.00 139.10 ? 707 BMA B C2 1 HETATM 12984 C C3 . BMA OA 5 . ? -41.070 30.905 41.503 1.00 136.18 ? 707 BMA B C3 1 HETATM 12985 C C4 . BMA OA 5 . ? -39.684 31.072 42.141 1.00 133.66 ? 707 BMA B C4 1 HETATM 12986 C C5 . BMA OA 5 . ? -39.091 32.408 41.693 1.00 139.54 ? 707 BMA B C5 1 HETATM 12987 C C6 . BMA OA 5 . ? -37.837 32.788 42.455 1.00 140.64 ? 707 BMA B C6 1 HETATM 12988 O O2 . BMA OA 5 . ? -41.997 30.730 39.324 1.00 119.29 ? 707 BMA B O2 1 HETATM 12989 O O3 . BMA OA 5 . ? -41.438 29.530 41.465 1.00 124.62 ? 707 BMA B O3 1 HETATM 12990 O O4 . BMA OA 5 . ? -39.789 31.040 43.557 1.00 121.66 ? 707 BMA B O4 1 HETATM 12991 O O5 . BMA OA 5 . ? -38.761 32.311 40.287 1.00 129.79 ? 707 BMA B O5 1 HETATM 12992 O O6 . BMA OA 5 . ? -38.176 32.910 43.830 1.00 137.64 ? 707 BMA B O6 1 HETATM 12993 MN MN . MN PA 7 . ? 17.929 35.760 40.351 1.00 65.12 ? 708 MN B MN 1 HETATM 12994 MN MN . MN QA 7 . ? 18.004 33.865 47.518 1.00 115.59 ? 709 MN B MN 1 HETATM 12995 MN MN . MN RA 7 . ? 16.368 38.505 35.267 1.00 99.50 ? 710 MN B MN 1 HETATM 12996 O O . HOH SA 8 . ? 14.898 44.369 39.206 1.00 90.56 ? 1101 HOH A O 1 HETATM 12997 O O . HOH SA 8 . ? 12.479 43.654 34.500 1.00 67.04 ? 1102 HOH A O 1 HETATM 12998 O O . HOH SA 8 . ? 11.984 42.412 30.154 1.00 52.09 ? 1103 HOH A O 1 HETATM 12999 O O . HOH TA 8 . ? 16.829 37.372 41.356 1.00 60.09 ? 801 HOH B O 1 HETATM 13000 O O . HOH TA 8 . ? 16.117 34.787 41.095 1.00 131.69 ? 802 HOH B O 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 . PHE A 1 ? 1.1772 0.9530 1.0063 -0.4609 -0.4326 0.2720 1 PHE A N 2 C CA . PHE A 1 ? 1.2109 1.0023 1.0129 -0.4926 -0.4584 0.2704 1 PHE A CA 3 C C . PHE A 1 ? 1.3973 1.1971 1.1483 -0.5151 -0.4802 0.2872 1 PHE A C 4 O O . PHE A 1 ? 1.5115 1.3228 1.2195 -0.5449 -0.4984 0.2795 1 PHE A O 5 C CB . PHE A 1 ? 1.2410 1.0603 1.1025 -0.4923 -0.4811 0.2913 1 PHE A CB 6 C CG . PHE A 1 ? 1.2761 1.1159 1.1821 -0.4790 -0.5010 0.3314 1 PHE A CG 7 C CD1 . PHE A 1 ? 1.2392 1.1011 1.1336 -0.5005 -0.5369 0.3592 1 PHE A CD1 8 C CD2 . PHE A 1 ? 1.2932 1.1314 1.2545 -0.4449 -0.4845 0.3409 1 PHE A CD2 9 C CE1 . PHE A 1 ? 1.2369 1.1165 1.1789 -0.4871 -0.5567 0.3979 1 PHE A CE1 10 C CE2 . PHE A 1 ? 1.3621 1.2169 1.3700 -0.4307 -0.5027 0.3749 1 PHE A CE2 11 C CZ . PHE A 1 ? 1.2179 1.0923 1.2189 -0.4512 -0.5391 0.4046 1 PHE A CZ 12 N N . ASN A 2 ? 1.2982 1.0934 1.0544 -0.5017 -0.4789 0.3103 2 ASN A N 13 C CA . ASN A 2 ? 1.4176 1.2241 1.1336 -0.5221 -0.5013 0.3356 2 ASN A CA 14 C C . ASN A 2 ? 1.4659 1.2570 1.1137 -0.5332 -0.4819 0.3171 2 ASN A C 15 O O . ASN A 2 ? 1.3566 1.1592 0.9667 -0.5513 -0.4972 0.3390 2 ASN A O 16 C CB . ASN A 2 ? 1.4022 1.2137 1.1699 -0.5035 -0.5164 0.3774 2 ASN A CB 17 C CG . ASN A 2 ? 1.3189 1.1073 1.1326 -0.4672 -0.4883 0.3692 2 ASN A CG 18 O OD1 . ASN A 2 ? 1.3159 1.0977 1.1538 -0.4512 -0.4666 0.3440 2 ASN A OD1 19 N ND2 . ASN A 2 ? 1.2726 1.0495 1.0990 -0.4551 -0.4897 0.3912 2 ASN A ND2 20 N N . LEU A 3 ? 1.3069 1.0754 0.9412 -0.5228 -0.4484 0.2793 3 LEU A N 21 C CA . LEU A 3 ? 1.3126 1.0698 0.8857 -0.5325 -0.4274 0.2584 3 LEU A CA 22 C C . LEU A 3 ? 1.3835 1.1576 0.8916 -0.5665 -0.4382 0.2398 3 LEU A C 23 O O . LEU A 3 ? 1.3784 1.1581 0.8893 -0.5770 -0.4476 0.2216 3 LEU A O 24 C CB . LEU A 3 ? 1.2774 1.0079 0.8601 -0.5108 -0.3899 0.2237 3 LEU A CB 25 C CG . LEU A 3 ? 1.2416 0.9556 0.8724 -0.4791 -0.3739 0.2355 3 LEU A CG 26 C CD1 . LEU A 3 ? 1.2019 0.8946 0.8386 -0.4612 -0.3394 0.2014 3 LEU A CD1 27 C CD2 . LEU A 3 ? 1.2680 0.9802 0.8813 -0.4811 -0.3773 0.2605 3 LEU A CD2 28 N N . ASP A 4 ? 1.4059 1.1898 0.8559 -0.5844 -0.4368 0.2438 4 ASP A N 29 C CA . ASP A 4 ? 1.4898 1.2954 0.8714 -0.6176 -0.4460 0.2249 4 ASP A CA 30 C C . ASP A 4 ? 1.6455 1.4360 0.9879 -0.6178 -0.4122 0.1730 4 ASP A C 31 O O . ASP A 4 ? 1.4636 1.2466 0.7851 -0.6108 -0.3872 0.1666 4 ASP A O 32 C CB . ASP A 4 ? 1.5121 1.3454 0.8487 -0.6402 -0.4643 0.2601 4 ASP A CB 33 C CG . ASP A 4 ? 1.8847 1.7458 1.1414 -0.6748 -0.4693 0.2372 4 ASP A CG 34 O OD1 . ASP A 4 ? 1.7047 1.5655 0.9136 -0.6794 -0.4421 0.2103 4 ASP A OD1 35 O OD2 . ASP A 4 ? 2.0260 1.9102 1.2793 -0.6901 -0.4910 0.2444 4 ASP A OD2 36 N N . VAL A 5 ? 1.5930 1.3789 0.9300 -0.6259 -0.4124 0.1364 5 VAL A N 37 C CA . VAL A 5 ? 1.4951 1.2660 0.7998 -0.6264 -0.3830 0.0843 5 VAL A CA 38 C C . VAL A 5 ? 1.6007 1.3980 0.8304 -0.6577 -0.3888 0.0615 5 VAL A C 39 O O . VAL A 5 ? 1.6774 1.4683 0.8790 -0.6563 -0.3617 0.0167 5 VAL A O 40 C CB . VAL A 5 ? 1.5011 1.2469 0.8492 -0.6150 -0.3771 0.0539 5 VAL A CB 41 C CG1 . VAL A 5 ? 1.4911 1.2197 0.9129 -0.5848 -0.3719 0.0787 5 VAL A CG1 42 C CG2 . VAL A 5 ? 1.7019 1.4629 1.0442 -0.6387 -0.4075 0.0478 5 VAL A CG2 43 N N . ASP A 6 ? 1.6038 1.4340 0.8164 -0.6750 -0.4149 0.0945 6 ASP A N 44 C CA . ASP A 6 ? 1.9116 1.7745 1.0675 -0.6955 -0.4129 0.0787 6 ASP A CA 45 C C . ASP A 6 ? 1.8788 1.7565 0.9833 -0.6999 -0.3867 0.0712 6 ASP A C 46 O O . ASP A 6 ? 1.9159 1.8003 0.9838 -0.7030 -0.3626 0.0263 6 ASP A O 47 C CB . ASP A 6 ? 2.2130 2.1093 1.3687 -0.7130 -0.4479 0.1224 6 ASP A CB 48 C CG . ASP A 6 ? 2.4283 2.3183 1.6309 -0.7115 -0.4731 0.1263 6 ASP A CG 49 O OD1 . ASP A 6 ? 2.4142 2.2814 1.6344 -0.7036 -0.4624 0.0856 6 ASP A OD1 50 O OD2 . ASP A 6 ? 2.5105 2.4195 1.7371 -0.7180 -0.5034 0.1715 6 ASP A OD2 51 N N . SER A 7 ? 1.9016 1.7855 1.0083 -0.6993 -0.3917 0.1155 7 SER A N 52 C CA . SER A 7 ? 1.8975 1.7999 0.9613 -0.7048 -0.3684 0.1166 7 SER A CA 53 C C . SER A 7 ? 1.8232 1.7030 0.9098 -0.6901 -0.3616 0.1434 7 SER A C 54 O O . SER A 7 ? 1.9626 1.8550 1.0559 -0.6947 -0.3768 0.1933 7 SER A O 55 C CB . SER A 7 ? 2.0122 1.9616 1.0432 -0.7282 -0.3836 0.1501 7 SER A CB 56 O OG . SER A 7 ? 2.3362 2.3088 1.3410 -0.7428 -0.3901 0.1233 7 SER A OG 57 N N . PRO A 8 ? 1.6607 1.5061 0.7710 -0.6676 -0.3352 0.1109 8 PRO A N 58 C CA . PRO A 8 ? 1.6809 1.5051 0.8304 -0.6428 -0.3159 0.1305 8 PRO A CA 59 C C . PRO A 8 ? 1.7119 1.5561 0.8148 -0.6520 -0.2914 0.1269 8 PRO A C 60 O O . PRO A 8 ? 1.9887 1.8659 1.0277 -0.6768 -0.2883 0.1087 8 PRO A O 61 C CB . PRO A 8 ? 1.4976 1.2839 0.6949 -0.6141 -0.2937 0.0943 8 PRO A CB 62 C CG . PRO A 8 ? 1.5350 1.3259 0.6965 -0.6268 -0.2863 0.0438 8 PRO A CG 63 C CD . PRO A 8 ? 1.6250 1.4483 0.7437 -0.6585 -0.3190 0.0560 8 PRO A CD 64 N N . ALA A 9 ? 1.5530 1.3804 0.6875 -0.6329 -0.2743 0.1433 9 ALA A N 65 C CA . ALA A 9 ? 1.6566 1.5036 0.7553 -0.6406 -0.2502 0.1430 9 ALA A CA 66 C C . ALA A 9 ? 1.5790 1.4069 0.6898 -0.6192 -0.2116 0.0970 9 ALA A C 67 O O . ALA A 9 ? 1.4806 1.2751 0.6460 -0.5921 -0.2017 0.0967 9 ALA A O 68 C CB . ALA A 9 ? 1.8006 1.6456 0.9251 -0.6385 -0.2604 0.1968 9 ALA A CB 69 N N . GLU A 10 ? 1.6582 1.5097 0.7187 -0.6313 -0.1900 0.0579 10 GLU A N 70 C CA . GLU A 10 ? 1.6307 1.4671 0.7036 -0.6116 -0.1537 0.0124 10 GLU A CA 71 C C . GLU A 10 ? 1.5387 1.3962 0.5960 -0.6127 -0.1276 0.0199 10 GLU A C 72 O O . GLU A 10 ? 1.5899 1.4901 0.5920 -0.6370 -0.1234 0.0246 10 GLU A O 73 C CB . GLU A 10 ? 1.7315 1.5765 0.7688 -0.6199 -0.1439 -0.0429 10 GLU A CB 74 C CG . GLU A 10 ? 1.9058 1.7263 0.9657 -0.6178 -0.1672 -0.0560 10 GLU A CG 75 C CD . GLU A 10 ? 2.2137 2.0401 1.2395 -0.6278 -0.1594 -0.1129 10 GLU A CD 76 O OE1 . GLU A 10 ? 2.4105 2.2643 1.4015 -0.6315 -0.1332 -0.1412 10 GLU A OE1 77 O OE2 . GLU A 10 ? 2.2388 2.0443 1.2856 -0.6269 -0.1768 -0.1278 10 GLU A OE2 78 N N . TYR A 11 ? 1.4845 1.3155 0.5907 -0.5874 -0.1104 0.0218 11 TYR A N 79 C CA . TYR A 11 ? 1.4809 1.3297 0.5816 -0.5863 -0.0846 0.0267 11 TYR A CA 80 C C . TYR A 11 ? 1.4728 1.3115 0.5898 -0.5656 -0.0503 -0.0223 11 TYR A C 81 O O . TYR A 11 ? 1.4244 1.2273 0.5839 -0.5431 -0.0487 -0.0427 11 TYR A O 82 C CB . TYR A 11 ? 1.5883 1.4180 0.7333 -0.5762 -0.0945 0.0724 11 TYR A CB 83 C CG . TYR A 11 ? 1.5595 1.3978 0.6964 -0.5952 -0.1284 0.1243 11 TYR A CG 84 C CD1 . TYR A 11 ? 1.4406 1.2532 0.6090 -0.5881 -0.1576 0.1421 11 TYR A CD1 85 C CD2 . TYR A 11 ? 1.8270 1.7016 0.9286 -0.6203 -0.1314 0.1579 11 TYR A CD2 86 C CE1 . TYR A 11 ? 1.4608 1.2812 0.6283 -0.6037 -0.1896 0.1907 11 TYR A CE1 87 C CE2 . TYR A 11 ? 1.9066 1.7883 1.0057 -0.6378 -0.1644 0.2091 11 TYR A CE2 88 C CZ . TYR A 11 ? 1.8690 1.7223 1.0024 -0.6285 -0.1938 0.2247 11 TYR A CZ 89 O OH . TYR A 11 ? 1.8386 1.6990 0.9757 -0.6442 -0.2277 0.2766 11 TYR A OH 90 N N . SER A 12 ? 1.6603 1.5334 0.7462 -0.5733 -0.0231 -0.0393 12 SER A N 91 C CA . SER A 12 ? 1.6442 1.5126 0.7464 -0.5539 0.0100 -0.0868 12 SER A CA 92 C C . SER A 12 ? 1.4672 1.3582 0.5774 -0.5500 0.0364 -0.0779 12 SER A C 93 O O . SER A 12 ? 1.5052 1.4402 0.5742 -0.5718 0.0431 -0.0622 12 SER A O 94 C CB . SER A 12 ? 1.8306 1.7219 0.8866 -0.5650 0.0216 -0.1362 12 SER A CB 95 O OG . SER A 12 ? 1.9807 1.9266 0.9755 -0.5918 0.0291 -0.1298 12 SER A OG 96 N N . GLY A 13 ? 1.4160 1.2796 0.5799 -0.5234 0.0505 -0.0863 13 GLY A N 97 C CA . GLY A 13 ? 1.4042 1.2876 0.5835 -0.5175 0.0757 -0.0814 13 GLY A CA 98 C C . GLY A 13 ? 1.5461 1.4474 0.7237 -0.5064 0.1098 -0.1321 13 GLY A C 99 O O . GLY A 13 ? 1.5930 1.4898 0.7547 -0.5047 0.1131 -0.1722 13 GLY A O 100 N N . PRO A 14 ? 1.5626 1.4844 0.7604 -0.4986 0.1347 -0.1313 14 PRO A N 101 C CA . PRO A 14 ? 1.5116 1.4539 0.7163 -0.4854 0.1692 -0.1781 14 PRO A CA 102 C C . PRO A 14 ? 1.4315 1.3296 0.6841 -0.4567 0.1720 -0.2122 14 PRO A C 103 O O . PRO A 14 ? 1.4862 1.3432 0.7782 -0.4435 0.1535 -0.1924 14 PRO A O 104 C CB . PRO A 14 ? 1.3972 1.3661 0.6250 -0.4829 0.1879 -0.1564 14 PRO A CB 105 C CG . PRO A 14 ? 1.3610 1.3001 0.6161 -0.4833 0.1616 -0.1074 14 PRO A CG 106 C CD . PRO A 14 ? 1.4101 1.3360 0.6306 -0.5014 0.1306 -0.0864 14 PRO A CD 107 N N . GLU A 15 ? 1.4197 1.3277 0.6704 -0.4475 0.1951 -0.2627 15 GLU A N 108 C CA . GLU A 15 ? 1.5292 1.3953 0.8254 -0.4225 0.1966 -0.2962 15 GLU A CA 109 C C . GLU A 15 ? 1.4118 1.2598 0.7740 -0.3966 0.2060 -0.2854 15 GLU A C 110 O O . GLU A 15 ? 1.3790 1.2577 0.7530 -0.3930 0.2268 -0.2792 15 GLU A O 111 C CB . GLU A 15 ? 1.6458 1.5280 0.9261 -0.4192 0.2197 -0.3554 15 GLU A CB 112 C CG . GLU A 15 ? 1.6855 1.5211 1.0121 -0.3968 0.2178 -0.3912 15 GLU A CG 113 C CD . GLU A 15 ? 2.0355 1.8836 1.3471 -0.3941 0.2388 -0.4534 15 GLU A CD 114 O OE1 . GLU A 15 ? 2.0505 1.9492 1.3231 -0.4042 0.2623 -0.4715 15 GLU A OE1 115 O OE2 . GLU A 15 ? 2.2413 2.0494 1.5812 -0.3822 0.2320 -0.4849 15 GLU A OE2 116 N N . GLY A 16 ? 1.3602 1.1618 0.7653 -0.3800 0.1898 -0.2817 16 GLY A N 117 C CA . GLY A 16 ? 1.3322 1.1164 0.7992 -0.3557 0.1961 -0.2724 16 GLY A CA 118 C C . GLY A 16 ? 1.3161 1.1028 0.7944 -0.3582 0.1850 -0.2249 16 GLY A C 119 O O . GLY A 16 ? 1.3040 1.0831 0.8288 -0.3407 0.1897 -0.2144 16 GLY A O 120 N N . SER A 17 ? 1.3201 1.1170 0.7573 -0.3803 0.1688 -0.1962 17 SER A N 121 C CA . SER A 17 ? 1.3148 1.1137 0.7612 -0.3850 0.1573 -0.1528 17 SER A CA 122 C C . SER A 17 ? 1.2847 1.0439 0.7530 -0.3782 0.1297 -0.1291 17 SER A C 123 O O . SER A 17 ? 1.2738 1.0281 0.7542 -0.3797 0.1177 -0.0964 17 SER A O 124 C CB . SER A 17 ? 1.3249 1.1565 0.7216 -0.4127 0.1536 -0.1302 17 SER A CB 125 O OG . SER A 17 ? 1.3291 1.1529 0.6865 -0.4287 0.1334 -0.1275 17 SER A OG 126 N N . TYR A 18 ? 1.2644 0.9969 0.7399 -0.3708 0.1202 -0.1469 18 TYR A N 127 C CA . TYR A 18 ? 1.2651 0.9653 0.7589 -0.3655 0.0950 -0.1268 18 TYR A CA 128 C C . TYR A 18 ? 1.2404 0.9441 0.7043 -0.3843 0.0730 -0.0939 18 TYR A C 129 O O . TYR A 18 ? 1.2028 0.8902 0.6876 -0.3792 0.0565 -0.0670 18 TYR A O 130 C CB . TYR A 18 ? 1.1844 0.8695 0.7289 -0.3445 0.0957 -0.1140 18 TYR A CB 131 C CG . TYR A 18 ? 1.1602 0.8337 0.7435 -0.3244 0.1090 -0.1393 18 TYR A CG 132 C CD1 . TYR A 18 ? 1.1194 0.7807 0.7480 -0.3059 0.1075 -0.1277 18 TYR A CD1 133 C CD2 . TYR A 18 ? 1.1880 0.8634 0.7641 -0.3241 0.1221 -0.1747 18 TYR A CD2 134 C CE1 . TYR A 18 ? 1.0994 0.7510 0.7669 -0.2884 0.1175 -0.1457 18 TYR A CE1 135 C CE2 . TYR A 18 ? 1.1836 0.8452 0.8019 -0.3052 0.1325 -0.1962 18 TYR A CE2 136 C CZ . TYR A 18 ? 1.1524 0.8022 0.8173 -0.2877 0.1296 -0.1790 18 TYR A CZ 137 O OH . TYR A 18 ? 1.4636 1.1004 1.1736 -0.2697 0.1380 -0.1955 18 TYR A OH 138 N N . PHE A 19 ? 1.2771 1.0039 0.6931 -0.4059 0.0728 -0.0968 19 PHE A N 139 C CA . PHE A 19 ? 1.2915 1.0235 0.6779 -0.4260 0.0498 -0.0646 19 PHE A CA 140 C C . PHE A 19 ? 1.2752 0.9782 0.6741 -0.4221 0.0243 -0.0570 19 PHE A C 141 O O . PHE A 19 ? 1.2715 0.9653 0.6665 -0.4206 0.0225 -0.0821 19 PHE A O 142 C CB . PHE A 19 ? 1.3295 1.0966 0.6592 -0.4507 0.0551 -0.0725 19 PHE A CB 143 C CG . PHE A 19 ? 1.3513 1.1273 0.6492 -0.4736 0.0295 -0.0369 19 PHE A CG 144 C CD1 . PHE A 19 ? 1.5822 1.3494 0.8609 -0.4828 0.0076 -0.0380 19 PHE A CD1 145 C CD2 . PHE A 19 ? 1.3552 1.1495 0.6447 -0.4871 0.0260 -0.0008 19 PHE A CD2 146 C CE1 . PHE A 19 ? 1.5027 1.2802 0.7555 -0.5036 -0.0177 -0.0028 19 PHE A CE1 147 C CE2 . PHE A 19 ? 1.4189 1.2208 0.6837 -0.5083 0.0006 0.0353 19 PHE A CE2 148 C CZ . PHE A 19 ? 1.3658 1.1600 0.6122 -0.5159 -0.0213 0.0347 19 PHE A CZ 149 N N . GLY A 20 ? 1.2733 0.9626 0.6907 -0.4202 0.0046 -0.0232 20 GLY A N 150 C CA . GLY A 20 ? 1.2236 0.8900 0.6586 -0.4149 -0.0187 -0.0132 20 GLY A CA 151 C C . GLY A 20 ? 1.1502 0.7928 0.6358 -0.3901 -0.0176 -0.0141 20 GLY A C 152 O O . GLY A 20 ? 1.3234 0.9504 0.8287 -0.3835 -0.0337 -0.0077 20 GLY A O 153 N N . PHE A 21 ? 1.1344 0.7784 0.6415 -0.3769 0.0013 -0.0209 21 PHE A N 154 C CA . PHE A 21 ? 1.1818 0.8090 0.7339 -0.3545 0.0032 -0.0209 21 PHE A CA 155 C C . PHE A 21 ? 1.1272 0.7437 0.6976 -0.3500 -0.0158 0.0071 21 PHE A C 156 O O . PHE A 21 ? 0.9774 0.5816 0.5794 -0.3341 -0.0210 0.0091 21 PHE A O 157 C CB . PHE A 21 ? 1.0640 0.6996 0.6333 -0.3438 0.0255 -0.0312 21 PHE A CB 158 C CG . PHE A 21 ? 0.9930 0.6165 0.6053 -0.3219 0.0287 -0.0338 21 PHE A CG 159 C CD1 . PHE A 21 ? 0.9891 0.6060 0.6202 -0.3112 0.0375 -0.0542 21 PHE A CD1 160 C CD2 . PHE A 21 ? 0.9496 0.5692 0.5840 -0.3129 0.0223 -0.0157 21 PHE A CD2 161 C CE1 . PHE A 21 ? 1.0281 0.6381 0.6982 -0.2930 0.0395 -0.0519 21 PHE A CE1 162 C CE2 . PHE A 21 ? 0.9116 0.5261 0.5810 -0.2944 0.0253 -0.0174 21 PHE A CE2 163 C CZ . PHE A 21 ? 0.9081 0.5194 0.5949 -0.2850 0.0338 -0.0333 21 PHE A CZ 164 N N . ALA A 22 ? 1.2131 0.8356 0.7651 -0.3641 -0.0260 0.0286 22 ALA A N 165 C CA . ALA A 22 ? 1.0159 0.6262 0.5868 -0.3607 -0.0459 0.0541 22 ALA A CA 166 C C . ALA A 22 ? 1.1434 0.7594 0.6874 -0.3816 -0.0644 0.0773 22 ALA A C 167 O O . ALA A 22 ? 1.4014 1.0351 0.9130 -0.3999 -0.0585 0.0807 22 ALA A O 168 C CB . ALA A 22 ? 1.0324 0.6392 0.6262 -0.3517 -0.0398 0.0607 22 ALA A CB 169 N N . VAL A 23 ? 1.2114 0.8161 0.7704 -0.3791 -0.0868 0.0948 23 VAL A N 170 C CA . VAL A 23 ? 1.2370 0.8473 0.7759 -0.3983 -0.1083 0.1210 23 VAL A CA 171 C C . VAL A 23 ? 1.3273 0.9211 0.9005 -0.3904 -0.1301 0.1471 23 VAL A C 172 O O . VAL A 23 ? 1.5045 1.0847 1.1140 -0.3695 -0.1320 0.1410 23 VAL A O 173 C CB . VAL A 23 ? 1.2222 0.8410 0.7387 -0.4086 -0.1184 0.1149 23 VAL A CB 174 C CG1 . VAL A 23 ? 1.3307 0.9674 0.8066 -0.4215 -0.1001 0.0898 23 VAL A CG1 175 C CG2 . VAL A 23 ? 1.0712 0.6771 0.6213 -0.3897 -0.1227 0.1039 23 VAL A CG2 176 N N . ASP A 24 ? 1.1664 0.7631 0.7294 -0.4073 -0.1462 0.1766 24 ASP A N 177 C CA . ASP A 24 ? 1.2969 0.8765 0.8950 -0.4013 -0.1702 0.2031 24 ASP A CA 178 C C . ASP A 24 ? 1.1538 0.7426 0.7324 -0.4259 -0.1920 0.2391 24 ASP A C 179 O O . ASP A 24 ? 1.3885 0.9987 0.9250 -0.4482 -0.1853 0.2442 24 ASP A O 180 C CB . ASP A 24 ? 1.5547 1.1157 1.1875 -0.3864 -0.1645 0.2015 24 ASP A CB 181 C CG . ASP A 24 ? 1.7466 1.2860 1.4266 -0.3694 -0.1842 0.2135 24 ASP A CG 182 O OD1 . ASP A 24 ? 1.7379 1.2770 1.4249 -0.3747 -0.2067 0.2356 24 ASP A OD1 183 O OD2 . ASP A 24 ? 1.8417 1.3667 1.5528 -0.3505 -0.1774 0.1997 24 ASP A OD2 184 N N . PHE A 25 ? 1.2768 0.8522 0.8877 -0.4215 -0.2179 0.2647 25 PHE A N 185 C CA . PHE A 25 ? 1.3364 0.9184 0.9381 -0.4437 -0.2426 0.3055 25 PHE A CA 186 C C . PHE A 25 ? 1.3505 0.9191 0.9725 -0.4476 -0.2461 0.3263 25 PHE A C 187 O O . PHE A 25 ? 1.2875 0.8348 0.9514 -0.4249 -0.2411 0.3129 25 PHE A O 188 C CB . PHE A 25 ? 1.2017 0.7765 0.8356 -0.4366 -0.2712 0.3262 25 PHE A CB 189 C CG . PHE A 25 ? 1.2616 0.8556 0.8732 -0.4404 -0.2744 0.3148 25 PHE A CG 190 C CD1 . PHE A 25 ? 1.2296 0.8177 0.8634 -0.4181 -0.2646 0.2858 25 PHE A CD1 191 C CD2 . PHE A 25 ? 1.2464 0.8661 0.8152 -0.4679 -0.2885 0.3340 25 PHE A CD2 192 C CE1 . PHE A 25 ? 1.1882 0.7925 0.8057 -0.4233 -0.2694 0.2764 25 PHE A CE1 193 C CE2 . PHE A 25 ? 1.2494 0.8856 0.7985 -0.4729 -0.2936 0.3215 25 PHE A CE2 194 C CZ . PHE A 25 ? 1.2116 0.8385 0.7871 -0.4507 -0.2844 0.2928 25 PHE A CZ 195 N N . PHE A 26 ? 1.2982 0.8911 0.8958 -0.4700 -0.2533 0.3516 26 PHE A N 196 C CA . PHE A 26 ? 1.4594 1.0528 1.0853 -0.4690 -0.2584 0.3689 26 PHE A CA 197 C C . PHE A 26 ? 1.4989 1.0998 1.1493 -0.4748 -0.2902 0.4070 26 PHE A C 198 O O . PHE A 26 ? 1.5792 1.2105 1.1948 -0.4988 -0.3002 0.4291 26 PHE A O 199 C CB . PHE A 26 ? 1.5028 1.1227 1.0871 -0.4903 -0.2376 0.3674 26 PHE A CB 200 C CG . PHE A 26 ? 1.5662 1.1878 1.1802 -0.4914 -0.2418 0.3853 26 PHE A CG 201 C CD1 . PHE A 26 ? 1.5483 1.2051 1.1349 -0.5167 -0.2410 0.4078 26 PHE A CD1 202 C CD2 . PHE A 26 ? 1.5011 1.0911 1.1708 -0.4681 -0.2466 0.3790 26 PHE A CD2 203 C CE1 . PHE A 26 ? 1.3544 1.0128 0.9710 -0.5192 -0.2457 0.4261 26 PHE A CE1 204 C CE2 . PHE A 26 ? 1.4219 1.0110 1.1197 -0.4709 -0.2518 0.3950 26 PHE A CE2 205 C CZ . PHE A 26 ? 1.4073 1.0299 1.0799 -0.4967 -0.2518 0.4199 26 PHE A CZ 206 N N . VAL A 27 ? 1.3269 0.9016 1.0381 -0.4529 -0.3058 0.4135 27 VAL A N 207 C CA . VAL A 27 ? 1.5049 1.0824 1.2507 -0.4548 -0.3371 0.4488 27 VAL A CA 208 C C . VAL A 27 ? 1.5457 1.1100 1.3356 -0.4497 -0.3446 0.4628 27 VAL A C 209 O O . VAL A 27 ? 1.3616 0.8946 1.2055 -0.4255 -0.3507 0.4539 27 VAL A O 210 C CB . VAL A 27 ? 1.5786 1.1368 1.3655 -0.4329 -0.3537 0.4468 27 VAL A CB 211 C CG1 . VAL A 27 ? 1.5893 1.1567 1.4087 -0.4381 -0.3869 0.4857 27 VAL A CG1 212 C CG2 . VAL A 27 ? 1.2811 0.8474 1.0296 -0.4361 -0.3446 0.4288 27 VAL A CG2 213 N N . PRO A 28 ? 1.3579 0.9472 1.1249 -0.4735 -0.3438 0.4839 28 PRO A N 214 C CA . PRO A 28 ? 1.3778 0.9574 1.1844 -0.4734 -0.3521 0.5009 28 PRO A CA 215 C C . PRO A 28 ? 1.6126 1.1784 1.4761 -0.4655 -0.3847 0.5296 28 PRO A C 216 O O . PRO A 28 ? 1.5968 1.1789 1.4562 -0.4729 -0.4036 0.5509 28 PRO A O 217 C CB . PRO A 28 ? 1.5517 1.1721 1.3137 -0.5050 -0.3456 0.5218 28 PRO A CB 218 C CG . PRO A 28 ? 1.4844 1.1291 1.1818 -0.5165 -0.3240 0.5014 28 PRO A CG 219 C CD . PRO A 28 ? 1.5818 1.2121 1.2830 -0.5027 -0.3335 0.4910 28 PRO A CD 220 N N . SER A 29 ? 1.7635 1.3001 1.6811 -0.4512 -0.3917 0.5295 29 SER A N 221 C CA . SER A 29 ? 1.6294 1.1502 1.6076 -0.4430 -0.4223 0.5555 29 SER A CA 222 C C . SER A 29 ? 1.4932 1.0409 1.4714 -0.4702 -0.4412 0.6003 29 SER A C 223 O O . SER A 29 ? 1.5270 1.0743 1.5453 -0.4712 -0.4696 0.6309 29 SER A O 224 C CB . SER A 29 ? 1.5279 1.0051 1.5650 -0.4170 -0.4223 0.5339 29 SER A CB 225 O OG . SER A 29 ? 1.4802 0.9540 1.5114 -0.4254 -0.4088 0.5275 29 SER A OG 226 N N . ALA A 30 ? 1.5004 1.0740 1.4356 -0.4927 -0.4251 0.6047 30 ALA A N 227 C CA . ALA A 30 ? 1.8972 1.4998 1.8312 -0.5200 -0.4398 0.6465 30 ALA A CA 228 C C . ALA A 30 ? 1.5747 1.2266 1.4566 -0.5468 -0.4450 0.6706 30 ALA A C 229 O O . ALA A 30 ? 1.6185 1.3038 1.4910 -0.5728 -0.4558 0.7060 30 ALA A O 230 C CB . ALA A 30 ? 1.9894 1.5979 1.9097 -0.5308 -0.4202 0.6405 30 ALA A CB 231 N N . SER A 31 ? 1.8529 1.5110 1.7010 -0.5417 -0.4378 0.6512 31 SER A N 232 C CA . SER A 31 ? 1.7428 1.4473 1.5376 -0.5674 -0.4418 0.6682 31 SER A CA 233 C C . SER A 31 ? 1.7356 1.4344 1.5315 -0.5565 -0.4539 0.6616 31 SER A C 234 O O . SER A 31 ? 1.5193 1.1841 1.3339 -0.5301 -0.4460 0.6314 31 SER A O 235 C CB . SER A 31 ? 1.7429 1.4770 1.4668 -0.5840 -0.4096 0.6460 31 SER A CB 236 O OG . SER A 31 ? 1.8488 1.6298 1.5190 -0.6101 -0.4124 0.6591 31 SER A OG 237 N N . SER A 32 ? 1.5974 1.3326 1.3743 -0.5781 -0.4734 0.6906 32 SER A N 238 C CA . SER A 32 ? 1.5903 1.3271 1.3663 -0.5724 -0.4871 0.6885 32 SER A CA 239 C C . SER A 32 ? 1.6139 1.3668 1.3197 -0.5803 -0.4634 0.6563 32 SER A C 240 O O . SER A 32 ? 1.7458 1.4923 1.4479 -0.5716 -0.4684 0.6438 32 SER A O 241 C CB . SER A 32 ? 1.6656 1.4368 1.4523 -0.5939 -0.5193 0.7335 32 SER A CB 242 O OG . SER A 32 ? 1.7376 1.5577 1.4687 -0.6282 -0.5138 0.7504 32 SER A OG 243 N N . ARG A 33 ? 1.5714 1.3459 1.2241 -0.5970 -0.4378 0.6431 33 ARG A N 244 C CA . ARG A 33 ? 1.5551 1.3443 1.1410 -0.6052 -0.4124 0.6095 33 ARG A CA 245 C C . ARG A 33 ? 1.6190 1.3657 1.2145 -0.5775 -0.3907 0.5687 33 ARG A C 246 O O . ARG A 33 ? 1.4739 1.1855 1.1184 -0.5550 -0.3881 0.5626 33 ARG A O 247 C CB . ARG A 33 ? 1.5801 1.4093 1.1113 -0.6308 -0.3902 0.6077 33 ARG A CB 248 C CG . ARG A 33 ? 1.8217 1.7017 1.3338 -0.6615 -0.4077 0.6452 33 ARG A CG 249 C CD . ARG A 33 ? 2.0857 2.0046 1.5560 -0.6828 -0.3840 0.6442 33 ARG A CD 250 N NE . ARG A 33 ? 2.1811 2.1134 1.5899 -0.6864 -0.3506 0.6019 33 ARG A NE 251 C CZ . ARG A 33 ? 2.2677 2.2312 1.6392 -0.6993 -0.3226 0.5893 33 ARG A CZ 252 N NH1 . ARG A 33 ? 2.2317 2.2170 1.6201 -0.7110 -0.3245 0.6177 33 ARG A NH1 253 N NH2 . ARG A 33 ? 2.2276 2.2014 1.5477 -0.7002 -0.2925 0.5481 33 ARG A NH2 254 N N . MET A 34 ? 1.8679 1.6186 1.4166 -0.5802 -0.3755 0.5402 34 MET A N 255 C CA . MET A 34 ? 1.7251 1.4408 1.2762 -0.5579 -0.3526 0.5013 34 MET A CA 256 C C . MET A 34 ? 1.4314 1.1662 0.9142 -0.5731 -0.3218 0.4714 34 MET A C 257 O O . MET A 34 ? 1.4673 1.2409 0.8973 -0.5985 -0.3212 0.4754 34 MET A O 258 C CB . MET A 34 ? 1.4107 1.1025 0.9889 -0.5394 -0.3671 0.4945 34 MET A CB 259 C CG . MET A 34 ? 1.7206 1.3802 1.3770 -0.5117 -0.3848 0.5062 34 MET A CG 260 S SD . MET A 34 ? 1.4464 1.0926 1.1399 -0.4941 -0.4076 0.5089 34 MET A SD 261 C CE . MET A 34 ? 1.4365 1.1258 1.1138 -0.5233 -0.4400 0.5515 34 MET A CE 262 N N . PHE A 35 ? 1.3921 1.1013 0.8779 -0.5571 -0.2957 0.4396 35 PHE A N 263 C CA . PHE A 35 ? 1.3902 1.1154 0.8190 -0.5692 -0.2636 0.4099 35 PHE A CA 264 C C . PHE A 35 ? 1.4966 1.1895 0.9243 -0.5519 -0.2452 0.3735 35 PHE A C 265 O O . PHE A 35 ? 1.5823 1.2410 1.0588 -0.5281 -0.2542 0.3695 35 PHE A O 266 C CB . PHE A 35 ? 1.3914 1.1292 0.8226 -0.5732 -0.2444 0.4104 35 PHE A CB 267 C CG . PHE A 35 ? 1.5740 1.3475 1.0043 -0.5931 -0.2592 0.4462 35 PHE A CG 268 C CD1 . PHE A 35 ? 1.4410 1.1998 0.9281 -0.5849 -0.2836 0.4773 35 PHE A CD1 269 C CD2 . PHE A 35 ? 1.6764 1.4996 1.0508 -0.6197 -0.2477 0.4475 35 PHE A CD2 270 C CE1 . PHE A 35 ? 1.5386 1.3297 1.0277 -0.6045 -0.2979 0.5127 35 PHE A CE1 271 C CE2 . PHE A 35 ? 1.6334 1.4927 1.0090 -0.6389 -0.2608 0.4820 35 PHE A CE2 272 C CZ . PHE A 35 ? 1.6326 1.4750 1.0659 -0.6321 -0.2867 0.5165 35 PHE A CZ 273 N N . LEU A 36 ? 1.3473 1.0604 0.7314 -0.5563 -0.2178 0.3378 36 LEU A N 274 C CA . LEU A 36 ? 1.4170 1.1131 0.8163 -0.5301 -0.1960 0.2906 36 LEU A CA 275 C C . LEU A 36 ? 1.3841 1.0769 0.7924 -0.5210 -0.1674 0.2712 36 LEU A C 276 O O . LEU A 36 ? 1.4412 1.1605 0.8195 -0.5396 -0.1540 0.2777 36 LEU A O 277 C CB . LEU A 36 ? 1.3652 1.0831 0.7210 -0.5366 -0.1863 0.2586 36 LEU A CB 278 C CG . LEU A 36 ? 1.4337 1.1535 0.7843 -0.5414 -0.2121 0.2657 36 LEU A CG 279 C CD1 . LEU A 36 ? 1.7742 1.5240 1.0875 -0.5727 -0.2355 0.3045 36 LEU A CD1 280 C CD2 . LEU A 36 ? 1.3678 1.0933 0.6963 -0.5368 -0.1975 0.2208 36 LEU A CD2 281 N N . LEU A 37 ? 1.2764 0.9406 0.7263 -0.4933 -0.1583 0.2489 37 LEU A N 282 C CA . LEU A 37 ? 1.2053 0.8676 0.6659 -0.4828 -0.1319 0.2274 37 LEU A CA 283 C C . LEU A 37 ? 1.4052 1.0689 0.8601 -0.4665 -0.1091 0.1835 37 LEU A C 284 O O . LEU A 37 ? 1.2158 0.8605 0.6945 -0.4478 -0.1144 0.1696 37 LEU A O 285 C CB . LEU A 37 ? 1.1765 0.8075 0.6896 -0.4654 -0.1395 0.2372 37 LEU A CB 286 C CG . LEU A 37 ? 1.3510 0.9752 0.8789 -0.4808 -0.1608 0.2796 37 LEU A CG 287 C CD1 . LEU A 37 ? 1.5107 1.1023 1.0920 -0.4613 -0.1661 0.2795 37 LEU A CD1 288 C CD2 . LEU A 37 ? 1.2366 0.8926 0.7294 -0.5079 -0.1497 0.2953 37 LEU A CD2 289 N N . VAL A 38 ? 1.3446 1.0326 0.7710 -0.4737 -0.0839 0.1627 38 VAL A N 290 C CA . VAL A 38 ? 1.3019 0.9912 0.7249 -0.4595 -0.0626 0.1216 38 VAL A CA 291 C C . VAL A 38 ? 1.3425 1.0371 0.7806 -0.4487 -0.0359 0.1032 38 VAL A C 292 O O . VAL A 38 ? 1.2331 0.9523 0.6537 -0.4628 -0.0233 0.1100 38 VAL A O 293 C CB . VAL A 38 ? 1.2417 0.9574 0.6152 -0.4766 -0.0567 0.1045 38 VAL A CB 294 C CG1 . VAL A 38 ? 1.2541 0.9632 0.6333 -0.4603 -0.0388 0.0618 38 VAL A CG1 295 C CG2 . VAL A 38 ? 1.2580 0.9746 0.6134 -0.4914 -0.0855 0.1265 38 VAL A CG2 296 N N . GLY A 39 ? 1.1965 0.8716 0.6686 -0.4244 -0.0278 0.0823 39 GLY A N 297 C CA . GLY A 39 ? 1.1083 0.7892 0.5989 -0.4126 -0.0045 0.0653 39 GLY A CA 298 C C . GLY A 39 ? 1.1635 0.8635 0.6354 -0.4118 0.0197 0.0325 39 GLY A C 299 O O . GLY A 39 ? 1.4369 1.1325 0.8966 -0.4100 0.0184 0.0134 39 GLY A O 300 N N . ALA A 40 ? 1.1650 0.8867 0.6381 -0.4128 0.0414 0.0250 40 ALA A N 301 C CA . ALA A 40 ? 1.2082 0.9490 0.6725 -0.4082 0.0672 -0.0087 40 ALA A CA 302 C C . ALA A 40 ? 1.1841 0.9316 0.6837 -0.3934 0.0862 -0.0164 40 ALA A C 303 O O . ALA A 40 ? 1.1961 0.9734 0.6889 -0.4025 0.1022 -0.0138 40 ALA A O 304 C CB . ALA A 40 ? 1.2486 1.0253 0.6652 -0.4314 0.0770 -0.0114 40 ALA A CB 305 N N . PRO A 41 ? 1.1437 0.8674 0.6820 -0.3713 0.0841 -0.0240 41 PRO A N 306 C CA . PRO A 41 ? 1.1165 0.8441 0.6927 -0.3568 0.0955 -0.0250 41 PRO A CA 307 C C . PRO A 41 ? 1.1549 0.9102 0.7375 -0.3522 0.1234 -0.0480 41 PRO A C 308 O O . PRO A 41 ? 1.4158 1.1870 1.0219 -0.3486 0.1332 -0.0420 41 PRO A O 309 C CB . PRO A 41 ? 1.0838 0.7833 0.6918 -0.3359 0.0863 -0.0307 41 PRO A CB 310 C CG . PRO A 41 ? 1.2898 0.9762 0.8797 -0.3374 0.0797 -0.0438 41 PRO A CG 311 C CD . PRO A 41 ? 1.1396 0.8350 0.6874 -0.3602 0.0700 -0.0311 41 PRO A CD 312 N N . LYS A 42 ? 1.2187 0.9803 0.7841 -0.3518 0.1354 -0.0752 42 LYS A N 313 C CA . LYS A 42 ? 1.2648 1.0526 0.8403 -0.3448 0.1631 -0.1015 42 LYS A CA 314 C C . LYS A 42 ? 1.2914 1.1191 0.8277 -0.3649 0.1787 -0.1051 42 LYS A C 315 O O . LYS A 42 ? 1.3109 1.1659 0.8514 -0.3601 0.2040 -0.1304 42 LYS A O 316 C CB . LYS A 42 ? 1.2569 1.0271 0.8455 -0.3292 0.1694 -0.1345 42 LYS A CB 317 C CG . LYS A 42 ? 1.2078 0.9515 0.8459 -0.3069 0.1626 -0.1319 42 LYS A CG 318 C CD . LYS A 42 ? 1.3214 1.0499 0.9821 -0.2915 0.1709 -0.1628 42 LYS A CD 319 C CE . LYS A 42 ? 1.2758 0.9859 0.9888 -0.2706 0.1655 -0.1542 42 LYS A CE 320 N NZ . LYS A 42 ? 1.5426 1.2333 1.2843 -0.2563 0.1699 -0.1791 42 LYS A NZ 321 N N . ALA A 43 ? 1.3621 1.1955 0.8621 -0.3874 0.1637 -0.0792 43 ALA A N 322 C CA . ALA A 43 ? 1.3471 1.2229 0.8058 -0.4102 0.1761 -0.0760 43 ALA A CA 323 C C . ALA A 43 ? 1.2757 1.1885 0.7536 -0.4122 0.1966 -0.0679 43 ALA A C 324 O O . ALA A 43 ? 1.2400 1.1423 0.7560 -0.4042 0.1909 -0.0498 43 ALA A O 325 C CB . ALA A 43 ? 1.2719 1.1440 0.6952 -0.4339 0.1514 -0.0417 43 ALA A CB 326 N N . ASN A 44 ? 1.3561 1.3154 0.8074 -0.4236 0.2204 -0.0823 44 ASN A N 327 C CA . ASN A 44 ? 1.3020 1.3055 0.7702 -0.4281 0.2422 -0.0742 44 ASN A CA 328 C C . ASN A 44 ? 1.4147 1.4402 0.8606 -0.4570 0.2308 -0.0300 44 ASN A C 329 O O . ASN A 44 ? 1.4854 1.5145 0.8863 -0.4780 0.2175 -0.0150 44 ASN A O 330 C CB . ASN A 44 ? 1.3039 1.3525 0.7583 -0.4251 0.2763 -0.1126 44 ASN A CB 331 C CG . ASN A 44 ? 1.3137 1.3527 0.8186 -0.3940 0.2940 -0.1474 44 ASN A CG 332 O OD1 . ASN A 44 ? 1.2912 1.3182 0.8451 -0.3799 0.2909 -0.1345 44 ASN A OD1 333 N ND2 . ASN A 44 ? 1.7825 1.8262 1.2773 -0.3834 0.3112 -0.1916 44 ASN A ND2 334 N N . THR A 45 ? 1.5353 1.5759 1.0154 -0.4592 0.2344 -0.0077 45 THR A N 335 C CA . THR A 45 ? 1.4209 1.4729 0.8921 -0.4858 0.2189 0.0382 45 THR A CA 336 C C . THR A 45 ? 1.3639 1.4778 0.8379 -0.5021 0.2430 0.0500 45 THR A C 337 O O . THR A 45 ? 1.2279 1.3736 0.7232 -0.4883 0.2714 0.0233 45 THR A O 338 C CB . THR A 45 ? 1.5222 1.5290 1.0346 -0.4787 0.1926 0.0626 45 THR A CB 339 O OG1 . THR A 45 ? 1.5469 1.5578 1.1078 -0.4590 0.2058 0.0487 45 THR A OG1 340 C CG2 . THR A 45 ? 1.6224 1.5737 1.1310 -0.4655 0.1680 0.0565 45 THR A CG2 341 N N . THR A 46 ? 1.5722 1.7041 1.0282 -0.5317 0.2307 0.0921 46 THR A N 342 C CA . THR A 46 ? 1.4462 1.6397 0.9049 -0.5524 0.2504 0.1121 46 THR A CA 343 C C . THR A 46 ? 1.3721 1.5626 0.8903 -0.5461 0.2493 0.1263 46 THR A C 344 O O . THR A 46 ? 1.3921 1.6339 0.9243 -0.5607 0.2663 0.1420 46 THR A O 345 C CB . THR A 46 ? 1.3193 1.5313 0.7448 -0.5853 0.2323 0.1568 46 THR A CB 346 O OG1 . THR A 46 ? 1.9654 2.2324 1.4117 -0.5946 0.2436 0.1759 46 THR A OG1 347 C CG2 . THR A 46 ? 1.2994 1.4517 0.7447 -0.5889 0.1913 0.1914 46 THR A CG2 348 N N . GLN A 47 ? 1.3579 1.4915 0.9103 -0.5256 0.2288 0.1211 47 GLN A N 349 C CA . GLN A 47 ? 1.2472 1.3736 0.8545 -0.5186 0.2240 0.1312 47 GLN A CA 350 C C . GLN A 47 ? 1.2583 1.4312 0.8954 -0.5038 0.2571 0.1058 47 GLN A C 351 O O . GLN A 47 ? 1.2137 1.3878 0.8492 -0.4805 0.2751 0.0675 47 GLN A O 352 C CB . GLN A 47 ? 1.1230 1.1843 0.7545 -0.4967 0.1988 0.1231 47 GLN A CB 353 C CG . GLN A 47 ? 1.1309 1.1449 0.7368 -0.5051 0.1679 0.1412 47 GLN A CG 354 C CD . GLN A 47 ? 1.4028 1.3595 1.0313 -0.4812 0.1473 0.1285 47 GLN A CD 355 O OE1 . GLN A 47 ? 1.5565 1.4845 1.1646 -0.4694 0.1401 0.1131 47 GLN A OE1 356 N NE2 . GLN A 47 ? 1.4164 1.3595 1.0869 -0.4752 0.1376 0.1351 47 GLN A NE2 357 N N . PRO A 48 ? 1.2975 1.5087 0.9661 -0.5174 0.2643 0.1280 48 PRO A N 358 C CA . PRO A 48 ? 1.1725 1.4363 0.8754 -0.5058 0.2958 0.1093 48 PRO A CA 359 C C . PRO A 48 ? 1.1257 1.3626 0.8714 -0.4712 0.2969 0.0797 48 PRO A C 360 O O . PRO A 48 ? 1.0738 1.2671 0.8449 -0.4645 0.2714 0.0896 48 PRO A O 361 C CB . PRO A 48 ? 1.1511 1.4473 0.8843 -0.5307 0.2912 0.1483 48 PRO A CB 362 C CG . PRO A 48 ? 1.1778 1.4552 0.8773 -0.5611 0.2665 0.1863 48 PRO A CG 363 C CD . PRO A 48 ? 1.2600 1.4685 0.9361 -0.5467 0.2419 0.1742 48 PRO A CD 364 N N . GLY A 49 ? 1.2454 1.5098 0.9996 -0.4499 0.3261 0.0437 49 GLY A N 365 C CA . GLY A 49 ? 1.1487 1.3946 0.9481 -0.4175 0.3293 0.0183 49 GLY A CA 366 C C . GLY A 49 ? 1.1487 1.3261 0.9403 -0.4002 0.3048 0.0074 49 GLY A C 367 O O . GLY A 49 ? 1.1462 1.3021 0.9771 -0.3779 0.2982 -0.0017 49 GLY A O 368 N N . ILE A 50 ? 1.1249 1.2716 0.8669 -0.4112 0.2908 0.0104 50 ILE A N 369 C CA . ILE A 50 ? 1.1670 1.2523 0.9004 -0.3971 0.2675 0.0026 50 ILE A CA 370 C C . ILE A 50 ? 1.2887 1.3632 0.9911 -0.3859 0.2785 -0.0302 50 ILE A C 371 O O . ILE A 50 ? 1.3572 1.4456 1.0128 -0.4028 0.2834 -0.0312 50 ILE A O 372 C CB . ILE A 50 ? 1.1685 1.2184 0.8774 -0.4169 0.2360 0.0340 50 ILE A CB 373 C CG1 . ILE A 50 ? 1.1429 1.1973 0.8852 -0.4284 0.2223 0.0635 50 ILE A CG1 374 C CG2 . ILE A 50 ? 1.0877 1.0801 0.7898 -0.4011 0.2143 0.0246 50 ILE A CG2 375 C CD1 . ILE A 50 ? 1.1022 1.1446 0.8932 -0.4064 0.2178 0.0547 50 ILE A CD1 376 N N . VAL A 51 ? 1.2016 1.2523 0.9312 -0.3586 0.2810 -0.0560 51 VAL A N 377 C CA . VAL A 51 ? 1.2154 1.2500 0.9238 -0.3466 0.2892 -0.0894 51 VAL A CA 378 C C . VAL A 51 ? 1.2107 1.1886 0.9026 -0.3431 0.2613 -0.0852 51 VAL A C 379 O O . VAL A 51 ? 1.1898 1.1374 0.9127 -0.3295 0.2450 -0.0768 51 VAL A O 380 C CB . VAL A 51 ? 1.2630 1.3064 1.0170 -0.3184 0.3101 -0.1213 51 VAL A CB 381 C CG1 . VAL A 51 ? 1.3045 1.3282 1.0385 -0.3078 0.3174 -0.1580 51 VAL A CG1 382 C CG2 . VAL A 51 ? 1.4437 1.5474 1.2206 -0.3195 0.3392 -0.1264 51 VAL A CG2 383 N N . GLU A 52 ? 1.2685 1.2369 0.9115 -0.3560 0.2560 -0.0909 52 GLU A N 384 C CA . GLU A 52 ? 1.2311 1.1515 0.8561 -0.3552 0.2300 -0.0861 52 GLU A CA 385 C C . GLU A 52 ? 1.1777 1.0720 0.8158 -0.3594 0.2035 -0.0522 52 GLU A C 386 O O . GLU A 52 ? 1.1515 1.0139 0.8164 -0.3429 0.1902 -0.0520 52 GLU A O 387 C CB . GLU A 52 ? 1.2599 1.1513 0.9097 -0.3303 0.2316 -0.1148 52 GLU A CB 388 C CG . GLU A 52 ? 1.4025 1.3093 1.0396 -0.3250 0.2541 -0.1539 52 GLU A CG 389 C CD . GLU A 52 ? 1.5725 1.4425 1.2343 -0.3037 0.2500 -0.1786 52 GLU A CD 390 O OE1 . GLU A 52 ? 1.6183 1.4561 1.3069 -0.2930 0.2313 -0.1629 52 GLU A OE1 391 O OE2 . GLU A 52 ? 1.5471 1.4215 1.2023 -0.2981 0.2654 -0.2142 52 GLU A OE2 392 N N . GLY A 53 ? 1.3424 1.2516 0.9624 -0.3821 0.1959 -0.0238 53 GLY A N 393 C CA . GLY A 53 ? 1.2905 1.1744 0.9241 -0.3873 0.1707 0.0059 53 GLY A CA 394 C C . GLY A 53 ? 1.2894 1.1318 0.9032 -0.3877 0.1457 0.0126 53 GLY A C 395 O O . GLY A 53 ? 1.3248 1.1365 0.9592 -0.3792 0.1265 0.0228 53 GLY A O 396 N N . GLY A 54 ? 1.3287 1.1735 0.9027 -0.3975 0.1461 0.0057 54 GLY A N 397 C CA . GLY A 54 ? 1.1378 0.9487 0.6931 -0.3997 0.1222 0.0136 54 GLY A CA 398 C C . GLY A 54 ? 1.1426 0.9585 0.6689 -0.4254 0.1059 0.0452 54 GLY A C 399 O O . GLY A 54 ? 1.4779 1.3124 1.0095 -0.4399 0.1067 0.0678 54 GLY A O 400 N N . GLN A 55 ? 1.1512 0.9512 0.6496 -0.4320 0.0897 0.0493 55 GLN A N 401 C CA . GLN A 55 ? 1.2245 1.0299 0.6957 -0.4568 0.0717 0.0821 55 GLN A CA 402 C C . GLN A 55 ? 1.3254 1.0937 0.7975 -0.4542 0.0425 0.0959 55 GLN A C 403 O O . GLN A 55 ? 1.3688 1.1144 0.8496 -0.4366 0.0388 0.0760 55 GLN A O 404 C CB . GLN A 55 ? 1.2107 1.0560 0.6328 -0.4769 0.0852 0.0764 55 GLN A CB 405 C CG . GLN A 55 ? 1.3393 1.2315 0.7557 -0.4886 0.1107 0.0769 55 GLN A CG 406 C CD . GLN A 55 ? 1.4598 1.3963 0.8224 -0.5119 0.1216 0.0760 55 GLN A CD 407 O OE1 . GLN A 55 ? 1.4043 1.3351 0.7325 -0.5189 0.1097 0.0718 55 GLN A OE1 408 N NE2 . GLN A 55 ? 1.7112 1.6959 1.0659 -0.5251 0.1441 0.0801 55 GLN A NE2 409 N N . VAL A 56 ? 1.4650 1.2290 0.9322 -0.4719 0.0214 0.1320 56 VAL A N 410 C CA . VAL A 56 ? 1.2667 1.0040 0.7313 -0.4737 -0.0068 0.1495 56 VAL A CA 411 C C . VAL A 56 ? 1.4212 1.1836 0.8453 -0.5028 -0.0168 0.1771 56 VAL A C 412 O O . VAL A 56 ? 1.3551 1.1317 0.7790 -0.5218 -0.0213 0.2080 56 VAL A O 413 C CB . VAL A 56 ? 1.1685 0.8704 0.6759 -0.4644 -0.0282 0.1695 56 VAL A CB 414 C CG1 . VAL A 56 ? 1.1417 0.8198 0.6501 -0.4653 -0.0567 0.1881 56 VAL A CG1 415 C CG2 . VAL A 56 ? 1.2740 0.9571 0.8169 -0.4372 -0.0185 0.1431 56 VAL A CG2 416 N N . LEU A 57 ? 1.5543 1.3240 0.9446 -0.5081 -0.0215 0.1676 57 LEU A N 417 C CA . LEU A 57 ? 1.6774 1.4793 1.0216 -0.5372 -0.0291 0.1906 57 LEU A CA 418 C C . LEU A 57 ? 1.5242 1.3060 0.8714 -0.5456 -0.0644 0.2253 57 LEU A C 419 O O . LEU A 57 ? 1.3120 1.0613 0.6823 -0.5280 -0.0792 0.2176 57 LEU A O 420 C CB . LEU A 57 ? 1.6470 1.4780 0.9456 -0.5418 -0.0111 0.1560 57 LEU A CB 421 C CG . LEU A 57 ? 1.4489 1.3076 0.7410 -0.5357 0.0253 0.1211 57 LEU A CG 422 C CD1 . LEU A 57 ? 1.3746 1.2045 0.7004 -0.5049 0.0376 0.0816 57 LEU A CD1 423 C CD2 . LEU A 57 ? 1.4735 1.3789 0.7078 -0.5555 0.0402 0.1047 57 LEU A CD2 424 N N . LYS A 58 ? 1.3329 1.1371 0.6595 -0.5730 -0.0779 0.2657 58 LYS A N 425 C CA . LYS A 58 ? 1.3547 1.1456 0.6839 -0.5840 -0.1128 0.3039 58 LYS A CA 426 C C . LYS A 58 ? 1.4000 1.2257 0.6723 -0.6050 -0.1183 0.3049 58 LYS A C 427 O O . LYS A 58 ? 1.5139 1.3876 0.7537 -0.6237 -0.1088 0.3094 58 LYS A O 428 C CB . LYS A 58 ? 1.6088 1.4071 0.9758 -0.5880 -0.1302 0.3411 58 LYS A CB 429 C CG . LYS A 58 ? 1.6505 1.4436 1.0364 -0.5916 -0.1671 0.3761 58 LYS A CG 430 C CD . LYS A 58 ? 1.4607 1.2483 0.8973 -0.5887 -0.1838 0.4074 58 LYS A CD 431 C CE . LYS A 58 ? 1.5726 1.4052 0.9918 -0.6080 -0.1681 0.4185 58 LYS A CE 432 N NZ . LYS A 58 ? 1.4870 1.3698 0.8593 -0.6337 -0.1720 0.4339 58 LYS A NZ 433 N N . CYS A 59 ? 1.3935 1.2012 0.6665 -0.5952 -0.1343 0.2933 59 CYS A N 434 C CA . CYS A 59 ? 1.6529 1.4916 0.8724 -0.6141 -0.1410 0.2882 59 CYS A CA 435 C C . CYS A 59 ? 1.4659 1.3084 0.6892 -0.6291 -0.1790 0.3338 59 CYS A C 436 O O . CYS A 59 ? 1.4435 1.2494 0.7085 -0.6154 -0.2027 0.3503 59 CYS A O 437 C CB . CYS A 59 ? 1.7677 1.5904 0.9871 -0.5943 -0.1331 0.2403 59 CYS A CB 438 S SG . CYS A 59 ? 1.6678 1.4932 0.8869 -0.5752 -0.0895 0.1824 59 CYS A SG 439 N N . ASP A 60 ? 1.5137 1.4061 0.7076 -0.6513 -0.1837 0.3481 60 ASP A N 440 C CA . ASP A 60 ? 1.7290 1.6354 0.9373 -0.6629 -0.2190 0.3878 60 ASP A CA 441 C C . ASP A 60 ? 1.7813 1.6930 0.9586 -0.6703 -0.2350 0.3776 60 ASP A C 442 O O . ASP A 60 ? 2.2608 2.2021 1.3846 -0.6822 -0.2191 0.3462 60 ASP A O 443 C CB . ASP A 60 ? 1.8381 1.7985 1.0310 -0.6852 -0.2177 0.4112 60 ASP A CB 444 C CG . ASP A 60 ? 2.0253 2.0009 1.2378 -0.6981 -0.2546 0.4562 60 ASP A CG 445 O OD1 . ASP A 60 ? 2.1515 2.1790 1.3340 -0.7216 -0.2566 0.4705 60 ASP A OD1 446 O OD2 . ASP A 60 ? 1.9699 1.9075 1.2305 -0.6840 -0.2811 0.4769 60 ASP A OD2 447 N N . TRP A 61 ? 1.5517 1.4358 0.7670 -0.6618 -0.2665 0.4018 61 TRP A N 448 C CA . TRP A 61 ? 1.5880 1.4762 0.7831 -0.6682 -0.2862 0.3967 61 TRP A CA 449 C C . TRP A 61 ? 1.6864 1.6250 0.8599 -0.6941 -0.3052 0.4210 61 TRP A C 450 O O . TRP A 61 ? 1.6538 1.6155 0.7873 -0.7072 -0.3089 0.4032 61 TRP A O 451 C CB . TRP A 61 ? 1.5331 1.3763 0.7837 -0.6477 -0.3120 0.4140 61 TRP A CB 452 C CG . TRP A 61 ? 1.6292 1.4794 0.8681 -0.6545 -0.3363 0.4148 61 TRP A CG 453 C CD1 . TRP A 61 ? 1.6416 1.4870 0.8435 -0.6548 -0.3302 0.3784 61 TRP A CD1 454 C CD2 . TRP A 61 ? 1.7541 1.6188 1.0224 -0.6617 -0.3721 0.4529 61 TRP A CD2 455 N NE1 . TRP A 61 ? 1.6944 1.5515 0.9016 -0.6624 -0.3602 0.3915 61 TRP A NE1 456 C CE2 . TRP A 61 ? 1.8643 1.7339 1.1117 -0.6669 -0.3855 0.4383 61 TRP A CE2 457 C CE3 . TRP A 61 ? 1.7879 1.6626 1.1011 -0.6642 -0.3948 0.4974 61 TRP A CE3 458 C CZ2 . TRP A 61 ? 1.8969 1.7826 1.1675 -0.6747 -0.4195 0.4681 61 TRP A CZ2 459 C CZ3 . TRP A 61 ? 1.8765 1.7660 1.2121 -0.6715 -0.4284 0.5268 61 TRP A CZ3 460 C CH2 . TRP A 61 ? 1.9273 1.8230 1.2417 -0.6769 -0.4400 0.5128 61 TRP A CH2 461 N N . SER A 62 ? 1.6430 1.5986 0.8455 -0.7014 -0.3178 0.4612 62 SER A N 462 C CA . SER A 62 ? 1.9878 1.9885 1.1805 -0.7255 -0.3405 0.4938 62 SER A CA 463 C C . SER A 62 ? 2.2794 2.3353 1.4037 -0.7497 -0.3210 0.4709 62 SER A C 464 O O . SER A 62 ? 2.3408 2.4222 1.4362 -0.7645 -0.3338 0.4675 62 SER A O 465 C CB . SER A 62 ? 2.1220 2.1289 1.3602 -0.7281 -0.3549 0.5395 62 SER A CB 466 O OG . SER A 62 ? 2.2181 2.2396 1.4431 -0.7308 -0.3269 0.5308 62 SER A OG 467 N N . SER A 63 ? 2.4116 2.4875 1.5126 -0.7526 -0.2897 0.4535 63 SER A N 468 C CA . SER A 63 ? 2.3704 2.5049 1.4129 -0.7741 -0.2697 0.4338 63 SER A CA 469 C C . SER A 63 ? 2.4753 2.6118 1.4819 -0.7651 -0.2282 0.3785 63 SER A C 470 O O . SER A 63 ? 2.4121 2.5231 1.4402 -0.7493 -0.2091 0.3700 63 SER A O 471 C CB . SER A 63 ? 2.0679 2.2462 1.1170 -0.7925 -0.2738 0.4746 63 SER A CB 472 O OG . SER A 63 ? 1.8100 1.9695 0.8924 -0.7802 -0.2598 0.4830 63 SER A OG 473 N N . THR A 64 ? 2.4549 2.6213 1.4104 -0.7744 -0.2151 0.3397 64 THR A N 474 C CA . THR A 64 ? 2.2500 2.4317 1.1691 -0.7683 -0.1748 0.2841 64 THR A CA 475 C C . THR A 64 ? 1.9707 2.0985 0.9045 -0.7427 -0.1579 0.2459 64 THR A C 476 O O . THR A 64 ? 1.8974 2.0321 0.8064 -0.7349 -0.1263 0.1952 64 THR A O 477 C CB . THR A 64 ? 2.0313 2.2548 0.9452 -0.7753 -0.1499 0.2927 64 THR A CB 478 O OG1 . THR A 64 ? 2.0758 2.2650 1.0374 -0.7620 -0.1497 0.3184 64 THR A OG1 479 C CG2 . THR A 64 ? 2.0779 2.3585 0.9762 -0.8020 -0.1658 0.3317 64 THR A CG2 480 N N . ARG A 65 ? 1.7229 1.7983 0.6991 -0.7290 -0.1788 0.2696 65 ARG A N 481 C CA . ARG A 65 ? 1.8964 1.9192 0.8894 -0.7054 -0.1662 0.2403 65 ARG A CA 482 C C . ARG A 65 ? 1.8600 1.8860 0.8533 -0.6953 -0.1286 0.2174 65 ARG A C 483 O O . ARG A 65 ? 1.9328 1.9350 0.9205 -0.6798 -0.1064 0.1742 65 ARG A O 484 C CB . ARG A 65 ? 1.9749 1.9852 0.9419 -0.7010 -0.1652 0.1930 65 ARG A CB 485 C CG . ARG A 65 ? 2.2253 2.2432 1.1878 -0.7137 -0.2000 0.2111 65 ARG A CG 486 C CD . ARG A 65 ? 2.1810 2.1613 1.1912 -0.7062 -0.2340 0.2577 65 ARG A CD 487 N NE . ARG A 65 ? 2.2745 2.2725 1.2859 -0.7210 -0.2678 0.2843 65 ARG A NE 488 C CZ . ARG A 65 ? 2.0630 2.0518 1.0673 -0.7210 -0.2830 0.2644 65 ARG A CZ 489 N NH1 . ARG A 65 ? 1.7426 1.7032 0.7399 -0.7070 -0.2682 0.2162 65 ARG A NH1 490 N NH2 . ARG A 65 ? 2.0374 2.0461 1.0460 -0.7354 -0.3137 0.2928 65 ARG A NH2 491 N N . ARG A 66 ? 1.7355 1.7926 0.7390 -0.7044 -0.1226 0.2469 66 ARG A N 492 C CA . ARG A 66 ? 1.6689 1.7363 0.6777 -0.6968 -0.0885 0.2309 66 ARG A CA 493 C C . ARG A 66 ? 1.6821 1.6962 0.7378 -0.6769 -0.0880 0.2419 66 ARG A C 494 O O . ARG A 66 ? 1.6214 1.5986 0.7132 -0.6714 -0.1166 0.2750 66 ARG A O 495 C CB . ARG A 66 ? 1.8598 1.9811 0.8665 -0.7144 -0.0849 0.2612 66 ARG A CB 496 C CG . ARG A 66 ? 2.1913 2.3745 1.1481 -0.7291 -0.0648 0.2331 66 ARG A CG 497 C CD . ARG A 66 ? 2.3026 2.5176 1.2554 -0.7243 -0.0255 0.2094 66 ARG A CD 498 N NE . ARG A 66 ? 2.3272 2.5643 1.3070 -0.7333 -0.0289 0.2549 66 ARG A NE 499 C CZ . ARG A 66 ? 2.1923 2.3980 1.2167 -0.7213 -0.0268 0.2728 66 ARG A CZ 500 N NH1 . ARG A 66 ? 1.9242 2.0769 0.9691 -0.7003 -0.0201 0.2502 66 ARG A NH1 501 N NH2 . ARG A 66 ? 1.9983 2.2262 1.0479 -0.7309 -0.0319 0.3132 66 ARG A NH2 502 N N . CYS A 67 ? 1.8251 1.8370 0.8838 -0.6651 -0.0547 0.2129 67 CYS A N 503 C CA . CYS A 67 ? 1.7437 1.7094 0.8470 -0.6468 -0.0502 0.2201 67 CYS A CA 504 C C . CYS A 67 ? 1.8756 1.8669 0.9976 -0.6465 -0.0256 0.2243 67 CYS A C 505 O O . CYS A 67 ? 2.0393 2.0719 1.1347 -0.6500 0.0041 0.1950 67 CYS A O 506 C CB . CYS A 67 ? 1.4667 1.3955 0.5940 -0.6163 -0.0374 0.1693 67 CYS A CB 507 S SG . CYS A 67 ? 2.6560 2.5495 1.7894 -0.6080 -0.0686 0.1632 67 CYS A SG 508 N N . GLN A 68 ? 1.8321 1.7995 1.0041 -0.6409 -0.0390 0.2586 68 GLN A N 509 C CA . GLN A 68 ? 1.7340 1.7214 0.9310 -0.6400 -0.0196 0.2650 68 GLN A CA 510 C C . GLN A 68 ? 1.5772 1.5151 0.8221 -0.6194 -0.0158 0.2606 68 GLN A C 511 O O . GLN A 68 ? 1.5964 1.4865 0.8726 -0.6083 -0.0401 0.2742 68 GLN A O 512 C CB . GLN A 68 ? 1.4953 1.5092 0.7111 -0.6552 -0.0405 0.3117 68 GLN A CB 513 C CG . GLN A 68 ? 1.6003 1.6672 0.7726 -0.6775 -0.0461 0.3212 68 GLN A CG 514 C CD . GLN A 68 ? 2.0311 2.1186 1.2263 -0.6929 -0.0708 0.3722 68 GLN A CD 515 O OE1 . GLN A 68 ? 2.1875 2.3211 1.3531 -0.7128 -0.0775 0.3873 68 GLN A OE1 516 N NE2 . GLN A 68 ? 2.1118 2.1653 1.3612 -0.6835 -0.0849 0.3980 68 GLN A NE2 517 N N . PRO A 69 ? 1.4471 1.3992 0.7014 -0.6134 0.0149 0.2402 69 PRO A N 518 C CA . PRO A 69 ? 1.3413 1.2540 0.6510 -0.5897 0.0178 0.2313 69 PRO A CA 519 C C . PRO A 69 ? 1.4056 1.3006 0.7597 -0.5933 -0.0054 0.2725 69 PRO A C 520 O O . PRO A 69 ? 1.4605 1.3912 0.8171 -0.6072 -0.0086 0.2973 69 PRO A O 521 C CB . PRO A 69 ? 1.3334 1.2802 0.6437 -0.5827 0.0554 0.1993 69 PRO A CB 522 C CG . PRO A 69 ? 1.3766 1.3692 0.6303 -0.5951 0.0740 0.1765 69 PRO A CG 523 C CD . PRO A 69 ? 1.5325 1.5411 0.7540 -0.6210 0.0486 0.2147 69 PRO A CD 524 N N . ILE A 70 ? 1.3175 1.1600 0.7134 -0.5755 -0.0226 0.2745 70 ILE A N 525 C CA . ILE A 70 ? 1.3442 1.1677 0.7932 -0.5692 -0.0425 0.2998 70 ILE A CA 526 C C . ILE A 70 ? 1.4427 1.2759 0.9156 -0.5641 -0.0196 0.2865 70 ILE A C 527 O O . ILE A 70 ? 1.6688 1.4921 1.1405 -0.5530 0.0014 0.2557 70 ILE A O 528 C CB . ILE A 70 ? 1.2592 1.0269 0.7460 -0.5488 -0.0687 0.3014 70 ILE A CB 529 C CG1 . ILE A 70 ? 1.2796 1.0398 0.7448 -0.5529 -0.0901 0.3127 70 ILE A CG1 530 C CG2 . ILE A 70 ? 1.3791 1.1288 0.9191 -0.5423 -0.0890 0.3241 70 ILE A CG2 531 C CD1 . ILE A 70 ? 1.2544 0.9658 0.7586 -0.5312 -0.1139 0.3125 70 ILE A CD1 532 N N . GLU A 71 ? 1.3093 1.1626 0.8064 -0.5728 -0.0240 0.3105 71 GLU A N 533 C CA . GLU A 71 ? 1.4379 1.3062 0.9589 -0.5702 -0.0033 0.3002 71 GLU A CA 534 C C . GLU A 71 ? 1.3559 1.1815 0.9323 -0.5552 -0.0223 0.3050 71 GLU A C 535 O O . GLU A 71 ? 1.3375 1.1558 0.9424 -0.5598 -0.0440 0.3324 71 GLU A O 536 C CB . GLU A 71 ? 1.5466 1.4709 1.0585 -0.5905 0.0079 0.3207 71 GLU A CB 537 C CG . GLU A 71 ? 1.6322 1.5898 1.1548 -0.5904 0.0389 0.3041 71 GLU A CG 538 C CD . GLU A 71 ? 2.0108 2.0313 1.5191 -0.6100 0.0531 0.3217 71 GLU A CD 539 O OE1 . GLU A 71 ? 2.1727 2.2352 1.6719 -0.6107 0.0856 0.3016 71 GLU A OE1 540 O OE2 . GLU A 71 ? 1.9909 2.0207 1.4995 -0.6241 0.0322 0.3556 71 GLU A OE2 541 N N . PHE A 72 ? 1.2752 1.0734 0.8665 -0.5371 -0.0138 0.2764 72 PHE A N 542 C CA . PHE A 72 ? 1.2254 0.9859 0.8654 -0.5209 -0.0293 0.2728 72 PHE A CA 543 C C . PHE A 72 ? 1.4675 1.2487 1.1359 -0.5253 -0.0178 0.2734 72 PHE A C 544 O O . PHE A 72 ? 1.8191 1.5841 1.5255 -0.5240 -0.0358 0.2867 72 PHE A O 545 C CB . PHE A 72 ? 1.2547 0.9800 0.8979 -0.4994 -0.0272 0.2425 72 PHE A CB 546 C CG . PHE A 72 ? 1.3428 1.0398 0.9736 -0.4914 -0.0455 0.2439 72 PHE A CG 547 C CD1 . PHE A 72 ? 1.5377 1.2487 1.1238 -0.5003 -0.0367 0.2406 72 PHE A CD1 548 C CD2 . PHE A 72 ? 1.1240 0.7826 0.7892 -0.4750 -0.0708 0.2471 72 PHE A CD2 549 C CE1 . PHE A 72 ? 1.3660 1.0532 0.9433 -0.4942 -0.0550 0.2435 72 PHE A CE1 550 C CE2 . PHE A 72 ? 1.1742 0.8109 0.8329 -0.4668 -0.0870 0.2492 72 PHE A CE2 551 C CZ . PHE A 72 ? 1.1643 0.8155 0.7800 -0.4768 -0.0802 0.2490 72 PHE A CZ 552 N N . ASP A 73 ? 1.1496 0.9675 0.8012 -0.5307 0.0125 0.2582 73 ASP A N 553 C CA . ASP A 73 ? 1.4244 1.2631 1.1062 -0.5321 0.0256 0.2542 73 ASP A CA 554 C C . ASP A 73 ? 1.5957 1.4949 1.2646 -0.5507 0.0485 0.2659 73 ASP A C 555 O O . ASP A 73 ? 1.5981 1.5150 1.2914 -0.5619 0.0413 0.2889 73 ASP A O 556 C CB . ASP A 73 ? 1.0963 0.9250 0.7855 -0.5149 0.0421 0.2206 73 ASP A CB 557 C CG . ASP A 73 ? 1.5419 1.3909 1.2678 -0.5143 0.0516 0.2164 73 ASP A CG 558 O OD1 . ASP A 73 ? 1.8193 1.6904 1.5511 -0.4966 0.0735 0.1897 73 ASP A OD1 559 O OD2 . ASP A 73 ? 1.6485 1.4938 1.4040 -0.5226 0.0347 0.2362 73 ASP A OD2 560 N N . ALA A 74 ? 1.4059 1.3373 1.0385 -0.5529 0.0770 0.2474 74 ALA A N 561 C CA . ALA A 74 ? 1.6845 1.6801 1.3013 -0.5668 0.1045 0.2503 74 ALA A CA 562 C C . ALA A 74 ? 1.3820 1.4069 1.0378 -0.5655 0.1218 0.2457 74 ALA A C 563 O O . ALA A 74 ? 1.1854 1.2673 0.8364 -0.5737 0.1473 0.2452 74 ALA A O 564 C CB . ALA A 74 ? 1.2316 1.2503 0.8358 -0.5853 0.0902 0.2848 74 ALA A CB 565 N N . THR A 75 ? 1.2967 1.2856 0.9919 -0.5547 0.1074 0.2416 75 THR A N 566 C CA . THR A 75 ? 1.3623 1.3765 1.0987 -0.5542 0.1185 0.2391 75 THR A CA 567 C C . THR A 75 ? 1.0847 1.1068 0.8314 -0.5270 0.1404 0.2004 75 THR A C 568 O O . THR A 75 ? 1.1255 1.1103 0.8639 -0.5038 0.1341 0.1769 75 THR A O 569 C CB . THR A 75 ? 1.3413 1.3160 1.1202 -0.5518 0.0871 0.2520 75 THR A CB 570 O OG1 . THR A 75 ? 1.4964 1.4559 1.2742 -0.5628 0.0620 0.2811 75 THR A OG1 571 C CG2 . THR A 75 ? 1.3265 1.3338 1.1478 -0.5561 0.0956 0.2547 75 THR A CG2 572 N N . GLY A 76 ? 1.1305 1.2029 0.9002 -0.5266 0.1647 0.1945 76 GLY A N 573 C CA . GLY A 76 ? 1.0493 1.1317 0.8409 -0.4973 0.1829 0.1605 76 GLY A CA 574 C C . GLY A 76 ? 1.0172 1.0686 0.8495 -0.4839 0.1633 0.1570 76 GLY A C 575 O O . GLY A 76 ? 1.0631 1.0732 0.8994 -0.4917 0.1347 0.1718 76 GLY A O 576 N N . ASN A 77 ? 0.9901 1.0627 0.8538 -0.4634 0.1784 0.1368 77 ASN A N 577 C CA . ASN A 77 ? 1.0056 1.0562 0.9055 -0.4501 0.1609 0.1322 77 ASN A CA 578 C C . ASN A 77 ? 1.2113 1.2783 1.1453 -0.4714 0.1480 0.1563 77 ASN A C 579 O O . ASN A 77 ? 1.1396 1.2575 1.0913 -0.4857 0.1647 0.1687 77 ASN A O 580 C CB . ASN A 77 ? 0.9555 1.0263 0.8807 -0.4221 0.1797 0.1066 77 ASN A CB 581 C CG . ASN A 77 ? 1.1673 1.2115 1.0664 -0.3998 0.1865 0.0817 77 ASN A CG 582 O OD1 . ASN A 77 ? 0.9582 0.9573 0.8304 -0.3983 0.1684 0.0810 77 ASN A OD1 583 N ND2 . ASN A 77 ? 1.7665 1.8388 1.6777 -0.3821 0.2121 0.0607 77 ASN A ND2 584 N N . ARG A 78 ? 1.0467 1.0717 0.9909 -0.4736 0.1182 0.1616 78 ARG A N 585 C CA . ARG A 78 ? 1.0799 1.1130 1.0597 -0.4925 0.1014 0.1798 78 ARG A CA 586 C C . ARG A 78 ? 1.0923 1.1568 1.1124 -0.4784 0.1080 0.1681 78 ARG A C 587 O O . ARG A 78 ? 0.9701 1.0337 0.9909 -0.4515 0.1174 0.1460 78 ARG A O 588 C CB . ARG A 78 ? 0.9673 0.9425 0.9442 -0.4985 0.0670 0.1842 78 ARG A CB 589 C CG . ARG A 78 ? 0.9967 0.9460 0.9478 -0.5192 0.0555 0.2060 78 ARG A CG 590 C CD . ARG A 78 ? 1.0030 0.8914 0.9554 -0.5196 0.0224 0.2055 78 ARG A CD 591 N NE . ARG A 78 ? 0.9831 0.8368 0.9127 -0.4921 0.0197 0.1804 78 ARG A NE 592 C CZ . ARG A 78 ? 1.0841 0.8869 1.0093 -0.4866 -0.0044 0.1752 78 ARG A CZ 593 N NH1 . ARG A 78 ? 1.0731 0.8525 1.0177 -0.4973 -0.0283 0.1883 78 ARG A NH1 594 N NH2 . ARG A 78 ? 1.2125 0.9920 1.1187 -0.4617 -0.0039 0.1535 78 ARG A NH2 595 N N . ASP A 79 ? 0.9399 1.0335 0.9962 -0.4976 0.1019 0.1853 79 ASP A N 596 C CA . ASP A 79 ? 1.0339 1.1673 1.1326 -0.4872 0.1087 0.1789 79 ASP A CA 597 C C . ASP A 79 ? 1.0291 1.1431 1.1542 -0.4917 0.0783 0.1790 79 ASP A C 598 O O . ASP A 79 ? 1.3494 1.4431 1.4802 -0.5158 0.0557 0.1939 79 ASP A O 599 C CB . ASP A 79 ? 1.3028 1.5017 1.4289 -0.5042 0.1309 0.1967 79 ASP A CB 600 C CG . ASP A 79 ? 1.5700 1.8008 1.6748 -0.4946 0.1659 0.1886 79 ASP A CG 601 O OD1 . ASP A 79 ? 1.4939 1.7827 1.6281 -0.4894 0.1911 0.1869 79 ASP A OD1 602 O OD2 . ASP A 79 ? 1.8712 2.0707 1.9310 -0.4922 0.1680 0.1828 79 ASP A OD2 603 N N . TYR A 80 ? 0.8855 1.0065 1.0274 -0.4688 0.0771 0.1621 80 TYR A N 604 C CA . TYR A 80 ? 0.8791 0.9949 1.0467 -0.4718 0.0509 0.1597 80 TYR A CA 605 C C . TYR A 80 ? 0.9356 1.1072 1.1519 -0.4881 0.0528 0.1759 80 TYR A C 606 O O . TYR A 80 ? 0.8896 1.0588 1.1281 -0.5043 0.0278 0.1811 80 TYR A O 607 C CB . TYR A 80 ? 0.8643 0.9700 1.0277 -0.4418 0.0483 0.1387 80 TYR A CB 608 C CG . TYR A 80 ? 0.9985 1.1073 1.1844 -0.4430 0.0228 0.1343 80 TYR A CG 609 C CD1 . TYR A 80 ? 0.8768 0.9406 1.0446 -0.4493 -0.0052 0.1248 80 TYR A CD1 610 C CD2 . TYR A 80 ? 1.1610 1.3198 1.3870 -0.4372 0.0266 0.1385 80 TYR A CD2 611 C CE1 . TYR A 80 ? 0.8652 0.9348 1.0494 -0.4512 -0.0285 0.1173 80 TYR A CE1 612 C CE2 . TYR A 80 ? 1.1361 1.3018 1.3797 -0.4399 0.0017 0.1351 80 TYR A CE2 613 C CZ . TYR A 80 ? 0.8990 1.0204 1.1190 -0.4475 -0.0255 0.1232 80 TYR A CZ 614 O OH . TYR A 80 ? 1.0358 1.1669 1.2693 -0.4511 -0.0502 0.1164 80 TYR A OH 615 N N . ALA A 81 ? 0.8856 1.1090 1.1199 -0.4839 0.0827 0.1824 81 ALA A N 616 C CA . ALA A 81 ? 0.8894 1.1748 1.1745 -0.4967 0.0895 0.1984 81 ALA A CA 617 C C . ALA A 81 ? 1.0870 1.4207 1.3772 -0.5000 0.1251 0.2077 81 ALA A C 618 O O . ALA A 81 ? 1.1541 1.4688 1.4042 -0.4995 0.1390 0.2046 81 ALA A O 619 C CB . ALA A 81 ? 0.8628 1.1754 1.1829 -0.4755 0.0867 0.1891 81 ALA A CB 620 N N . LYS A 82 ? 1.2604 1.6595 1.5998 -0.5042 0.1392 0.2188 82 LYS A N 621 C CA . LYS A 82 ? 1.3419 1.7977 1.6915 -0.5090 0.1747 0.2273 82 LYS A CA 622 C C . LYS A 82 ? 1.5136 1.9605 1.8280 -0.4828 0.2032 0.2045 82 LYS A C 623 O O . LYS A 82 ? 1.9244 2.3572 2.1962 -0.4934 0.2132 0.2066 82 LYS A O 624 C CB . LYS A 82 ? 1.2082 1.7369 1.6226 -0.5062 0.1876 0.2356 82 LYS A CB 625 C CG . LYS A 82 ? 1.1023 1.6984 1.5348 -0.5211 0.2199 0.2507 82 LYS A CG 626 C CD . LYS A 82 ? 1.1968 1.7832 1.6069 -0.5605 0.2087 0.2773 82 LYS A CD 627 C CE . LYS A 82 ? 1.2630 1.9107 1.6847 -0.5675 0.2387 0.2903 82 LYS A CE 628 N NZ . LYS A 82 ? 1.1353 1.8462 1.6235 -0.5683 0.2435 0.3013 82 LYS A NZ 629 N N . ASP A 83 ? 0.9778 1.4327 1.3108 -0.4500 0.2148 0.1837 83 ASP A N 630 C CA . ASP A 83 ? 0.9776 1.3970 1.2712 -0.4251 0.2280 0.1587 83 ASP A CA 631 C C . ASP A 83 ? 1.1700 1.5402 1.4591 -0.4052 0.2033 0.1466 83 ASP A C 632 O O . ASP A 83 ? 1.2657 1.6532 1.5914 -0.3824 0.2056 0.1391 83 ASP A O 633 C CB . ASP A 83 ? 1.2176 1.6849 1.5346 -0.4022 0.2660 0.1420 83 ASP A CB 634 C CG . ASP A 83 ? 1.5648 2.0978 1.8972 -0.4212 0.2928 0.1546 83 ASP A CG 635 O OD1 . ASP A 83 ? 1.8179 2.3499 2.1062 -0.4343 0.3074 0.1540 83 ASP A OD1 636 O OD2 . ASP A 83 ? 1.3061 1.8957 1.6951 -0.4236 0.2994 0.1664 83 ASP A OD2 637 N N . ASP A 84 ? 1.0952 1.4067 1.3407 -0.4140 0.1797 0.1463 84 ASP A N 638 C CA . ASP A 84 ? 0.9163 1.1799 1.1473 -0.3960 0.1584 0.1335 84 ASP A CA 639 C C . ASP A 84 ? 0.9496 1.1541 1.1245 -0.4009 0.1476 0.1275 84 ASP A C 640 O O . ASP A 84 ? 0.9953 1.1676 1.1565 -0.4174 0.1215 0.1353 84 ASP A O 641 C CB . ASP A 84 ? 0.9082 1.1736 1.1667 -0.4044 0.1289 0.1431 84 ASP A CB 642 C CG . ASP A 84 ? 1.2675 1.5088 1.5247 -0.3809 0.1142 0.1305 84 ASP A CG 643 O OD1 . ASP A 84 ? 1.2625 1.5387 1.5603 -0.3659 0.1171 0.1318 84 ASP A OD1 644 O OD2 . ASP A 84 ? 1.6952 1.8854 1.9127 -0.3775 0.0998 0.1210 84 ASP A OD2 645 N N . PRO A 85 ? 0.9938 1.1841 1.1385 -0.3872 0.1667 0.1132 85 PRO A N 646 C CA . PRO A 85 ? 0.9165 1.0560 1.0095 -0.3936 0.1571 0.1102 85 PRO A CA 647 C C . PRO A 85 ? 0.9992 1.0887 1.0788 -0.3904 0.1263 0.1073 85 PRO A C 648 O O . PRO A 85 ? 0.9247 1.0072 1.0166 -0.3702 0.1198 0.0967 85 PRO A O 649 C CB . PRO A 85 ? 0.9401 1.0748 1.0133 -0.3720 0.1799 0.0897 85 PRO A CB 650 C CG . PRO A 85 ? 1.0976 1.2890 1.2070 -0.3641 0.2081 0.0856 85 PRO A CG 651 C CD . PRO A 85 ? 1.1673 1.3879 1.3268 -0.3654 0.1971 0.0979 85 PRO A CD 652 N N . LEU A 86 ? 0.8942 0.9515 0.9505 -0.4104 0.1076 0.1175 86 LEU A N 653 C CA . LEU A 86 ? 0.8708 0.8813 0.9149 -0.4084 0.0791 0.1124 86 LEU A CA 654 C C . LEU A 86 ? 0.8752 0.8459 0.8831 -0.3908 0.0797 0.0979 86 LEU A C 655 O O . LEU A 86 ? 1.1022 1.0409 1.1015 -0.3804 0.0620 0.0883 86 LEU A O 656 C CB . LEU A 86 ? 1.1207 1.1107 1.1623 -0.4362 0.0580 0.1285 86 LEU A CB 657 C CG . LEU A 86 ? 0.8896 0.8246 0.9138 -0.4353 0.0303 0.1211 86 LEU A CG 658 C CD1 . LEU A 86 ? 0.8757 0.8096 0.9214 -0.4287 0.0113 0.1098 86 LEU A CD1 659 C CD2 . LEU A 86 ? 1.1531 1.0628 1.1709 -0.4613 0.0152 0.1389 86 LEU A CD2 660 N N . GLU A 87 ? 0.9529 0.9289 0.9393 -0.3883 0.1003 0.0955 87 GLU A N 661 C CA . GLU A 87 ? 0.8883 0.8294 0.8411 -0.3743 0.1010 0.0830 87 GLU A CA 662 C C . GLU A 87 ? 1.1430 1.1055 1.0865 -0.3643 0.1288 0.0726 87 GLU A C 663 O O . GLU A 87 ? 0.9237 0.9263 0.8789 -0.3726 0.1480 0.0770 87 GLU A O 664 C CB . GLU A 87 ? 0.9430 0.8477 0.8660 -0.3909 0.0847 0.0933 87 GLU A CB 665 C CG . GLU A 87 ? 1.2429 1.1681 1.1589 -0.4170 0.0917 0.1133 87 GLU A CG 666 C CD . GLU A 87 ? 1.1851 1.0730 1.0809 -0.4346 0.0702 0.1289 87 GLU A CD 667 O OE1 . GLU A 87 ? 1.1372 1.0397 1.0281 -0.4587 0.0717 0.1506 87 GLU A OE1 668 O OE2 . GLU A 87 ? 1.0508 0.8967 0.9381 -0.4242 0.0517 0.1207 87 GLU A OE2 669 N N . PHE A 88 ? 1.3333 1.2709 1.2580 -0.3466 0.1311 0.0573 88 PHE A N 670 C CA . PHE A 88 ? 0.9767 0.9280 0.8910 -0.3370 0.1554 0.0428 88 PHE A CA 671 C C . PHE A 88 ? 0.9523 0.8690 0.8237 -0.3387 0.1505 0.0374 88 PHE A C 672 O O . PHE A 88 ? 0.9748 0.8581 0.8387 -0.3262 0.1376 0.0309 88 PHE A O 673 C CB . PHE A 88 ? 0.9451 0.9057 0.8903 -0.3113 0.1649 0.0278 88 PHE A CB 674 C CG . PHE A 88 ? 0.9380 0.9286 0.9277 -0.3081 0.1626 0.0360 88 PHE A CG 675 C CD1 . PHE A 88 ? 0.9547 0.9919 0.9738 -0.3102 0.1824 0.0373 88 PHE A CD1 676 C CD2 . PHE A 88 ? 0.9154 0.8915 0.9177 -0.3034 0.1404 0.0419 88 PHE A CD2 677 C CE1 . PHE A 88 ? 0.9499 1.0174 1.0128 -0.3080 0.1785 0.0466 88 PHE A CE1 678 C CE2 . PHE A 88 ? 0.9095 0.9158 0.9508 -0.3022 0.1360 0.0499 88 PHE A CE2 679 C CZ . PHE A 88 ? 0.9281 0.9796 1.0012 -0.3047 0.1543 0.0534 88 PHE A CZ 680 N N . LYS A 89 ? 0.9641 0.8931 0.8078 -0.3554 0.1607 0.0416 89 LYS A N 681 C CA . LYS A 89 ? 0.9718 0.8726 0.7735 -0.3612 0.1537 0.0405 89 LYS A CA 682 C C . LYS A 89 ? 1.1373 1.0442 0.9220 -0.3500 0.1733 0.0170 89 LYS A C 683 O O . LYS A 89 ? 1.3582 1.2449 1.1082 -0.3542 0.1681 0.0133 89 LYS A O 684 C CB . LYS A 89 ? 1.0633 0.9725 0.8413 -0.3894 0.1481 0.0635 89 LYS A CB 685 C CG . LYS A 89 ? 1.1413 1.0367 0.9373 -0.4024 0.1254 0.0862 89 LYS A CG 686 C CD . LYS A 89 ? 1.2184 1.1260 0.9981 -0.4319 0.1209 0.1129 89 LYS A CD 687 C CE . LYS A 89 ? 1.0814 0.9716 0.8856 -0.4451 0.0970 0.1338 89 LYS A CE 688 N NZ . LYS A 89 ? 1.1123 1.0161 0.9079 -0.4758 0.0918 0.1644 89 LYS A NZ 689 N N . SER A 90 ? 1.3237 1.2585 1.1355 -0.3357 0.1948 0.0003 90 SER A N 690 C CA . SER A 90 ? 1.1481 1.0864 0.9507 -0.3230 0.2136 -0.0268 90 SER A CA 691 C C . SER A 90 ? 1.0720 0.9683 0.8760 -0.3052 0.2005 -0.0381 90 SER A C 692 O O . SER A 90 ? 1.0447 0.9286 0.8799 -0.2909 0.1903 -0.0340 90 SER A O 693 C CB . SER A 90 ? 1.1823 1.1599 1.0229 -0.3099 0.2393 -0.0420 90 SER A CB 694 O OG . SER A 90 ? 1.4455 1.4685 1.2824 -0.3272 0.2552 -0.0334 90 SER A OG 695 N N . HIS A 91 ? 1.1062 0.9844 0.8757 -0.3076 0.2003 -0.0508 91 HIS A N 696 C CA . HIS A 91 ? 1.1010 0.9412 0.8698 -0.2940 0.1877 -0.0602 91 HIS A CA 697 C C . HIS A 91 ? 1.0699 0.8822 0.8421 -0.2940 0.1617 -0.0393 91 HIS A C 698 O O . HIS A 91 ? 1.0122 0.8052 0.8053 -0.2781 0.1532 -0.0415 91 HIS A O 699 C CB . HIS A 91 ? 1.1153 0.9563 0.9244 -0.2703 0.1999 -0.0797 91 HIS A CB 700 C CG . HIS A 91 ? 1.1743 1.0446 0.9905 -0.2663 0.2271 -0.1040 91 HIS A CG 701 N ND1 . HIS A 91 ? 1.2396 1.1041 1.0307 -0.2671 0.2372 -0.1299 91 HIS A ND1 702 C CD2 . HIS A 91 ? 1.2453 1.1531 1.0925 -0.2610 0.2468 -0.1083 91 HIS A CD2 703 C CE1 . HIS A 91 ? 1.2842 1.1808 1.0894 -0.2614 0.2631 -0.1516 91 HIS A CE1 704 N NE2 . HIS A 91 ? 1.2705 1.1949 1.1115 -0.2571 0.2699 -0.1380 91 HIS A NE2 705 N N . GLN A 92 ? 1.2797 1.0913 1.0326 -0.3121 0.1494 -0.0190 92 GLN A N 706 C CA . GLN A 92 ? 1.2396 1.0263 0.9977 -0.3122 0.1257 -0.0023 92 GLN A CA 707 C C . GLN A 92 ? 0.9667 0.7210 0.7003 -0.3124 0.1096 -0.0015 92 GLN A C 708 O O . GLN A 92 ? 0.9824 0.7151 0.7214 -0.3092 0.0909 0.0083 92 GLN A O 709 C CB . GLN A 92 ? 0.9980 0.7943 0.7538 -0.3312 0.1176 0.0189 92 GLN A CB 710 C CG . GLN A 92 ? 0.9698 0.7664 0.6892 -0.3530 0.1140 0.0309 92 GLN A CG 711 C CD . GLN A 92 ? 1.0498 0.8559 0.7730 -0.3732 0.1054 0.0551 92 GLN A CD 712 O OE1 . GLN A 92 ? 1.2811 1.0878 1.0333 -0.3709 0.0988 0.0612 92 GLN A OE1 713 N NE2 . GLN A 92 ? 1.1810 0.9957 0.8754 -0.3947 0.1042 0.0703 92 GLN A NE2 714 N N . TRP A 93 ? 0.9842 0.7378 0.6924 -0.3161 0.1170 -0.0134 93 TRP A N 715 C CA . TRP A 93 ? 1.1514 0.8787 0.8371 -0.3177 0.1020 -0.0130 93 TRP A CA 716 C C . TRP A 93 ? 1.0637 0.7776 0.7327 -0.3324 0.0814 0.0101 93 TRP A C 717 O O . TRP A 93 ? 1.1755 0.8651 0.8496 -0.3261 0.0638 0.0165 93 TRP A O 718 C CB . TRP A 93 ? 1.1790 0.8855 0.8883 -0.2978 0.0948 -0.0200 93 TRP A CB 719 C CG . TRP A 93 ? 0.9778 0.6845 0.6956 -0.2864 0.1081 -0.0419 93 TRP A CG 720 C CD1 . TRP A 93 ? 1.1964 0.9215 0.9350 -0.2779 0.1278 -0.0568 93 TRP A CD1 721 C CD2 . TRP A 93 ? 0.9790 0.6654 0.6901 -0.2821 0.1014 -0.0514 93 TRP A CD2 722 N NE1 . TRP A 93 ? 1.1795 0.8935 0.9255 -0.2680 0.1335 -0.0763 93 TRP A NE1 723 C CE2 . TRP A 93 ? 1.0477 0.7379 0.7764 -0.2716 0.1171 -0.0730 93 TRP A CE2 724 C CE3 . TRP A 93 ? 0.9609 0.6268 0.6567 -0.2861 0.0831 -0.0434 93 TRP A CE3 725 C CZ2 . TRP A 93 ? 1.1371 0.8088 0.8677 -0.2667 0.1140 -0.0869 93 TRP A CZ2 726 C CZ3 . TRP A 93 ? 0.9608 0.6126 0.6575 -0.2817 0.0806 -0.0560 93 TRP A CZ3 727 C CH2 . TRP A 93 ? 1.0545 0.7079 0.7679 -0.2728 0.0954 -0.0776 93 TRP A CH2 728 N N . PHE A 94 ? 0.9849 0.7163 0.6372 -0.3519 0.0837 0.0238 94 PHE A N 729 C CA . PHE A 94 ? 1.1776 0.8952 0.8180 -0.3672 0.0628 0.0489 94 PHE A CA 730 C C . PHE A 94 ? 1.1994 0.9064 0.8079 -0.3756 0.0522 0.0521 94 PHE A C 731 O O . PHE A 94 ? 1.2253 0.9512 0.8049 -0.3854 0.0638 0.0436 94 PHE A O 732 C CB . PHE A 94 ? 1.2947 1.0360 0.9308 -0.3878 0.0671 0.0674 94 PHE A CB 733 C CG . PHE A 94 ? 1.2669 0.9939 0.8929 -0.4060 0.0447 0.0964 94 PHE A CG 734 C CD1 . PHE A 94 ? 1.2450 0.9439 0.8971 -0.4016 0.0241 0.1084 94 PHE A CD1 735 C CD2 . PHE A 94 ? 1.2609 1.0035 0.8524 -0.4276 0.0436 0.1117 94 PHE A CD2 736 C CE1 . PHE A 94 ? 1.1460 0.8283 0.7958 -0.4170 0.0023 0.1353 94 PHE A CE1 737 C CE2 . PHE A 94 ? 1.1694 0.8988 0.7562 -0.4447 0.0209 0.1427 94 PHE A CE2 738 C CZ . PHE A 94 ? 1.0535 0.7505 0.6724 -0.4388 0.0000 0.1547 94 PHE A CZ 739 N N . GLY A 95 ? 1.2045 0.8834 0.8192 -0.3717 0.0299 0.0634 95 GLY A N 740 C CA . GLY A 95 ? 1.2428 0.9114 0.8334 -0.3784 0.0165 0.0687 95 GLY A CA 741 C C . GLY A 95 ? 1.2724 0.9252 0.8724 -0.3600 0.0146 0.0505 95 GLY A C 742 O O . GLY A 95 ? 1.2222 0.8687 0.8045 -0.3644 0.0048 0.0509 95 GLY A O 743 N N . ALA A 96 ? 1.2311 0.8798 0.8601 -0.3409 0.0229 0.0369 96 ALA A N 744 C CA . ALA A 96 ? 1.0237 0.6596 0.6668 -0.3240 0.0212 0.0236 96 ALA A CA 745 C C . ALA A 96 ? 0.9888 0.6050 0.6413 -0.3194 -0.0007 0.0370 96 ALA A C 746 O O . ALA A 96 ? 1.3103 0.9183 0.9676 -0.3113 -0.0063 0.0316 96 ALA A O 747 C CB . ALA A 96 ? 1.0135 0.6542 0.6866 -0.3063 0.0338 0.0114 96 ALA A CB 748 N N . SER A 97 ? 1.1262 0.7351 0.7852 -0.3243 -0.0131 0.0542 97 SER A N 749 C CA . SER A 97 ? 0.9986 0.5892 0.6697 -0.3199 -0.0342 0.0669 97 SER A CA 750 C C . SER A 97 ? 0.9525 0.5369 0.6150 -0.3372 -0.0493 0.0902 97 SER A C 751 O O . SER A 97 ? 0.9591 0.5470 0.6249 -0.3454 -0.0465 0.0974 97 SER A O 752 C CB . SER A 97 ? 1.0146 0.5974 0.7176 -0.3005 -0.0361 0.0604 97 SER A CB 753 O OG . SER A 97 ? 1.2355 0.8225 0.9481 -0.3023 -0.0306 0.0602 97 SER A OG 754 N N . VAL A 98 ? 0.9705 0.5472 0.6248 -0.3437 -0.0664 0.1043 98 VAL A N 755 C CA . VAL A 98 ? 1.0009 0.5716 0.6499 -0.3609 -0.0840 0.1316 98 VAL A CA 756 C C . VAL A 98 ? 1.2953 0.8460 0.9673 -0.3531 -0.1077 0.1453 98 VAL A C 757 O O . VAL A 98 ? 1.4622 1.0140 1.1313 -0.3482 -0.1138 0.1429 98 VAL A O 758 C CB . VAL A 98 ? 1.2842 0.8747 0.8923 -0.3845 -0.0821 0.1420 98 VAL A CB 759 C CG1 . VAL A 98 ? 1.3971 0.9829 1.0017 -0.4030 -0.1042 0.1764 98 VAL A CG1 760 C CG2 . VAL A 98 ? 1.6939 1.3075 1.2827 -0.3928 -0.0580 0.1298 98 VAL A CG2 761 N N . ARG A 99 ? 1.0197 0.5525 0.7182 -0.3518 -0.1215 0.1589 99 ARG A N 762 C CA . ARG A 99 ? 1.0189 0.5317 0.7460 -0.3432 -0.1446 0.1722 99 ARG A CA 763 C C . ARG A 99 ? 1.2686 0.7684 1.0041 -0.3604 -0.1648 0.2038 99 ARG A C 764 O O . ARG A 99 ? 1.7003 1.2036 1.4391 -0.3673 -0.1603 0.2077 99 ARG A O 765 C CB . ARG A 99 ? 1.0947 0.5938 0.8586 -0.3175 -0.1431 0.1519 99 ARG A CB 766 C CG . ARG A 99 ? 1.2135 0.7238 0.9795 -0.2991 -0.1327 0.1311 99 ARG A CG 767 C CD . ARG A 99 ? 1.2971 0.8076 1.0678 -0.2979 -0.1481 0.1436 99 ARG A CD 768 N NE . ARG A 99 ? 1.5918 1.1204 1.3329 -0.3057 -0.1395 0.1390 99 ARG A NE 769 C CZ . ARG A 99 ? 1.7934 1.3321 1.5393 -0.2925 -0.1292 0.1216 99 ARG A CZ 770 N NH1 . ARG A 99 ? 1.7528 1.2904 1.5284 -0.2710 -0.1248 0.1086 99 ARG A NH1 771 N NH2 . ARG A 99 ? 1.7867 1.3377 1.5080 -0.3018 -0.1237 0.1170 99 ARG A NH2 772 N N . SER A 100 ? 1.1494 0.6447 0.8950 -0.3616 -0.1862 0.2249 100 SER A N 773 C CA . SER A 100 ? 1.2189 0.7144 0.9799 -0.3706 -0.2057 0.2546 100 SER A CA 774 C C . SER A 100 ? 1.2612 0.7369 1.0688 -0.3537 -0.2291 0.2647 100 SER A C 775 O O . SER A 100 ? 1.6795 1.1556 1.4888 -0.3498 -0.2393 0.2700 100 SER A O 776 C CB . SER A 100 ? 1.4169 0.9372 1.1355 -0.3975 -0.2102 0.2791 100 SER A CB 777 O OG . SER A 100 ? 1.5807 1.1041 1.3169 -0.4062 -0.2319 0.3115 100 SER A OG 778 N N . LYS A 101 ? 1.1231 0.5814 0.9709 -0.3439 -0.2378 0.2667 101 LYS A N 779 C CA . LYS A 101 ? 1.3004 0.7392 1.1970 -0.3290 -0.2608 0.2779 101 LYS A CA 780 C C . LYS A 101 ? 1.3235 0.7640 1.2352 -0.3424 -0.2795 0.3105 101 LYS A C 781 O O . LYS A 101 ? 1.1921 0.6285 1.1116 -0.3478 -0.2759 0.3107 101 LYS A O 782 C CB . LYS A 101 ? 1.5010 0.9137 1.4387 -0.3039 -0.2574 0.2489 101 LYS A CB 783 C CG . LYS A 101 ? 1.6173 1.0077 1.6110 -0.2875 -0.2804 0.2576 101 LYS A CG 784 C CD . LYS A 101 ? 1.4263 0.7924 1.4572 -0.2623 -0.2759 0.2234 101 LYS A CD 785 C CE . LYS A 101 ? 1.5732 0.9166 1.6635 -0.2448 -0.2981 0.2294 101 LYS A CE 786 N NZ . LYS A 101 ? 1.7125 1.0639 1.8146 -0.2412 -0.3130 0.2508 101 LYS A NZ 787 N N . GLN A 102 ? 1.3347 0.7830 1.2519 -0.3489 -0.3005 0.3395 102 GLN A N 788 C CA . GLN A 102 ? 1.2725 0.7273 1.2034 -0.3639 -0.3210 0.3755 102 GLN A CA 789 C C . GLN A 102 ? 1.2568 0.7361 1.1452 -0.3902 -0.3094 0.3872 102 GLN A C 790 O O . GLN A 102 ? 1.9042 1.4099 1.7407 -0.4074 -0.2982 0.3889 102 GLN A O 791 C CB . GLN A 102 ? 1.2609 0.6856 1.2542 -0.3469 -0.3350 0.3749 102 GLN A CB 792 C CG . GLN A 102 ? 1.4308 0.8346 1.4726 -0.3218 -0.3497 0.3684 102 GLN A CG 793 C CD . GLN A 102 ? 1.9132 1.2857 2.0172 -0.3044 -0.3623 0.3626 102 GLN A CD 794 O OE1 . GLN A 102 ? 2.0218 1.3803 2.1319 -0.3024 -0.3520 0.3441 102 GLN A OE1 795 N NE2 . GLN A 102 ? 1.9926 1.3546 2.1451 -0.2920 -0.3855 0.3779 102 GLN A NE2 796 N N . ASP A 103 ? 1.3552 0.8263 1.2669 -0.3938 -0.3120 0.3943 103 ASP A N 797 C CA . ASP A 103 ? 1.4459 0.9425 1.3250 -0.4187 -0.3020 0.4083 103 ASP A CA 798 C C . ASP A 103 ? 1.4425 0.9387 1.3042 -0.4160 -0.2743 0.3768 103 ASP A C 799 O O . ASP A 103 ? 1.2654 0.7834 1.1040 -0.4345 -0.2627 0.3841 103 ASP A O 800 C CB . ASP A 103 ? 1.3369 0.8289 1.2528 -0.4275 -0.3221 0.4384 103 ASP A CB 801 C CG . ASP A 103 ? 1.6594 1.1902 1.5407 -0.4585 -0.3251 0.4729 103 ASP A CG 802 O OD1 . ASP A 103 ? 1.8456 1.4034 1.6795 -0.4734 -0.3028 0.4648 103 ASP A OD1 803 O OD2 . ASP A 103 ? 1.6142 1.1505 1.5171 -0.4683 -0.3497 0.5081 103 ASP A OD2 804 N N . LYS A 104 ? 1.3969 0.8716 1.2715 -0.3933 -0.2641 0.3428 104 LYS A N 805 C CA . LYS A 104 ? 1.1914 0.6660 1.0542 -0.3891 -0.2399 0.3124 104 LYS A CA 806 C C . LYS A 104 ? 1.6391 1.1344 1.4526 -0.3944 -0.2186 0.2965 104 LYS A C 807 O O . LYS A 104 ? 1.7876 1.2828 1.5888 -0.3889 -0.2215 0.2935 104 LYS A O 808 C CB . LYS A 104 ? 1.2371 0.6799 1.1409 -0.3630 -0.2406 0.2829 104 LYS A CB 809 C CG . LYS A 104 ? 1.2338 0.6513 1.1894 -0.3562 -0.2603 0.2914 104 LYS A CG 810 C CD . LYS A 104 ? 1.4670 0.8890 1.4271 -0.3702 -0.2558 0.2960 104 LYS A CD 811 C CE . LYS A 104 ? 1.6514 1.0438 1.6653 -0.3626 -0.2752 0.2992 104 LYS A CE 812 N NZ . LYS A 104 ? 1.8903 1.2772 1.9278 -0.3661 -0.3003 0.3328 104 LYS A NZ 813 N N . ILE A 105 ? 1.4483 0.9615 1.2363 -0.4054 -0.1975 0.2865 105 ILE A N 814 C CA . ILE A 105 ? 1.1326 0.6632 0.8776 -0.4099 -0.1751 0.2679 105 ILE A CA 815 C C . ILE A 105 ? 1.2510 0.7786 1.0013 -0.4003 -0.1547 0.2384 105 ILE A C 816 O O . ILE A 105 ? 1.5011 1.0346 1.2626 -0.4068 -0.1499 0.2406 105 ILE A O 817 C CB . ILE A 105 ? 1.1572 0.7226 0.8563 -0.4375 -0.1665 0.2862 105 ILE A CB 818 C CG1 . ILE A 105 ? 1.1900 0.7636 0.8777 -0.4489 -0.1874 0.3152 105 ILE A CG1 819 C CG2 . ILE A 105 ? 1.1381 0.7183 0.7961 -0.4417 -0.1409 0.2622 105 ILE A CG2 820 C CD1 . ILE A 105 ? 1.2194 0.8317 0.8568 -0.4771 -0.1793 0.3313 105 ILE A CD1 821 N N . LEU A 106 ? 1.0770 0.5972 0.8207 -0.3857 -0.1440 0.2124 106 LEU A N 822 C CA . LEU A 106 ? 1.2390 0.7585 0.9879 -0.3759 -0.1262 0.1850 106 LEU A CA 823 C C . LEU A 106 ? 1.1884 0.7277 0.9017 -0.3792 -0.1032 0.1687 106 LEU A C 824 O O . LEU A 106 ? 1.2793 0.8211 0.9820 -0.3690 -0.1016 0.1591 106 LEU A O 825 C CB . LEU A 106 ? 1.1439 0.6385 0.9255 -0.3512 -0.1337 0.1652 106 LEU A CB 826 C CG . LEU A 106 ? 1.1534 0.6476 0.9425 -0.3410 -0.1195 0.1383 106 LEU A CG 827 C CD1 . LEU A 106 ? 1.2461 0.7447 1.0498 -0.3502 -0.1190 0.1421 106 LEU A CD1 828 C CD2 . LEU A 106 ? 1.0625 0.5399 0.8782 -0.3161 -0.1263 0.1180 106 LEU A CD2 829 N N . ALA A 107 ? 1.0883 0.6495 0.7907 -0.3877 -0.0846 0.1628 107 ALA A N 830 C CA . ALA A 107 ? 1.1974 0.7850 0.8758 -0.3836 -0.0604 0.1427 107 ALA A CA 831 C C . ALA A 107 ? 0.9786 0.5759 0.6738 -0.3728 -0.0441 0.1230 107 ALA A C 832 O O . ALA A 107 ? 1.0053 0.6037 0.7163 -0.3810 -0.0459 0.1307 107 ALA A O 833 C CB . ALA A 107 ? 1.4205 1.0351 1.0640 -0.4067 -0.0513 0.1558 107 ALA A CB 834 N N . CYS A 108 ? 1.1370 0.7426 0.8310 -0.3556 -0.0296 0.0996 108 CYS A N 835 C CA . CYS A 108 ? 0.9698 0.5849 0.6836 -0.3428 -0.0172 0.0828 108 CYS A CA 836 C C . CYS A 108 ? 1.2005 0.8423 0.9039 -0.3405 0.0068 0.0684 108 CYS A C 837 O O . CYS A 108 ? 1.2099 0.8587 0.8911 -0.3431 0.0145 0.0634 108 CYS A O 838 C CB . CYS A 108 ? 0.9021 0.5019 0.6355 -0.3206 -0.0243 0.0693 108 CYS A CB 839 S SG . CYS A 108 ? 1.3791 0.9476 1.1323 -0.3178 -0.0505 0.0789 108 CYS A SG 840 N N . ALA A 109 ? 1.2623 0.9189 0.9846 -0.3352 0.0174 0.0608 109 ALA A N 841 C CA . ALA A 109 ? 1.0371 0.7187 0.7606 -0.3292 0.0397 0.0464 109 ALA A CA 842 C C . ALA A 109 ? 0.9416 0.6251 0.6920 -0.3093 0.0424 0.0340 109 ALA A C 843 O O . ALA A 109 ? 1.0251 0.7214 0.7952 -0.3090 0.0443 0.0350 109 ALA A O 844 C CB . ALA A 109 ? 0.9069 0.6155 0.6295 -0.3449 0.0522 0.0534 109 ALA A CB 845 N N . PRO A 110 ? 0.9492 0.6226 0.7009 -0.2941 0.0415 0.0244 110 PRO A N 846 C CA . PRO A 110 ? 0.8218 0.4981 0.5968 -0.2761 0.0412 0.0170 110 PRO A CA 847 C C . PRO A 110 ? 0.8512 0.5522 0.6458 -0.2695 0.0571 0.0107 110 PRO A C 848 O O . PRO A 110 ? 1.1429 0.8523 0.9582 -0.2588 0.0547 0.0098 110 PRO A O 849 C CB . PRO A 110 ? 0.8160 0.4796 0.5855 -0.2659 0.0389 0.0117 110 PRO A CB 850 C CG . PRO A 110 ? 0.9154 0.5637 0.6602 -0.2784 0.0305 0.0180 110 PRO A CG 851 C CD . PRO A 110 ? 0.8902 0.5506 0.6210 -0.2953 0.0386 0.0225 110 PRO A CD 852 N N . LEU A 111 ? 0.8961 0.6111 0.6855 -0.2755 0.0731 0.0062 111 LEU A N 853 C CA . LEU A 111 ? 0.9783 0.7176 0.7922 -0.2672 0.0891 -0.0004 111 LEU A CA 854 C C . LEU A 111 ? 0.8745 0.6375 0.6996 -0.2777 0.0941 0.0065 111 LEU A C 855 O O . LEU A 111 ? 0.9068 0.6946 0.7549 -0.2722 0.1081 0.0024 111 LEU A O 856 C CB . LEU A 111 ? 1.1778 0.9210 0.9868 -0.2639 0.1058 -0.0145 111 LEU A CB 857 C CG . LEU A 111 ? 1.0477 0.7829 0.8775 -0.2457 0.1074 -0.0225 111 LEU A CG 858 C CD1 . LEU A 111 ? 0.8483 0.5605 0.6692 -0.2421 0.0900 -0.0165 111 LEU A CD1 859 C CD2 . LEU A 111 ? 1.3076 1.0421 1.1355 -0.2428 0.1226 -0.0403 111 LEU A CD2 860 N N . TYR A 112 ? 0.8632 0.6187 0.6759 -0.2929 0.0819 0.0181 112 TYR A N 861 C CA . TYR A 112 ? 0.8963 0.6722 0.7218 -0.3059 0.0827 0.0279 112 TYR A CA 862 C C . TYR A 112 ? 0.9703 0.7622 0.8282 -0.2960 0.0801 0.0270 112 TYR A C 863 O O . TYR A 112 ? 0.8444 0.6235 0.7079 -0.2853 0.0675 0.0244 112 TYR A O 864 C CB . TYR A 112 ? 0.8894 0.6457 0.7008 -0.3230 0.0647 0.0417 112 TYR A CB 865 C CG . TYR A 112 ? 0.8955 0.6650 0.7247 -0.3376 0.0587 0.0535 112 TYR A CG 866 C CD1 . TYR A 112 ? 0.8769 0.6713 0.7048 -0.3556 0.0697 0.0646 112 TYR A CD1 867 C CD2 . TYR A 112 ? 0.9013 0.6601 0.7483 -0.3347 0.0415 0.0531 112 TYR A CD2 868 C CE1 . TYR A 112 ? 0.9712 0.7784 0.8189 -0.3711 0.0630 0.0776 112 TYR A CE1 869 C CE2 . TYR A 112 ? 0.9828 0.7516 0.8480 -0.3498 0.0337 0.0628 112 TYR A CE2 870 C CZ . TYR A 112 ? 0.8736 0.6658 0.7408 -0.3684 0.0440 0.0764 112 TYR A CZ 871 O OH . TYR A 112 ? 0.8838 0.6869 0.7727 -0.3854 0.0351 0.0881 112 TYR A OH 872 N N . HIS A 113 ? 1.0566 0.8805 0.9358 -0.3005 0.0918 0.0299 113 HIS A N 873 C CA . HIS A 113 ? 1.2835 1.1294 1.1962 -0.2915 0.0901 0.0305 113 HIS A CA 874 C C . HIS A 113 ? 1.2633 1.1251 1.1906 -0.3080 0.0813 0.0416 113 HIS A C 875 O O . HIS A 113 ? 1.1516 1.0145 1.0688 -0.3267 0.0821 0.0503 113 HIS A O 876 C CB . HIS A 113 ? 1.3275 1.2011 1.2643 -0.2784 0.1110 0.0239 113 HIS A CB 877 C CG . HIS A 113 ? 1.2444 1.1022 1.1792 -0.2600 0.1156 0.0134 113 HIS A CG 878 N ND1 . HIS A 113 ? 1.0431 0.8932 0.9893 -0.2462 0.1042 0.0148 113 HIS A ND1 879 C CD2 . HIS A 113 ? 1.3177 1.1673 1.2414 -0.2546 0.1296 0.0017 113 HIS A CD2 880 C CE1 . HIS A 113 ? 0.9557 0.7923 0.9009 -0.2336 0.1106 0.0070 113 HIS A CE1 881 N NE2 . HIS A 113 ? 1.2130 1.0470 1.1450 -0.2382 0.1254 -0.0026 113 HIS A NE2 882 N N . TRP A 114 ? 1.0447 0.9207 0.9966 -0.3028 0.0717 0.0426 114 TRP A N 883 C CA . TRP A 114 ? 1.0277 0.9128 0.9931 -0.3194 0.0576 0.0509 114 TRP A CA 884 C C . TRP A 114 ? 1.0989 1.0278 1.1016 -0.3215 0.0633 0.0572 114 TRP A C 885 O O . TRP A 114 ? 1.3331 1.2849 1.3471 -0.3352 0.0740 0.0659 114 TRP A O 886 C CB . TRP A 114 ? 0.8619 0.7227 0.8197 -0.3166 0.0342 0.0448 114 TRP A CB 887 C CG . TRP A 114 ? 0.9270 0.7790 0.8899 -0.3363 0.0161 0.0493 114 TRP A CG 888 C CD1 . TRP A 114 ? 1.3270 1.1886 1.2995 -0.3576 0.0176 0.0623 114 TRP A CD1 889 C CD2 . TRP A 114 ? 1.0151 0.8469 0.9757 -0.3374 -0.0067 0.0402 114 TRP A CD2 890 N NE1 . TRP A 114 ? 1.2838 1.1288 1.2632 -0.3725 -0.0046 0.0633 114 TRP A NE1 891 C CE2 . TRP A 114 ? 1.2696 1.0951 1.2416 -0.3597 -0.0196 0.0474 114 TRP A CE2 892 C CE3 . TRP A 114 ? 1.1658 0.9868 1.1168 -0.3220 -0.0169 0.0260 114 TRP A CE3 893 C CZ2 . TRP A 114 ? 1.5074 1.3114 1.4828 -0.3661 -0.0433 0.0374 114 TRP A CZ2 894 C CZ3 . TRP A 114 ? 1.6375 1.4420 1.5885 -0.3277 -0.0382 0.0151 114 TRP A CZ3 895 C CH2 . TRP A 114 ? 1.6188 1.4126 1.5826 -0.3491 -0.0517 0.0191 114 TRP A CH2 896 N N . ARG A 115 ? 0.9916 0.9357 1.0137 -0.3076 0.0573 0.0545 115 ARG A N 897 C CA . ARG A 115 ? 1.1305 1.1139 1.1891 -0.3101 0.0524 0.0618 115 ARG A CA 898 C C . ARG A 115 ? 0.9846 0.9611 1.0417 -0.3232 0.0264 0.0612 115 ARG A C 899 O O . ARG A 115 ? 1.0849 1.0916 1.1677 -0.3258 0.0170 0.0655 115 ARG A O 900 C CB . ARG A 115 ? 1.0031 1.0232 1.0892 -0.3207 0.0689 0.0716 115 ARG A CB 901 C CG . ARG A 115 ? 0.8818 0.9053 0.9701 -0.3479 0.0598 0.0814 115 ARG A CG 902 C CD . ARG A 115 ? 1.0399 1.0937 1.1619 -0.3585 0.0441 0.0892 115 ARG A CD 903 N NE . ARG A 115 ? 1.0249 1.1309 1.1888 -0.3550 0.0594 0.0983 115 ARG A NE 904 C CZ . ARG A 115 ? 0.8966 1.0376 1.0958 -0.3631 0.0474 0.1071 115 ARG A CZ 905 N NH1 . ARG A 115 ? 0.8687 0.9961 1.0625 -0.3758 0.0200 0.1054 115 ARG A NH1 906 N NH2 . ARG A 115 ? 0.9357 1.1262 1.1773 -0.3582 0.0625 0.1163 115 ARG A NH2 907 N N . THR A 116 ? 0.8723 0.8091 0.9007 -0.3306 0.0142 0.0545 116 THR A N 908 C CA . THR A 116 ? 1.3324 1.2537 1.3580 -0.3436 -0.0105 0.0489 116 THR A CA 909 C C . THR A 116 ? 1.3396 1.2830 1.3926 -0.3663 -0.0181 0.0593 116 THR A C 910 O O . THR A 116 ? 1.6032 1.5626 1.6683 -0.3771 -0.0040 0.0726 116 THR A O 911 C CB . THR A 116 ? 1.2346 1.1641 1.2584 -0.3306 -0.0242 0.0378 116 THR A CB 912 O OG1 . THR A 116 ? 0.9829 0.9581 1.0370 -0.3303 -0.0242 0.0462 116 THR A OG1 913 C CG2 . THR A 116 ? 1.0934 1.0109 1.0972 -0.3085 -0.0148 0.0322 116 THR A CG2 914 N N . GLU A 117 ? 0.8950 0.8408 0.9571 -0.3748 -0.0405 0.0525 117 GLU A N 915 C CA . GLU A 117 ? 0.9412 0.9114 1.0339 -0.3971 -0.0506 0.0623 117 GLU A CA 916 C C . GLU A 117 ? 1.2189 1.2376 1.3398 -0.3942 -0.0552 0.0655 117 GLU A C 917 O O . GLU A 117 ? 1.2739 1.3196 1.4246 -0.4127 -0.0630 0.0753 117 GLU A O 918 C CB . GLU A 117 ? 1.1542 1.0883 1.2419 -0.4152 -0.0764 0.0528 117 GLU A CB 919 C CG . GLU A 117 ? 1.0181 0.9402 1.1182 -0.4401 -0.0771 0.0695 117 GLU A CG 920 C CD . GLU A 117 ? 1.2838 1.1504 1.3614 -0.4438 -0.0863 0.0645 117 GLU A CD 921 O OE1 . GLU A 117 ? 1.3761 1.2143 1.4293 -0.4259 -0.0911 0.0457 117 GLU A OE1 922 O OE2 . GLU A 117 ? 1.3702 1.2240 1.4569 -0.4650 -0.0890 0.0813 117 GLU A OE2 923 N N . MET A 118 ? 1.3446 1.3765 1.4585 -0.3724 -0.0516 0.0599 118 MET A N 924 C CA . MET A 118 ? 1.1247 1.1986 1.2602 -0.3704 -0.0636 0.0623 118 MET A CA 925 C C . MET A 118 ? 1.1266 1.2448 1.2936 -0.3568 -0.0451 0.0791 118 MET A C 926 O O . MET A 118 ? 1.1498 1.3058 1.3540 -0.3670 -0.0430 0.0927 118 MET A O 927 C CB . MET A 118 ? 0.9248 0.9875 1.0321 -0.3581 -0.0781 0.0457 118 MET A CB 928 C CG . MET A 118 ? 0.9251 0.9392 1.0016 -0.3652 -0.0923 0.0247 118 MET A CG 929 S SD . MET A 118 ? 1.7734 1.7798 1.8152 -0.3490 -0.1050 0.0022 118 MET A SD 930 C CE . MET A 118 ? 0.9343 0.8785 0.9515 -0.3556 -0.1149 -0.0206 118 MET A CE 931 N N . LYS A 119 ? 0.9382 1.0519 1.0941 -0.3337 -0.0322 0.0784 119 LYS A N 932 C CA . LYS A 119 ? 0.9173 1.0653 1.1063 -0.3180 -0.0139 0.0924 119 LYS A CA 933 C C . LYS A 119 ? 1.0417 1.1752 1.2302 -0.3147 0.0125 0.0928 119 LYS A C 934 O O . LYS A 119 ? 1.3672 1.4669 1.5282 -0.3257 0.0144 0.0856 119 LYS A O 935 C CB . LYS A 119 ? 0.9486 1.0994 1.1309 -0.2960 -0.0150 0.0934 119 LYS A CB 936 C CG . LYS A 119 ? 1.1442 1.3101 1.3159 -0.2995 -0.0407 0.0912 119 LYS A CG 937 C CD . LYS A 119 ? 1.4562 1.6212 1.6137 -0.2797 -0.0405 0.0936 119 LYS A CD 938 C CE . LYS A 119 ? 1.3244 1.4405 1.4435 -0.2718 -0.0306 0.0796 119 LYS A CE 939 N NZ . LYS A 119 ? 0.9988 1.1164 1.1067 -0.2542 -0.0303 0.0842 119 LYS A NZ 940 N N . GLN A 120 ? 0.9138 1.0740 1.1337 -0.2996 0.0322 0.1006 120 GLN A N 941 C CA . GLN A 120 ? 0.9218 1.0694 1.1368 -0.2935 0.0586 0.0960 120 GLN A CA 942 C C . GLN A 120 ? 1.1496 1.2685 1.3450 -0.2720 0.0661 0.0876 120 GLN A C 943 O O . GLN A 120 ? 1.3179 1.4533 1.5392 -0.2538 0.0686 0.0931 120 GLN A O 944 C CB . GLN A 120 ? 0.9306 1.1242 1.1939 -0.2897 0.0784 0.1047 120 GLN A CB 945 C CG . GLN A 120 ? 1.1194 1.3052 1.3762 -0.2824 0.1075 0.0957 120 GLN A CG 946 C CD . GLN A 120 ? 1.4581 1.6935 1.7615 -0.2814 0.1289 0.1014 120 GLN A CD 947 O OE1 . GLN A 120 ? 1.3799 1.6526 1.7140 -0.2949 0.1217 0.1144 120 GLN A OE1 948 N NE2 . GLN A 120 ? 1.4846 1.7225 1.7953 -0.2654 0.1554 0.0902 120 GLN A NE2 949 N N . GLU A 121 ? 1.0714 1.1476 1.2241 -0.2751 0.0682 0.0766 121 GLU A N 950 C CA . GLU A 121 ? 1.0799 1.1262 1.2112 -0.2581 0.0720 0.0688 121 GLU A CA 951 C C . GLU A 121 ? 1.1099 1.1284 1.2152 -0.2588 0.0894 0.0585 121 GLU A C 952 O O . GLU A 121 ? 1.3934 1.4188 1.4961 -0.2724 0.0996 0.0586 121 GLU A O 953 C CB . GLU A 121 ? 1.1142 1.1363 1.2148 -0.2596 0.0501 0.0650 121 GLU A CB 954 C CG . GLU A 121 ? 1.3226 1.3735 1.4401 -0.2601 0.0310 0.0726 121 GLU A CG 955 C CD . GLU A 121 ? 1.6658 1.7318 1.7996 -0.2407 0.0306 0.0811 121 GLU A CD 956 O OE1 . GLU A 121 ? 1.6802 1.7213 1.7986 -0.2284 0.0379 0.0771 121 GLU A OE1 957 O OE2 . GLU A 121 ? 1.6701 1.7741 1.8340 -0.2389 0.0217 0.0938 121 GLU A OE2 958 N N . ARG A 122 ? 0.9109 0.9019 0.9982 -0.2452 0.0927 0.0511 122 ARG A N 959 C CA . ARG A 122 ? 0.9013 0.8580 0.9513 -0.2497 0.0995 0.0411 122 ARG A CA 960 C C . ARG A 122 ? 0.9825 0.9072 1.0061 -0.2432 0.0851 0.0377 122 ARG A C 961 O O . ARG A 122 ? 1.4173 1.3393 1.4501 -0.2272 0.0864 0.0376 122 ARG A O 962 C CB . ARG A 122 ? 0.9169 0.8761 0.9749 -0.2396 0.1232 0.0320 122 ARG A CB 963 C CG . ARG A 122 ? 0.9353 0.9309 1.0190 -0.2450 0.1414 0.0326 122 ARG A CG 964 C CD . ARG A 122 ? 0.9702 0.9697 1.0644 -0.2316 0.1656 0.0181 122 ARG A CD 965 N NE . ARG A 122 ? 1.2019 1.1731 1.2521 -0.2386 0.1721 0.0059 122 ARG A NE 966 C CZ . ARG A 122 ? 1.1103 1.0950 1.1457 -0.2489 0.1900 -0.0017 122 ARG A CZ 967 N NH1 . ARG A 122 ? 1.0048 1.0318 1.0680 -0.2527 0.2051 0.0009 122 ARG A NH1 968 N NH2 . ARG A 122 ? 1.1273 1.0874 1.1203 -0.2561 0.1928 -0.0111 122 ARG A NH2 969 N N . GLU A 123 ? 0.9248 0.8266 0.9193 -0.2555 0.0712 0.0359 123 GLU A N 970 C CA . GLU A 123 ? 1.0891 0.9649 1.0608 -0.2492 0.0579 0.0315 123 GLU A CA 971 C C . GLU A 123 ? 1.0920 0.9324 1.0308 -0.2550 0.0578 0.0257 123 GLU A C 972 O O . GLU A 123 ? 1.0802 0.9090 1.0061 -0.2704 0.0520 0.0270 123 GLU A O 973 C CB . GLU A 123 ? 1.1207 1.0028 1.0924 -0.2547 0.0380 0.0320 123 GLU A CB 974 C CG . GLU A 123 ? 1.1317 1.0513 1.1330 -0.2484 0.0347 0.0396 123 GLU A CG 975 C CD . GLU A 123 ? 1.2060 1.1335 1.2011 -0.2520 0.0143 0.0365 123 GLU A CD 976 O OE1 . GLU A 123 ? 0.9082 0.8693 0.9240 -0.2484 0.0086 0.0440 123 GLU A OE1 977 O OE2 . GLU A 123 ? 1.4918 1.3934 1.4626 -0.2582 0.0034 0.0260 123 GLU A OE2 978 N N . PRO A 124 ? 0.9215 0.7454 0.8497 -0.2435 0.0627 0.0213 124 PRO A N 979 C CA . PRO A 124 ? 0.9948 0.7877 0.8935 -0.2480 0.0612 0.0170 124 PRO A CA 980 C C . PRO A 124 ? 1.0708 0.8430 0.9533 -0.2513 0.0427 0.0159 124 PRO A C 981 O O . PRO A 124 ? 0.8652 0.6256 0.7400 -0.2411 0.0373 0.0127 124 PRO A O 982 C CB . PRO A 124 ? 1.0271 0.8130 0.9271 -0.2337 0.0690 0.0131 124 PRO A CB 983 C CG . PRO A 124 ? 1.0404 0.8473 0.9667 -0.2209 0.0669 0.0180 124 PRO A CG 984 C CD . PRO A 124 ? 0.9786 0.8133 0.9258 -0.2265 0.0681 0.0227 124 PRO A CD 985 N N . VAL A 125 ? 0.8698 0.6389 0.7509 -0.2652 0.0333 0.0181 125 VAL A N 986 C CA . VAL A 125 ? 0.8122 0.5578 0.6823 -0.2682 0.0155 0.0143 125 VAL A CA 987 C C . VAL A 125 ? 0.8391 0.5555 0.6883 -0.2721 0.0134 0.0161 125 VAL A C 988 O O . VAL A 125 ? 0.8057 0.5017 0.6473 -0.2665 0.0021 0.0114 125 VAL A O 989 C CB . VAL A 125 ? 0.8235 0.5704 0.7036 -0.2834 0.0036 0.0161 125 VAL A CB 990 C CG1 . VAL A 125 ? 0.8317 0.6066 0.7305 -0.2795 -0.0004 0.0125 125 VAL A CG1 991 C CG2 . VAL A 125 ? 1.0891 0.8419 0.9712 -0.3009 0.0118 0.0278 125 VAL A CG2 992 N N . GLY A 126 ? 0.9637 0.6816 0.8044 -0.2817 0.0247 0.0227 126 GLY A N 993 C CA . GLY A 126 ? 0.9686 0.6638 0.7879 -0.2891 0.0215 0.0275 126 GLY A CA 994 C C . GLY A 126 ? 1.0430 0.7233 0.8611 -0.3064 0.0076 0.0377 126 GLY A C 995 O O . GLY A 126 ? 1.0409 0.7193 0.8746 -0.3089 -0.0037 0.0361 126 GLY A O 996 N N . THR A 127 ? 1.0136 0.6838 0.8143 -0.3194 0.0070 0.0489 127 THR A N 997 C CA . THR A 127 ? 0.8849 0.5385 0.6869 -0.3372 -0.0083 0.0638 127 THR A CA 998 C C . THR A 127 ? 0.9036 0.5390 0.6846 -0.3442 -0.0149 0.0752 127 THR A C 999 O O . THR A 127 ? 1.1899 0.8336 0.9509 -0.3415 -0.0035 0.0726 127 THR A O 1000 C CB . THR A 127 ? 1.1278 0.8047 0.9371 -0.3566 -0.0011 0.0762 127 THR A CB 1001 O OG1 . THR A 127 ? 1.2344 0.8925 1.0515 -0.3745 -0.0193 0.0929 127 THR A OG1 1002 C CG2 . THR A 127 ? 1.1141 0.8148 0.9027 -0.3647 0.0185 0.0816 127 THR A CG2 1003 N N . CYS A 128 ? 0.9816 0.5916 0.7692 -0.3532 -0.0349 0.0878 128 CYS A N 1004 C CA . CYS A 128 ? 0.9461 0.5408 0.7171 -0.3621 -0.0444 0.1040 128 CYS A CA 1005 C C . CYS A 128 ? 1.2573 0.8485 1.0313 -0.3873 -0.0550 0.1304 128 CYS A C 1006 O O . CYS A 128 ? 1.2338 0.8317 1.0255 -0.3975 -0.0558 0.1348 128 CYS A O 1007 C CB . CYS A 128 ? 0.9436 0.5087 0.7241 -0.3466 -0.0612 0.0979 128 CYS A CB 1008 S SG . CYS A 128 ? 1.7702 1.3426 1.5494 -0.3191 -0.0501 0.0719 128 CYS A SG 1009 N N . PHE A 129 ? 1.1428 0.7253 0.9010 -0.3987 -0.0645 0.1503 129 PHE A N 1010 C CA . PHE A 129 ? 1.0332 0.6206 0.7987 -0.4158 -0.0765 0.1779 129 PHE A CA 1011 C C . PHE A 129 ? 1.2279 0.7926 1.0009 -0.4105 -0.0990 0.1923 129 PHE A C 1012 O O . PHE A 129 ? 1.3139 0.8776 1.0639 -0.4093 -0.0995 0.1947 129 PHE A O 1013 C CB . PHE A 129 ? 1.0494 0.6730 0.7841 -0.4379 -0.0592 0.1927 129 PHE A CB 1014 C CG . PHE A 129 ? 1.2992 0.9502 1.0378 -0.4460 -0.0389 0.1854 129 PHE A CG 1015 C CD1 . PHE A 129 ? 1.2374 0.9078 0.9674 -0.4305 -0.0165 0.1588 129 PHE A CD1 1016 C CD2 . PHE A 129 ? 1.0540 0.7207 0.8140 -0.4589 -0.0426 0.2021 129 PHE A CD2 1017 C CE1 . PHE A 129 ? 1.3723 1.0737 1.1135 -0.4323 0.0017 0.1514 129 PHE A CE1 1018 C CE2 . PHE A 129 ? 1.0441 0.7401 0.8117 -0.4666 -0.0243 0.1968 129 PHE A CE2 1019 C CZ . PHE A 129 ? 1.4189 1.1331 1.1775 -0.4527 -0.0018 0.1712 129 PHE A CZ 1020 N N . LEU A 130 ? 1.3301 0.8765 1.1379 -0.4079 -0.1182 0.2017 130 LEU A N 1021 C CA . LEU A 130 ? 1.1014 0.6270 0.9239 -0.4034 -0.1404 0.2179 130 LEU A CA 1022 C C . LEU A 130 ? 1.3626 0.9028 1.1864 -0.4244 -0.1497 0.2521 130 LEU A C 1023 O O . LEU A 130 ? 1.7054 1.2503 1.5492 -0.4336 -0.1513 0.2597 130 LEU A O 1024 C CB . LEU A 130 ? 1.0884 0.5801 0.9525 -0.3840 -0.1560 0.2021 130 LEU A CB 1025 C CG . LEU A 130 ? 1.0986 0.5652 0.9800 -0.3693 -0.1743 0.2052 130 LEU A CG 1026 C CD1 . LEU A 130 ? 1.4230 0.8605 1.3401 -0.3482 -0.1823 0.1786 130 LEU A CD1 1027 C CD2 . LEU A 130 ? 1.5110 0.9751 1.4054 -0.3811 -0.1934 0.2394 130 LEU A CD2 1028 N N . GLN A 131 ? 1.3017 0.8510 1.1041 -0.4331 -0.1567 0.2735 131 GLN A N 1029 C CA . GLN A 131 ? 1.4750 1.0432 1.2739 -0.4545 -0.1664 0.3088 131 GLN A CA 1030 C C . GLN A 131 ? 1.4116 0.9628 1.2260 -0.4514 -0.1922 0.3307 131 GLN A C 1031 O O . GLN A 131 ? 1.3074 0.8579 1.1021 -0.4469 -0.1953 0.3298 131 GLN A O 1032 C CB . GLN A 131 ? 1.4388 1.0491 1.1881 -0.4751 -0.1472 0.3172 131 GLN A CB 1033 C CG . GLN A 131 ? 1.7225 1.3580 1.4584 -0.4974 -0.1585 0.3546 131 GLN A CG 1034 C CD . GLN A 131 ? 1.5771 1.2576 1.2598 -0.5173 -0.1377 0.3578 131 GLN A CD 1035 O OE1 . GLN A 131 ? 1.5879 1.2892 1.2546 -0.5209 -0.1124 0.3401 131 GLN A OE1 1036 N NE2 . GLN A 131 ? 1.5755 1.2733 1.2313 -0.5304 -0.1481 0.3794 131 GLN A NE2 1037 N N . ASP A 132 ? 1.2409 0.7780 1.0933 -0.4541 -0.2118 0.3507 132 ASP A N 1038 C CA . ASP A 132 ? 1.3715 0.8975 1.2408 -0.4541 -0.2373 0.3768 132 ASP A CA 1039 C C . ASP A 132 ? 1.3157 0.8685 1.1793 -0.4799 -0.2476 0.4174 132 ASP A C 1040 O O . ASP A 132 ? 1.3402 0.8859 1.2368 -0.4863 -0.2582 0.4324 132 ASP A O 1041 C CB . ASP A 132 ? 1.3764 0.8596 1.3009 -0.4332 -0.2556 0.3667 132 ASP A CB 1042 C CG . ASP A 132 ? 1.7764 1.2467 1.7270 -0.4312 -0.2830 0.3937 132 ASP A CG 1043 O OD1 . ASP A 132 ? 2.2933 1.7824 2.2168 -0.4387 -0.2875 0.4110 132 ASP A OD1 1044 O OD2 . ASP A 132 ? 1.6931 1.1345 1.6926 -0.4225 -0.3008 0.3968 132 ASP A OD2 1045 N N . GLY A 133 ? 1.7634 1.3489 1.5840 -0.4957 -0.2446 0.4343 133 GLY A N 1046 C CA . GLY A 133 ? 1.7190 1.3323 1.5312 -0.5189 -0.2596 0.4754 133 GLY A CA 1047 C C . GLY A 133 ? 1.8931 1.5394 1.6974 -0.5419 -0.2501 0.4938 133 GLY A C 1048 O O . GLY A 133 ? 2.3714 2.0585 2.1453 -0.5650 -0.2501 0.5203 133 GLY A O 1049 N N . THR A 134 ? 1.7682 1.3999 1.6000 -0.5363 -0.2419 0.4793 134 THR A N 1050 C CA . THR A 134 ? 1.8533 1.5169 1.6808 -0.5563 -0.2296 0.4922 134 THR A CA 1051 C C . THR A 134 ? 1.8434 1.5024 1.6737 -0.5471 -0.2061 0.4582 134 THR A C 1052 O O . THR A 134 ? 2.0453 1.7386 1.8404 -0.5553 -0.1803 0.4468 134 THR A O 1053 C CB . THR A 134 ? 1.7097 1.3626 1.5834 -0.5661 -0.2536 0.5243 134 THR A CB 1054 O OG1 . THR A 134 ? 1.8083 1.4079 1.7317 -0.5441 -0.2710 0.5094 134 THR A OG1 1055 C CG2 . THR A 134 ? 1.4880 1.1631 1.3537 -0.5838 -0.2740 0.5661 134 THR A CG2 1056 N N . LYS A 135 ? 1.4649 1.0821 1.3396 -0.5298 -0.2163 0.4416 135 LYS A N 1057 C CA . LYS A 135 ? 1.4370 1.0470 1.3246 -0.5219 -0.2004 0.4123 135 LYS A CA 1058 C C . LYS A 135 ? 1.3772 0.9827 1.2395 -0.5046 -0.1812 0.3754 135 LYS A C 1059 O O . LYS A 135 ? 1.2691 0.8565 1.1223 -0.4905 -0.1871 0.3661 135 LYS A O 1060 C CB . LYS A 135 ? 1.5255 1.0924 1.4676 -0.5102 -0.2200 0.4053 135 LYS A CB 1061 C CG . LYS A 135 ? 1.6926 1.2534 1.6520 -0.5052 -0.2082 0.3779 135 LYS A CG 1062 C CD . LYS A 135 ? 1.6005 1.1166 1.6106 -0.4932 -0.2290 0.3667 135 LYS A CD 1063 C CE . LYS A 135 ? 1.5074 1.0198 1.5331 -0.4901 -0.2194 0.3386 135 LYS A CE 1064 N NZ . LYS A 135 ? 1.4598 0.9285 1.5313 -0.4785 -0.2392 0.3224 135 LYS A NZ 1065 N N . THR A 136 ? 1.3311 0.9547 1.1846 -0.5062 -0.1591 0.3560 136 THR A N 1066 C CA . THR A 136 ? 1.2949 0.9160 1.1277 -0.4912 -0.1407 0.3220 136 THR A CA 1067 C C . THR A 136 ? 1.4951 1.1022 1.3558 -0.4806 -0.1357 0.2959 136 THR A C 1068 O O . THR A 136 ? 1.7716 1.3998 1.6431 -0.4930 -0.1277 0.3006 136 THR A O 1069 C CB . THR A 136 ? 1.3216 0.9866 1.1078 -0.5045 -0.1145 0.3213 136 THR A CB 1070 O OG1 . THR A 136 ? 1.3949 1.0785 1.1523 -0.5180 -0.1201 0.3464 136 THR A OG1 1071 C CG2 . THR A 136 ? 1.1556 0.8135 0.9215 -0.4886 -0.0980 0.2878 136 THR A CG2 1072 N N . VAL A 137 ? 1.1519 0.7267 1.0245 -0.4584 -0.1407 0.2687 137 VAL A N 1073 C CA . VAL A 137 ? 1.1298 0.6928 1.0251 -0.4481 -0.1375 0.2415 137 VAL A CA 1074 C C . VAL A 137 ? 1.1872 0.7582 1.0582 -0.4365 -0.1183 0.2137 137 VAL A C 1075 O O . VAL A 137 ? 1.2455 0.8144 1.0907 -0.4290 -0.1134 0.2093 137 VAL A O 1076 C CB . VAL A 137 ? 1.1395 0.6599 1.0727 -0.4320 -0.1595 0.2288 137 VAL A CB 1077 C CG1 . VAL A 137 ? 1.2342 0.7438 1.1969 -0.4437 -0.1792 0.2556 137 VAL A CG1 1078 C CG2 . VAL A 137 ? 1.1289 0.6268 1.0546 -0.4125 -0.1652 0.2172 137 VAL A CG2 1079 N N . GLU A 138 ? 1.2008 0.7819 1.0812 -0.4362 -0.1084 0.1964 138 GLU A N 1080 C CA . GLU A 138 ? 1.1672 0.7554 1.0296 -0.4253 -0.0917 0.1709 138 GLU A CA 1081 C C . GLU A 138 ? 1.0237 0.5811 0.9039 -0.4048 -0.1031 0.1441 138 GLU A C 1082 O O . GLU A 138 ? 1.2569 0.7990 1.1671 -0.4035 -0.1173 0.1376 138 GLU A O 1083 C CB . GLU A 138 ? 1.3387 0.9613 1.2006 -0.4373 -0.0733 0.1686 138 GLU A CB 1084 C CG . GLU A 138 ? 1.4666 1.0998 1.3110 -0.4279 -0.0544 0.1458 138 GLU A CG 1085 C CD . GLU A 138 ? 1.4533 1.1264 1.3067 -0.4342 -0.0365 0.1429 138 GLU A CD 1086 O OE1 . GLU A 138 ? 1.4885 1.1679 1.3659 -0.4507 -0.0445 0.1548 138 GLU A OE1 1087 O OE2 . GLU A 138 ? 1.2604 0.9600 1.1015 -0.4207 -0.0150 0.1287 138 GLU A OE2 1088 N N . TYR A 139 ? 1.3702 0.9200 1.2315 -0.3898 -0.0968 0.1278 139 TYR A N 1089 C CA . TYR A 139 ? 1.2649 0.7915 1.1383 -0.3706 -0.1051 0.1016 139 TYR A CA 1090 C C . TYR A 139 ? 1.0241 0.5742 0.8823 -0.3573 -0.0860 0.0805 139 TYR A C 1091 O O . TYR A 139 ? 1.1815 0.7451 1.0179 -0.3490 -0.0721 0.0795 139 TYR A O 1092 C CB . TYR A 139 ? 0.9981 0.4992 0.8729 -0.3563 -0.1171 0.1016 139 TYR A CB 1093 C CG . TYR A 139 ? 0.9896 0.4693 0.8761 -0.3363 -0.1245 0.0739 139 TYR A CG 1094 C CD1 . TYR A 139 ? 1.3891 0.8535 1.3033 -0.3322 -0.1372 0.0572 139 TYR A CD1 1095 C CD2 . TYR A 139 ? 0.9691 0.4529 0.8413 -0.3177 -0.1168 0.0624 139 TYR A CD2 1096 C CE1 . TYR A 139 ? 1.1952 0.6465 1.1178 -0.3125 -0.1423 0.0285 139 TYR A CE1 1097 C CE2 . TYR A 139 ? 0.9606 0.4378 0.8448 -0.2954 -0.1201 0.0368 139 TYR A CE2 1098 C CZ . TYR A 139 ? 1.1517 0.6143 1.0595 -0.2924 -0.1320 0.0190 139 TYR A CZ 1099 O OH . TYR A 139 ? 1.2841 0.7454 1.2010 -0.2703 -0.1336 -0.0090 139 TYR A OH 1100 N N . ALA A 140 ? 0.9475 0.5073 0.8206 -0.3526 -0.0859 0.0637 140 ALA A N 1101 C CA . ALA A 140 ? 0.9161 0.5058 0.7818 -0.3372 -0.0689 0.0467 140 ALA A CA 1102 C C . ALA A 140 ? 0.9113 0.4982 0.7912 -0.3237 -0.0780 0.0229 140 ALA A C 1103 O O . ALA A 140 ? 0.9554 0.5600 0.8470 -0.3291 -0.0784 0.0172 140 ALA A O 1104 C CB . ALA A 140 ? 0.9083 0.5323 0.7740 -0.3496 -0.0533 0.0561 140 ALA A CB 1105 N N . PRO A 141 ? 0.9113 0.4800 0.7901 -0.3065 -0.0852 0.0085 141 PRO A N 1106 C CA . PRO A 141 ? 1.0593 0.6274 0.9481 -0.2930 -0.0935 -0.0171 141 PRO A CA 1107 C C . PRO A 141 ? 0.9832 0.5899 0.8648 -0.2831 -0.0803 -0.0277 141 PRO A C 1108 O O . PRO A 141 ? 1.1608 0.7774 1.0498 -0.2800 -0.0873 -0.0452 141 PRO A O 1109 C CB . PRO A 141 ? 1.1754 0.7234 1.0624 -0.2757 -0.0984 -0.0263 141 PRO A CB 1110 C CG . PRO A 141 ? 0.9932 0.5438 0.8637 -0.2763 -0.0875 -0.0070 141 PRO A CG 1111 C CD . PRO A 141 ? 0.9740 0.5260 0.8417 -0.2989 -0.0853 0.0154 141 PRO A CD 1112 N N . CYS A 142 ? 1.0720 0.7001 0.9406 -0.2788 -0.0628 -0.0170 142 CYS A N 1113 C CA . CYS A 142 ? 1.1516 0.8157 1.0184 -0.2696 -0.0509 -0.0217 142 CYS A CA 1114 C C . CYS A 142 ? 1.1186 0.8055 0.9972 -0.2831 -0.0482 -0.0148 142 CYS A C 1115 O O . CYS A 142 ? 1.0542 0.7723 0.9376 -0.2772 -0.0420 -0.0171 142 CYS A O 1116 C CB . CYS A 142 ? 1.3465 1.0212 1.2015 -0.2599 -0.0346 -0.0133 142 CYS A CB 1117 S SG . CYS A 142 ? 1.0759 0.7567 0.9239 -0.2375 -0.0329 -0.0245 142 CYS A SG 1118 N N . ARG A 143 ? 1.1062 0.7801 0.9923 -0.3019 -0.0534 -0.0037 143 ARG A N 1119 C CA . ARG A 143 ? 0.8738 0.5713 0.7753 -0.3167 -0.0514 0.0043 143 ARG A CA 1120 C C . ARG A 143 ? 0.9585 0.6486 0.8753 -0.3249 -0.0714 -0.0078 143 ARG A C 1121 O O . ARG A 143 ? 1.3896 1.0480 1.3134 -0.3358 -0.0865 -0.0077 143 ARG A O 1122 C CB . ARG A 143 ? 0.8676 0.5622 0.7693 -0.3349 -0.0447 0.0251 143 ARG A CB 1123 C CG . ARG A 143 ? 0.8672 0.5937 0.7870 -0.3497 -0.0384 0.0357 143 ARG A CG 1124 C CD . ARG A 143 ? 0.8769 0.6099 0.7925 -0.3657 -0.0265 0.0560 143 ARG A CD 1125 N NE . ARG A 143 ? 0.9923 0.6948 0.9078 -0.3836 -0.0418 0.0683 143 ARG A NE 1126 C CZ . ARG A 143 ? 1.0709 0.7754 0.9781 -0.3998 -0.0354 0.0888 143 ARG A CZ 1127 N NH1 . ARG A 143 ? 1.1478 0.8838 1.0439 -0.3995 -0.0123 0.0946 143 ARG A NH1 1128 N NH2 . ARG A 143 ? 0.9506 0.6268 0.8615 -0.4165 -0.0524 0.1036 143 ARG A NH2 1129 N N . SER A 144 ? 1.0116 0.7309 0.9350 -0.3201 -0.0728 -0.0179 144 SER A N 1130 C CA . SER A 144 ? 1.2195 0.9344 1.1533 -0.3257 -0.0926 -0.0357 144 SER A CA 1131 C C . SER A 144 ? 1.0698 0.8276 1.0128 -0.3270 -0.0932 -0.0385 144 SER A C 1132 O O . SER A 144 ? 0.9376 0.7278 0.8843 -0.3233 -0.0781 -0.0242 144 SER A O 1133 C CB . SER A 144 ? 1.3326 1.0262 1.2536 -0.3095 -0.1012 -0.0593 144 SER A CB 1134 O OG . SER A 144 ? 0.9116 0.6303 0.8168 -0.2899 -0.0885 -0.0629 144 SER A OG 1135 N N . GLN A 145 ? 0.9585 0.7166 0.9068 -0.3318 -0.1117 -0.0579 145 GLN A N 1136 C CA . GLN A 145 ? 1.0500 0.8502 1.0073 -0.3359 -0.1168 -0.0606 145 GLN A CA 1137 C C . GLN A 145 ? 1.2029 1.0345 1.1429 -0.3158 -0.1097 -0.0673 145 GLN A C 1138 O O . GLN A 145 ? 1.5006 1.3735 1.4468 -0.3168 -0.1122 -0.0641 145 GLN A O 1139 C CB . GLN A 145 ? 1.4346 1.2238 1.4025 -0.3509 -0.1413 -0.0809 145 GLN A CB 1140 C CG . GLN A 145 ? 1.6028 1.3509 1.5891 -0.3704 -0.1525 -0.0759 145 GLN A CG 1141 C CD . GLN A 145 ? 1.4990 1.2664 1.5096 -0.3914 -0.1486 -0.0483 145 GLN A CD 1142 O OE1 . GLN A 145 ? 1.5211 1.3219 1.5329 -0.3870 -0.1296 -0.0286 145 GLN A OE1 1143 N NE2 . GLN A 145 ? 1.2864 1.0335 1.3198 -0.4143 -0.1665 -0.0472 145 GLN A NE2 1144 N N . ASP A 146 ? 1.0435 0.8580 0.9641 -0.2987 -0.1019 -0.0740 146 ASP A N 1145 C CA . ASP A 146 ? 1.2051 1.0495 1.1106 -0.2805 -0.0933 -0.0751 146 ASP A CA 1146 C C . ASP A 146 ? 1.1426 0.9974 1.0523 -0.2728 -0.0733 -0.0500 146 ASP A C 1147 O O . ASP A 146 ? 1.2589 1.0857 1.1629 -0.2685 -0.0635 -0.0446 146 ASP A O 1148 C CB . ASP A 146 ? 1.3283 1.1527 1.2139 -0.2664 -0.0956 -0.0965 146 ASP A CB 1149 C CG . ASP A 146 ? 1.3889 1.2485 1.2591 -0.2496 -0.0871 -0.0956 146 ASP A CG 1150 O OD1 . ASP A 146 ? 1.7443 1.6458 1.6179 -0.2505 -0.0866 -0.0847 146 ASP A OD1 1151 O OD2 . ASP A 146 ? 1.0962 0.9436 0.9534 -0.2360 -0.0817 -0.1037 146 ASP A OD2 1152 N N . ILE A 147 ? 1.0151 0.9105 0.9366 -0.2709 -0.0682 -0.0355 147 ILE A N 1153 C CA . ILE A 147 ? 1.1747 1.0788 1.1102 -0.2666 -0.0504 -0.0135 147 ILE A CA 1154 C C . ILE A 147 ? 1.2851 1.2192 1.2237 -0.2508 -0.0414 -0.0010 147 ILE A C 1155 O O . ILE A 147 ? 1.4469 1.3981 1.3726 -0.2427 -0.0476 -0.0064 147 ILE A O 1156 C CB . ILE A 147 ? 0.9275 0.8502 0.8899 -0.2809 -0.0499 -0.0012 147 ILE A CB 1157 C CG1 . ILE A 147 ? 0.9480 0.9143 0.9242 -0.2840 -0.0618 0.0011 147 ILE A CG1 1158 C CG2 . ILE A 147 ? 0.9134 0.8067 0.8771 -0.2990 -0.0578 -0.0072 147 ILE A CG2 1159 C CD1 . ILE A 147 ? 0.9363 0.9282 0.9447 -0.2965 -0.0607 0.0156 147 ILE A CD1 1160 N N . ASP A 148 ? 1.0012 0.9425 0.9592 -0.2473 -0.0267 0.0158 148 ASP A N 1161 C CA . ASP A 148 ? 0.9857 0.9471 0.9559 -0.2327 -0.0165 0.0310 148 ASP A CA 1162 C C . ASP A 148 ? 1.1079 1.0521 1.0582 -0.2202 -0.0122 0.0282 148 ASP A C 1163 O O . ASP A 148 ? 1.4030 1.3127 1.3344 -0.2210 -0.0099 0.0174 148 ASP A O 1164 C CB . ASP A 148 ? 1.2165 1.2242 1.2021 -0.2313 -0.0266 0.0416 148 ASP A CB 1165 C CG . ASP A 148 ? 1.1655 1.1959 1.1748 -0.2442 -0.0330 0.0457 148 ASP A CG 1166 O OD1 . ASP A 148 ? 1.1073 1.1262 1.1319 -0.2501 -0.0229 0.0482 148 ASP A OD1 1167 O OD2 . ASP A 148 ? 1.1485 1.2117 1.1608 -0.2493 -0.0482 0.0470 148 ASP A OD2 1168 N N . ALA A 149 ? 1.0987 1.0699 1.0559 -0.2097 -0.0122 0.0407 149 ALA A N 1169 C CA . ALA A 149 ? 1.0627 1.0252 1.0060 -0.1988 -0.0082 0.0424 149 ALA A CA 1170 C C . ALA A 149 ? 1.0033 0.9726 0.9191 -0.1987 -0.0190 0.0276 149 ALA A C 1171 O O . ALA A 149 ? 0.9905 0.9394 0.8888 -0.1935 -0.0164 0.0186 149 ALA A O 1172 C CB . ALA A 149 ? 1.3089 1.2980 1.2756 -0.1889 -0.0039 0.0657 149 ALA A CB 1173 N N . ASP A 150 ? 1.0275 1.0285 0.9411 -0.2043 -0.0312 0.0242 150 ASP A N 1174 C CA . ASP A 150 ? 1.0560 1.0694 0.9434 -0.2045 -0.0417 0.0053 150 ASP A CA 1175 C C . ASP A 150 ? 1.0361 1.0074 0.9080 -0.2085 -0.0447 -0.0210 150 ASP A C 1176 O O . ASP A 150 ? 1.0563 1.0234 0.9085 -0.2029 -0.0475 -0.0388 150 ASP A O 1177 C CB . ASP A 150 ? 1.1202 1.1751 1.0087 -0.2128 -0.0559 0.0044 150 ASP A CB 1178 C CG . ASP A 150 ? 1.6028 1.6764 1.4619 -0.2129 -0.0662 -0.0188 150 ASP A CG 1179 O OD1 . ASP A 150 ? 1.7436 1.8200 1.5860 -0.2026 -0.0601 -0.0229 150 ASP A OD1 1180 O OD2 . ASP A 150 ? 1.7556 1.8431 1.6096 -0.2234 -0.0803 -0.0344 150 ASP A OD2 1181 N N . GLY A 151 ? 1.0015 0.9438 0.8850 -0.2180 -0.0441 -0.0219 151 GLY A N 1182 C CA . GLY A 151 ? 0.9844 0.8852 0.8592 -0.2239 -0.0488 -0.0408 151 GLY A CA 1183 C C . GLY A 151 ? 0.9673 0.8313 0.8411 -0.2203 -0.0377 -0.0348 151 GLY A C 1184 O O . GLY A 151 ? 1.2354 1.1026 1.1073 -0.2097 -0.0275 -0.0245 151 GLY A O 1185 N N . GLN A 152 ? 0.9696 0.7998 0.8453 -0.2307 -0.0412 -0.0399 152 GLN A N 1186 C CA . GLN A 152 ? 1.0524 0.8488 0.9243 -0.2304 -0.0335 -0.0342 152 GLN A CA 1187 C C . GLN A 152 ? 0.9139 0.7114 0.7968 -0.2371 -0.0213 -0.0170 152 GLN A C 1188 O O . GLN A 152 ? 0.8586 0.6314 0.7361 -0.2404 -0.0153 -0.0122 152 GLN A O 1189 C CB . GLN A 152 ? 1.0518 0.8115 0.9201 -0.2384 -0.0451 -0.0466 152 GLN A CB 1190 C CG . GLN A 152 ? 0.9314 0.6855 0.7918 -0.2295 -0.0559 -0.0687 152 GLN A CG 1191 C CD . GLN A 152 ? 1.3715 1.0880 1.2376 -0.2380 -0.0702 -0.0814 152 GLN A CD 1192 O OE1 . GLN A 152 ? 1.6112 1.3153 1.4880 -0.2544 -0.0762 -0.0749 152 GLN A OE1 1193 N NE2 . GLN A 152 ? 1.6083 1.3072 1.4708 -0.2270 -0.0758 -0.0982 152 GLN A NE2 1194 N N . GLY A 153 ? 0.8825 0.7111 0.7814 -0.2394 -0.0180 -0.0083 153 GLY A N 1195 C CA . GLY A 153 ? 0.8801 0.7152 0.7941 -0.2447 -0.0054 0.0047 153 GLY A CA 1196 C C . GLY A 153 ? 0.8533 0.6764 0.7637 -0.2367 0.0099 0.0109 153 GLY A C 1197 O O . GLY A 153 ? 0.9080 0.7207 0.8186 -0.2438 0.0194 0.0144 153 GLY A O 1198 N N . PHE A 154 ? 0.9187 0.7462 0.8262 -0.2229 0.0122 0.0122 154 PHE A N 1199 C CA . PHE A 154 ? 0.8398 0.6554 0.7467 -0.2155 0.0245 0.0168 154 PHE A CA 1200 C C . PHE A 154 ? 0.8689 0.6546 0.7538 -0.2140 0.0216 0.0106 154 PHE A C 1201 O O . PHE A 154 ? 1.2250 1.0006 1.1079 -0.2084 0.0289 0.0132 154 PHE A O 1202 C CB . PHE A 154 ? 0.8528 0.6925 0.7781 -0.2029 0.0287 0.0268 154 PHE A CB 1203 C CG . PHE A 154 ? 0.8648 0.7306 0.8186 -0.2027 0.0346 0.0356 154 PHE A CG 1204 C CD1 . PHE A 154 ? 1.0392 0.9329 1.0034 -0.2069 0.0254 0.0389 154 PHE A CD1 1205 C CD2 . PHE A 154 ? 0.8626 0.7257 0.8344 -0.1986 0.0490 0.0387 154 PHE A CD2 1206 C CE1 . PHE A 154 ? 1.1171 1.0378 1.1120 -0.2065 0.0301 0.0487 154 PHE A CE1 1207 C CE2 . PHE A 154 ? 0.8823 0.7709 0.8857 -0.1965 0.0553 0.0459 154 PHE A CE2 1208 C CZ . PHE A 154 ? 1.0052 0.9234 1.0214 -0.2005 0.0456 0.0525 154 PHE A CZ 1209 N N . CYS A 155 ? 0.9904 0.7622 0.8626 -0.2190 0.0096 0.0021 155 CYS A N 1210 C CA . CYS A 155 ? 1.1026 0.8487 0.9592 -0.2162 0.0043 -0.0035 155 CYS A CA 1211 C C . CYS A 155 ? 1.0730 0.7971 0.9207 -0.2199 0.0113 0.0013 155 CYS A C 1212 O O . CYS A 155 ? 0.9107 0.6249 0.7520 -0.2130 0.0110 0.0014 155 CYS A O 1213 C CB . CYS A 155 ? 0.8474 0.5764 0.6988 -0.2236 -0.0095 -0.0131 155 CYS A CB 1214 S SG . CYS A 155 ? 2.1372 1.8315 1.9771 -0.2214 -0.0177 -0.0176 155 CYS A SG 1215 N N . GLN A 156 ? 1.0749 0.7953 0.9220 -0.2315 0.0174 0.0052 156 GLN A N 1216 C CA . GLN A 156 ? 0.9737 0.6762 0.8069 -0.2384 0.0229 0.0081 156 GLN A CA 1217 C C . GLN A 156 ? 1.1981 0.8747 1.0175 -0.2416 0.0100 0.0081 156 GLN A C 1218 O O . GLN A 156 ? 1.0951 0.7593 0.9044 -0.2393 0.0102 0.0094 156 GLN A O 1219 C CB . GLN A 156 ? 0.7869 0.4932 0.6224 -0.2294 0.0340 0.0079 156 GLN A CB 1220 C CG . GLN A 156 ? 1.0200 0.7495 0.8761 -0.2239 0.0463 0.0088 156 GLN A CG 1221 C CD . GLN A 156 ? 1.0784 0.8054 0.9413 -0.2155 0.0555 0.0075 156 GLN A CD 1222 O OE1 . GLN A 156 ? 0.8310 0.5723 0.7156 -0.2048 0.0584 0.0114 156 GLN A OE1 1223 N NE2 . GLN A 156 ? 0.9359 0.6447 0.7815 -0.2215 0.0586 0.0028 156 GLN A NE2 1224 N N . GLY A 157 ? 1.1858 0.8538 1.0082 -0.2469 -0.0023 0.0064 157 GLY A N 1225 C CA . GLY A 157 ? 0.9488 0.5906 0.7657 -0.2490 -0.0163 0.0068 157 GLY A CA 1226 C C . GLY A 157 ? 1.0144 0.6410 0.8170 -0.2621 -0.0162 0.0185 157 GLY A C 1227 O O . GLY A 157 ? 1.1336 0.7679 0.9310 -0.2755 -0.0089 0.0256 157 GLY A O 1228 N N . GLY A 158 ? 0.8271 0.4364 0.6235 -0.2588 -0.0243 0.0211 158 GLY A N 1229 C CA . GLY A 158 ? 0.9479 0.5464 0.7277 -0.2715 -0.0260 0.0334 158 GLY A CA 1230 C C . GLY A 158 ? 0.9930 0.5986 0.7612 -0.2662 -0.0163 0.0309 158 GLY A C 1231 O O . GLY A 158 ? 0.8970 0.4982 0.6475 -0.2767 -0.0164 0.0380 158 GLY A O 1232 N N . PHE A 159 ? 1.2181 0.8360 0.9968 -0.2511 -0.0090 0.0212 159 PHE A N 1233 C CA . PHE A 159 ? 1.2064 0.8287 0.9810 -0.2453 -0.0018 0.0187 159 PHE A CA 1234 C C . PHE A 159 ? 1.1722 0.7797 0.9411 -0.2453 -0.0139 0.0240 159 PHE A C 1235 O O . PHE A 159 ? 0.8844 0.4898 0.6424 -0.2496 -0.0121 0.0251 159 PHE A O 1236 C CB . PHE A 159 ? 1.0941 0.7327 0.8863 -0.2297 0.0047 0.0126 159 PHE A CB 1237 C CG . PHE A 159 ? 0.8263 0.4698 0.6208 -0.2256 0.0135 0.0111 159 PHE A CG 1238 C CD1 . PHE A 159 ? 0.8030 0.4542 0.5994 -0.2283 0.0268 0.0070 159 PHE A CD1 1239 C CD2 . PHE A 159 ? 1.1700 0.8107 0.9691 -0.2189 0.0082 0.0133 159 PHE A CD2 1240 C CE1 . PHE A 159 ? 0.9443 0.5957 0.7476 -0.2242 0.0335 0.0037 159 PHE A CE1 1241 C CE2 . PHE A 159 ? 0.8394 0.4821 0.6445 -0.2168 0.0144 0.0125 159 PHE A CE2 1242 C CZ . PHE A 159 ? 0.8672 0.5129 0.6748 -0.2194 0.0265 0.0069 159 PHE A CZ 1243 N N . SER A 160 ? 0.8159 0.4138 0.5948 -0.2403 -0.0270 0.0261 160 SER A N 1244 C CA . SER A 160 ? 1.0724 0.6572 0.8522 -0.2395 -0.0406 0.0332 160 SER A CA 1245 C C . SER A 160 ? 1.1666 0.7346 0.9569 -0.2407 -0.0554 0.0375 160 SER A C 1246 O O . SER A 160 ? 1.4396 1.0082 1.2425 -0.2344 -0.0559 0.0287 160 SER A O 1247 C CB . SER A 160 ? 1.0820 0.6771 0.8760 -0.2236 -0.0396 0.0283 160 SER A CB 1248 O OG . SER A 160 ? 0.8893 0.4953 0.6989 -0.2099 -0.0373 0.0188 160 SER A OG 1249 N N . ILE A 161 ? 1.0957 0.6484 0.8824 -0.2494 -0.0691 0.0511 161 ILE A N 1250 C CA . ILE A 161 ? 0.8830 0.4155 0.6846 -0.2519 -0.0857 0.0586 161 ILE A CA 1251 C C . ILE A 161 ? 0.9084 0.4286 0.7217 -0.2486 -0.1024 0.0701 161 ILE A C 1252 O O . ILE A 161 ? 0.9767 0.5039 0.7781 -0.2524 -0.1030 0.0777 161 ILE A O 1253 C CB . ILE A 161 ? 0.9428 0.4681 0.7311 -0.2734 -0.0883 0.0727 161 ILE A CB 1254 C CG1 . ILE A 161 ? 0.9143 0.4493 0.6731 -0.2896 -0.0836 0.0848 161 ILE A CG1 1255 C CG2 . ILE A 161 ? 0.8950 0.4300 0.6843 -0.2752 -0.0765 0.0622 161 ILE A CG2 1256 C CD1 . ILE A 161 ? 1.5036 1.0406 1.2461 -0.3119 -0.0832 0.0999 161 ILE A CD1 1257 N N . ASP A 162 ? 1.2317 0.7337 1.0714 -0.2415 -0.1169 0.0707 162 ASP A N 1258 C CA . ASP A 162 ? 1.1893 0.6784 1.0479 -0.2377 -0.1351 0.0839 162 ASP A CA 1259 C C . ASP A 162 ? 1.1188 0.5804 1.0067 -0.2365 -0.1528 0.0887 162 ASP A C 1260 O O . ASP A 162 ? 1.2136 0.6671 1.1104 -0.2344 -0.1504 0.0750 162 ASP A O 1261 C CB . ASP A 162 ? 1.0698 0.5733 0.9452 -0.2164 -0.1314 0.0714 162 ASP A CB 1262 C CG . ASP A 162 ? 1.5008 1.0077 1.3774 -0.2196 -0.1422 0.0891 162 ASP A CG 1263 O OD1 . ASP A 162 ? 1.5770 1.0697 1.4503 -0.2344 -0.1581 0.1113 162 ASP A OD1 1264 O OD2 . ASP A 162 ? 1.5598 1.0855 1.4412 -0.2088 -0.1358 0.0828 162 ASP A OD2 1265 N N . PHE A 163 ? 1.1586 0.6054 1.0643 -0.2384 -0.1723 0.1086 163 PHE A N 1266 C CA . PHE A 163 ? 1.0065 0.4231 0.9484 -0.2361 -0.1923 0.1155 163 PHE A CA 1267 C C . PHE A 163 ? 1.0923 0.5034 1.0749 -0.2107 -0.2010 0.1043 163 PHE A C 1268 O O . PHE A 163 ? 1.0088 0.4392 0.9909 -0.2016 -0.1978 0.1052 163 PHE A O 1269 C CB . PHE A 163 ? 1.0382 0.4408 0.9755 -0.2596 -0.2111 0.1526 163 PHE A CB 1270 C CG . PHE A 163 ? 1.2424 0.6527 1.1524 -0.2815 -0.2036 0.1625 163 PHE A CG 1271 C CD1 . PHE A 163 ? 1.2041 0.6378 1.0702 -0.2997 -0.1920 0.1731 163 PHE A CD1 1272 C CD2 . PHE A 163 ? 1.1399 0.5391 1.0708 -0.2822 -0.2070 0.1592 163 PHE A CD2 1273 C CE1 . PHE A 163 ? 1.2047 0.6521 1.0489 -0.3175 -0.1830 0.1808 163 PHE A CE1 1274 C CE2 . PHE A 163 ? 1.1466 0.5598 1.0566 -0.3011 -0.1991 0.1694 163 PHE A CE2 1275 C CZ . PHE A 163 ? 1.1491 0.5875 1.0162 -0.3183 -0.1866 0.1805 163 PHE A CZ 1276 N N . THR A 164 ? 1.2903 0.6762 1.3108 -0.1993 -0.2119 0.0926 164 THR A N 1277 C CA . THR A 164 ? 1.4000 0.7784 1.4662 -0.1744 -0.2217 0.0820 164 THR A CA 1278 C C . THR A 164 ? 1.4558 0.8024 1.5579 -0.1805 -0.2498 0.1110 164 THR A C 1279 O O . THR A 164 ? 1.6958 1.0282 1.7840 -0.2055 -0.2610 0.1401 164 THR A O 1280 C CB . THR A 164 ? 1.2459 0.6196 1.3353 -0.1528 -0.2142 0.0420 164 THR A CB 1281 O OG1 . THR A 164 ? 1.1755 0.5152 1.2792 -0.1630 -0.2265 0.0408 164 THR A OG1 1282 C CG2 . THR A 164 ? 1.0069 0.4147 1.0611 -0.1486 -0.1884 0.0178 164 THR A CG2 1283 N N . LYS A 165 ? 1.2398 0.5776 1.3903 -0.1576 -0.2609 0.1043 165 LYS A N 1284 C CA . LYS A 165 ? 1.2032 0.5093 1.3985 -0.1595 -0.2897 0.1320 165 LYS A CA 1285 C C . LYS A 165 ? 1.2820 0.5629 1.5011 -0.1597 -0.2965 0.1230 165 LYS A C 1286 O O . LYS A 165 ? 1.4523 0.7258 1.6914 -0.1678 -0.3130 0.1501 165 LYS A O 1287 C CB . LYS A 165 ? 1.1369 0.4482 1.3827 -0.1306 -0.2966 0.1239 165 LYS A CB 1288 C CG . LYS A 165 ? 1.2850 0.6371 1.5111 -0.1273 -0.2871 0.1322 165 LYS A CG 1289 C CD . LYS A 165 ? 1.3890 0.7527 1.6691 -0.0962 -0.2902 0.1195 165 LYS A CD 1290 C CE . LYS A 165 ? 1.6303 0.9689 1.9645 -0.0939 -0.3213 0.1513 165 LYS A CE 1291 N NZ . LYS A 165 ? 1.6367 0.9299 2.0201 -0.0839 -0.3365 0.1411 165 LYS A NZ 1292 N N . ALA A 166 ? 1.3381 0.6116 1.5539 -0.1512 -0.2835 0.0844 166 ALA A N 1293 C CA . ALA A 166 ? 1.5374 0.7911 1.7763 -0.1489 -0.2877 0.0678 166 ALA A CA 1294 C C . ALA A 166 ? 1.5219 0.7838 1.7215 -0.1763 -0.2810 0.0823 166 ALA A C 1295 O O . ALA A 166 ? 1.6821 0.9308 1.8939 -0.1785 -0.2825 0.0682 166 ALA A O 1296 C CB . ALA A 166 ? 1.8283 1.0738 2.0845 -0.1254 -0.2783 0.0156 166 ALA A CB 1297 N N . ASP A 167 ? 1.4285 0.7137 1.5827 -0.1965 -0.2733 0.1085 167 ASP A N 1298 C CA . ASP A 167 ? 1.3774 0.6773 1.4925 -0.2212 -0.2633 0.1210 167 ASP A CA 1299 C C . ASP A 167 ? 1.2147 0.5177 1.3120 -0.2193 -0.2464 0.0860 167 ASP A C 1300 O O . ASP A 167 ? 1.2526 0.5528 1.3501 -0.2295 -0.2450 0.0822 167 ASP A O 1301 C CB . ASP A 167 ? 1.7444 1.0340 1.8806 -0.2343 -0.2782 0.1456 167 ASP A CB 1302 C CG . ASP A 167 ? 1.9412 1.2394 2.0779 -0.2459 -0.2932 0.1887 167 ASP A CG 1303 O OD1 . ASP A 167 ? 1.8594 1.1813 1.9575 -0.2569 -0.2861 0.2046 167 ASP A OD1 1304 O OD2 . ASP A 167 ? 2.1785 1.4608 2.3546 -0.2448 -0.3132 0.2063 167 ASP A OD2 1305 N N . ARG A 168 ? 1.3556 0.6658 1.4391 -0.2068 -0.2352 0.0618 168 ARG A N 1306 C CA . ARG A 168 ? 1.2116 0.5362 1.2687 -0.2067 -0.2176 0.0334 168 ARG A CA 1307 C C . ARG A 168 ? 1.2272 0.5882 1.2362 -0.2173 -0.1980 0.0458 168 ARG A C 1308 O O . ARG A 168 ? 1.2088 0.5855 1.2082 -0.2125 -0.1946 0.0570 168 ARG A O 1309 C CB . ARG A 168 ? 1.0694 0.4048 1.1433 -0.1770 -0.2089 -0.0077 168 ARG A CB 1310 C CG . ARG A 168 ? 1.1041 0.4152 1.2065 -0.1699 -0.2173 -0.0387 168 ARG A CG 1311 C CD . ARG A 168 ? 1.2575 0.5936 1.3611 -0.1435 -0.2026 -0.0821 168 ARG A CD 1312 N NE . ARG A 168 ? 1.4977 0.8125 1.6250 -0.1372 -0.2108 -0.1168 168 ARG A NE 1313 C CZ . ARG A 168 ? 1.4473 0.7694 1.5546 -0.1486 -0.2060 -0.1324 168 ARG A CZ 1314 N NH1 . ARG A 168 ? 1.1528 0.5031 1.2193 -0.1652 -0.1922 -0.1152 168 ARG A NH1 1315 N NH2 . ARG A 168 ? 1.6873 0.9888 1.8178 -0.1433 -0.2158 -0.1663 168 ARG A NH2 1316 N N . VAL A 169 ? 1.1775 0.5517 1.1598 -0.2318 -0.1860 0.0432 169 VAL A N 1317 C CA . VAL A 169 ? 0.9978 0.4050 0.9392 -0.2398 -0.1663 0.0499 169 VAL A CA 1318 C C . VAL A 169 ? 1.0521 0.4875 0.9837 -0.2208 -0.1478 0.0208 169 VAL A C 1319 O O . VAL A 169 ? 1.1623 0.6009 1.0999 -0.2147 -0.1441 -0.0023 169 VAL A O 1320 C CB . VAL A 169 ? 1.0003 0.4127 0.9211 -0.2645 -0.1612 0.0634 169 VAL A CB 1321 C CG1 . VAL A 169 ? 1.4256 0.8731 1.3113 -0.2665 -0.1380 0.0592 169 VAL A CG1 1322 C CG2 . VAL A 169 ? 1.0253 0.4299 0.9473 -0.2832 -0.1733 0.0979 169 VAL A CG2 1323 N N . LEU A 170 ? 1.1246 0.5818 1.0419 -0.2127 -0.1374 0.0234 170 LEU A N 1324 C CA . LEU A 170 ? 1.0894 0.5775 0.9957 -0.1984 -0.1193 0.0030 170 LEU A CA 1325 C C . LEU A 170 ? 1.1043 0.6130 0.9798 -0.2116 -0.1037 0.0107 170 LEU A C 1326 O O . LEU A 170 ? 1.3403 0.8540 1.1988 -0.2206 -0.1002 0.0271 170 LEU A O 1327 C CB . LEU A 170 ? 0.9038 0.4057 0.8188 -0.1814 -0.1171 0.0011 170 LEU A CB 1328 C CG . LEU A 170 ? 0.9029 0.4396 0.8096 -0.1674 -0.0993 -0.0159 170 LEU A CG 1329 C CD1 . LEU A 170 ? 0.9255 0.4686 0.8412 -0.1564 -0.0967 -0.0426 170 LEU A CD1 1330 C CD2 . LEU A 170 ? 1.0785 0.6312 0.9974 -0.1529 -0.0978 -0.0142 170 LEU A CD2 1331 N N . LEU A 171 ? 1.1237 0.6450 0.9938 -0.2125 -0.0949 -0.0025 171 LEU A N 1332 C CA . LEU A 171 ? 1.0926 0.6336 0.9407 -0.2231 -0.0801 0.0034 171 LEU A CA 1333 C C . LEU A 171 ? 1.4017 0.9717 1.2473 -0.2105 -0.0667 -0.0128 171 LEU A C 1334 O O . LEU A 171 ? 1.6986 1.2740 1.5522 -0.2057 -0.0686 -0.0283 171 LEU A O 1335 C CB . LEU A 171 ? 1.0837 0.6149 0.9298 -0.2421 -0.0837 0.0113 171 LEU A CB 1336 C CG . LEU A 171 ? 1.0778 0.6287 0.9059 -0.2551 -0.0690 0.0192 171 LEU A CG 1337 C CD1 . LEU A 171 ? 1.4944 1.0328 1.3212 -0.2769 -0.0758 0.0361 171 LEU A CD1 1338 C CD2 . LEU A 171 ? 0.8934 0.4676 0.7245 -0.2485 -0.0590 0.0044 171 LEU A CD2 1339 N N . GLY A 172 ? 1.2750 0.8641 1.1104 -0.2061 -0.0548 -0.0083 172 GLY A N 1340 C CA . GLY A 172 ? 1.3131 0.9317 1.1471 -0.1971 -0.0425 -0.0165 172 GLY A CA 1341 C C . GLY A 172 ? 1.0904 0.7212 0.9145 -0.2067 -0.0307 -0.0087 172 GLY A C 1342 O O . GLY A 172 ? 0.9227 0.5421 0.7376 -0.2198 -0.0293 0.0014 172 GLY A O 1343 N N . GLY A 173 ? 1.0388 0.6959 0.8661 -0.1999 -0.0221 -0.0132 173 GLY A N 1344 C CA . GLY A 173 ? 0.9924 0.6638 0.8176 -0.2035 -0.0097 -0.0056 173 GLY A CA 1345 C C . GLY A 173 ? 1.0821 0.7826 0.9155 -0.1915 -0.0034 -0.0062 173 GLY A C 1346 O O . GLY A 173 ? 1.3882 1.1041 1.2247 -0.1841 -0.0076 -0.0144 173 GLY A O 1347 N N . PRO A 174 ? 0.8611 0.5704 0.6986 -0.1903 0.0062 0.0026 174 PRO A N 1348 C CA . PRO A 174 ? 0.8596 0.5958 0.7086 -0.1805 0.0115 0.0088 174 PRO A CA 1349 C C . PRO A 174 ? 0.9588 0.7214 0.8167 -0.1792 0.0138 0.0106 174 PRO A C 1350 O O . PRO A 174 ? 1.2841 1.0740 1.1488 -0.1715 0.0143 0.0161 174 PRO A O 1351 C CB . PRO A 174 ? 1.2102 0.9375 1.0646 -0.1824 0.0188 0.0171 174 PRO A CB 1352 C CG . PRO A 174 ? 0.9531 0.6591 0.7974 -0.1936 0.0211 0.0130 174 PRO A CG 1353 C CD . PRO A 174 ? 0.7833 0.4751 0.6150 -0.1989 0.0114 0.0072 174 PRO A CD 1354 N N . GLY A 175 ? 0.8317 0.5899 0.6900 -0.1875 0.0148 0.0082 175 GLY A N 1355 C CA . GLY A 175 ? 0.9277 0.7121 0.7993 -0.1871 0.0173 0.0131 175 GLY A CA 1356 C C . GLY A 175 ? 0.9294 0.7334 0.7987 -0.1878 0.0084 0.0061 175 GLY A C 1357 O O . GLY A 175 ? 1.3673 1.1949 1.2482 -0.1894 0.0086 0.0112 175 GLY A O 1358 N N . SER A 176 ? 0.8896 0.6847 0.7462 -0.1865 -0.0001 -0.0069 176 SER A N 1359 C CA . SER A 176 ? 0.9522 0.7632 0.8052 -0.1876 -0.0096 -0.0194 176 SER A CA 1360 C C . SER A 176 ? 1.2032 1.0554 1.0562 -0.1791 -0.0097 -0.0163 176 SER A C 1361 O O . SER A 176 ? 1.4143 1.2772 1.2652 -0.1701 -0.0054 -0.0110 176 SER A O 1362 C CB . SER A 176 ? 0.9343 0.7204 0.7778 -0.1873 -0.0188 -0.0374 176 SER A CB 1363 O OG . SER A 176 ? 0.9066 0.6617 0.7517 -0.1993 -0.0236 -0.0391 176 SER A OG 1364 N N . PHE A 177 ? 1.0190 0.8969 0.8746 -0.1835 -0.0154 -0.0178 177 PHE A N 1365 C CA . PHE A 177 ? 1.0294 0.9525 0.8814 -0.1783 -0.0182 -0.0148 177 PHE A CA 1366 C C . PHE A 177 ? 1.0502 0.9955 0.9136 -0.1715 -0.0097 0.0104 177 PHE A C 1367 O O . PHE A 177 ? 1.0620 1.0244 0.9188 -0.1639 -0.0070 0.0138 177 PHE A O 1368 C CB . PHE A 177 ? 1.0518 0.9817 0.8852 -0.1721 -0.0230 -0.0367 177 PHE A CB 1369 C CG . PHE A 177 ? 1.0545 0.9472 0.8829 -0.1761 -0.0307 -0.0612 177 PHE A CG 1370 C CD1 . PHE A 177 ? 1.0369 0.9008 0.8625 -0.1695 -0.0291 -0.0709 177 PHE A CD1 1371 C CD2 . PHE A 177 ? 1.0223 0.9086 0.8531 -0.1873 -0.0410 -0.0722 177 PHE A CD2 1372 C CE1 . PHE A 177 ? 1.0478 0.8756 0.8742 -0.1730 -0.0381 -0.0902 177 PHE A CE1 1373 C CE2 . PHE A 177 ? 1.0071 0.8564 0.8383 -0.1923 -0.0499 -0.0920 177 PHE A CE2 1374 C CZ . PHE A 177 ? 0.9983 0.8173 0.8279 -0.1847 -0.0487 -0.1005 177 PHE A CZ 1375 N N . TYR A 178 ? 1.0943 1.0406 0.9785 -0.1744 -0.0056 0.0280 178 TYR A N 1376 C CA . TYR A 178 ? 0.9723 0.9307 0.8757 -0.1684 0.0015 0.0525 178 TYR A CA 1377 C C . TYR A 178 ? 1.0152 0.9497 0.9150 -0.1631 0.0081 0.0532 178 TYR A C 1378 O O . TYR A 178 ? 0.9585 0.9124 0.8633 -0.1576 0.0100 0.0679 178 TYR A O 1379 C CB . TYR A 178 ? 0.9953 1.0042 0.9023 -0.1656 -0.0037 0.0692 178 TYR A CB 1380 C CG . TYR A 178 ? 1.0122 1.0468 0.9368 -0.1702 -0.0094 0.0805 178 TYR A CG 1381 C CD1 . TYR A 178 ? 1.0175 1.0556 0.9759 -0.1674 -0.0052 0.1039 178 TYR A CD1 1382 C CD2 . TYR A 178 ? 1.0502 1.1052 0.9611 -0.1772 -0.0200 0.0670 178 TYR A CD2 1383 C CE1 . TYR A 178 ? 0.9933 1.0575 0.9732 -0.1705 -0.0109 0.1157 178 TYR A CE1 1384 C CE2 . TYR A 178 ? 1.0543 1.1359 0.9838 -0.1823 -0.0267 0.0788 178 TYR A CE2 1385 C CZ . TYR A 178 ? 1.0245 1.1120 0.9894 -0.1785 -0.0219 0.1043 178 TYR A CZ 1386 O OH . TYR A 178 ? 1.0409 1.1574 1.0294 -0.1825 -0.0290 0.1175 178 TYR A OH 1387 N N . TRP A 179 ? 1.1545 1.0491 1.0464 -0.1664 0.0105 0.0391 179 TRP A N 1388 C CA . TRP A 179 ? 0.9235 0.7914 0.8132 -0.1638 0.0155 0.0394 179 TRP A CA 1389 C C . TRP A 179 ? 0.9275 0.8068 0.8057 -0.1574 0.0133 0.0358 179 TRP A C 1390 O O . TRP A 179 ? 0.9103 0.7822 0.7936 -0.1543 0.0168 0.0438 179 TRP A O 1391 C CB . TRP A 179 ? 0.8676 0.7328 0.7802 -0.1618 0.0226 0.0574 179 TRP A CB 1392 C CG . TRP A 179 ? 0.8529 0.7012 0.7770 -0.1664 0.0279 0.0553 179 TRP A CG 1393 C CD1 . TRP A 179 ? 0.8466 0.6620 0.7647 -0.1714 0.0331 0.0455 179 TRP A CD1 1394 C CD2 . TRP A 179 ? 0.8627 0.7313 0.8065 -0.1668 0.0289 0.0632 179 TRP A CD2 1395 N NE1 . TRP A 179 ? 0.9564 0.7718 0.8885 -0.1744 0.0393 0.0452 179 TRP A NE1 1396 C CE2 . TRP A 179 ? 0.8835 0.7305 0.8341 -0.1709 0.0368 0.0562 179 TRP A CE2 1397 C CE3 . TRP A 179 ? 0.8846 0.7909 0.8415 -0.1643 0.0236 0.0765 179 TRP A CE3 1398 C CZ2 . TRP A 179 ? 0.9469 0.8089 0.9208 -0.1711 0.0407 0.0610 179 TRP A CZ2 1399 C CZ3 . TRP A 179 ? 0.8906 0.8101 0.8711 -0.1652 0.0252 0.0833 179 TRP A CZ3 1400 C CH2 . TRP A 179 ? 0.8772 0.7744 0.8677 -0.1678 0.0343 0.0751 179 TRP A CH2 1401 N N . GLN A 180 ? 0.9783 0.8768 0.8424 -0.1557 0.0075 0.0222 180 GLN A N 1402 C CA . GLN A 180 ? 1.0121 0.9182 0.8652 -0.1486 0.0067 0.0113 180 GLN A CA 1403 C C . GLN A 180 ? 0.9862 0.8490 0.8357 -0.1495 0.0051 -0.0011 180 GLN A C 1404 O O . GLN A 180 ? 0.9909 0.8500 0.8413 -0.1438 0.0067 -0.0012 180 GLN A O 1405 C CB . GLN A 180 ? 1.0730 1.0069 0.9115 -0.1462 0.0010 -0.0071 180 GLN A CB 1406 C CG . GLN A 180 ? 1.0999 1.0862 0.9372 -0.1454 0.0011 0.0063 180 GLN A CG 1407 C CD . GLN A 180 ? 1.1126 1.1270 0.9311 -0.1446 -0.0053 -0.0167 180 GLN A CD 1408 O OE1 . GLN A 180 ? 1.1080 1.1018 0.9172 -0.1421 -0.0090 -0.0444 180 GLN A OE1 1409 N NE2 . GLN A 180 ? 1.2324 1.2943 1.0464 -0.1470 -0.0078 -0.0055 180 GLN A NE2 1410 N N . GLY A 181 ? 0.9607 0.7939 0.8080 -0.1577 0.0013 -0.0088 181 GLY A N 1411 C CA . GLY A 181 ? 0.9223 0.7161 0.7659 -0.1612 -0.0025 -0.0171 181 GLY A CA 1412 C C . GLY A 181 ? 0.9508 0.7367 0.7887 -0.1580 -0.0114 -0.0384 181 GLY A C 1413 O O . GLY A 181 ? 1.2795 1.0932 1.1140 -0.1506 -0.0126 -0.0498 181 GLY A O 1414 N N . GLN A 182 ? 0.9534 0.7024 0.7913 -0.1638 -0.0181 -0.0440 182 GLN A N 1415 C CA . GLN A 182 ? 1.0893 0.8233 0.9290 -0.1602 -0.0284 -0.0640 182 GLN A CA 1416 C C . GLN A 182 ? 1.0168 0.7107 0.8614 -0.1645 -0.0357 -0.0609 182 GLN A C 1417 O O . GLN A 182 ? 0.8830 0.5610 0.7244 -0.1743 -0.0334 -0.0448 182 GLN A O 1418 C CB . GLN A 182 ? 1.1360 0.8712 0.9745 -0.1676 -0.0356 -0.0768 182 GLN A CB 1419 C CG . GLN A 182 ? 0.9181 0.6266 0.7592 -0.1840 -0.0397 -0.0675 182 GLN A CG 1420 C CD . GLN A 182 ? 0.9632 0.6683 0.8082 -0.1923 -0.0503 -0.0817 182 GLN A CD 1421 O OE1 . GLN A 182 ? 1.2267 0.9297 1.0747 -0.2060 -0.0510 -0.0726 182 GLN A OE1 1422 N NE2 . GLN A 182 ? 1.0697 0.7754 0.9166 -0.1844 -0.0587 -0.1054 182 GLN A NE2 1423 N N . LEU A 183 ? 1.1393 0.8186 0.9926 -0.1569 -0.0447 -0.0767 183 LEU A N 1424 C CA . LEU A 183 ? 1.0072 0.6480 0.8698 -0.1612 -0.0554 -0.0722 183 LEU A CA 1425 C C . LEU A 183 ? 1.2364 0.8519 1.1082 -0.1677 -0.0687 -0.0855 183 LEU A C 1426 O O . LEU A 183 ? 1.0602 0.6861 0.9356 -0.1608 -0.0715 -0.1083 183 LEU A O 1427 C CB . LEU A 183 ? 0.9473 0.5880 0.8221 -0.1461 -0.0570 -0.0764 183 LEU A CB 1428 C CG . LEU A 183 ? 0.9437 0.6092 0.8147 -0.1401 -0.0460 -0.0630 183 LEU A CG 1429 C CD1 . LEU A 183 ? 0.9733 0.6413 0.8617 -0.1251 -0.0490 -0.0687 183 LEU A CD1 1430 C CD2 . LEU A 183 ? 0.8999 0.5510 0.7613 -0.1544 -0.0444 -0.0402 183 LEU A CD2 1431 N N . ILE A 184 ? 1.1293 0.7131 1.0048 -0.1823 -0.0775 -0.0710 184 ILE A N 1432 C CA . ILE A 184 ? 0.9466 0.5027 0.8358 -0.1912 -0.0923 -0.0790 184 ILE A CA 1433 C C . ILE A 184 ? 1.0396 0.5579 0.9452 -0.1949 -0.1065 -0.0670 184 ILE A C 1434 O O . ILE A 184 ? 1.2355 0.7457 1.1331 -0.2065 -0.1061 -0.0421 184 ILE A O 1435 C CB . ILE A 184 ? 0.9298 0.4889 0.8110 -0.2110 -0.0908 -0.0682 184 ILE A CB 1436 C CG1 . ILE A 184 ? 0.8989 0.4974 0.7671 -0.2075 -0.0778 -0.0748 184 ILE A CG1 1437 C CG2 . ILE A 184 ? 1.0454 0.5776 0.9444 -0.2215 -0.1076 -0.0767 184 ILE A CG2 1438 C CD1 . ILE A 184 ? 1.0355 0.6432 0.8999 -0.2248 -0.0743 -0.0627 184 ILE A CD1 1439 N N . SER A 185 ? 1.1068 0.6034 1.0365 -0.1850 -0.1197 -0.0852 185 SER A N 1440 C CA . SER A 185 ? 1.2073 0.6672 1.1602 -0.1868 -0.1359 -0.0725 185 SER A CA 1441 C C . SER A 185 ? 1.3291 0.7532 1.3046 -0.1992 -0.1544 -0.0751 185 SER A C 1442 O O . SER A 185 ? 1.3959 0.8157 1.3837 -0.1931 -0.1593 -0.1037 185 SER A O 1443 C CB . SER A 185 ? 1.2125 0.6726 1.1855 -0.1628 -0.1377 -0.0882 185 SER A CB 1444 O OG . SER A 185 ? 1.3487 0.7752 1.3475 -0.1638 -0.1544 -0.0716 185 SER A OG 1445 N N . ASP A 186 ? 1.1621 0.5620 1.1428 -0.2178 -0.1653 -0.0446 186 ASP A N 1446 C CA . ASP A 186 ? 1.2877 0.6517 1.2944 -0.2328 -0.1850 -0.0394 186 ASP A CA 1447 C C . ASP A 186 ? 1.4139 0.7502 1.4437 -0.2370 -0.2009 -0.0114 186 ASP A C 1448 O O . ASP A 186 ? 1.2213 0.5664 1.2352 -0.2416 -0.1975 0.0145 186 ASP A O 1449 C CB . ASP A 186 ? 1.4018 0.7768 1.3914 -0.2578 -0.1807 -0.0243 186 ASP A CB 1450 C CG . ASP A 186 ? 1.5574 0.9534 1.5400 -0.2548 -0.1731 -0.0530 186 ASP A CG 1451 O OD1 . ASP A 186 ? 1.5423 0.9173 1.5489 -0.2538 -0.1871 -0.0751 186 ASP A OD1 1452 O OD2 . ASP A 186 ? 1.6450 1.0782 1.5997 -0.2540 -0.1545 -0.0533 186 ASP A OD2 1453 N N . GLN A 187 ? 1.2862 0.6000 1.3537 -0.2325 -0.2152 -0.0167 187 GLN A N 1454 C CA . GLN A 187 ? 1.2926 0.5905 1.3859 -0.2339 -0.2290 0.0123 187 GLN A CA 1455 C C . GLN A 187 ? 1.3228 0.6349 1.3998 -0.2593 -0.2278 0.0513 187 GLN A C 1456 O O . GLN A 187 ? 1.1389 0.4603 1.2085 -0.2740 -0.2233 0.0510 187 GLN A O 1457 C CB . GLN A 187 ? 1.3658 0.6343 1.5053 -0.2222 -0.2448 -0.0057 187 GLN A CB 1458 C CG . GLN A 187 ? 1.4907 0.7490 1.6476 -0.1953 -0.2446 -0.0499 187 GLN A CG 1459 C CD . GLN A 187 ? 1.8265 1.0597 2.0230 -0.1854 -0.2567 -0.0768 187 GLN A CD 1460 O OE1 . GLN A 187 ? 1.6640 0.8851 1.8754 -0.2002 -0.2662 -0.0615 187 GLN A OE1 1461 N NE2 . GLN A 187 ? 2.0164 1.2433 2.2306 -0.1600 -0.2561 -0.1183 187 GLN A NE2 1462 N N . VAL A 188 ? 1.1829 0.4997 1.2544 -0.2647 -0.2324 0.0842 188 VAL A N 1463 C CA . VAL A 188 ? 1.1462 0.4809 1.1987 -0.2885 -0.2314 0.1210 188 VAL A CA 1464 C C . VAL A 188 ? 1.3859 0.7094 1.4651 -0.3007 -0.2429 0.1318 188 VAL A C 1465 O O . VAL A 188 ? 1.1788 0.5206 1.2420 -0.3201 -0.2360 0.1453 188 VAL A O 1466 C CB . VAL A 188 ? 1.1541 0.4936 1.2012 -0.2916 -0.2399 0.1532 188 VAL A CB 1467 C CG1 . VAL A 188 ? 1.1679 0.5275 1.1956 -0.3170 -0.2408 0.1900 188 VAL A CG1 1468 C CG2 . VAL A 188 ? 1.2301 0.5833 1.2479 -0.2835 -0.2282 0.1452 188 VAL A CG2 1469 N N . ALA A 189 ? 1.5397 0.8332 1.6619 -0.2888 -0.2606 0.1251 189 ALA A N 1470 C CA . ALA A 189 ? 1.2534 0.5311 1.4066 -0.2991 -0.2742 0.1336 189 ALA A CA 1471 C C . ALA A 189 ? 1.2456 0.5292 1.3926 -0.3067 -0.2648 0.1100 189 ALA A C 1472 O O . ALA A 189 ? 1.3325 0.6224 1.4837 -0.3262 -0.2677 0.1277 189 ALA A O 1473 C CB . ALA A 189 ? 1.4214 0.6637 1.6241 -0.2809 -0.2937 0.1221 189 ALA A CB 1474 N N . GLU A 190 ? 1.2222 0.5062 1.3598 -0.2920 -0.2544 0.0710 190 GLU A N 1475 C CA . GLU A 190 ? 1.2151 0.5091 1.3440 -0.2988 -0.2461 0.0468 190 GLU A CA 1476 C C . GLU A 190 ? 1.2855 0.6139 1.3806 -0.3198 -0.2314 0.0687 190 GLU A C 1477 O O . GLU A 190 ? 1.3000 0.6370 1.4001 -0.3363 -0.2316 0.0739 190 GLU A O 1478 C CB . GLU A 190 ? 1.3736 0.6672 1.4935 -0.2790 -0.2384 0.0032 190 GLU A CB 1479 C CG . GLU A 190 ? 1.6467 0.9115 1.8011 -0.2619 -0.2507 -0.0325 190 GLU A CG 1480 C CD . GLU A 190 ? 1.9023 1.1642 2.0673 -0.2730 -0.2553 -0.0509 190 GLU A CD 1481 O OE1 . GLU A 190 ? 2.0579 1.2931 2.2557 -0.2649 -0.2687 -0.0719 190 GLU A OE1 1482 O OE2 . GLU A 190 ? 1.8223 1.1093 1.9645 -0.2898 -0.2461 -0.0448 190 GLU A OE2 1483 N N . ILE A 191 ? 1.1530 0.5016 1.2155 -0.3191 -0.2187 0.0808 191 ILE A N 1484 C CA . ILE A 191 ? 1.1275 0.5101 1.1562 -0.3364 -0.2024 0.0980 191 ILE A CA 1485 C C . ILE A 191 ? 1.3535 0.7466 1.3871 -0.3589 -0.2069 0.1340 191 ILE A C 1486 O O . ILE A 191 ? 1.6612 1.0780 1.6847 -0.3752 -0.1974 0.1410 191 ILE A O 1487 C CB . ILE A 191 ? 1.1390 0.5372 1.1332 -0.3314 -0.1899 0.1049 191 ILE A CB 1488 C CG1 . ILE A 191 ? 1.1795 0.5696 1.1685 -0.3103 -0.1855 0.0717 191 ILE A CG1 1489 C CG2 . ILE A 191 ? 1.2130 0.6458 1.1731 -0.3483 -0.1717 0.1189 191 ILE A CG2 1490 C CD1 . ILE A 191 ? 1.2082 0.6125 1.1651 -0.3057 -0.1735 0.0768 191 ILE A CD1 1491 N N . VAL A 192 ? 1.1816 0.5592 1.2327 -0.3602 -0.2221 0.1578 192 VAL A N 1492 C CA . VAL A 192 ? 1.2096 0.5986 1.2651 -0.3822 -0.2287 0.1952 192 VAL A CA 1493 C C . VAL A 192 ? 1.4560 0.8316 1.5462 -0.3914 -0.2402 0.1937 192 VAL A C 1494 O O . VAL A 192 ? 1.5990 0.9964 1.6853 -0.4118 -0.2358 0.2120 192 VAL A O 1495 C CB . VAL A 192 ? 1.2364 0.6147 1.3004 -0.3816 -0.2444 0.2241 192 VAL A CB 1496 C CG1 . VAL A 192 ? 1.2813 0.6747 1.3489 -0.4059 -0.2525 0.2645 192 VAL A CG1 1497 C CG2 . VAL A 192 ? 1.4088 0.8021 1.4379 -0.3753 -0.2346 0.2273 192 VAL A CG2 1498 N N . SER A 193 ? 1.3577 0.6983 1.4823 -0.3765 -0.2546 0.1706 193 SER A N 1499 C CA . SER A 193 ? 1.5173 0.8391 1.6784 -0.3846 -0.2690 0.1679 193 SER A CA 1500 C C . SER A 193 ? 1.4787 0.8141 1.6353 -0.3918 -0.2594 0.1441 193 SER A C 1501 O O . SER A 193 ? 1.3100 0.6450 1.4873 -0.4079 -0.2671 0.1526 193 SER A O 1502 C CB . SER A 193 ? 1.4256 0.7053 1.6249 -0.3652 -0.2871 0.1463 193 SER A CB 1503 O OG . SER A 193 ? 1.3070 0.5794 1.4988 -0.3439 -0.2789 0.1030 193 SER A OG 1504 N N . LYS A 194 ? 1.2437 0.5923 1.3750 -0.3807 -0.2440 0.1159 194 LYS A N 1505 C CA . LYS A 194 ? 1.2292 0.5917 1.3575 -0.3856 -0.2372 0.0909 194 LYS A CA 1506 C C . LYS A 194 ? 1.2997 0.7041 1.4013 -0.4031 -0.2199 0.1092 194 LYS A C 1507 O O . LYS A 194 ? 1.4174 0.8390 1.5156 -0.4079 -0.2137 0.0919 194 LYS A O 1508 C CB . LYS A 194 ? 1.2262 0.5815 1.3444 -0.3641 -0.2325 0.0485 194 LYS A CB 1509 C CG . LYS A 194 ? 1.2941 0.6123 1.4426 -0.3480 -0.2484 0.0184 194 LYS A CG 1510 C CD . LYS A 194 ? 1.4160 0.7256 1.5893 -0.3591 -0.2596 0.0027 194 LYS A CD 1511 C CE . LYS A 194 ? 1.7965 1.0664 2.0023 -0.3443 -0.2763 -0.0249 194 LYS A CE 1512 N NZ . LYS A 194 ? 1.9490 1.2124 2.1436 -0.3186 -0.2714 -0.0626 194 LYS A NZ 1513 N N . TYR A 195 ? 1.1950 0.6183 1.2783 -0.4130 -0.2124 0.1434 195 TYR A N 1514 C CA . TYR A 195 ? 1.3390 0.8041 1.3950 -0.4274 -0.1931 0.1578 195 TYR A CA 1515 C C . TYR A 195 ? 1.1875 0.6722 1.2608 -0.4503 -0.1946 0.1761 195 TYR A C 1516 O O . TYR A 195 ? 1.6378 1.1188 1.7272 -0.4635 -0.2050 0.2043 195 TYR A O 1517 C CB . TYR A 195 ? 1.3008 0.7823 1.3268 -0.4304 -0.1833 0.1841 195 TYR A CB 1518 C CG . TYR A 195 ? 1.1710 0.6968 1.1698 -0.4464 -0.1623 0.1991 195 TYR A CG 1519 C CD1 . TYR A 195 ? 1.2353 0.7851 1.2317 -0.4675 -0.1604 0.2332 195 TYR A CD1 1520 C CD2 . TYR A 195 ? 1.1714 0.7167 1.1482 -0.4407 -0.1441 0.1789 195 TYR A CD2 1521 C CE1 . TYR A 195 ? 1.2821 0.8758 1.2549 -0.4815 -0.1390 0.2442 195 TYR A CE1 1522 C CE2 . TYR A 195 ? 1.2926 0.8788 1.2482 -0.4544 -0.1235 0.1905 195 TYR A CE2 1523 C CZ . TYR A 195 ? 1.4554 1.0663 1.4091 -0.4743 -0.1201 0.2218 195 TYR A CZ 1524 O OH . TYR A 195 ? 1.8383 1.4934 1.7720 -0.4871 -0.0973 0.2306 195 TYR A OH 1525 N N . ASP A 196 ? 1.1665 0.6740 1.2381 -0.4555 -0.1851 0.1612 196 ASP A N 1526 C CA . ASP A 196 ? 1.1782 0.7130 1.2651 -0.4776 -0.1832 0.1782 196 ASP A CA 1527 C C . ASP A 196 ? 1.3492 0.9311 1.4093 -0.4857 -0.1586 0.1869 196 ASP A C 1528 O O . ASP A 196 ? 1.2692 0.8619 1.3155 -0.4765 -0.1481 0.1644 196 ASP A O 1529 C CB . ASP A 196 ? 1.1890 0.7117 1.3048 -0.4787 -0.1962 0.1528 196 ASP A CB 1530 C CG . ASP A 196 ? 1.6039 1.1463 1.7456 -0.5025 -0.2009 0.1734 196 ASP A CG 1531 O OD1 . ASP A 196 ? 1.4819 1.0637 1.6135 -0.5175 -0.1860 0.1999 196 ASP A OD1 1532 O OD2 . ASP A 196 ? 1.7519 1.2712 1.9245 -0.5064 -0.2194 0.1619 196 ASP A OD2 1533 N N . PRO A 197 ? 1.1602 0.7721 1.2131 -0.5030 -0.1490 0.2196 197 PRO A N 1534 C CA . PRO A 197 ? 1.3202 0.9799 1.3490 -0.5108 -0.1232 0.2274 197 PRO A CA 1535 C C . PRO A 197 ? 1.3778 1.0659 1.4232 -0.5174 -0.1157 0.2156 197 PRO A C 1536 O O . PRO A 197 ? 1.2017 0.9248 1.2305 -0.5176 -0.0940 0.2119 197 PRO A O 1537 C CB . PRO A 197 ? 1.3136 0.9986 1.3387 -0.5302 -0.1191 0.2646 197 PRO A CB 1538 C CG . PRO A 197 ? 1.2009 0.8574 1.2602 -0.5376 -0.1443 0.2774 197 PRO A CG 1539 C CD . PRO A 197 ? 1.1992 0.8043 1.2675 -0.5169 -0.1620 0.2509 197 PRO A CD 1540 N N . ASN A 198 ? 1.3716 1.0456 1.4511 -0.5230 -0.1340 0.2094 198 ASN A N 1541 C CA . ASN A 198 ? 1.2547 0.9568 1.3536 -0.5311 -0.1310 0.1997 198 ASN A CA 1542 C C . ASN A 198 ? 1.2496 0.9345 1.3474 -0.5156 -0.1381 0.1637 198 ASN A C 1543 O O . ASN A 198 ? 1.4668 1.1751 1.5794 -0.5213 -0.1383 0.1534 198 ASN A O 1544 C CB . ASN A 198 ? 1.3198 1.0216 1.4561 -0.5491 -0.1474 0.2136 198 ASN A CB 1545 C CG . ASN A 198 ? 1.3564 1.0875 1.4949 -0.5679 -0.1387 0.2517 198 ASN A CG 1546 O OD1 . ASN A 198 ? 1.4395 1.2088 1.5551 -0.5709 -0.1154 0.2652 198 ASN A OD1 1547 N ND2 . ASN A 198 ? 1.2208 0.9355 1.3867 -0.5811 -0.1573 0.2686 198 ASN A ND2 1548 N N . VAL A 199 ? 1.2299 0.8773 1.3106 -0.4967 -0.1444 0.1455 199 VAL A N 1549 C CA . VAL A 199 ? 1.2089 0.8415 1.2838 -0.4814 -0.1506 0.1110 199 VAL A CA 1550 C C . VAL A 199 ? 1.0414 0.6801 1.0808 -0.4669 -0.1330 0.1035 199 VAL A C 1551 O O . VAL A 199 ? 1.1864 0.8029 1.2077 -0.4556 -0.1311 0.1062 199 VAL A O 1552 C CB . VAL A 199 ? 1.3477 0.9321 1.4361 -0.4696 -0.1732 0.0896 199 VAL A CB 1553 C CG1 . VAL A 199 ? 1.5102 1.0859 1.5895 -0.4549 -0.1788 0.0524 199 VAL A CG1 1554 C CG2 . VAL A 199 ? 1.1414 0.7161 1.2661 -0.4847 -0.1907 0.0961 199 VAL A CG2 1555 N N . TYR A 200 ? 1.0620 0.7319 1.0937 -0.4679 -0.1209 0.0950 200 TYR A N 1556 C CA . TYR A 200 ? 1.2537 0.9378 1.2553 -0.4498 -0.0999 0.0879 200 TYR A CA 1557 C C . TYR A 200 ? 1.2218 0.8797 1.2087 -0.4242 -0.1069 0.0596 200 TYR A C 1558 O O . TYR A 200 ? 1.2373 0.8922 1.2003 -0.4066 -0.0943 0.0561 200 TYR A O 1559 C CB . TYR A 200 ? 0.9547 0.6919 0.9617 -0.4458 -0.0807 0.0873 200 TYR A CB 1560 C CG . TYR A 200 ? 1.1592 0.9308 1.1828 -0.4692 -0.0701 0.1137 200 TYR A CG 1561 C CD1 . TYR A 200 ? 1.0231 0.7904 1.0370 -0.4845 -0.0636 0.1379 200 TYR A CD1 1562 C CD2 . TYR A 200 ? 1.2441 1.0570 1.2940 -0.4768 -0.0670 0.1159 200 TYR A CD2 1563 C CE1 . TYR A 200 ? 0.9935 0.7990 1.0216 -0.5056 -0.0519 0.1624 200 TYR A CE1 1564 C CE2 . TYR A 200 ? 1.2754 1.1250 1.3436 -0.4980 -0.0558 0.1404 200 TYR A CE2 1565 C CZ . TYR A 200 ? 1.1107 0.9572 1.1672 -0.5129 -0.0475 0.1633 200 TYR A CZ 1566 O OH . TYR A 200 ? 1.1240 1.0140 1.1975 -0.5315 -0.0340 0.1871 200 TYR A OH 1567 N N . SER A 201 ? 1.2498 0.8911 1.2515 -0.4230 -0.1269 0.0386 201 SER A N 1568 C CA . SER A 201 ? 1.1331 0.7532 1.1222 -0.3998 -0.1336 0.0101 201 SER A CA 1569 C C . SER A 201 ? 1.2334 0.8034 1.2383 -0.4047 -0.1585 -0.0002 201 SER A C 1570 O O . SER A 201 ? 1.5169 1.0776 1.5453 -0.4164 -0.1765 -0.0104 201 SER A O 1571 C CB . SER A 201 ? 1.2534 0.9044 1.2421 -0.3892 -0.1335 -0.0123 201 SER A CB 1572 O OG . SER A 201 ? 1.3610 1.0564 1.3419 -0.3832 -0.1120 -0.0014 201 SER A OG 1573 N N . ILE A 202 ? 1.0273 0.5664 1.0226 -0.3937 -0.1594 0.0013 202 ILE A N 1574 C CA . ILE A 202 ? 1.1576 0.6593 1.1758 -0.3875 -0.1767 -0.0054 202 ILE A CA 1575 C C . ILE A 202 ? 1.2054 0.6831 1.2182 -0.3660 -0.1848 -0.0397 202 ILE A C 1576 O O . ILE A 202 ? 1.5296 1.0087 1.5190 -0.3507 -0.1744 -0.0435 202 ILE A O 1577 C CB . ILE A 202 ? 1.2276 0.7178 1.2472 -0.3886 -0.1730 0.0249 202 ILE A CB 1578 C CG1 . ILE A 202 ? 1.1474 0.6633 1.1728 -0.4107 -0.1660 0.0577 202 ILE A CG1 1579 C CG2 . ILE A 202 ? 1.1034 0.5553 1.1491 -0.3798 -0.1906 0.0186 202 ILE A CG2 1580 C CD1 . ILE A 202 ? 1.2723 0.7830 1.2944 -0.4151 -0.1637 0.0889 202 ILE A CD1 1581 N N . LYS A 203 ? 1.4076 0.8683 1.4428 -0.3631 -0.2013 -0.0659 203 LYS A N 1582 C CA . LYS A 203 ? 1.4757 0.9149 1.5097 -0.3419 -0.2089 -0.1020 203 LYS A CA 1583 C C . LYS A 203 ? 1.3994 0.8047 1.4525 -0.3297 -0.2137 -0.0952 203 LYS A C 1584 O O . LYS A 203 ? 1.1611 0.5475 1.2429 -0.3373 -0.2236 -0.0837 203 LYS A O 1585 C CB . LYS A 203 ? 1.4828 0.9208 1.5312 -0.3434 -0.2235 -0.1375 203 LYS A CB 1586 C CG . LYS A 203 ? 1.5525 0.9729 1.5997 -0.3205 -0.2300 -0.1801 203 LYS A CG 1587 C CD . LYS A 203 ? 1.8398 1.2625 1.8985 -0.3234 -0.2435 -0.2173 203 LYS A CD 1588 C CE . LYS A 203 ? 1.9013 1.3124 1.9563 -0.2991 -0.2469 -0.2630 203 LYS A CE 1589 N NZ . LYS A 203 ? 1.7354 1.1085 1.8141 -0.2840 -0.2477 -0.2595 203 LYS A NZ 1590 N N . TYR A 204 ? 1.5103 0.9085 1.5480 -0.3117 -0.2076 -0.1006 204 TYR A N 1591 C CA . TYR A 204 ? 1.5790 0.9481 1.6355 -0.2987 -0.2129 -0.0939 204 TYR A CA 1592 C C . TYR A 204 ? 1.6811 1.0301 1.7516 -0.2767 -0.2214 -0.1355 204 TYR A C 1593 O O . TYR A 204 ? 1.7714 1.1325 1.8218 -0.2630 -0.2166 -0.1633 204 TYR A O 1594 C CB . TYR A 204 ? 1.3656 0.7415 1.3997 -0.2938 -0.2012 -0.0694 204 TYR A CB 1595 C CG . TYR A 204 ? 1.3684 0.7638 1.3892 -0.3134 -0.1917 -0.0292 204 TYR A CG 1596 C CD1 . TYR A 204 ? 1.3404 0.7662 1.3307 -0.3224 -0.1765 -0.0226 204 TYR A CD1 1597 C CD2 . TYR A 204 ? 1.4122 0.7974 1.4502 -0.3229 -0.1978 0.0017 204 TYR A CD2 1598 C CE1 . TYR A 204 ? 1.2571 0.7035 1.2357 -0.3389 -0.1658 0.0100 204 TYR A CE1 1599 C CE2 . TYR A 204 ? 1.6201 1.0277 1.6432 -0.3407 -0.1886 0.0358 204 TYR A CE2 1600 C CZ . TYR A 204 ? 1.5113 0.9498 1.5050 -0.3480 -0.1717 0.0381 204 TYR A CZ 1601 O OH . TYR A 204 ? 1.6066 1.0694 1.5857 -0.3648 -0.1607 0.0684 204 TYR A OH 1602 N N . ASN A 205 ? 1.4805 0.8001 1.5853 -0.2730 -0.2342 -0.1399 205 ASN A N 1603 C CA . ASN A 205 ? 1.3899 0.6891 1.5119 -0.2498 -0.2409 -0.1785 205 ASN A CA 1604 C C . ASN A 205 ? 1.4174 0.7105 1.5381 -0.2299 -0.2360 -0.1732 205 ASN A C 1605 O O . ASN A 205 ? 1.3768 0.6702 1.4930 -0.2364 -0.2329 -0.1345 205 ASN A O 1606 C CB . ASN A 205 ? 1.4531 0.7197 1.6147 -0.2518 -0.2568 -0.1821 205 ASN A CB 1607 C CG . ASN A 205 ? 1.7889 1.0604 1.9545 -0.2704 -0.2635 -0.1934 205 ASN A CG 1608 O OD1 . ASN A 205 ? 1.9322 1.2298 2.0742 -0.2742 -0.2583 -0.2164 205 ASN A OD1 1609 N ND2 . ASN A 205 ? 1.7831 1.0307 1.9800 -0.2830 -0.2767 -0.1762 205 ASN A ND2 1610 N N . ASN A 206 ? 1.6092 0.9004 1.7338 -0.2057 -0.2353 -0.2130 206 ASN A N 1611 C CA . ASN A 206 ? 1.5756 0.8659 1.7013 -0.1848 -0.2303 -0.2137 206 ASN A CA 1612 C C . ASN A 206 ? 1.3765 0.6919 1.4650 -0.1916 -0.2177 -0.1899 206 ASN A C 1613 O O . ASN A 206 ? 1.3356 0.6487 1.4239 -0.1893 -0.2147 -0.1607 206 ASN A O 1614 C CB . ASN A 206 ? 1.4389 0.6993 1.6006 -0.1798 -0.2407 -0.1875 206 ASN A CB 1615 C CG . ASN A 206 ? 1.6441 0.8759 1.8453 -0.1735 -0.2547 -0.2073 206 ASN A CG 1616 O OD1 . ASN A 206 ? 1.8396 1.0507 2.0639 -0.1868 -0.2664 -0.1788 206 ASN A OD1 1617 N ND2 . ASN A 206 ? 1.7289 0.9617 1.9380 -0.1531 -0.2535 -0.2570 206 ASN A ND2 1618 N N . GLN A 207 ? 1.3867 0.7428 1.4410 -0.1971 -0.2033 -0.1978 207 GLN A N 1619 C CA . GLN A 207 ? 1.2723 0.6704 1.2895 -0.1985 -0.1820 -0.1741 207 GLN A CA 1620 C C . GLN A 207 ? 1.3446 0.7826 1.3437 -0.1742 -0.1648 -0.1980 207 GLN A C 1621 O O . GLN A 207 ? 1.5498 1.0120 1.5389 -0.1674 -0.1609 -0.2292 207 GLN A O 1622 C CB . GLN A 207 ? 1.2663 0.6870 1.2617 -0.2200 -0.1765 -0.1612 207 GLN A CB 1623 C CG . GLN A 207 ? 1.3099 0.7702 1.2727 -0.2211 -0.1552 -0.1377 207 GLN A CG 1624 C CD . GLN A 207 ? 1.4340 0.9181 1.3817 -0.2398 -0.1494 -0.1259 207 GLN A CD 1625 O OE1 . GLN A 207 ? 1.7484 1.2565 1.6896 -0.2389 -0.1480 -0.1465 207 GLN A OE1 1626 N NE2 . GLN A 207 ? 1.1230 0.6045 1.0658 -0.2570 -0.1458 -0.0927 207 GLN A NE2 1627 N N . LEU A 208 ? 1.3728 0.8204 1.3675 -0.1627 -0.1551 -0.1816 208 LEU A N 1628 C CA . LEU A 208 ? 1.3484 0.8375 1.3278 -0.1418 -0.1380 -0.1971 208 LEU A CA 1629 C C . LEU A 208 ? 1.3731 0.9015 1.3186 -0.1495 -0.1205 -0.1751 208 LEU A C 1630 O O . LEU A 208 ? 1.6308 1.1555 1.5689 -0.1581 -0.1165 -0.1438 208 LEU A O 1631 C CB . LEU A 208 ? 1.2903 0.7698 1.2901 -0.1242 -0.1384 -0.1929 208 LEU A CB 1632 C CG . LEU A 208 ? 1.0896 0.5290 1.1312 -0.1127 -0.1559 -0.2140 208 LEU A CG 1633 C CD1 . LEU A 208 ? 1.1194 0.5510 1.1839 -0.0981 -0.1575 -0.2002 208 LEU A CD1 1634 C CD2 . LEU A 208 ? 1.1266 0.5810 1.1731 -0.0960 -0.1534 -0.2629 208 LEU A CD2 1635 N N . ALA A 209 ? 1.2845 0.8511 1.2107 -0.1466 -0.1109 -0.1920 209 ALA A N 1636 C CA . ALA A 209 ? 1.1428 0.7461 1.0430 -0.1531 -0.0959 -0.1716 209 ALA A CA 1637 C C . ALA A 209 ? 1.0618 0.7148 0.9459 -0.1394 -0.0835 -0.1887 209 ALA A C 1638 O O . ALA A 209 ? 1.1436 0.8087 1.0273 -0.1331 -0.0874 -0.2196 209 ALA A O 1639 C CB . ALA A 209 ? 0.9927 0.5915 0.8866 -0.1745 -0.1002 -0.1597 209 ALA A CB 1640 N N . THR A 210 ? 1.0442 0.7270 0.9152 -0.1360 -0.0691 -0.1683 210 THR A N 1641 C CA . THR A 210 ? 1.0666 0.8016 0.9217 -0.1271 -0.0572 -0.1749 210 THR A CA 1642 C C . THR A 210 ? 1.0917 0.8473 0.9331 -0.1401 -0.0580 -0.1717 210 THR A C 1643 O O . THR A 210 ? 1.2607 0.9944 1.1049 -0.1555 -0.0630 -0.1569 210 THR A O 1644 C CB . THR A 210 ? 1.0644 0.8223 0.9152 -0.1215 -0.0436 -0.1500 210 THR A CB 1645 O OG1 . THR A 210 ? 1.0776 0.8249 0.9240 -0.1357 -0.0411 -0.1215 210 THR A OG1 1646 C CG2 . THR A 210 ? 1.0755 0.8145 0.9426 -0.1103 -0.0443 -0.1500 210 THR A CG2 1647 N N . ARG A 211 ? 1.0860 0.8877 0.9131 -0.1345 -0.0531 -0.1841 211 ARG A N 1648 C CA . ARG A 211 ? 1.1963 1.0227 1.0124 -0.1465 -0.0560 -0.1807 211 ARG A CA 1649 C C . ARG A 211 ? 1.1459 1.0264 0.9485 -0.1428 -0.0443 -0.1628 211 ARG A C 1650 O O . ARG A 211 ? 1.1058 1.0068 0.9063 -0.1310 -0.0340 -0.1571 211 ARG A O 1651 C CB . ARG A 211 ? 1.2691 1.0979 1.0817 -0.1482 -0.0683 -0.2166 211 ARG A CB 1652 C CG . ARG A 211 ? 1.5257 1.3950 1.3244 -0.1333 -0.0636 -0.2448 211 ARG A CG 1653 C CD . ARG A 211 ? 1.8396 1.7060 1.6351 -0.1365 -0.0773 -0.2848 211 ARG A CD 1654 N NE . ARG A 211 ? 1.9340 1.8531 1.7084 -0.1255 -0.0718 -0.3122 211 ARG A NE 1655 C CZ . ARG A 211 ? 1.9543 1.8827 1.7198 -0.1267 -0.0820 -0.3525 211 ARG A CZ 1656 N NH1 . ARG A 211 ? 1.8153 1.7002 1.5950 -0.1390 -0.0997 -0.3684 211 ARG A NH1 1657 N NH2 . ARG A 211 ? 1.9588 1.9418 1.7010 -0.1167 -0.0749 -0.3771 211 ARG A NH2 1658 N N . THR A 212 ? 1.1485 1.0527 0.9456 -0.1536 -0.0468 -0.1511 212 THR A N 1659 C CA . THR A 212 ? 1.0973 1.0487 0.8878 -0.1527 -0.0381 -0.1259 212 THR A CA 1660 C C . THR A 212 ? 1.1177 1.1188 0.8925 -0.1414 -0.0321 -0.1359 212 THR A C 1661 O O . THR A 212 ? 1.2172 1.2292 0.9806 -0.1365 -0.0365 -0.1687 212 THR A O 1662 C CB . THR A 212 ? 1.0998 1.0723 0.8905 -0.1656 -0.0450 -0.1154 212 THR A CB 1663 O OG1 . THR A 212 ? 1.2292 1.2474 1.0183 -0.1639 -0.0383 -0.0880 212 THR A OG1 1664 C CG2 . THR A 212 ? 1.1066 1.0941 0.8848 -0.1703 -0.0578 -0.1466 212 THR A CG2 1665 N N . ALA A 213 ? 1.1257 1.1576 0.9016 -0.1376 -0.0217 -0.1074 213 ALA A N 1666 C CA . ALA A 213 ? 1.1243 1.2098 0.8868 -0.1285 -0.0139 -0.1086 213 ALA A CA 1667 C C . ALA A 213 ? 1.1210 1.2574 0.8794 -0.1347 -0.0128 -0.0774 213 ALA A C 1668 O O . ALA A 213 ? 1.1125 1.2422 0.8794 -0.1447 -0.0191 -0.0607 213 ALA A O 1669 C CB . ALA A 213 ? 1.1316 1.2083 0.9045 -0.1177 -0.0030 -0.1005 213 ALA A CB 1670 N N . GLN A 214 ? 1.1254 1.3154 0.8735 -0.1291 -0.0049 -0.0681 214 GLN A N 1671 C CA . GLN A 214 ? 1.1115 1.3541 0.8580 -0.1353 -0.0049 -0.0333 214 GLN A CA 1672 C C . GLN A 214 ? 1.1070 1.3236 0.8822 -0.1395 -0.0033 0.0057 214 GLN A C 1673 O O . GLN A 214 ? 1.1141 1.2864 0.9053 -0.1358 0.0021 0.0089 214 GLN A O 1674 C CB . GLN A 214 ? 1.1071 1.4114 0.8400 -0.1292 0.0050 -0.0261 214 GLN A CB 1675 C CG . GLN A 214 ? 1.1429 1.4868 0.8448 -0.1247 0.0051 -0.0658 214 GLN A CG 1676 C CD . GLN A 214 ? 1.3213 1.6330 1.0242 -0.1115 0.0115 -0.1047 214 GLN A CD 1677 O OE1 . GLN A 214 ? 1.3219 1.5766 1.0470 -0.1077 0.0127 -0.1028 214 GLN A OE1 1678 N NE2 . GLN A 214 ? 1.3716 1.7220 1.0516 -0.1041 0.0152 -0.1407 214 GLN A NE2 1679 N N . ALA A 215 ? 1.0835 1.3288 0.8662 -0.1472 -0.0089 0.0346 215 ALA A N 1680 C CA . ALA A 215 ? 1.0646 1.2865 0.8787 -0.1502 -0.0082 0.0688 215 ALA A CA 1681 C C . ALA A 215 ? 1.0397 1.2630 0.8705 -0.1456 0.0012 0.0951 215 ALA A C 1682 O O . ALA A 215 ? 1.0129 1.2076 0.8718 -0.1467 0.0027 0.1177 215 ALA A O 1683 C CB . ALA A 215 ? 1.0983 1.3577 0.9213 -0.1577 -0.0173 0.0949 215 ALA A CB 1684 N N . ILE A 216 ? 1.1027 1.3607 0.9181 -0.1408 0.0075 0.0907 216 ILE A N 1685 C CA . ILE A 216 ? 1.0163 1.2802 0.8484 -0.1378 0.0159 0.1152 216 ILE A CA 1686 C C . ILE A 216 ? 1.0160 1.2159 0.8631 -0.1341 0.0199 0.1041 216 ILE A C 1687 O O . ILE A 216 ? 1.1468 1.3338 1.0165 -0.1346 0.0236 0.1273 216 ILE A O 1688 C CB . ILE A 216 ? 1.0225 1.3417 0.8342 -0.1330 0.0236 0.1087 216 ILE A CB 1689 C CG1 . ILE A 216 ? 1.2874 1.6674 1.0704 -0.1365 0.0190 0.1018 216 ILE A CG1 1690 C CG2 . ILE A 216 ? 0.9867 1.3317 0.8196 -0.1343 0.0300 0.1475 216 ILE A CG2 1691 C CD1 . ILE A 216 ? 1.5091 1.9312 1.3025 -0.1461 0.0120 0.1456 216 ILE A CD1 1692 N N . PHE A 217 ? 1.0419 1.2022 0.8768 -0.1317 0.0176 0.0694 217 PHE A N 1693 C CA . PHE A 217 ? 1.0437 1.1470 0.8880 -0.1293 0.0196 0.0574 217 PHE A CA 1694 C C . PHE A 217 ? 1.0305 1.0873 0.8900 -0.1356 0.0161 0.0642 217 PHE A C 1695 O O . PHE A 217 ? 1.0314 1.0414 0.8949 -0.1359 0.0167 0.0539 217 PHE A O 1696 C CB . PHE A 217 ? 1.0828 1.1685 0.9096 -0.1234 0.0182 0.0188 217 PHE A CB 1697 C CG . PHE A 217 ? 1.0976 1.2274 0.9117 -0.1146 0.0239 0.0056 217 PHE A CG 1698 C CD1 . PHE A 217 ? 1.1021 1.2326 0.9265 -0.1075 0.0311 0.0084 217 PHE A CD1 1699 C CD2 . PHE A 217 ? 1.1041 1.2781 0.8965 -0.1135 0.0223 -0.0110 217 PHE A CD2 1700 C CE1 . PHE A 217 ? 1.1136 1.2896 0.9291 -0.0981 0.0385 -0.0048 217 PHE A CE1 1701 C CE2 . PHE A 217 ? 1.1151 1.3342 0.8945 -0.1045 0.0297 -0.0267 217 PHE A CE2 1702 C CZ . PHE A 217 ? 1.1193 1.3402 0.9114 -0.0961 0.0388 -0.0235 217 PHE A CZ 1703 N N . ASP A 218 ? 1.0250 1.0983 0.8932 -0.1407 0.0126 0.0815 218 ASP A N 1704 C CA . ASP A 218 ? 0.9932 1.0303 0.8791 -0.1453 0.0112 0.0874 218 ASP A CA 1705 C C . ASP A 218 ? 0.9521 0.9558 0.8590 -0.1450 0.0165 0.1007 218 ASP A C 1706 O O . ASP A 218 ? 1.0596 1.0788 0.9774 -0.1431 0.0192 0.1194 218 ASP A O 1707 C CB . ASP A 218 ? 0.9913 1.0601 0.8907 -0.1488 0.0065 0.1085 218 ASP A CB 1708 C CG . ASP A 218 ? 1.1720 1.2611 1.0528 -0.1525 -0.0011 0.0910 218 ASP A CG 1709 O OD1 . ASP A 218 ? 1.2420 1.3490 1.1358 -0.1565 -0.0066 0.1048 218 ASP A OD1 1710 O OD2 . ASP A 218 ? 1.1728 1.2592 1.0291 -0.1514 -0.0027 0.0630 218 ASP A OD2 1711 N N . ASP A 219 ? 0.9697 0.9297 0.8815 -0.1480 0.0177 0.0904 219 ASP A N 1712 C CA . ASP A 219 ? 0.9205 0.8460 0.8492 -0.1490 0.0222 0.0973 219 ASP A CA 1713 C C . ASP A 219 ? 0.8962 0.8101 0.8182 -0.1473 0.0235 0.0934 219 ASP A C 1714 O O . ASP A 219 ? 1.0714 0.9739 1.0106 -0.1482 0.0254 0.1065 219 ASP A O 1715 C CB . ASP A 219 ? 0.8701 0.8090 0.8304 -0.1483 0.0232 0.1250 219 ASP A CB 1716 C CG . ASP A 219 ? 0.8825 0.8392 0.8551 -0.1488 0.0208 0.1324 219 ASP A CG 1717 O OD1 . ASP A 219 ? 1.0351 0.9666 1.0154 -0.1503 0.0237 0.1226 219 ASP A OD1 1718 O OD2 . ASP A 219 ? 0.9150 0.9148 0.8898 -0.1480 0.0160 0.1488 219 ASP A OD2 1719 N N . SER A 220 ? 0.9223 0.8394 0.8229 -0.1447 0.0215 0.0750 220 SER A N 1720 C CA . SER A 220 ? 0.9163 0.8236 0.8133 -0.1419 0.0221 0.0697 220 SER A CA 1721 C C . SER A 220 ? 0.9880 0.8469 0.8809 -0.1465 0.0204 0.0576 220 SER A C 1722 O O . SER A 220 ? 1.0515 0.8968 0.9492 -0.1469 0.0199 0.0605 220 SER A O 1723 C CB . SER A 220 ? 0.9710 0.9026 0.8516 -0.1351 0.0209 0.0532 220 SER A CB 1724 O OG . SER A 220 ? 1.0052 0.9883 0.8852 -0.1320 0.0231 0.0643 220 SER A OG 1725 N N . TYR A 221 ? 0.8952 0.7322 0.7797 -0.1512 0.0189 0.0460 221 TYR A N 1726 C CA . TYR A 221 ? 0.9410 0.7374 0.8175 -0.1577 0.0172 0.0358 221 TYR A CA 1727 C C . TYR A 221 ? 1.0688 0.8512 0.9346 -0.1557 0.0112 0.0236 221 TYR A C 1728 O O . TYR A 221 ? 1.0676 0.8280 0.9330 -0.1589 0.0090 0.0251 221 TYR A O 1729 C CB . TYR A 221 ? 0.8118 0.5892 0.6989 -0.1622 0.0206 0.0453 221 TYR A CB 1730 C CG . TYR A 221 ? 0.8053 0.5851 0.7077 -0.1640 0.0265 0.0533 221 TYR A CG 1731 C CD1 . TYR A 221 ? 0.8449 0.6069 0.7606 -0.1670 0.0299 0.0580 221 TYR A CD1 1732 C CD2 . TYR A 221 ? 0.8843 0.6842 0.7907 -0.1623 0.0277 0.0549 221 TYR A CD2 1733 C CE1 . TYR A 221 ? 0.8441 0.6068 0.7796 -0.1663 0.0355 0.0632 221 TYR A CE1 1734 C CE2 . TYR A 221 ? 1.1063 0.9098 1.0327 -0.1623 0.0326 0.0633 221 TYR A CE2 1735 C CZ . TYR A 221 ? 1.0395 0.8236 0.9818 -0.1633 0.0371 0.0669 221 TYR A CZ 1736 O OH . TYR A 221 ? 1.2900 1.0764 1.2578 -0.1610 0.0423 0.0731 221 TYR A OH 1737 N N . LEU A 222 ? 0.9254 0.7208 0.7845 -0.1502 0.0075 0.0109 222 LEU A N 1738 C CA . LEU A 222 ? 0.9200 0.6984 0.7747 -0.1469 0.0007 -0.0027 222 LEU A CA 1739 C C . LEU A 222 ? 0.9575 0.6969 0.8053 -0.1570 -0.0052 -0.0071 222 LEU A C 1740 O O . LEU A 222 ? 1.1658 0.8993 1.0088 -0.1642 -0.0052 -0.0097 222 LEU A O 1741 C CB . LEU A 222 ? 1.0694 0.8692 0.9207 -0.1383 -0.0017 -0.0199 222 LEU A CB 1742 C CG . LEU A 222 ? 0.9816 0.7584 0.8337 -0.1339 -0.0103 -0.0383 222 LEU A CG 1743 C CD1 . LEU A 222 ? 0.9880 0.7615 0.8508 -0.1268 -0.0109 -0.0343 222 LEU A CD1 1744 C CD2 . LEU A 222 ? 1.0237 0.8211 0.8725 -0.1260 -0.0122 -0.0605 222 LEU A CD2 1745 N N . GLY A 223 ? 1.1222 0.8388 0.9705 -0.1586 -0.0107 -0.0056 223 GLY A N 1746 C CA . GLY A 223 ? 1.1316 0.8151 0.9721 -0.1700 -0.0174 -0.0053 223 GLY A CA 1747 C C . GLY A 223 ? 1.1235 0.7954 0.9572 -0.1806 -0.0131 0.0059 223 GLY A C 1748 O O . GLY A 223 ? 1.1643 0.8163 0.9875 -0.1924 -0.0154 0.0077 223 GLY A O 1749 N N . TYR A 224 ? 1.0080 0.6937 0.8482 -0.1772 -0.0070 0.0132 224 TYR A N 1750 C CA . TYR A 224 ? 0.7806 0.4544 0.6165 -0.1862 -0.0036 0.0196 224 TYR A CA 1751 C C . TYR A 224 ? 0.8717 0.5233 0.6978 -0.1940 -0.0132 0.0217 224 TYR A C 1752 O O . TYR A 224 ? 1.0022 0.6385 0.8140 -0.2062 -0.0130 0.0223 224 TYR A O 1753 C CB . TYR A 224 ? 0.8298 0.5202 0.6806 -0.1810 0.0016 0.0276 224 TYR A CB 1754 C CG . TYR A 224 ? 0.9054 0.5849 0.7569 -0.1888 0.0071 0.0298 224 TYR A CG 1755 C CD1 . TYR A 224 ? 0.7604 0.4500 0.6236 -0.1865 0.0161 0.0318 224 TYR A CD1 1756 C CD2 . TYR A 224 ? 0.8575 0.5175 0.6998 -0.1981 0.0025 0.0288 224 TYR A CD2 1757 C CE1 . TYR A 224 ? 0.7539 0.4316 0.6226 -0.1915 0.0215 0.0301 224 TYR A CE1 1758 C CE2 . TYR A 224 ? 0.8731 0.5227 0.7156 -0.2049 0.0078 0.0255 224 TYR A CE2 1759 C CZ . TYR A 224 ? 0.9072 0.5644 0.7645 -0.2007 0.0178 0.0249 224 TYR A CZ 1760 O OH . TYR A 224 ? 1.0194 0.6644 0.8815 -0.2054 0.0234 0.0181 224 TYR A OH 1761 N N . SER A 225 ? 0.8388 0.4926 0.6737 -0.1869 -0.0216 0.0231 225 SER A N 1762 C CA . SER A 225 ? 0.9709 0.6066 0.8017 -0.1929 -0.0338 0.0279 225 SER A CA 1763 C C . SER A 225 ? 1.1353 0.7696 0.9787 -0.1826 -0.0428 0.0239 225 SER A C 1764 O O . SER A 225 ? 0.9999 0.6534 0.8560 -0.1691 -0.0384 0.0163 225 SER A O 1765 C CB . SER A 225 ? 1.0755 0.7155 0.9121 -0.1948 -0.0365 0.0358 225 SER A CB 1766 O OG . SER A 225 ? 1.1527 0.8166 1.0099 -0.1818 -0.0332 0.0374 225 SER A OG 1767 N N . VAL A 226 ? 1.2127 0.8256 1.0538 -0.1891 -0.0556 0.0288 226 VAL A N 1768 C CA . VAL A 226 ? 1.0929 0.6990 0.9521 -0.1786 -0.0658 0.0242 226 VAL A CA 1769 C C . VAL A 226 ? 1.0930 0.6871 0.9628 -0.1803 -0.0810 0.0363 226 VAL A C 1770 O O . VAL A 226 ? 1.2817 0.8669 1.1370 -0.1949 -0.0866 0.0495 226 VAL A O 1771 C CB . VAL A 226 ? 0.9892 0.5769 0.8444 -0.1838 -0.0699 0.0185 226 VAL A CB 1772 C CG1 . VAL A 226 ? 0.8749 0.4786 0.7255 -0.1798 -0.0575 0.0053 226 VAL A CG1 1773 C CG2 . VAL A 226 ? 0.8341 0.4026 0.6703 -0.2042 -0.0752 0.0324 226 VAL A CG2 1774 N N . ALA A 227 ? 0.8918 0.4881 0.7880 -0.1647 -0.0878 0.0309 227 ALA A N 1775 C CA . ALA A 227 ? 0.9227 0.5088 0.8379 -0.1631 -0.1041 0.0430 227 ALA A CA 1776 C C . ALA A 227 ? 1.0547 0.6333 1.0008 -0.1458 -0.1113 0.0309 227 ALA A C 1777 O O . ALA A 227 ? 1.0443 0.6335 0.9954 -0.1333 -0.1014 0.0104 227 ALA A O 1778 C CB . ALA A 227 ? 0.9600 0.5690 0.8845 -0.1595 -0.1027 0.0508 227 ALA A CB 1779 N N . VAL A 228 ? 1.1072 0.6678 1.0750 -0.1449 -0.1292 0.0429 228 VAL A N 1780 C CA . VAL A 228 ? 1.0127 0.5604 1.0161 -0.1276 -0.1379 0.0303 228 VAL A CA 1781 C C . VAL A 228 ? 1.0879 0.6430 1.1295 -0.1133 -0.1489 0.0378 228 VAL A C 1782 O O . VAL A 228 ? 1.1992 0.7559 1.2397 -0.1235 -0.1592 0.0613 228 VAL A O 1783 C CB . VAL A 228 ? 0.9681 0.4775 0.9726 -0.1397 -0.1530 0.0375 228 VAL A CB 1784 C CG1 . VAL A 228 ? 0.9554 0.4609 0.9345 -0.1481 -0.1419 0.0238 228 VAL A CG1 1785 C CG2 . VAL A 228 ? 1.2158 0.7112 1.2065 -0.1614 -0.1677 0.0695 228 VAL A CG2 1786 N N . GLY A 229 ? 1.0526 0.6146 1.1285 -0.0895 -0.1465 0.0161 229 GLY A N 1787 C CA . GLY A 229 ? 1.0857 0.6581 1.2062 -0.0712 -0.1549 0.0187 229 GLY A CA 1788 C C . GLY A 229 ? 1.1340 0.7167 1.2857 -0.0441 -0.1464 -0.0150 229 GLY A C 1789 O O . GLY A 229 ? 1.3212 0.9140 1.4531 -0.0406 -0.1312 -0.0392 229 GLY A O 1790 N N . ASP A 230 ? 1.1569 0.7396 1.3581 -0.0243 -0.1559 -0.0180 230 ASP A N 1791 C CA . ASP A 230 ? 1.2017 0.7930 1.4352 0.0032 -0.1477 -0.0552 230 ASP A CA 1792 C C . ASP A 230 ? 1.2452 0.8907 1.4998 0.0247 -0.1308 -0.0672 230 ASP A C 1793 O O . ASP A 230 ? 1.2723 0.9305 1.5652 0.0347 -0.1384 -0.0531 230 ASP A O 1794 C CB . ASP A 230 ? 1.3130 0.8624 1.5955 0.0141 -0.1696 -0.0574 230 ASP A CB 1795 C CG . ASP A 230 ? 1.3858 0.9445 1.7093 0.0457 -0.1617 -0.0994 230 ASP A CG 1796 O OD1 . ASP A 230 ? 1.3407 0.9207 1.7101 0.0675 -0.1621 -0.1017 230 ASP A OD1 1797 O OD2 . ASP A 230 ? 1.6029 1.1499 1.9139 0.0489 -0.1552 -0.1313 230 ASP A OD2 1798 N N . PHE A 231 ? 1.2714 0.9518 1.5014 0.0305 -0.1082 -0.0915 231 PHE A N 1799 C CA . PHE A 231 ? 1.3321 1.0723 1.5736 0.0469 -0.0885 -0.1011 231 PHE A CA 1800 C C . PHE A 231 ? 1.3588 1.1217 1.6334 0.0776 -0.0772 -0.1427 231 PHE A C 1801 O O . PHE A 231 ? 1.4116 1.2307 1.6965 0.0927 -0.0585 -0.1534 231 PHE A O 1802 C CB . PHE A 231 ? 1.3495 1.1203 1.5417 0.0313 -0.0710 -0.0953 231 PHE A CB 1803 C CG . PHE A 231 ? 1.2994 1.0489 1.4615 0.0033 -0.0803 -0.0602 231 PHE A CG 1804 C CD1 . PHE A 231 ? 1.3131 1.0827 1.4838 -0.0037 -0.0828 -0.0327 231 PHE A CD1 1805 C CD2 . PHE A 231 ? 1.2356 0.9463 1.3632 -0.0160 -0.0870 -0.0563 231 PHE A CD2 1806 C CE1 . PHE A 231 ? 1.2544 1.0043 1.3971 -0.0290 -0.0915 -0.0053 231 PHE A CE1 1807 C CE2 . PHE A 231 ? 1.2494 0.9435 1.3498 -0.0403 -0.0938 -0.0278 231 PHE A CE2 1808 C CZ . PHE A 231 ? 1.2528 0.9659 1.3597 -0.0464 -0.0960 -0.0040 231 PHE A CZ 1809 N N . ASN A 232 ? 1.4641 1.1846 1.7560 0.0860 -0.0884 -0.1666 232 ASN A N 1810 C CA . ASN A 232 ? 1.4539 1.1892 1.7788 0.1156 -0.0794 -0.2120 232 ASN A CA 1811 C C . ASN A 232 ? 1.3689 1.0680 1.7580 0.1339 -0.0988 -0.2158 232 ASN A C 1812 O O . ASN A 232 ? 1.3791 1.0471 1.7860 0.1229 -0.1195 -0.1791 232 ASN A O 1813 C CB . ASN A 232 ? 1.3565 1.0762 1.6495 0.1122 -0.0747 -0.2466 232 ASN A CB 1814 C CG . ASN A 232 ? 1.3252 0.9839 1.5965 0.0867 -0.0946 -0.2282 232 ASN A CG 1815 O OD1 . ASN A 232 ? 1.4547 1.0816 1.7354 0.0731 -0.1122 -0.1917 232 ASN A OD1 1816 N ND2 . ASN A 232 ? 1.3163 0.9621 1.5577 0.0790 -0.0922 -0.2523 232 ASN A ND2 1817 N N . GLY A 233 ? 1.3935 1.0978 1.8176 0.1619 -0.0924 -0.2609 233 GLY A N 1818 C CA . GLY A 233 ? 1.5650 1.2381 2.0594 0.1846 -0.1091 -0.2701 233 GLY A CA 1819 C C . GLY A 233 ? 1.7781 1.3735 2.2875 0.1707 -0.1394 -0.2544 233 GLY A C 1820 O O . GLY A 233 ? 1.9148 1.4800 2.4813 0.1808 -0.1599 -0.2393 233 GLY A O 1821 N N . ASP A 234 ? 1.7784 1.3438 2.2392 0.1467 -0.1431 -0.2549 234 ASP A N 1822 C CA . ASP A 234 ? 1.5554 1.0503 2.0279 0.1306 -0.1707 -0.2396 234 ASP A CA 1823 C C . ASP A 234 ? 1.3766 0.8511 1.8443 0.1065 -0.1901 -0.1802 234 ASP A C 1824 O O . ASP A 234 ? 1.2885 0.8005 1.7459 0.1032 -0.1833 -0.1538 234 ASP A O 1825 C CB . ASP A 234 ? 1.3526 0.8287 1.7753 0.1111 -0.1676 -0.2574 234 ASP A CB 1826 C CG . ASP A 234 ? 1.5756 1.0933 1.9290 0.0903 -0.1484 -0.2422 234 ASP A CG 1827 O OD1 . ASP A 234 ? 1.7845 1.3145 2.1195 0.0747 -0.1495 -0.2003 234 ASP A OD1 1828 O OD2 . ASP A 234 ? 1.6443 1.1823 1.9630 0.0894 -0.1332 -0.2730 234 ASP A OD2 1829 N N . GLY A 235 ? 1.3334 0.7500 1.8089 0.0887 -0.2149 -0.1593 235 GLY A N 1830 C CA . GLY A 235 ? 1.3420 0.7402 1.8097 0.0638 -0.2345 -0.1037 235 GLY A CA 1831 C C . GLY A 235 ? 1.4373 0.8262 1.8390 0.0289 -0.2329 -0.0824 235 GLY A C 1832 O O . GLY A 235 ? 1.7601 1.1381 2.1443 0.0051 -0.2463 -0.0386 235 GLY A O 1833 N N . ILE A 236 ? 1.3878 0.7844 1.7533 0.0260 -0.2162 -0.1141 236 ILE A N 1834 C CA . ILE A 236 ? 1.4179 0.8066 1.7266 -0.0047 -0.2135 -0.0985 236 ILE A CA 1835 C C . ILE A 236 ? 1.3718 0.8077 1.6291 -0.0152 -0.1931 -0.0851 236 ILE A C 1836 O O . ILE A 236 ? 1.1888 0.6683 1.4399 0.0013 -0.1729 -0.1071 236 ILE A O 1837 C CB . ILE A 236 ? 1.4732 0.8487 1.7690 -0.0048 -0.2075 -0.1367 236 ILE A CB 1838 C CG1 . ILE A 236 ? 1.2986 0.6245 1.6508 0.0071 -0.2282 -0.1558 236 ILE A CG1 1839 C CG2 . ILE A 236 ? 1.5900 0.9572 1.8347 -0.0366 -0.2065 -0.1173 236 ILE A CG2 1840 C CD1 . ILE A 236 ? 1.3364 0.6771 1.7254 0.0418 -0.2184 -0.2069 236 ILE A CD1 1841 N N . ASP A 237 ? 1.5999 1.0278 1.8222 -0.0430 -0.1988 -0.0488 237 ASP A N 1842 C CA . ASP A 237 ? 1.2799 0.7448 1.4546 -0.0557 -0.1816 -0.0362 237 ASP A CA 1843 C C . ASP A 237 ? 1.1204 0.6102 1.2622 -0.0535 -0.1596 -0.0656 237 ASP A C 1844 O O . ASP A 237 ? 1.1521 0.6219 1.2844 -0.0600 -0.1610 -0.0808 237 ASP A O 1845 C CB . ASP A 237 ? 1.2161 0.6639 1.3583 -0.0864 -0.1915 0.0012 237 ASP A CB 1846 C CG . ASP A 237 ? 1.7015 1.1338 1.8686 -0.0919 -0.2135 0.0356 237 ASP A CG 1847 O OD1 . ASP A 237 ? 1.8926 1.3263 2.0290 -0.1151 -0.2184 0.0659 237 ASP A OD1 1848 O OD2 . ASP A 237 ? 1.8249 1.2456 2.0430 -0.0729 -0.2263 0.0318 237 ASP A OD2 1849 N N . ASP A 238 ? 1.1308 0.6660 1.2575 -0.0454 -0.1407 -0.0712 238 ASP A N 1850 C CA . ASP A 238 ? 1.1384 0.7038 1.2343 -0.0439 -0.1204 -0.0937 238 ASP A CA 1851 C C . ASP A 238 ? 1.2615 0.8385 1.3137 -0.0662 -0.1122 -0.0708 238 ASP A C 1852 O O . ASP A 238 ? 1.1808 0.7444 1.2253 -0.0816 -0.1208 -0.0417 238 ASP A O 1853 C CB . ASP A 238 ? 1.1869 0.7990 1.2981 -0.0197 -0.1043 -0.1154 238 ASP A CB 1854 C CG . ASP A 238 ? 1.4193 1.0220 1.5767 0.0052 -0.1104 -0.1435 238 ASP A CG 1855 O OD1 . ASP A 238 ? 1.6398 1.2107 1.8051 0.0064 -0.1189 -0.1652 238 ASP A OD1 1856 O OD2 . ASP A 238 ? 1.4630 1.0896 1.6523 0.0235 -0.1074 -0.1445 238 ASP A OD2 1857 N N . PHE A 239 ? 1.3381 0.9414 1.3628 -0.0677 -0.0959 -0.0843 239 PHE A N 1858 C CA . PHE A 239 ? 1.0607 0.6694 1.0487 -0.0879 -0.0888 -0.0664 239 PHE A CA 1859 C C . PHE A 239 ? 1.0764 0.7268 1.0526 -0.0855 -0.0733 -0.0580 239 PHE A C 1860 O O . PHE A 239 ? 1.1171 0.8035 1.0947 -0.0723 -0.0605 -0.0740 239 PHE A O 1861 C CB . PHE A 239 ? 1.0465 0.6509 1.0148 -0.0951 -0.0849 -0.0819 239 PHE A CB 1862 C CG . PHE A 239 ? 1.0791 0.6417 1.0603 -0.1007 -0.1010 -0.0886 239 PHE A CG 1863 C CD1 . PHE A 239 ? 1.0520 0.6116 1.0335 -0.0976 -0.1012 -0.1153 239 PHE A CD1 1864 C CD2 . PHE A 239 ? 1.0165 0.5440 1.0104 -0.1109 -0.1174 -0.0666 239 PHE A CD2 1865 C CE1 . PHE A 239 ? 1.1120 0.6309 1.1096 -0.1044 -0.1177 -0.1205 239 PHE A CE1 1866 C CE2 . PHE A 239 ? 1.0165 0.5055 1.0262 -0.1178 -0.1335 -0.0685 239 PHE A CE2 1867 C CZ . PHE A 239 ? 1.2102 0.6932 1.2236 -0.1146 -0.1338 -0.0958 239 PHE A CZ 1868 N N . VAL A 240 ? 1.0471 0.6934 1.0120 -0.0997 -0.0751 -0.0327 240 VAL A N 1869 C CA . VAL A 240 ? 1.0259 0.7051 0.9813 -0.1015 -0.0628 -0.0219 240 VAL A CA 1870 C C . VAL A 240 ? 1.1439 0.8172 1.0695 -0.1194 -0.0571 -0.0120 240 VAL A C 1871 O O . VAL A 240 ? 1.1332 0.7784 1.0461 -0.1348 -0.0649 -0.0005 240 VAL A O 1872 C CB . VAL A 240 ? 1.0169 0.6994 0.9883 -0.1024 -0.0699 -0.0032 240 VAL A CB 1873 C CG1 . VAL A 240 ? 1.0125 0.7271 0.9782 -0.1058 -0.0584 0.0080 240 VAL A CG1 1874 C CG2 . VAL A 240 ? 1.0654 0.7559 1.0724 -0.0830 -0.0754 -0.0122 240 VAL A CG2 1875 N N . SER A 241 ? 0.9972 0.6996 0.9130 -0.1171 -0.0432 -0.0158 241 SER A N 1876 C CA . SER A 241 ? 1.0082 0.7073 0.9024 -0.1311 -0.0370 -0.0078 241 SER A CA 1877 C C . SER A 241 ? 0.9394 0.6692 0.8342 -0.1308 -0.0260 0.0029 241 SER A C 1878 O O . SER A 241 ? 0.9809 0.7455 0.8846 -0.1194 -0.0183 -0.0009 241 SER A O 1879 C CB . SER A 241 ? 1.0314 0.7291 0.9147 -0.1318 -0.0342 -0.0219 241 SER A CB 1880 O OG . SER A 241 ? 1.0565 0.7545 0.9243 -0.1435 -0.0276 -0.0137 241 SER A OG 1881 N N . GLY A 242 ? 0.8937 0.6115 0.7802 -0.1439 -0.0254 0.0164 242 GLY A N 1882 C CA . GLY A 242 ? 0.9363 0.6760 0.8268 -0.1457 -0.0167 0.0277 242 GLY A CA 1883 C C . GLY A 242 ? 1.0966 0.8499 0.9796 -0.1457 -0.0077 0.0252 242 GLY A C 1884 O O . GLY A 242 ? 1.3105 1.0462 1.1807 -0.1513 -0.0082 0.0184 242 GLY A O 1885 N N . VAL A 243 ? 1.0262 0.8139 0.9190 -0.1403 -0.0001 0.0334 243 VAL A N 1886 C CA . VAL A 243 ? 1.1275 0.9334 1.0168 -0.1406 0.0069 0.0362 243 VAL A CA 1887 C C . VAL A 243 ? 0.8773 0.7028 0.7824 -0.1431 0.0117 0.0569 243 VAL A C 1888 O O . VAL A 243 ? 0.8963 0.7600 0.8113 -0.1372 0.0160 0.0664 243 VAL A O 1889 C CB . VAL A 243 ? 0.9683 0.8031 0.8520 -0.1304 0.0091 0.0231 243 VAL A CB 1890 C CG1 . VAL A 243 ? 1.0154 0.8810 0.9089 -0.1192 0.0114 0.0208 243 VAL A CG1 1891 C CG2 . VAL A 243 ? 1.1456 1.0064 1.0264 -0.1316 0.0144 0.0297 243 VAL A CG2 1892 N N . PRO A 244 ? 0.8357 0.6352 0.7444 -0.1527 0.0109 0.0638 244 PRO A N 1893 C CA . PRO A 244 ? 0.8644 0.6675 0.7928 -0.1575 0.0118 0.0814 244 PRO A CA 1894 C C . PRO A 244 ? 0.8218 0.6539 0.7663 -0.1556 0.0172 0.0987 244 PRO A C 1895 O O . PRO A 244 ? 1.0008 0.8474 0.9666 -0.1578 0.0170 0.1173 244 PRO A O 1896 C CB . PRO A 244 ? 0.7826 0.5455 0.7054 -0.1675 0.0096 0.0749 244 PRO A CB 1897 C CG . PRO A 244 ? 0.7879 0.5384 0.6917 -0.1675 0.0117 0.0608 244 PRO A CG 1898 C CD . PRO A 244 ? 0.8160 0.5803 0.7097 -0.1601 0.0090 0.0525 244 PRO A CD 1899 N N . ARG A 245 ? 0.8248 0.6661 0.7618 -0.1528 0.0204 0.0951 245 ARG A N 1900 C CA . ARG A 245 ? 0.8287 0.6986 0.7823 -0.1517 0.0235 0.1145 245 ARG A CA 1901 C C . ARG A 245 ? 0.8634 0.7833 0.8119 -0.1451 0.0256 0.1212 245 ARG A C 1902 O O . ARG A 245 ? 1.1319 1.0836 1.0918 -0.1450 0.0269 0.1408 245 ARG A O 1903 C CB . ARG A 245 ? 0.8339 0.6906 0.7867 -0.1530 0.0251 0.1099 245 ARG A CB 1904 C CG . ARG A 245 ? 0.9938 0.8175 0.9642 -0.1582 0.0260 0.1122 245 ARG A CG 1905 C CD . ARG A 245 ? 0.8846 0.7094 0.8637 -0.1568 0.0291 0.1131 245 ARG A CD 1906 N NE . ARG A 245 ? 1.0843 0.9505 1.0759 -0.1527 0.0280 0.1334 245 ARG A NE 1907 C CZ . ARG A 245 ? 1.0071 0.8873 1.0302 -0.1523 0.0266 0.1588 245 ARG A CZ 1908 N NH1 . ARG A 245 ? 0.7925 0.6446 0.8404 -0.1551 0.0264 0.1639 245 ARG A NH1 1909 N NH2 . ARG A 245 ? 1.0468 0.9693 1.0776 -0.1500 0.0244 0.1797 245 ARG A NH2 1910 N N . ALA A 246 ? 0.8989 0.8275 0.8314 -0.1396 0.0257 0.1048 246 ALA A N 1911 C CA . ALA A 246 ? 0.9860 0.9636 0.9096 -0.1323 0.0292 0.1036 246 ALA A CA 1912 C C . ALA A 246 ? 0.9981 1.0175 0.9391 -0.1321 0.0330 0.1281 246 ALA A C 1913 O O . ALA A 246 ? 1.0229 1.0289 0.9854 -0.1381 0.0314 0.1459 246 ALA A O 1914 C CB . ALA A 246 ? 1.1979 1.1691 1.1044 -0.1248 0.0284 0.0752 246 ALA A CB 1915 N N . ALA A 247 ? 1.0277 1.0997 0.9592 -0.1262 0.0381 0.1281 247 ALA A N 1916 C CA . ALA A 247 ? 0.9468 1.0704 0.8924 -0.1265 0.0434 0.1528 247 ALA A CA 1917 C C . ALA A 247 ? 0.9571 1.0831 0.9292 -0.1368 0.0405 0.1900 247 ALA A C 1918 O O . ALA A 247 ? 0.9697 1.0960 0.9659 -0.1418 0.0400 0.2098 247 ALA A O 1919 C CB . ALA A 247 ? 0.9649 1.0866 0.9209 -0.1225 0.0457 0.1468 247 ALA A CB 1920 N N . ARG A 248 ? 1.0444 1.1711 1.0153 -0.1399 0.0374 0.1993 248 ARG A N 1921 C CA . ARG A 248 ? 1.1051 1.2254 1.1062 -0.1481 0.0328 0.2325 248 ARG A CA 1922 C C . ARG A 248 ? 0.8916 0.9592 0.9169 -0.1533 0.0290 0.2344 248 ARG A C 1923 O O . ARG A 248 ? 0.7919 0.8657 0.8472 -0.1600 0.0267 0.2621 248 ARG A O 1924 C CB . ARG A 248 ? 1.0966 1.2796 1.1125 -0.1526 0.0342 0.2710 248 ARG A CB 1925 C CG . ARG A 248 ? 1.2015 1.4286 1.2176 -0.1520 0.0410 0.2788 248 ARG A CG 1926 C CD . ARG A 248 ? 1.3979 1.6142 1.4529 -0.1611 0.0377 0.3084 248 ARG A CD 1927 N NE . ARG A 248 ? 1.4794 1.7429 1.5386 -0.1613 0.0447 0.3180 248 ARG A NE 1928 C CZ . ARG A 248 ? 1.4726 1.7406 1.5661 -0.1705 0.0423 0.3462 248 ARG A CZ 1929 N NH1 . ARG A 248 ? 1.3857 1.6098 1.5117 -0.1801 0.0323 0.3650 248 ARG A NH1 1930 N NH2 . ARG A 248 ? 1.3568 1.6739 1.4545 -0.1701 0.0500 0.3542 248 ARG A NH2 1931 N N . THR A 249 ? 0.9005 0.9186 0.9115 -0.1513 0.0278 0.2043 249 THR A N 1932 C CA . THR A 249 ? 0.8562 0.8208 0.8810 -0.1566 0.0239 0.1979 249 THR A CA 1933 C C . THR A 249 ? 0.8662 0.8281 0.8981 -0.1595 0.0224 0.1986 249 THR A C 1934 O O . THR A 249 ? 0.7835 0.7039 0.8224 -0.1651 0.0178 0.1907 249 THR A O 1935 C CB . THR A 249 ? 0.7966 0.7440 0.8551 -0.1625 0.0202 0.2198 249 THR A CB 1936 O OG1 . THR A 249 ? 1.0222 0.9173 1.0786 -0.1637 0.0192 0.1983 249 THR A OG1 1937 C CG2 . THR A 249 ? 0.8557 0.8085 0.9477 -0.1701 0.0162 0.2464 249 THR A CG2 1938 N N . LEU A 250 ? 0.9583 0.9671 0.9879 -0.1557 0.0264 0.2064 250 LEU A N 1939 C CA . LEU A 250 ? 0.9859 0.9983 1.0229 -0.1564 0.0255 0.2050 250 LEU A CA 1940 C C . LEU A 250 ? 0.8874 0.8590 0.9044 -0.1530 0.0223 0.1737 250 LEU A C 1941 O O . LEU A 250 ? 0.8330 0.7850 0.8595 -0.1574 0.0169 0.1721 250 LEU A O 1942 C CB . LEU A 250 ? 0.8443 0.9202 0.8797 -0.1499 0.0333 0.2133 250 LEU A CB 1943 C CG . LEU A 250 ? 0.9286 1.0537 0.9910 -0.1568 0.0357 0.2518 250 LEU A CG 1944 C CD1 . LEU A 250 ? 0.8481 1.0421 0.9000 -0.1487 0.0464 0.2532 250 LEU A CD1 1945 C CD2 . LEU A 250 ? 1.1169 1.2241 1.2120 -0.1673 0.0290 0.2689 250 LEU A CD2 1946 N N . GLY A 251 ? 0.9127 0.8731 0.9035 -0.1464 0.0241 0.1510 251 GLY A N 1947 C CA . GLY A 251 ? 0.9195 0.8429 0.8920 -0.1440 0.0201 0.1247 251 GLY A CA 1948 C C . GLY A 251 ? 0.9642 0.9111 0.9301 -0.1332 0.0221 0.1107 251 GLY A C 1949 O O . GLY A 251 ? 1.1327 1.1200 1.1130 -0.1293 0.0263 0.1220 251 GLY A O 1950 N N . MET A 252 ? 0.9447 0.8671 0.8920 -0.1282 0.0192 0.0864 252 MET A N 1951 C CA . MET A 252 ? 1.0024 0.9403 0.9474 -0.1160 0.0201 0.0688 252 MET A CA 1952 C C . MET A 252 ? 1.0097 0.9021 0.9469 -0.1158 0.0109 0.0508 252 MET A C 1953 O O . MET A 252 ? 0.9650 0.8181 0.8917 -0.1257 0.0054 0.0500 252 MET A O 1954 C CB . MET A 252 ? 1.0457 1.0181 0.9768 -0.1069 0.0272 0.0558 252 MET A CB 1955 C CG . MET A 252 ? 1.0542 1.0883 0.9934 -0.1030 0.0369 0.0711 252 MET A CG 1956 S SD . MET A 252 ? 1.1171 1.1956 1.0349 -0.0915 0.0443 0.0478 252 MET A SD 1957 C CE . MET A 252 ? 1.5690 1.7255 1.4979 -0.0892 0.0565 0.0713 252 MET A CE 1958 N N . VAL A 253 ? 1.0644 0.9648 1.0093 -0.1045 0.0093 0.0377 253 VAL A N 1959 C CA . VAL A 253 ? 1.0671 0.9280 1.0084 -0.1028 -0.0008 0.0220 253 VAL A CA 1960 C C . VAL A 253 ? 1.1442 1.0189 1.0869 -0.0869 0.0013 -0.0025 253 VAL A C 1961 O O . VAL A 253 ? 1.2213 1.1314 1.1802 -0.0740 0.0070 -0.0074 253 VAL A O 1962 C CB . VAL A 253 ? 1.0442 0.8896 1.0025 -0.1056 -0.0101 0.0322 253 VAL A CB 1963 C CG1 . VAL A 253 ? 1.0539 0.8687 1.0152 -0.1003 -0.0212 0.0182 253 VAL A CG1 1964 C CG2 . VAL A 253 ? 0.9705 0.7903 0.9220 -0.1232 -0.0151 0.0486 253 VAL A CG2 1965 N N . TYR A 254 ? 1.1335 0.9814 1.0610 -0.0883 -0.0032 -0.0189 254 TYR A N 1966 C CA . TYR A 254 ? 1.1855 1.0404 1.1146 -0.0747 -0.0030 -0.0463 254 TYR A CA 1967 C C . TYR A 254 ? 1.1793 0.9973 1.1248 -0.0691 -0.0155 -0.0568 254 TYR A C 1968 O O . TYR A 254 ? 1.1287 0.9064 1.0720 -0.0808 -0.0263 -0.0454 254 TYR A O 1969 C CB . TYR A 254 ? 1.1663 1.0147 1.0737 -0.0801 -0.0028 -0.0588 254 TYR A CB 1970 C CG . TYR A 254 ? 1.1809 1.0692 1.0747 -0.0841 0.0076 -0.0487 254 TYR A CG 1971 C CD1 . TYR A 254 ? 1.2222 1.1556 1.1237 -0.0801 0.0175 -0.0336 254 TYR A CD1 1972 C CD2 . TYR A 254 ? 1.1567 1.0399 1.0332 -0.0925 0.0065 -0.0515 254 TYR A CD2 1973 C CE1 . TYR A 254 ? 1.2115 1.1820 1.1033 -0.0848 0.0250 -0.0197 254 TYR A CE1 1974 C CE2 . TYR A 254 ? 1.1704 1.0910 1.0380 -0.0960 0.0139 -0.0392 254 TYR A CE2 1975 C CZ . TYR A 254 ? 1.1882 1.1516 1.0633 -0.0922 0.0227 -0.0224 254 TYR A CZ 1976 O OH . TYR A 254 ? 1.1524 1.1538 1.0214 -0.0968 0.0283 -0.0057 254 TYR A OH 1977 N N . ILE A 255 ? 1.2288 1.0629 1.1923 -0.0512 -0.0139 -0.0782 255 ILE A N 1978 C CA . ILE A 255 ? 1.2235 1.0216 1.2086 -0.0436 -0.0270 -0.0903 255 ILE A CA 1979 C C . ILE A 255 ? 1.2413 1.0330 1.2266 -0.0332 -0.0282 -0.1242 255 ILE A C 1980 O O . ILE A 255 ? 1.3223 1.1533 1.3105 -0.0180 -0.0172 -0.1467 255 ILE A O 1981 C CB . ILE A 255 ? 1.2546 1.0707 1.2732 -0.0291 -0.0271 -0.0866 255 ILE A CB 1982 C CG1 . ILE A 255 ? 1.2197 1.0310 1.2405 -0.0426 -0.0318 -0.0535 255 ILE A CG1 1983 C CG2 . ILE A 255 ? 1.2452 1.0277 1.2925 -0.0172 -0.0407 -0.1026 255 ILE A CG2 1984 C CD1 . ILE A 255 ? 1.2419 1.0656 1.2987 -0.0316 -0.0365 -0.0458 255 ILE A CD1 1985 N N . TYR A 256 ? 1.2020 0.9460 1.1838 -0.0426 -0.0418 -0.1281 256 TYR A N 1986 C CA . TYR A 256 ? 1.2104 0.9402 1.1949 -0.0360 -0.0466 -0.1603 256 TYR A CA 1987 C C . TYR A 256 ? 1.2648 0.9547 1.2847 -0.0262 -0.0620 -0.1709 256 TYR A C 1988 O O . TYR A 256 ? 1.4332 1.0937 1.4667 -0.0330 -0.0736 -0.1467 256 TYR A O 1989 C CB . TYR A 256 ? 1.1712 0.8788 1.1299 -0.0552 -0.0514 -0.1570 256 TYR A CB 1990 C CG . TYR A 256 ? 1.1632 0.9097 1.0922 -0.0630 -0.0381 -0.1498 256 TYR A CG 1991 C CD1 . TYR A 256 ? 1.1236 0.8668 1.0369 -0.0792 -0.0356 -0.1200 256 TYR A CD1 1992 C CD2 . TYR A 256 ? 1.1952 0.9827 1.1132 -0.0540 -0.0285 -0.1731 256 TYR A CD2 1993 C CE1 . TYR A 256 ? 1.1212 0.8978 1.0142 -0.0852 -0.0249 -0.1116 256 TYR A CE1 1994 C CE2 . TYR A 256 ? 1.1896 1.0142 1.0833 -0.0617 -0.0185 -0.1621 256 TYR A CE2 1995 C CZ . TYR A 256 ? 1.1569 0.9742 1.0410 -0.0768 -0.0172 -0.1303 256 TYR A CZ 1996 O OH . TYR A 256 ? 1.3250 1.1773 1.1915 -0.0833 -0.0086 -0.1176 256 TYR A OH 1997 N N . ASP A 257 ? 1.2361 0.9255 1.2720 -0.0103 -0.0631 -0.2075 257 ASP A N 1998 C CA . ASP A 257 ? 1.3575 1.0066 1.4341 0.0014 -0.0787 -0.2211 257 ASP A CA 1999 C C . ASP A 257 ? 1.3585 0.9491 1.4365 -0.0182 -0.0988 -0.2062 257 ASP A C 2000 O O . ASP A 257 ? 1.4776 1.0619 1.5255 -0.0368 -0.0988 -0.2008 257 ASP A O 2001 C CB . ASP A 257 ? 1.3010 0.9640 1.3937 0.0231 -0.0740 -0.2696 257 ASP A CB 2002 C CG . ASP A 257 ? 1.4103 1.0331 1.5542 0.0396 -0.0894 -0.2863 257 ASP A CG 2003 O OD1 . ASP A 257 ? 1.5411 1.1846 1.7170 0.0609 -0.0840 -0.2918 257 ASP A OD1 2004 O OD2 . ASP A 257 ? 1.5678 1.1392 1.7238 0.0312 -0.1075 -0.2924 257 ASP A OD2 2005 N N . GLY A 258 ? 1.3176 0.8685 1.4329 -0.0144 -0.1163 -0.1971 258 GLY A N 2006 C CA . GLY A 258 ? 1.3047 0.8032 1.4247 -0.0343 -0.1364 -0.1766 258 GLY A CA 2007 C C . GLY A 258 ? 1.3579 0.8216 1.4939 -0.0342 -0.1484 -0.2052 258 GLY A C 2008 O O . GLY A 258 ? 1.2068 0.6391 1.3332 -0.0559 -0.1600 -0.1911 258 GLY A O 2009 N N . LYS A 259 ? 1.3986 0.8692 1.5606 -0.0103 -0.1457 -0.2465 259 LYS A N 2010 C CA . LYS A 259 ? 1.2207 0.6580 1.4011 -0.0084 -0.1578 -0.2810 259 LYS A CA 2011 C C . LYS A 259 ? 1.2788 0.7398 1.4159 -0.0206 -0.1477 -0.2998 259 LYS A C 2012 O O . LYS A 259 ? 1.3459 0.7780 1.4745 -0.0415 -0.1595 -0.2938 259 LYS A O 2013 C CB . LYS A 259 ? 1.2448 0.6832 1.4685 0.0230 -0.1573 -0.3239 259 LYS A CB 2014 C CG . LYS A 259 ? 1.3814 0.7949 1.6574 0.0371 -0.1699 -0.3059 259 LYS A CG 2015 C CD . LYS A 259 ? 1.5556 0.9564 1.8847 0.0675 -0.1738 -0.3522 259 LYS A CD 2016 C CE . LYS A 259 ? 1.5988 0.9454 1.9490 0.0613 -0.1932 -0.3788 259 LYS A CE 2017 N NZ . LYS A 259 ? 1.7301 1.0580 2.1381 0.0920 -0.1987 -0.4267 259 LYS A NZ 2018 N N . ASN A 260 ? 1.3816 0.8986 1.4935 -0.0081 -0.1265 -0.3207 260 ASN A N 2019 C CA . ASN A 260 ? 1.2580 0.8076 1.3270 -0.0194 -0.1163 -0.3332 260 ASN A CA 2020 C C . ASN A 260 ? 1.5258 1.1243 1.5583 -0.0255 -0.0977 -0.3034 260 ASN A C 2021 O O . ASN A 260 ? 1.6295 1.2432 1.6706 -0.0170 -0.0905 -0.2834 260 ASN A O 2022 C CB . ASN A 260 ? 1.2771 0.8524 1.3466 -0.0012 -0.1098 -0.3877 260 ASN A CB 2023 C CG . ASN A 260 ? 1.7522 1.3659 1.8380 0.0272 -0.0944 -0.4067 260 ASN A CG 2024 O OD1 . ASN A 260 ? 1.8675 1.4812 1.9727 0.0343 -0.0921 -0.3799 260 ASN A OD1 2025 N ND2 . ASN A 260 ? 2.2793 1.9295 2.3575 0.0430 -0.0838 -0.4538 260 ASN A ND2 2026 N N . MET A 261 ? 1.4351 1.0577 1.4308 -0.0406 -0.0913 -0.2997 261 MET A N 2027 C CA . MET A 261 ? 1.3036 0.9595 1.2698 -0.0511 -0.0780 -0.2652 261 MET A CA 2028 C C . MET A 261 ? 1.2254 0.9433 1.1781 -0.0360 -0.0582 -0.2726 261 MET A C 2029 O O . MET A 261 ? 1.2185 0.9679 1.1492 -0.0437 -0.0472 -0.2463 261 MET A O 2030 C CB . MET A 261 ? 1.6057 1.2623 1.5445 -0.0731 -0.0801 -0.2549 261 MET A CB 2031 C CG . MET A 261 ? 1.5193 1.1778 1.4418 -0.0890 -0.0749 -0.2125 261 MET A CG 2032 S SD . MET A 261 ? 1.6051 1.2183 1.5498 -0.0935 -0.0849 -0.1825 261 MET A SD 2033 C CE . MET A 261 ? 1.0431 0.6640 0.9609 -0.1144 -0.0772 -0.1438 261 MET A CE 2034 N N . SER A 262 ? 1.4621 1.1987 1.4300 -0.0147 -0.0538 -0.3085 262 SER A N 2035 C CA . SER A 262 ? 1.4461 1.2470 1.4039 0.0004 -0.0341 -0.3166 262 SER A CA 2036 C C . SER A 262 ? 1.3427 1.1605 1.3069 0.0012 -0.0254 -0.2786 262 SER A C 2037 O O . SER A 262 ? 1.3642 1.1445 1.3531 0.0009 -0.0348 -0.2601 262 SER A O 2038 C CB . SER A 262 ? 1.3512 1.1636 1.3330 0.0255 -0.0309 -0.3622 262 SER A CB 2039 O OG . SER A 262 ? 1.3302 1.1045 1.3551 0.0374 -0.0394 -0.3585 262 SER A OG 2040 N N . SER A 263 ? 1.2907 1.1660 1.2334 0.0007 -0.0090 -0.2658 263 SER A N 2041 C CA . SER A 263 ? 1.2995 1.1957 1.2487 0.0000 -0.0007 -0.2307 263 SER A CA 2042 C C . SER A 263 ? 1.3288 1.2410 1.3119 0.0215 0.0046 -0.2413 263 SER A C 2043 O O . SER A 263 ? 1.5065 1.4356 1.5016 0.0400 0.0091 -0.2790 263 SER A O 2044 C CB . SER A 263 ? 1.3023 1.2566 1.2238 -0.0070 0.0140 -0.2133 263 SER A CB 2045 O OG . SER A 263 ? 1.3220 1.2992 1.2544 -0.0073 0.0218 -0.1818 263 SER A OG 2046 N N . LEU A 264 ? 1.3379 1.2464 1.3380 0.0191 0.0039 -0.2096 264 LEU A N 2047 C CA . LEU A 264 ? 1.3680 1.2952 1.4046 0.0383 0.0083 -0.2136 264 LEU A CA 2048 C C . LEU A 264 ? 1.3990 1.3809 1.4351 0.0367 0.0227 -0.1858 264 LEU A C 2049 O O . LEU A 264 ? 1.4764 1.5175 1.5173 0.0507 0.0391 -0.1990 264 LEU A O 2050 C CB . LEU A 264 ? 1.3555 1.2254 1.4232 0.0376 -0.0104 -0.2009 264 LEU A CB 2051 C CG . LEU A 264 ? 1.3349 1.1515 1.4189 0.0431 -0.0262 -0.2275 264 LEU A CG 2052 C CD1 . LEU A 264 ? 1.3132 1.0797 1.4290 0.0405 -0.0456 -0.2060 264 LEU A CD1 2053 C CD2 . LEU A 264 ? 1.4457 1.2871 1.5502 0.0689 -0.0178 -0.2735 264 LEU A CD2 2054 N N . TYR A 265 ? 1.3959 1.3591 1.4270 0.0187 0.0163 -0.1478 265 TYR A N 2055 C CA . TYR A 265 ? 1.4266 1.4336 1.4612 0.0137 0.0265 -0.1181 265 TYR A CA 2056 C C . TYR A 265 ? 1.4036 1.4049 1.4089 -0.0089 0.0261 -0.0897 265 TYR A C 2057 O O . TYR A 265 ? 1.3570 1.3140 1.3432 -0.0215 0.0163 -0.0887 265 TYR A O 2058 C CB . TYR A 265 ? 1.4577 1.4509 1.5273 0.0163 0.0179 -0.0994 265 TYR A CB 2059 C CG . TYR A 265 ? 1.5652 1.5662 1.6730 0.0406 0.0179 -0.1239 265 TYR A CG 2060 C CD1 . TYR A 265 ? 1.6289 1.6936 1.7582 0.0579 0.0347 -0.1321 265 TYR A CD1 2061 C CD2 . TYR A 265 ? 1.6076 1.5539 1.7336 0.0466 0.0012 -0.1378 265 TYR A CD2 2062 C CE1 . TYR A 265 ? 1.6168 1.6904 1.7860 0.0825 0.0360 -0.1570 265 TYR A CE1 2063 C CE2 . TYR A 265 ? 1.6314 1.5821 1.7990 0.0705 0.0001 -0.1605 265 TYR A CE2 2064 C CZ . TYR A 265 ? 1.6414 1.6558 1.8312 0.0895 0.0181 -0.1717 265 TYR A CZ 2065 O OH . TYR A 265 ? 1.7517 1.7723 1.9877 0.1157 0.0183 -0.1966 265 TYR A OH 2066 N N . ASN A 266 ? 1.4499 1.4973 1.4556 -0.0138 0.0369 -0.0661 266 ASN A N 2067 C CA . ASN A 266 ? 1.3705 1.4137 1.3573 -0.0337 0.0363 -0.0375 266 ASN A CA 2068 C C . ASN A 266 ? 1.3318 1.3835 1.3382 -0.0428 0.0351 -0.0047 266 ASN A C 2069 O O . ASN A 266 ? 1.3548 1.4390 1.3875 -0.0337 0.0398 -0.0006 266 ASN A O 2070 C CB . ASN A 266 ? 1.3270 1.4197 1.2920 -0.0349 0.0490 -0.0378 266 ASN A CB 2071 C CG . ASN A 266 ? 1.3203 1.3919 1.2583 -0.0370 0.0452 -0.0597 266 ASN A CG 2072 O OD1 . ASN A 266 ? 1.3168 1.3325 1.2507 -0.0419 0.0330 -0.0678 266 ASN A OD1 2073 N ND2 . ASN A 266 ? 1.3656 1.4851 1.2847 -0.0346 0.0549 -0.0678 266 ASN A ND2 2074 N N . PHE A 267 ? 1.2613 1.2842 1.2569 -0.0610 0.0287 0.0171 267 PHE A N 2075 C CA . PHE A 267 ? 1.2047 1.2334 1.2170 -0.0727 0.0265 0.0472 267 PHE A CA 2076 C C . PHE A 267 ? 1.1367 1.1728 1.1360 -0.0865 0.0303 0.0672 267 PHE A C 2077 O O . PHE A 267 ? 1.1236 1.1400 1.1003 -0.0902 0.0297 0.0593 267 PHE A O 2078 C CB . PHE A 267 ? 1.2198 1.1957 1.2383 -0.0814 0.0109 0.0521 267 PHE A CB 2079 C CG . PHE A 267 ? 1.2266 1.1983 1.2670 -0.0688 0.0045 0.0407 267 PHE A CG 2080 C CD1 . PHE A 267 ? 1.2595 1.2022 1.2942 -0.0590 -0.0010 0.0166 267 PHE A CD1 2081 C CD2 . PHE A 267 ? 1.2290 1.2259 1.3001 -0.0670 0.0030 0.0557 267 PHE A CD2 2082 C CE1 . PHE A 267 ? 1.2995 1.2366 1.3606 -0.0463 -0.0083 0.0078 267 PHE A CE1 2083 C CE2 . PHE A 267 ? 1.2773 1.2722 1.3739 -0.0541 -0.0037 0.0469 267 PHE A CE2 2084 C CZ . PHE A 267 ? 1.3121 1.2761 1.4046 -0.0430 -0.0095 0.0230 267 PHE A CZ 2085 N N . THR A 268 ? 1.0961 1.1614 1.1139 -0.0942 0.0335 0.0943 268 THR A N 2086 C CA . THR A 268 ? 1.0559 1.1286 1.0697 -0.1067 0.0357 0.1168 268 THR A CA 2087 C C . THR A 268 ? 1.1149 1.1766 1.1527 -0.1212 0.0290 0.1440 268 THR A C 2088 O O . THR A 268 ? 1.2010 1.2887 1.2634 -0.1210 0.0292 0.1558 268 THR A O 2089 C CB . THR A 268 ? 1.0336 1.1720 1.0453 -0.1016 0.0490 0.1256 268 THR A CB 2090 O OG1 . THR A 268 ? 1.0825 1.2331 1.0716 -0.0882 0.0545 0.0958 268 THR A OG1 2091 C CG2 . THR A 268 ? 0.9792 1.1218 0.9887 -0.1142 0.0488 0.1507 268 THR A CG2 2092 N N . GLY A 269 ? 0.9769 1.0005 1.0098 -0.1338 0.0228 0.1523 269 GLY A N 2093 C CA . GLY A 269 ? 1.0758 1.0849 1.1318 -0.1484 0.0155 0.1747 269 GLY A CA 2094 C C . GLY A 269 ? 1.0052 1.0643 1.0856 -0.1531 0.0215 0.2055 269 GLY A C 2095 O O . GLY A 269 ? 1.0648 1.1609 1.1373 -0.1482 0.0306 0.2119 269 GLY A O 2096 N N . GLU A 270 ? 1.0044 1.0670 1.1148 -0.1640 0.0154 0.2263 270 GLU A N 2097 C CA . GLU A 270 ? 1.0491 1.1600 1.1881 -0.1712 0.0195 0.2606 270 GLU A CA 2098 C C . GLU A 270 ? 0.8273 0.9136 0.9816 -0.1850 0.0133 0.2819 270 GLU A C 2099 O O . GLU A 270 ? 1.1415 1.2646 1.3205 -0.1923 0.0154 0.3145 270 GLU A O 2100 C CB . GLU A 270 ? 1.0204 1.1543 1.1910 -0.1768 0.0157 0.2751 270 GLU A CB 2101 C CG . GLU A 270 ? 1.1138 1.2869 1.2812 -0.1611 0.0240 0.2600 270 GLU A CG 2102 C CD . GLU A 270 ? 1.7147 1.9197 1.9196 -0.1667 0.0209 0.2787 270 GLU A CD 2103 O OE1 . GLU A 270 ? 1.8992 2.0888 2.1301 -0.1846 0.0100 0.3014 270 GLU A OE1 2104 O OE2 . GLU A 270 ? 1.8733 2.1191 2.0845 -0.1530 0.0291 0.2698 270 GLU A OE2 2105 N N . GLN A 271 ? 0.7693 0.7949 0.9112 -0.1884 0.0058 0.2642 271 GLN A N 2106 C CA . GLN A 271 ? 0.7435 0.7399 0.9038 -0.1992 -0.0002 0.2791 271 GLN A CA 2107 C C . GLN A 271 ? 0.8231 0.7883 0.9586 -0.1929 0.0025 0.2601 271 GLN A C 2108 O O . GLN A 271 ? 1.0120 0.9461 1.1185 -0.1874 0.0025 0.2301 271 GLN A O 2109 C CB . GLN A 271 ? 0.9421 0.8940 1.1231 -0.2130 -0.0133 0.2774 271 GLN A CB 2110 C CG . GLN A 271 ? 0.8414 0.7562 1.0453 -0.2226 -0.0199 0.2865 271 GLN A CG 2111 C CD . GLN A 271 ? 1.0473 0.9133 1.2645 -0.2357 -0.0329 0.2748 271 GLN A CD 2112 O OE1 . GLN A 271 ? 1.1108 0.9845 1.3382 -0.2433 -0.0400 0.2782 271 GLN A OE1 2113 N NE2 . GLN A 271 ? 1.2089 1.0265 1.4264 -0.2384 -0.0363 0.2594 271 GLN A NE2 2114 N N . MET A 272 ? 0.9792 0.9549 1.1294 -0.1945 0.0039 0.2806 272 MET A N 2115 C CA . MET A 272 ? 0.8689 0.8225 1.0027 -0.1886 0.0064 0.2674 272 MET A CA 2116 C C . MET A 272 ? 0.8225 0.7128 0.9591 -0.1933 0.0004 0.2474 272 MET A C 2117 O O . MET A 272 ? 0.9605 0.8252 1.1215 -0.2035 -0.0075 0.2522 272 MET A O 2118 C CB . MET A 272 ? 0.7555 0.7415 0.9105 -0.1896 0.0076 0.2995 272 MET A CB 2119 C CG . MET A 272 ? 0.8802 0.9365 1.0294 -0.1866 0.0145 0.3205 272 MET A CG 2120 S SD . MET A 272 ? 0.9939 1.0902 1.1446 -0.1843 0.0165 0.3460 272 MET A SD 2121 C CE . MET A 272 ? 0.9315 0.9856 1.1336 -0.1941 0.0052 0.3725 272 MET A CE 2122 N N . ALA A 273 ? 0.9707 0.8387 1.0816 -0.1865 0.0043 0.2236 273 ALA A N 2123 C CA . ALA A 273 ? 0.9599 0.7754 1.0697 -0.1894 0.0021 0.2023 273 ALA A CA 2124 C C . ALA A 273 ? 1.0470 0.8293 1.1415 -0.1959 -0.0031 0.1799 273 ALA A C 2125 O O . ALA A 273 ? 1.0003 0.7428 1.0869 -0.1992 -0.0041 0.1586 273 ALA A O 2126 C CB . ALA A 273 ? 0.7867 0.5861 0.9388 -0.1944 -0.0022 0.2203 273 ALA A CB 2127 N N . ALA A 274 ? 0.8716 0.6740 0.9622 -0.1978 -0.0062 0.1848 274 ALA A N 2128 C CA . ALA A 274 ? 0.7622 0.5394 0.8406 -0.2047 -0.0136 0.1682 274 ALA A CA 2129 C C . ALA A 274 ? 1.0220 0.7796 1.0607 -0.2002 -0.0114 0.1408 274 ALA A C 2130 O O . ALA A 274 ? 1.0018 0.7363 1.0259 -0.2068 -0.0182 0.1266 274 ALA A O 2131 C CB . ALA A 274 ? 0.7330 0.5429 0.8232 -0.2062 -0.0175 0.1833 274 ALA A CB 2132 N N . TYR A 275 ? 0.9764 0.7454 0.9994 -0.1905 -0.0030 0.1357 275 TYR A N 2133 C CA . TYR A 275 ? 0.9366 0.6908 0.9260 -0.1866 -0.0009 0.1135 275 TYR A CA 2134 C C . TYR A 275 ? 0.9042 0.6652 0.8806 -0.1848 -0.0063 0.1081 275 TYR A C 2135 O O . TYR A 275 ? 0.7661 0.5017 0.7228 -0.1894 -0.0116 0.0938 275 TYR A O 2136 C CB . TYR A 275 ? 0.9278 0.6416 0.9046 -0.1942 -0.0016 0.0955 275 TYR A CB 2137 C CG . TYR A 275 ? 0.8653 0.5741 0.8258 -0.1892 0.0064 0.0838 275 TYR A CG 2138 C CD1 . TYR A 275 ? 0.7593 0.4808 0.7374 -0.1836 0.0128 0.0928 275 TYR A CD1 2139 C CD2 . TYR A 275 ? 0.7564 0.4502 0.6870 -0.1909 0.0063 0.0668 275 TYR A CD2 2140 C CE1 . TYR A 275 ? 0.7574 0.4779 0.7243 -0.1796 0.0193 0.0835 275 TYR A CE1 2141 C CE2 . TYR A 275 ? 0.7570 0.4490 0.6759 -0.1879 0.0133 0.0580 275 TYR A CE2 2142 C CZ . TYR A 275 ? 0.7870 0.4931 0.7244 -0.1820 0.0199 0.0655 275 TYR A CZ 2143 O OH . TYR A 275 ? 0.8730 0.5806 0.8023 -0.1795 0.0261 0.0579 275 TYR A OH 2144 N N . PHE A 276 ? 0.9653 0.7637 0.9548 -0.1780 -0.0047 0.1210 276 PHE A N 2145 C CA . PHE A 276 ? 0.8625 0.6737 0.8466 -0.1720 -0.0080 0.1155 276 PHE A CA 2146 C C . PHE A 276 ? 0.9456 0.7441 0.9034 -0.1650 -0.0066 0.0958 276 PHE A C 2147 O O . PHE A 276 ? 0.8424 0.6540 0.7922 -0.1583 0.0005 0.0915 276 PHE A O 2148 C CB . PHE A 276 ? 0.8320 0.6933 0.8358 -0.1639 -0.0025 0.1308 276 PHE A CB 2149 C CG . PHE A 276 ? 0.8658 0.7457 0.8702 -0.1541 -0.0038 0.1233 276 PHE A CG 2150 C CD1 . PHE A 276 ? 0.9411 0.8248 0.9641 -0.1579 -0.0114 0.1311 276 PHE A CD1 2151 C CD2 . PHE A 276 ? 0.9073 0.8023 0.8978 -0.1408 0.0021 0.1078 276 PHE A CD2 2152 C CE1 . PHE A 276 ? 0.9199 0.8225 0.9500 -0.1469 -0.0125 0.1247 276 PHE A CE1 2153 C CE2 . PHE A 276 ? 0.9581 0.8687 0.9548 -0.1297 0.0012 0.0984 276 PHE A CE2 2154 C CZ . PHE A 276 ? 0.9717 0.8868 0.9897 -0.1319 -0.0057 0.1076 276 PHE A CZ 2155 N N . GLY A 277 ? 1.0956 0.8697 1.0417 -0.1679 -0.0150 0.0856 277 GLY A N 2156 C CA . GLY A 277 ? 0.8586 0.6161 0.7836 -0.1639 -0.0161 0.0697 277 GLY A CA 2157 C C . GLY A 277 ? 0.8782 0.6017 0.7824 -0.1745 -0.0169 0.0617 277 GLY A C 2158 O O . GLY A 277 ? 0.9148 0.6278 0.8033 -0.1730 -0.0157 0.0513 277 GLY A O 2159 N N . PHE A 278 ? 1.0330 0.7410 0.9384 -0.1856 -0.0186 0.0654 278 PHE A N 2160 C CA . PHE A 278 ? 0.8928 0.5722 0.7778 -0.1960 -0.0179 0.0554 278 PHE A CA 2161 C C . PHE A 278 ? 0.9779 0.6392 0.8424 -0.2019 -0.0273 0.0498 278 PHE A C 2162 O O . PHE A 278 ? 1.1632 0.8091 1.0075 -0.2075 -0.0254 0.0419 278 PHE A O 2163 C CB . PHE A 278 ? 0.8061 0.4730 0.6983 -0.2062 -0.0187 0.0565 278 PHE A CB 2164 C CG . PHE A 278 ? 0.9514 0.5926 0.8210 -0.2168 -0.0170 0.0426 278 PHE A CG 2165 C CD1 . PHE A 278 ? 1.0856 0.7234 0.9520 -0.2146 -0.0056 0.0347 278 PHE A CD1 2166 C CD2 . PHE A 278 ? 0.8262 0.4514 0.6781 -0.2293 -0.0266 0.0376 278 PHE A CD2 2167 C CE1 . PHE A 278 ? 0.9706 0.5906 0.8172 -0.2237 -0.0016 0.0205 278 PHE A CE1 2168 C CE2 . PHE A 278 ? 0.9429 0.5507 0.7706 -0.2398 -0.0235 0.0236 278 PHE A CE2 2169 C CZ . PHE A 278 ? 0.8920 0.4979 0.7174 -0.2365 -0.0098 0.0142 278 PHE A CZ 2170 N N . SER A 279 ? 0.8523 0.5182 0.7252 -0.2012 -0.0379 0.0565 279 SER A N 2171 C CA . SER A 279 ? 0.9716 0.6228 0.8316 -0.2059 -0.0498 0.0564 279 SER A CA 2172 C C . SER A 279 ? 1.0545 0.7216 0.9360 -0.1938 -0.0568 0.0623 279 SER A C 2173 O O . SER A 279 ? 1.0121 0.7019 0.9161 -0.1873 -0.0550 0.0688 279 SER A O 2174 C CB . SER A 279 ? 1.2174 0.8530 1.0632 -0.2227 -0.0595 0.0584 279 SER A CB 2175 O OG . SER A 279 ? 0.9140 0.5607 0.7797 -0.2242 -0.0654 0.0663 279 SER A OG 2176 N N . VAL A 280 ? 1.1171 0.7734 0.9950 -0.1907 -0.0645 0.0604 280 VAL A N 2177 C CA . VAL A 280 ? 0.8560 0.5248 0.7585 -0.1770 -0.0714 0.0629 280 VAL A CA 2178 C C . VAL A 280 ? 0.9027 0.5518 0.8042 -0.1830 -0.0890 0.0704 280 VAL A C 2179 O O . VAL A 280 ? 1.0742 0.7007 0.9524 -0.1961 -0.0940 0.0718 280 VAL A O 2180 C CB . VAL A 280 ? 0.9662 0.6455 0.8764 -0.1608 -0.0628 0.0502 280 VAL A CB 2181 C CG1 . VAL A 280 ? 0.8866 0.5962 0.8035 -0.1532 -0.0477 0.0477 280 VAL A CG1 2182 C CG2 . VAL A 280 ? 1.0644 0.7196 0.9536 -0.1669 -0.0625 0.0423 280 VAL A CG2 2183 N N . ALA A 281 ? 1.0371 0.6980 0.9663 -0.1736 -0.0984 0.0771 281 ALA A N 2184 C CA . ALA A 281 ? 1.0202 0.6652 0.9562 -0.1777 -0.1175 0.0881 281 ALA A CA 2185 C C . ALA A 281 ? 0.9838 0.6424 0.9597 -0.1572 -0.1227 0.0874 281 ALA A C 2186 O O . ALA A 281 ? 0.9602 0.6486 0.9585 -0.1438 -0.1134 0.0832 281 ALA A O 2187 C CB . ALA A 281 ? 1.0023 0.6463 0.9287 -0.1955 -0.1299 0.1029 281 ALA A CB 2188 N N . ALA A 282 ? 1.0755 0.7137 1.0627 -0.1548 -0.1374 0.0920 282 ALA A N 2189 C CA . ALA A 282 ? 0.9884 0.6353 1.0188 -0.1337 -0.1437 0.0894 282 ALA A CA 2190 C C . ALA A 282 ? 0.9933 0.6279 1.0423 -0.1394 -0.1680 0.1114 282 ALA A C 2191 O O . ALA A 282 ? 0.9922 0.5981 1.0276 -0.1521 -0.1816 0.1222 282 ALA A O 2192 C CB . ALA A 282 ? 1.0146 0.6473 1.0523 -0.1196 -0.1383 0.0696 282 ALA A CB 2193 N N . THR A 283 ? 1.0119 0.6718 1.0937 -0.1310 -0.1738 0.1204 283 THR A N 2194 C CA . THR A 283 ? 1.0314 0.6862 1.1375 -0.1349 -0.1984 0.1436 283 THR A CA 2195 C C . THR A 283 ? 1.2012 0.8882 1.3611 -0.1125 -0.1988 0.1433 283 THR A C 2196 O O . THR A 283 ? 1.3854 1.1028 1.5548 -0.0998 -0.1795 0.1285 283 THR A O 2197 C CB . THR A 283 ? 1.1529 0.8081 1.2284 -0.1624 -0.2106 0.1640 283 THR A CB 2198 O OG1 . THR A 283 ? 1.2493 0.8939 1.2752 -0.1788 -0.1969 0.1541 283 THR A OG1 2199 C CG2 . THR A 283 ? 1.3652 1.0003 1.4420 -0.1753 -0.2376 0.1888 283 THR A CG2 2200 N N . ASP A 284 ? 1.1189 0.8027 1.3160 -0.1077 -0.2206 0.1613 284 ASP A N 2201 C CA . ASP A 284 ? 1.2123 0.9316 1.4642 -0.0875 -0.2218 0.1638 284 ASP A CA 2202 C C . ASP A 284 ? 1.2980 1.0379 1.5508 -0.1057 -0.2370 0.1899 284 ASP A C 2203 O O . ASP A 284 ? 1.1026 0.8294 1.3598 -0.1184 -0.2625 0.2144 284 ASP A O 2204 C CB . ASP A 284 ? 1.1398 0.8456 1.4443 -0.0660 -0.2361 0.1651 284 ASP A CB 2205 C CG . ASP A 284 ? 1.1865 0.9329 1.5532 -0.0418 -0.2350 0.1649 284 ASP A CG 2206 O OD1 . ASP A 284 ? 1.4401 1.1811 1.8549 -0.0314 -0.2557 0.1800 284 ASP A OD1 2207 O OD2 . ASP A 284 ? 1.2113 0.9972 1.5813 -0.0332 -0.2136 0.1513 284 ASP A OD2 2208 N N . ILE A 285 ? 1.2755 1.0491 1.5254 -0.1081 -0.2225 0.1859 285 ILE A N 2209 C CA . ILE A 285 ? 1.1066 0.8986 1.3533 -0.1287 -0.2360 0.2072 285 ILE A CA 2210 C C . ILE A 285 ? 1.1250 0.9517 1.4330 -0.1163 -0.2496 0.2241 285 ILE A C 2211 O O . ILE A 285 ? 1.1996 1.0334 1.5124 -0.1337 -0.2721 0.2477 285 ILE A O 2212 C CB . ILE A 285 ? 1.0733 0.8829 1.2929 -0.1399 -0.2167 0.1980 285 ILE A CB 2213 C CG1 . ILE A 285 ? 1.0490 0.8477 1.2328 -0.1716 -0.2317 0.2118 285 ILE A CG1 2214 C CG2 . ILE A 285 ? 1.0961 0.9551 1.3606 -0.1235 -0.2034 0.1968 285 ILE A CG2 2215 C CD1 . ILE A 285 ? 1.0160 0.7729 1.1478 -0.1893 -0.2387 0.2099 285 ILE A CD1 2216 N N . ASN A 286 ? 1.1579 1.0093 1.5134 -0.0862 -0.2361 0.2110 286 ASN A N 2217 C CA . ASN A 286 ? 1.1862 1.0788 1.6060 -0.0711 -0.2443 0.2245 286 ASN A CA 2218 C C . ASN A 286 ? 1.1969 1.0755 1.6636 -0.0540 -0.2647 0.2338 286 ASN A C 2219 O O . ASN A 286 ? 1.2644 1.1764 1.7919 -0.0382 -0.2727 0.2450 286 ASN A O 2220 C CB . ASN A 286 ? 1.2208 1.1601 1.6701 -0.0480 -0.2156 0.2053 286 ASN A CB 2221 C CG . ASN A 286 ? 1.2569 1.1826 1.6976 -0.0258 -0.1937 0.1730 286 ASN A CG 2222 O OD1 . ASN A 286 ? 1.2595 1.1387 1.6625 -0.0323 -0.1966 0.1638 286 ASN A OD1 2223 N ND2 . ASN A 286 ? 1.3064 1.2762 1.7816 -0.0006 -0.1714 0.1551 286 ASN A ND2 2224 N N . GLY A 287 ? 1.1785 1.0086 1.6210 -0.0572 -0.2736 0.2309 287 GLY A N 2225 C CA . GLY A 287 ? 1.2047 1.0141 1.6916 -0.0437 -0.2959 0.2433 287 GLY A CA 2226 C C . GLY A 287 ? 1.2828 1.1075 1.8324 -0.0046 -0.2827 0.2203 287 GLY A C 2227 O O . GLY A 287 ? 1.2063 1.0303 1.8160 0.0125 -0.3008 0.2322 287 GLY A O 2228 N N . ASP A 288 ? 1.4831 1.3231 2.0195 0.0096 -0.2514 0.1867 288 ASP A N 2229 C CA . ASP A 288 ? 1.3577 1.2177 1.9463 0.0468 -0.2344 0.1575 288 ASP A CA 2230 C C . ASP A 288 ? 1.2663 1.0776 1.8471 0.0583 -0.2326 0.1325 288 ASP A C 2231 O O . ASP A 288 ? 1.3149 1.1358 1.9290 0.0880 -0.2166 0.1000 288 ASP A O 2232 C CB . ASP A 288 ? 1.3184 1.2305 1.8985 0.0557 -0.2015 0.1355 288 ASP A CB 2233 C CG . ASP A 288 ? 1.5241 1.4192 2.0352 0.0415 -0.1819 0.1163 288 ASP A CG 2234 O OD1 . ASP A 288 ? 1.5236 1.3791 1.9838 0.0146 -0.1934 0.1294 288 ASP A OD1 2235 O OD2 . ASP A 288 ? 1.7037 1.6289 2.2121 0.0575 -0.1547 0.0884 288 ASP A OD2 2236 N N . ASP A 289 ? 1.2341 0.9959 1.7696 0.0334 -0.2484 0.1467 289 ASP A N 2237 C CA . ASP A 289 ? 1.2309 0.9421 1.7548 0.0369 -0.2508 0.1294 289 ASP A CA 2238 C C . ASP A 289 ? 1.2829 0.9966 1.7654 0.0411 -0.2212 0.0916 289 ASP A C 2239 O O . ASP A 289 ? 1.2404 0.9149 1.7071 0.0413 -0.2211 0.0747 289 ASP A O 2240 C CB . ASP A 289 ? 1.4467 1.1416 2.0443 0.0666 -0.2637 0.1215 289 ASP A CB 2241 C CG . ASP A 289 ? 1.6980 1.3786 2.3343 0.0592 -0.2988 0.1639 289 ASP A CG 2242 O OD1 . ASP A 289 ? 1.8456 1.5645 2.5293 0.0704 -0.3049 0.1786 289 ASP A OD1 2243 O OD2 . ASP A 289 ? 1.5799 1.2140 2.2001 0.0411 -0.3207 0.1847 289 ASP A OD2 2244 N N . TYR A 290 ? 1.3928 1.1542 1.8596 0.0433 -0.1975 0.0808 290 TYR A N 2245 C CA . TYR A 290 ? 1.2911 1.0609 1.7135 0.0427 -0.1710 0.0519 290 TYR A CA 2246 C C . TYR A 290 ? 1.2685 1.0301 1.6262 0.0100 -0.1692 0.0691 290 TYR A C 2247 O O . TYR A 290 ? 1.4434 1.2313 1.7939 -0.0038 -0.1704 0.0903 290 TYR A O 2248 C CB . TYR A 290 ? 1.3368 1.1671 1.7818 0.0652 -0.1449 0.0300 290 TYR A CB 2249 C CG . TYR A 290 ? 1.3571 1.1974 1.8579 0.1007 -0.1389 -0.0006 290 TYR A CG 2250 C CD1 . TYR A 290 ? 1.3571 1.2258 1.9239 0.1212 -0.1453 0.0069 290 TYR A CD1 2251 C CD2 . TYR A 290 ? 1.3712 1.1935 1.8610 0.1140 -0.1272 -0.0389 290 TYR A CD2 2252 C CE1 . TYR A 290 ? 1.3678 1.2461 1.9898 0.1560 -0.1386 -0.0247 290 TYR A CE1 2253 C CE2 . TYR A 290 ? 1.4168 1.2468 1.9581 0.1472 -0.1215 -0.0722 290 TYR A CE2 2254 C CZ . TYR A 290 ? 1.3908 1.2484 1.9989 0.1690 -0.1264 -0.0659 290 TYR A CZ 2255 O OH . TYR A 290 ? 1.4531 1.3188 2.1165 0.2042 -0.1196 -0.1023 290 TYR A OH 2256 N N . ALA A 291 ? 1.2259 0.9514 1.5405 -0.0021 -0.1668 0.0588 291 ALA A N 2257 C CA . ALA A 291 ? 1.1775 0.8921 1.4334 -0.0310 -0.1642 0.0714 291 ALA A CA 2258 C C . ALA A 291 ? 1.1899 0.9472 1.4258 -0.0326 -0.1413 0.0647 291 ALA A C 2259 O O . ALA A 291 ? 1.2416 1.0287 1.4884 -0.0138 -0.1218 0.0413 291 ALA A O 2260 C CB . ALA A 291 ? 1.2374 0.9107 1.4588 -0.0399 -0.1639 0.0591 291 ALA A CB 2261 N N . ASP A 292 ? 1.1685 0.9295 1.3758 -0.0560 -0.1442 0.0853 292 ASP A N 2262 C CA . ASP A 292 ? 1.1577 0.9562 1.3518 -0.0605 -0.1262 0.0851 292 ASP A CA 2263 C C . ASP A 292 ? 1.1114 0.8899 1.2526 -0.0815 -0.1191 0.0843 292 ASP A C 2264 O O . ASP A 292 ? 1.0611 0.8022 1.1749 -0.0987 -0.1314 0.0919 292 ASP A O 2265 C CB . ASP A 292 ? 1.1533 0.9787 1.3711 -0.0682 -0.1360 0.1091 292 ASP A CB 2266 C CG . ASP A 292 ? 1.2073 1.0460 1.4802 -0.0504 -0.1491 0.1156 292 ASP A CG 2267 O OD1 . ASP A 292 ? 1.1886 1.0055 1.4695 -0.0607 -0.1730 0.1355 292 ASP A OD1 2268 O OD2 . ASP A 292 ? 1.2953 1.1686 1.6045 -0.0257 -0.1355 0.1008 292 ASP A OD2 2269 N N . VAL A 293 ? 1.1191 0.9254 1.2480 -0.0800 -0.0992 0.0762 293 VAL A N 2270 C CA . VAL A 293 ? 1.0764 0.8665 1.1622 -0.0950 -0.0903 0.0724 293 VAL A CA 2271 C C . VAL A 293 ? 1.0302 0.8249 1.1014 -0.1154 -0.0913 0.0896 293 VAL A C 2272 O O . VAL A 293 ? 1.1680 0.9971 1.2606 -0.1144 -0.0870 0.0996 293 VAL A O 2273 C CB . VAL A 293 ? 1.1240 0.9396 1.2038 -0.0816 -0.0692 0.0534 293 VAL A CB 2274 C CG1 . VAL A 293 ? 1.2401 1.0401 1.2809 -0.0962 -0.0615 0.0517 293 VAL A CG1 2275 C CG2 . VAL A 293 ? 1.2136 1.0226 1.3064 -0.0619 -0.0683 0.0305 293 VAL A CG2 2276 N N . PHE A 294 ? 0.9839 0.7446 1.0206 -0.1341 -0.0966 0.0921 294 PHE A N 2277 C CA . PHE A 294 ? 1.0974 0.8560 1.1181 -0.1534 -0.0970 0.1023 294 PHE A CA 2278 C C . PHE A 294 ? 1.0583 0.8079 1.0509 -0.1583 -0.0823 0.0927 294 PHE A C 2279 O O . PHE A 294 ? 1.2468 0.9719 1.2160 -0.1598 -0.0808 0.0826 294 PHE A O 2280 C CB . PHE A 294 ? 0.9980 0.7287 1.0028 -0.1723 -0.1161 0.1124 294 PHE A CB 2281 C CG . PHE A 294 ? 1.0283 0.7711 1.0631 -0.1707 -0.1335 0.1268 294 PHE A CG 2282 C CD1 . PHE A 294 ? 0.9698 0.7062 1.0230 -0.1584 -0.1434 0.1279 294 PHE A CD1 2283 C CD2 . PHE A 294 ? 1.1223 0.8823 1.1708 -0.1819 -0.1413 0.1401 294 PHE A CD2 2284 C CE1 . PHE A 294 ? 1.0714 0.8207 1.1574 -0.1558 -0.1605 0.1431 294 PHE A CE1 2285 C CE2 . PHE A 294 ? 0.9599 0.7344 1.0387 -0.1810 -0.1585 0.1551 294 PHE A CE2 2286 C CZ . PHE A 294 ? 1.0425 0.8127 1.1407 -0.1672 -0.1679 0.1572 294 PHE A CZ 2287 N N . ILE A 295 ? 0.9083 0.6789 0.9071 -0.1614 -0.0726 0.0981 295 ILE A N 2288 C CA . ILE A 295 ? 0.8887 0.6550 0.8686 -0.1645 -0.0593 0.0921 295 ILE A CA 2289 C C . ILE A 295 ? 1.0302 0.7878 1.0066 -0.1812 -0.0606 0.1003 295 ILE A C 2290 O O . ILE A 295 ? 1.1481 0.9271 1.1482 -0.1843 -0.0617 0.1131 295 ILE A O 2291 C CB . ILE A 295 ? 0.9103 0.7143 0.9040 -0.1493 -0.0440 0.0903 295 ILE A CB 2292 C CG1 . ILE A 295 ? 0.9591 0.7727 0.9587 -0.1314 -0.0423 0.0766 295 ILE A CG1 2293 C CG2 . ILE A 295 ? 0.8779 0.6777 0.8539 -0.1529 -0.0330 0.0869 295 ILE A CG2 2294 C CD1 . ILE A 295 ? 1.0095 0.8703 1.0253 -0.1157 -0.0282 0.0737 295 ILE A CD1 2295 N N . GLY A 296 ? 0.9543 0.6814 0.9040 -0.1919 -0.0601 0.0921 296 GLY A N 2296 C CA . GLY A 296 ? 1.0252 0.7395 0.9721 -0.2063 -0.0606 0.0941 296 GLY A CA 2297 C C . GLY A 296 ? 1.0931 0.8191 1.0504 -0.2026 -0.0472 0.0968 296 GLY A C 2298 O O . GLY A 296 ? 1.0615 0.7945 1.0117 -0.1928 -0.0366 0.0917 296 GLY A O 2299 N N . ALA A 297 ? 1.1844 0.9123 1.1607 -0.2116 -0.0494 0.1062 297 ALA A N 2300 C CA . ALA A 297 ? 1.0851 0.8193 1.0761 -0.2108 -0.0399 0.1125 297 ALA A CA 2301 C C . ALA A 297 ? 1.1282 0.8365 1.1272 -0.2260 -0.0463 0.1108 297 ALA A C 2302 O O . ALA A 297 ? 1.2354 0.9542 1.2639 -0.2323 -0.0513 0.1256 297 ALA A O 2303 C CB . ALA A 297 ? 0.8092 0.5860 0.8291 -0.2028 -0.0348 0.1322 297 ALA A CB 2304 N N . PRO A 298 ? 1.0412 0.7169 1.0152 -0.2325 -0.0461 0.0918 298 PRO A N 2305 C CA . PRO A 298 ? 1.1519 0.7995 1.1264 -0.2473 -0.0532 0.0814 298 PRO A CA 2306 C C . PRO A 298 ? 1.1633 0.8065 1.1720 -0.2496 -0.0507 0.0888 298 PRO A C 2307 O O . PRO A 298 ? 1.3351 0.9591 1.3557 -0.2624 -0.0598 0.0834 298 PRO A O 2308 C CB . PRO A 298 ? 1.1902 0.8137 1.1290 -0.2492 -0.0475 0.0587 298 PRO A CB 2309 C CG . PRO A 298 ? 1.0895 0.7266 1.0222 -0.2349 -0.0351 0.0610 298 PRO A CG 2310 C CD . PRO A 298 ? 0.7672 0.4335 0.7118 -0.2260 -0.0378 0.0778 298 PRO A CD 2311 N N . LEU A 299 ? 0.9636 0.6242 0.9891 -0.2382 -0.0399 0.1011 299 LEU A N 2312 C CA . LEU A 299 ? 0.9542 0.6107 1.0162 -0.2398 -0.0384 0.1125 299 LEU A CA 2313 C C . LEU A 299 ? 0.9190 0.6067 1.0177 -0.2415 -0.0431 0.1430 299 LEU A C 2314 O O . LEU A 299 ? 0.9905 0.6800 1.1243 -0.2434 -0.0431 0.1597 299 LEU A O 2315 C CB . LEU A 299 ? 0.9025 0.5613 0.9649 -0.2282 -0.0256 0.1116 299 LEU A CB 2316 C CG . LEU A 299 ? 0.7882 0.4204 0.8203 -0.2269 -0.0190 0.0832 299 LEU A CG 2317 C CD1 . LEU A 299 ? 0.8607 0.4962 0.9044 -0.2164 -0.0078 0.0851 299 LEU A CD1 2318 C CD2 . LEU A 299 ? 0.8189 0.4158 0.8482 -0.2393 -0.0253 0.0617 299 LEU A CD2 2319 N N . PHE A 300 ? 0.9725 0.6869 1.0659 -0.2407 -0.0469 0.1516 300 PHE A N 2320 C CA . PHE A 300 ? 0.7574 0.5096 0.8846 -0.2423 -0.0494 0.1807 300 PHE A CA 2321 C C . PHE A 300 ? 0.7769 0.5138 0.9407 -0.2587 -0.0615 0.1918 300 PHE A C 2322 O O . PHE A 300 ? 0.9963 0.7008 1.1536 -0.2705 -0.0726 0.1745 300 PHE A O 2323 C CB . PHE A 300 ? 1.0748 0.8551 1.1926 -0.2384 -0.0520 0.1827 300 PHE A CB 2324 C CG . PHE A 300 ? 1.0275 0.8530 1.1807 -0.2399 -0.0529 0.2114 300 PHE A CG 2325 C CD1 . PHE A 300 ? 0.7671 0.6387 0.9272 -0.2280 -0.0404 0.2279 300 PHE A CD1 2326 C CD2 . PHE A 300 ? 1.1844 1.0104 1.3636 -0.2543 -0.0664 0.2219 300 PHE A CD2 2327 C CE1 . PHE A 300 ? 0.7387 0.6586 0.9305 -0.2299 -0.0392 0.2549 300 PHE A CE1 2328 C CE2 . PHE A 300 ? 0.8470 0.7194 1.0617 -0.2566 -0.0664 0.2503 300 PHE A CE2 2329 C CZ . PHE A 300 ? 0.8328 0.7536 1.0536 -0.2441 -0.0517 0.2672 300 PHE A CZ 2330 N N . MET A 301 ? 0.7739 0.5352 0.9763 -0.2606 -0.0603 0.2213 301 MET A N 2331 C CA . MET A 301 ? 0.8376 0.5852 1.0826 -0.2771 -0.0730 0.2361 301 MET A CA 2332 C C . MET A 301 ? 1.0444 0.8363 1.3183 -0.2843 -0.0783 0.2657 301 MET A C 2333 O O . MET A 301 ? 1.2547 1.0941 1.5435 -0.2780 -0.0694 0.2932 301 MET A O 2334 C CB . MET A 301 ? 0.8028 0.5399 1.0797 -0.2769 -0.0703 0.2516 301 MET A CB 2335 C CG . MET A 301 ? 0.8118 0.5075 1.0693 -0.2693 -0.0645 0.2234 301 MET A CG 2336 S SD . MET A 301 ? 1.0952 0.7777 1.3992 -0.2665 -0.0639 0.2404 301 MET A SD 2337 C CE . MET A 301 ? 0.7997 0.5451 1.1154 -0.2594 -0.0550 0.2852 301 MET A CE 2338 N N . ASP A 302 ? 0.9685 0.7486 1.2502 -0.2981 -0.0928 0.2601 302 ASP A N 2339 C CA . ASP A 302 ? 1.0766 0.8989 1.3916 -0.3068 -0.0993 0.2883 302 ASP A CA 2340 C C . ASP A 302 ? 1.1367 0.9535 1.4951 -0.3180 -0.1092 0.3042 302 ASP A C 2341 O O . ASP A 302 ? 0.9278 0.7072 1.2891 -0.3163 -0.1104 0.2905 302 ASP A O 2342 C CB . ASP A 302 ? 1.0651 0.8868 1.3640 -0.3115 -0.1101 0.2732 302 ASP A CB 2343 C CG . ASP A 302 ? 1.2220 0.9986 1.5286 -0.3322 -0.1303 0.2579 302 ASP A CG 2344 O OD1 . ASP A 302 ? 1.3204 1.0559 1.6188 -0.3316 -0.1301 0.2367 302 ASP A OD1 2345 O OD2 . ASP A 302 ? 1.3750 1.1639 1.6910 -0.3427 -0.1439 0.2611 302 ASP A OD2 2346 N N . ARG A 303 ? 1.0699 0.9267 1.4609 -0.3256 -0.1154 0.3298 303 ARG A N 2347 C CA . ARG A 303 ? 0.8453 0.7011 1.2756 -0.3337 -0.1257 0.3438 303 ARG A CA 2348 C C . ARG A 303 ? 0.9219 0.7447 1.3550 -0.3476 -0.1445 0.3225 303 ARG A C 2349 O O . ARG A 303 ? 0.9744 0.8115 1.4011 -0.3542 -0.1520 0.3202 303 ARG A O 2350 C CB . ARG A 303 ? 1.3401 1.2625 1.8064 -0.3351 -0.1220 0.3863 303 ARG A CB 2351 C CG . ARG A 303 ? 0.9772 0.9386 1.4425 -0.3232 -0.1042 0.4101 303 ARG A CG 2352 C CD . ARG A 303 ? 0.8343 0.7698 1.3132 -0.3197 -0.1056 0.4139 303 ARG A CD 2353 N NE . ARG A 303 ? 0.9503 0.9261 1.4268 -0.3093 -0.0910 0.4381 303 ARG A NE 2354 C CZ . ARG A 303 ? 1.1092 1.0797 1.6035 -0.3055 -0.0919 0.4523 303 ARG A CZ 2355 N NH1 . ARG A 303 ? 1.0253 0.9502 1.5444 -0.3105 -0.1056 0.4440 303 ARG A NH1 2356 N NH2 . ARG A 303 ? 1.3777 1.3902 1.8662 -0.2971 -0.0798 0.4749 303 ARG A NH2 2357 N N . GLY A 304 ? 1.0457 0.8257 1.4898 -0.3523 -0.1527 0.3070 304 GLY A N 2358 C CA . GLY A 304 ? 1.1181 0.8683 1.5666 -0.3670 -0.1706 0.2865 304 GLY A CA 2359 C C . GLY A 304 ? 1.1597 0.9458 1.6519 -0.3788 -0.1830 0.3166 304 GLY A C 2360 O O . GLY A 304 ? 0.9594 0.7949 1.4776 -0.3750 -0.1763 0.3533 304 GLY A O 2361 N N . SER A 305 ? 1.3503 1.1143 1.8499 -0.3938 -0.2011 0.3013 305 SER A N 2362 C CA . SER A 305 ? 1.2890 1.0838 1.8318 -0.4069 -0.2153 0.3284 305 SER A CA 2363 C C . SER A 305 ? 1.0116 0.8132 1.5980 -0.4065 -0.2148 0.3552 305 SER A C 2364 O O . SER A 305 ? 1.0100 0.8567 1.6342 -0.4119 -0.2190 0.3917 305 SER A O 2365 C CB . SER A 305 ? 1.3245 1.0880 1.8643 -0.4242 -0.2360 0.3028 305 SER A CB 2366 O OG . SER A 305 ? 1.6812 1.3872 2.2143 -0.4268 -0.2391 0.2708 305 SER A OG 2367 N N . ASP A 306 ? 1.1602 0.9188 1.7429 -0.4001 -0.2102 0.3382 306 ASP A N 2368 C CA . ASP A 306 ? 1.2454 1.0055 1.8706 -0.3990 -0.2117 0.3632 306 ASP A CA 2369 C C . ASP A 306 ? 1.2749 1.0802 1.9044 -0.3850 -0.1952 0.3970 306 ASP A C 2370 O O . ASP A 306 ? 1.2579 1.0811 1.9246 -0.3843 -0.1968 0.4280 306 ASP A O 2371 C CB . ASP A 306 ? 1.2504 0.9466 1.8749 -0.3973 -0.2143 0.3312 306 ASP A CB 2372 C CG . ASP A 306 ? 1.6647 1.3313 2.2416 -0.3840 -0.1993 0.2974 306 ASP A CG 2373 O OD1 . ASP A 306 ? 1.5621 1.2457 2.1013 -0.3806 -0.1920 0.2894 306 ASP A OD1 2374 O OD2 . ASP A 306 ? 1.7678 1.3948 2.3476 -0.3771 -0.1955 0.2796 306 ASP A OD2 2375 N N . GLY A 307 ? 1.1330 0.9580 1.7246 -0.3746 -0.1803 0.3912 307 GLY A N 2376 C CA . GLY A 307 ? 0.9444 0.8155 1.5339 -0.3621 -0.1638 0.4196 307 GLY A CA 2377 C C . GLY A 307 ? 1.1312 0.9722 1.6988 -0.3482 -0.1522 0.4042 307 GLY A C 2378 O O . GLY A 307 ? 1.3186 1.1942 1.8794 -0.3376 -0.1386 0.4242 307 GLY A O 2379 N N . LYS A 308 ? 1.1354 0.9145 1.6924 -0.3485 -0.1573 0.3682 308 LYS A N 2380 C CA . LYS A 308 ? 0.9607 0.7087 1.4998 -0.3353 -0.1467 0.3509 308 LYS A CA 2381 C C . LYS A 308 ? 0.9321 0.6718 1.4192 -0.3279 -0.1347 0.3241 308 LYS A C 2382 O O . LYS A 308 ? 1.2699 0.9989 1.7330 -0.3349 -0.1395 0.3024 308 LYS A O 2383 C CB . LYS A 308 ? 1.0037 0.6917 1.5580 -0.3382 -0.1558 0.3233 308 LYS A CB 2384 C CG . LYS A 308 ? 1.7538 1.4118 2.2990 -0.3240 -0.1454 0.3079 308 LYS A CG 2385 C CD . LYS A 308 ? 1.7481 1.3467 2.3077 -0.3264 -0.1531 0.2754 308 LYS A CD 2386 C CE . LYS A 308 ? 1.8285 1.3995 2.3810 -0.3112 -0.1419 0.2586 308 LYS A CE 2387 N NZ . LYS A 308 ? 1.7305 1.2443 2.2964 -0.3124 -0.1476 0.2226 308 LYS A NZ 2388 N N . LEU A 309 ? 0.9113 0.6575 1.3828 -0.3144 -0.1208 0.3276 309 LEU A N 2389 C CA . LEU A 309 ? 1.0273 0.7646 1.4518 -0.3070 -0.1096 0.3043 309 LEU A CA 2390 C C . LEU A 309 ? 1.0733 0.7522 1.4724 -0.3095 -0.1131 0.2587 309 LEU A C 2391 O O . LEU A 309 ? 1.1904 0.8316 1.6071 -0.3106 -0.1180 0.2432 309 LEU A O 2392 C CB . LEU A 309 ? 0.8663 0.6195 1.2837 -0.2931 -0.0955 0.3174 309 LEU A CB 2393 C CG . LEU A 309 ? 0.8420 0.6605 1.2694 -0.2897 -0.0879 0.3584 309 LEU A CG 2394 C CD1 . LEU A 309 ? 0.8300 0.6588 1.2504 -0.2773 -0.0767 0.3683 309 LEU A CD1 2395 C CD2 . LEU A 309 ? 0.9614 0.8132 1.3638 -0.2920 -0.0826 0.3597 309 LEU A CD2 2396 N N . GLN A 310 ? 0.8933 0.5669 1.2517 -0.3106 -0.1107 0.2376 310 GLN A N 2397 C CA . GLN A 310 ? 1.2535 0.8790 1.5804 -0.3134 -0.1126 0.1948 310 GLN A CA 2398 C C . GLN A 310 ? 1.3195 0.9472 1.6003 -0.3081 -0.1043 0.1816 310 GLN A C 2399 O O . GLN A 310 ? 1.3767 1.0389 1.6480 -0.3080 -0.1035 0.1994 310 GLN A O 2400 C CB . GLN A 310 ? 1.1271 0.7379 1.4562 -0.3292 -0.1287 0.1792 310 GLN A CB 2401 C CG . GLN A 310 ? 1.1203 0.7681 1.4453 -0.3370 -0.1367 0.1968 310 GLN A CG 2402 C CD . GLN A 310 ? 1.3292 0.9663 1.6632 -0.3536 -0.1549 0.1859 310 GLN A CD 2403 O OE1 . GLN A 310 ? 1.1726 0.7778 1.5217 -0.3601 -0.1616 0.1689 310 GLN A OE1 2404 N NE2 . GLN A 310 ? 1.3704 1.0347 1.6968 -0.3609 -0.1638 0.1954 310 GLN A NE2 2405 N N . GLU A 311 ? 1.4045 0.9961 1.6583 -0.3040 -0.0984 0.1503 311 GLU A N 2406 C CA . GLU A 311 ? 1.2613 0.8522 1.4704 -0.2997 -0.0914 0.1379 311 GLU A CA 2407 C C . GLU A 311 ? 1.1653 0.7481 1.3378 -0.3097 -0.1012 0.1161 311 GLU A C 2408 O O . GLU A 311 ? 1.3362 0.8861 1.4976 -0.3200 -0.1087 0.0880 311 GLU A O 2409 C CB . GLU A 311 ? 1.2269 0.7916 1.4209 -0.2885 -0.0787 0.1143 311 GLU A CB 2410 C CG . GLU A 311 ? 1.3253 0.8980 1.4662 -0.2776 -0.0670 0.0961 311 GLU A CG 2411 C CD . GLU A 311 ? 1.5507 1.1034 1.6820 -0.2670 -0.0537 0.0757 311 GLU A CD 2412 O OE1 . GLU A 311 ? 1.6382 1.1796 1.7279 -0.2660 -0.0481 0.0487 311 GLU A OE1 2413 O OE2 . GLU A 311 ? 1.5907 1.1419 1.7583 -0.2601 -0.0491 0.0888 311 GLU A OE2 2414 N N . VAL A 312 ? 1.1462 0.7629 1.3001 -0.3050 -0.1005 0.1283 312 VAL A N 2415 C CA . VAL A 312 ? 1.2267 0.8433 1.3519 -0.3140 -0.1120 0.1163 312 VAL A CA 2416 C C . VAL A 312 ? 1.0552 0.6850 1.1382 -0.3002 -0.1021 0.1091 312 VAL A C 2417 O O . VAL A 312 ? 1.2313 0.8415 1.2753 -0.3036 -0.1036 0.0857 312 VAL A O 2418 C CB . VAL A 312 ? 1.1819 0.8278 1.3381 -0.3236 -0.1257 0.1418 312 VAL A CB 2419 C CG1 . VAL A 312 ? 0.9048 0.5283 1.0874 -0.3428 -0.1422 0.1363 312 VAL A CG1 2420 C CG2 . VAL A 312 ? 1.2780 0.9654 1.4679 -0.3128 -0.1159 0.1753 312 VAL A CG2 2421 N N . GLY A 313 ? 0.8992 0.5640 0.9915 -0.2857 -0.0923 0.1296 313 GLY A N 2422 C CA . GLY A 313 ? 1.0989 0.7780 1.1598 -0.2721 -0.0843 0.1250 313 GLY A CA 2423 C C . GLY A 313 ? 1.2663 0.9792 1.3375 -0.2691 -0.0907 0.1412 313 GLY A C 2424 O O . GLY A 313 ? 1.3147 1.0345 1.4067 -0.2811 -0.1045 0.1508 313 GLY A O 2425 N N . GLN A 314 ? 1.1289 0.8635 1.1883 -0.2528 -0.0811 0.1430 314 GLN A N 2426 C CA . GLN A 314 ? 0.9674 0.7388 1.0430 -0.2451 -0.0836 0.1571 314 GLN A CA 2427 C C . GLN A 314 ? 0.9374 0.7093 0.9867 -0.2315 -0.0801 0.1453 314 GLN A C 2428 O O . GLN A 314 ? 0.9828 0.7438 1.0097 -0.2229 -0.0693 0.1337 314 GLN A O 2429 C CB . GLN A 314 ? 1.0097 0.8231 1.1180 -0.2368 -0.0727 0.1785 314 GLN A CB 2430 C CG . GLN A 314 ? 1.0175 0.8761 1.1516 -0.2302 -0.0741 0.1941 314 GLN A CG 2431 C CD . GLN A 314 ? 0.9187 0.8242 1.0839 -0.2255 -0.0626 0.2172 314 GLN A CD 2432 O OE1 . GLN A 314 ? 0.9179 0.8421 1.0740 -0.2129 -0.0478 0.2167 314 GLN A OE1 2433 N NE2 . GLN A 314 ? 1.1307 1.0583 1.3330 -0.2374 -0.0702 0.2389 314 GLN A NE2 2434 N N . VAL A 315 ? 0.8970 0.6811 0.9530 -0.2300 -0.0906 0.1495 315 VAL A N 2435 C CA . VAL A 315 ? 0.9763 0.7599 1.0163 -0.2168 -0.0900 0.1408 315 VAL A CA 2436 C C . VAL A 315 ? 1.1560 0.9827 1.2264 -0.2001 -0.0852 0.1507 315 VAL A C 2437 O O . VAL A 315 ? 1.1298 0.9808 1.2302 -0.2032 -0.0932 0.1649 315 VAL A O 2438 C CB . VAL A 315 ? 0.9499 0.7085 0.9716 -0.2278 -0.1080 0.1364 315 VAL A CB 2439 C CG1 . VAL A 315 ? 0.9743 0.7316 0.9877 -0.2141 -0.1093 0.1315 315 VAL A CG1 2440 C CG2 . VAL A 315 ? 0.9721 0.6931 0.9599 -0.2438 -0.1102 0.1229 315 VAL A CG2 2441 N N . SER A 316 ? 1.1683 1.0064 1.2319 -0.1826 -0.0718 0.1416 316 SER A N 2442 C CA . SER A 316 ? 1.0404 0.9215 1.1304 -0.1644 -0.0643 0.1449 316 SER A CA 2443 C C . SER A 316 ? 1.0840 0.9573 1.1785 -0.1545 -0.0745 0.1376 316 SER A C 2444 O O . SER A 316 ? 1.1795 1.0243 1.2509 -0.1499 -0.0758 0.1232 316 SER A O 2445 C CB . SER A 316 ? 0.9473 0.8477 1.0279 -0.1506 -0.0456 0.1361 316 SER A CB 2446 O OG . SER A 316 ? 1.0000 0.9473 1.1043 -0.1330 -0.0361 0.1360 316 SER A OG 2447 N N . VAL A 317 ? 0.9763 0.8757 1.1046 -0.1518 -0.0826 0.1496 317 VAL A N 2448 C CA . VAL A 317 ? 1.0129 0.9085 1.1556 -0.1410 -0.0939 0.1463 317 VAL A CA 2449 C C . VAL A 317 ? 1.0687 1.0060 1.2411 -0.1156 -0.0804 0.1389 317 VAL A C 2450 O O . VAL A 317 ? 1.0896 1.0733 1.2953 -0.1106 -0.0743 0.1500 317 VAL A O 2451 C CB . VAL A 317 ? 0.9892 0.8870 1.1534 -0.1540 -0.1145 0.1642 317 VAL A CB 2452 C CG1 . VAL A 317 ? 1.0237 0.9225 1.2112 -0.1406 -0.1270 0.1646 317 VAL A CG1 2453 C CG2 . VAL A 317 ? 0.9405 0.7978 1.0712 -0.1793 -0.1282 0.1664 317 VAL A CG2 2454 N N . SER A 318 ? 1.0997 1.0219 1.2610 -0.1001 -0.0756 0.1190 318 SER A N 2455 C CA . SER A 318 ? 1.1764 1.1354 1.3616 -0.0748 -0.0613 0.1044 318 SER A CA 2456 C C . SER A 318 ? 1.2212 1.1685 1.4334 -0.0590 -0.0733 0.0967 318 SER A C 2457 O O . SER A 318 ? 1.2110 1.1152 1.4068 -0.0584 -0.0825 0.0861 318 SER A O 2458 C CB . SER A 318 ? 1.1976 1.1529 1.3527 -0.0678 -0.0452 0.0838 318 SER A CB 2459 O OG . SER A 318 ? 1.1510 1.1152 1.2846 -0.0821 -0.0360 0.0937 318 SER A OG 2460 N N . LEU A 319 ? 1.2625 1.2498 1.5203 -0.0464 -0.0736 0.1038 319 LEU A N 2461 C CA . LEU A 319 ? 1.2983 1.2789 1.5927 -0.0291 -0.0857 0.0988 319 LEU A CA 2462 C C . LEU A 319 ? 1.3754 1.3752 1.6865 -0.0001 -0.0693 0.0688 319 LEU A C 2463 O O . LEU A 319 ? 1.4144 1.4675 1.7390 0.0126 -0.0487 0.0606 319 LEU A O 2464 C CB . LEU A 319 ? 1.3070 1.3228 1.6481 -0.0290 -0.0955 0.1212 319 LEU A CB 2465 C CG . LEU A 319 ? 1.2306 1.2314 1.5594 -0.0582 -0.1141 0.1489 319 LEU A CG 2466 C CD1 . LEU A 319 ? 1.2467 1.2865 1.6271 -0.0570 -0.1251 0.1702 319 LEU A CD1 2467 C CD2 . LEU A 319 ? 1.1717 1.1119 1.4681 -0.0733 -0.1350 0.1516 319 LEU A CD2 2468 N N . GLN A 320 ? 1.3661 1.3235 1.6765 0.0093 -0.0788 0.0524 320 GLN A N 2469 C CA . GLN A 320 ? 1.4034 1.3708 1.7311 0.0367 -0.0662 0.0192 320 GLN A CA 2470 C C . GLN A 320 ? 1.4116 1.4093 1.8025 0.0618 -0.0683 0.0155 320 GLN A C 2471 O O . GLN A 320 ? 1.3841 1.3657 1.8052 0.0590 -0.0894 0.0363 320 GLN A O 2472 C CB . GLN A 320 ? 1.4657 1.3724 1.7725 0.0356 -0.0774 0.0033 320 GLN A CB 2473 C CG . GLN A 320 ? 1.4573 1.3665 1.7828 0.0627 -0.0674 -0.0349 320 GLN A CG 2474 C CD . GLN A 320 ? 1.3637 1.2091 1.6817 0.0606 -0.0840 -0.0458 320 GLN A CD 2475 O OE1 . GLN A 320 ? 1.3809 1.2173 1.7068 0.0778 -0.0784 -0.0789 320 GLN A OE1 2476 N NE2 . GLN A 320 ? 1.3145 1.1168 1.6175 0.0384 -0.1051 -0.0179 320 GLN A NE2 2477 N N . ARG A 321 ? 1.4371 1.4820 1.8487 0.0863 -0.0462 -0.0112 321 ARG A N 2478 C CA . ARG A 321 ? 1.4731 1.5510 1.9487 0.1145 -0.0443 -0.0211 321 ARG A CA 2479 C C . ARG A 321 ? 1.5614 1.6195 2.0534 0.1415 -0.0400 -0.0630 321 ARG A C 2480 O O . ARG A 321 ? 1.4607 1.4809 1.9128 0.1359 -0.0394 -0.0823 321 ARG A O 2481 C CB . ARG A 321 ? 1.4277 1.5875 1.9232 0.1229 -0.0207 -0.0181 321 ARG A CB 2482 C CG . ARG A 321 ? 1.4073 1.5885 1.9046 0.0987 -0.0284 0.0242 321 ARG A CG 2483 C CD . ARG A 321 ? 1.4460 1.5985 1.9807 0.0944 -0.0572 0.0490 321 ARG A CD 2484 N NE . ARG A 321 ? 1.4728 1.6424 2.0074 0.0691 -0.0673 0.0869 321 ARG A NE 2485 C CZ . ARG A 321 ? 1.4443 1.5948 2.0026 0.0580 -0.0940 0.1138 321 ARG A CZ 2486 N NH1 . ARG A 321 ? 1.4988 1.6131 2.0842 0.0703 -0.1133 0.1108 321 ARG A NH1 2487 N NH2 . ARG A 321 ? 1.3090 1.4767 1.8651 0.0337 -0.1028 0.1445 321 ARG A NH2 2488 N N . ALA A 322 ? 1.6630 1.7470 2.2171 0.1708 -0.0375 -0.0778 322 ALA A N 2489 C CA . ALA A 322 ? 1.5548 1.6166 2.1357 0.1988 -0.0359 -0.1199 322 ALA A CA 2490 C C . ALA A 322 ? 1.5523 1.6462 2.1005 0.2097 -0.0079 -0.1622 322 ALA A C 2491 O O . ALA A 322 ? 1.5331 1.5913 2.0744 0.2205 -0.0090 -0.1979 322 ALA A O 2492 C CB . ALA A 322 ? 1.5545 1.6424 2.2157 0.2294 -0.0384 -0.1260 322 ALA A CB 2493 N N . SER A 323 ? 1.5732 1.7359 2.1016 0.2054 0.0159 -0.1566 323 SER A N 2494 C CA . SER A 323 ? 1.6079 1.8137 2.1032 0.2141 0.0431 -0.1923 323 SER A CA 2495 C C . SER A 323 ? 1.7013 1.8706 2.1267 0.1885 0.0404 -0.1910 323 SER A C 2496 O O . SER A 323 ? 1.7387 1.9172 2.1348 0.1951 0.0537 -0.2265 323 SER A O 2497 C CB . SER A 323 ? 1.4725 1.7702 1.9738 0.2165 0.0687 -0.1808 323 SER A CB 2498 O OG . SER A 323 ? 1.4326 1.7351 1.9083 0.1856 0.0626 -0.1331 323 SER A OG 2499 N N . GLY A 324 ? 1.7050 1.8351 2.1050 0.1595 0.0229 -0.1513 324 GLY A N 2500 C CA . GLY A 324 ? 1.7406 1.8389 2.0791 0.1348 0.0204 -0.1456 324 GLY A CA 2501 C C . GLY A 324 ? 1.6155 1.7560 1.9230 0.1136 0.0319 -0.1148 324 GLY A C 2502 O O . GLY A 324 ? 1.5236 1.6396 1.7854 0.0912 0.0286 -0.1022 324 GLY A O 2503 N N . ASP A 325 ? 1.6660 1.8710 2.0027 0.1209 0.0451 -0.1019 325 ASP A N 2504 C CA . ASP A 325 ? 1.5927 1.8382 1.9106 0.1000 0.0536 -0.0677 325 ASP A CA 2505 C C . ASP A 325 ? 1.5403 1.7458 1.8632 0.0771 0.0315 -0.0284 325 ASP A C 2506 O O . ASP A 325 ? 1.6121 1.8029 1.9748 0.0830 0.0168 -0.0193 325 ASP A O 2507 C CB . ASP A 325 ? 1.6236 1.9566 1.9738 0.1144 0.0758 -0.0662 325 ASP A CB 2508 C CG . ASP A 325 ? 1.7581 2.1413 2.0942 0.1339 0.1005 -0.1050 325 ASP A CG 2509 O OD1 . ASP A 325 ? 1.7333 2.1950 2.0729 0.1364 0.1223 -0.0984 325 ASP A OD1 2510 O OD2 . ASP A 325 ? 1.8896 2.2356 2.2106 0.1453 0.0976 -0.1418 325 ASP A OD2 2511 N N . PHE A 326 ? 1.4585 1.6479 1.7421 0.0511 0.0286 -0.0060 326 PHE A N 2512 C CA . PHE A 326 ? 1.4259 1.5731 1.7060 0.0276 0.0078 0.0255 326 PHE A CA 2513 C C . PHE A 326 ? 1.3765 1.5681 1.6802 0.0157 0.0096 0.0584 326 PHE A C 2514 O O . PHE A 326 ? 1.3518 1.5970 1.6525 0.0134 0.0273 0.0664 326 PHE A O 2515 C CB . PHE A 326 ? 1.4179 1.5183 1.6466 0.0062 0.0024 0.0294 326 PHE A CB 2516 C CG . PHE A 326 ? 1.4500 1.4939 1.6588 0.0107 -0.0070 0.0058 326 PHE A CG 2517 C CD1 . PHE A 326 ? 1.4013 1.3870 1.6064 -0.0011 -0.0290 0.0161 326 PHE A CD1 2518 C CD2 . PHE A 326 ? 1.4818 1.5333 1.6755 0.0250 0.0054 -0.0257 326 PHE A CD2 2519 C CE1 . PHE A 326 ? 1.3742 1.3103 1.5639 0.0009 -0.0381 -0.0017 326 PHE A CE1 2520 C CE2 . PHE A 326 ? 1.4693 1.4682 1.6485 0.0272 -0.0049 -0.0463 326 PHE A CE2 2521 C CZ . PHE A 326 ? 1.4108 1.3518 1.5895 0.0149 -0.0264 -0.0327 326 PHE A CZ 2522 N N . GLN A 327 ? 1.3579 1.5278 1.6856 0.0067 -0.0104 0.0790 327 GLN A N 2523 C CA . GLN A 327 ? 1.3107 1.5103 1.6588 -0.0104 -0.0145 0.1119 327 GLN A CA 2524 C C . GLN A 327 ? 1.2696 1.4184 1.5818 -0.0398 -0.0299 0.1294 327 GLN A C 2525 O O . GLN A 327 ? 1.3687 1.4658 1.6717 -0.0486 -0.0504 0.1314 327 GLN A O 2526 C CB . GLN A 327 ? 1.3404 1.5556 1.7416 -0.0022 -0.0278 0.1231 327 GLN A CB 2527 C CG . GLN A 327 ? 1.3753 1.6107 1.7975 -0.0241 -0.0386 0.1579 327 GLN A CG 2528 C CD . GLN A 327 ? 1.4304 1.6737 1.9025 -0.0185 -0.0569 0.1704 327 GLN A CD 2529 O OE1 . GLN A 327 ? 1.6682 1.9177 2.1705 0.0067 -0.0564 0.1541 327 GLN A OE1 2530 N NE2 . GLN A 327 ? 1.2510 1.4936 1.7345 -0.0421 -0.0745 0.1991 327 GLN A NE2 2531 N N . THR A 328 ? 1.2247 1.3901 1.5179 -0.0548 -0.0200 0.1423 328 THR A N 2532 C CA . THR A 328 ? 1.1703 1.2868 1.4280 -0.0793 -0.0307 0.1519 328 THR A CA 2533 C C . THR A 328 ? 1.1072 1.2336 1.3822 -0.1020 -0.0402 0.1813 328 THR A C 2534 O O . THR A 328 ? 1.0868 1.2659 1.3876 -0.1035 -0.0297 0.1982 328 THR A O 2535 C CB . THR A 328 ? 1.1616 1.2760 1.3824 -0.0805 -0.0151 0.1424 328 THR A CB 2536 O OG1 . THR A 328 ? 1.2216 1.3272 1.4266 -0.0611 -0.0076 0.1133 328 THR A OG1 2537 C CG2 . THR A 328 ? 1.0988 1.1599 1.2865 -0.1026 -0.0257 0.1486 328 THR A CG2 2538 N N . THR A 329 ? 1.0818 1.1585 1.3426 -0.1205 -0.0605 0.1869 329 THR A N 2539 C CA . THR A 329 ? 1.0151 1.0898 1.2865 -0.1449 -0.0721 0.2096 329 THR A CA 2540 C C . THR A 329 ? 0.9728 1.0008 1.2043 -0.1620 -0.0737 0.2055 329 THR A C 2541 O O . THR A 329 ? 1.1726 1.1742 1.3705 -0.1548 -0.0662 0.1874 329 THR A O 2542 C CB . THR A 329 ? 1.0118 1.0721 1.3018 -0.1544 -0.0962 0.2186 329 THR A CB 2543 O OG1 . THR A 329 ? 1.2436 1.3186 1.5552 -0.1327 -0.0976 0.2105 329 THR A OG1 2544 C CG2 . THR A 329 ? 1.0371 1.1321 1.3654 -0.1702 -0.1035 0.2444 329 THR A CG2 2545 N N . LYS A 330 ? 0.9274 0.9456 1.1658 -0.1843 -0.0838 0.2211 330 LYS A N 2546 C CA . LYS A 330 ? 0.8878 0.8618 1.0948 -0.1997 -0.0855 0.2156 330 LYS A CA 2547 C C . LYS A 330 ? 0.9856 0.9262 1.1914 -0.2233 -0.1069 0.2197 330 LYS A C 2548 O O . LYS A 330 ? 1.0753 1.0378 1.3146 -0.2346 -0.1175 0.2373 330 LYS A O 2549 C CB . LYS A 330 ? 0.8633 0.8617 1.0803 -0.2020 -0.0706 0.2286 330 LYS A CB 2550 C CG . LYS A 330 ? 0.9053 0.9310 1.1104 -0.1818 -0.0498 0.2205 330 LYS A CG 2551 C CD . LYS A 330 ? 1.1371 1.1765 1.3426 -0.1872 -0.0383 0.2337 330 LYS A CD 2552 C CE . LYS A 330 ? 1.1004 1.1644 1.2864 -0.1689 -0.0199 0.2227 330 LYS A CE 2553 N NZ . LYS A 330 ? 1.2585 1.3310 1.4406 -0.1750 -0.0114 0.2365 330 LYS A NZ 2554 N N . LEU A 331 ? 1.0572 0.9476 1.2243 -0.2314 -0.1133 0.2025 331 LEU A N 2555 C CA . LEU A 331 ? 0.9890 0.8469 1.1463 -0.2538 -0.1332 0.2002 331 LEU A CA 2556 C C . LEU A 331 ? 0.9889 0.8112 1.1267 -0.2668 -0.1300 0.1903 331 LEU A C 2557 O O . LEU A 331 ? 1.1399 0.9345 1.2436 -0.2619 -0.1213 0.1732 331 LEU A O 2558 C CB . LEU A 331 ? 0.9433 0.7768 1.0721 -0.2536 -0.1458 0.1884 331 LEU A CB 2559 C CG . LEU A 331 ? 1.2169 1.0252 1.3315 -0.2769 -0.1687 0.1861 331 LEU A CG 2560 C CD1 . LEU A 331 ? 1.4326 1.2702 1.5887 -0.2877 -0.1844 0.2056 331 LEU A CD1 2561 C CD2 . LEU A 331 ? 1.1619 0.9514 1.2461 -0.2752 -0.1790 0.1785 331 LEU A CD2 2562 N N . ASN A 332 ? 0.8519 0.6756 1.0157 -0.2833 -0.1376 0.2013 332 ASN A N 2563 C CA . ASN A 332 ? 0.8434 0.6336 1.0001 -0.2950 -0.1357 0.1926 332 ASN A CA 2564 C C . ASN A 332 ? 0.9785 0.7239 1.1041 -0.3119 -0.1501 0.1702 332 ASN A C 2565 O O . ASN A 332 ? 1.1634 0.9084 1.2843 -0.3231 -0.1679 0.1693 332 ASN A O 2566 C CB . ASN A 332 ? 0.8039 0.6129 1.0073 -0.3061 -0.1387 0.2150 332 ASN A CB 2567 C CG . ASN A 332 ? 0.9890 0.8404 1.2164 -0.2912 -0.1204 0.2359 332 ASN A CG 2568 O OD1 . ASN A 332 ? 1.2019 1.0731 1.4129 -0.2718 -0.1066 0.2320 332 ASN A OD1 2569 N ND2 . ASN A 332 ? 1.0389 0.9056 1.3054 -0.3013 -0.1210 0.2584 332 ASN A ND2 2570 N N . GLY A 333 ? 1.0063 0.7175 1.1111 -0.3137 -0.1422 0.1519 333 GLY A N 2571 C CA . GLY A 333 ? 1.1234 0.7950 1.1979 -0.3293 -0.1523 0.1268 333 GLY A CA 2572 C C . GLY A 333 ? 1.1833 0.8437 1.2834 -0.3511 -0.1700 0.1272 333 GLY A C 2573 O O . GLY A 333 ? 1.3179 1.0030 1.4613 -0.3554 -0.1762 0.1508 333 GLY A O 2574 N N . PHE A 334 ? 1.1332 0.7579 1.2071 -0.3657 -0.1781 0.1001 334 PHE A N 2575 C CA . PHE A 334 ? 1.1341 0.7453 1.2273 -0.3877 -0.1974 0.0941 334 PHE A CA 2576 C C . PHE A 334 ? 1.1566 0.7351 1.2542 -0.3871 -0.1890 0.0685 334 PHE A C 2577 O O . PHE A 334 ? 1.2831 0.8630 1.4244 -0.3862 -0.1880 0.0780 334 PHE A O 2578 C CB . PHE A 334 ? 1.2640 0.8727 1.3225 -0.4039 -0.2171 0.0813 334 PHE A CB 2579 C CG . PHE A 334 ? 1.0692 0.7115 1.1211 -0.3963 -0.2218 0.1026 334 PHE A CG 2580 C CD1 . PHE A 334 ? 1.3538 0.9957 1.3644 -0.3840 -0.2125 0.0958 334 PHE A CD1 2581 C CD2 . PHE A 334 ? 0.9903 0.6659 1.0821 -0.4003 -0.2352 0.1298 334 PHE A CD2 2582 C CE1 . PHE A 334 ? 1.3520 1.0215 1.3625 -0.3752 -0.2176 0.1147 334 PHE A CE1 2583 C CE2 . PHE A 334 ? 1.3110 1.0178 1.4027 -0.3901 -0.2389 0.1477 334 PHE A CE2 2584 C CZ . PHE A 334 ? 1.2875 0.9890 1.3394 -0.3771 -0.2306 0.1397 334 PHE A CZ 2585 N N . GLU A 335 ? 1.2879 0.8384 1.3424 -0.3879 -0.1830 0.0369 335 GLU A N 2586 C CA . GLU A 335 ? 1.1610 0.6798 1.2214 -0.3859 -0.1736 0.0090 335 GLU A CA 2587 C C . GLU A 335 ? 1.0391 0.5543 1.1196 -0.3677 -0.1533 0.0191 335 GLU A C 2588 O O . GLU A 335 ? 1.1374 0.6692 1.2070 -0.3573 -0.1443 0.0374 335 GLU A O 2589 C CB . GLU A 335 ? 1.2267 0.7225 1.2335 -0.3940 -0.1734 -0.0298 335 GLU A CB 2590 C CG . GLU A 335 ? 1.4674 0.9672 1.4514 -0.4140 -0.1948 -0.0426 335 GLU A CG 2591 C CD . GLU A 335 ? 1.6924 1.1742 1.6217 -0.4228 -0.1930 -0.0823 335 GLU A CD 2592 O OE1 . GLU A 335 ? 1.7720 1.2597 1.6747 -0.4401 -0.2105 -0.0942 335 GLU A OE1 2593 O OE2 . GLU A 335 ? 1.8360 1.3011 1.7487 -0.4127 -0.1740 -0.1010 335 GLU A OE2 2594 N N . VAL A 336 ? 1.1451 0.6384 1.2562 -0.3641 -0.1469 0.0071 336 VAL A N 2595 C CA . VAL A 336 ? 1.2854 0.7752 1.4189 -0.3476 -0.1297 0.0177 336 VAL A CA 2596 C C . VAL A 336 ? 1.2462 0.7126 1.3432 -0.3410 -0.1162 -0.0105 336 VAL A C 2597 O O . VAL A 336 ? 1.3302 0.7739 1.3980 -0.3493 -0.1181 -0.0464 336 VAL A O 2598 C CB . VAL A 336 ? 1.0309 0.5078 1.2170 -0.3459 -0.1293 0.0216 336 VAL A CB 2599 C CG1 . VAL A 336 ? 1.0125 0.5221 1.2382 -0.3476 -0.1372 0.0620 336 VAL A CG1 2600 C CG2 . VAL A 336 ? 1.6631 1.1075 1.8471 -0.3584 -0.1375 -0.0160 336 VAL A CG2 2601 N N . PHE A 337 ? 1.2136 0.6914 1.3111 -0.3257 -0.1018 0.0058 337 PHE A N 2602 C CA . PHE A 337 ? 1.1818 0.6534 1.2469 -0.3129 -0.0838 -0.0160 337 PHE A CA 2603 C C . PHE A 337 ? 1.1995 0.6772 1.2049 -0.3187 -0.0841 -0.0344 337 PHE A C 2604 O O . PHE A 337 ? 1.2204 0.6886 1.1940 -0.3153 -0.0724 -0.0604 337 PHE A O 2605 C CB . PHE A 337 ? 1.2938 0.7300 1.3779 -0.3115 -0.0780 -0.0452 337 PHE A CB 2606 C CG . PHE A 337 ? 1.1709 0.5986 1.3179 -0.3051 -0.0783 -0.0244 337 PHE A CG 2607 C CD1 . PHE A 337 ? 1.0383 0.4956 1.2077 -0.2936 -0.0728 0.0144 337 PHE A CD1 2608 C CD2 . PHE A 337 ? 1.2398 0.6396 1.4187 -0.3072 -0.0806 -0.0438 337 PHE A CD2 2609 C CE1 . PHE A 337 ? 1.2509 0.7105 1.4726 -0.2862 -0.0717 0.0369 337 PHE A CE1 2610 C CE2 . PHE A 337 ? 1.0541 0.4544 1.2842 -0.2976 -0.0791 -0.0213 337 PHE A CE2 2611 C CZ . PHE A 337 ? 1.1749 0.6066 1.4262 -0.2874 -0.0751 0.0205 337 PHE A CZ 2612 N N . ALA A 338 ? 1.2444 0.7409 1.2380 -0.3275 -0.0978 -0.0185 338 ALA A N 2613 C CA . ALA A 338 ? 0.9888 0.4940 0.9312 -0.3340 -0.1019 -0.0280 338 ALA A CA 2614 C C . ALA A 338 ? 1.1246 0.6512 1.0470 -0.3185 -0.0891 -0.0142 338 ALA A C 2615 O O . ALA A 338 ? 1.2946 0.8235 1.1745 -0.3209 -0.0869 -0.0246 338 ALA A O 2616 C CB . ALA A 338 ? 1.2441 0.7613 1.1885 -0.3491 -0.1237 -0.0145 338 ALA A CB 2617 N N . ARG A 339 ? 1.2609 0.8042 1.2145 -0.3041 -0.0816 0.0098 339 ARG A N 2618 C CA . ARG A 339 ? 1.2931 0.8579 1.2333 -0.2893 -0.0713 0.0229 339 ARG A CA 2619 C C . ARG A 339 ? 1.0745 0.6539 0.9911 -0.2937 -0.0826 0.0312 339 ARG A C 2620 O O . ARG A 339 ? 1.1441 0.7205 1.0240 -0.2951 -0.0811 0.0218 339 ARG A O 2621 C CB . ARG A 339 ? 1.0220 0.5765 0.9381 -0.2818 -0.0550 0.0045 339 ARG A CB 2622 C CG . ARG A 339 ? 1.0182 0.5605 0.9646 -0.2746 -0.0441 -0.0014 339 ARG A CG 2623 C CD . ARG A 339 ? 1.1465 0.6850 1.0749 -0.2656 -0.0272 -0.0170 339 ARG A CD 2624 N NE . ARG A 339 ? 0.8897 0.4209 0.8554 -0.2559 -0.0179 -0.0169 339 ARG A NE 2625 C CZ . ARG A 339 ? 1.1596 0.6895 1.1238 -0.2461 -0.0030 -0.0279 339 ARG A CZ 2626 N NH1 . ARG A 339 ? 1.5202 1.0562 1.4459 -0.2461 0.0051 -0.0400 339 ARG A NH1 2627 N NH2 . ARG A 339 ? 1.4207 0.9448 1.4254 -0.2370 0.0030 -0.0244 339 ARG A NH2 2628 N N . PHE A 340 ? 0.8745 0.4715 0.8170 -0.2959 -0.0942 0.0513 340 PHE A N 2629 C CA . PHE A 340 ? 0.8844 0.4951 0.8162 -0.3015 -0.1089 0.0608 340 PHE A CA 2630 C C . PHE A 340 ? 1.0456 0.6710 0.9615 -0.2881 -0.1040 0.0684 340 PHE A C 2631 O O . PHE A 340 ? 1.3309 0.9560 1.2245 -0.2938 -0.1148 0.0687 340 PHE A O 2632 C CB . PHE A 340 ? 1.1689 0.8002 1.1417 -0.3048 -0.1201 0.0820 340 PHE A CB 2633 C CG . PHE A 340 ? 0.8661 0.5178 0.8393 -0.3066 -0.1345 0.0957 340 PHE A CG 2634 C CD1 . PHE A 340 ? 0.8938 0.5352 0.8417 -0.3225 -0.1515 0.0881 340 PHE A CD1 2635 C CD2 . PHE A 340 ? 0.8854 0.5696 0.8863 -0.2922 -0.1312 0.1163 340 PHE A CD2 2636 C CE1 . PHE A 340 ? 1.0390 0.7003 0.9926 -0.3237 -0.1667 0.1038 340 PHE A CE1 2637 C CE2 . PHE A 340 ? 1.0514 0.7550 1.0594 -0.2917 -0.1443 0.1285 340 PHE A CE2 2638 C CZ . PHE A 340 ? 1.0365 0.7276 1.0228 -0.3073 -0.1629 0.1237 340 PHE A CZ 2639 N N . GLY A 341 ? 1.1328 0.7710 1.0614 -0.2712 -0.0893 0.0749 341 GLY A N 2640 C CA . GLY A 341 ? 1.3342 0.9858 1.2538 -0.2579 -0.0855 0.0802 341 GLY A CA 2641 C C . GLY A 341 ? 1.2089 0.8451 1.0970 -0.2545 -0.0754 0.0663 341 GLY A C 2642 O O . GLY A 341 ? 1.1560 0.8013 1.0421 -0.2419 -0.0692 0.0688 341 GLY A O 2643 N N . SER A 342 ? 1.1363 0.7507 1.0013 -0.2661 -0.0736 0.0503 342 SER A N 2644 C CA . SER A 342 ? 1.1502 0.7536 0.9884 -0.2645 -0.0621 0.0373 342 SER A CA 2645 C C . SER A 342 ? 1.1368 0.7403 0.9506 -0.2655 -0.0678 0.0409 342 SER A C 2646 O O . SER A 342 ? 1.2438 0.8479 1.0498 -0.2578 -0.0587 0.0391 342 SER A O 2647 C CB . SER A 342 ? 1.1409 0.7254 0.9607 -0.2771 -0.0586 0.0174 342 SER A CB 2648 O OG . SER A 342 ? 1.3197 0.8993 1.1677 -0.2744 -0.0528 0.0133 342 SER A OG 2649 N N . ALA A 343 ? 1.1762 0.7792 0.9804 -0.2761 -0.0845 0.0477 343 ALA A N 2650 C CA . ALA A 343 ? 1.1722 0.7740 0.9582 -0.2784 -0.0932 0.0555 343 ALA A CA 2651 C C . ALA A 343 ? 1.1888 0.8009 0.9933 -0.2771 -0.1113 0.0728 343 ALA A C 2652 O O . ALA A 343 ? 1.3233 0.9390 1.1323 -0.2876 -0.1239 0.0766 343 ALA A O 2653 C CB . ALA A 343 ? 1.2040 0.7950 0.9498 -0.2967 -0.0956 0.0468 343 ALA A CB 2654 N N . ILE A 344 ? 0.8663 0.4836 0.6846 -0.2640 -0.1133 0.0820 344 ILE A N 2655 C CA . ILE A 344 ? 1.0147 0.6427 0.8566 -0.2593 -0.1297 0.0978 344 ILE A CA 2656 C C . ILE A 344 ? 1.0337 0.6511 0.8638 -0.2624 -0.1419 0.1074 344 ILE A C 2657 O O . ILE A 344 ? 1.4358 1.0466 1.2682 -0.2521 -0.1354 0.1049 344 ILE A O 2658 C CB . ILE A 344 ? 0.9350 0.5823 0.8152 -0.2376 -0.1219 0.1000 344 ILE A CB 2659 C CG1 . ILE A 344 ? 0.8596 0.5184 0.7514 -0.2352 -0.1084 0.0943 344 ILE A CG1 2660 C CG2 . ILE A 344 ? 0.8647 0.5277 0.7753 -0.2321 -0.1375 0.1148 344 ILE A CG2 2661 C CD1 . ILE A 344 ? 0.8605 0.5462 0.7861 -0.2162 -0.0995 0.0982 344 ILE A CD1 2662 N N . ALA A 345 ? 0.9555 0.5720 0.7745 -0.2779 -0.1610 0.1197 345 ALA A N 2663 C CA . ALA A 345 ? 1.2278 0.8350 1.0356 -0.2845 -0.1756 0.1343 345 ALA A CA 2664 C C . ALA A 345 ? 1.0301 0.6462 0.8706 -0.2793 -0.1972 0.1549 345 ALA A C 2665 O O . ALA A 345 ? 0.9447 0.5725 0.7887 -0.2894 -0.2115 0.1637 345 ALA A O 2666 C CB . ALA A 345 ? 1.3360 0.9376 1.0977 -0.3096 -0.1808 0.1346 345 ALA A CB 2667 N N . PRO A 346 ? 0.9437 0.5541 0.8116 -0.2630 -0.2005 0.1616 346 PRO A N 2668 C CA . PRO A 346 ? 0.9468 0.5631 0.8500 -0.2568 -0.2224 0.1822 346 PRO A CA 2669 C C . PRO A 346 ? 0.9933 0.6049 0.8732 -0.2799 -0.2457 0.2048 346 PRO A C 2670 O O . PRO A 346 ? 1.1187 0.7155 0.9681 -0.2924 -0.2461 0.2088 346 PRO A O 2671 C CB . PRO A 346 ? 0.9460 0.5499 0.8773 -0.2361 -0.2186 0.1787 346 PRO A CB 2672 C CG . PRO A 346 ? 0.9533 0.5548 0.8714 -0.2276 -0.1928 0.1542 346 PRO A CG 2673 C CD . PRO A 346 ? 0.9139 0.5128 0.7858 -0.2487 -0.1846 0.1485 346 PRO A CD 2674 N N . LEU A 347 ? 1.1819 0.8096 1.0763 -0.2867 -0.2654 0.2210 347 LEU A N 2675 C CA . LEU A 347 ? 1.2010 0.8300 1.0718 -0.3103 -0.2900 0.2448 347 LEU A CA 2676 C C . LEU A 347 ? 1.1244 0.7510 1.0351 -0.3024 -0.3139 0.2734 347 LEU A C 2677 O O . LEU A 347 ? 1.0736 0.7029 0.9704 -0.3213 -0.3375 0.2994 347 LEU A O 2678 C CB . LEU A 347 ? 1.1355 0.7844 0.9933 -0.3274 -0.3006 0.2460 347 LEU A CB 2679 C CG . LEU A 347 ? 1.0726 0.7218 0.9005 -0.3343 -0.2796 0.2175 347 LEU A CG 2680 C CD1 . LEU A 347 ? 1.1502 0.8163 0.9706 -0.3524 -0.2942 0.2187 347 LEU A CD1 2681 C CD2 . LEU A 347 ? 1.1797 0.8137 0.9555 -0.3476 -0.2654 0.2041 347 LEU A CD2 2682 N N . GLY A 348 ? 1.1096 0.7324 1.0709 -0.2743 -0.3081 0.2683 348 GLY A N 2683 C CA . GLY A 348 ? 1.1805 0.8031 1.1932 -0.2618 -0.3305 0.2921 348 GLY A CA 2684 C C . GLY A 348 ? 1.3024 0.9538 1.3390 -0.2650 -0.3478 0.3068 348 GLY A C 2685 O O . GLY A 348 ? 1.3641 1.0342 1.3991 -0.2637 -0.3353 0.2910 348 GLY A O 2686 N N . ASP A 349 ? 1.1599 0.8160 1.2206 -0.2706 -0.3777 0.3392 349 ASP A N 2687 C CA . ASP A 349 ? 1.2782 0.9643 1.3601 -0.2774 -0.3977 0.3566 349 ASP A CA 2688 C C . ASP A 349 ? 1.4543 1.1470 1.4802 -0.3139 -0.4167 0.3737 349 ASP A C 2689 O O . ASP A 349 ? 1.5128 1.1992 1.5285 -0.3282 -0.4392 0.4023 349 ASP A O 2690 C CB . ASP A 349 ? 1.2211 0.9147 1.3741 -0.2579 -0.4200 0.3818 349 ASP A CB 2691 C CG . ASP A 349 ? 1.3914 1.1218 1.5806 -0.2578 -0.4354 0.3950 349 ASP A CG 2692 O OD1 . ASP A 349 ? 1.5919 1.3402 1.7542 -0.2712 -0.4270 0.3818 349 ASP A OD1 2693 O OD2 . ASP A 349 ? 1.2722 1.0136 1.5212 -0.2439 -0.4565 0.4188 349 ASP A OD2 2694 N N . LEU A 350 ? 1.3738 1.0803 1.3649 -0.3294 -0.4081 0.3562 350 LEU A N 2695 C CA . LEU A 350 ? 1.1482 0.8605 1.0769 -0.3641 -0.4202 0.3610 350 LEU A CA 2696 C C . LEU A 350 ? 1.1806 0.9188 1.1217 -0.3812 -0.4565 0.3934 350 LEU A C 2697 O O . LEU A 350 ? 1.4913 1.2333 1.3952 -0.4058 -0.4772 0.4153 350 LEU A O 2698 C CB . LEU A 350 ? 1.1540 0.8683 1.0467 -0.3731 -0.3984 0.3268 350 LEU A CB 2699 C CG . LEU A 350 ? 1.1735 0.8903 0.9962 -0.4064 -0.4027 0.3186 350 LEU A CG 2700 C CD1 . LEU A 350 ? 1.2681 0.9693 1.0464 -0.4167 -0.3977 0.3232 350 LEU A CD1 2701 C CD2 . LEU A 350 ? 1.1543 0.8674 0.9563 -0.4089 -0.3795 0.2819 350 LEU A CD2 2702 N N . ASP A 351 ? 1.1911 0.9510 1.1846 -0.3689 -0.4643 0.3977 351 ASP A N 2703 C CA . ASP A 351 ? 1.3672 1.1561 1.3797 -0.3841 -0.4994 0.4280 351 ASP A CA 2704 C C . ASP A 351 ? 1.4920 1.2860 1.5697 -0.3654 -0.5214 0.4630 351 ASP A C 2705 O O . ASP A 351 ? 1.4786 1.2991 1.5859 -0.3733 -0.5523 0.4926 351 ASP A O 2706 C CB . ASP A 351 ? 1.3797 1.1935 1.4156 -0.3846 -0.4978 0.4150 351 ASP A CB 2707 C CG . ASP A 351 ? 1.4225 1.2383 1.5163 -0.3504 -0.4729 0.3988 351 ASP A CG 2708 O OD1 . ASP A 351 ? 1.4235 1.2672 1.5590 -0.3460 -0.4770 0.4008 351 ASP A OD1 2709 O OD2 . ASP A 351 ? 1.5687 1.3613 1.6661 -0.3291 -0.4494 0.3843 351 ASP A OD2 2710 N N . GLN A 352 ? 1.4596 1.2280 1.5623 -0.3404 -0.5064 0.4588 352 GLN A N 2711 C CA . GLN A 352 ? 1.2423 1.0085 1.4146 -0.3174 -0.5237 0.4859 352 GLN A CA 2712 C C . GLN A 352 ? 1.2677 1.0651 1.5130 -0.2963 -0.5297 0.4902 352 GLN A C 2713 O O . GLN A 352 ? 1.2328 1.0444 1.5338 -0.2884 -0.5571 0.5225 352 GLN A O 2714 C CB . GLN A 352 ? 1.2210 0.9880 1.3821 -0.3398 -0.5602 0.5299 352 GLN A CB 2715 C CG . GLN A 352 ? 1.6579 1.3963 1.7607 -0.3567 -0.5547 0.5321 352 GLN A CG 2716 C CD . GLN A 352 ? 1.7184 1.4215 1.8560 -0.3294 -0.5389 0.5237 352 GLN A CD 2717 O OE1 . GLN A 352 ? 1.7706 1.4698 1.9821 -0.2993 -0.5427 0.5280 352 GLN A OE1 2718 N NE2 . GLN A 352 ? 1.2325 0.9111 1.3183 -0.3399 -0.5211 0.5101 352 GLN A NE2 2719 N N . ASP A 353 ? 1.4242 1.2342 1.6715 -0.2873 -0.5041 0.4594 353 ASP A N 2720 C CA . ASP A 353 ? 1.2135 1.0593 1.5272 -0.2690 -0.5052 0.4614 353 ASP A CA 2721 C C . ASP A 353 ? 1.2623 1.1061 1.6486 -0.2282 -0.4938 0.4570 353 ASP A C 2722 O O . ASP A 353 ? 1.3481 1.2248 1.8016 -0.2090 -0.4981 0.4644 353 ASP A O 2723 C CB . ASP A 353 ? 1.2002 1.0604 1.4924 -0.2743 -0.4807 0.4320 353 ASP A CB 2724 C CG . ASP A 353 ? 1.5441 1.3749 1.7945 -0.2670 -0.4448 0.3965 353 ASP A CG 2725 O OD1 . ASP A 353 ? 1.7621 1.5648 2.0107 -0.2523 -0.4359 0.3913 353 ASP A OD1 2726 O OD2 . ASP A 353 ? 1.5412 1.3768 1.7633 -0.2764 -0.4268 0.3747 353 ASP A OD2 2727 N N . GLY A 354 ? 1.1346 0.9415 1.5085 -0.2153 -0.4793 0.4434 354 GLY A N 2728 C CA . GLY A 354 ? 1.1323 0.9321 1.5688 -0.1768 -0.4662 0.4312 354 GLY A CA 2729 C C . GLY A 354 ? 1.1357 0.9291 1.5544 -0.1606 -0.4262 0.3887 354 GLY A C 2730 O O . GLY A 354 ? 1.1994 0.9815 1.6531 -0.1311 -0.4104 0.3698 354 GLY A O 2731 N N . PHE A 355 ? 1.1377 0.9387 1.5027 -0.1803 -0.4108 0.3735 355 PHE A N 2732 C CA . PHE A 355 ? 1.1388 0.9362 1.4822 -0.1690 -0.3746 0.3374 355 PHE A CA 2733 C C . PHE A 355 ? 1.1421 0.9098 1.4067 -0.1942 -0.3650 0.3252 355 PHE A C 2734 O O . PHE A 355 ? 1.2849 1.0535 1.5076 -0.2238 -0.3786 0.3367 355 PHE A O 2735 C CB . PHE A 355 ? 1.1376 0.9778 1.5043 -0.1643 -0.3611 0.3294 355 PHE A CB 2736 C CG . PHE A 355 ? 1.1561 1.0338 1.6027 -0.1394 -0.3678 0.3407 355 PHE A CG 2737 C CD1 . PHE A 355 ? 1.1737 1.0612 1.6653 -0.1042 -0.3464 0.3202 355 PHE A CD1 2738 C CD2 . PHE A 355 ? 1.1617 1.0678 1.6393 -0.1511 -0.3954 0.3704 355 PHE A CD2 2739 C CE1 . PHE A 355 ? 1.2862 1.2119 1.8542 -0.0794 -0.3504 0.3280 355 PHE A CE1 2740 C CE2 . PHE A 355 ? 1.4384 1.3828 1.9947 -0.1271 -0.4011 0.3814 355 PHE A CE2 2741 C CZ . PHE A 355 ? 1.4490 1.4035 2.0515 -0.0904 -0.3775 0.3596 355 PHE A CZ 2742 N N . ASN A 356 ? 1.1040 0.8475 1.3498 -0.1822 -0.3416 0.3006 356 ASN A N 2743 C CA . ASN A 356 ? 1.1416 0.8587 1.3190 -0.2027 -0.3301 0.2878 356 ASN A CA 2744 C C . ASN A 356 ? 1.1919 0.9244 1.3347 -0.2189 -0.3168 0.2751 356 ASN A C 2745 O O . ASN A 356 ? 1.2739 1.0345 1.4457 -0.2082 -0.3061 0.2680 356 ASN A O 2746 C CB . ASN A 356 ? 1.0776 0.7705 1.2500 -0.1846 -0.3077 0.2636 356 ASN A CB 2747 C CG . ASN A 356 ? 1.0743 0.7436 1.2786 -0.1717 -0.3223 0.2745 356 ASN A CG 2748 O OD1 . ASN A 356 ? 1.3098 0.9740 1.5254 -0.1824 -0.3501 0.3041 356 ASN A OD1 2749 N ND2 . ASN A 356 ? 1.0821 0.7368 1.3023 -0.1495 -0.3051 0.2513 356 ASN A ND2 2750 N N . ASP A 357 ? 1.1197 0.8345 1.2027 -0.2450 -0.3177 0.2725 357 ASP A N 2751 C CA . ASP A 357 ? 1.0488 0.7717 1.0990 -0.2619 -0.3073 0.2588 357 ASP A CA 2752 C C . ASP A 357 ? 1.0072 0.7069 1.0133 -0.2639 -0.2823 0.2342 357 ASP A C 2753 O O . ASP A 357 ? 1.1732 0.8530 1.1732 -0.2542 -0.2748 0.2294 357 ASP A O 2754 C CB . ASP A 357 ? 1.1122 0.8400 1.1327 -0.2924 -0.3321 0.2746 357 ASP A CB 2755 C CG . ASP A 357 ? 1.3513 1.1011 1.4150 -0.2920 -0.3615 0.3043 357 ASP A CG 2756 O OD1 . ASP A 357 ? 1.4167 1.1903 1.5364 -0.2725 -0.3599 0.3079 357 ASP A OD1 2757 O OD2 . ASP A 357 ? 1.3890 1.1354 1.4320 -0.3110 -0.3863 0.3254 357 ASP A OD2 2758 N N . ILE A 358 ? 1.0457 0.7476 1.0250 -0.2765 -0.2705 0.2190 358 ILE A N 2759 C CA . ILE A 358 ? 1.0354 0.7189 0.9807 -0.2761 -0.2462 0.1961 358 ILE A CA 2760 C C . ILE A 358 ? 1.0819 0.7607 0.9885 -0.2988 -0.2432 0.1838 358 ILE A C 2761 O O . ILE A 358 ? 1.0671 0.7594 0.9803 -0.3119 -0.2565 0.1892 358 ILE A O 2762 C CB . ILE A 358 ? 1.1505 0.8442 1.1266 -0.2511 -0.2230 0.1826 358 ILE A CB 2763 C CG1 . ILE A 358 ? 1.1589 0.8320 1.1089 -0.2446 -0.2026 0.1649 358 ILE A CG1 2764 C CG2 . ILE A 358 ? 0.9300 0.6436 0.9197 -0.2542 -0.2154 0.1779 358 ILE A CG2 2765 C CD1 . ILE A 358 ? 1.1139 0.7995 1.0919 -0.2199 -0.1827 0.1531 358 ILE A CD1 2766 N N . ALA A 359 ? 1.1224 0.7823 0.9916 -0.3033 -0.2262 0.1660 359 ALA A N 2767 C CA . ALA A 359 ? 1.0010 0.6536 0.8352 -0.3221 -0.2209 0.1494 359 ALA A CA 2768 C C . ALA A 359 ? 0.9652 0.6106 0.8007 -0.3112 -0.1946 0.1290 359 ALA A C 2769 O O . ALA A 359 ? 1.1394 0.7767 0.9717 -0.2981 -0.1793 0.1233 359 ALA A O 2770 C CB . ALA A 359 ? 0.9894 0.6299 0.7730 -0.3422 -0.2273 0.1477 359 ALA A CB 2771 N N . ILE A 360 ? 1.0371 0.6854 0.8799 -0.3176 -0.1912 0.1195 360 ILE A N 2772 C CA . ILE A 360 ? 1.0711 0.7132 0.9193 -0.3090 -0.1691 0.1037 360 ILE A CA 2773 C C . ILE A 360 ? 1.0737 0.6993 0.8924 -0.3269 -0.1662 0.0837 360 ILE A C 2774 O O . ILE A 360 ? 1.1521 0.7784 0.9671 -0.3439 -0.1813 0.0819 360 ILE A O 2775 C CB . ILE A 360 ? 0.8825 0.5445 0.7775 -0.2973 -0.1655 0.1124 360 ILE A CB 2776 C CG1 . ILE A 360 ? 0.8691 0.5516 0.7945 -0.2785 -0.1675 0.1282 360 ILE A CG1 2777 C CG2 . ILE A 360 ? 0.8641 0.5217 0.7660 -0.2889 -0.1443 0.1011 360 ILE A CG2 2778 C CD1 . ILE A 360 ? 0.8545 0.5650 0.8248 -0.2662 -0.1614 0.1375 360 ILE A CD1 2779 N N . ALA A 361 ? 0.9292 0.5409 0.7290 -0.3227 -0.1472 0.0670 361 ALA A N 2780 C CA . ALA A 361 ? 1.0959 0.6919 0.8664 -0.3373 -0.1422 0.0439 361 ALA A CA 2781 C C . ALA A 361 ? 1.2397 0.8267 1.0323 -0.3304 -0.1266 0.0301 361 ALA A C 2782 O O . ALA A 361 ? 1.3333 0.9239 1.1463 -0.3133 -0.1119 0.0346 361 ALA A O 2783 C CB . ALA A 361 ? 1.2896 0.8787 1.0188 -0.3411 -0.1336 0.0351 361 ALA A CB 2784 N N . ALA A 362 ? 1.4185 0.9935 1.2072 -0.3445 -0.1313 0.0131 362 ALA A N 2785 C CA . ALA A 362 ? 1.1256 0.6867 0.9367 -0.3401 -0.1187 -0.0015 362 ALA A CA 2786 C C . ALA A 362 ? 1.0270 0.5701 0.8048 -0.3492 -0.1100 -0.0329 362 ALA A C 2787 O O . ALA A 362 ? 1.0416 0.5737 0.8101 -0.3652 -0.1196 -0.0515 362 ALA A O 2788 C CB . ALA A 362 ? 0.9757 0.5367 0.8236 -0.3476 -0.1321 0.0049 362 ALA A CB 2789 N N . PRO A 363 ? 0.9969 0.5391 0.7577 -0.3392 -0.0915 -0.0404 363 PRO A N 2790 C CA . PRO A 363 ? 1.0279 0.5621 0.7523 -0.3460 -0.0798 -0.0682 363 PRO A CA 2791 C C . PRO A 363 ? 1.4186 0.9333 1.1533 -0.3504 -0.0746 -0.0986 363 PRO A C 2792 O O . PRO A 363 ? 1.6249 1.1353 1.3253 -0.3627 -0.0725 -0.1258 363 PRO A O 2793 C CB . PRO A 363 ? 1.2801 0.8199 1.0063 -0.3295 -0.0601 -0.0635 363 PRO A CB 2794 C CG . PRO A 363 ? 0.9626 0.5152 0.7081 -0.3189 -0.0663 -0.0334 363 PRO A CG 2795 C CD . PRO A 363 ? 0.9559 0.5088 0.7345 -0.3202 -0.0802 -0.0219 363 PRO A CD 2796 N N . TYR A 364 ? 1.3879 0.8920 1.1703 -0.3401 -0.0719 -0.0943 364 TYR A N 2797 C CA . TYR A 364 ? 1.0693 0.5503 0.8718 -0.3420 -0.0676 -0.1218 364 TYR A CA 2798 C C . TYR A 364 ? 1.1881 0.6574 1.0109 -0.3568 -0.0886 -0.1233 364 TYR A C 2799 O O . TYR A 364 ? 1.6364 1.0825 1.4835 -0.3599 -0.0892 -0.1449 364 TYR A O 2800 C CB . TYR A 364 ? 1.2428 0.7180 1.0886 -0.3222 -0.0517 -0.1152 364 TYR A CB 2801 C CG . TYR A 364 ? 1.1088 0.5983 0.9361 -0.3092 -0.0331 -0.1124 364 TYR A CG 2802 C CD1 . TYR A 364 ? 1.0370 0.5454 0.8715 -0.2982 -0.0314 -0.0823 364 TYR A CD1 2803 C CD2 . TYR A 364 ? 1.2207 0.7071 1.0229 -0.3089 -0.0174 -0.1413 364 TYR A CD2 2804 C CE1 . TYR A 364 ? 1.2466 0.7671 1.0657 -0.2884 -0.0166 -0.0803 364 TYR A CE1 2805 C CE2 . TYR A 364 ? 1.4495 0.9514 1.2375 -0.2990 -0.0014 -0.1369 364 TYR A CE2 2806 C CZ . TYR A 364 ? 1.3680 0.8853 1.1650 -0.2895 -0.0021 -0.1059 364 TYR A CZ 2807 O OH . TYR A 364 ? 1.4337 0.9653 1.2187 -0.2813 0.0118 -0.1019 364 TYR A OH 2808 N N . GLY A 365 ? 1.2544 0.7396 1.0710 -0.3659 -0.1067 -0.1000 365 GLY A N 2809 C CA . GLY A 365 ? 1.2649 0.7442 1.0990 -0.3825 -0.1289 -0.0991 365 GLY A CA 2810 C C . GLY A 365 ? 1.4105 0.8852 1.1997 -0.4044 -0.1414 -0.1272 365 GLY A C 2811 O O . GLY A 365 ? 1.4396 0.9127 1.1870 -0.4062 -0.1296 -0.1529 365 GLY A O 2812 N N . GLY A 366 ? 1.1743 0.6507 0.9720 -0.4221 -0.1654 -0.1219 366 GLY A N 2813 C CA . GLY A 366 ? 1.2248 0.7044 0.9812 -0.4428 -0.1802 -0.1459 366 GLY A CA 2814 C C . GLY A 366 ? 1.8732 1.3327 1.6404 -0.4457 -0.1779 -0.1870 366 GLY A C 2815 O O . GLY A 366 ? 1.5952 1.0352 1.4117 -0.4334 -0.1692 -0.1927 366 GLY A O 2816 N N . GLU A 367 ? 1.9676 1.4331 1.6903 -0.4620 -0.1866 -0.2154 367 GLU A N 2817 C CA . GLU A 367 ? 1.9465 1.3946 1.6760 -0.4646 -0.1852 -0.2605 367 GLU A CA 2818 C C . GLU A 367 ? 1.9578 1.3914 1.6733 -0.4510 -0.1577 -0.2931 367 GLU A C 2819 O O . GLU A 367 ? 1.8535 1.3019 1.5143 -0.4534 -0.1450 -0.3006 367 GLU A O 2820 C CB . GLU A 367 ? 1.9857 1.4508 1.6693 -0.4864 -0.2039 -0.2806 367 GLU A CB 2821 C CG . GLU A 367 ? 2.1394 1.5891 1.8235 -0.4886 -0.2024 -0.3331 367 GLU A CG 2822 C CD . GLU A 367 ? 2.3329 1.8063 1.9538 -0.5084 -0.2143 -0.3564 367 GLU A CD 2823 O OE1 . GLU A 367 ? 2.2992 1.8004 1.8691 -0.5188 -0.2175 -0.3335 367 GLU A OE1 2824 O OE2 . GLU A 367 ? 2.3341 1.7989 1.9578 -0.5136 -0.2217 -0.3966 367 GLU A OE2 2825 N N . ASP A 368 ? 2.0302 1.4365 1.7986 -0.4371 -0.1493 -0.3106 368 ASP A N 2826 C CA . ASP A 368 ? 1.9127 1.3033 1.6808 -0.4213 -0.1240 -0.3420 368 ASP A CA 2827 C C . ASP A 368 ? 1.5112 0.9131 1.2556 -0.4112 -0.1020 -0.3218 368 ASP A C 2828 O O . ASP A 368 ? 1.4568 0.8651 1.1657 -0.4072 -0.0815 -0.3473 368 ASP A O 2829 C CB . ASP A 368 ? 1.9982 1.3935 1.7210 -0.4286 -0.1210 -0.3924 368 ASP A CB 2830 C CG . ASP A 368 ? 2.2917 1.6657 2.0348 -0.4098 -0.0994 -0.4310 368 ASP A CG 2831 O OD1 . ASP A 368 ? 2.2438 1.5898 2.0505 -0.3943 -0.0971 -0.4233 368 ASP A OD1 2832 O OD2 . ASP A 368 ? 2.5126 1.9002 2.2091 -0.4103 -0.0849 -0.4669 368 ASP A OD2 2833 N N . LYS A 369 ? 1.3043 0.7116 1.0700 -0.4073 -0.1064 -0.2764 369 LYS A N 2834 C CA . LYS A 369 ? 1.5298 0.9484 1.2862 -0.3940 -0.0881 -0.2529 369 LYS A CA 2835 C C . LYS A 369 ? 1.5574 1.0035 1.2481 -0.4005 -0.0806 -0.2570 369 LYS A C 2836 O O . LYS A 369 ? 1.7835 1.2399 1.4626 -0.3873 -0.0588 -0.2592 369 LYS A O 2837 C CB . LYS A 369 ? 1.8794 1.2811 1.6744 -0.3725 -0.0654 -0.2665 369 LYS A CB 2838 C CG . LYS A 369 ? 1.9926 1.4093 1.8092 -0.3521 -0.0521 -0.2301 369 LYS A CG 2839 C CD . LYS A 369 ? 2.0365 1.4357 1.9017 -0.3325 -0.0353 -0.2390 369 LYS A CD 2840 C CE . LYS A 369 ? 1.8080 1.2251 1.6940 -0.3142 -0.0249 -0.2019 369 LYS A CE 2841 N NZ . LYS A 369 ? 1.6326 1.0351 1.5716 -0.2961 -0.0122 -0.2042 369 LYS A NZ 2842 N N . LYS A 370 ? 1.3777 0.8378 1.0274 -0.4219 -0.0999 -0.2556 370 LYS A N 2843 C CA . LYS A 370 ? 1.3220 0.8106 0.9100 -0.4314 -0.0963 -0.2537 370 LYS A CA 2844 C C . LYS A 370 ? 1.4378 0.9470 1.0245 -0.4264 -0.1027 -0.2056 370 LYS A C 2845 O O . LYS A 370 ? 1.4679 0.9990 1.0133 -0.4306 -0.0981 -0.1961 370 LYS A O 2846 C CB . LYS A 370 ? 1.3665 0.8637 0.9069 -0.4586 -0.1148 -0.2758 370 LYS A CB 2847 C CG . LYS A 370 ? 1.4225 0.9126 0.9511 -0.4596 -0.1033 -0.3287 370 LYS A CG 2848 C CD . LYS A 370 ? 1.4925 1.0100 0.9625 -0.4810 -0.1157 -0.3456 370 LYS A CD 2849 C CE . LYS A 370 ? 2.0270 1.5489 1.5059 -0.4961 -0.1488 -0.3248 370 LYS A CE 2850 N NZ . LYS A 370 ? 2.2361 1.7872 1.6581 -0.5174 -0.1621 -0.3397 370 LYS A NZ 2851 N N . GLY A 371 ? 1.3964 0.8997 1.0302 -0.4175 -0.1133 -0.1757 371 GLY A N 2852 C CA . GLY A 371 ? 1.1747 0.6957 0.8145 -0.4100 -0.1189 -0.1342 371 GLY A CA 2853 C C . GLY A 371 ? 1.3196 0.8536 0.9549 -0.4250 -0.1467 -0.1112 371 GLY A C 2854 O O . GLY A 371 ? 1.6255 1.1633 1.2296 -0.4463 -0.1624 -0.1256 371 GLY A O 2855 N N . ILE A 372 ? 1.1368 0.6801 0.8042 -0.4135 -0.1530 -0.0760 372 ILE A N 2856 C CA . ILE A 372 ? 1.2082 0.7667 0.8821 -0.4240 -0.1787 -0.0508 372 ILE A CA 2857 C C . ILE A 372 ? 1.2464 0.8205 0.9382 -0.4081 -0.1787 -0.0156 372 ILE A C 2858 O O . ILE A 372 ? 1.2078 0.7790 0.9239 -0.3879 -0.1613 -0.0092 372 ILE A O 2859 C CB . ILE A 372 ? 1.3781 0.9293 1.0951 -0.4293 -0.1925 -0.0505 372 ILE A CB 2860 C CG1 . ILE A 372 ? 1.2278 0.7978 0.9472 -0.4449 -0.2215 -0.0293 372 ILE A CG1 2861 C CG2 . ILE A 372 ? 1.6593 1.2075 1.4305 -0.4081 -0.1799 -0.0345 372 ILE A CG2 2862 C CD1 . ILE A 372 ? 1.5117 1.0780 1.2754 -0.4528 -0.2364 -0.0267 372 ILE A CD1 2863 N N . VAL A 373 ? 1.2671 0.8580 0.9474 -0.4174 -0.1992 0.0061 373 VAL A N 2864 C CA . VAL A 373 ? 1.1421 0.7463 0.8425 -0.4026 -0.2020 0.0373 373 VAL A CA 2865 C C . VAL A 373 ? 1.2190 0.8400 0.9502 -0.4068 -0.2264 0.0613 373 VAL A C 2866 O O . VAL A 373 ? 1.1482 0.7772 0.8606 -0.4274 -0.2482 0.0633 373 VAL A O 2867 C CB . VAL A 373 ? 1.2767 0.8861 0.9370 -0.4067 -0.2022 0.0454 373 VAL A CB 2868 C CG1 . VAL A 373 ? 1.2814 0.9004 0.9685 -0.3916 -0.2085 0.0761 373 VAL A CG1 2869 C CG2 . VAL A 373 ? 1.3328 0.9307 0.9678 -0.4015 -0.1767 0.0241 373 VAL A CG2 2870 N N . TYR A 374 ? 1.2270 0.8569 1.0055 -0.3876 -0.2224 0.0793 374 TYR A N 2871 C CA . TYR A 374 ? 1.0334 0.6841 0.8500 -0.3882 -0.2423 0.1025 374 TYR A CA 2872 C C . TYR A 374 ? 1.0508 0.7160 0.8777 -0.3766 -0.2505 0.1278 374 TYR A C 2873 O O . TYR A 374 ? 1.1844 0.8450 1.0138 -0.3584 -0.2350 0.1298 374 TYR A O 2874 C CB . TYR A 374 ? 0.9872 0.6449 0.8543 -0.3753 -0.2326 0.1064 374 TYR A CB 2875 C CG . TYR A 374 ? 1.1267 0.7679 0.9954 -0.3865 -0.2276 0.0853 374 TYR A CG 2876 C CD1 . TYR A 374 ? 1.1795 0.8238 1.0617 -0.4061 -0.2474 0.0845 374 TYR A CD1 2877 C CD2 . TYR A 374 ? 1.0420 0.6638 0.9030 -0.3776 -0.2047 0.0665 374 TYR A CD2 2878 C CE1 . TYR A 374 ? 1.1115 0.7364 1.0002 -0.4165 -0.2445 0.0640 374 TYR A CE1 2879 C CE2 . TYR A 374 ? 1.1350 0.7387 1.0040 -0.3864 -0.2013 0.0475 374 TYR A CE2 2880 C CZ . TYR A 374 ? 1.1706 0.7741 1.0539 -0.4058 -0.2212 0.0455 374 TYR A CZ 2881 O OH . TYR A 374 ? 1.3813 0.9626 1.2773 -0.4147 -0.2193 0.0253 374 TYR A OH 2882 N N . ILE A 375 ? 1.1358 0.8180 0.9717 -0.3875 -0.2764 0.1469 375 ILE A N 2883 C CA . ILE A 375 ? 1.0986 0.7941 0.9532 -0.3763 -0.2879 0.1729 375 ILE A CA 2884 C C . ILE A 375 ? 1.1095 0.8301 1.0252 -0.3624 -0.2944 0.1910 375 ILE A C 2885 O O . ILE A 375 ? 1.1435 0.8792 1.0779 -0.3753 -0.3096 0.1964 375 ILE A O 2886 C CB . ILE A 375 ? 1.0627 0.7634 0.8853 -0.3980 -0.3144 0.1867 375 ILE A CB 2887 C CG1 . ILE A 375 ? 1.0826 0.7661 0.8517 -0.4050 -0.3055 0.1779 375 ILE A CG1 2888 C CG2 . ILE A 375 ? 1.0662 0.7857 0.9282 -0.3880 -0.3341 0.2188 375 ILE A CG2 2889 C CD1 . ILE A 375 ? 1.4375 1.1069 1.1610 -0.4204 -0.2920 0.1465 375 ILE A CD1 2890 N N . PHE A 376 ? 0.9920 0.7190 0.9397 -0.3365 -0.2825 0.1991 376 PHE A N 2891 C CA . PHE A 376 ? 1.0795 0.8356 1.0864 -0.3200 -0.2846 0.2143 376 PHE A CA 2892 C C . PHE A 376 ? 1.0991 0.8665 1.1333 -0.3063 -0.2985 0.2351 376 PHE A C 2893 O O . PHE A 376 ? 1.0081 0.7617 1.0381 -0.2905 -0.2890 0.2325 376 PHE A O 2894 C CB . PHE A 376 ? 1.0156 0.7765 1.0443 -0.2989 -0.2563 0.2029 376 PHE A CB 2895 C CG . PHE A 376 ? 1.2118 0.9633 1.2266 -0.3101 -0.2440 0.1870 376 PHE A CG 2896 C CD1 . PHE A 376 ? 1.1622 0.8851 1.1358 -0.3131 -0.2283 0.1666 376 PHE A CD1 2897 C CD2 . PHE A 376 ? 1.2134 0.9849 1.2608 -0.3177 -0.2486 0.1937 376 PHE A CD2 2898 C CE1 . PHE A 376 ? 1.0670 0.7794 1.0343 -0.3217 -0.2178 0.1522 376 PHE A CE1 2899 C CE2 . PHE A 376 ? 0.9095 0.6687 0.9500 -0.3281 -0.2392 0.1806 376 PHE A CE2 2900 C CZ . PHE A 376 ? 1.0823 0.8109 1.0836 -0.3293 -0.2239 0.1593 376 PHE A CZ 2901 N N . ASN A 377 ? 1.1293 0.9213 1.1953 -0.3125 -0.3223 0.2560 377 ASN A N 2902 C CA . ASN A 377 ? 1.0432 0.8482 1.1462 -0.2980 -0.3377 0.2779 377 ASN A CA 2903 C C . ASN A 377 ? 1.0512 0.8780 1.2110 -0.2660 -0.3206 0.2773 377 ASN A C 2904 O O . ASN A 377 ? 1.0227 0.8714 1.2061 -0.2608 -0.3065 0.2713 377 ASN A O 2905 C CB . ASN A 377 ? 1.0703 0.8978 1.1906 -0.3159 -0.3706 0.3022 377 ASN A CB 2906 C CG . ASN A 377 ? 1.1417 0.9523 1.2035 -0.3469 -0.3906 0.3046 377 ASN A CG 2907 O OD1 . ASN A 377 ? 1.5379 1.3586 1.5854 -0.3715 -0.4065 0.3053 377 ASN A OD1 2908 N ND2 . ASN A 377 ? 1.1028 0.8896 1.1304 -0.3471 -0.3899 0.3056 377 ASN A ND2 2909 N N . GLY A 378 ? 1.0934 0.9153 1.2760 -0.2451 -0.3219 0.2832 378 GLY A N 2910 C CA . GLY A 378 ? 1.0927 0.9368 1.3290 -0.2132 -0.3059 0.2787 378 GLY A CA 2911 C C . GLY A 378 ? 1.1470 1.0280 1.4463 -0.2040 -0.3242 0.3010 378 GLY A C 2912 O O . GLY A 378 ? 1.1357 1.0172 1.4394 -0.2181 -0.3532 0.3235 378 GLY A O 2913 N N . ARG A 379 ? 1.1618 1.0779 1.5106 -0.1804 -0.3070 0.2957 379 ARG A N 2914 C CA . ARG A 379 ? 1.2114 1.1689 1.6286 -0.1671 -0.3201 0.3148 379 ARG A CA 2915 C C . ARG A 379 ? 1.3594 1.3341 1.8252 -0.1290 -0.3007 0.3017 379 ARG A C 2916 O O . ARG A 379 ? 1.4015 1.3556 1.8447 -0.1154 -0.2786 0.2778 379 ARG A O 2917 C CB . ARG A 379 ? 1.1588 1.1571 1.5964 -0.1808 -0.3203 0.3243 379 ARG A CB 2918 C CG . ARG A 379 ? 1.2045 1.1897 1.6035 -0.2183 -0.3437 0.3360 379 ARG A CG 2919 C CD . ARG A 379 ? 1.2973 1.3197 1.7205 -0.2320 -0.3430 0.3432 379 ARG A CD 2920 N NE . ARG A 379 ? 1.3628 1.3900 1.7769 -0.2254 -0.3113 0.3248 379 ARG A NE 2921 C CZ . ARG A 379 ? 1.3826 1.4387 1.8159 -0.2366 -0.3054 0.3300 379 ARG A CZ 2922 N NH1 . ARG A 379 ? 1.4617 1.5437 1.9245 -0.2555 -0.3290 0.3505 379 ARG A NH1 2923 N NH2 . ARG A 379 ? 1.2464 1.3065 1.6711 -0.2304 -0.2775 0.3166 379 ARG A NH2 2924 N N . SER A 380 ? 1.3169 1.3315 1.8509 -0.1119 -0.3091 0.3159 380 SER A N 2925 C CA . SER A 380 ? 1.2029 1.2392 1.7895 -0.0738 -0.2909 0.3008 380 SER A CA 2926 C C . SER A 380 ? 1.2062 1.2773 1.7932 -0.0623 -0.2558 0.2796 380 SER A C 2927 O O . SER A 380 ? 1.2304 1.3111 1.8352 -0.0338 -0.2332 0.2561 380 SER A O 2928 C CB . SER A 380 ? 1.1783 1.2529 1.8427 -0.0584 -0.3093 0.3224 380 SER A CB 2929 O OG . SER A 380 ? 1.1694 1.2912 1.8565 -0.0735 -0.3146 0.3413 380 SER A OG 2930 N N . THR A 381 ? 1.1924 1.2829 1.7599 -0.0857 -0.2524 0.2883 381 THR A N 2931 C CA . THR A 381 ? 1.2305 1.3571 1.7977 -0.0801 -0.2219 0.2757 381 THR A CA 2932 C C . THR A 381 ? 1.1992 1.2870 1.6994 -0.0902 -0.2052 0.2557 381 THR A C 2933 O O . THR A 381 ? 1.1804 1.2915 1.6705 -0.0905 -0.1822 0.2480 381 THR A O 2934 C CB . THR A 381 ? 1.2762 1.4448 1.8648 -0.1011 -0.2277 0.2984 381 THR A CB 2935 O OG1 . THR A 381 ? 1.3878 1.5182 1.9261 -0.1360 -0.2451 0.3066 381 THR A OG1 2936 C CG2 . THR A 381 ? 1.2345 1.4438 1.8913 -0.0938 -0.2470 0.3212 381 THR A CG2 2937 N N . GLY A 382 ? 1.2062 1.2376 1.6629 -0.0988 -0.2174 0.2497 382 GLY A N 2938 C CA . GLY A 382 ? 1.1654 1.1586 1.5593 -0.1113 -0.2052 0.2335 382 GLY A CA 2939 C C . GLY A 382 ? 1.1141 1.0780 1.4657 -0.1456 -0.2234 0.2454 382 GLY A C 2940 O O . GLY A 382 ? 1.1758 1.1434 1.5414 -0.1600 -0.2486 0.2654 382 GLY A O 2941 N N . LEU A 383 ? 1.0780 1.0145 1.3787 -0.1583 -0.2111 0.2320 383 LEU A N 2942 C CA . LEU A 383 ? 1.1135 1.0192 1.3701 -0.1890 -0.2252 0.2362 383 LEU A CA 2943 C C . LEU A 383 ? 1.1044 1.0355 1.3800 -0.2089 -0.2367 0.2523 383 LEU A C 2944 O O . LEU A 383 ? 1.2306 1.1971 1.5357 -0.2041 -0.2231 0.2558 383 LEU A O 2945 C CB . LEU A 383 ? 1.0181 0.8950 1.2260 -0.1945 -0.2061 0.2168 383 LEU A CB 2946 C CG . LEU A 383 ? 0.9877 0.8304 1.1477 -0.2235 -0.2173 0.2148 383 LEU A CG 2947 C CD1 . LEU A 383 ? 1.0721 0.8845 1.2047 -0.2312 -0.2359 0.2177 383 LEU A CD1 2948 C CD2 . LEU A 383 ? 0.9380 0.7616 1.0637 -0.2265 -0.1962 0.1970 383 LEU A CD2 2949 N N . ASN A 384 ? 1.0195 0.9341 1.2777 -0.2327 -0.2626 0.2627 384 ASN A N 2950 C CA . ASN A 384 ? 1.0098 0.9397 1.2775 -0.2569 -0.2765 0.2739 384 ASN A CA 2951 C C . ASN A 384 ? 1.0448 0.9503 1.2741 -0.2728 -0.2635 0.2580 384 ASN A C 2952 O O . ASN A 384 ? 1.0116 0.8776 1.1897 -0.2822 -0.2625 0.2429 384 ASN A O 2953 C CB . ASN A 384 ? 1.0124 0.9336 1.2696 -0.2782 -0.3097 0.2877 384 ASN A CB 2954 C CG . ASN A 384 ? 1.0365 0.9816 1.3165 -0.3013 -0.3280 0.3013 384 ASN A CG 2955 O OD1 . ASN A 384 ? 1.0851 1.0329 1.3658 -0.3118 -0.3181 0.2950 384 ASN A OD1 2956 N ND2 . ASN A 384 ? 1.2126 1.1750 1.5139 -0.3104 -0.3568 0.3214 384 ASN A ND2 2957 N N . ALA A 385 ? 0.9654 0.8960 1.2228 -0.2759 -0.2538 0.2629 385 ALA A N 2958 C CA . ALA A 385 ? 0.9104 0.8203 1.1432 -0.2866 -0.2396 0.2500 385 ALA A CA 2959 C C . ALA A 385 ? 0.9285 0.8072 1.1310 -0.3172 -0.2583 0.2432 385 ALA A C 2960 O O . ALA A 385 ? 0.9867 0.8388 1.1648 -0.3265 -0.2488 0.2285 385 ALA A O 2961 C CB . ALA A 385 ? 1.1233 1.0726 1.4004 -0.2811 -0.2248 0.2620 385 ALA A CB 2962 N N . VAL A 386 ? 1.0254 0.9087 1.2308 -0.3327 -0.2855 0.2530 386 VAL A N 2963 C CA . VAL A 386 ? 0.9421 0.7996 1.1164 -0.3630 -0.3053 0.2437 386 VAL A CA 2964 C C . VAL A 386 ? 1.1171 0.9452 1.2367 -0.3697 -0.3156 0.2325 386 VAL A C 2965 O O . VAL A 386 ? 1.5436 1.3841 1.6680 -0.3652 -0.3305 0.2470 386 VAL A O 2966 C CB . VAL A 386 ? 0.9531 0.8395 1.1653 -0.3819 -0.3321 0.2626 386 VAL A CB 2967 C CG1 . VAL A 386 ? 0.9760 0.8348 1.1534 -0.4144 -0.3526 0.2479 386 VAL A CG1 2968 C CG2 . VAL A 386 ? 0.9104 0.8324 1.1810 -0.3763 -0.3217 0.2781 386 VAL A CG2 2969 N N . PRO A 387 ? 0.9771 0.7682 1.0471 -0.3803 -0.3074 0.2081 387 PRO A N 2970 C CA . PRO A 387 ? 1.2632 1.0299 1.2773 -0.3885 -0.3140 0.1970 387 PRO A CA 2971 C C . PRO A 387 ? 1.2014 0.9762 1.2012 -0.4134 -0.3465 0.2057 387 PRO A C 2972 O O . PRO A 387 ? 1.1706 0.9477 1.1753 -0.4349 -0.3611 0.2008 387 PRO A O 2973 C CB . PRO A 387 ? 0.9948 0.7277 0.9698 -0.3961 -0.2972 0.1676 387 PRO A CB 2974 C CG . PRO A 387 ? 1.1001 0.8365 1.1092 -0.4035 -0.2958 0.1649 387 PRO A CG 2975 C CD . PRO A 387 ? 1.0482 0.8209 1.1158 -0.3862 -0.2925 0.1908 387 PRO A CD 2976 N N . SER A 388 ? 1.0353 0.8146 1.0191 -0.4115 -0.3592 0.2194 388 SER A N 2977 C CA . SER A 388 ? 1.2002 0.9928 1.1709 -0.4348 -0.3923 0.2330 388 SER A CA 2978 C C . SER A 388 ? 1.2141 0.9845 1.1151 -0.4602 -0.3986 0.2118 388 SER A C 2979 O O . SER A 388 ? 1.1553 0.9365 1.0364 -0.4857 -0.4258 0.2159 388 SER A O 2980 C CB . SER A 388 ? 1.2335 1.0436 1.2247 -0.4217 -0.4059 0.2623 388 SER A CB 2981 O OG . SER A 388 ? 1.1762 0.9643 1.1328 -0.4114 -0.3927 0.2577 388 SER A OG 2982 N N . GLN A 389 ? 1.2033 0.9465 1.0674 -0.4536 -0.3734 0.1885 389 GLN A N 2983 C CA . GLN A 389 ? 1.4073 1.1331 1.2053 -0.4751 -0.3743 0.1651 389 GLN A CA 2984 C C . GLN A 389 ? 1.2755 0.9732 1.0538 -0.4678 -0.3437 0.1325 389 GLN A C 2985 O O . GLN A 389 ? 1.1030 0.7928 0.9030 -0.4436 -0.3202 0.1331 389 GLN A O 2986 C CB . GLN A 389 ? 1.1708 0.9006 0.9328 -0.4778 -0.3824 0.1813 389 GLN A CB 2987 C CG . GLN A 389 ? 1.2215 0.9458 0.9130 -0.5045 -0.3879 0.1623 389 GLN A CG 2988 C CD . GLN A 389 ? 1.3091 1.0437 0.9687 -0.5106 -0.3997 0.1863 389 GLN A CD 2989 O OE1 . GLN A 389 ? 1.8285 1.5660 1.5194 -0.4920 -0.4004 0.2136 389 GLN A OE1 2990 N NE2 . GLN A 389 ? 1.2940 1.0352 0.8919 -0.5374 -0.4095 0.1761 389 GLN A NE2 2991 N N . ILE A 390 ? 1.3022 0.9863 1.0406 -0.4887 -0.3448 0.1030 390 ILE A N 2992 C CA . ILE A 390 ? 1.4109 1.0684 1.1307 -0.4829 -0.3174 0.0700 390 ILE A CA 2993 C C . ILE A 390 ? 1.5769 1.2281 1.2300 -0.4956 -0.3118 0.0504 390 ILE A C 2994 O O . ILE A 390 ? 1.8499 1.5115 1.4644 -0.5204 -0.3315 0.0445 390 ILE A O 2995 C CB . ILE A 390 ? 1.1914 0.8352 0.9310 -0.4936 -0.3191 0.0464 390 ILE A CB 2996 C CG1 . ILE A 390 ? 1.3606 1.0026 1.1622 -0.4728 -0.3055 0.0582 390 ILE A CG1 2997 C CG2 . ILE A 390 ? 1.2226 0.8410 0.9213 -0.5011 -0.3029 0.0049 390 ILE A CG2 2998 C CD1 . ILE A 390 ? 1.5451 1.2161 1.3954 -0.4657 -0.3204 0.0944 390 ILE A CD1 2999 N N . LEU A 391 ? 1.4007 1.0391 1.0404 -0.4795 -0.2851 0.0416 391 LEU A N 3000 C CA . LEU A 391 ? 1.3901 1.0257 0.9701 -0.4902 -0.2749 0.0220 391 LEU A CA 3001 C C . LEU A 391 ? 1.2355 0.8488 0.8073 -0.4860 -0.2500 -0.0177 391 LEU A C 3002 O O . LEU A 391 ? 1.1979 0.7980 0.7959 -0.4643 -0.2274 -0.0202 391 LEU A O 3003 C CB . LEU A 391 ? 1.4174 1.0586 0.9872 -0.4775 -0.2652 0.0444 391 LEU A CB 3004 C CG . LEU A 391 ? 1.2887 0.9484 0.8716 -0.4781 -0.2886 0.0851 391 LEU A CG 3005 C CD1 . LEU A 391 ? 1.3098 0.9690 0.8795 -0.4682 -0.2780 0.1016 391 LEU A CD1 3006 C CD2 . LEU A 391 ? 1.3163 0.9957 0.8674 -0.5065 -0.3182 0.0925 391 LEU A CD2 3007 N N . GLU A 392 ? 1.2857 0.8959 0.8224 -0.5067 -0.2550 -0.0496 392 GLU A N 3008 C CA . GLU A 392 ? 1.3226 0.9114 0.8515 -0.5027 -0.2318 -0.0909 392 GLU A CA 3009 C C . GLU A 392 ? 1.4631 1.0620 0.9280 -0.5143 -0.2201 -0.1140 392 GLU A C 3010 O O . GLU A 392 ? 1.7619 1.3747 1.1822 -0.5386 -0.2349 -0.1287 392 GLU A O 3011 C CB . GLU A 392 ? 1.4563 1.0291 1.0051 -0.5148 -0.2437 -0.1169 392 GLU A CB 3012 C CG . GLU A 392 ? 1.6907 1.2818 1.2175 -0.5407 -0.2748 -0.1145 392 GLU A CG 3013 C CD . GLU A 392 ? 1.9950 1.5758 1.5534 -0.5428 -0.2819 -0.1388 392 GLU A CD 3014 O OE1 . GLU A 392 ? 1.9832 1.5395 1.5821 -0.5274 -0.2655 -0.1552 392 GLU A OE1 3015 O OE2 . GLU A 392 ? 2.0323 1.6301 1.5773 -0.5606 -0.3050 -0.1400 392 GLU A OE2 3016 N N . GLY A 393 ? 1.3195 0.9153 0.7798 -0.4977 -0.1933 -0.1166 393 GLY A N 3017 C CA . GLY A 393 ? 1.6335 1.2434 1.0379 -0.5068 -0.1779 -0.1366 393 GLY A CA 3018 C C . GLY A 393 ? 1.5934 1.1912 0.9820 -0.5122 -0.1644 -0.1889 393 GLY A C 3019 O O . GLY A 393 ? 1.7587 1.3301 1.1898 -0.4968 -0.1524 -0.2080 393 GLY A O 3020 N N . GLN A 394 ? 1.5406 1.1589 0.8693 -0.5341 -0.1665 -0.2124 394 GLN A N 3021 C CA . GLN A 394 ? 1.9768 1.5876 1.2909 -0.5365 -0.1518 -0.2665 394 GLN A CA 3022 C C . GLN A 394 ? 1.8948 1.5180 1.1755 -0.5314 -0.1201 -0.2891 394 GLN A C 3023 O O . GLN A 394 ? 1.7361 1.3943 0.9615 -0.5463 -0.1177 -0.2851 394 GLN A O 3024 C CB . GLN A 394 ? 2.2786 1.9127 1.5599 -0.5555 -0.1711 -0.2811 394 GLN A CB 3025 C CG . GLN A 394 ? 2.3705 1.9986 1.6826 -0.5634 -0.2040 -0.2583 394 GLN A CG 3026 C CD . GLN A 394 ? 2.3696 2.0216 1.6616 -0.5786 -0.2286 -0.2082 394 GLN A CD 3027 O OE1 . GLN A 394 ? 2.2348 1.9015 1.4970 -0.5818 -0.2223 -0.1858 394 GLN A OE1 3028 N NE2 . GLN A 394 ? 2.2497 1.9062 1.5617 -0.5882 -0.2582 -0.1893 394 GLN A NE2 3029 N N . TRP A 395 ? 2.0784 1.6781 1.3996 -0.5080 -0.0954 -0.3089 395 TRP A N 3030 C CA . TRP A 395 ? 1.8549 1.4671 1.1574 -0.4987 -0.0627 -0.3349 395 TRP A CA 3031 C C . TRP A 395 ? 2.0010 1.5805 1.3512 -0.4786 -0.0443 -0.3741 395 TRP A C 3032 O O . TRP A 395 ? 1.9986 1.5474 1.4076 -0.4641 -0.0510 -0.3610 395 TRP A O 3033 C CB . TRP A 395 ? 1.6122 1.2401 0.9199 -0.4864 -0.0499 -0.2945 395 TRP A CB 3034 C CG . TRP A 395 ? 1.7251 1.3862 0.9851 -0.5064 -0.0651 -0.2586 395 TRP A CG 3035 C CD1 . TRP A 395 ? 1.7166 1.3782 0.9915 -0.5068 -0.0858 -0.2085 395 TRP A CD1 3036 C CD2 . TRP A 395 ? 1.5792 1.2793 0.7711 -0.5293 -0.0616 -0.2690 395 TRP A CD2 3037 N NE1 . TRP A 395 ? 1.5565 1.2515 0.7809 -0.5282 -0.0970 -0.1849 395 TRP A NE1 3038 C CE2 . TRP A 395 ? 1.5486 1.2696 0.7194 -0.5435 -0.0826 -0.2195 395 TRP A CE2 3039 C CE3 . TRP A 395 ? 1.8532 1.5750 1.0008 -0.5390 -0.0423 -0.3156 395 TRP A CE3 3040 C CZ2 . TRP A 395 ? 1.9743 1.7375 1.0810 -0.5687 -0.0864 -0.2105 395 TRP A CZ2 3041 C CZ3 . TRP A 395 ? 2.1166 1.8855 1.2021 -0.5611 -0.0433 -0.3074 395 TRP A CZ3 3042 C CH2 . TRP A 395 ? 2.2102 1.9982 1.2699 -0.5795 -0.0666 -0.2551 395 TRP A CH2 3043 N N . ALA A 396 ? 2.1034 1.6958 1.4367 -0.4733 -0.0207 -0.4171 396 ALA A N 3044 C CA . ALA A 396 ? 1.9501 1.5147 1.3350 -0.4509 -0.0046 -0.4549 396 ALA A CA 3045 C C . ALA A 396 ? 1.8643 1.4168 1.2822 -0.4313 0.0211 -0.4493 396 ALA A C 3046 O O . ALA A 396 ? 1.8750 1.4586 1.2675 -0.4287 0.0391 -0.4368 396 ALA A O 3047 C CB . ALA A 396 ? 2.0297 1.6142 1.3885 -0.4506 0.0081 -0.5055 396 ALA A CB 3048 N N . ALA A 397 ? 1.7985 1.3141 1.2840 -0.4120 0.0213 -0.4497 397 ALA A N 3049 C CA . ALA A 397 ? 1.6498 1.1603 1.1827 -0.3855 0.0431 -0.4379 397 ALA A CA 3050 C C . ALA A 397 ? 1.9789 1.4950 1.5138 -0.3739 0.0727 -0.4868 397 ALA A C 3051 O O . ALA A 397 ? 2.2571 1.7564 1.8109 -0.3689 0.0727 -0.5271 397 ALA A O 3052 C CB . ALA A 397 ? 1.6278 1.1012 1.2316 -0.3707 0.0316 -0.4185 397 ALA A CB 3053 N N . ARG A 398 ? 1.8995 1.4458 1.4238 -0.3644 0.0963 -0.4779 398 ARG A N 3054 C CA . ARG A 398 ? 1.9077 1.4659 1.4393 -0.3509 0.1271 -0.5215 398 ARG A CA 3055 C C . ARG A 398 ? 1.7639 1.3132 1.3608 -0.3226 0.1435 -0.5059 398 ARG A C 3056 O O . ARG A 398 ? 1.9520 1.4698 1.6069 -0.3051 0.1472 -0.5270 398 ARG A O 3057 C CB . ARG A 398 ? 1.8125 1.4224 1.2757 -0.3654 0.1442 -0.5300 398 ARG A CB 3058 C CG . ARG A 398 ? 1.7700 1.4065 1.1985 -0.3787 0.1334 -0.4747 398 ARG A CG 3059 C CD . ARG A 398 ? 1.9005 1.5900 1.2729 -0.3907 0.1539 -0.4795 398 ARG A CD 3060 N NE . ARG A 398 ? 2.1064 1.8176 1.4545 -0.4024 0.1432 -0.4245 398 ARG A NE 3061 C CZ . ARG A 398 ? 2.0373 1.7532 1.4165 -0.3891 0.1512 -0.3902 398 ARG A CZ 3062 N NH1 . ARG A 398 ? 1.9599 1.6637 1.3944 -0.3640 0.1697 -0.4024 398 ARG A NH1 3063 N NH2 . ARG A 398 ? 1.9378 1.6701 1.2951 -0.4012 0.1392 -0.3435 398 ARG A NH2 3064 N N . SER A 399 ? 1.6866 1.2634 1.2761 -0.3192 0.1515 -0.4678 399 SER A N 3065 C CA . SER A 399 ? 1.8502 1.4250 1.4970 -0.2948 0.1654 -0.4497 399 SER A CA 3066 C C . SER A 399 ? 1.9705 1.5126 1.6676 -0.2855 0.1445 -0.4123 399 SER A C 3067 O O . SER A 399 ? 1.8150 1.3350 1.5738 -0.2658 0.1485 -0.4151 399 SER A O 3068 C CB . SER A 399 ? 1.7427 1.3593 1.3635 -0.2969 0.1794 -0.4225 399 SER A CB 3069 O OG . SER A 399 ? 1.7329 1.3490 1.4083 -0.2751 0.1894 -0.4022 399 SER A OG 3070 N N . MET A 400 ? 1.9688 1.5107 1.6405 -0.2998 0.1222 -0.3762 400 MET A N 3071 C CA . MET A 400 ? 1.6290 1.1492 1.3414 -0.2926 0.1036 -0.3380 400 MET A CA 3072 C C . MET A 400 ? 1.7491 1.2582 1.4358 -0.3118 0.0767 -0.3255 400 MET A C 3073 O O . MET A 400 ? 1.9428 1.4612 1.5801 -0.3304 0.0722 -0.3456 400 MET A O 3074 C CB . MET A 400 ? 1.2391 0.7803 0.9571 -0.2845 0.1081 -0.2979 400 MET A CB 3075 C CG . MET A 400 ? 1.1966 0.7620 0.8597 -0.3019 0.1006 -0.2749 400 MET A CG 3076 S SD . MET A 400 ? 1.3001 0.8805 0.9788 -0.2923 0.1003 -0.2288 400 MET A SD 3077 C CE . MET A 400 ? 1.5440 1.0970 1.2746 -0.2803 0.0820 -0.2047 400 MET A CE 3078 N N . PRO A 401 ? 1.6273 1.1203 1.3477 -0.3079 0.0587 -0.2925 401 PRO A N 3079 C CA . PRO A 401 ? 1.4142 0.9033 1.1109 -0.3260 0.0336 -0.2775 401 PRO A CA 3080 C C . PRO A 401 ? 1.2579 0.7751 0.8983 -0.3404 0.0293 -0.2597 401 PRO A C 3081 O O . PRO A 401 ? 1.3193 0.8532 0.9575 -0.3331 0.0369 -0.2348 401 PRO A O 3082 C CB . PRO A 401 ? 1.2194 0.6965 0.9646 -0.3159 0.0207 -0.2406 401 PRO A CB 3083 C CG . PRO A 401 ? 1.3566 0.8381 1.1380 -0.2945 0.0385 -0.2304 401 PRO A CG 3084 C CD . PRO A 401 ? 1.6980 1.1770 1.4801 -0.2888 0.0589 -0.2704 401 PRO A CD 3085 N N . PRO A 402 ? 1.3066 0.8288 0.9035 -0.3617 0.0155 -0.2712 402 PRO A N 3086 C CA . PRO A 402 ? 1.4397 0.9889 0.9842 -0.3776 0.0085 -0.2517 402 PRO A CA 3087 C C . PRO A 402 ? 1.5372 1.0850 1.0962 -0.3777 -0.0126 -0.2080 402 PRO A C 3088 O O . PRO A 402 ? 1.8854 1.4339 1.4272 -0.3934 -0.0347 -0.1996 402 PRO A O 3089 C CB . PRO A 402 ? 1.6484 1.2028 1.1479 -0.4001 -0.0011 -0.2811 402 PRO A CB 3090 C CG . PRO A 402 ? 1.3150 0.8374 0.8522 -0.3978 -0.0105 -0.3044 402 PRO A CG 3091 C CD . PRO A 402 ? 1.2700 0.7713 0.8723 -0.3733 -0.0012 -0.2931 402 PRO A CD 3092 N N . SER A 403 ? 1.2545 0.8020 0.8458 -0.3602 -0.0060 -0.1824 403 SER A N 3093 C CA . SER A 403 ? 1.1477 0.6919 0.7636 -0.3556 -0.0232 -0.1468 403 SER A CA 3094 C C . SER A 403 ? 1.2755 0.8347 0.8552 -0.3718 -0.0416 -0.1255 403 SER A C 3095 O O . SER A 403 ? 1.6400 1.2155 1.1906 -0.3765 -0.0368 -0.1152 403 SER A O 3096 C CB . SER A 403 ? 1.1757 0.7232 0.8224 -0.3358 -0.0115 -0.1263 403 SER A CB 3097 O OG . SER A 403 ? 1.1085 0.6476 0.7844 -0.3216 0.0070 -0.1449 403 SER A OG 3098 N N . PHE A 404 ? 1.4773 1.0315 1.0640 -0.3805 -0.0638 -0.1156 404 PHE A N 3099 C CA . PHE A 404 ? 1.1381 0.7067 0.6950 -0.3967 -0.0846 -0.0949 404 PHE A CA 3100 C C . PHE A 404 ? 1.2387 0.8075 0.8313 -0.3857 -0.0977 -0.0606 404 PHE A C 3101 O O . PHE A 404 ? 1.6611 1.2214 1.2913 -0.3792 -0.1045 -0.0567 404 PHE A O 3102 C CB . PHE A 404 ? 1.3120 0.8803 0.8460 -0.4176 -0.1016 -0.1125 404 PHE A CB 3103 C CG . PHE A 404 ? 1.3110 0.8967 0.8159 -0.4356 -0.1257 -0.0888 404 PHE A CG 3104 C CD1 . PHE A 404 ? 1.3370 0.9429 0.7898 -0.4515 -0.1255 -0.0878 404 PHE A CD1 3105 C CD2 . PHE A 404 ? 1.3261 0.9116 0.8584 -0.4369 -0.1489 -0.0652 404 PHE A CD2 3106 C CE1 . PHE A 404 ? 1.2553 0.8784 0.6842 -0.4687 -0.1499 -0.0618 404 PHE A CE1 3107 C CE2 . PHE A 404 ? 1.2521 0.8548 0.7631 -0.4525 -0.1726 -0.0413 404 PHE A CE2 3108 C CZ . PHE A 404 ? 1.3093 0.9297 0.7687 -0.4685 -0.1741 -0.0387 404 PHE A CZ 3109 N N . GLY A 405 ? 1.2099 0.7897 0.7922 -0.3842 -0.1012 -0.0360 405 GLY A N 3110 C CA . GLY A 405 ? 1.0421 0.6216 0.6617 -0.3669 -0.1044 -0.0105 405 GLY A CA 3111 C C . GLY A 405 ? 1.5080 1.0845 1.1376 -0.3510 -0.0814 -0.0162 405 GLY A C 3112 O O . GLY A 405 ? 2.0734 1.6531 1.6756 -0.3565 -0.0678 -0.0301 405 GLY A O 3113 N N . TYR A 406 ? 1.3356 0.9103 1.0037 -0.3324 -0.0776 -0.0047 406 TYR A N 3114 C CA . TYR A 406 ? 1.2311 0.8057 0.9132 -0.3167 -0.0588 -0.0071 406 TYR A CA 3115 C C . TYR A 406 ? 0.9702 0.5505 0.6353 -0.3178 -0.0592 0.0065 406 TYR A C 3116 O O . TYR A 406 ? 1.3527 0.9343 1.0324 -0.3051 -0.0495 0.0105 406 TYR A O 3117 C CB . TYR A 406 ? 0.9621 0.5317 0.6387 -0.3166 -0.0400 -0.0327 406 TYR A CB 3118 C CG . TYR A 406 ? 1.1803 0.7516 0.8805 -0.2996 -0.0223 -0.0342 406 TYR A CG 3119 C CD1 . TYR A 406 ? 1.1619 0.7299 0.9004 -0.2862 -0.0181 -0.0333 406 TYR A CD1 3120 C CD2 . TYR A 406 ? 1.2935 0.8722 0.9786 -0.2987 -0.0108 -0.0342 406 TYR A CD2 3121 C CE1 . TYR A 406 ? 1.4027 0.9756 1.1621 -0.2718 -0.0039 -0.0323 406 TYR A CE1 3122 C CE2 . TYR A 406 ? 1.2594 0.8422 0.9671 -0.2843 0.0035 -0.0349 406 TYR A CE2 3123 C CZ . TYR A 406 ? 1.3897 0.9700 1.1336 -0.2708 0.0065 -0.0341 406 TYR A CZ 3124 O OH . TYR A 406 ? 1.2649 0.8525 1.0305 -0.2576 0.0187 -0.0324 406 TYR A OH 3125 N N . SER A 407 ? 0.9767 0.5606 0.6118 -0.3344 -0.0722 0.0147 407 SER A N 3126 C CA . SER A 407 ? 1.4454 1.0325 1.0708 -0.3378 -0.0799 0.0350 407 SER A CA 3127 C C . SER A 407 ? 1.2018 0.7924 0.8151 -0.3516 -0.1040 0.0528 407 SER A C 3128 O O . SER A 407 ? 1.0364 0.6327 0.6205 -0.3689 -0.1099 0.0457 407 SER A O 3129 C CB . SER A 407 ? 1.4328 1.0265 1.0283 -0.3476 -0.0662 0.0289 407 SER A CB 3130 O OG . SER A 407 ? 1.5948 1.1967 1.1535 -0.3656 -0.0645 0.0150 407 SER A OG 3131 N N . MET A 408 ? 1.3137 0.9020 0.9500 -0.3441 -0.1185 0.0750 408 MET A N 3132 C CA . MET A 408 ? 1.2170 0.8096 0.8499 -0.3551 -0.1435 0.0960 408 MET A CA 3133 C C . MET A 408 ? 1.2419 0.8297 0.8940 -0.3489 -0.1557 0.1206 408 MET A C 3134 O O . MET A 408 ? 1.4284 1.0087 1.1088 -0.3305 -0.1477 0.1188 408 MET A O 3135 C CB . MET A 408 ? 1.0579 0.6536 0.7171 -0.3495 -0.1541 0.0957 408 MET A CB 3136 C CG . MET A 408 ? 1.0443 0.6428 0.6855 -0.3617 -0.1519 0.0760 408 MET A CG 3137 S SD . MET A 408 ? 1.1799 0.7836 0.8591 -0.3571 -0.1671 0.0814 408 MET A SD 3138 C CE . MET A 408 ? 0.9570 0.5599 0.6852 -0.3278 -0.1531 0.0849 408 MET A CE 3139 N N . LYS A 409 ? 1.0802 0.6722 0.7174 -0.3648 -0.1762 0.1434 409 LYS A N 3140 C CA . LYS A 409 ? 1.1814 0.7657 0.8451 -0.3588 -0.1927 0.1693 409 LYS A CA 3141 C C . LYS A 409 ? 1.0950 0.6872 0.7643 -0.3689 -0.2212 0.1946 409 LYS A C 3142 O O . LYS A 409 ? 1.1010 0.7053 0.7332 -0.3923 -0.2317 0.2041 409 LYS A O 3143 C CB . LYS A 409 ? 1.2275 0.8071 0.8722 -0.3692 -0.1888 0.1796 409 LYS A CB 3144 C CG . LYS A 409 ? 1.3860 0.9489 1.0692 -0.3558 -0.1979 0.1958 409 LYS A CG 3145 C CD . LYS A 409 ? 1.5608 1.1149 1.2788 -0.3291 -0.1830 0.1742 409 LYS A CD 3146 C CE . LYS A 409 ? 1.7782 1.3149 1.5350 -0.3149 -0.1921 0.1841 409 LYS A CE 3147 N NZ . LYS A 409 ? 1.8487 1.3822 1.6341 -0.2900 -0.1770 0.1607 409 LYS A NZ 3148 N N . GLY A 410 ? 1.1542 0.7429 0.8703 -0.3513 -0.2334 0.2049 410 GLY A N 3149 C CA . GLY A 410 ? 1.2913 0.8884 1.0231 -0.3577 -0.2618 0.2317 410 GLY A CA 3150 C C . GLY A 410 ? 1.2764 0.8614 1.0420 -0.3502 -0.2792 0.2587 410 GLY A C 3151 O O . GLY A 410 ? 1.2551 0.8252 1.0182 -0.3494 -0.2727 0.2609 410 GLY A O 3152 N N . ALA A 411 ? 1.3381 0.9297 1.1393 -0.3450 -0.3026 0.2796 411 ALA A N 3153 C CA . ALA A 411 ? 1.3457 0.9243 1.1961 -0.3309 -0.3201 0.3023 411 ALA A CA 3154 C C . ALA A 411 ? 1.2922 0.8589 1.1288 -0.3484 -0.3357 0.3315 411 ALA A C 3155 O O . ALA A 411 ? 1.4630 1.0086 1.3367 -0.3357 -0.3415 0.3410 411 ALA A O 3156 C CB . ALA A 411 ? 1.3348 0.8986 1.2241 -0.3009 -0.3014 0.2788 411 ALA A CB 3157 N N . THR A 412 ? 1.1649 0.7461 0.9494 -0.3782 -0.3427 0.3455 412 THR A N 3158 C CA . THR A 412 ? 1.2050 0.7826 0.9754 -0.3988 -0.3601 0.3802 412 THR A CA 3159 C C . THR A 412 ? 1.2447 0.8500 0.9753 -0.4284 -0.3813 0.4057 412 THR A C 3160 O O . THR A 412 ? 1.4294 1.0542 1.1145 -0.4416 -0.3710 0.3855 412 THR A O 3161 C CB . THR A 412 ? 1.3666 0.9356 1.1022 -0.4081 -0.3378 0.3683 412 THR A CB 3162 O OG1 . THR A 412 ? 1.5980 1.1429 1.3699 -0.3820 -0.3204 0.3448 412 THR A OG1 3163 C CG2 . THR A 412 ? 1.2472 0.8184 0.9731 -0.4292 -0.3554 0.4061 412 THR A CG2 3164 N N . ASP A 413 ? 1.2806 0.8877 1.0292 -0.4393 -0.4121 0.4497 413 ASP A N 3165 C CA . ASP A 413 ? 1.3232 0.9606 1.0346 -0.4689 -0.4360 0.4784 413 ASP A CA 3166 C C . ASP A 413 ? 1.5291 1.1864 1.1965 -0.4937 -0.4338 0.4915 413 ASP A C 3167 O O . ASP A 413 ? 1.8366 1.4953 1.5376 -0.4901 -0.4446 0.5134 413 ASP A O 3168 C CB . ASP A 413 ? 1.3366 0.9831 1.1071 -0.4593 -0.4696 0.5103 413 ASP A CB 3169 C CG . ASP A 413 ? 1.6948 1.3793 1.4323 -0.4881 -0.4953 0.5359 413 ASP A CG 3170 O OD1 . ASP A 413 ? 2.1066 1.8062 1.7767 -0.5114 -0.4880 0.5226 413 ASP A OD1 3171 O OD2 . ASP A 413 ? 1.4009 1.1008 1.1814 -0.4876 -0.5230 0.5678 413 ASP A OD2 3172 N N . ILE A 414 ? 1.4556 1.1300 1.0493 -0.5188 -0.4190 0.4771 414 ILE A N 3173 C CA . ILE A 414 ? 1.4065 1.1059 0.9544 -0.5424 -0.4108 0.4839 414 ILE A CA 3174 C C . ILE A 414 ? 1.4579 1.2001 0.9804 -0.5701 -0.4362 0.5131 414 ILE A C 3175 O O . ILE A 414 ? 1.4906 1.2592 0.9907 -0.5891 -0.4351 0.5279 414 ILE A O 3176 C CB . ILE A 414 ? 1.3997 1.1006 0.8829 -0.5533 -0.3772 0.4473 414 ILE A CB 3177 C CG1 . ILE A 414 ? 1.5911 1.3115 1.0436 -0.5693 -0.3616 0.4514 414 ILE A CG1 3178 C CG2 . ILE A 414 ? 1.4164 1.1456 0.8527 -0.5677 -0.3779 0.4249 414 ILE A CG2 3179 C CD1 . ILE A 414 ? 1.5110 1.2331 0.9145 -0.5733 -0.3252 0.4120 414 ILE A CD1 3180 N N . ASP A 415 ? 1.5995 1.3514 1.1287 -0.5729 -0.4587 0.5216 415 ASP A N 3181 C CA . ASP A 415 ? 1.5147 1.3092 1.0242 -0.5992 -0.4838 0.5475 415 ASP A CA 3182 C C . ASP A 415 ? 1.5265 1.3241 1.1071 -0.5906 -0.5143 0.5883 415 ASP A C 3183 O O . ASP A 415 ? 1.5855 1.4185 1.1606 -0.6122 -0.5362 0.6167 415 ASP A O 3184 C CB . ASP A 415 ? 1.5221 1.3304 0.9977 -0.6100 -0.4928 0.5323 415 ASP A CB 3185 C CG . ASP A 415 ? 1.9972 1.7687 1.4960 -0.5849 -0.4854 0.5092 415 ASP A CG 3186 O OD1 . ASP A 415 ? 2.2780 2.0221 1.7875 -0.5651 -0.4552 0.4803 415 ASP A OD1 3187 O OD2 . ASP A 415 ? 1.8973 1.6755 1.4191 -0.5805 -0.5039 0.5103 415 ASP A OD2 3188 N N . LYS A 416 ? 1.4905 1.2517 1.1385 -0.5586 -0.5145 0.5892 416 LYS A N 3189 C CA . LYS A 416 ? 1.4978 1.2559 1.2229 -0.5437 -0.5424 0.6218 416 LYS A CA 3190 C C . LYS A 416 ? 1.6353 1.4174 1.3732 -0.5515 -0.5700 0.6393 416 LYS A C 3191 O O . LYS A 416 ? 1.5662 1.3674 1.3428 -0.5573 -0.5971 0.6746 416 LYS A O 3192 C CB . LYS A 416 ? 1.5362 1.3101 1.2726 -0.5575 -0.5525 0.6531 416 LYS A CB 3193 C CG . LYS A 416 ? 1.5203 1.2703 1.2581 -0.5476 -0.5290 0.6397 416 LYS A CG 3194 C CD . LYS A 416 ? 1.8941 1.6585 1.6548 -0.5599 -0.5434 0.6750 416 LYS A CD 3195 C CE . LYS A 416 ? 1.9238 1.6630 1.6938 -0.5488 -0.5222 0.6623 416 LYS A CE 3196 N NZ . LYS A 416 ? 1.5844 1.3354 1.3831 -0.5604 -0.5383 0.6988 416 LYS A NZ 3197 N N . ASN A 417 ? 1.6951 1.4767 1.4023 -0.5522 -0.5636 0.6151 417 ASN A N 3198 C CA . ASN A 417 ? 1.5114 1.3185 1.2250 -0.5618 -0.5886 0.6277 417 ASN A CA 3199 C C . ASN A 417 ? 1.4766 1.2649 1.2672 -0.5298 -0.6001 0.6307 417 ASN A C 3200 O O . ASN A 417 ? 1.7388 1.5476 1.5457 -0.5337 -0.6207 0.6407 417 ASN A O 3201 C CB . ASN A 417 ? 1.7100 1.5324 1.3459 -0.5838 -0.5782 0.5992 417 ASN A CB 3202 C CG . ASN A 417 ? 1.6926 1.4823 1.3235 -0.5636 -0.5576 0.5639 417 ASN A CG 3203 O OD1 . ASN A 417 ? 1.6764 1.4320 1.3227 -0.5430 -0.5344 0.5493 417 ASN A OD1 3204 N ND2 . ASN A 417 ? 1.4683 1.2702 1.0820 -0.5696 -0.5648 0.5478 417 ASN A ND2 3205 N N . GLY A 418 ? 1.4411 1.1931 1.2802 -0.4982 -0.5856 0.6202 418 GLY A N 3206 C CA . GLY A 418 ? 1.4096 1.1455 1.3256 -0.4649 -0.5922 0.6200 418 GLY A CA 3207 C C . GLY A 418 ? 1.4473 1.1618 1.3535 -0.4490 -0.5700 0.5859 418 GLY A C 3208 O O . GLY A 418 ? 1.4873 1.1859 1.4559 -0.4185 -0.5676 0.5795 418 GLY A O 3209 N N . TYR A 419 ? 1.3639 1.0816 1.1956 -0.4688 -0.5511 0.5603 419 TYR A N 3210 C CA . TYR A 419 ? 1.3173 1.0289 1.1487 -0.4510 -0.5197 0.5105 419 TYR A CA 3211 C C . TYR A 419 ? 1.3011 0.9930 1.0870 -0.4515 -0.4842 0.4766 419 TYR A C 3212 O O . TYR A 419 ? 1.3315 1.0301 1.0574 -0.4775 -0.4818 0.4815 419 TYR A O 3213 C CB . TYR A 419 ? 1.5231 1.2648 1.3239 -0.4691 -0.5269 0.4978 419 TYR A CB 3214 C CG . TYR A 419 ? 1.4076 1.1732 1.2569 -0.4681 -0.5610 0.5282 419 TYR A CG 3215 C CD1 . TYR A 419 ? 1.4413 1.2280 1.2833 -0.4912 -0.5982 0.5745 419 TYR A CD1 3216 C CD2 . TYR A 419 ? 1.3000 1.0715 1.2036 -0.4451 -0.5565 0.5128 419 TYR A CD2 3217 C CE1 . TYR A 419 ? 1.5806 1.3917 1.4705 -0.4902 -0.6309 0.6041 419 TYR A CE1 3218 C CE2 . TYR A 419 ? 1.3102 1.1076 1.2624 -0.4441 -0.5873 0.5411 419 TYR A CE2 3219 C CZ . TYR A 419 ? 1.4802 1.2966 1.4264 -0.4662 -0.6249 0.5864 419 TYR A CZ 3220 O OH . TYR A 419 ? 1.3688 1.2133 1.3669 -0.4650 -0.6571 0.6166 419 TYR A OH 3221 N N . PRO A 420 ? 1.2544 0.9263 1.0692 -0.4230 -0.4561 0.4424 420 PRO A N 3222 C CA . PRO A 420 ? 1.2343 0.8883 1.0152 -0.4199 -0.4222 0.4095 420 PRO A CA 3223 C C . PRO A 420 ? 1.2893 0.9578 1.0101 -0.4379 -0.4053 0.3787 420 PRO A C 3224 O O . PRO A 420 ? 1.6808 1.3679 1.3988 -0.4449 -0.4152 0.3736 420 PRO A O 3225 C CB . PRO A 420 ? 1.1875 0.8230 1.0240 -0.3838 -0.4034 0.3862 420 PRO A CB 3226 C CG . PRO A 420 ? 1.1771 0.8306 1.0573 -0.3728 -0.4182 0.3916 420 PRO A CG 3227 C CD . PRO A 420 ? 1.2573 0.9271 1.1409 -0.3920 -0.4553 0.4345 420 PRO A CD 3228 N N . ASP A 421 ? 1.3390 0.9991 1.0163 -0.4448 -0.3806 0.3576 421 ASP A N 3229 C CA . ASP A 421 ? 1.2901 0.9629 0.9097 -0.4626 -0.3647 0.3277 421 ASP A CA 3230 C C . ASP A 421 ? 1.3496 1.0051 0.9662 -0.4460 -0.3286 0.2887 421 ASP A C 3231 O O . ASP A 421 ? 1.2494 0.8857 0.9047 -0.4224 -0.3173 0.2858 421 ASP A O 3232 C CB . ASP A 421 ? 1.2940 0.9852 0.8529 -0.4950 -0.3730 0.3442 421 ASP A CB 3233 C CG . ASP A 421 ? 1.5710 1.2772 1.1401 -0.5098 -0.4103 0.3928 421 ASP A CG 3234 O OD1 . ASP A 421 ? 1.6771 1.4091 1.2203 -0.5309 -0.4311 0.4019 421 ASP A OD1 3235 O OD2 . ASP A 421 ? 1.9525 1.6442 1.5590 -0.5002 -0.4205 0.4226 421 ASP A OD2 3236 N N . LEU A 422 ? 1.3368 0.8570 1.1831 -0.3722 -0.1736 0.1795 422 LEU A N 3237 C CA . LEU A 422 ? 1.2398 0.7475 1.0726 -0.3614 -0.1554 0.1444 422 LEU A CA 3238 C C . LEU A 422 ? 1.2236 0.7596 1.0253 -0.3741 -0.1402 0.1414 422 LEU A C 3239 O O . LEU A 422 ? 1.2397 0.8125 1.0114 -0.3862 -0.1355 0.1474 422 LEU A O 3240 C CB . LEU A 422 ? 1.1780 0.6794 0.9950 -0.3465 -0.1464 0.1137 422 LEU A CB 3241 C CG . LEU A 422 ? 1.1491 0.6443 0.9499 -0.3363 -0.1272 0.0788 422 LEU A CG 3242 C CD1 . LEU A 422 ? 1.1806 0.6446 1.0099 -0.3241 -0.1277 0.0673 422 LEU A CD1 3243 C CD2 . LEU A 422 ? 1.2486 0.7453 1.0348 -0.3253 -0.1203 0.0558 422 LEU A CD2 3244 N N . ILE A 423 ? 1.1837 0.7044 0.9938 -0.3707 -0.1327 0.1300 423 ILE A N 3245 C CA . ILE A 423 ? 1.2155 0.7594 0.9986 -0.3801 -0.1168 0.1219 423 ILE A CA 3246 C C . ILE A 423 ? 1.1727 0.7067 0.9397 -0.3665 -0.0990 0.0823 423 ILE A C 3247 O O . ILE A 423 ? 1.1867 0.6894 0.9727 -0.3510 -0.0981 0.0649 423 ILE A O 3248 C CB . ILE A 423 ? 1.1868 0.7241 0.9905 -0.3877 -0.1201 0.1385 423 ILE A CB 3249 C CG1 . ILE A 423 ? 1.2196 0.7641 1.0490 -0.4009 -0.1401 0.1812 423 ILE A CG1 3250 C CG2 . ILE A 423 ? 1.1959 0.7618 0.9705 -0.3985 -0.1036 0.1316 423 ILE A CG2 3251 C CD1 . ILE A 423 ? 1.4423 0.9780 1.2998 -0.4083 -0.1460 0.2002 423 ILE A CD1 3252 N N . VAL A 424 ? 1.1727 0.7359 0.9070 -0.3722 -0.0854 0.0682 424 VAL A N 3253 C CA . VAL A 424 ? 1.1420 0.6990 0.8646 -0.3612 -0.0690 0.0332 424 VAL A CA 3254 C C . VAL A 424 ? 1.1495 0.7321 0.8515 -0.3716 -0.0549 0.0250 424 VAL A C 3255 O O . VAL A 424 ? 1.4490 1.0690 1.1281 -0.3836 -0.0511 0.0274 424 VAL A O 3256 C CB . VAL A 424 ? 1.1779 0.7426 0.8873 -0.3544 -0.0662 0.0160 424 VAL A CB 3257 C CG1 . VAL A 424 ? 1.1046 0.6650 0.8071 -0.3444 -0.0502 -0.0171 424 VAL A CG1 3258 C CG2 . VAL A 424 ? 1.3349 0.8755 1.0647 -0.3433 -0.0794 0.0226 424 VAL A CG2 3259 N N . GLY A 425 ? 1.1233 0.6885 0.8345 -0.3668 -0.0471 0.0141 425 GLY A N 3260 C CA . GLY A 425 ? 1.2314 0.8187 0.9263 -0.3757 -0.0336 0.0053 425 GLY A CA 3261 C C . GLY A 425 ? 1.1941 0.7886 0.8752 -0.3686 -0.0183 -0.0281 425 GLY A C 3262 O O . GLY A 425 ? 1.0728 0.6437 0.7640 -0.3537 -0.0161 -0.0460 425 GLY A O 3263 N N . ALA A 426 ? 1.2669 0.8968 0.9276 -0.3794 -0.0084 -0.0362 426 ALA A N 3264 C CA . ALA A 426 ? 1.0969 0.7341 0.7508 -0.3738 0.0061 -0.0686 426 ALA A CA 3265 C C . ALA A 426 ? 1.1262 0.7770 0.7752 -0.3811 0.0174 -0.0744 426 ALA A C 3266 O O . ALA A 426 ? 1.4480 1.1357 1.0811 -0.3955 0.0197 -0.0667 426 ALA A O 3267 C CB . ALA A 426 ? 1.1203 0.7902 0.7582 -0.3779 0.0077 -0.0811 426 ALA A CB 3268 N N . PHE A 427 ? 1.1807 0.8051 0.8432 -0.3714 0.0244 -0.0881 427 PHE A N 3269 C CA . PHE A 427 ? 1.1506 0.7828 0.8115 -0.3776 0.0340 -0.0913 427 PHE A CA 3270 C C . PHE A 427 ? 1.2708 0.9244 0.9246 -0.3776 0.0485 -0.1208 427 PHE A C 3271 O O . PHE A 427 ? 1.4725 1.1395 1.1232 -0.3838 0.0576 -0.1262 427 PHE A O 3272 C CB . PHE A 427 ? 1.1615 0.7560 0.8425 -0.3682 0.0331 -0.0889 427 PHE A CB 3273 C CG . PHE A 427 ? 1.1440 0.7164 0.8371 -0.3524 0.0395 -0.1128 427 PHE A CG 3274 C CD1 . PHE A 427 ? 1.0196 0.5949 0.7149 -0.3504 0.0524 -0.1325 427 PHE A CD1 3275 C CD2 . PHE A 427 ? 1.2806 0.8316 0.9848 -0.3399 0.0322 -0.1140 427 PHE A CD2 3276 C CE1 . PHE A 427 ? 1.1364 0.6948 0.8455 -0.3369 0.0575 -0.1507 427 PHE A CE1 3277 C CE2 . PHE A 427 ? 1.4083 0.9443 1.1246 -0.3263 0.0379 -0.1328 427 PHE A CE2 3278 C CZ . PHE A 427 ? 1.3876 0.9277 1.1068 -0.3251 0.0502 -0.1500 427 PHE A CZ 3279 N N . GLY A 428 ? 1.2684 0.9253 0.9233 -0.3704 0.0500 -0.1401 428 GLY A N 3280 C CA . GLY A 428 ? 1.1202 0.7991 0.7743 -0.3704 0.0615 -0.1693 428 GLY A CA 3281 C C . GLY A 428 ? 1.3815 1.1090 1.0154 -0.3853 0.0641 -0.1707 428 GLY A C 3282 O O . GLY A 428 ? 1.5457 1.2973 1.1767 -0.3906 0.0746 -0.1870 428 GLY A O 3283 N N . VAL A 429 ? 1.4385 1.1838 1.0591 -0.3922 0.0544 -0.1536 429 VAL A N 3284 C CA . VAL A 429 ? 1.2092 1.0073 0.8086 -0.4075 0.0553 -0.1502 429 VAL A CA 3285 C C . VAL A 429 ? 1.2575 1.0658 0.8481 -0.4203 0.0508 -0.1161 429 VAL A C 3286 O O . VAL A 429 ? 1.2997 1.1553 0.8724 -0.4347 0.0502 -0.1052 429 VAL A O 3287 C CB . VAL A 429 ? 1.3168 1.1368 0.9064 -0.4095 0.0468 -0.1497 429 VAL A CB 3288 C CG1 . VAL A 429 ? 1.1792 1.0077 0.7766 -0.4014 0.0526 -0.1873 429 VAL A CG1 3289 C CG2 . VAL A 429 ? 1.3278 1.1109 0.9249 -0.4032 0.0334 -0.1248 429 VAL A CG2 3290 N N . ASP A 430 ? 1.5796 1.3459 1.1850 -0.4150 0.0472 -0.0994 430 ASP A N 3291 C CA . ASP A 430 ? 1.4340 1.2015 1.0398 -0.4256 0.0407 -0.0655 430 ASP A CA 3292 C C . ASP A 430 ? 1.2494 1.0388 0.8468 -0.4360 0.0272 -0.0351 430 ASP A C 3293 O O . ASP A 430 ? 1.2869 1.1210 0.8702 -0.4520 0.0266 -0.0174 430 ASP A O 3294 C CB . ASP A 430 ? 1.2699 1.0714 0.8664 -0.4372 0.0516 -0.0682 430 ASP A CB 3295 C CG . ASP A 430 ? 1.5111 1.2920 1.1179 -0.4277 0.0646 -0.0966 430 ASP A CG 3296 O OD1 . ASP A 430 ? 1.8774 1.6644 1.4856 -0.4339 0.0707 -0.0916 430 ASP A OD1 3297 O OD2 . ASP A 430 ? 1.7327 1.4925 1.3481 -0.4144 0.0682 -0.1223 430 ASP A OD2 3298 N N . ARG A 431 ? 1.2444 1.0046 0.8516 -0.4272 0.0161 -0.0279 431 ARG A N 3299 C CA . ARG A 431 ? 1.2767 1.0550 0.8786 -0.4356 0.0023 -0.0002 431 ARG A CA 3300 C C . ARG A 431 ? 1.2488 0.9808 0.8731 -0.4260 -0.0121 0.0175 431 ARG A C 3301 O O . ARG A 431 ? 1.2015 0.8911 0.8417 -0.4106 -0.0104 0.0015 431 ARG A O 3302 C CB . ARG A 431 ? 1.3074 1.1202 0.8906 -0.4366 0.0046 -0.0191 431 ARG A CB 3303 C CG . ARG A 431 ? 1.4395 1.3153 0.9996 -0.4511 0.0133 -0.0266 431 ARG A CG 3304 C CD . ARG A 431 ? 1.4083 1.3152 0.9548 -0.4492 0.0161 -0.0539 431 ARG A CD 3305 N NE . ARG A 431 ? 1.5938 1.5704 1.1173 -0.4650 0.0200 -0.0544 431 ARG A NE 3306 C CZ . ARG A 431 ? 1.7500 1.7612 1.2651 -0.4687 0.0336 -0.0808 431 ARG A CZ 3307 N NH1 . ARG A 431 ? 1.7987 1.7782 1.3275 -0.4581 0.0443 -0.1070 431 ARG A NH1 3308 N NH2 . ARG A 431 ? 1.7633 1.8439 1.2573 -0.4831 0.0364 -0.0810 431 ARG A NH2 3309 N N . ALA A 432 ? 1.2751 1.0189 0.9022 -0.4354 -0.0266 0.0509 432 ALA A N 3310 C CA . ALA A 432 ? 1.2599 0.9649 0.9109 -0.4272 -0.0421 0.0684 432 ALA A CA 3311 C C . ALA A 432 ? 1.2939 1.0237 0.9373 -0.4345 -0.0541 0.0885 432 ALA A C 3312 O O . ALA A 432 ? 1.3311 1.1064 0.9606 -0.4514 -0.0570 0.1105 432 ALA A O 3313 C CB . ALA A 432 ? 1.3505 1.0331 1.0277 -0.4308 -0.0512 0.0954 432 ALA A CB 3314 N N . ILE A 433 ? 1.2798 0.9828 0.9326 -0.4221 -0.0612 0.0816 433 ILE A N 3315 C CA . ILE A 433 ? 1.3146 1.0393 0.9601 -0.4275 -0.0722 0.0971 433 ILE A CA 3316 C C . ILE A 433 ? 1.3031 0.9938 0.9780 -0.4221 -0.0905 0.1220 433 ILE A C 3317 O O . ILE A 433 ? 1.2705 0.9170 0.9659 -0.4060 -0.0920 0.1085 433 ILE A O 3318 C CB . ILE A 433 ? 1.3177 1.0499 0.9462 -0.4186 -0.0645 0.0644 433 ILE A CB 3319 C CG1 . ILE A 433 ? 1.3499 1.1178 0.9545 -0.4236 -0.0478 0.0370 433 ILE A CG1 3320 C CG2 . ILE A 433 ? 1.3598 1.1153 0.9808 -0.4243 -0.0764 0.0804 433 ILE A CG2 3321 C CD1 . ILE A 433 ? 1.4291 1.1677 1.0410 -0.4105 -0.0340 0.0048 433 ILE A CD1 3322 N N . LEU A 434 ? 1.3268 1.0417 1.0055 -0.4359 -0.1046 0.1585 434 LEU A N 3323 C CA . LEU A 434 ? 1.3165 1.0031 1.0273 -0.4325 -0.1239 0.1848 434 LEU A CA 3324 C C . LEU A 434 ? 1.3403 1.0391 1.0427 -0.4313 -0.1319 0.1878 434 LEU A C 3325 O O . LEU A 434 ? 1.3752 1.1200 1.0585 -0.4460 -0.1354 0.2058 434 LEU A O 3326 C CB . LEU A 434 ? 1.3253 1.0266 1.0560 -0.4491 -0.1371 0.2290 434 LEU A CB 3327 C CG . LEU A 434 ? 1.3167 0.9903 1.0910 -0.4483 -0.1596 0.2618 434 LEU A CG 3328 C CD1 . LEU A 434 ? 1.4174 1.1231 1.1884 -0.4598 -0.1736 0.2926 434 LEU A CD1 3329 C CD2 . LEU A 434 ? 1.3500 0.9681 1.1504 -0.4261 -0.1627 0.2374 434 LEU A CD2 3330 N N . TYR A 435 ? 1.3551 1.0157 1.0719 -0.4138 -0.1348 0.1699 435 TYR A N 3331 C CA . TYR A 435 ? 1.3330 0.9995 1.0458 -0.4109 -0.1432 0.1721 435 TYR A CA 3332 C C . TYR A 435 ? 1.3293 0.9787 1.0763 -0.4123 -0.1647 0.2066 435 TYR A C 3333 O O . TYR A 435 ? 1.3005 0.9110 1.0816 -0.4032 -0.1718 0.2097 435 TYR A O 3334 C CB . TYR A 435 ? 1.3010 0.9399 1.0115 -0.3915 -0.1345 0.1345 435 TYR A CB 3335 C CG . TYR A 435 ? 1.3009 0.9582 0.9827 -0.3901 -0.1154 0.1008 435 TYR A CG 3336 C CD1 . TYR A 435 ? 1.2694 0.9079 0.9534 -0.3826 -0.1021 0.0784 435 TYR A CD1 3337 C CD2 . TYR A 435 ? 1.3880 1.0825 1.0436 -0.3961 -0.1114 0.0907 435 TYR A CD2 3338 C CE1 . TYR A 435 ? 1.2654 0.9201 0.9285 -0.3812 -0.0858 0.0483 435 TYR A CE1 3339 C CE2 . TYR A 435 ? 1.3302 1.0414 0.9661 -0.3944 -0.0953 0.0580 435 TYR A CE2 3340 C CZ . TYR A 435 ? 1.2932 0.9835 0.9339 -0.3870 -0.0827 0.0377 435 TYR A CZ 3341 O OH . TYR A 435 ? 1.2836 0.9899 0.9098 -0.3852 -0.0678 0.0058 435 TYR A OH 3342 N N . ARG A 436 ? 1.3559 1.0364 1.0960 -0.4236 -0.1758 0.2315 436 ARG A N 3343 C CA . ARG A 436 ? 1.3601 1.0297 1.1349 -0.4273 -0.1977 0.2685 436 ARG A CA 3344 C C . ARG A 436 ? 1.3631 1.0161 1.1452 -0.4156 -0.2058 0.2608 436 ARG A C 3345 O O . ARG A 436 ? 1.7575 1.4329 1.5099 -0.4152 -0.1990 0.2447 436 ARG A O 3346 C CB . ARG A 436 ? 1.4213 1.1415 1.1887 -0.4507 -0.2071 0.3107 436 ARG A CB 3347 C CG . ARG A 436 ? 1.5123 1.2632 1.2610 -0.4639 -0.1954 0.3142 436 ARG A CG 3348 C CD . ARG A 436 ? 1.4519 1.2465 1.2078 -0.4867 -0.2083 0.3645 436 ARG A CD 3349 N NE . ARG A 436 ? 1.6674 1.5155 1.3967 -0.4991 -0.2123 0.3795 436 ARG A NE 3350 C CZ . ARG A 436 ? 1.7568 1.6148 1.5060 -0.5062 -0.2320 0.4159 436 ARG A CZ 3351 N NH1 . ARG A 436 ? 1.7178 1.5339 1.5167 -0.5018 -0.2498 0.4404 436 ARG A NH1 3352 N NH2 . ARG A 436 ? 1.7112 1.6223 1.4327 -0.5176 -0.2344 0.4270 436 ARG A NH2 3353 N N . ALA A 437 ? 1.3335 0.9482 1.1577 -0.4059 -0.2207 0.2713 437 ALA A N 3354 C CA . ALA A 437 ? 1.3243 0.9197 1.1601 -0.3929 -0.2285 0.2626 437 ALA A CA 3355 C C . ALA A 437 ? 1.4966 1.1207 1.3334 -0.4055 -0.2445 0.2966 437 ALA A C 3356 O O . ALA A 437 ? 1.5917 1.2267 1.4523 -0.4188 -0.2601 0.3363 437 ALA A O 3357 C CB . ALA A 437 ? 1.2800 0.8267 1.1623 -0.3765 -0.2381 0.2569 437 ALA A CB 3358 N N . ARG A 438 ? 1.5557 1.1932 1.3688 -0.4017 -0.2412 0.2820 438 ARG A N 3359 C CA . ARG A 438 ? 1.4239 1.0873 1.2376 -0.4115 -0.2563 0.3105 438 ARG A CA 3360 C C . ARG A 438 ? 1.3759 1.0018 1.2354 -0.4003 -0.2745 0.3224 438 ARG A C 3361 O O . ARG A 438 ? 1.3483 0.9338 1.2255 -0.3812 -0.2710 0.2952 438 ARG A O 3362 C CB . ARG A 438 ? 1.4490 1.1403 1.2228 -0.4107 -0.2463 0.2873 438 ARG A CB 3363 C CG . ARG A 438 ? 1.6057 1.3334 1.3374 -0.4190 -0.2276 0.2670 438 ARG A CG 3364 C CD . ARG A 438 ? 1.7834 1.5087 1.4912 -0.4068 -0.2133 0.2242 438 ARG A CD 3365 N NE . ARG A 438 ? 1.5668 1.3075 1.2685 -0.4067 -0.2220 0.2273 438 ARG A NE 3366 C CZ . ARG A 438 ? 1.5237 1.3129 1.1945 -0.4175 -0.2193 0.2234 438 ARG A CZ 3367 N NH1 . ARG A 438 ? 1.5598 1.3886 1.2030 -0.4291 -0.2079 0.2155 438 ARG A NH1 3368 N NH2 . ARG A 438 ? 1.5383 1.3386 1.2066 -0.4166 -0.2282 0.2262 438 ARG A NH2 3369 N N . PRO A 439 ? 1.3835 1.0254 1.2641 -0.4122 -0.2945 0.3636 439 PRO A N 3370 C CA . PRO A 439 ? 1.3679 0.9775 1.2950 -0.4021 -0.3134 0.3756 439 PRO A CA 3371 C C . PRO A 439 ? 1.4122 1.0106 1.3273 -0.3871 -0.3096 0.3477 439 PRO A C 3372 O O . PRO A 439 ? 1.7617 1.3883 1.6340 -0.3903 -0.2981 0.3326 439 PRO A O 3373 C CB . PRO A 439 ? 1.3846 1.0261 1.3282 -0.4220 -0.3338 0.4280 439 PRO A CB 3374 C CG . PRO A 439 ? 1.3984 1.0796 1.3174 -0.4413 -0.3268 0.4462 439 PRO A CG 3375 C CD . PRO A 439 ? 1.4112 1.1040 1.2784 -0.4362 -0.3013 0.4032 439 PRO A CD 3376 N N . VAL A 440 ? 1.3505 0.9099 1.3053 -0.3706 -0.3194 0.3400 440 VAL A N 3377 C CA . VAL A 440 ? 1.3819 0.9298 1.3301 -0.3555 -0.3165 0.3150 440 VAL A CA 3378 C C . VAL A 440 ? 1.3990 0.9488 1.3755 -0.3578 -0.3380 0.3432 440 VAL A C 3379 O O . VAL A 440 ? 1.3392 0.8691 1.3651 -0.3567 -0.3561 0.3653 440 VAL A O 3380 C CB . VAL A 440 ? 1.3543 0.8609 1.3231 -0.3325 -0.3089 0.2785 440 VAL A CB 3381 C CG1 . VAL A 440 ? 1.3019 0.7996 1.2695 -0.3175 -0.3081 0.2578 440 VAL A CG1 3382 C CG2 . VAL A 440 ? 1.4292 0.9356 1.3685 -0.3297 -0.2871 0.2497 440 VAL A CG2 3383 N N . ILE A 441 ? 1.4238 0.9977 1.3717 -0.3607 -0.3367 0.3415 441 ILE A N 3384 C CA . ILE A 441 ? 1.4535 1.0327 1.4238 -0.3635 -0.3563 0.3678 441 ILE A CA 3385 C C . ILE A 441 ? 1.3799 0.9366 1.3564 -0.3442 -0.3546 0.3400 441 ILE A C 3386 O O . ILE A 441 ? 1.3857 0.9497 1.3266 -0.3380 -0.3386 0.3099 441 ILE A O 3387 C CB . ILE A 441 ? 1.4391 1.0703 1.3750 -0.3841 -0.3597 0.3937 441 ILE A CB 3388 C CG1 . ILE A 441 ? 1.6226 1.2837 1.5509 -0.4042 -0.3608 0.4231 441 ILE A CG1 3389 C CG2 . ILE A 441 ? 1.4344 1.0717 1.3956 -0.3874 -0.3811 0.4234 441 ILE A CG2 3390 C CD1 . ILE A 441 ? 1.5089 1.2295 1.4032 -0.4254 -0.3641 0.4492 441 ILE A CD1 3391 N N . THR A 442 ? 1.5097 1.0404 1.5348 -0.3347 -0.3717 0.3503 442 THR A N 3392 C CA . THR A 442 ? 1.6071 1.1202 1.6423 -0.3172 -0.3725 0.3284 442 THR A CA 3393 C C . THR A 442 ? 1.5565 1.0892 1.5966 -0.3256 -0.3891 0.3564 442 THR A C 3394 O O . THR A 442 ? 1.4720 1.0012 1.5525 -0.3316 -0.4100 0.3899 442 THR A O 3395 C CB . THR A 442 ? 1.6721 1.1449 1.7600 -0.2981 -0.3796 0.3143 442 THR A CB 3396 O OG1 . THR A 442 ? 1.7463 1.2038 1.8286 -0.2902 -0.3642 0.2875 442 THR A OG1 3397 C CG2 . THR A 442 ? 1.5065 0.9670 1.6035 -0.2802 -0.3797 0.2918 442 THR A CG2 3398 N N . VAL A 443 ? 1.5061 1.0598 1.5077 -0.3262 -0.3805 0.3431 443 VAL A N 3399 C CA . VAL A 443 ? 1.4180 0.9954 1.4176 -0.3351 -0.3946 0.3676 443 VAL A CA 3400 C C . VAL A 443 ? 1.4269 0.9888 1.4341 -0.3184 -0.3948 0.3459 443 VAL A C 3401 O O . VAL A 443 ? 1.5440 1.1008 1.5274 -0.3072 -0.3777 0.3106 443 VAL A O 3402 C CB . VAL A 443 ? 1.4516 1.0775 1.3993 -0.3538 -0.3872 0.3751 443 VAL A CB 3403 C CG1 . VAL A 443 ? 1.5025 1.1321 1.4087 -0.3475 -0.3630 0.3334 443 VAL A CG1 3404 C CG2 . VAL A 443 ? 1.4735 1.1258 1.4152 -0.3608 -0.3998 0.3933 443 VAL A CG2 3405 N N . ASN A 444 ? 1.4559 1.0112 1.4995 -0.3168 -0.4146 0.3683 444 ASN A N 3406 C CA . ASN A 444 ? 1.5257 1.0689 1.5792 -0.3017 -0.4165 0.3511 444 ASN A CA 3407 C C . ASN A 444 ? 1.4930 1.0661 1.5322 -0.3128 -0.4274 0.3727 444 ASN A C 3408 O O . ASN A 444 ? 1.4877 1.0680 1.5544 -0.3221 -0.4478 0.4090 444 ASN A O 3409 C CB . ASN A 444 ? 1.7421 1.2498 1.8552 -0.2860 -0.4300 0.3513 444 ASN A CB 3410 C CG . ASN A 444 ? 1.7107 1.1913 1.8412 -0.2740 -0.4205 0.3279 444 ASN A CG 3411 O OD1 . ASN A 444 ? 1.6293 1.0913 1.8053 -0.2725 -0.4335 0.3412 444 ASN A OD1 3412 N ND2 . ASN A 444 ? 1.5578 1.0371 1.6548 -0.2657 -0.3984 0.2931 444 ASN A ND2 3413 N N . ALA A 445 ? 1.6361 1.2271 1.6347 -0.3119 -0.4144 0.3502 445 ALA A N 3414 C CA . ALA A 445 ? 1.5198 1.1395 1.5028 -0.3202 -0.4229 0.3632 445 ALA A CA 3415 C C . ALA A 445 ? 1.4647 1.0631 1.4812 -0.3055 -0.4337 0.3607 445 ALA A C 3416 O O . ALA A 445 ? 1.4826 1.0479 1.5256 -0.2870 -0.4297 0.3394 445 ALA A O 3417 C CB . ALA A 445 ? 1.5102 1.1562 1.4429 -0.3238 -0.4057 0.3367 445 ALA A CB 3418 N N . GLY A 446 ? 1.5567 1.1775 1.5719 -0.3140 -0.4475 0.3823 446 GLY A N 3419 C CA . GLY A 446 ? 1.7160 1.3219 1.7577 -0.3011 -0.4568 0.3788 446 GLY A CA 3420 C C . GLY A 446 ? 1.5908 1.2307 1.6074 -0.3112 -0.4627 0.3882 446 GLY A C 3421 O O . GLY A 446 ? 1.5348 1.2120 1.5255 -0.3303 -0.4668 0.4096 446 GLY A O 3422 N N . LEU A 447 ? 1.5049 1.1351 1.5295 -0.2984 -0.4631 0.3719 447 LEU A N 3423 C CA . LEU A 447 ? 1.5322 1.1931 1.5338 -0.3060 -0.4677 0.3755 447 LEU A CA 3424 C C . LEU A 447 ? 1.5508 1.1952 1.5831 -0.2927 -0.4780 0.3744 447 LEU A C 3425 O O . LEU A 447 ? 1.5486 1.1613 1.6053 -0.2739 -0.4723 0.3532 447 LEU A O 3426 C CB . LEU A 447 ? 1.5484 1.2268 1.5051 -0.3067 -0.4479 0.3420 447 LEU A CB 3427 C CG . LEU A 447 ? 1.5752 1.2908 1.5034 -0.3161 -0.4506 0.3396 447 LEU A CG 3428 C CD1 . LEU A 447 ? 1.5907 1.3476 1.5058 -0.3377 -0.4650 0.3754 447 LEU A CD1 3429 C CD2 . LEU A 447 ? 1.5810 1.3090 1.4737 -0.3152 -0.4309 0.3028 447 LEU A CD2 3430 N N . GLU A 448 ? 1.5371 1.2064 1.5680 -0.3026 -0.4930 0.3972 448 GLU A N 3431 C CA . GLU A 448 ? 1.5846 1.2428 1.6418 -0.2915 -0.5032 0.3970 448 GLU A CA 3432 C C . GLU A 448 ? 1.6433 1.3393 1.6791 -0.3048 -0.5132 0.4119 448 GLU A C 3433 O O . GLU A 448 ? 1.6048 1.3375 1.6139 -0.3238 -0.5171 0.4308 448 GLU A O 3434 C CB . GLU A 448 ? 1.5640 1.1957 1.6767 -0.2847 -0.5208 0.4205 448 GLU A CB 3435 C CG . GLU A 448 ? 1.8266 1.4757 1.9534 -0.3031 -0.5397 0.4655 448 GLU A CG 3436 C CD . GLU A 448 ? 2.1279 1.7496 2.3178 -0.2955 -0.5594 0.4875 448 GLU A CD 3437 O OE1 . GLU A 448 ? 2.1425 1.7692 2.3557 -0.3078 -0.5740 0.5227 448 GLU A OE1 3438 O OE2 . GLU A 448 ? 2.1720 1.7691 2.3912 -0.2773 -0.5607 0.4698 448 GLU A OE2 3439 N N . VAL A 449 ? 1.5659 1.2562 1.6141 -0.2947 -0.5175 0.4029 449 VAL A N 3440 C CA . VAL A 449 ? 1.5825 1.3079 1.6118 -0.3055 -0.5267 0.4128 449 VAL A CA 3441 C C . VAL A 449 ? 1.6217 1.3399 1.6892 -0.3015 -0.5470 0.4363 449 VAL A C 3442 O O . VAL A 449 ? 1.5251 1.2099 1.6274 -0.2837 -0.5476 0.4259 449 VAL A O 3443 C CB . VAL A 449 ? 1.5789 1.3125 1.5789 -0.2996 -0.5111 0.3750 449 VAL A CB 3444 C CG1 . VAL A 449 ? 1.5751 1.3320 1.5327 -0.3099 -0.4958 0.3575 449 VAL A CG1 3445 C CG2 . VAL A 449 ? 1.5982 1.2931 1.6216 -0.2772 -0.5002 0.3470 449 VAL A CG2 3446 N N . TYR A 450 ? 1.6445 1.3974 1.7058 -0.3182 -0.5636 0.4682 450 TYR A N 3447 C CA . TYR A 450 ? 1.6192 1.3700 1.7166 -0.3170 -0.5848 0.4950 450 TYR A CA 3448 C C . TYR A 450 ? 1.6624 1.4448 1.7382 -0.3226 -0.5899 0.4923 450 TYR A C 3449 O O . TYR A 450 ? 1.8048 1.6322 1.8489 -0.3410 -0.5945 0.5068 450 TYR A O 3450 C CB . TYR A 450 ? 1.6595 1.4248 1.7790 -0.3327 -0.6050 0.5434 450 TYR A CB 3451 C CG . TYR A 450 ? 1.6139 1.3494 1.7647 -0.3291 -0.6055 0.5533 450 TYR A CG 3452 C CD1 . TYR A 450 ? 1.6236 1.3135 1.8005 -0.3081 -0.5952 0.5246 450 TYR A CD1 3453 C CD2 . TYR A 450 ? 1.7419 1.4981 1.8981 -0.3472 -0.6172 0.5923 450 TYR A CD2 3454 C CE1 . TYR A 450 ? 1.9045 1.5686 2.1122 -0.3046 -0.5966 0.5316 450 TYR A CE1 3455 C CE2 . TYR A 450 ? 2.0453 1.7743 2.2341 -0.3444 -0.6191 0.6019 450 TYR A CE2 3456 C CZ . TYR A 450 ? 2.1269 1.8089 2.3416 -0.3228 -0.6089 0.5702 450 TYR A CZ 3457 O OH . TYR A 450 ? 2.0187 1.6748 2.2677 -0.3198 -0.6115 0.5776 450 TYR A OH 3458 N N . PRO A 451 ? 1.5291 1.2917 1.6227 -0.3070 -0.5894 0.4739 451 PRO A N 3459 C CA . PRO A 451 ? 1.5144 1.2339 1.6356 -0.2840 -0.5794 0.4468 451 PRO A CA 3460 C C . PRO A 451 ? 1.5311 1.2460 1.6214 -0.2763 -0.5555 0.4050 451 PRO A C 3461 O O . PRO A 451 ? 1.5349 1.2798 1.5861 -0.2872 -0.5489 0.3940 451 PRO A O 3462 C CB . PRO A 451 ? 1.5195 1.2370 1.6656 -0.2766 -0.5920 0.4518 451 PRO A CB 3463 C CG . PRO A 451 ? 1.5774 1.3381 1.6896 -0.2931 -0.5982 0.4603 451 PRO A CG 3464 C CD . PRO A 451 ? 1.5223 1.3128 1.6112 -0.3134 -0.6025 0.4850 451 PRO A CD 3465 N N . SER A 452 ? 1.6358 1.3166 1.7457 -0.2580 -0.5434 0.3819 452 SER A N 3466 C CA . SER A 452 ? 1.5631 1.2388 1.6497 -0.2500 -0.5216 0.3449 452 SER A CA 3467 C C . SER A 452 ? 1.5131 1.2003 1.5914 -0.2457 -0.5188 0.3267 452 SER A C 3468 O O . SER A 452 ? 1.5109 1.2111 1.5609 -0.2485 -0.5059 0.3034 452 SER A O 3469 C CB . SER A 452 ? 1.6071 1.2480 1.7194 -0.2315 -0.5106 0.3275 452 SER A CB 3470 O OG . SER A 452 ? 1.5551 1.1800 1.7035 -0.2154 -0.5160 0.3238 452 SER A OG 3471 N N . ILE A 453 ? 1.6734 1.3558 1.7801 -0.2387 -0.5315 0.3371 453 ILE A N 3472 C CA . ILE A 453 ? 1.4789 1.1715 1.5830 -0.2343 -0.5306 0.3222 453 ILE A CA 3473 C C . ILE A 453 ? 1.4804 1.2062 1.5687 -0.2505 -0.5460 0.3404 453 ILE A C 3474 O O . ILE A 453 ? 1.4790 1.2086 1.5866 -0.2547 -0.5640 0.3691 453 ILE A O 3475 C CB . ILE A 453 ? 1.4568 1.1270 1.6016 -0.2156 -0.5338 0.3192 453 ILE A CB 3476 C CG1 . ILE A 453 ? 1.4484 1.0928 1.6075 -0.1992 -0.5178 0.2985 453 ILE A CG1 3477 C CG2 . ILE A 453 ? 1.4413 1.1238 1.5854 -0.2123 -0.5341 0.3070 453 ILE A CG2 3478 C CD1 . ILE A 453 ? 1.5142 1.1413 1.7150 -0.1803 -0.5205 0.2948 453 ILE A CD1 3479 N N . LEU A 454 ? 1.4789 1.2306 1.5346 -0.2594 -0.5394 0.3228 454 LEU A N 3480 C CA . LEU A 454 ? 1.4906 1.2815 1.5258 -0.2761 -0.5525 0.3358 454 LEU A CA 3481 C C . LEU A 454 ? 1.4863 1.2839 1.5355 -0.2714 -0.5614 0.3322 454 LEU A C 3482 O O . LEU A 454 ? 1.4949 1.2848 1.5480 -0.2616 -0.5515 0.3051 454 LEU A O 3483 C CB . LEU A 454 ? 1.4990 1.3197 1.4936 -0.2883 -0.5419 0.3155 454 LEU A CB 3484 C CG . LEU A 454 ? 1.5062 1.3219 1.4835 -0.2927 -0.5302 0.3137 454 LEU A CG 3485 C CD1 . LEU A 454 ? 1.5079 1.3588 1.4467 -0.3051 -0.5212 0.2923 454 LEU A CD1 3486 C CD2 . LEU A 454 ? 1.5166 1.3340 1.5020 -0.3015 -0.5430 0.3520 454 LEU A CD2 3487 N N . ASN A 455 ? 1.5342 1.3474 1.5935 -0.2789 -0.5809 0.3612 455 ASN A N 3488 C CA . ASN A 455 ? 1.4862 1.3120 1.5554 -0.2775 -0.5913 0.3602 455 ASN A CA 3489 C C . ASN A 455 ? 1.4889 1.3620 1.5236 -0.2947 -0.5962 0.3551 455 ASN A C 3490 O O . ASN A 455 ? 1.4968 1.4014 1.5157 -0.3107 -0.6080 0.3799 455 ASN A O 3491 C CB . ASN A 455 ? 1.4831 1.3003 1.5856 -0.2753 -0.6105 0.3936 455 ASN A CB 3492 C CG . ASN A 455 ? 1.4779 1.3067 1.5927 -0.2731 -0.6215 0.3933 455 ASN A CG 3493 O OD1 . ASN A 455 ? 1.6169 1.4510 1.7236 -0.2689 -0.6134 0.3658 455 ASN A OD1 3494 N ND2 . ASN A 455 ? 1.4840 1.3166 1.6218 -0.2760 -0.6409 0.4249 455 ASN A ND2 3495 N N . GLN A 456 ? 1.4756 1.3566 1.5015 -0.2913 -0.5878 0.3226 456 GLN A N 3496 C CA . GLN A 456 ? 1.4815 1.4083 1.4766 -0.3057 -0.5902 0.3078 456 GLN A CA 3497 C C . GLN A 456 ? 1.5354 1.4952 1.5314 -0.3156 -0.6109 0.3291 456 GLN A C 3498 O O . GLN A 456 ? 1.6134 1.6207 1.5820 -0.3309 -0.6171 0.3266 456 GLN A O 3499 C CB . GLN A 456 ? 1.4659 1.3882 1.4620 -0.2977 -0.5775 0.2668 456 GLN A CB 3500 C CG . GLN A 456 ? 1.4710 1.4336 1.4352 -0.3102 -0.5728 0.2404 456 GLN A CG 3501 C CD . GLN A 456 ? 1.4829 1.4336 1.4564 -0.3009 -0.5593 0.2003 456 GLN A CD 3502 O OE1 . GLN A 456 ? 1.4399 1.3568 1.4429 -0.2862 -0.5548 0.1947 456 GLN A OE1 3503 N NE2 . GLN A 456 ? 1.7085 1.6894 1.6593 -0.3096 -0.5532 0.1728 456 GLN A NE2 3504 N N . ASP A 457 ? 1.6266 1.5637 1.6549 -0.3068 -0.6216 0.3493 457 ASP A N 3505 C CA . ASP A 457 ? 1.6583 1.6227 1.6924 -0.3148 -0.6419 0.3713 457 ASP A CA 3506 C C . ASP A 457 ? 1.7208 1.6971 1.7574 -0.3258 -0.6570 0.4156 457 ASP A C 3507 O O . ASP A 457 ? 1.6966 1.6989 1.7382 -0.3345 -0.6754 0.4405 457 ASP A O 3508 C CB . ASP A 457 ? 1.7545 1.6907 1.8252 -0.2994 -0.6463 0.3689 457 ASP A CB 3509 C CG . ASP A 457 ? 1.8425 1.8086 1.9182 -0.3072 -0.6661 0.3849 457 ASP A CG 3510 O OD1 . ASP A 457 ? 1.8612 1.8736 1.9087 -0.3220 -0.6720 0.3792 457 ASP A OD1 3511 O OD2 . ASP A 457 ? 1.8082 1.7538 1.9167 -0.2983 -0.6760 0.4024 457 ASP A OD2 3512 N N . ASN A 458 ? 1.8507 1.8094 1.8861 -0.3261 -0.6500 0.4265 458 ASN A N 3513 C CA . ASN A 458 ? 1.8483 1.8167 1.8918 -0.3368 -0.6648 0.4703 458 ASN A CA 3514 C C . ASN A 458 ? 1.7666 1.7834 1.7697 -0.3570 -0.6641 0.4777 458 ASN A C 3515 O O . ASN A 458 ? 1.8616 1.8719 1.8480 -0.3580 -0.6500 0.4663 458 ASN A O 3516 C CB . ASN A 458 ? 1.9102 1.8277 1.9864 -0.3235 -0.6599 0.4798 458 ASN A CB 3517 C CG . ASN A 458 ? 1.9681 1.8924 2.0549 -0.3349 -0.6727 0.5219 458 ASN A CG 3518 O OD1 . ASN A 458 ? 1.9634 1.9263 2.0449 -0.3512 -0.6900 0.5541 458 ASN A OD1 3519 N ND2 . ASN A 458 ? 2.2166 2.1044 2.3213 -0.3264 -0.6647 0.5225 458 ASN A ND2 3520 N N . LYS A 459 ? 1.5994 1.6677 1.5878 -0.3731 -0.6801 0.4976 459 LYS A N 3521 C CA . LYS A 459 ? 1.7039 1.8331 1.6507 -0.3933 -0.6808 0.5013 459 LYS A CA 3522 C C . LYS A 459 ? 2.0304 2.1874 1.9787 -0.4100 -0.6955 0.5524 459 LYS A C 3523 O O . LYS A 459 ? 2.2313 2.4478 2.1462 -0.4285 -0.6986 0.5618 459 LYS A O 3524 C CB . LYS A 459 ? 1.7786 1.9579 1.7044 -0.4012 -0.6881 0.4847 459 LYS A CB 3525 C CG . LYS A 459 ? 1.6546 1.8108 1.5826 -0.3864 -0.6753 0.4352 459 LYS A CG 3526 C CD . LYS A 459 ? 1.8633 2.0771 1.7629 -0.3965 -0.6782 0.4087 459 LYS A CD 3527 C CE . LYS A 459 ? 1.8672 2.0560 1.7773 -0.3819 -0.6676 0.3620 459 LYS A CE 3528 N NZ . LYS A 459 ? 1.8472 1.9984 1.7948 -0.3687 -0.6761 0.3710 459 LYS A NZ 3529 N N . THR A 460 ? 2.0800 2.1966 2.0695 -0.4035 -0.7049 0.5848 460 THR A N 3530 C CA . THR A 460 ? 2.2334 2.3735 2.2411 -0.4181 -0.7262 0.6407 460 THR A CA 3531 C C . THR A 460 ? 2.1164 2.3144 2.0921 -0.4407 -0.7287 0.6654 460 THR A C 3532 O O . THR A 460 ? 2.2469 2.4933 2.2229 -0.4579 -0.7479 0.7066 460 THR A O 3533 C CB . THR A 460 ? 2.0942 2.1748 2.1531 -0.4060 -0.7307 0.6632 460 THR A CB 3534 O OG1 . THR A 460 ? 2.2841 2.3883 2.3625 -0.4220 -0.7505 0.7181 460 THR A OG1 3535 C CG2 . THR A 460 ? 1.6226 1.6636 1.6767 -0.3951 -0.7093 0.6352 460 THR A CG2 3536 N N . CYS A 461 ? 1.5949 1.7915 1.5443 -0.4413 -0.7102 0.6426 461 CYS A N 3537 C CA . CYS A 461 ? 1.7001 1.9516 1.6216 -0.4622 -0.7120 0.6675 461 CYS A CA 3538 C C . CYS A 461 ? 1.7417 2.0350 1.6107 -0.4683 -0.6940 0.6264 461 CYS A C 3539 O O . CYS A 461 ? 1.8384 2.0960 1.6990 -0.4539 -0.6744 0.5802 461 CYS A O 3540 C CB . CYS A 461 ? 1.9531 2.1672 1.9012 -0.4608 -0.7107 0.6933 461 CYS A CB 3541 S SG . CYS A 461 ? 2.7475 2.8946 2.6946 -0.4398 -0.6830 0.6434 461 CYS A SG 3542 N N . SER A 462 ? 1.7600 2.1319 1.5964 -0.4898 -0.7014 0.6441 462 SER A N 3543 C CA . SER A 462 ? 1.7960 2.2176 1.5847 -0.4989 -0.6860 0.6130 462 SER A CA 3544 C C . SER A 462 ? 1.8155 2.3326 1.5734 -0.5239 -0.6985 0.6416 462 SER A C 3545 O O . SER A 462 ? 1.6999 2.2478 1.4691 -0.5318 -0.7146 0.6719 462 SER A O 3546 C CB . SER A 462 ? 1.9101 2.3242 1.6803 -0.4864 -0.6715 0.5501 462 SER A CB 3547 O OG . SER A 462 ? 2.1809 2.6258 1.9143 -0.4909 -0.6541 0.5150 462 SER A OG 3548 N N . LEU A 463 ? 2.0308 2.5941 1.7521 -0.5348 -0.6865 0.6285 463 LEU A N 3549 C CA . LEU A 463 ? 2.1540 2.8111 1.8432 -0.5535 -0.6844 0.6355 463 LEU A CA 3550 C C . LEU A 463 ? 2.1690 2.8648 1.8141 -0.5561 -0.6671 0.5858 463 LEU A C 3551 O O . LEU A 463 ? 2.0865 2.8160 1.7149 -0.5664 -0.6564 0.5962 463 LEU A O 3552 C CB . LEU A 463 ? 1.9928 2.6753 1.6993 -0.5680 -0.6861 0.6938 463 LEU A CB 3553 C CG . LEU A 463 ? 1.8584 2.6187 1.5620 -0.5839 -0.6894 0.7221 463 LEU A CG 3554 C CD1 . LEU A 463 ? 1.7328 2.5065 1.4652 -0.5980 -0.6928 0.7823 463 LEU A CD1 3555 C CD2 . LEU A 463 ? 1.7262 2.5700 1.3813 -0.5921 -0.6758 0.6842 463 LEU A CD2 3556 N N . PRO A 464 ? 2.0408 2.7306 1.6721 -0.5460 -0.6626 0.5300 464 PRO A N 3557 C CA . PRO A 464 ? 1.9543 2.6660 1.5545 -0.5442 -0.6424 0.4761 464 PRO A CA 3558 C C . PRO A 464 ? 2.1096 2.9204 1.6749 -0.5574 -0.6372 0.4574 464 PRO A C 3559 O O . PRO A 464 ? 2.1928 3.0259 1.7437 -0.5521 -0.6315 0.4035 464 PRO A O 3560 C CB . PRO A 464 ? 1.6305 2.2799 1.2472 -0.5222 -0.6324 0.4219 464 PRO A CB 3561 C CG . PRO A 464 ? 1.5911 2.2031 1.2410 -0.5150 -0.6490 0.4470 464 PRO A CG 3562 C CD . PRO A 464 ? 1.7681 2.4284 1.4186 -0.5334 -0.6695 0.5095 464 PRO A CD 3563 N N . GLY A 465 ? 2.0552 2.9207 1.6137 -0.5717 -0.6348 0.4983 465 GLY A N 3564 C CA . GLY A 465 ? 2.0009 2.9601 1.5307 -0.5819 -0.6246 0.4809 465 GLY A CA 3565 C C . GLY A 465 ? 1.9410 2.9352 1.4717 -0.5802 -0.6329 0.4662 465 GLY A C 3566 O O . GLY A 465 ? 1.9428 2.9744 1.4546 -0.5758 -0.6255 0.4118 465 GLY A O 3567 N N . THR A 466 ? 1.8937 2.8739 1.4496 -0.5831 -0.6486 0.5135 466 THR A N 3568 C CA . THR A 466 ? 2.0963 3.1025 1.6571 -0.5816 -0.6588 0.5066 466 THR A CA 3569 C C . THR A 466 ? 2.1717 3.1324 1.7375 -0.5653 -0.6620 0.4528 466 THR A C 3570 O O . THR A 466 ? 2.3225 3.3236 1.8705 -0.5618 -0.6557 0.4007 466 THR A O 3571 C CB . THR A 466 ? 2.0191 3.1281 1.5522 -0.5929 -0.6508 0.4937 466 THR A CB 3572 O OG1 . THR A 466 ? 2.1402 3.2953 1.6669 -0.6088 -0.6443 0.5369 466 THR A OG1 3573 C CG2 . THR A 466 ? 1.7982 2.9352 1.3411 -0.5946 -0.6640 0.5056 466 THR A CG2 3574 N N . ALA A 467 ? 2.0020 2.8784 1.5960 -0.5550 -0.6718 0.4653 467 ALA A N 3575 C CA . ALA A 467 ? 2.0188 2.8456 1.6242 -0.5402 -0.6758 0.4201 467 ALA A CA 3576 C C . ALA A 467 ? 2.3045 3.0610 1.9480 -0.5317 -0.6927 0.4519 467 ALA A C 3577 O O . ALA A 467 ? 2.4016 3.1538 2.0633 -0.5369 -0.7019 0.5059 467 ALA A O 3578 C CB . ALA A 467 ? 1.6522 2.4441 1.2487 -0.5337 -0.6635 0.3805 467 ALA A CB 3579 N N . LEU A 468 ? 2.2615 2.9596 1.9229 -0.5159 -0.6919 0.4154 468 LEU A N 3580 C CA . LEU A 468 ? 2.0554 2.6833 1.7571 -0.5020 -0.7002 0.4341 468 LEU A CA 3581 C C . LEU A 468 ? 1.8899 2.4432 1.6183 -0.4929 -0.6946 0.4650 468 LEU A C 3582 O O . LEU A 468 ? 1.9332 2.4906 1.6490 -0.4990 -0.6861 0.4777 468 LEU A O 3583 C CB . LEU A 468 ? 1.9958 2.5844 1.7130 -0.4842 -0.6927 0.3805 468 LEU A CB 3584 C CG . LEU A 468 ? 2.0719 2.7209 1.7743 -0.4890 -0.6995 0.3429 468 LEU A CG 3585 C CD1 . LEU A 468 ? 1.9968 2.6973 1.6675 -0.4945 -0.6863 0.2948 468 LEU A CD1 3586 C CD2 . LEU A 468 ? 2.0927 2.6884 1.8276 -0.4713 -0.7002 0.3147 468 LEU A CD2 3587 N N . LYS A 469 ? 1.8581 2.3455 1.6249 -0.4781 -0.6997 0.4757 469 LYS A N 3588 C CA . LYS A 469 ? 1.7730 2.1866 1.5708 -0.4664 -0.6948 0.4981 469 LYS A CA 3589 C C . LYS A 469 ? 1.6736 2.0244 1.4803 -0.4464 -0.6737 0.4514 469 LYS A C 3590 O O . LYS A 469 ? 1.6545 1.9953 1.4645 -0.4364 -0.6690 0.4120 469 LYS A O 3591 C CB . LYS A 469 ? 1.6790 2.0590 1.5169 -0.4610 -0.7126 0.5366 469 LYS A CB 3592 C CG . LYS A 469 ? 1.7113 2.1210 1.5582 -0.4773 -0.7313 0.5990 469 LYS A CG 3593 C CD . LYS A 469 ? 1.7200 2.0907 1.6131 -0.4697 -0.7487 0.6327 469 LYS A CD 3594 C CE . LYS A 469 ? 1.6031 1.9907 1.5162 -0.4839 -0.7671 0.6967 469 LYS A CE 3595 N NZ . LYS A 469 ? 1.6355 2.1053 1.5206 -0.5045 -0.7650 0.7132 469 LYS A NZ 3596 N N . VAL A 470 ? 1.6435 1.9537 1.4564 -0.4411 -0.6616 0.4572 470 VAL A N 3597 C CA . VAL A 470 ? 1.8479 2.1010 1.6695 -0.4230 -0.6414 0.4172 470 VAL A CA 3598 C C . VAL A 470 ? 1.7693 1.9541 1.6250 -0.4101 -0.6387 0.4391 470 VAL A C 3599 O O . VAL A 470 ? 1.5600 1.7430 1.4320 -0.4164 -0.6517 0.4843 470 VAL A O 3600 C CB . VAL A 470 ? 1.8729 2.1508 1.6608 -0.4285 -0.6240 0.3862 470 VAL A CB 3601 C CG1 . VAL A 470 ? 1.9495 2.2951 1.7072 -0.4389 -0.6255 0.3552 470 VAL A CG1 3602 C CG2 . VAL A 470 ? 1.6338 1.9292 1.4097 -0.4414 -0.6246 0.4221 470 VAL A CG2 3603 N N . SER A 471 ? 1.7594 1.8907 1.6291 -0.3920 -0.6226 0.4068 471 SER A N 3604 C CA . SER A 471 ? 1.6359 1.7054 1.5372 -0.3782 -0.6180 0.4200 471 SER A CA 3605 C C . SER A 471 ? 1.6451 1.7099 1.5314 -0.3825 -0.6056 0.4217 471 SER A C 3606 O O . SER A 471 ? 1.5517 1.6183 1.4164 -0.3804 -0.5885 0.3867 471 SER A O 3607 C CB . SER A 471 ? 1.5523 1.5721 1.4760 -0.3571 -0.6067 0.3867 471 SER A CB 3608 O OG . SER A 471 ? 1.6902 1.6560 1.6461 -0.3431 -0.6035 0.3986 471 SER A OG 3609 N N . CYS A 472 ? 1.7834 1.8409 1.6850 -0.3882 -0.6150 0.4627 472 CYS A N 3610 C CA . CYS A 472 ? 1.6354 1.6951 1.5234 -0.3951 -0.6061 0.4705 472 CYS A CA 3611 C C . CYS A 472 ? 1.6412 1.6417 1.5653 -0.3823 -0.6036 0.4833 472 CYS A C 3612 O O . CYS A 472 ? 1.7554 1.7346 1.7163 -0.3788 -0.6187 0.5139 472 CYS A O 3613 C CB . CYS A 472 ? 1.6435 1.7630 1.5136 -0.4184 -0.6202 0.5102 472 CYS A CB 3614 S SG . CYS A 472 ? 2.2852 2.4075 2.1946 -0.4251 -0.6487 0.5702 472 CYS A SG 3615 N N . PHE A 473 ? 1.6173 1.5925 1.5326 -0.3750 -0.5848 0.4582 473 PHE A N 3616 C CA . PHE A 473 ? 1.5615 1.4875 1.5074 -0.3645 -0.5814 0.4681 473 PHE A CA 3617 C C . PHE A 473 ? 1.5709 1.5154 1.5034 -0.3788 -0.5803 0.4899 473 PHE A C 3618 O O . PHE A 473 ? 1.5696 1.5672 1.4678 -0.3965 -0.5813 0.4969 473 PHE A O 3619 C CB . PHE A 473 ? 1.5527 1.4337 1.5042 -0.3444 -0.5616 0.4262 473 PHE A CB 3620 C CG . PHE A 473 ? 1.5546 1.4538 1.4677 -0.3470 -0.5428 0.3892 473 PHE A CG 3621 C CD1 . PHE A 473 ? 1.5651 1.4572 1.4642 -0.3487 -0.5290 0.3808 473 PHE A CD1 3622 C CD2 . PHE A 473 ? 1.5475 1.4700 1.4423 -0.3472 -0.5396 0.3618 473 PHE A CD2 3623 C CE1 . PHE A 473 ? 1.5635 1.4721 1.4310 -0.3507 -0.5123 0.3461 473 PHE A CE1 3624 C CE2 . PHE A 473 ? 1.5530 1.4919 1.4189 -0.3491 -0.5236 0.3262 473 PHE A CE2 3625 C CZ . PHE A 473 ? 1.5526 1.4845 1.4048 -0.3507 -0.5098 0.3184 473 PHE A CZ 3626 N N . ASN A 474 ? 1.6084 1.5121 1.5692 -0.3711 -0.5785 0.4999 474 ASN A N 3627 C CA . ASN A 474 ? 1.5963 1.5128 1.5502 -0.3837 -0.5780 0.5222 474 ASN A CA 3628 C C . ASN A 474 ? 1.5947 1.4769 1.5434 -0.3729 -0.5573 0.4921 474 ASN A C 3629 O O . ASN A 474 ? 1.5880 1.4241 1.5575 -0.3535 -0.5487 0.4672 474 ASN A O 3630 C CB . ASN A 474 ? 1.7115 1.6167 1.7102 -0.3883 -0.5992 0.5707 474 ASN A CB 3631 C CG . ASN A 474 ? 2.1415 2.0924 2.1416 -0.4046 -0.6207 0.6094 474 ASN A CG 3632 O OD1 . ASN A 474 ? 2.3236 2.2651 2.3460 -0.3980 -0.6323 0.6143 474 ASN A OD1 3633 N ND2 . ASN A 474 ? 2.2030 2.2069 2.1793 -0.4265 -0.6263 0.6380 474 ASN A ND2 3634 N N . VAL A 475 ? 1.7034 1.6116 1.6241 -0.3858 -0.5494 0.4951 475 VAL A N 3635 C CA . VAL A 475 ? 1.6875 1.5668 1.6022 -0.3776 -0.5305 0.4697 475 VAL A CA 3636 C C . VAL A 475 ? 1.8480 1.7230 1.7798 -0.3864 -0.5366 0.5029 475 VAL A C 3637 O O . VAL A 475 ? 2.0000 1.9201 1.9117 -0.4059 -0.5416 0.5284 475 VAL A O 3638 C CB . VAL A 475 ? 1.6024 1.5128 1.4690 -0.3829 -0.5120 0.4348 475 VAL A CB 3639 C CG1 . VAL A 475 ? 1.6034 1.4839 1.4656 -0.3748 -0.4932 0.4111 475 VAL A CG1 3640 C CG2 . VAL A 475 ? 1.5939 1.5070 1.4496 -0.3740 -0.5069 0.4009 475 VAL A CG2 3641 N N . ARG A 476 ? 1.8217 1.6452 1.7927 -0.3719 -0.5365 0.5023 476 ARG A N 3642 C CA . ARG A 476 ? 1.7440 1.5565 1.7401 -0.3781 -0.5434 0.5318 476 ARG A CA 3643 C C . ARG A 476 ? 1.6856 1.4661 1.6769 -0.3675 -0.5239 0.5016 476 ARG A C 3644 O O . ARG A 476 ? 1.7644 1.5026 1.7738 -0.3476 -0.5152 0.4725 476 ARG A O 3645 C CB . ARG A 476 ? 1.6633 1.4449 1.7192 -0.3713 -0.5643 0.5607 476 ARG A CB 3646 C CG . ARG A 476 ? 1.5344 1.3038 1.6266 -0.3779 -0.5751 0.5939 476 ARG A CG 3647 C CD . ARG A 476 ? 1.5116 1.2475 1.6698 -0.3688 -0.5962 0.6166 476 ARG A CD 3648 N NE . ARG A 476 ? 1.7733 1.4968 1.9740 -0.3752 -0.6088 0.6489 476 ARG A NE 3649 C CZ . ARG A 476 ? 2.0562 1.8087 2.2780 -0.3945 -0.6299 0.7011 476 ARG A CZ 3650 N NH1 . ARG A 476 ? 2.0842 1.8819 2.2853 -0.4092 -0.6401 0.7263 476 ARG A NH1 3651 N NH2 . ARG A 476 ? 2.0151 1.7530 2.2808 -0.3993 -0.6413 0.7289 476 ARG A NH2 3652 N N . PHE A 477 ? 1.6531 1.4574 1.6201 -0.3812 -0.5170 0.5092 477 PHE A N 3653 C CA . PHE A 477 ? 1.7601 1.5374 1.7212 -0.3730 -0.4989 0.4831 477 PHE A CA 3654 C C . PHE A 477 ? 1.8006 1.5708 1.7885 -0.3814 -0.5075 0.5156 477 PHE A C 3655 O O . PHE A 477 ? 1.7912 1.6006 1.7731 -0.4014 -0.5185 0.5529 477 PHE A O 3656 C CB . PHE A 477 ? 1.6964 1.5047 1.6033 -0.3791 -0.4790 0.4530 477 PHE A CB 3657 C CG . PHE A 477 ? 1.6612 1.5307 1.5361 -0.4028 -0.4837 0.4777 477 PHE A CG 3658 C CD1 . PHE A 477 ? 1.8103 1.6967 1.6731 -0.4148 -0.4785 0.4902 477 PHE A CD1 3659 C CD2 . PHE A 477 ? 1.6249 1.5386 1.4811 -0.4132 -0.4930 0.4875 477 PHE A CD2 3660 C CE1 . PHE A 477 ? 1.8822 1.8312 1.7150 -0.4367 -0.4823 0.5129 477 PHE A CE1 3661 C CE2 . PHE A 477 ? 1.6410 1.6182 1.4668 -0.4350 -0.4971 0.5090 477 PHE A CE2 3662 C CZ . PHE A 477 ? 1.7517 1.7479 1.5655 -0.4468 -0.4915 0.5220 477 PHE A CZ 3663 N N . CYS A 478 ? 1.7934 1.5157 1.8130 -0.3661 -0.5030 0.5014 478 CYS A N 3664 C CA . CYS A 478 ? 1.8303 1.5386 1.8844 -0.3714 -0.5121 0.5288 478 CYS A CA 3665 C C . CYS A 478 ? 1.7604 1.4569 1.7948 -0.3685 -0.4924 0.5038 478 CYS A C 3666 O O . CYS A 478 ? 1.6714 1.3445 1.6915 -0.3527 -0.4744 0.4616 478 CYS A O 3667 C CB . CYS A 478 ? 1.8131 1.4765 1.9312 -0.3561 -0.5274 0.5357 478 CYS A CB 3668 S SG . CYS A 478 ? 2.8550 2.5280 3.0045 -0.3582 -0.5521 0.5660 478 CYS A SG 3669 N N . LEU A 479 ? 1.7113 1.4258 1.7463 -0.3843 -0.4962 0.5317 479 LEU A N 3670 C CA . LEU A 479 ? 1.6269 1.3349 1.6416 -0.3841 -0.4783 0.5116 479 LEU A CA 3671 C C . LEU A 479 ? 1.5291 1.2211 1.5853 -0.3895 -0.4893 0.5409 479 LEU A C 3672 O O . LEU A 479 ? 1.5557 1.2765 1.6252 -0.4080 -0.5055 0.5864 479 LEU A O 3673 C CB . LEU A 479 ? 1.6611 1.4214 1.6169 -0.4006 -0.4655 0.5078 479 LEU A CB 3674 C CG . LEU A 479 ? 1.5652 1.3220 1.4886 -0.3978 -0.4421 0.4743 479 LEU A CG 3675 C CD1 . LEU A 479 ? 1.5648 1.2868 1.4806 -0.3761 -0.4255 0.4249 479 LEU A CD1 3676 C CD2 . LEU A 479 ? 1.5912 1.4071 1.4634 -0.4164 -0.4338 0.4763 479 LEU A CD2 3677 N N . LYS A 480 ? 1.6300 1.2783 1.7088 -0.3736 -0.4811 0.5154 480 LYS A N 3678 C CA . LYS A 480 ? 1.8226 1.4540 1.9406 -0.3777 -0.4895 0.5368 480 LYS A CA 3679 C C . LYS A 480 ? 1.7164 1.3346 1.8106 -0.3722 -0.4678 0.5050 480 LYS A C 3680 O O . LYS A 480 ? 1.6772 1.2807 1.7453 -0.3576 -0.4490 0.4616 480 LYS A O 3681 C CB . LYS A 480 ? 1.8649 1.4526 2.0527 -0.3629 -0.5073 0.5417 480 LYS A CB 3682 C CG . LYS A 480 ? 1.8068 1.3520 2.0053 -0.3368 -0.4944 0.4924 480 LYS A CG 3683 C CD . LYS A 480 ? 1.7827 1.2901 2.0548 -0.3232 -0.5132 0.4970 480 LYS A CD 3684 C CE . LYS A 480 ? 1.8101 1.2834 2.0924 -0.2972 -0.5005 0.4474 480 LYS A CE 3685 N NZ . LYS A 480 ? 1.9443 1.4089 2.2003 -0.2923 -0.4794 0.4175 480 LYS A NZ 3686 N N . ALA A 481 ? 1.5717 1.1965 1.6774 -0.3846 -0.4713 0.5286 481 ALA A N 3687 C CA . ALA A 481 ? 1.5786 1.1926 1.6642 -0.3812 -0.4521 0.5024 481 ALA A CA 3688 C C . ALA A 481 ? 1.7998 1.3929 1.9348 -0.3843 -0.4638 0.5249 481 ALA A C 3689 O O . ALA A 481 ? 1.9939 1.6039 2.1588 -0.4001 -0.4835 0.5717 481 ALA A O 3690 C CB . ALA A 481 ? 1.5644 1.2256 1.5883 -0.3974 -0.4366 0.5013 481 ALA A CB 3691 N N . ASP A 482 ? 1.8124 1.3703 1.9581 -0.3693 -0.4522 0.4922 482 ASP A N 3692 C CA . ASP A 482 ? 1.8411 1.3779 2.0325 -0.3710 -0.4612 0.5070 482 ASP A CA 3693 C C . ASP A 482 ? 1.6945 1.2220 1.8563 -0.3657 -0.4385 0.4735 482 ASP A C 3694 O O . ASP A 482 ? 1.5814 1.1176 1.6920 -0.3602 -0.4172 0.4401 482 ASP A O 3695 C CB . ASP A 482 ? 1.8640 1.3579 2.1256 -0.3539 -0.4787 0.5024 482 ASP A CB 3696 C CG . ASP A 482 ? 1.9909 1.4787 2.3116 -0.3556 -0.4931 0.5239 482 ASP A CG 3697 O OD1 . ASP A 482 ? 1.8872 1.4068 2.2021 -0.3752 -0.4974 0.5596 482 ASP A OD1 3698 O OD2 . ASP A 482 ? 2.1755 1.6382 2.5480 -0.3339 -0.4974 0.4992 482 ASP A OD2 3699 N N . GLY A 483 ? 1.6451 1.1551 1.8424 -0.3674 -0.4439 0.4827 483 GLY A N 3700 C CA . GLY A 483 ? 1.5981 1.0993 1.7717 -0.3632 -0.4240 0.4541 483 GLY A CA 3701 C C . GLY A 483 ? 1.6034 1.0806 1.8298 -0.3635 -0.4348 0.4663 483 GLY A C 3702 O O . GLY A 483 ? 1.7272 1.1957 2.0141 -0.3590 -0.4552 0.4851 483 GLY A O 3703 N N . LYS A 484 ? 1.6601 1.1357 1.8644 -0.3645 -0.4186 0.4493 484 LYS A N 3704 C CA . LYS A 484 ? 1.5808 1.0374 1.8316 -0.3628 -0.4257 0.4548 484 LYS A CA 3705 C C . LYS A 484 ? 1.4214 0.9015 1.6403 -0.3828 -0.4162 0.4729 484 LYS A C 3706 O O . LYS A 484 ? 1.3635 0.8729 1.5197 -0.3894 -0.3970 0.4619 484 LYS A O 3707 C CB . LYS A 484 ? 1.3719 0.7919 1.6405 -0.3368 -0.4156 0.4046 484 LYS A CB 3708 C CG . LYS A 484 ? 1.4309 0.8328 1.7404 -0.3147 -0.4254 0.3850 484 LYS A CG 3709 C CD . LYS A 484 ? 1.5640 0.9392 1.8651 -0.2927 -0.4101 0.3333 484 LYS A CD 3710 C CE . LYS A 484 ? 1.7103 1.0755 2.0298 -0.2828 -0.4019 0.3110 484 LYS A CE 3711 N NZ . LYS A 484 ? 1.7124 1.0586 2.0223 -0.2619 -0.3866 0.2618 484 LYS A NZ 3712 N N . GLY A 485 ? 1.3464 0.8324 1.6077 -0.3831 -0.4242 0.4888 485 GLY A N 3713 C CA . GLY A 485 ? 1.4734 0.9827 1.7111 -0.4011 -0.4163 0.5071 485 GLY A CA 3714 C C . GLY A 485 ? 1.5324 1.0919 1.7540 -0.4269 -0.4252 0.5579 485 GLY A C 3715 O O . GLY A 485 ? 1.6503 1.2266 1.9043 -0.4289 -0.4437 0.5861 485 GLY A O 3716 N N . VAL A 486 ? 1.5281 1.1160 1.6998 -0.4468 -0.4119 0.5689 486 VAL A N 3717 C CA . VAL A 486 ? 1.6250 1.2711 1.7755 -0.4720 -0.4178 0.6154 486 VAL A CA 3718 C C . VAL A 486 ? 1.6186 1.2989 1.7081 -0.4767 -0.4070 0.6056 486 VAL A C 3719 O O . VAL A 486 ? 1.4324 1.1179 1.4691 -0.4694 -0.3835 0.5641 486 VAL A O 3720 C CB . VAL A 486 ? 1.4913 1.1666 1.6219 -0.4875 -0.4074 0.6283 486 VAL A CB 3721 C CG1 . VAL A 486 ? 1.4618 1.2066 1.5592 -0.5138 -0.4099 0.6712 486 VAL A CG1 3722 C CG2 . VAL A 486 ? 1.4139 1.0745 1.6094 -0.4770 -0.4180 0.6345 486 VAL A CG2 3723 N N . LEU A 487 ? 1.7310 1.4381 1.8315 -0.4875 -0.4244 0.6423 487 LEU A N 3724 C CA . LEU A 487 ? 1.6931 1.4368 1.7442 -0.4905 -0.4178 0.6346 487 LEU A CA 3725 C C . LEU A 487 ? 1.8813 1.6531 1.9625 -0.5053 -0.4432 0.6884 487 LEU A C 3726 O O . LEU A 487 ? 2.0331 1.7795 2.1798 -0.4985 -0.4631 0.7072 487 LEU A O 3727 C CB . LEU A 487 ? 1.5363 1.2410 1.5732 -0.4660 -0.4065 0.5821 487 LEU A CB 3728 C CG . LEU A 487 ? 1.6282 1.2872 1.7166 -0.4495 -0.4234 0.5794 487 LEU A CG 3729 C CD1 . LEU A 487 ? 1.6264 1.2671 1.6842 -0.4300 -0.4088 0.5307 487 LEU A CD1 3730 C CD2 . LEU A 487 ? 1.6101 1.2188 1.7598 -0.4384 -0.4328 0.5768 487 LEU A CD2 3731 N N . PRO A 488 ? 1.8167 1.6494 1.8533 -0.5210 -0.4411 0.7052 488 PRO A N 3732 C CA . PRO A 488 ? 1.8322 1.7037 1.8945 -0.5395 -0.4652 0.7637 488 PRO A CA 3733 C C . PRO A 488 ? 1.8631 1.7022 1.9713 -0.5247 -0.4830 0.7643 488 PRO A C 3734 O O . PRO A 488 ? 1.8997 1.6834 2.0130 -0.5047 -0.4778 0.7259 488 PRO A O 3735 C CB . PRO A 488 ? 1.7111 1.6552 1.7060 -0.5542 -0.4537 0.7641 488 PRO A CB 3736 C CG . PRO A 488 ? 1.4972 1.4224 1.4422 -0.5362 -0.4278 0.6982 488 PRO A CG 3737 C CD . PRO A 488 ? 1.4997 1.3703 1.4633 -0.5221 -0.4172 0.6697 488 PRO A CD 3738 N N . ARG A 489 ? 1.7968 1.6766 1.9395 -0.5330 -0.5024 0.8035 489 ARG A N 3739 C CA . ARG A 489 ? 1.8556 1.7110 2.0483 -0.5201 -0.5208 0.8072 489 ARG A CA 3740 C C . ARG A 489 ? 1.9663 1.8426 2.1159 -0.5255 -0.5212 0.8086 489 ARG A C 3741 O O . ARG A 489 ? 2.0298 1.8827 2.2107 -0.5139 -0.5336 0.8059 489 ARG A O 3742 C CB . ARG A 489 ? 1.5282 1.4130 1.7912 -0.5257 -0.5436 0.8489 489 ARG A CB 3743 C CG . ARG A 489 ? 1.7318 1.5919 2.0478 -0.5177 -0.5469 0.8469 489 ARG A CG 3744 C CD . ARG A 489 ? 1.8520 1.7401 2.2430 -0.5234 -0.5717 0.8886 489 ARG A CD 3745 N NE . ARG A 489 ? 1.9752 1.9405 2.3487 -0.5496 -0.5758 0.9334 489 ARG A NE 3746 C CZ . ARG A 489 ? 2.0657 2.0800 2.4386 -0.5632 -0.5876 0.9649 489 ARG A CZ 3747 N NH1 . ARG A 489 ? 1.9574 1.9486 2.3464 -0.5530 -0.5970 0.9573 489 ARG A NH1 3748 N NH2 . ARG A 489 ? 2.1181 2.2076 2.4754 -0.5868 -0.5898 1.0031 489 ARG A NH2 3749 N N . LYS A 490 ? 1.9080 1.8311 1.9860 -0.5426 -0.5077 0.8111 490 LYS A N 3750 C CA . LYS A 490 ? 1.7778 1.7294 1.8106 -0.5443 -0.5047 0.8011 490 LYS A CA 3751 C C . LYS A 490 ? 1.7676 1.7366 1.7297 -0.5384 -0.4755 0.7472 490 LYS A C 3752 O O . LYS A 490 ? 1.6598 1.6594 1.5912 -0.5483 -0.4617 0.7435 490 LYS A O 3753 C CB . LYS A 490 ? 1.5778 1.6050 1.6092 -0.5669 -0.5198 0.8515 490 LYS A CB 3754 C CG . LYS A 490 ? 1.6564 1.6784 1.7635 -0.5622 -0.5440 0.8798 490 LYS A CG 3755 C CD . LYS A 490 ? 1.7534 1.8460 1.8497 -0.5788 -0.5549 0.9123 490 LYS A CD 3756 C CE . LYS A 490 ? 1.8472 2.0222 1.9263 -0.6022 -0.5523 0.9434 490 LYS A CE 3757 N NZ . LYS A 490 ? 1.6064 1.7839 1.7554 -0.6052 -0.5653 0.9737 490 LYS A NZ 3758 N N . LEU A 491 ? 1.7271 1.6768 1.6673 -0.5223 -0.4669 0.7059 491 LEU A N 3759 C CA . LEU A 491 ? 1.6802 1.6404 1.5616 -0.5145 -0.4411 0.6521 491 LEU A CA 3760 C C . LEU A 491 ? 1.8277 1.8360 1.6700 -0.5200 -0.4407 0.6456 491 LEU A C 3761 O O . LEU A 491 ? 2.0093 2.0211 1.8732 -0.5217 -0.4586 0.6702 491 LEU A O 3762 C CB . LEU A 491 ? 1.5561 1.4459 1.4482 -0.4880 -0.4285 0.6015 491 LEU A CB 3763 C CG . LEU A 491 ? 1.5018 1.3388 1.4374 -0.4790 -0.4299 0.6021 491 LEU A CG 3764 C CD1 . LEU A 491 ? 1.4797 1.2534 1.4293 -0.4524 -0.4209 0.5555 491 LEU A CD1 3765 C CD2 . LEU A 491 ? 1.5476 1.4059 1.4587 -0.4891 -0.4154 0.5994 491 LEU A CD2 3766 N N . ASN A 492 ? 1.7361 1.7823 1.5238 -0.5227 -0.4211 0.6114 492 ASN A N 3767 C CA . ASN A 492 ? 1.8014 1.8955 1.5514 -0.5271 -0.4196 0.5983 492 ASN A CA 3768 C C . ASN A 492 ? 1.8100 1.8704 1.5395 -0.5065 -0.4032 0.5384 492 ASN A C 3769 O O . ASN A 492 ? 1.7268 1.7840 1.4293 -0.5006 -0.3829 0.4982 492 ASN A O 3770 C CB . ASN A 492 ? 1.8273 2.0050 1.5326 -0.5483 -0.4126 0.6067 492 ASN A CB 3771 C CG . ASN A 492 ? 1.8923 2.1280 1.6101 -0.5717 -0.4334 0.6707 492 ASN A CG 3772 O OD1 . ASN A 492 ? 1.8948 2.1022 1.6613 -0.5735 -0.4529 0.7131 492 ASN A OD1 3773 N ND2 . ASN A 492 ? 1.9483 2.2685 1.6246 -0.5900 -0.4301 0.6778 492 ASN A ND2 3774 N N . PHE A 493 ? 1.9268 1.9636 1.6720 -0.4961 -0.4128 0.5344 493 PHE A N 3775 C CA . PHE A 493 ? 1.8565 1.8639 1.5874 -0.4774 -0.4000 0.4830 493 PHE A CA 3776 C C . PHE A 493 ? 1.9192 1.9810 1.6151 -0.4845 -0.4001 0.4707 493 PHE A C 3777 O O . PHE A 493 ? 2.0192 2.1251 1.7151 -0.4989 -0.4161 0.5066 493 PHE A O 3778 C CB . PHE A 493 ? 1.7130 1.6550 1.4870 -0.4586 -0.4091 0.4813 493 PHE A CB 3779 C CG . PHE A 493 ? 1.6224 1.5045 1.4261 -0.4446 -0.4031 0.4706 493 PHE A CG 3780 C CD1 . PHE A 493 ? 1.7369 1.6044 1.5780 -0.4507 -0.4158 0.5083 493 PHE A CD1 3781 C CD2 . PHE A 493 ? 1.6032 1.4456 1.4004 -0.4256 -0.3855 0.4231 493 PHE A CD2 3782 C CE1 . PHE A 493 ? 1.7388 1.5533 1.6088 -0.4374 -0.4108 0.4957 493 PHE A CE1 3783 C CE2 . PHE A 493 ? 1.5721 1.3642 1.3957 -0.4127 -0.3801 0.4123 493 PHE A CE2 3784 C CZ . PHE A 493 ? 1.5504 1.3285 1.4098 -0.4183 -0.3926 0.4470 493 PHE A CZ 3785 N N . GLN A 494 ? 1.7671 1.8273 1.4360 -0.4744 -0.3829 0.4201 494 GLN A N 3786 C CA . GLN A 494 ? 1.8160 1.9210 1.4568 -0.4779 -0.3829 0.4005 494 GLN A CA 3787 C C . GLN A 494 ? 1.7467 1.8038 1.4022 -0.4579 -0.3816 0.3700 494 GLN A C 3788 O O . GLN A 494 ? 1.6604 1.6805 1.3153 -0.4428 -0.3662 0.3301 494 GLN A O 3789 C CB . GLN A 494 ? 1.8955 2.0488 1.4955 -0.4846 -0.3656 0.3658 494 GLN A CB 3790 C CG . GLN A 494 ? 2.1040 2.3025 1.6892 -0.5026 -0.3634 0.3912 494 GLN A CG 3791 C CD . GLN A 494 ? 2.2494 2.5071 1.8331 -0.5234 -0.3821 0.4436 494 GLN A CD 3792 O OE1 . GLN A 494 ? 2.1959 2.4859 1.7726 -0.5276 -0.3928 0.4492 494 GLN A OE1 3793 N NE2 . GLN A 494 ? 2.2661 2.5399 1.8582 -0.5369 -0.3868 0.4839 494 GLN A NE2 3794 N N . VAL A 495 ? 1.7942 1.8545 1.4641 -0.4584 -0.3982 0.3907 495 VAL A N 3795 C CA . VAL A 495 ? 1.8043 1.8192 1.4931 -0.4400 -0.3994 0.3688 495 VAL A CA 3796 C C . VAL A 495 ? 1.8215 1.8718 1.4850 -0.4402 -0.3966 0.3383 495 VAL A C 3797 O O . VAL A 495 ? 1.8794 1.9913 1.5210 -0.4560 -0.4042 0.3511 495 VAL A O 3798 C CB . VAL A 495 ? 1.7089 1.6984 1.4359 -0.4379 -0.4201 0.4082 495 VAL A CB 3799 C CG1 . VAL A 495 ? 1.7292 1.6681 1.4785 -0.4172 -0.4197 0.3843 495 VAL A CG1 3800 C CG2 . VAL A 495 ? 1.6444 1.6057 1.4012 -0.4399 -0.4260 0.4407 495 VAL A CG2 3801 N N . GLU A 496 ? 1.7964 1.8100 1.4653 -0.4229 -0.3861 0.2980 496 GLU A N 3802 C CA . GLU A 496 ? 1.7373 1.7770 1.3901 -0.4209 -0.3838 0.2659 496 GLU A CA 3803 C C . GLU A 496 ? 1.6982 1.6972 1.3776 -0.4058 -0.3912 0.2614 496 GLU A C 3804 O O . GLU A 496 ? 1.6366 1.5793 1.3406 -0.3896 -0.3859 0.2531 496 GLU A O 3805 C CB . GLU A 496 ? 1.7415 1.7832 1.3770 -0.4154 -0.3641 0.2181 496 GLU A CB 3806 C CG . GLU A 496 ? 1.8550 1.9310 1.4762 -0.4153 -0.3623 0.1824 496 GLU A CG 3807 C CD . GLU A 496 ? 2.0798 2.2337 1.6716 -0.4347 -0.3695 0.1908 496 GLU A CD 3808 O OE1 . GLU A 496 ? 2.0635 2.2496 1.6482 -0.4361 -0.3746 0.1716 496 GLU A OE1 3809 O OE2 . GLU A 496 ? 2.0996 2.2854 1.6764 -0.4488 -0.3704 0.2167 496 GLU A OE2 3810 N N . LEU A 497 ? 1.7500 1.7810 1.4246 -0.4111 -0.4033 0.2667 497 LEU A N 3811 C CA . LEU A 497 ? 1.5983 1.5966 1.2978 -0.3981 -0.4114 0.2645 497 LEU A CA 3812 C C . LEU A 497 ? 1.5931 1.6069 1.2828 -0.3930 -0.4062 0.2239 497 LEU A C 3813 O O . LEU A 497 ? 1.5782 1.6478 1.2432 -0.4050 -0.4084 0.2137 497 LEU A O 3814 C CB . LEU A 497 ? 1.6022 1.6171 1.3135 -0.4071 -0.4328 0.3084 497 LEU A CB 3815 C CG . LEU A 497 ? 1.6123 1.6004 1.3493 -0.4088 -0.4424 0.3509 497 LEU A CG 3816 C CD1 . LEU A 497 ? 1.6129 1.6209 1.3650 -0.4180 -0.4649 0.3935 497 LEU A CD1 3817 C CD2 . LEU A 497 ? 1.6120 1.5309 1.3812 -0.3884 -0.4359 0.3390 497 LEU A CD2 3818 N N . LEU A 498 ? 1.7405 1.7072 1.4520 -0.3751 -0.3998 0.2007 498 LEU A N 3819 C CA . LEU A 498 ? 1.6951 1.6693 1.4067 -0.3686 -0.3959 0.1638 498 LEU A CA 3820 C C . LEU A 498 ? 1.5536 1.4983 1.2927 -0.3570 -0.4059 0.1705 498 LEU A C 3821 O O . LEU A 498 ? 1.5449 1.4413 1.3092 -0.3440 -0.4047 0.1798 498 LEU A O 3822 C CB . LEU A 498 ? 1.8145 1.7655 1.5283 -0.3585 -0.3772 0.1257 498 LEU A CB 3823 C CG . LEU A 498 ? 1.8761 1.8698 1.5639 -0.3681 -0.3671 0.0965 498 LEU A CG 3824 C CD1 . LEU A 498 ? 1.9216 1.9627 1.5999 -0.3746 -0.3742 0.0753 498 LEU A CD1 3825 C CD2 . LEU A 498 ? 1.6743 1.6974 1.3379 -0.3829 -0.3662 0.1191 498 LEU A CD2 3826 N N . LEU A 499 ? 1.5488 1.5253 1.2836 -0.3617 -0.4159 0.1646 499 LEU A N 3827 C CA . LEU A 499 ? 1.6346 1.5886 1.3945 -0.3519 -0.4263 0.1711 499 LEU A CA 3828 C C . LEU A 499 ? 1.7879 1.7228 1.5633 -0.3386 -0.4177 0.1332 499 LEU A C 3829 O O . LEU A 499 ? 1.5078 1.4710 1.2714 -0.3425 -0.4123 0.1016 499 LEU A O 3830 C CB . LEU A 499 ? 1.5340 1.5330 1.2841 -0.3645 -0.4439 0.1904 499 LEU A CB 3831 C CG . LEU A 499 ? 1.5550 1.5695 1.3008 -0.3767 -0.4571 0.2373 499 LEU A CG 3832 C CD1 . LEU A 499 ? 1.6160 1.6805 1.3516 -0.3895 -0.4743 0.2542 499 LEU A CD1 3833 C CD2 . LEU A 499 ? 1.5621 1.5217 1.3410 -0.3649 -0.4615 0.2630 499 LEU A CD2 3834 N N . ASP A 500 ? 1.8627 1.7518 1.6676 -0.3231 -0.4173 0.1371 500 ASP A N 3835 C CA . ASP A 500 ? 1.7264 1.5953 1.5522 -0.3100 -0.4105 0.1080 500 ASP A CA 3836 C C . ASP A 500 ? 1.5404 1.4072 1.3608 -0.3078 -0.3937 0.0756 500 ASP A C 3837 O O . ASP A 500 ? 1.5293 1.4212 1.3459 -0.3114 -0.3916 0.0466 500 ASP A O 3838 C CB . ASP A 500 ? 1.6319 1.5293 1.4606 -0.3136 -0.4219 0.0976 500 ASP A CB 3839 C CG . ASP A 500 ? 1.6512 1.5225 1.5109 -0.2992 -0.4193 0.0790 500 ASP A CG 3840 O OD1 . ASP A 500 ? 1.4973 1.3907 1.3624 -0.3012 -0.4251 0.0601 500 ASP A OD1 3841 O OD2 . ASP A 500 ? 1.7549 1.5863 1.6350 -0.2860 -0.4118 0.0834 500 ASP A OD2 3842 N N . LYS A 501 ? 1.5632 1.4004 1.3858 -0.3019 -0.3824 0.0797 501 LYS A N 3843 C CA . LYS A 501 ? 1.6753 1.5097 1.4928 -0.3004 -0.3664 0.0524 501 LYS A CA 3844 C C . LYS A 501 ? 1.7252 1.5386 1.5703 -0.2873 -0.3592 0.0271 501 LYS A C 3845 O O . LYS A 501 ? 1.7318 1.5514 1.5776 -0.2874 -0.3491 -0.0006 501 LYS A O 3846 C CB . LYS A 501 ? 1.6816 1.4916 1.4939 -0.2982 -0.3573 0.0662 501 LYS A CB 3847 C CG . LYS A 501 ? 1.5681 1.3828 1.3684 -0.3004 -0.3419 0.0418 501 LYS A CG 3848 C CD . LYS A 501 ? 1.5771 1.3657 1.3747 -0.2974 -0.3334 0.0556 501 LYS A CD 3849 C CE . LYS A 501 ? 1.6567 1.4022 1.4824 -0.2801 -0.3271 0.0549 501 LYS A CE 3850 N NZ . LYS A 501 ? 1.6662 1.4055 1.5056 -0.2724 -0.3158 0.0248 501 LYS A NZ 3851 N N . LEU A 502 ? 1.7418 1.5324 1.6122 -0.2764 -0.3648 0.0375 502 LEU A N 3852 C CA . LEU A 502 ? 1.6861 1.4587 1.5863 -0.2642 -0.3587 0.0189 502 LEU A CA 3853 C C . LEU A 502 ? 1.8069 1.6065 1.7119 -0.2695 -0.3609 -0.0100 502 LEU A C 3854 O O . LEU A 502 ? 2.0678 1.8661 1.9826 -0.2674 -0.3510 -0.0346 502 LEU A O 3855 C CB . LEU A 502 ? 1.5989 1.3507 1.5244 -0.2530 -0.3662 0.0364 502 LEU A CB 3856 C CG . LEU A 502 ? 1.6119 1.3303 1.5508 -0.2404 -0.3587 0.0503 502 LEU A CG 3857 C CD1 . LEU A 502 ? 1.7233 1.4275 1.6902 -0.2287 -0.3654 0.0622 502 LEU A CD1 3858 C CD2 . LEU A 502 ? 1.3901 1.0963 1.3363 -0.2344 -0.3424 0.0315 502 LEU A CD2 3859 N N . LYS A 503 ? 1.7467 1.5717 1.6476 -0.2763 -0.3746 -0.0081 503 LYS A N 3860 C CA . LYS A 503 ? 1.8130 1.6725 1.7122 -0.2841 -0.3778 -0.0380 503 LYS A CA 3861 C C . LYS A 503 ? 1.9560 1.8580 1.8197 -0.2998 -0.3856 -0.0334 503 LYS A C 3862 O O . LYS A 503 ? 1.9379 1.8584 1.7957 -0.3049 -0.3992 -0.0185 503 LYS A O 3863 C CB . LYS A 503 ? 1.9457 1.8050 1.8760 -0.2784 -0.3874 -0.0463 503 LYS A CB 3864 C CG . LYS A 503 ? 2.0490 1.9480 1.9803 -0.2869 -0.3957 -0.0751 503 LYS A CG 3865 C CD . LYS A 503 ? 2.0828 1.9813 2.0428 -0.2822 -0.4082 -0.0753 503 LYS A CD 3866 C CE . LYS A 503 ? 1.9817 1.8764 1.9311 -0.2827 -0.4192 -0.0404 503 LYS A CE 3867 N NZ . LYS A 503 ? 1.7883 1.6405 1.7584 -0.2694 -0.4155 -0.0165 503 LYS A NZ 3868 N N . GLN A 504 ? 1.9970 1.9169 1.8372 -0.3076 -0.3768 -0.0441 504 GLN A N 3869 C CA . GLN A 504 ? 2.0553 2.0287 1.8669 -0.3227 -0.3817 -0.0557 504 GLN A CA 3870 C C . GLN A 504 ? 2.0058 2.0001 1.8253 -0.3237 -0.3744 -0.1002 504 GLN A C 3871 O O . GLN A 504 ? 2.1262 2.1701 1.9265 -0.3348 -0.3774 -0.1197 504 GLN A O 3872 C CB . GLN A 504 ? 2.0550 2.0405 1.8333 -0.3326 -0.3790 -0.0304 504 GLN A CB 3873 C CG . GLN A 504 ? 2.0613 2.0064 1.8421 -0.3255 -0.3651 -0.0217 504 GLN A CG 3874 C CD . GLN A 504 ? 2.3284 2.2809 2.0829 -0.3348 -0.3658 0.0101 504 GLN A CD 3875 O OE1 . GLN A 504 ? 2.4862 2.4647 2.2262 -0.3445 -0.3783 0.0348 504 GLN A OE1 3876 N NE2 . GLN A 504 ? 2.3256 2.2562 2.0761 -0.3321 -0.3530 0.0109 504 GLN A NE2 3877 N N . LYS A 505 ? 1.7537 1.7125 1.6040 -0.3119 -0.3651 -0.1162 505 LYS A N 3878 C CA . LYS A 505 ? 1.6702 1.6394 1.5314 -0.3118 -0.3556 -0.1544 505 LYS A CA 3879 C C . LYS A 505 ? 1.7864 1.7688 1.6823 -0.3088 -0.3626 -0.1884 505 LYS A C 3880 O O . LYS A 505 ? 1.8926 1.8444 1.8245 -0.2985 -0.3649 -0.1862 505 LYS A O 3881 C CB . LYS A 505 ? 1.6256 1.5504 1.5018 -0.3018 -0.3411 -0.1506 505 LYS A CB 3882 C CG . LYS A 505 ? 1.7960 1.7016 1.6454 -0.3028 -0.3346 -0.1177 505 LYS A CG 3883 C CD . LYS A 505 ? 1.9093 1.8543 1.7186 -0.3171 -0.3340 -0.1161 505 LYS A CD 3884 C CE . LYS A 505 ? 1.8574 1.7812 1.6463 -0.3180 -0.3279 -0.0840 505 LYS A CE 3885 N NZ . LYS A 505 ? 1.9197 1.8851 1.6712 -0.3333 -0.3302 -0.0736 505 LYS A NZ 3886 N N . GLY A 506 ? 1.6783 1.7092 1.5654 -0.3179 -0.3661 -0.2206 506 GLY A N 3887 C CA . GLY A 506 ? 1.6307 1.6797 1.5532 -0.3159 -0.3740 -0.2581 506 GLY A CA 3888 C C . GLY A 506 ? 1.7383 1.7844 1.6771 -0.3133 -0.3887 -0.2460 506 GLY A C 3889 O O . GLY A 506 ? 1.8885 1.9304 1.8691 -0.3077 -0.3951 -0.2684 506 GLY A O 3890 N N . ALA A 507 ? 1.8094 1.8579 1.7185 -0.3175 -0.3948 -0.2096 507 ALA A N 3891 C CA . ALA A 507 ? 1.9814 2.0254 1.9035 -0.3150 -0.4087 -0.1934 507 ALA A CA 3892 C C . ALA A 507 ? 1.9116 1.9826 1.7939 -0.3251 -0.4177 -0.1628 507 ALA A C 3893 O O . ALA A 507 ? 1.8765 1.9773 1.7220 -0.3354 -0.4143 -0.1573 507 ALA A O 3894 C CB . ALA A 507 ? 1.9326 1.9203 1.8848 -0.3015 -0.4054 -0.1702 507 ALA A CB 3895 N N . ILE A 508 ? 1.7334 1.7950 1.6256 -0.3224 -0.4297 -0.1413 508 ILE A N 3896 C CA . ILE A 508 ? 1.6334 1.7232 1.4952 -0.3322 -0.4413 -0.1123 508 ILE A CA 3897 C C . ILE A 508 ? 1.7075 1.7675 1.5509 -0.3315 -0.4375 -0.0674 508 ILE A C 3898 O O . ILE A 508 ? 1.7530 1.7631 1.6173 -0.3196 -0.4327 -0.0506 508 ILE A O 3899 C CB . ILE A 508 ? 1.8461 1.9398 1.7288 -0.3298 -0.4570 -0.1086 508 ILE A CB 3900 C CG1 . ILE A 508 ? 1.6556 1.7736 1.5103 -0.3393 -0.4696 -0.0727 508 ILE A CG1 3901 C CG2 . ILE A 508 ? 1.8975 1.9352 1.8197 -0.3145 -0.4547 -0.0989 508 ILE A CG2 3902 C CD1 . ILE A 508 ? 1.5159 1.7006 1.3336 -0.3556 -0.4744 -0.0813 508 ILE A CD1 3903 N N . ARG A 509 ? 1.7517 1.8459 1.5585 -0.3443 -0.4402 -0.0487 509 ARG A N 3904 C CA . ARG A 509 ? 1.6489 1.7211 1.4419 -0.3456 -0.4405 -0.0043 509 ARG A CA 3905 C C . ARG A 509 ? 1.5989 1.6789 1.3931 -0.3486 -0.4577 0.0269 509 ARG A C 3906 O O . ARG A 509 ? 1.7575 1.8876 1.5367 -0.3597 -0.4693 0.0244 509 ARG A O 3907 C CB . ARG A 509 ? 1.7242 1.8288 1.4815 -0.3585 -0.4353 0.0044 509 ARG A CB 3908 C CG . ARG A 509 ? 1.8628 1.9644 1.6167 -0.3567 -0.4186 -0.0269 509 ARG A CG 3909 C CD . ARG A 509 ? 1.8309 1.9579 1.5513 -0.3686 -0.4131 -0.0107 509 ARG A CD 3910 N NE . ARG A 509 ? 1.7392 1.8649 1.4560 -0.3671 -0.3972 -0.0407 509 ARG A NE 3911 C CZ . ARG A 509 ? 2.0136 2.1412 1.7099 -0.3726 -0.3880 -0.0283 509 ARG A CZ 3912 N NH1 . ARG A 509 ? 2.1432 2.2736 1.8231 -0.3802 -0.3937 0.0143 509 ARG A NH1 3913 N NH2 . ARG A 509 ? 2.1222 2.2486 1.8177 -0.3707 -0.3738 -0.0578 509 ARG A NH2 3914 N N . ARG A 510 ? 1.4852 1.5181 1.2987 -0.3386 -0.4594 0.0552 510 ARG A N 3915 C CA . ARG A 510 ? 1.4672 1.4994 1.2913 -0.3383 -0.4754 0.0818 510 ARG A CA 3916 C C . ARG A 510 ? 1.4841 1.5269 1.2917 -0.3478 -0.4850 0.1258 510 ARG A C 3917 O O . ARG A 510 ? 1.4870 1.5300 1.3044 -0.3484 -0.4993 0.1517 510 ARG A O 3918 C CB . ARG A 510 ? 1.4503 1.4289 1.3110 -0.3208 -0.4733 0.0848 510 ARG A CB 3919 C CG . ARG A 510 ? 1.5378 1.5056 1.4219 -0.3116 -0.4657 0.0465 510 ARG A CG 3920 C CD . ARG A 510 ? 1.4952 1.4147 1.3990 -0.2977 -0.4506 0.0431 510 ARG A CD 3921 N NE . ARG A 510 ? 1.4404 1.3233 1.3697 -0.2854 -0.4539 0.0658 510 ARG A NE 3922 C CZ . ARG A 510 ? 1.4160 1.2601 1.3588 -0.2738 -0.4436 0.0748 510 ARG A CZ 3923 N NH1 . ARG A 510 ? 1.4559 1.2905 1.3882 -0.2734 -0.4295 0.0649 510 ARG A NH1 3924 N NH2 . ARG A 510 ? 1.4101 1.2271 1.3776 -0.2623 -0.4473 0.0927 510 ARG A NH2 3925 N N . ALA A 511 ? 1.5553 1.6076 1.3409 -0.3556 -0.4779 0.1356 511 ALA A N 3926 C CA . ALA A 511 ? 1.5180 1.5804 1.2931 -0.3654 -0.4875 0.1798 511 ALA A CA 3927 C C . ALA A 511 ? 1.5326 1.6453 1.2728 -0.3825 -0.4851 0.1837 511 ALA A C 3928 O O . ALA A 511 ? 1.5747 1.6893 1.3026 -0.3824 -0.4705 0.1591 511 ALA A O 3929 C CB . ALA A 511 ? 1.5205 1.5252 1.3174 -0.3539 -0.4829 0.2017 511 ALA A CB 3930 N N . LEU A 512 ? 1.5594 1.7150 1.2854 -0.3973 -0.4999 0.2164 512 LEU A N 3931 C CA . LEU A 512 ? 1.7753 1.9873 1.4687 -0.4152 -0.4997 0.2271 512 LEU A CA 3932 C C . LEU A 512 ? 1.7875 2.0033 1.4836 -0.4251 -0.5122 0.2828 512 LEU A C 3933 O O . LEU A 512 ? 1.9194 2.1085 1.6404 -0.4204 -0.5250 0.3108 512 LEU A O 3934 C CB . LEU A 512 ? 1.9246 2.2092 1.5942 -0.4275 -0.5065 0.2069 512 LEU A CB 3935 C CG . LEU A 512 ? 1.8440 2.1319 1.5180 -0.4189 -0.4993 0.1520 512 LEU A CG 3936 C CD1 . LEU A 512 ? 1.8019 2.1664 1.4553 -0.4319 -0.5096 0.1365 512 LEU A CD1 3937 C CD2 . LEU A 512 ? 1.7445 2.0178 1.4137 -0.4135 -0.4798 0.1164 512 LEU A CD2 3938 N N . PHE A 513 ? 1.6869 1.9371 1.3607 -0.4388 -0.5092 0.2991 513 PHE A N 3939 C CA . PHE A 513 ? 1.7470 2.0098 1.4254 -0.4510 -0.5227 0.3545 513 PHE A CA 3940 C C . PHE A 513 ? 1.7400 2.0715 1.4041 -0.4676 -0.5407 0.3783 513 PHE A C 3941 O O . PHE A 513 ? 1.8043 2.1940 1.4407 -0.4754 -0.5389 0.3511 513 PHE A O 3942 C CB . PHE A 513 ? 1.8097 2.0862 1.4717 -0.4603 -0.5132 0.3657 513 PHE A CB 3943 C CG . PHE A 513 ? 1.6901 1.8976 1.3702 -0.4451 -0.4984 0.3529 513 PHE A CG 3944 C CD1 . PHE A 513 ? 1.6652 1.8677 1.3289 -0.4399 -0.4789 0.3111 513 PHE A CD1 3945 C CD2 . PHE A 513 ? 1.6008 1.7506 1.3163 -0.4357 -0.5047 0.3816 513 PHE A CD2 3946 C CE1 . PHE A 513 ? 1.5917 1.7339 1.2716 -0.4264 -0.4656 0.3004 513 PHE A CE1 3947 C CE2 . PHE A 513 ? 1.6005 1.6916 1.3323 -0.4216 -0.4914 0.3682 513 PHE A CE2 3948 C CZ . PHE A 513 ? 1.5972 1.6850 1.3100 -0.4172 -0.4717 0.3287 513 PHE A CZ 3949 N N . LEU A 514 ? 1.6369 1.9629 1.3223 -0.4726 -0.5586 0.4280 514 LEU A N 3950 C CA . LEU A 514 ? 1.6195 2.0062 1.2970 -0.4874 -0.5778 0.4557 514 LEU A CA 3951 C C . LEU A 514 ? 1.6271 2.1039 1.2651 -0.5093 -0.5788 0.4634 514 LEU A C 3952 O O . LEU A 514 ? 1.6074 2.1407 1.2193 -0.5149 -0.5784 0.4340 514 LEU A O 3953 C CB . LEU A 514 ? 1.6462 2.0085 1.3589 -0.4897 -0.5969 0.5129 514 LEU A CB 3954 C CG . LEU A 514 ? 1.8437 2.2581 1.5568 -0.5028 -0.6189 0.5458 514 LEU A CG 3955 C CD1 . LEU A 514 ? 1.7794 2.1380 1.5357 -0.4900 -0.6320 0.5638 514 LEU A CD1 3956 C CD2 . LEU A 514 ? 1.9753 2.4500 1.6800 -0.5257 -0.6316 0.5998 514 LEU A CD2 3957 N N . TYR A 515 ? 1.8235 2.3163 1.4592 -0.5216 -0.5806 0.5023 515 TYR A N 3958 C CA . TYR A 515 ? 1.8367 2.4208 1.4373 -0.5441 -0.5832 0.5186 515 TYR A CA 3959 C C . TYR A 515 ? 1.7766 2.3957 1.3408 -0.5441 -0.5635 0.4640 515 TYR A C 3960 O O . TYR A 515 ? 1.6550 2.3580 1.1868 -0.5579 -0.5651 0.4524 515 TYR A O 3961 C CB . TYR A 515 ? 1.9031 2.4907 1.5155 -0.5566 -0.5893 0.5747 515 TYR A CB 3962 C CG . TYR A 515 ? 1.9097 2.4840 1.5588 -0.5618 -0.6126 0.6351 515 TYR A CG 3963 C CD1 . TYR A 515 ? 1.8966 2.3863 1.5913 -0.5478 -0.6163 0.6530 515 TYR A CD1 3964 C CD2 . TYR A 515 ? 1.9537 2.6020 1.5954 -0.5801 -0.6301 0.6727 515 TYR A CD2 3965 C CE1 . TYR A 515 ? 1.9412 2.4185 1.6750 -0.5520 -0.6385 0.7064 515 TYR A CE1 3966 C CE2 . TYR A 515 ? 1.9889 2.6197 1.6742 -0.5823 -0.6451 0.7232 515 TYR A CE2 3967 C CZ . TYR A 515 ? 1.9940 2.5425 1.7221 -0.5704 -0.6555 0.7443 515 TYR A CZ 3968 O OH . TYR A 515 ? 2.0027 2.5335 1.7801 -0.5720 -0.6698 0.7905 515 TYR A OH 3969 N N . SER A 516 ? 1.8271 2.3842 1.3985 -0.5286 -0.5453 0.4299 516 SER A N 3970 C CA . SER A 516 ? 1.8816 2.4643 1.4247 -0.5276 -0.5263 0.3791 516 SER A CA 3971 C C . SER A 516 ? 1.7773 2.3704 1.3135 -0.5183 -0.5220 0.3223 516 SER A C 3972 O O . SER A 516 ? 1.6456 2.2888 1.1561 -0.5223 -0.5121 0.2812 516 SER A O 3973 C CB . SER A 516 ? 1.9566 2.4690 1.5126 -0.5147 -0.5091 0.3653 516 SER A CB 3974 O OG . SER A 516 ? 2.0016 2.5062 1.5662 -0.5235 -0.5132 0.4149 516 SER A OG 3975 N N . ARG A 517 ? 1.8439 2.3908 1.4063 -0.5059 -0.5302 0.3199 517 ARG A N 3976 C CA . ARG A 517 ? 1.8466 2.3914 1.4118 -0.4952 -0.5274 0.2685 517 ARG A CA 3977 C C . ARG A 517 ? 1.7516 2.2667 1.3161 -0.4830 -0.5067 0.2149 517 ARG A C 3978 O O . ARG A 517 ? 1.6962 2.2435 1.2514 -0.4813 -0.5017 0.1665 517 ARG A O 3979 C CB . ARG A 517 ? 1.7934 2.4310 1.3324 -0.5098 -0.5377 0.2577 517 ARG A CB 3980 C CG . ARG A 517 ? 1.6830 2.3162 1.2351 -0.5004 -0.5440 0.2232 517 ARG A CG 3981 C CD . ARG A 517 ? 1.7216 2.4521 1.2464 -0.5145 -0.5523 0.2038 517 ARG A CD 3982 N NE . ARG A 517 ? 1.8033 2.5955 1.3118 -0.5336 -0.5685 0.2577 517 ARG A NE 3983 C CZ . ARG A 517 ? 1.7761 2.5735 1.2966 -0.5367 -0.5869 0.2896 517 ARG A CZ 3984 N NH1 . ARG A 517 ? 1.6593 2.4036 1.2071 -0.5216 -0.5910 0.2718 517 ARG A NH1 3985 N NH2 . ARG A 517 ? 1.8374 2.6909 1.3470 -0.5531 -0.5985 0.3396 517 ARG A NH2 3986 N N . SER A 518 ? 1.8005 2.2547 1.3778 -0.4744 -0.4955 0.2239 518 SER A N 3987 C CA . SER A 518 ? 1.8447 2.2688 1.4226 -0.4637 -0.4758 0.1796 518 SER A CA 3988 C C . SER A 518 ? 1.7160 2.0491 1.3251 -0.4459 -0.4685 0.1854 518 SER A C 3989 O O . SER A 518 ? 1.8481 2.1477 1.4723 -0.4452 -0.4760 0.2283 518 SER A O 3990 C CB . SER A 518 ? 1.8950 2.3644 1.4442 -0.4764 -0.4659 0.1800 518 SER A CB 3991 O OG . SER A 518 ? 1.9114 2.3652 1.4625 -0.4832 -0.4694 0.2317 518 SER A OG 3992 N N . PRO A 519 ? 1.5688 1.8640 1.1902 -0.4315 -0.4544 0.1416 519 PRO A N 3993 C CA . PRO A 519 ? 1.6069 1.8220 1.2568 -0.4142 -0.4461 0.1432 519 PRO A CA 3994 C C . PRO A 519 ? 1.9406 2.1322 1.5860 -0.4157 -0.4366 0.1638 519 PRO A C 3995 O O . PRO A 519 ? 2.0228 2.1532 1.6915 -0.4034 -0.4330 0.1760 519 PRO A O 3996 C CB . PRO A 519 ? 1.5295 1.7284 1.1904 -0.4023 -0.4340 0.0903 519 PRO A CB 3997 C CG . PRO A 519 ? 1.5238 1.7905 1.1578 -0.4143 -0.4306 0.0602 519 PRO A CG 3998 C CD . PRO A 519 ? 1.5469 1.8758 1.1598 -0.4306 -0.4466 0.0878 519 PRO A CD 3999 N N . SER A 520 ? 1.9608 2.2030 1.5776 -0.4304 -0.4328 0.1669 520 SER A N 4000 C CA . SER A 520 ? 1.7772 2.0014 1.3894 -0.4328 -0.4236 0.1843 520 SER A CA 4001 C C . SER A 520 ? 1.6801 1.9527 1.2743 -0.4520 -0.4339 0.2297 520 SER A C 4002 O O . SER A 520 ? 1.7151 2.0556 1.2882 -0.4663 -0.4429 0.2352 520 SER A O 4003 C CB . SER A 520 ? 1.6864 1.9193 1.2847 -0.4308 -0.4051 0.1414 520 SER A CB 4004 O OG . SER A 520 ? 1.5602 1.7509 1.1791 -0.4141 -0.3965 0.1021 520 SER A OG 4005 N N . HIS A 521 ? 1.6324 1.8723 1.2372 -0.4524 -0.4330 0.2624 521 HIS A N 4006 C CA . HIS A 521 ? 1.7751 2.0560 1.3698 -0.4706 -0.4431 0.3101 521 HIS A CA 4007 C C . HIS A 521 ? 1.8885 2.1454 1.4848 -0.4714 -0.4324 0.3208 521 HIS A C 4008 O O . HIS A 521 ? 1.8843 2.0749 1.5019 -0.4558 -0.4236 0.3093 521 HIS A O 4009 C CB . HIS A 521 ? 1.8534 2.1186 1.4738 -0.4723 -0.4634 0.3573 521 HIS A CB 4010 C CG . HIS A 521 ? 1.8221 2.1311 1.4385 -0.4919 -0.4764 0.4111 521 HIS A CG 4011 N ND1 . HIS A 521 ? 1.6578 1.9345 1.2951 -0.4934 -0.4784 0.4458 521 HIS A ND1 4012 C CD2 . HIS A 521 ? 1.8653 2.2507 1.4619 -0.5113 -0.4890 0.4374 521 HIS A CD2 4013 C CE1 . HIS A 521 ? 1.6790 2.0086 1.3117 -0.5132 -0.4920 0.4932 521 HIS A CE1 4014 N NE2 . HIS A 521 ? 1.8795 2.2772 1.4862 -0.5246 -0.4984 0.4900 521 HIS A NE2 4015 N N . SER A 522 ? 1.9261 2.2401 1.5002 -0.4897 -0.4334 0.3432 522 SER A N 4016 C CA . SER A 522 ? 1.7965 2.0949 1.3712 -0.4926 -0.4242 0.3559 522 SER A CA 4017 C C . SER A 522 ? 1.8549 2.1726 1.4411 -0.5081 -0.4399 0.4181 522 SER A C 4018 O O . SER A 522 ? 2.1841 2.5601 1.7612 -0.5235 -0.4545 0.4481 522 SER A O 4019 C CB . SER A 522 ? 1.7598 2.1087 1.2997 -0.5001 -0.4081 0.3223 522 SER A CB 4020 O OG . SER A 522 ? 1.7531 2.0800 1.2896 -0.4854 -0.3942 0.2652 522 SER A OG 4021 N N . LYS A 523 ? 1.7470 2.0172 1.3560 -0.5042 -0.4377 0.4380 523 LYS A N 4022 C CA . LYS A 523 ? 1.8782 2.1597 1.5072 -0.5181 -0.4535 0.4979 523 LYS A CA 4023 C C . LYS A 523 ? 1.9056 2.1717 1.5385 -0.5210 -0.4439 0.5068 523 LYS A C 4024 O O . LYS A 523 ? 1.6610 1.8684 1.3040 -0.5052 -0.4304 0.4775 523 LYS A O 4025 C CB . LYS A 523 ? 1.8093 2.0344 1.4838 -0.5081 -0.4702 0.5252 523 LYS A CB 4026 C CG . LYS A 523 ? 1.7981 2.0625 1.4890 -0.5251 -0.4942 0.5844 523 LYS A CG 4027 C CD . LYS A 523 ? 1.8210 2.1058 1.5240 -0.5413 -0.5007 0.6318 523 LYS A CD 4028 C CE . LYS A 523 ? 1.9734 2.2987 1.6978 -0.5588 -0.5261 0.6944 523 LYS A CE 4029 N NZ . LYS A 523 ? 2.0814 2.4904 1.7675 -0.5738 -0.5305 0.6968 523 LYS A NZ 4030 N N . ASN A 524 ? 2.0430 2.3648 1.6685 -0.5419 -0.4515 0.5488 524 ASN A N 4031 C CA . ASN A 524 ? 1.9966 2.3059 1.6320 -0.5470 -0.4463 0.5675 524 ASN A CA 4032 C C . ASN A 524 ? 1.8806 2.1466 1.5678 -0.5472 -0.4652 0.6183 524 ASN A C 4033 O O . ASN A 524 ? 1.9411 2.2451 1.6425 -0.5627 -0.4848 0.6688 524 ASN A O 4034 C CB . ASN A 524 ? 2.2218 2.6188 1.8234 -0.5701 -0.4439 0.5864 524 ASN A CB 4035 C CG . ASN A 524 ? 2.4608 2.9069 2.0144 -0.5703 -0.4261 0.5338 524 ASN A CG 4036 O OD1 . ASN A 524 ? 2.3709 2.7952 1.9167 -0.5559 -0.4195 0.4889 524 ASN A OD1 4037 N ND2 . ASN A 524 ? 3.0279 3.5427 2.5521 -0.5868 -0.4190 0.5390 524 ASN A ND2 4038 N N . MET A 525 ? 1.7038 1.8928 1.4222 -0.5301 -0.4601 0.6049 525 MET A N 4039 C CA . MET A 525 ? 1.8432 1.9873 1.6171 -0.5279 -0.4784 0.6467 525 MET A CA 4040 C C . MET A 525 ? 2.0336 2.1703 1.8269 -0.5358 -0.4785 0.6733 525 MET A C 4041 O O . MET A 525 ? 2.0281 2.1896 1.7903 -0.5417 -0.4623 0.6571 525 MET A O 4042 C CB . MET A 525 ? 1.6451 1.7089 1.4496 -0.5024 -0.4765 0.6165 525 MET A CB 4043 C CG . MET A 525 ? 1.7084 1.7713 1.5087 -0.4942 -0.4820 0.6011 525 MET A CG 4044 S SD . MET A 525 ? 2.0548 2.0287 1.8986 -0.4657 -0.4826 0.5750 525 MET A SD 4045 C CE . MET A 525 ? 1.6432 1.5868 1.5529 -0.4692 -0.5063 0.6296 525 MET A CE 4046 N N . THR A 526 ? 1.9922 2.0942 1.8409 -0.5358 -0.4975 0.7138 526 THR A N 4047 C CA . THR A 526 ? 1.7790 1.8590 1.6596 -0.5398 -0.5000 0.7376 526 THR A CA 4048 C C . THR A 526 ? 1.8334 1.8397 1.7787 -0.5238 -0.5142 0.7458 526 THR A C 4049 O O . THR A 526 ? 1.9965 1.9959 1.9735 -0.5229 -0.5332 0.7695 526 THR A O 4050 C CB . THR A 526 ? 1.7584 1.9049 1.6433 -0.5673 -0.5145 0.7985 526 THR A CB 4051 O OG1 . THR A 526 ? 1.7585 1.9810 1.5821 -0.5817 -0.5014 0.7879 526 THR A OG1 4052 C CG2 . THR A 526 ? 1.8860 2.0090 1.8052 -0.5714 -0.5165 0.8213 526 THR A CG2 4053 N N . ILE A 527 ? 1.8349 1.7883 1.8013 -0.5110 -0.5054 0.7249 527 ILE A N 4054 C CA . ILE A 527 ? 1.8437 1.7286 1.8718 -0.4937 -0.5173 0.7243 527 ILE A CA 4055 C C . ILE A 527 ? 1.7624 1.6294 1.8396 -0.5003 -0.5284 0.7577 527 ILE A C 4056 O O . ILE A 527 ? 1.6604 1.5665 1.7210 -0.5179 -0.5253 0.7806 527 ILE A O 4057 C CB . ILE A 527 ? 1.7331 1.5627 1.7509 -0.4674 -0.4977 0.6619 527 ILE A CB 4058 C CG1 . ILE A 527 ? 1.7987 1.6562 1.7529 -0.4648 -0.4780 0.6219 527 ILE A CG1 4059 C CG2 . ILE A 527 ? 1.6703 1.4466 1.7400 -0.4486 -0.5110 0.6560 527 ILE A CG2 4060 C CD1 . ILE A 527 ? 1.8707 1.7440 1.8197 -0.4636 -0.4877 0.6251 527 ILE A CD1 4061 N N . SER A 528 ? 1.6965 1.5059 1.8365 -0.4857 -0.5418 0.7588 528 SER A N 4062 C CA . SER A 528 ? 1.5306 1.3177 1.7266 -0.4831 -0.5489 0.7711 528 SER A CA 4063 C C . SER A 528 ? 1.7556 1.4725 1.9710 -0.4586 -0.5397 0.7253 528 SER A C 4064 O O . SER A 528 ? 2.0867 1.7840 2.2684 -0.4438 -0.5244 0.6818 528 SER A O 4065 C CB . SER A 528 ? 1.5074 1.3125 1.7760 -0.4837 -0.5728 0.8049 528 SER A CB 4066 O OG . SER A 528 ? 1.5306 1.4056 1.7832 -0.5070 -0.5809 0.8472 528 SER A OG 4067 N N . ARG A 529 ? 1.6694 1.3636 1.9411 -0.4481 -0.5443 0.7208 529 ARG A N 4068 C CA . ARG A 529 ? 1.6474 1.2833 1.9372 -0.4246 -0.5344 0.6751 529 ARG A CA 4069 C C . ARG A 529 ? 2.0166 1.6232 2.3827 -0.4032 -0.5501 0.6648 529 ARG A C 4070 O O . ARG A 529 ? 2.1884 1.8171 2.5986 -0.4074 -0.5698 0.6951 529 ARG A O 4071 C CB . ARG A 529 ? 1.7810 1.4120 2.0666 -0.4272 -0.5228 0.6673 529 ARG A CB 4072 C CG . ARG A 529 ? 1.8956 1.5541 2.1063 -0.4471 -0.5052 0.6715 529 ARG A CG 4073 C CD . ARG A 529 ? 2.1112 1.7769 2.3276 -0.4532 -0.4983 0.6759 529 ARG A CD 4074 N NE . ARG A 529 ? 1.9158 1.5300 2.1662 -0.4310 -0.4923 0.6381 529 ARG A NE 4075 C CZ . ARG A 529 ? 1.6697 1.2802 1.9435 -0.4300 -0.4898 0.6376 529 ARG A CZ 4076 N NH1 . ARG A 529 ? 1.4560 1.1101 1.7242 -0.4500 -0.4927 0.6739 529 ARG A NH1 4077 N NH2 . ARG A 529 ? 1.8343 1.4009 2.1372 -0.4087 -0.4843 0.6004 529 ARG A NH2 4078 N N . GLY A 530 ? 2.0185 1.5789 2.4005 -0.3806 -0.5411 0.6207 530 GLY A N 4079 C CA . GLY A 530 ? 2.1372 1.6713 2.5906 -0.3585 -0.5535 0.6035 530 GLY A CA 4080 C C . GLY A 530 ? 2.1976 1.7145 2.6593 -0.3440 -0.5579 0.5854 530 GLY A C 4081 O O . GLY A 530 ? 2.2935 1.7824 2.8001 -0.3216 -0.5608 0.5552 530 GLY A O 4082 N N . GLY A 531 ? 1.9394 1.4757 2.3581 -0.3565 -0.5583 0.6028 531 GLY A N 4083 C CA . GLY A 531 ? 1.8298 1.3519 2.2533 -0.3440 -0.5625 0.5878 531 GLY A CA 4084 C C . GLY A 531 ? 2.0713 1.6285 2.4809 -0.3607 -0.5752 0.6259 531 GLY A C 4085 O O . GLY A 531 ? 2.1912 1.7873 2.5704 -0.3837 -0.5767 0.6608 531 GLY A O 4086 N N . LEU A 532 ? 2.0853 1.6322 2.5171 -0.3490 -0.5841 0.6182 532 LEU A N 4087 C CA . LEU A 532 ? 1.9666 1.5462 2.3968 -0.3621 -0.5988 0.6531 532 LEU A CA 4088 C C . LEU A 532 ? 1.8824 1.4914 2.2346 -0.3825 -0.5899 0.6693 532 LEU A C 4089 O O . LEU A 532 ? 1.8391 1.4924 2.1742 -0.4045 -0.5944 0.7061 532 LEU A O 4090 C CB . LEU A 532 ? 1.8424 1.4537 2.3291 -0.3736 -0.6190 0.6942 532 LEU A CB 4091 C CG . LEU A 532 ? 1.8409 1.4355 2.4130 -0.3570 -0.6366 0.6891 532 LEU A CG 4092 C CD1 . LEU A 532 ? 1.9088 1.5379 2.5126 -0.3694 -0.6576 0.7291 532 LEU A CD1 4093 C CD2 . LEU A 532 ? 1.8002 1.3513 2.3838 -0.3301 -0.6295 0.6410 532 LEU A CD2 4094 N N . MET A 533 ? 1.7135 1.3076 2.0199 -0.3729 -0.5747 0.6350 533 MET A N 4095 C CA . MET A 533 ? 1.6505 1.2870 1.8825 -0.3837 -0.5580 0.6267 533 MET A CA 4096 C C . MET A 533 ? 1.6481 1.3334 1.8706 -0.4050 -0.5743 0.6731 533 MET A C 4097 O O . MET A 533 ? 1.7957 1.4772 2.0549 -0.4036 -0.5936 0.6944 533 MET A O 4098 C CB . MET A 533 ? 1.4981 1.1201 1.6993 -0.3648 -0.5410 0.5778 533 MET A CB 4099 C CG . MET A 533 ? 1.5585 1.1310 1.7856 -0.3399 -0.5313 0.5358 533 MET A CG 4100 S SD . MET A 533 ? 2.2865 1.8533 2.4673 -0.3219 -0.5078 0.4818 533 MET A SD 4101 C CE . MET A 533 ? 1.7299 1.2464 1.9496 -0.2955 -0.4997 0.4419 533 MET A CE 4102 N N . GLN A 534 ? 1.7043 1.4386 1.8780 -0.4248 -0.5664 0.6881 534 GLN A N 4103 C CA . GLN A 534 ? 1.7507 1.5421 1.9043 -0.4457 -0.5785 0.7272 534 GLN A CA 4104 C C . GLN A 534 ? 1.9526 1.7630 2.0550 -0.4403 -0.5659 0.6946 534 GLN A C 4105 O O . GLN A 534 ? 1.8392 1.6579 1.8906 -0.4366 -0.5430 0.6555 534 GLN A O 4106 C CB . GLN A 534 ? 1.6295 1.4727 1.7537 -0.4695 -0.5758 0.7569 534 GLN A CB 4107 C CG . GLN A 534 ? 1.6971 1.6094 1.7964 -0.4922 -0.5873 0.7968 534 GLN A CG 4108 C CD . GLN A 534 ? 1.9511 1.9228 2.0119 -0.5146 -0.5806 0.8183 534 GLN A CD 4109 O OE1 . GLN A 534 ? 2.0008 2.0144 1.9999 -0.5200 -0.5633 0.7935 534 GLN A OE1 4110 N NE2 . GLN A 534 ? 1.9625 1.9427 2.0648 -0.5263 -0.5926 0.8589 534 GLN A NE2 4111 N N . CYS A 535 ? 2.0153 1.8323 2.1348 -0.4400 -0.5817 0.7110 535 CYS A N 4112 C CA . CYS A 535 ? 1.6594 1.4884 1.7399 -0.4329 -0.5722 0.6797 535 CYS A CA 4113 C C . CYS A 535 ? 1.5737 1.4707 1.6187 -0.4542 -0.5796 0.7074 535 CYS A C 4114 O O . CYS A 535 ? 1.5579 1.4836 1.6280 -0.4705 -0.6010 0.7591 535 CYS A O 4115 C CB . CYS A 535 ? 1.5511 1.3363 1.6746 -0.4138 -0.5823 0.6692 535 CYS A CB 4116 S SG . CYS A 535 ? 2.2166 1.9285 2.3890 -0.3881 -0.5766 0.6376 535 CYS A SG 4117 N N . GLU A 536 ? 1.7718 1.6967 1.7604 -0.4541 -0.5626 0.6726 536 GLU A N 4118 C CA . GLU A 536 ? 1.8391 1.8297 1.7926 -0.4712 -0.5687 0.6894 536 GLU A CA 4119 C C . GLU A 536 ? 1.8005 1.7791 1.7586 -0.4597 -0.5741 0.6732 536 GLU A C 4120 O O . GLU A 536 ? 1.5888 1.5107 1.5750 -0.4389 -0.5716 0.6490 536 GLU A O 4121 C CB . GLU A 536 ? 1.8150 1.8514 1.7062 -0.4798 -0.5482 0.6606 536 GLU A CB 4122 C CG . GLU A 536 ? 1.8720 1.9235 1.7551 -0.4913 -0.5411 0.6742 536 GLU A CG 4123 C CD . GLU A 536 ? 1.8855 1.9844 1.7858 -0.5146 -0.5614 0.7375 536 GLU A CD 4124 O OE1 . GLU A 536 ? 1.9603 2.1096 1.8515 -0.5278 -0.5751 0.7640 536 GLU A OE1 4125 O OE2 . GLU A 536 ? 1.8892 1.9766 1.8139 -0.5202 -0.5644 0.7621 536 GLU A OE2 4126 N N . GLU A 537 ? 1.9682 2.0031 1.8988 -0.4732 -0.5813 0.6860 537 GLU A N 4127 C CA . GLU A 537 ? 1.8362 1.8649 1.7708 -0.4642 -0.5878 0.6737 537 GLU A CA 4128 C C . GLU A 537 ? 1.6289 1.7152 1.5087 -0.4728 -0.5796 0.6510 537 GLU A C 4129 O O . GLU A 537 ? 1.7357 1.8867 1.5848 -0.4929 -0.5814 0.6702 537 GLU A O 4130 C CB . GLU A 537 ? 1.9625 1.9948 1.9432 -0.4711 -0.6155 0.7256 537 GLU A CB 4131 C CG . GLU A 537 ? 1.9471 1.9573 1.9452 -0.4578 -0.6234 0.7137 537 GLU A CG 4132 C CD . GLU A 537 ? 1.8220 1.7575 1.8561 -0.4320 -0.6168 0.6827 537 GLU A CD 4133 O OE1 . GLU A 537 ? 1.5708 1.4700 1.6267 -0.4253 -0.6112 0.6791 537 GLU A OE1 4134 O OE2 . GLU A 537 ? 1.9317 1.8477 1.9728 -0.4185 -0.6175 0.6618 537 GLU A OE2 4135 N N . LEU A 538 ? 1.6171 1.6822 1.4871 -0.4574 -0.5708 0.6094 538 LEU A N 4136 C CA . LEU A 538 ? 1.7693 1.8838 1.5941 -0.4630 -0.5638 0.5819 538 LEU A CA 4137 C C . LEU A 538 ? 1.6660 1.7582 1.5031 -0.4494 -0.5685 0.5627 538 LEU A C 4138 O O . LEU A 538 ? 1.6093 1.6405 1.4784 -0.4304 -0.5664 0.5493 538 LEU A O 4139 C CB . LEU A 538 ? 1.6593 1.7763 1.4472 -0.4590 -0.5392 0.5347 538 LEU A CB 4140 C CG . LEU A 538 ? 1.6420 1.8311 1.3809 -0.4729 -0.5330 0.5157 538 LEU A CG 4141 C CD1 . LEU A 538 ? 1.6683 1.9260 1.3941 -0.4974 -0.5459 0.5624 538 LEU A CD1 4142 C CD2 . LEU A 538 ? 1.6226 1.8058 1.3342 -0.4669 -0.5092 0.4684 538 LEU A CD2 4143 N N . ILE A 539 ? 1.6085 1.7532 1.4209 -0.4591 -0.5749 0.5610 539 ILE A N 4144 C CA . ILE A 539 ? 1.7159 1.8455 1.5401 -0.4482 -0.5811 0.5462 539 ILE A CA 4145 C C . ILE A 539 ? 1.7308 1.8821 1.5195 -0.4442 -0.5669 0.4950 539 ILE A C 4146 O O . ILE A 539 ? 1.7316 1.9446 1.4830 -0.4585 -0.5640 0.4866 539 ILE A O 4147 C CB . ILE A 539 ? 1.7828 1.9510 1.6198 -0.4617 -0.6057 0.5920 539 ILE A CB 4148 C CG1 . ILE A 539 ? 1.6195 1.7782 1.4644 -0.4515 -0.6116 0.5740 539 ILE A CG1 4149 C CG2 . ILE A 539 ? 1.8675 2.1197 1.6670 -0.4861 -0.6107 0.6125 539 ILE A CG2 4150 C CD1 . ILE A 539 ? 1.6390 1.8257 1.5036 -0.4621 -0.6365 0.6195 539 ILE A CD1 4151 N N . ALA A 540 ? 1.5960 1.6980 1.3995 -0.4244 -0.5584 0.4605 540 ALA A N 4152 C CA . ALA A 540 ? 1.5823 1.6967 1.3627 -0.4186 -0.5463 0.4119 540 ALA A CA 4153 C C . ALA A 540 ? 1.6407 1.7463 1.4387 -0.4105 -0.5568 0.4069 540 ALA A C 4154 O O . ALA A 540 ? 1.8135 1.8854 1.6454 -0.4035 -0.5685 0.4324 540 ALA A O 4155 C CB . ALA A 540 ? 1.5792 1.6473 1.3613 -0.4031 -0.5250 0.3729 540 ALA A CB 4156 N N . TYR A 541 ? 1.6883 1.8241 1.4661 -0.4113 -0.5531 0.3728 541 TYR A N 4157 C CA . TYR A 541 ? 1.5834 1.7171 1.3764 -0.4053 -0.5639 0.3679 541 TYR A CA 4158 C C . TYR A 541 ? 1.5597 1.6730 1.3545 -0.3912 -0.5509 0.3176 541 TYR A C 4159 O O . TYR A 541 ? 1.5517 1.6630 1.3318 -0.3886 -0.5345 0.2848 541 TYR A O 4160 C CB . TYR A 541 ? 1.5881 1.7921 1.3603 -0.4236 -0.5799 0.3856 541 TYR A CB 4161 C CG . TYR A 541 ? 1.7403 2.0025 1.4755 -0.4330 -0.5722 0.3492 541 TYR A CG 4162 C CD1 . TYR A 541 ? 1.7773 2.0802 1.4827 -0.4460 -0.5645 0.3492 541 TYR A CD1 4163 C CD2 . TYR A 541 ? 1.7637 2.0424 1.4965 -0.4288 -0.5733 0.3139 541 TYR A CD2 4164 C CE1 . TYR A 541 ? 1.8138 2.1734 1.4876 -0.4539 -0.5576 0.3128 541 TYR A CE1 4165 C CE2 . TYR A 541 ? 1.6993 2.0327 1.4031 -0.4366 -0.5673 0.2769 541 TYR A CE2 4166 C CZ . TYR A 541 ? 1.7896 2.1642 1.4639 -0.4489 -0.5593 0.2755 541 TYR A CZ 4167 O OH . TYR A 541 ? 1.7912 2.2235 1.4388 -0.4561 -0.5535 0.2357 541 TYR A OH 4168 N N . LEU A 542 ? 1.6699 1.7684 1.4858 -0.3825 -0.5593 0.3134 542 LEU A N 4169 C CA . LEU A 542 ? 1.5281 1.6046 1.3543 -0.3688 -0.5495 0.2712 542 LEU A CA 4170 C C . LEU A 542 ? 1.5225 1.6477 1.3363 -0.3762 -0.5579 0.2511 542 LEU A C 4171 O O . LEU A 542 ? 1.5305 1.6867 1.3428 -0.3852 -0.5749 0.2756 542 LEU A O 4172 C CB . LEU A 542 ? 1.5185 1.5373 1.3833 -0.3509 -0.5510 0.2786 542 LEU A CB 4173 C CG . LEU A 542 ? 1.5132 1.4954 1.3956 -0.3340 -0.5372 0.2416 542 LEU A CG 4174 C CD1 . LEU A 542 ? 1.6566 1.6187 1.5304 -0.3296 -0.5181 0.2223 542 LEU A CD1 4175 C CD2 . LEU A 542 ? 1.5028 1.4403 1.4224 -0.3183 -0.5415 0.2544 542 LEU A CD2 4176 N N . ARG A 543 ? 1.5111 1.6441 1.3188 -0.3725 -0.5467 0.2063 543 ARG A N 4177 C CA . ARG A 543 ? 1.5390 1.7157 1.3406 -0.3776 -0.5543 0.1802 543 ARG A CA 4178 C C . ARG A 543 ? 1.5712 1.7240 1.4030 -0.3680 -0.5654 0.1857 543 ARG A C 4179 O O . ARG A 543 ? 1.6278 1.7255 1.4876 -0.3535 -0.5615 0.1939 543 ARG A O 4180 C CB . ARG A 543 ? 1.5050 1.6881 1.3032 -0.3737 -0.5402 0.1290 543 ARG A CB 4181 C CG . ARG A 543 ? 1.5391 1.7514 1.3073 -0.3833 -0.5289 0.1176 543 ARG A CG 4182 C CD . ARG A 543 ? 1.5354 1.7470 1.3089 -0.3772 -0.5155 0.0657 543 ARG A CD 4183 N NE . ARG A 543 ? 1.6443 1.8829 1.3910 -0.3854 -0.5039 0.0522 543 ARG A NE 4184 C CZ . ARG A 543 ? 1.7638 2.0684 1.4856 -0.3979 -0.5056 0.0291 543 ARG A CZ 4185 N NH1 . ARG A 543 ? 1.8066 2.1576 1.5267 -0.4039 -0.5188 0.0161 543 ARG A NH1 4186 N NH2 . ARG A 543 ? 1.8270 2.1540 1.5261 -0.4044 -0.4940 0.0177 543 ARG A NH2 4187 N N . ASP A 544 ? 1.5133 1.7109 1.3396 -0.3760 -0.5792 0.1805 544 ASP A N 4188 C CA . ASP A 544 ? 1.5522 1.7321 1.4068 -0.3677 -0.5902 0.1831 544 ASP A CA 4189 C C . ASP A 544 ? 1.5254 1.6718 1.4061 -0.3530 -0.5799 0.1435 544 ASP A C 4190 O O . ASP A 544 ? 1.4822 1.6328 1.3566 -0.3520 -0.5671 0.1097 544 ASP A O 4191 C CB . ASP A 544 ? 1.7083 1.9488 1.5496 -0.3809 -0.6079 0.1858 544 ASP A CB 4192 C CG . ASP A 544 ? 1.9451 2.2410 1.7644 -0.3897 -0.6048 0.1436 544 ASP A CG 4193 O OD1 . ASP A 544 ? 1.9500 2.2769 1.7750 -0.3917 -0.6149 0.1224 544 ASP A OD1 4194 O OD2 . ASP A 544 ? 2.0590 2.3689 1.8569 -0.3944 -0.5926 0.1302 544 ASP A OD2 4195 N N . GLU A 545 ? 1.5552 1.6699 1.4677 -0.3418 -0.5859 0.1495 545 GLU A N 4196 C CA . GLU A 545 ? 1.5851 1.6631 1.5292 -0.3269 -0.5770 0.1213 545 GLU A CA 4197 C C . GLU A 545 ? 1.7129 1.8196 1.6579 -0.3296 -0.5741 0.0749 545 GLU A C 4198 O O . GLU A 545 ? 1.7061 1.7857 1.6734 -0.3195 -0.5629 0.0491 545 GLU A O 4199 C CB . GLU A 545 ? 1.7320 1.7864 1.7081 -0.3175 -0.5877 0.1370 545 GLU A CB 4200 C CG . GLU A 545 ? 1.8775 1.9059 1.8598 -0.3141 -0.5934 0.1807 545 GLU A CG 4201 C CD . GLU A 545 ? 1.9950 2.0624 1.9596 -0.3282 -0.6114 0.2101 545 GLU A CD 4202 O OE1 . GLU A 545 ? 1.9890 2.1069 1.9241 -0.3429 -0.6154 0.2013 545 GLU A OE1 4203 O OE2 . GLU A 545 ? 2.0356 2.0859 2.0174 -0.3246 -0.6218 0.2422 545 GLU A OE2 4204 N N . SER A 546 ? 1.8404 2.0045 1.7641 -0.3431 -0.5850 0.0642 546 SER A N 4205 C CA . SER A 546 ? 1.7545 1.9515 1.6841 -0.3457 -0.5856 0.0173 546 SER A CA 4206 C C . SER A 546 ? 1.6994 1.9060 1.6152 -0.3478 -0.5704 -0.0136 546 SER A C 4207 O O . SER A 546 ? 1.7344 1.9379 1.6727 -0.3424 -0.5653 -0.0532 546 SER A O 4208 C CB . SER A 546 ? 1.6689 1.9309 1.5792 -0.3595 -0.6025 0.0139 546 SER A CB 4209 O OG . SER A 546 ? 1.5966 1.9008 1.4654 -0.3738 -0.6033 0.0328 546 SER A OG 4210 N N . GLU A 547 ? 1.5891 1.8077 1.4712 -0.3558 -0.5640 0.0053 547 GLU A N 4211 C CA . GLU A 547 ? 1.5393 1.7764 1.4033 -0.3600 -0.5508 -0.0226 547 GLU A CA 4212 C C . GLU A 547 ? 1.4791 1.6633 1.3689 -0.3464 -0.5344 -0.0415 547 GLU A C 4213 O O . GLU A 547 ? 1.5402 1.7378 1.4316 -0.3468 -0.5257 -0.0787 547 GLU A O 4214 C CB . GLU A 547 ? 1.7012 1.9602 1.5257 -0.3715 -0.5479 0.0078 547 GLU A CB 4215 C CG . GLU A 547 ? 1.8644 2.1912 1.6593 -0.3881 -0.5629 0.0225 547 GLU A CG 4216 C CD . GLU A 547 ? 1.9535 2.3124 1.7108 -0.4012 -0.5589 0.0462 547 GLU A CD 4217 O OE1 . GLU A 547 ? 1.8700 2.2336 1.6153 -0.4020 -0.5448 0.0238 547 GLU A OE1 4218 O OE2 . GLU A 547 ? 1.9650 2.3453 1.7070 -0.4110 -0.5704 0.0885 547 GLU A OE2 4219 N N . PHE A 548 ? 1.4720 1.5994 1.3834 -0.3344 -0.5304 -0.0161 548 PHE A N 4220 C CA . PHE A 548 ? 1.5251 1.6051 1.4614 -0.3216 -0.5152 -0.0296 548 PHE A CA 4221 C C . PHE A 548 ? 1.5513 1.5883 1.5279 -0.3077 -0.5178 -0.0204 548 PHE A C 4222 O O . PHE A 548 ? 1.6480 1.6913 1.6339 -0.3078 -0.5314 -0.0065 548 PHE A O 4223 C CB . PHE A 548 ? 1.5552 1.6108 1.4711 -0.3208 -0.5022 -0.0076 548 PHE A CB 4224 C CG . PHE A 548 ? 1.5017 1.5285 1.4166 -0.3172 -0.5064 0.0370 548 PHE A CG 4225 C CD1 . PHE A 548 ? 1.4366 1.4113 1.3778 -0.3026 -0.4991 0.0492 548 PHE A CD1 4226 C CD2 . PHE A 548 ? 1.5290 1.5839 1.4196 -0.3285 -0.5183 0.0665 548 PHE A CD2 4227 C CE1 . PHE A 548 ? 1.4359 1.3860 1.3802 -0.2983 -0.5035 0.0863 548 PHE A CE1 4228 C CE2 . PHE A 548 ? 1.4970 1.5247 1.3931 -0.3248 -0.5235 0.1065 548 PHE A CE2 4229 C CZ . PHE A 548 ? 1.4825 1.4572 1.4061 -0.3093 -0.5161 0.1146 548 PHE A CZ 4230 N N . ARG A 549 ? 1.4753 1.4717 1.4760 -0.2960 -0.5047 -0.0272 549 ARG A N 4231 C CA . ARG A 549 ? 1.4882 1.4493 1.5296 -0.2828 -0.5057 -0.0208 549 ARG A CA 4232 C C . ARG A 549 ? 1.5752 1.4924 1.6220 -0.2719 -0.4956 0.0077 549 ARG A C 4233 O O . ARG A 549 ? 1.6616 1.5633 1.7167 -0.2667 -0.5022 0.0348 549 ARG A O 4234 C CB . ARG A 549 ? 1.5863 1.5439 1.6636 -0.2778 -0.5014 -0.0563 549 ARG A CB 4235 C CG . ARG A 549 ? 1.7160 1.7147 1.8009 -0.2858 -0.5138 -0.0881 549 ARG A CG 4236 C CD . ARG A 549 ? 1.8351 1.8243 1.9682 -0.2792 -0.5123 -0.1194 549 ARG A CD 4237 N NE . ARG A 549 ? 2.0317 2.0599 2.1785 -0.2858 -0.5258 -0.1524 549 ARG A NE 4238 C CZ . ARG A 549 ? 1.9255 1.9620 2.0939 -0.2852 -0.5406 -0.1503 549 ARG A CZ 4239 N NH1 . ARG A 549 ? 1.8150 1.8237 1.9934 -0.2782 -0.5435 -0.1160 549 ARG A NH1 4240 N NH2 . ARG A 549 ? 1.8671 1.9415 2.0484 -0.2913 -0.5528 -0.1840 549 ARG A NH2 4241 N N . ASP A 550 ? 1.5339 1.4330 1.5777 -0.2682 -0.4801 -0.0002 550 ASP A N 4242 C CA . ASP A 550 ? 1.5042 1.3636 1.5590 -0.2563 -0.4694 0.0199 550 ASP A CA 4243 C C . ASP A 550 ? 1.3773 1.2272 1.4121 -0.2567 -0.4732 0.0543 550 ASP A C 4244 O O . ASP A 550 ? 1.3818 1.2460 1.3846 -0.2664 -0.4734 0.0625 550 ASP A O 4245 C CB . ASP A 550 ? 1.4684 1.3163 1.5188 -0.2545 -0.4527 0.0038 550 ASP A CB 4246 C CG . ASP A 550 ? 1.4485 1.2620 1.5015 -0.2441 -0.4414 0.0242 550 ASP A CG 4247 O OD1 . ASP A 550 ? 1.4888 1.2824 1.5660 -0.2333 -0.4429 0.0399 550 ASP A OD1 4248 O OD2 . ASP A 550 ? 1.5500 1.3587 1.5814 -0.2466 -0.4310 0.0232 550 ASP A OD2 4249 N N . LYS A 551 ? 1.4010 1.2285 1.4587 -0.2462 -0.4768 0.0744 551 LYS A N 4250 C CA . LYS A 551 ? 1.3809 1.1943 1.4310 -0.2437 -0.4808 0.1058 551 LYS A CA 4251 C C . LYS A 551 ? 1.3719 1.1523 1.4324 -0.2313 -0.4674 0.1132 551 LYS A C 4252 O O . LYS A 551 ? 1.5747 1.3408 1.6343 -0.2276 -0.4699 0.1360 551 LYS A O 4253 C CB . LYS A 551 ? 1.4965 1.3109 1.5660 -0.2402 -0.4956 0.1228 551 LYS A CB 4254 C CG . LYS A 551 ? 1.4863 1.3359 1.5450 -0.2526 -0.5105 0.1179 551 LYS A CG 4255 C CD . LYS A 551 ? 1.4754 1.3244 1.5554 -0.2486 -0.5249 0.1351 551 LYS A CD 4256 C CE . LYS A 551 ? 1.4853 1.3725 1.5532 -0.2615 -0.5403 0.1302 551 LYS A CE 4257 N NZ . LYS A 551 ? 1.5639 1.4508 1.6534 -0.2578 -0.5548 0.1467 551 LYS A NZ 4258 N N . LEU A 552 ? 1.3432 1.1134 1.4164 -0.2249 -0.4539 0.0937 552 LEU A N 4259 C CA . LEU A 552 ? 1.3355 1.0788 1.4233 -0.2118 -0.4412 0.0990 552 LEU A CA 4260 C C . LEU A 552 ? 1.3340 1.0689 1.3982 -0.2144 -0.4297 0.0972 552 LEU A C 4261 O O . LEU A 552 ? 1.3440 1.0636 1.4048 -0.2098 -0.4284 0.1142 552 LEU A O 4262 C CB . LEU A 552 ? 1.4688 1.2070 1.5876 -0.2028 -0.4333 0.0836 552 LEU A CB 4263 C CG . LEU A 552 ? 1.5279 1.2635 1.6795 -0.1934 -0.4405 0.0938 552 LEU A CG 4264 C CD1 . LEU A 552 ? 1.5256 1.2603 1.7102 -0.1864 -0.4330 0.0811 552 LEU A CD1 4265 C CD2 . LEU A 552 ? 1.3096 1.0293 1.4672 -0.1828 -0.4403 0.1155 552 LEU A CD2 4266 N N . THR A 553 ? 1.3257 1.0707 1.3772 -0.2213 -0.4217 0.0758 553 THR A N 4267 C CA . THR A 553 ? 1.4030 1.1410 1.4333 -0.2238 -0.4098 0.0720 553 THR A CA 4268 C C . THR A 553 ? 1.5430 1.2838 1.5473 -0.2316 -0.4162 0.0929 553 THR A C 4269 O O . THR A 553 ? 1.5811 1.3456 1.5677 -0.2435 -0.4275 0.0982 553 THR A O 4270 C CB . THR A 553 ? 1.4328 1.1883 1.4517 -0.2326 -0.4034 0.0447 553 THR A CB 4271 O OG1 . THR A 553 ? 1.4685 1.2205 1.5186 -0.2257 -0.3990 0.0272 553 THR A OG1 4272 C CG2 . THR A 553 ? 1.5108 1.2588 1.5090 -0.2349 -0.3906 0.0411 553 THR A CG2 4273 N N . PRO A 554 ? 1.4362 1.1550 1.4411 -0.2249 -0.4099 0.1057 554 PRO A N 4274 C CA . PRO A 554 ? 1.3881 1.1054 1.3777 -0.2308 -0.4170 0.1288 554 PRO A CA 4275 C C . PRO A 554 ? 1.4121 1.1534 1.3681 -0.2474 -0.4178 0.1269 554 PRO A C 4276 O O . PRO A 554 ? 1.3945 1.1461 1.3382 -0.2516 -0.4078 0.1044 554 PRO A O 4277 C CB . PRO A 554 ? 1.3766 1.0660 1.3768 -0.2193 -0.4064 0.1324 554 PRO A CB 4278 C CG . PRO A 554 ? 1.3657 1.0439 1.3923 -0.2050 -0.3983 0.1194 554 PRO A CG 4279 C CD . PRO A 554 ? 1.3779 1.0738 1.4024 -0.2107 -0.3966 0.0995 554 PRO A CD 4280 N N . ILE A 555 ? 1.4298 1.1826 1.3737 -0.2570 -0.4299 0.1512 555 ILE A N 4281 C CA . ILE A 555 ? 1.4468 1.2276 1.3587 -0.2734 -0.4311 0.1542 555 ILE A CA 4282 C C . ILE A 555 ? 1.4585 1.2216 1.3642 -0.2732 -0.4233 0.1647 555 ILE A C 4283 O O . ILE A 555 ? 1.4802 1.2274 1.3983 -0.2708 -0.4308 0.1901 555 ILE A O 4284 C CB . ILE A 555 ? 1.4661 1.2759 1.3684 -0.2860 -0.4494 0.1782 555 ILE A CB 4285 C CG1 . ILE A 555 ? 1.4550 1.2827 1.3647 -0.2859 -0.4576 0.1665 555 ILE A CG1 4286 C CG2 . ILE A 555 ? 1.5445 1.3903 1.4133 -0.3037 -0.4501 0.1831 555 ILE A CG2 4287 C CD1 . ILE A 555 ? 1.4850 1.3426 1.3870 -0.2976 -0.4763 0.1904 555 ILE A CD1 4288 N N . THR A 556 ? 1.4516 1.2177 1.3412 -0.2756 -0.4091 0.1445 556 THR A N 4289 C CA . THR A 556 ? 1.4528 1.2005 1.3379 -0.2743 -0.4001 0.1508 556 THR A CA 4290 C C . THR A 556 ? 1.5996 1.3745 1.4574 -0.2915 -0.4042 0.1663 556 THR A C 4291 O O . THR A 556 ? 1.4965 1.3021 1.3295 -0.3021 -0.3995 0.1506 556 THR A O 4292 C CB . THR A 556 ? 1.4224 1.1562 1.3078 -0.2667 -0.3816 0.1221 556 THR A CB 4293 O OG1 . THR A 556 ? 1.3940 1.1033 1.3078 -0.2505 -0.3775 0.1132 556 THR A OG1 4294 C CG2 . THR A 556 ? 1.5472 1.2659 1.4251 -0.2670 -0.3727 0.1280 556 THR A CG2 4295 N N . ILE A 557 ? 1.7444 1.5100 1.6096 -0.2941 -0.4135 0.1972 557 ILE A N 4296 C CA . ILE A 557 ? 1.5239 1.3152 1.3678 -0.3105 -0.4183 0.2180 557 ILE A CA 4297 C C . ILE A 557 ? 1.5203 1.2963 1.3567 -0.3094 -0.4038 0.2097 557 ILE A C 4298 O O . ILE A 557 ? 1.5122 1.2513 1.3703 -0.2974 -0.3996 0.2121 557 ILE A O 4299 C CB . ILE A 557 ? 1.5495 1.3383 1.4107 -0.3150 -0.4366 0.2583 557 ILE A CB 4300 C CG1 . ILE A 557 ? 1.5613 1.3709 1.4269 -0.3185 -0.4520 0.2689 557 ILE A CG1 4301 C CG2 . ILE A 557 ? 1.5855 1.4001 1.4291 -0.3321 -0.4409 0.2832 557 ILE A CG2 4302 C CD1 . ILE A 557 ? 1.5361 1.3138 1.4334 -0.3013 -0.4549 0.2626 557 ILE A CD1 4303 N N . PHE A 558 ? 1.5249 1.3318 1.3315 -0.3215 -0.3962 0.1982 558 PHE A N 4304 C CA . PHE A 558 ? 1.5208 1.3162 1.3183 -0.3207 -0.3811 0.1863 558 PHE A CA 4305 C C . PHE A 558 ? 1.5761 1.3964 1.3555 -0.3369 -0.3849 0.2109 558 PHE A C 4306 O O . PHE A 558 ? 1.6863 1.5532 1.4401 -0.3522 -0.3885 0.2138 558 PHE A O 4307 C CB . PHE A 558 ? 1.4970 1.3046 1.2794 -0.3192 -0.3664 0.1473 558 PHE A CB 4308 C CG . PHE A 558 ? 1.4892 1.2852 1.2631 -0.3179 -0.3504 0.1329 558 PHE A CG 4309 C CD1 . PHE A 558 ? 1.4686 1.2224 1.2629 -0.3028 -0.3408 0.1248 558 PHE A CD1 4310 C CD2 . PHE A 558 ? 1.4985 1.3293 1.2444 -0.3317 -0.3450 0.1266 558 PHE A CD2 4311 C CE1 . PHE A 558 ? 1.4602 1.2042 1.2470 -0.3017 -0.3264 0.1119 558 PHE A CE1 4312 C CE2 . PHE A 558 ? 1.4957 1.3158 1.2348 -0.3305 -0.3304 0.1134 558 PHE A CE2 4313 C CZ . PHE A 558 ? 1.4823 1.2577 1.2419 -0.3155 -0.3213 0.1064 558 PHE A CZ 4314 N N . MET A 559 ? 1.5637 1.3553 1.3585 -0.3335 -0.3846 0.2284 559 MET A N 4315 C CA . MET A 559 ? 1.5878 1.3983 1.3719 -0.3481 -0.3884 0.2549 559 MET A CA 4316 C C . MET A 559 ? 1.5811 1.3808 1.3539 -0.3467 -0.3712 0.2368 559 MET A C 4317 O O . MET A 559 ? 1.5523 1.3124 1.3414 -0.3316 -0.3614 0.2195 559 MET A O 4318 C CB . MET A 559 ? 1.7131 1.5005 1.5293 -0.3469 -0.4041 0.2923 559 MET A CB 4319 C CG . MET A 559 ? 1.6927 1.4919 1.5073 -0.3604 -0.4083 0.3217 559 MET A CG 4320 S SD . MET A 559 ? 1.6215 1.3808 1.4867 -0.3544 -0.4248 0.3574 559 MET A SD 4321 C CE . MET A 559 ? 2.0490 1.8329 1.9068 -0.3738 -0.4282 0.3899 559 MET A CE 4322 N N . GLU A 560 ? 1.6042 1.4424 1.3493 -0.3625 -0.3677 0.2409 560 GLU A N 4323 C CA . GLU A 560 ? 1.6233 1.4552 1.3567 -0.3628 -0.3519 0.2255 560 GLU A CA 4324 C C . GLU A 560 ? 1.7064 1.5706 1.4259 -0.3809 -0.3565 0.2550 560 GLU A C 4325 O O . GLU A 560 ? 1.6819 1.5960 1.3822 -0.3966 -0.3649 0.2707 560 GLU A O 4326 C CB . GLU A 560 ? 1.6384 1.4879 1.3497 -0.3610 -0.3367 0.1837 560 GLU A CB 4327 C CG . GLU A 560 ? 1.9657 1.7976 1.6719 -0.3563 -0.3189 0.1615 560 GLU A CG 4328 C CD . GLU A 560 ? 2.0645 1.9083 1.7586 -0.3524 -0.3055 0.1194 560 GLU A CD 4329 O OE1 . GLU A 560 ? 1.9286 1.8124 1.6075 -0.3601 -0.3092 0.1080 560 GLU A OE1 4330 O OE2 . GLU A 560 ? 2.0437 1.8581 1.7462 -0.3415 -0.2921 0.0975 560 GLU A OE2 4331 N N . TYR A 561 ? 1.8524 1.6911 1.5823 -0.3790 -0.3513 0.2632 561 TYR A N 4332 C CA . TYR A 561 ? 1.8121 1.6790 1.5338 -0.3960 -0.3561 0.2942 561 TYR A CA 4333 C C . TYR A 561 ? 1.8252 1.7017 1.5247 -0.3996 -0.3384 0.2735 561 TYR A C 4334 O O . TYR A 561 ? 1.7419 1.5875 1.4429 -0.3862 -0.3236 0.2405 561 TYR A O 4335 C CB . TYR A 561 ? 1.6696 1.5029 1.4291 -0.3939 -0.3697 0.3302 561 TYR A CB 4336 C CG . TYR A 561 ? 1.6153 1.3884 1.4037 -0.3740 -0.3631 0.3125 561 TYR A CG 4337 C CD1 . TYR A 561 ? 1.6661 1.4195 1.4578 -0.3717 -0.3527 0.3062 561 TYR A CD1 4338 C CD2 . TYR A 561 ? 1.5923 1.3320 1.4053 -0.3575 -0.3675 0.3024 561 TYR A CD2 4339 C CE1 . TYR A 561 ? 1.8115 1.5153 1.6293 -0.3536 -0.3469 0.2892 561 TYR A CE1 4340 C CE2 . TYR A 561 ? 1.6904 1.3824 1.5293 -0.3394 -0.3614 0.2855 561 TYR A CE2 4341 C CZ . TYR A 561 ? 1.8821 1.5572 1.7231 -0.3375 -0.3512 0.2786 561 TYR A CZ 4342 O OH . TYR A 561 ? 2.0351 1.6678 1.9016 -0.3195 -0.3454 0.2609 561 TYR A OH 4343 N N . ARG A 562 ? 1.9429 1.8652 1.6230 -0.4181 -0.3405 0.2948 562 ARG A N 4344 C CA . ARG A 562 ? 2.0289 1.9747 1.6827 -0.4245 -0.3244 0.2752 562 ARG A CA 4345 C C . ARG A 562 ? 2.0862 2.0193 1.7513 -0.4302 -0.3240 0.3005 562 ARG A C 4346 O O . ARG A 562 ? 2.1861 2.0883 1.8541 -0.4215 -0.3104 0.2795 562 ARG A O 4347 C CB . ARG A 562 ? 2.1472 2.1664 1.7659 -0.4418 -0.3246 0.2735 562 ARG A CB 4348 C CG . ARG A 562 ? 2.1356 2.1822 1.7266 -0.4455 -0.3064 0.2404 562 ARG A CG 4349 C CD . ARG A 562 ? 2.0666 2.0848 1.6580 -0.4289 -0.2926 0.1899 562 ARG A CD 4350 N NE . ARG A 562 ? 2.0766 2.1116 1.6650 -0.4260 -0.2988 0.1740 562 ARG A NE 4351 C CZ . ARG A 562 ? 2.0332 2.0259 1.6444 -0.4116 -0.3038 0.1685 562 ARG A CZ 4352 N NH1 . ARG A 562 ? 2.0483 1.9817 1.6861 -0.3984 -0.3030 0.1762 562 ARG A NH1 4353 N NH2 . ARG A 562 ? 1.9707 1.9830 1.5787 -0.4104 -0.3097 0.1544 562 ARG A NH2 4354 N N . LEU A 563 ? 2.0204 1.9794 1.6937 -0.4454 -0.3397 0.3465 563 LEU A N 4355 C CA . LEU A 563 ? 1.9901 1.9482 1.6751 -0.4548 -0.3419 0.3765 563 LEU A CA 4356 C C . LEU A 563 ? 1.8657 1.8625 1.5166 -0.4647 -0.3256 0.3595 563 LEU A C 4357 O O . LEU A 563 ? 1.7282 1.6949 1.3796 -0.4562 -0.3112 0.3358 563 LEU A O 4358 C CB . LEU A 563 ? 1.9390 1.8272 1.6621 -0.4386 -0.3416 0.3742 563 LEU A CB 4359 C CG . LEU A 563 ? 1.7462 1.6246 1.4907 -0.4462 -0.3459 0.4044 563 LEU A CG 4360 C CD1 . LEU A 563 ? 1.7922 1.6956 1.5596 -0.4621 -0.3686 0.4598 563 LEU A CD1 4361 C CD2 . LEU A 563 ? 1.6377 1.4489 1.4165 -0.4273 -0.3426 0.3892 563 LEU A CD2 4362 N N . ASP A 564 ? 1.9568 2.0238 1.5776 -0.4821 -0.3276 0.3691 564 ASP A N 4363 C CA . ASP A 564 ? 1.8941 2.0090 1.4849 -0.4947 -0.3149 0.3610 564 ASP A CA 4364 C C . ASP A 564 ? 1.8996 1.9963 1.5111 -0.5006 -0.3175 0.3937 564 ASP A C 4365 O O . ASP A 564 ? 1.7369 1.8348 1.3738 -0.5093 -0.3352 0.4413 564 ASP A O 4366 C CB . ASP A 564 ? 1.8983 2.0993 1.4590 -0.5148 -0.3208 0.3769 564 ASP A CB 4367 C CG . ASP A 564 ? 2.0507 2.2709 1.5982 -0.5103 -0.3240 0.3532 564 ASP A CG 4368 O OD1 . ASP A 564 ? 2.1791 2.3526 1.7336 -0.4921 -0.3165 0.3147 564 ASP A OD1 4369 O OD2 . ASP A 564 ? 1.9946 2.2793 1.5256 -0.5255 -0.3342 0.3737 564 ASP A OD2 4370 N N . TYR A 565 ? 2.0762 2.1565 1.6809 -0.4962 -0.3011 0.3703 565 TYR A N 4371 C CA . TYR A 565 ? 1.9524 2.0086 1.5820 -0.5002 -0.3046 0.4003 565 TYR A CA 4372 C C . TYR A 565 ? 1.8585 1.9813 1.4693 -0.5228 -0.3049 0.4297 565 TYR A C 4373 O O . TYR A 565 ? 1.7712 1.9247 1.3527 -0.5268 -0.2885 0.4046 565 TYR A O 4374 C CB . TYR A 565 ? 1.9246 1.9247 1.5619 -0.4837 -0.2883 0.3650 565 TYR A CB 4375 C CG . TYR A 565 ? 1.9299 1.8793 1.5741 -0.4617 -0.2816 0.3245 565 TYR A CG 4376 C CD1 . TYR A 565 ? 2.1195 2.0179 1.7990 -0.4488 -0.2935 0.3342 565 TYR A CD1 4377 C CD2 . TYR A 565 ? 1.7866 1.7408 1.4054 -0.4537 -0.2637 0.2767 565 TYR A CD2 4378 C CE1 . TYR A 565 ? 2.2010 2.0580 1.8870 -0.4291 -0.2871 0.2989 565 TYR A CE1 4379 C CE2 . TYR A 565 ? 1.9270 1.8374 1.5552 -0.4344 -0.2582 0.2430 565 TYR A CE2 4380 C CZ . TYR A 565 ? 2.0684 1.9319 1.7286 -0.4224 -0.2695 0.2550 565 TYR A CZ 4381 O OH . TYR A 565 ? 2.0742 1.8994 1.7439 -0.4037 -0.2639 0.2236 565 TYR A OH 4382 N N . ARG A 566 ? 1.9199 2.0654 1.5508 -0.5377 -0.3239 0.4843 566 ARG A N 4383 C CA . ARG A 566 ? 1.8496 2.0433 1.4754 -0.5574 -0.3250 0.5188 566 ARG A CA 4384 C C . ARG A 566 ? 1.8273 1.9806 1.5042 -0.5596 -0.3421 0.5653 566 ARG A C 4385 O O . ARG A 566 ? 1.6639 1.8225 1.3686 -0.5667 -0.3630 0.6080 566 ARG A O 4386 C CB . ARG A 566 ? 1.8608 2.1467 1.4568 -0.5789 -0.3313 0.5435 566 ARG A CB 4387 C CG . ARG A 566 ? 1.9064 2.2446 1.4521 -0.5794 -0.3129 0.4949 566 ARG A CG 4388 C CD . ARG A 566 ? 1.9258 2.2623 1.4552 -0.5772 -0.2923 0.4644 566 ARG A CD 4389 N NE . ARG A 566 ? 2.0405 2.4176 1.5295 -0.5744 -0.2750 0.4115 566 ARG A NE 4390 C CZ . ARG A 566 ? 1.8769 2.2115 1.3623 -0.5552 -0.2644 0.3595 566 ARG A CZ 4391 N NH1 . ARG A 566 ? 1.9676 2.2220 1.4833 -0.5377 -0.2685 0.3549 566 ARG A NH1 4392 N NH2 . ARG A 566 ? 1.6812 2.0554 1.1361 -0.5536 -0.2505 0.3128 566 ARG A NH2 4393 N N . THR A 567 ? 1.9579 2.0707 1.6496 -0.5531 -0.3333 0.5555 567 THR A N 4394 C CA . THR A 567 ? 1.9716 2.0537 1.7116 -0.5574 -0.3473 0.5969 567 THR A CA 4395 C C . THR A 567 ? 1.8130 1.8947 1.5426 -0.5596 -0.3314 0.5838 567 THR A C 4396 O O . THR A 567 ? 1.8825 1.9451 1.5863 -0.5468 -0.3109 0.5335 567 THR A O 4397 C CB . THR A 567 ? 1.7072 1.7071 1.4962 -0.5372 -0.3577 0.5907 567 THR A CB 4398 O OG1 . THR A 567 ? 1.7413 1.6898 1.5474 -0.5253 -0.3477 0.5688 567 THR A OG1 4399 C CG2 . THR A 567 ? 1.6201 1.5959 1.3950 -0.5198 -0.3531 0.5515 567 THR A CG2 4400 N N . ALA A 568 ? 1.8745 1.9784 1.6268 -0.5764 -0.3414 0.6306 568 ALA A N 4401 C CA . ALA A 568 ? 1.8512 1.9658 1.5933 -0.5822 -0.3279 0.6256 568 ALA A CA 4402 C C . ALA A 568 ? 1.6556 1.7205 1.4552 -0.5812 -0.3412 0.6564 568 ALA A C 4403 O O . ALA A 568 ? 1.5485 1.5575 1.3615 -0.5660 -0.3317 0.6264 568 ALA A O 4404 C CB . ALA A 568 ? 1.8365 2.0457 1.5431 -0.6072 -0.3249 0.6523 568 ALA A CB 4405 N N . ALA A 569 ? 1.7570 1.8429 1.5941 -0.5968 -0.3646 0.7159 569 ALA A N 4406 C CA . ALA A 569 ? 2.0119 2.0836 1.9020 -0.6065 -0.3798 0.7615 569 ALA A CA 4407 C C . ALA A 569 ? 2.1626 2.2901 2.0229 -0.6236 -0.3667 0.7714 569 ALA A C 4408 O O . ALA A 569 ? 2.0416 2.1574 1.9357 -0.6261 -0.3697 0.7879 569 ALA A O 4409 C CB . ALA A 569 ? 1.9455 1.9279 1.8827 -0.5851 -0.3820 0.7376 569 ALA A CB 4410 N N . ASP A 570 ? 2.2658 2.4596 2.0665 -0.6319 -0.3522 0.7548 570 ASP A N 4411 C CA . ASP A 570 ? 2.2538 2.5138 2.0150 -0.6474 -0.3367 0.7553 570 ASP A CA 4412 C C . ASP A 570 ? 2.1328 2.3516 1.8832 -0.6342 -0.3156 0.7095 570 ASP A C 4413 O O . ASP A 570 ? 2.1974 2.4645 1.9136 -0.6438 -0.2999 0.7001 570 ASP A O 4414 C CB . ASP A 570 ? 2.2096 2.5271 2.0039 -0.6669 -0.3520 0.8145 570 ASP A CB 4415 C CG . ASP A 570 ? 2.1762 2.5924 1.9230 -0.6843 -0.3390 0.8167 570 ASP A CG 4416 O OD1 . ASP A 570 ? 2.2889 2.7319 1.9725 -0.6863 -0.3222 0.7826 570 ASP A OD1 4417 O OD2 . ASP A 570 ? 1.9583 2.4267 1.7317 -0.6950 -0.3456 0.8492 570 ASP A OD2 4418 N N . THR A 571 ? 2.0422 2.1756 1.8205 -0.6120 -0.3147 0.6793 571 THR A N 4419 C CA . THR A 571 ? 2.1270 2.2230 1.8958 -0.5997 -0.2952 0.6372 571 THR A CA 4420 C C . THR A 571 ? 1.8776 1.9895 1.5903 -0.5896 -0.2722 0.5793 571 THR A C 4421 O O . THR A 571 ? 1.6622 1.7354 1.3703 -0.5718 -0.2695 0.5443 571 THR A O 4422 C CB . THR A 571 ? 2.1853 2.1918 2.0027 -0.5797 -0.3018 0.6235 571 THR A CB 4423 O OG1 . THR A 571 ? 2.2338 2.2297 2.1050 -0.5904 -0.3203 0.6730 571 THR A OG1 4424 C CG2 . THR A 571 ? 2.1042 2.0706 1.9030 -0.5625 -0.2793 0.5682 571 THR A CG2 4425 N N . THR A 572 ? 1.8952 2.0635 1.5698 -0.6009 -0.2562 0.5693 572 THR A N 4426 C CA . THR A 572 ? 2.0031 2.2014 1.6270 -0.5952 -0.2359 0.5182 572 THR A CA 4427 C C . THR A 572 ? 2.0418 2.2584 1.6547 -0.5940 -0.2452 0.5182 572 THR A C 4428 O O . THR A 572 ? 1.8820 2.1581 1.4906 -0.6116 -0.2577 0.5580 572 THR A O 4429 C CB . THR A 572 ? 2.3030 2.4380 1.9223 -0.5726 -0.2177 0.4603 572 THR A CB 4430 O OG1 . THR A 572 ? 2.3296 2.4311 1.9733 -0.5718 -0.2151 0.4687 572 THR A OG1 4431 C CG2 . THR A 572 ? 2.2407 2.4188 1.8121 -0.5714 -0.1964 0.4131 572 THR A CG2 4432 N N . GLY A 573 ? 2.0316 2.1972 1.6420 -0.5732 -0.2395 0.4749 573 GLY A N 4433 C CA . GLY A 573 ? 1.9305 2.0795 1.5531 -0.5671 -0.2539 0.4824 573 GLY A CA 4434 C C . GLY A 573 ? 1.7973 1.8625 1.4392 -0.5421 -0.2485 0.4443 573 GLY A C 4435 O O . GLY A 573 ? 1.8221 1.8679 1.4481 -0.5313 -0.2301 0.4018 573 GLY A O 4436 N N . LEU A 574 ? 1.7235 1.7426 1.3998 -0.5327 -0.2643 0.4585 574 LEU A N 4437 C CA . LEU A 574 ? 1.7012 1.6470 1.3957 -0.5085 -0.2597 0.4223 574 LEU A CA 4438 C C . LEU A 574 ? 1.7043 1.6350 1.4089 -0.5004 -0.2718 0.4231 574 LEU A C 4439 O O . LEU A 574 ? 1.8148 1.7447 1.5492 -0.5067 -0.2920 0.4636 574 LEU A O 4440 C CB . LEU A 574 ? 1.5762 1.4656 1.3158 -0.5015 -0.2662 0.4354 574 LEU A CB 4441 C CG . LEU A 574 ? 1.4745 1.2988 1.2251 -0.4778 -0.2547 0.3911 574 LEU A CG 4442 C CD1 . LEU A 574 ? 1.4755 1.3108 1.1915 -0.4756 -0.2313 0.3536 574 LEU A CD1 4443 C CD2 . LEU A 574 ? 1.4356 1.2097 1.2375 -0.4715 -0.2666 0.4088 574 LEU A CD2 4444 N N . GLN A 575 ? 1.5838 1.5037 1.2660 -0.4867 -0.2602 0.3794 575 GLN A N 4445 C CA . GLN A 575 ? 1.6158 1.5254 1.3041 -0.4790 -0.2703 0.3774 575 GLN A CA 4446 C C . GLN A 575 ? 1.6098 1.4481 1.3308 -0.4569 -0.2721 0.3587 575 GLN A C 4447 O O . GLN A 575 ? 1.8816 1.6885 1.5974 -0.4427 -0.2568 0.3207 575 GLN A O 4448 C CB . GLN A 575 ? 1.9474 1.8934 1.5950 -0.4782 -0.2585 0.3425 575 GLN A CB 4449 C CG . GLN A 575 ? 1.9633 1.9712 1.5734 -0.4930 -0.2458 0.3344 575 GLN A CG 4450 C CD . GLN A 575 ? 1.9210 1.9613 1.4971 -0.4900 -0.2344 0.2931 575 GLN A CD 4451 O OE1 . GLN A 575 ? 2.0062 2.0216 1.5865 -0.4771 -0.2360 0.2719 575 GLN A OE1 4452 N NE2 . GLN A 575 ? 1.8723 1.9701 1.4172 -0.5018 -0.2233 0.2806 575 GLN A NE2 4453 N N . PRO A 576 ? 1.5173 1.3324 1.2740 -0.4539 -0.2913 0.3854 576 PRO A N 4454 C CA . PRO A 576 ? 1.4875 1.2410 1.2756 -0.4323 -0.2936 0.3656 576 PRO A CA 4455 C C . PRO A 576 ? 1.5228 1.2697 1.2891 -0.4186 -0.2836 0.3267 576 PRO A C 4456 O O . PRO A 576 ? 1.6083 1.3948 1.3475 -0.4265 -0.2838 0.3263 576 PRO A O 4457 C CB . PRO A 576 ? 1.4670 1.2094 1.2978 -0.4355 -0.3182 0.4065 576 PRO A CB 4458 C CG . PRO A 576 ? 1.4930 1.2952 1.3028 -0.4561 -0.3269 0.4390 576 PRO A CG 4459 C CD . PRO A 576 ? 1.5140 1.3605 1.2864 -0.4701 -0.3123 0.4353 576 PRO A CD 4460 N N . ILE A 577 ? 1.4688 1.1692 1.2482 -0.3988 -0.2753 0.2948 577 ILE A N 4461 C CA . ILE A 577 ? 1.5146 1.2057 1.2809 -0.3851 -0.2674 0.2612 577 ILE A CA 4462 C C . ILE A 577 ? 1.5515 1.2053 1.3540 -0.3708 -0.2806 0.2659 577 ILE A C 4463 O O . ILE A 577 ? 1.5479 1.1705 1.3872 -0.3652 -0.2898 0.2790 577 ILE A O 4464 C CB . ILE A 577 ? 1.5853 1.2593 1.3366 -0.3733 -0.2463 0.2195 577 ILE A CB 4465 C CG1 . ILE A 577 ? 1.8625 1.5375 1.5985 -0.3629 -0.2383 0.1878 577 ILE A CG1 4466 C CG2 . ILE A 577 ? 1.5619 1.1886 1.3447 -0.3592 -0.2451 0.2125 577 ILE A CG2 4467 C CD1 . ILE A 577 ? 1.7520 1.4750 1.4590 -0.3758 -0.2399 0.1900 577 ILE A CD1 4468 N N . LEU A 578 ? 1.4829 1.1418 1.2773 -0.3650 -0.2821 0.2543 578 LEU A N 4469 C CA . LEU A 578 ? 1.4576 1.0854 1.2844 -0.3511 -0.2937 0.2563 578 LEU A CA 4470 C C . LEU A 578 ? 1.4722 1.0577 1.3179 -0.3309 -0.2843 0.2272 578 LEU A C 4471 O O . LEU A 578 ? 1.4759 1.0587 1.3039 -0.3273 -0.2673 0.2021 578 LEU A O 4472 C CB . LEU A 578 ? 1.4538 1.0991 1.2649 -0.3495 -0.2958 0.2481 578 LEU A CB 4473 C CG . LEU A 578 ? 1.5010 1.1904 1.2966 -0.3677 -0.3079 0.2768 578 LEU A CG 4474 C CD1 . LEU A 578 ? 1.5986 1.3343 1.3521 -0.3825 -0.2962 0.2689 578 LEU A CD1 4475 C CD2 . LEU A 578 ? 1.5872 1.2781 1.3857 -0.3614 -0.3157 0.2730 578 LEU A CD2 4476 N N . ASN A 579 ? 1.5022 1.0580 1.3854 -0.3179 -0.2956 0.2308 579 ASN A N 4477 C CA . ASN A 579 ? 1.3806 0.9021 1.2842 -0.2980 -0.2881 0.2033 579 ASN A CA 4478 C C . ASN A 579 ? 1.3948 0.9202 1.2710 -0.2890 -0.2698 0.1688 579 ASN A C 4479 O O . ASN A 579 ? 1.4297 0.9730 1.2875 -0.2912 -0.2691 0.1648 579 ASN A O 4480 C CB . ASN A 579 ? 1.6718 1.1699 1.6176 -0.2853 -0.3038 0.2096 579 ASN A CB 4481 C CG . ASN A 579 ? 1.7882 1.2558 1.7613 -0.2656 -0.2986 0.1843 579 ASN A CG 4482 O OD1 . ASN A 579 ? 1.7451 1.2099 1.7010 -0.2560 -0.2817 0.1552 579 ASN A OD1 4483 N ND2 . ASN A 579 ? 1.7709 1.2179 1.7896 -0.2595 -0.3139 0.1953 579 ASN A ND2 4484 N N . GLN A 580 ? 1.6185 1.1284 1.4947 -0.2794 -0.2559 0.1451 580 GLN A N 4485 C CA . GLN A 580 ? 1.5576 1.0711 1.4125 -0.2716 -0.2383 0.1144 580 GLN A CA 4486 C C . GLN A 580 ? 1.5316 1.0443 1.3919 -0.2609 -0.2405 0.1043 580 GLN A C 4487 O O . GLN A 580 ? 1.4134 0.9458 1.2517 -0.2659 -0.2365 0.0979 580 GLN A O 4488 C CB . GLN A 580 ? 1.5740 1.0673 1.4392 -0.2597 -0.2267 0.0939 580 GLN A CB 4489 C CG . GLN A 580 ? 1.6232 1.1221 1.4693 -0.2535 -0.2088 0.0657 580 GLN A CG 4490 C CD . GLN A 580 ? 1.7745 1.2565 1.6320 -0.2417 -0.1982 0.0476 580 GLN A CD 4491 O OE1 . GLN A 580 ? 1.7127 1.1778 1.5939 -0.2365 -0.2046 0.0527 580 GLN A OE1 4492 N NE2 . GLN A 580 ? 1.6847 1.1726 1.5282 -0.2376 -0.1829 0.0261 580 GLN A NE2 4493 N N . PHE A 581 ? 1.7485 1.2403 1.6400 -0.2460 -0.2471 0.1018 581 PHE A N 4494 C CA . PHE A 581 ? 1.8752 1.3671 1.7755 -0.2358 -0.2507 0.0953 581 PHE A CA 4495 C C . PHE A 581 ? 1.9296 1.4246 1.8438 -0.2417 -0.2698 0.1212 581 PHE A C 4496 O O . PHE A 581 ? 2.1200 1.5997 2.0652 -0.2383 -0.2827 0.1349 581 PHE A O 4497 C CB . PHE A 581 ? 1.8781 1.3522 1.8045 -0.2158 -0.2468 0.0766 581 PHE A CB 4498 C CG . PHE A 581 ? 1.8599 1.3352 1.7736 -0.2092 -0.2283 0.0521 581 PHE A CG 4499 C CD1 . PHE A 581 ? 1.8576 1.3222 1.7779 -0.2055 -0.2217 0.0439 581 PHE A CD1 4500 C CD2 . PHE A 581 ? 1.6343 1.1223 1.5325 -0.2071 -0.2183 0.0383 581 PHE A CD2 4501 C CE1 . PHE A 581 ? 1.6640 1.1316 1.5737 -0.2000 -0.2052 0.0233 581 PHE A CE1 4502 C CE2 . PHE A 581 ? 1.7556 1.2458 1.6466 -0.2017 -0.2025 0.0185 581 PHE A CE2 4503 C CZ . PHE A 581 ? 1.7039 1.1844 1.5996 -0.1982 -0.1957 0.0115 581 PHE A CZ 4504 N N . THR A 582 ? 1.6433 1.1590 1.5373 -0.2503 -0.2722 0.1267 582 THR A N 4505 C CA . THR A 582 ? 1.6194 1.1444 1.5209 -0.2585 -0.2899 0.1529 582 THR A CA 4506 C C . THR A 582 ? 1.7471 1.2985 1.6210 -0.2661 -0.2878 0.1492 582 THR A C 4507 O O . THR A 582 ? 1.8338 1.4041 1.6783 -0.2746 -0.2765 0.1379 582 THR A O 4508 C CB . THR A 582 ? 1.7263 1.2584 1.6301 -0.2745 -0.3005 0.1826 582 THR A CB 4509 O OG1 . THR A 582 ? 1.7266 1.2322 1.6678 -0.2665 -0.3082 0.1893 582 THR A OG1 4510 C CG2 . THR A 582 ? 1.6955 1.2488 1.5977 -0.2872 -0.3169 0.2113 582 THR A CG2 4511 N N . PRO A 583 ? 1.7290 1.2826 1.6144 -0.2628 -0.2991 0.1571 583 PRO A N 4512 C CA . PRO A 583 ? 1.5954 1.1749 1.4579 -0.2699 -0.2989 0.1532 583 PRO A CA 4513 C C . PRO A 583 ? 1.6077 1.2189 1.4472 -0.2904 -0.3062 0.1745 583 PRO A C 4514 O O . PRO A 583 ? 1.6167 1.2290 1.4687 -0.2983 -0.3195 0.2035 583 PRO A O 4515 C CB . PRO A 583 ? 1.7759 1.3463 1.6624 -0.2600 -0.3108 0.1591 583 PRO A CB 4516 C CG . PRO A 583 ? 1.8417 1.3903 1.7616 -0.2552 -0.3230 0.1777 583 PRO A CG 4517 C CD . PRO A 583 ? 1.7170 1.2498 1.6399 -0.2510 -0.3122 0.1667 583 PRO A CD 4518 N N . ALA A 584 ? 1.7580 1.3978 1.5672 -0.2989 -0.2979 0.1601 584 ALA A N 4519 C CA . ALA A 584 ? 1.7667 1.4461 1.5516 -0.3182 -0.3042 0.1771 584 ALA A CA 4520 C C . ALA A 584 ? 1.6704 1.3682 1.4556 -0.3214 -0.3174 0.1874 584 ALA A C 4521 O O . ALA A 584 ? 1.5882 1.3238 1.3550 -0.3371 -0.3252 0.2035 584 ALA A O 4522 C CB . ALA A 584 ? 1.9900 1.6955 1.7438 -0.3257 -0.2893 0.1533 584 ALA A CB 4523 N N . ASN A 585 ? 1.7575 1.4314 1.5640 -0.3066 -0.3199 0.1784 585 ASN A N 4524 C CA . ASN A 585 ? 1.5696 1.2575 1.3793 -0.3076 -0.3318 0.1855 585 ASN A CA 4525 C C . ASN A 585 ? 1.4856 1.1410 1.3293 -0.2916 -0.3394 0.1893 585 ASN A C 4526 O O . ASN A 585 ? 1.4417 1.0670 1.3035 -0.2770 -0.3315 0.1757 585 ASN A O 4527 C CB . ASN A 585 ? 1.5742 1.2847 1.3631 -0.3086 -0.3232 0.1569 585 ASN A CB 4528 C CG . ASN A 585 ? 1.8181 1.5029 1.6176 -0.2927 -0.3089 0.1263 585 ASN A CG 4529 O OD1 . ASN A 585 ? 1.7661 1.4297 1.5883 -0.2793 -0.3114 0.1227 585 ASN A OD1 4530 N ND2 . ASN A 585 ? 2.4080 2.0976 2.1927 -0.2944 -0.2941 0.1050 585 ASN A ND2 4531 N N . ILE A 586 ? 1.4925 1.1578 1.3452 -0.2944 -0.3548 0.2074 586 ILE A N 4532 C CA . ILE A 586 ? 1.4719 1.1119 1.3569 -0.2797 -0.3628 0.2101 586 ILE A CA 4533 C C . ILE A 586 ? 1.4884 1.1480 1.3684 -0.2818 -0.3706 0.2096 586 ILE A C 4534 O O . ILE A 586 ? 1.5150 1.2088 1.3723 -0.2969 -0.3762 0.2188 586 ILE A O 4535 C CB . ILE A 586 ? 1.5577 1.1810 1.4736 -0.2795 -0.3785 0.2403 586 ILE A CB 4536 C CG1 . ILE A 586 ? 1.7401 1.3341 1.6932 -0.2607 -0.3833 0.2350 586 ILE A CG1 4537 C CG2 . ILE A 586 ? 1.4980 1.1497 1.4089 -0.2967 -0.3959 0.2737 586 ILE A CG2 4538 C CD1 . ILE A 586 ? 1.7717 1.3429 1.7320 -0.2438 -0.3669 0.2051 586 ILE A CD1 4539 N N . SER A 587 ? 1.4714 1.1127 1.3727 -0.2667 -0.3709 0.1984 587 SER A N 4540 C CA . SER A 587 ? 1.4811 1.1389 1.3799 -0.2673 -0.3772 0.1950 587 SER A CA 4541 C C . SER A 587 ? 1.4737 1.1151 1.4049 -0.2568 -0.3903 0.2083 587 SER A C 4542 O O . SER A 587 ? 1.4432 1.0570 1.4015 -0.2423 -0.3885 0.2052 587 SER A O 4543 C CB . SER A 587 ? 1.5863 1.2462 1.4761 -0.2605 -0.3624 0.1621 587 SER A CB 4544 O OG . SER A 587 ? 1.8688 1.5487 1.7298 -0.2712 -0.3520 0.1481 587 SER A OG 4545 N N . ARG A 588 ? 1.5890 1.2504 1.5179 -0.2642 -0.4036 0.2220 588 ARG A N 4546 C CA . ARG A 588 ? 1.4913 1.1413 1.4497 -0.2548 -0.4162 0.2327 588 ARG A CA 4547 C C . ARG A 588 ? 1.4865 1.1552 1.4358 -0.2554 -0.4174 0.2205 588 ARG A C 4548 O O . ARG A 588 ? 1.4895 1.1848 1.4105 -0.2664 -0.4132 0.2098 588 ARG A O 4549 C CB . ARG A 588 ? 1.5224 1.1766 1.4957 -0.2636 -0.4358 0.2687 588 ARG A CB 4550 C CG . ARG A 588 ? 1.5766 1.2055 1.5751 -0.2591 -0.4386 0.2816 588 ARG A CG 4551 C CD . ARG A 588 ? 1.7425 1.3396 1.7777 -0.2379 -0.4367 0.2684 588 ARG A CD 4552 N NE . ARG A 588 ? 1.8515 1.4256 1.9155 -0.2327 -0.4408 0.2776 588 ARG A NE 4553 C CZ . ARG A 588 ? 1.8349 1.3936 1.8981 -0.2258 -0.4271 0.2599 588 ARG A CZ 4554 N NH1 . ARG A 588 ? 1.6884 1.2518 1.7234 -0.2235 -0.4084 0.2339 588 ARG A NH1 4555 N NH2 . ARG A 588 ? 1.9189 1.4578 2.0124 -0.2213 -0.4331 0.2682 588 ARG A NH2 4556 N N . GLN A 589 ? 1.5192 1.1756 1.4946 -0.2434 -0.4234 0.2207 589 GLN A N 4557 C CA . GLN A 589 ? 1.4649 1.1365 1.4369 -0.2427 -0.4250 0.2089 589 GLN A CA 4558 C C . GLN A 589 ? 1.4805 1.1580 1.4696 -0.2437 -0.4435 0.2304 589 GLN A C 4559 O O . GLN A 589 ? 1.4868 1.1454 1.5047 -0.2356 -0.4522 0.2462 589 GLN A O 4560 C CB . GLN A 589 ? 1.4255 1.0805 1.4125 -0.2263 -0.4116 0.1837 589 GLN A CB 4561 C CG . GLN A 589 ? 1.4112 1.0667 1.3805 -0.2268 -0.3937 0.1597 589 GLN A CG 4562 C CD . GLN A 589 ? 1.4245 1.0693 1.4110 -0.2123 -0.3822 0.1387 589 GLN A CD 4563 O OE1 . GLN A 589 ? 1.3652 1.0023 1.3766 -0.2011 -0.3866 0.1419 589 GLN A OE1 4564 N NE2 . GLN A 589 ? 1.5760 1.2227 1.5512 -0.2128 -0.3676 0.1182 589 GLN A NE2 4565 N N . ALA A 590 ? 1.4809 1.1862 1.4541 -0.2536 -0.4500 0.2294 590 ALA A N 4566 C CA . ALA A 590 ? 1.4868 1.2010 1.4745 -0.2549 -0.4671 0.2473 590 ALA A CA 4567 C C . ALA A 590 ? 1.4674 1.1833 1.4637 -0.2463 -0.4641 0.2267 590 ALA A C 4568 O O . ALA A 590 ? 1.4513 1.1747 1.4342 -0.2464 -0.4521 0.2011 590 ALA A O 4569 C CB . ALA A 590 ? 1.5037 1.2542 1.4680 -0.2745 -0.4798 0.2668 590 ALA A CB 4570 N N . HIS A 591 ? 1.4735 1.1826 1.4955 -0.2389 -0.4754 0.2381 591 HIS A N 4571 C CA . HIS A 591 ? 1.4440 1.1545 1.4787 -0.2305 -0.4738 0.2218 591 HIS A CA 4572 C C . HIS A 591 ? 1.4488 1.1793 1.4870 -0.2373 -0.4914 0.2363 591 HIS A C 4573 O O . HIS A 591 ? 1.4620 1.1906 1.5130 -0.2392 -0.5057 0.2624 591 HIS A O 4574 C CB . HIS A 591 ? 1.4283 1.1109 1.4956 -0.2110 -0.4675 0.2165 591 HIS A CB 4575 C CG . HIS A 591 ? 1.4860 1.1526 1.5513 -0.2031 -0.4496 0.1995 591 HIS A CG 4576 N ND1 . HIS A 591 ? 1.7738 1.4279 1.8345 -0.2041 -0.4463 0.2066 591 HIS A ND1 4577 C CD2 . HIS A 591 ? 1.4419 1.1041 1.5112 -0.1944 -0.4347 0.1770 591 HIS A CD2 4578 C CE1 . HIS A 591 ? 1.7173 1.3602 1.7770 -0.1961 -0.4297 0.1878 591 HIS A CE1 4579 N NE2 . HIS A 591 ? 1.5103 1.1585 1.5752 -0.1903 -0.4225 0.1705 591 HIS A NE2 4580 N N . ILE A 592 ? 1.4434 1.1934 1.4732 -0.2411 -0.4910 0.2191 592 ILE A N 4581 C CA . ILE A 592 ? 1.4465 1.2165 1.4811 -0.2464 -0.5070 0.2289 592 ILE A CA 4582 C C . ILE A 592 ? 1.4344 1.1836 1.5051 -0.2309 -0.5109 0.2337 592 ILE A C 4583 O O . ILE A 592 ? 1.4837 1.2147 1.5711 -0.2175 -0.4988 0.2177 592 ILE A O 4584 C CB . ILE A 592 ? 1.4384 1.2369 1.4565 -0.2546 -0.5057 0.2051 592 ILE A CB 4585 C CG1 . ILE A 592 ? 1.4464 1.2677 1.4301 -0.2681 -0.4991 0.1948 592 ILE A CG1 4586 C CG2 . ILE A 592 ? 1.4771 1.3002 1.4978 -0.2615 -0.5234 0.2158 592 ILE A CG2 4587 C CD1 . ILE A 592 ? 1.4372 1.2902 1.4070 -0.2762 -0.4985 0.1673 592 ILE A CD1 4588 N N . LEU A 593 ? 1.4394 1.1940 1.5229 -0.2330 -0.5279 0.2567 593 LEU A N 4589 C CA . LEU A 593 ? 1.4294 1.1664 1.5486 -0.2183 -0.5328 0.2627 593 LEU A CA 4590 C C . LEU A 593 ? 1.4108 1.1551 1.5393 -0.2132 -0.5297 0.2431 593 LEU A C 4591 O O . LEU A 593 ? 1.5087 1.2772 1.6258 -0.2234 -0.5379 0.2396 593 LEU A O 4592 C CB . LEU A 593 ? 1.4380 1.1806 1.5702 -0.2230 -0.5531 0.2929 593 LEU A CB 4593 C CG . LEU A 593 ? 1.4301 1.1521 1.6029 -0.2081 -0.5604 0.3051 593 LEU A CG 4594 C CD1 . LEU A 593 ? 1.4345 1.1596 1.6187 -0.2154 -0.5798 0.3378 593 LEU A CD1 4595 C CD2 . LEU A 593 ? 1.6406 1.3675 1.8306 -0.2005 -0.5626 0.2956 593 LEU A CD2 4596 N N . LEU A 594 ? 1.3863 1.1124 1.5376 -0.1977 -0.5182 0.2306 594 LEU A N 4597 C CA . LEU A 594 ? 1.3628 1.0946 1.5303 -0.1918 -0.5155 0.2153 594 LEU A CA 4598 C C . LEU A 594 ? 1.3522 1.0684 1.5552 -0.1740 -0.5123 0.2185 594 LEU A C 4599 O O . LEU A 594 ? 1.3480 1.0488 1.5590 -0.1635 -0.5009 0.2152 594 LEU A O 4600 C CB . LEU A 594 ? 1.3490 1.0851 1.5038 -0.1942 -0.5008 0.1899 594 LEU A CB 4601 C CG . LEU A 594 ? 1.3427 1.0872 1.5167 -0.1909 -0.4991 0.1736 594 LEU A CG 4602 C CD1 . LEU A 594 ? 1.5061 1.2726 1.6772 -0.2011 -0.5152 0.1751 594 LEU A CD1 4603 C CD2 . LEU A 594 ? 1.3195 1.0654 1.4863 -0.1928 -0.4848 0.1499 594 LEU A CD2 4604 N N . ASP A 595 ? 1.3731 1.0965 1.5971 -0.1706 -0.5224 0.2241 595 ASP A N 4605 C CA . ASP A 595 ? 1.4454 1.1609 1.7045 -0.1541 -0.5203 0.2268 595 ASP A CA 4606 C C . ASP A 595 ? 1.4563 1.1556 1.7294 -0.1432 -0.5193 0.2371 595 ASP A C 4607 O O . ASP A 595 ? 1.3859 1.0787 1.6765 -0.1293 -0.5075 0.2290 595 ASP A O 4608 C CB . ASP A 595 ? 1.4287 1.1456 1.6993 -0.1463 -0.5048 0.2087 595 ASP A CB 4609 C CG . ASP A 595 ? 1.5369 1.2692 1.8078 -0.1543 -0.5079 0.1978 595 ASP A CG 4610 O OD1 . ASP A 595 ? 1.4570 1.1933 1.7105 -0.1622 -0.5007 0.1822 595 ASP A OD1 4611 O OD2 . ASP A 595 ? 1.4267 1.1673 1.7177 -0.1526 -0.5183 0.2039 595 ASP A OD2 4612 N N . CYS A 596 ? 1.4873 1.1827 1.7554 -0.1497 -0.5323 0.2547 596 CYS A N 4613 C CA . CYS A 596 ? 1.6891 1.3685 1.9766 -0.1399 -0.5342 0.2641 596 CYS A CA 4614 C C . CYS A 596 ? 1.7305 1.4093 2.0537 -0.1301 -0.5472 0.2766 596 CYS A C 4615 O O . CYS A 596 ? 1.8437 1.5108 2.1908 -0.1210 -0.5516 0.2835 596 CYS A O 4616 C CB . CYS A 596 ? 1.8754 1.5497 2.1438 -0.1522 -0.5415 0.2782 596 CYS A CB 4617 S SG . CYS A 596 ? 2.6951 2.3640 2.9309 -0.1578 -0.5237 0.2628 596 CYS A SG 4618 N N . GLY A 597 ? 1.6716 1.3636 2.0012 -0.1318 -0.5538 0.2783 597 GLY A N 4619 C CA . GLY A 597 ? 1.6924 1.3859 2.0565 -0.1222 -0.5652 0.2888 597 GLY A CA 4620 C C . GLY A 597 ? 1.5487 1.2432 1.9172 -0.1316 -0.5864 0.3127 597 GLY A C 4621 O O . GLY A 597 ? 1.4692 1.1680 1.8111 -0.1474 -0.5930 0.3228 597 GLY A O 4622 N N . GLU A 598 ? 1.5058 1.1992 1.9094 -0.1220 -0.5974 0.3226 598 GLU A N 4623 C CA . GLU A 598 ? 1.5195 1.2149 1.9344 -0.1298 -0.6190 0.3476 598 GLU A CA 4624 C C . GLU A 598 ? 1.6214 1.3029 2.0431 -0.1326 -0.6264 0.3623 598 GLU A C 4625 O O . GLU A 598 ? 1.7855 1.4708 2.2081 -0.1444 -0.6441 0.3866 598 GLU A O 4626 C CB . GLU A 598 ? 1.5389 1.2364 1.9940 -0.1173 -0.6281 0.3526 598 GLU A CB 4627 C CG . GLU A 598 ? 1.8386 1.5500 2.2942 -0.1133 -0.6214 0.3399 598 GLU A CG 4628 C CD . GLU A 598 ? 1.9109 1.6264 2.4067 -0.1010 -0.6305 0.3459 598 GLU A CD 4629 O OE1 . GLU A 598 ? 1.8878 1.6143 2.3923 -0.0945 -0.6236 0.3356 598 GLU A OE1 4630 O OE2 . GLU A 598 ? 1.7933 1.5017 2.3148 -0.0981 -0.6450 0.3616 598 GLU A OE2 4631 N N . ASP A 599 ? 1.6179 1.2848 2.0465 -0.1221 -0.6135 0.3483 599 ASP A N 4632 C CA . ASP A 599 ? 1.3890 1.0409 1.8297 -0.1232 -0.6198 0.3597 599 ASP A CA 4633 C C . ASP A 599 ? 1.4076 1.0628 1.8079 -0.1419 -0.6185 0.3680 599 ASP A C 4634 O O . ASP A 599 ? 1.3588 1.0047 1.7663 -0.1471 -0.6262 0.3831 599 ASP A O 4635 C CB . ASP A 599 ? 1.4216 1.0595 1.8854 -0.1047 -0.6065 0.3389 599 ASP A CB 4636 C CG . ASP A 599 ? 1.7508 1.3935 2.1876 -0.1004 -0.5832 0.3132 599 ASP A CG 4637 O OD1 . ASP A 599 ? 1.6621 1.3132 2.0599 -0.1138 -0.5772 0.3115 599 ASP A OD1 4638 O OD2 . ASP A 599 ? 1.8848 1.5254 2.3411 -0.0835 -0.5714 0.2943 599 ASP A OD2 4639 N N . ASN A 600 ? 1.7168 1.3869 2.0779 -0.1516 -0.6092 0.3576 600 ASN A N 4640 C CA . ASN A 600 ? 1.7037 1.3820 2.0235 -0.1684 -0.6048 0.3595 600 ASN A CA 4641 C C . ASN A 600 ? 1.6657 1.3271 1.9814 -0.1639 -0.5919 0.3496 600 ASN A C 4642 O O . ASN A 600 ? 1.6892 1.3531 1.9834 -0.1769 -0.5934 0.3599 600 ASN A O 4643 C CB . ASN A 600 ? 1.5929 1.2855 1.9054 -0.1861 -0.6249 0.3903 600 ASN A CB 4644 C CG . ASN A 600 ? 1.6936 1.4109 1.9932 -0.1957 -0.6348 0.3961 600 ASN A CG 4645 O OD1 . ASN A 600 ? 1.6957 1.4230 1.9775 -0.1950 -0.6247 0.3747 600 ASN A OD1 4646 N ND2 . ASN A 600 ? 1.7274 1.4559 2.0390 -0.2049 -0.6557 0.4254 600 ASN A ND2 4647 N N . VAL A 601 ? 1.6105 1.2580 1.9475 -0.1458 -0.5794 0.3299 601 VAL A N 4648 C CA . VAL A 601 ? 1.6955 1.3285 2.0299 -0.1396 -0.5657 0.3165 601 VAL A CA 4649 C C . VAL A 601 ? 1.5789 1.2111 1.9188 -0.1235 -0.5469 0.2891 601 VAL A C 4650 O O . VAL A 601 ? 1.3385 0.9757 1.7026 -0.1119 -0.5480 0.2842 601 VAL A O 4651 C CB . VAL A 601 ? 1.3579 0.9735 1.7291 -0.1333 -0.5769 0.3292 601 VAL A CB 4652 C CG1 . VAL A 601 ? 1.3311 0.9422 1.7491 -0.1156 -0.5837 0.3259 601 VAL A CG1 4653 C CG2 . VAL A 601 ? 1.3514 0.9533 1.7185 -0.1285 -0.5636 0.3151 601 VAL A CG2 4654 N N . CYS A 602 ? 1.3830 1.0116 1.7010 -0.1234 -0.5300 0.2727 602 CYS A N 4655 C CA . CYS A 602 ? 1.3472 0.9791 1.6689 -0.1099 -0.5119 0.2493 602 CYS A CA 4656 C C . CYS A 602 ? 1.3447 0.9669 1.6962 -0.0924 -0.5063 0.2387 602 CYS A C 4657 O O . CYS A 602 ? 1.4694 1.0788 1.8197 -0.0933 -0.5052 0.2384 602 CYS A O 4658 C CB . CYS A 602 ? 1.4030 1.0390 1.6877 -0.1187 -0.4964 0.2361 602 CYS A CB 4659 S SG . CYS A 602 ? 1.4052 1.0584 1.6594 -0.1366 -0.5011 0.2395 602 CYS A SG 4660 N N . LYS A 603 ? 1.3889 1.0201 1.7684 -0.0766 -0.5030 0.2292 603 LYS A N 4661 C CA . LYS A 603 ? 1.4960 1.1258 1.9068 -0.0582 -0.4977 0.2153 603 LYS A CA 4662 C C . LYS A 603 ? 1.4427 1.0902 1.8527 -0.0465 -0.4786 0.1956 603 LYS A C 4663 O O . LYS A 603 ? 1.3456 1.0100 1.7753 -0.0370 -0.4780 0.1931 603 LYS A O 4664 C CB . LYS A 603 ? 1.5138 1.1436 1.9673 -0.0479 -0.5135 0.2225 603 LYS A CB 4665 C CG . LYS A 603 ? 1.3697 0.9820 1.8365 -0.0563 -0.5333 0.2425 603 LYS A CG 4666 C CD . LYS A 603 ? 1.5856 1.1998 2.0958 -0.0474 -0.5499 0.2512 603 LYS A CD 4667 C CE . LYS A 603 ? 1.7587 1.3553 2.2927 -0.0538 -0.5704 0.2714 603 LYS A CE 4668 N NZ . LYS A 603 ? 1.5988 1.1828 2.1611 -0.0429 -0.5693 0.2585 603 LYS A NZ 4669 N N . PRO A 604 ? 1.4408 1.0868 1.8292 -0.0477 -0.4633 0.1832 604 PRO A N 4670 C CA . PRO A 604 ? 1.2816 0.9467 1.6676 -0.0388 -0.4449 0.1674 604 PRO A CA 4671 C C . PRO A 604 ? 1.3265 1.0076 1.7463 -0.0183 -0.4397 0.1532 604 PRO A C 4672 O O . PRO A 604 ? 1.5901 1.2621 2.0309 -0.0106 -0.4463 0.1484 604 PRO A O 4673 C CB . PRO A 604 ? 1.2894 0.9450 1.6445 -0.0469 -0.4329 0.1601 604 PRO A CB 4674 C CG . PRO A 604 ? 1.3005 0.9352 1.6363 -0.0629 -0.4449 0.1739 604 PRO A CG 4675 C CD . PRO A 604 ? 1.3652 0.9929 1.7300 -0.0590 -0.4630 0.1858 604 PRO A CD 4676 N N . LYS A 605 ? 1.2652 0.9731 1.6930 -0.0097 -0.4285 0.1464 605 LYS A N 4677 C CA . LYS A 605 ? 1.4166 1.1494 1.8718 0.0095 -0.4202 0.1305 605 LYS A CA 4678 C C . LYS A 605 ? 1.3844 1.1332 1.8229 0.0112 -0.4007 0.1193 605 LYS A C 4679 O O . LYS A 605 ? 1.3467 1.1120 1.7766 0.0073 -0.3922 0.1240 605 LYS A O 4680 C CB . LYS A 605 ? 1.5224 1.2810 2.0051 0.0190 -0.4236 0.1340 605 LYS A CB 4681 C CG . LYS A 605 ? 1.6616 1.4512 2.1769 0.0397 -0.4176 0.1169 605 LYS A CG 4682 C CD . LYS A 605 ? 1.6814 1.4961 2.2247 0.0481 -0.4230 0.1223 605 LYS A CD 4683 C CE . LYS A 605 ? 1.6068 1.4566 2.1846 0.0693 -0.4181 0.1032 605 LYS A CE 4684 N NZ . LYS A 605 ? 1.6389 1.5227 2.2091 0.0762 -0.3986 0.0908 605 LYS A NZ 4685 N N . LEU A 606 ? 1.3935 1.1380 1.8307 0.0170 -0.3945 0.1049 606 LEU A N 4686 C CA . LEU A 606 ? 1.4093 1.1638 1.8266 0.0160 -0.3772 0.0958 606 LEU A CA 4687 C C . LEU A 606 ? 1.4939 1.2851 1.9324 0.0342 -0.3655 0.0782 606 LEU A C 4688 O O . LEU A 606 ? 1.6180 1.4140 2.0811 0.0472 -0.3702 0.0645 606 LEU A O 4689 C CB . LEU A 606 ? 1.3606 1.0838 1.7546 0.0063 -0.3777 0.0934 606 LEU A CB 4690 C CG . LEU A 606 ? 1.2764 0.9695 1.6461 -0.0127 -0.3883 0.1102 606 LEU A CG 4691 C CD1 . LEU A 606 ? 1.3270 0.9932 1.6804 -0.0204 -0.3905 0.1087 606 LEU A CD1 4692 C CD2 . LEU A 606 ? 1.2725 0.9718 1.6190 -0.0241 -0.3807 0.1170 606 LEU A CD2 4693 N N . GLU A 607 ? 1.3224 1.1422 1.7540 0.0350 -0.3510 0.0785 607 GLU A N 4694 C CA . GLU A 607 ? 1.2761 1.1396 1.7250 0.0510 -0.3386 0.0641 607 GLU A CA 4695 C C . GLU A 607 ? 1.2351 1.1094 1.6629 0.0468 -0.3224 0.0611 607 GLU A C 4696 O O . GLU A 607 ? 1.2330 1.0955 1.6409 0.0331 -0.3190 0.0742 607 GLU A O 4697 C CB . GLU A 607 ? 1.4895 1.3926 1.9617 0.0587 -0.3377 0.0716 607 GLU A CB 4698 C CG . GLU A 607 ? 1.7453 1.6407 2.2408 0.0633 -0.3535 0.0750 607 GLU A CG 4699 C CD . GLU A 607 ? 1.7053 1.6382 2.2215 0.0688 -0.3526 0.0851 607 GLU A CD 4700 O OE1 . GLU A 607 ? 1.6898 1.6612 2.2074 0.0714 -0.3394 0.0880 607 GLU A OE1 4701 O OE2 . GLU A 607 ? 1.5809 1.5061 2.1138 0.0699 -0.3656 0.0918 607 GLU A OE2 4702 N N . VAL A 608 ? 1.3604 1.2587 1.7951 0.0589 -0.3132 0.0427 608 VAL A N 4703 C CA . VAL A 608 ? 1.2709 1.1830 1.6878 0.0561 -0.2979 0.0394 608 VAL A CA 4704 C C . VAL A 608 ? 1.2303 1.2025 1.6657 0.0714 -0.2857 0.0293 608 VAL A C 4705 O O . VAL A 608 ? 1.2170 1.2102 1.6710 0.0865 -0.2862 0.0090 608 VAL A O 4706 C CB . VAL A 608 ? 1.2919 1.1702 1.6908 0.0524 -0.2977 0.0268 608 VAL A CB 4707 C CG1 . VAL A 608 ? 1.4839 1.3543 1.9045 0.0644 -0.3076 0.0088 608 VAL A CG1 4708 C CG2 . VAL A 608 ? 1.2519 1.1531 1.6385 0.0538 -0.2814 0.0190 608 VAL A CG2 4709 N N . SER A 609 ? 1.2399 1.2426 1.6727 0.0672 -0.2753 0.0437 609 SER A N 4710 C CA . SER A 609 ? 1.1853 1.2524 1.6345 0.0796 -0.2632 0.0393 609 SER A CA 4711 C C . SER A 609 ? 1.1833 1.2636 1.6156 0.0751 -0.2492 0.0396 609 SER A C 4712 O O . SER A 609 ? 1.1892 1.2357 1.6014 0.0603 -0.2481 0.0512 609 SER A O 4713 C CB . SER A 609 ? 1.2270 1.3300 1.6955 0.0797 -0.2632 0.0598 609 SER A CB 4714 O OG . SER A 609 ? 1.2512 1.3443 1.7364 0.0845 -0.2760 0.0593 609 SER A OG 4715 N N . VAL A 610 ? 1.2226 1.3548 1.6644 0.0880 -0.2389 0.0259 610 VAL A N 4716 C CA . VAL A 610 ? 1.2214 1.3727 1.6494 0.0851 -0.2256 0.0254 610 VAL A CA 4717 C C . VAL A 610 ? 1.3158 1.5475 1.7622 0.0974 -0.2142 0.0244 610 VAL A C 4718 O O . VAL A 610 ? 1.4428 1.7122 1.9085 0.1127 -0.2156 0.0081 610 VAL A O 4719 C CB . VAL A 610 ? 1.1935 1.3117 1.6048 0.0867 -0.2255 0.0017 610 VAL A CB 4720 C CG1 . VAL A 610 ? 1.3184 1.4484 1.7485 0.1036 -0.2315 -0.0259 610 VAL A CG1 4721 C CG2 . VAL A 610 ? 1.1925 1.3355 1.5911 0.0854 -0.2114 -0.0007 610 VAL A CG2 4722 N N . ASP A 611 ? 1.3845 1.6454 1.8269 0.0906 -0.2034 0.0421 611 ASP A N 4723 C CA . ASP A 611 ? 1.5371 1.8804 1.9967 0.1002 -0.1926 0.0464 611 ASP A CA 4724 C C . ASP A 611 ? 1.6613 2.0312 2.1087 0.1033 -0.1808 0.0336 611 ASP A C 4725 O O . ASP A 611 ? 1.6576 1.9788 2.0836 0.0977 -0.1810 0.0222 611 ASP A O 4726 C CB . ASP A 611 ? 1.5772 1.9473 2.0512 0.0904 -0.1904 0.0826 611 ASP A CB 4727 C CG . ASP A 611 ? 1.5872 2.0401 2.0880 0.1017 -0.1857 0.0905 611 ASP A CG 4728 O OD1 . ASP A 611 ? 1.3378 1.8453 1.8421 0.1156 -0.1783 0.0705 611 ASP A OD1 4729 O OD2 . ASP A 611 ? 1.7825 2.2484 2.3020 0.0967 -0.1897 0.1161 611 ASP A OD2 4730 N N . SER A 612 ? 1.7096 2.1602 2.1710 0.1121 -0.1706 0.0366 612 SER A N 4731 C CA . SER A 612 ? 1.6717 2.1615 2.1246 0.1186 -0.1597 0.0199 612 SER A CA 4732 C C . SER A 612 ? 1.6220 2.1042 2.0608 0.1047 -0.1517 0.0404 612 SER A C 4733 O O . SER A 612 ? 1.5104 1.9716 1.9308 0.1041 -0.1478 0.0235 612 SER A O 4734 C CB . SER A 612 ? 1.5611 2.1494 2.0346 0.1333 -0.1518 0.0151 612 SER A CB 4735 O OG . SER A 612 ? 1.4525 2.0899 1.9403 0.1260 -0.1468 0.0526 612 SER A OG 4736 N N . ASP A 613 ? 1.5864 2.0857 2.0372 0.0938 -0.1502 0.0765 613 ASP A N 4737 C CA . ASP A 613 ? 1.5073 2.0204 1.9553 0.0825 -0.1420 0.0990 613 ASP A CA 4738 C C . ASP A 613 ? 1.5601 2.1484 2.0081 0.0931 -0.1301 0.0878 613 ASP A C 4739 O O . ASP A 613 ? 1.4887 2.1554 1.9551 0.1029 -0.1258 0.0923 613 ASP A O 4740 C CB . ASP A 613 ? 1.5131 1.9451 1.9375 0.0697 -0.1447 0.0949 613 ASP A CB 4741 C CG . ASP A 613 ? 1.6780 2.1177 2.1053 0.0566 -0.1383 0.1212 613 ASP A CG 4742 O OD1 . ASP A 613 ? 1.7547 2.1812 2.1982 0.0450 -0.1428 0.1494 613 ASP A OD1 4743 O OD2 . ASP A 613 ? 1.5377 1.9971 1.9539 0.0581 -0.1296 0.1131 613 ASP A OD2 4744 N N . GLN A 614 ? 1.5676 2.1360 1.9953 0.0912 -0.1249 0.0731 614 GLN A N 4745 C CA . GLN A 614 ? 1.3657 2.0018 1.7910 0.1023 -0.1146 0.0562 614 GLN A CA 4746 C C . GLN A 614 ? 1.3710 2.0239 1.7976 0.1207 -0.1174 0.0162 614 GLN A C 4747 O O . GLN A 614 ? 1.4879 2.0754 1.9033 0.1230 -0.1251 -0.0093 614 GLN A O 4748 C CB . GLN A 614 ? 1.3635 1.9680 1.7672 0.0954 -0.1094 0.0489 614 GLN A CB 4749 C CG . GLN A 614 ? 1.5873 2.1979 1.9957 0.0798 -0.1045 0.0862 614 GLN A CG 4750 C CD . GLN A 614 ? 1.6552 2.3635 2.0774 0.0835 -0.0938 0.1023 614 GLN A CD 4751 O OE1 . GLN A 614 ? 1.6848 2.4607 2.1109 0.0982 -0.0893 0.0837 614 GLN A OE1 4752 N NE2 . GLN A 614 ? 1.5362 2.2552 1.9681 0.0701 -0.0903 0.1369 614 GLN A NE2 4753 N N . LYS A 615 ? 1.3694 2.1127 1.8127 0.1337 -0.1117 0.0108 615 LYS A N 4754 C CA . LYS A 615 ? 1.3705 2.1397 1.8210 0.1527 -0.1142 -0.0302 615 LYS A CA 4755 C C . LYS A 615 ? 1.4628 2.2478 1.9013 0.1614 -0.1086 -0.0648 615 LYS A C 4756 O O . LYS A 615 ? 1.4687 2.2576 1.9132 0.1765 -0.1125 -0.1052 615 LYS A O 4757 C CB . LYS A 615 ? 1.0702 1.9349 1.5449 0.1639 -0.1105 -0.0247 615 LYS A CB 4758 C CG . LYS A 615 ? 1.0181 1.8623 1.5090 0.1625 -0.1196 -0.0091 615 LYS A CG 4759 C CD . LYS A 615 ? 1.1049 2.0456 1.6202 0.1769 -0.1162 -0.0133 615 LYS A CD 4760 C CE . LYS A 615 ? 1.0466 1.9647 1.5788 0.1765 -0.1258 -0.0005 615 LYS A CE 4761 N NZ . LYS A 615 ? 0.9902 1.8255 1.5186 0.1810 -0.1382 -0.0301 615 LYS A NZ 4762 N N . LYS A 616 ? 1.1992 1.9933 1.6238 0.1519 -0.1002 -0.0492 616 LYS A N 4763 C CA . LYS A 616 ? 1.0918 1.9039 1.5047 0.1589 -0.0943 -0.0792 616 LYS A CA 4764 C C . LYS A 616 ? 1.0506 1.8070 1.4416 0.1434 -0.0914 -0.0643 616 LYS A C 4765 O O . LYS A 616 ? 1.1356 1.8913 1.5256 0.1290 -0.0879 -0.0253 616 LYS A O 4766 C CB . LYS A 616 ? 1.1306 2.0607 1.5544 0.1696 -0.0835 -0.0822 616 LYS A CB 4767 C CG . LYS A 616 ? 1.2024 2.1883 1.6332 0.1579 -0.0760 -0.0326 616 LYS A CG 4768 C CD . LYS A 616 ? 1.1629 2.2747 1.6072 0.1694 -0.0665 -0.0347 616 LYS A CD 4769 C CE . LYS A 616 ? 1.0675 2.2241 1.5312 0.1853 -0.0702 -0.0560 616 LYS A CE 4770 N NZ . LYS A 616 ? 0.9483 2.0744 1.4253 0.1773 -0.0770 -0.0233 616 LYS A NZ 4771 N N . ILE A 617 ? 1.0348 1.7443 1.4115 0.1464 -0.0936 -0.0959 617 ILE A N 4772 C CA . ILE A 617 ? 1.0661 1.7312 1.4219 0.1339 -0.0898 -0.0876 617 ILE A CA 4773 C C . ILE A 617 ? 1.2058 1.9182 1.5567 0.1441 -0.0826 -0.1175 617 ILE A C 4774 O O . ILE A 617 ? 1.3068 2.0482 1.6676 0.1606 -0.0850 -0.1554 617 ILE A O 4775 C CB . ILE A 617 ? 1.0917 1.6484 1.4328 0.1248 -0.0995 -0.0939 617 ILE A CB 4776 C CG1 . ILE A 617 ? 1.1976 1.7282 1.5439 0.1384 -0.1081 -0.1361 617 ILE A CG1 4777 C CG2 . ILE A 617 ? 1.1065 1.6195 1.4512 0.1132 -0.1062 -0.0632 617 ILE A CG2 4778 C CD1 . ILE A 617 ? 1.3834 1.8140 1.7168 0.1291 -0.1181 -0.1402 617 ILE A CD1 4779 N N . TYR A 618 ? 1.1214 1.8436 1.4596 0.1347 -0.0744 -0.1015 618 TYR A N 4780 C CA . TYR A 618 ? 0.9937 1.7733 1.3279 0.1437 -0.0666 -0.1256 618 TYR A CA 4781 C C . TYR A 618 ? 1.0832 1.7941 1.4013 0.1430 -0.0699 -0.1546 618 TYR A C 4782 O O . TYR A 618 ? 1.0565 1.6902 1.3594 0.1288 -0.0723 -0.1394 618 TYR A O 4783 C CB . TYR A 618 ? 0.9642 1.8064 1.2974 0.1348 -0.0558 -0.0905 618 TYR A CB 4784 C CG . TYR A 618 ? 0.9625 1.8753 1.3153 0.1347 -0.0534 -0.0587 618 TYR A CG 4785 C CD1 . TYR A 618 ? 1.2279 2.1147 1.5873 0.1190 -0.0550 -0.0132 618 TYR A CD1 4786 C CD2 . TYR A 618 ? 0.9772 1.9834 1.3448 0.1506 -0.0502 -0.0756 618 TYR A CD2 4787 C CE1 . TYR A 618 ? 1.2362 2.1871 1.6172 0.1185 -0.0537 0.0176 618 TYR A CE1 4788 C CE2 . TYR A 618 ? 0.9484 2.0221 1.3347 0.1502 -0.0481 -0.0451 618 TYR A CE2 4789 C CZ . TYR A 618 ? 1.0343 2.0789 1.4277 0.1338 -0.0500 0.0027 618 TYR A CZ 4790 O OH . TYR A 618 ? 0.9698 2.0816 1.3852 0.1329 -0.0486 0.0350 618 TYR A OH 4791 N N . ILE A 619 ? 1.1989 1.9420 1.5228 0.1589 -0.0703 -0.1974 619 ILE A N 4792 C CA . ILE A 619 ? 1.2301 1.9084 1.5479 0.1618 -0.0769 -0.2314 619 ILE A CA 4793 C C . ILE A 619 ? 1.1771 1.8235 1.4735 0.1503 -0.0713 -0.2242 619 ILE A C 4794 O O . ILE A 619 ? 1.2896 1.8671 1.5783 0.1478 -0.0771 -0.2422 619 ILE A O 4795 C CB . ILE A 619 ? 1.1293 1.8605 1.4662 0.1831 -0.0794 -0.2816 619 ILE A CB 4796 C CG1 . ILE A 619 ? 1.2476 1.9012 1.5908 0.1874 -0.0917 -0.3154 619 ILE A CG1 4797 C CG2 . ILE A 619 ? 1.3062 2.1179 1.6390 0.1887 -0.0685 -0.2937 619 ILE A CG2 4798 C CD1 . ILE A 619 ? 1.1403 1.8371 1.5122 0.2091 -0.0978 -0.3657 619 ILE A CD1 4799 N N . GLY A 620 ? 1.0390 1.7359 1.3281 0.1429 -0.0605 -0.1965 620 GLY A N 4800 C CA . GLY A 620 ? 1.1733 1.8458 1.4444 0.1324 -0.0549 -0.1889 620 GLY A CA 4801 C C . GLY A 620 ? 1.3647 1.9782 1.6236 0.1123 -0.0539 -0.1476 620 GLY A C 4802 O O . GLY A 620 ? 1.1759 1.7509 1.4198 0.1025 -0.0510 -0.1432 620 GLY A O 4803 N N . ASP A 621 ? 1.5855 2.1923 1.8529 0.1064 -0.0568 -0.1191 621 ASP A N 4804 C CA . ASP A 621 ? 1.5766 2.1398 1.8389 0.0881 -0.0562 -0.0797 621 ASP A CA 4805 C C . ASP A 621 ? 1.5048 1.9737 1.7596 0.0802 -0.0661 -0.0796 621 ASP A C 4806 O O . ASP A 621 ? 1.5971 2.0344 1.8516 0.0884 -0.0738 -0.1065 621 ASP A O 4807 C CB . ASP A 621 ? 1.5297 2.1560 1.8108 0.0849 -0.0528 -0.0431 621 ASP A CB 4808 C CG . ASP A 621 ? 1.6474 2.2581 1.9306 0.0674 -0.0495 -0.0030 621 ASP A CG 4809 O OD1 . ASP A 621 ? 1.8026 2.3353 2.0729 0.0563 -0.0524 -0.0014 621 ASP A OD1 4810 O OD2 . ASP A 621 ? 1.5257 2.2046 1.8261 0.0647 -0.0444 0.0271 621 ASP A OD2 4811 N N . ASP A 622 ? 1.3151 1.7422 1.5664 0.0641 -0.0664 -0.0491 622 ASP A N 4812 C CA . ASP A 622 ? 1.3304 1.6804 1.5764 0.0554 -0.0755 -0.0435 622 ASP A CA 4813 C C . ASP A 622 ? 1.3772 1.7496 1.6422 0.0528 -0.0786 -0.0160 622 ASP A C 4814 O O . ASP A 622 ? 1.4026 1.7960 1.6788 0.0433 -0.0749 0.0153 622 ASP A O 4815 C CB . ASP A 622 ? 1.3642 1.6518 1.5948 0.0395 -0.0747 -0.0327 622 ASP A CB 4816 C CG . ASP A 622 ? 1.7120 1.9794 1.9249 0.0412 -0.0713 -0.0573 622 ASP A CG 4817 O OD1 . ASP A 622 ? 1.8071 2.0814 2.0183 0.0536 -0.0738 -0.0874 622 ASP A OD1 4818 O OD2 . ASP A 622 ? 1.7374 1.9821 1.9407 0.0302 -0.0667 -0.0473 622 ASP A OD2 4819 N N . ASN A 623 ? 1.2556 1.6235 1.5274 0.0612 -0.0860 -0.0273 623 ASN A N 4820 C CA . ASN A 623 ? 1.3142 1.7160 1.6065 0.0618 -0.0886 -0.0047 623 ASN A CA 4821 C C . ASN A 623 ? 1.3693 1.7079 1.6622 0.0497 -0.0973 0.0133 623 ASN A C 4822 O O . ASN A 623 ? 1.6163 1.8923 1.8966 0.0484 -0.1052 -0.0025 623 ASN A O 4823 C CB . ASN A 623 ? 1.4207 1.8653 1.7240 0.0791 -0.0914 -0.0272 623 ASN A CB 4824 C CG . ASN A 623 ? 1.4675 1.9848 1.7731 0.0923 -0.0832 -0.0478 623 ASN A CG 4825 O OD1 . ASN A 623 ? 1.4902 2.0878 1.8098 0.0964 -0.0765 -0.0333 623 ASN A OD1 4826 N ND2 . ASN A 623 ? 1.4738 1.9664 1.7673 0.0987 -0.0841 -0.0817 623 ASN A ND2 4827 N N . PRO A 624 ? 1.2274 1.5849 1.5375 0.0406 -0.0965 0.0470 624 PRO A N 4828 C CA . PRO A 624 ? 1.2960 1.6044 1.6124 0.0296 -0.1051 0.0647 624 PRO A CA 4829 C C . PRO A 624 ? 1.4600 1.7722 1.7859 0.0377 -0.1130 0.0599 624 PRO A C 4830 O O . PRO A 624 ? 1.5202 1.8717 1.8690 0.0379 -0.1142 0.0821 624 PRO A O 4831 C CB . PRO A 624 ? 1.3135 1.6579 1.6542 0.0200 -0.1016 0.1013 624 PRO A CB 4832 C CG . PRO A 624 ? 1.3151 1.7105 1.6549 0.0226 -0.0909 0.1027 624 PRO A CG 4833 C CD . PRO A 624 ? 1.2458 1.6726 1.5727 0.0388 -0.0878 0.0715 624 PRO A CD 4834 N N . LEU A 625 ? 1.4228 1.6951 1.7337 0.0441 -0.1191 0.0323 625 LEU A N 4835 C CA . LEU A 625 ? 1.4038 1.6766 1.7246 0.0525 -0.1275 0.0252 625 LEU A CA 4836 C C . LEU A 625 ? 1.1932 1.4073 1.5131 0.0411 -0.1377 0.0386 625 LEU A C 4837 O O . LEU A 625 ? 1.2094 1.3611 1.5107 0.0316 -0.1417 0.0331 625 LEU A O 4838 C CB . LEU A 625 ? 1.3510 1.6116 1.6630 0.0651 -0.1308 -0.0103 625 LEU A CB 4839 C CG . LEU A 625 ? 1.2703 1.5319 1.5958 0.0754 -0.1402 -0.0213 625 LEU A CG 4840 C CD1 . LEU A 625 ? 1.2983 1.6373 1.6473 0.0846 -0.1362 -0.0105 625 LEU A CD1 4841 C CD2 . LEU A 625 ? 1.3228 1.5692 1.6454 0.0872 -0.1446 -0.0570 625 LEU A CD2 4842 N N . THR A 626 ? 1.1666 1.4044 1.5071 0.0420 -0.1419 0.0561 626 THR A N 4843 C CA . THR A 626 ? 1.1842 1.3739 1.5271 0.0318 -0.1521 0.0691 626 THR A CA 4844 C C . THR A 626 ? 1.3859 1.5807 1.7398 0.0408 -0.1607 0.0634 626 THR A C 4845 O O . THR A 626 ? 1.4319 1.6842 1.8069 0.0494 -0.1586 0.0714 626 THR A O 4846 C CB . THR A 626 ? 1.1448 1.3507 1.5078 0.0205 -0.1509 0.1013 626 THR A CB 4847 O OG1 . THR A 626 ? 1.2702 1.4755 1.6277 0.0127 -0.1430 0.1073 626 THR A OG1 4848 C CG2 . THR A 626 ? 1.1438 1.2968 1.5086 0.0095 -0.1619 0.1103 626 THR A CG2 4849 N N . LEU A 627 ? 1.3604 1.4976 1.7012 0.0385 -0.1707 0.0507 627 LEU A N 4850 C CA . LEU A 627 ? 1.1903 1.3261 1.5423 0.0464 -0.1803 0.0454 627 LEU A CA 4851 C C . LEU A 627 ? 1.1800 1.2922 1.5406 0.0360 -0.1890 0.0668 627 LEU A C 4852 O O . LEU A 627 ? 1.2519 1.3138 1.5987 0.0227 -0.1936 0.0720 627 LEU A O 4853 C CB . LEU A 627 ? 1.2055 1.2969 1.5435 0.0507 -0.1878 0.0202 627 LEU A CB 4854 C CG . LEU A 627 ? 1.2156 1.3284 1.5506 0.0629 -0.1819 -0.0058 627 LEU A CG 4855 C CD1 . LEU A 627 ? 1.2291 1.2978 1.5601 0.0673 -0.1925 -0.0277 627 LEU A CD1 4856 C CD2 . LEU A 627 ? 1.3294 1.5185 1.6861 0.0782 -0.1753 -0.0109 627 LEU A CD2 4857 N N . ILE A 628 ? 1.1565 1.3083 1.5408 0.0423 -0.1913 0.0782 628 ILE A N 4858 C CA . ILE A 628 ? 1.1461 1.2799 1.5424 0.0339 -0.2005 0.0974 628 ILE A CA 4859 C C . ILE A 628 ? 1.1598 1.2600 1.5530 0.0380 -0.2127 0.0851 628 ILE A C 4860 O O . ILE A 628 ? 1.1541 1.2833 1.5601 0.0515 -0.2143 0.0750 628 ILE A O 4861 C CB . ILE A 628 ? 1.1141 1.3097 1.5411 0.0372 -0.1972 0.1202 628 ILE A CB 4862 C CG1 . ILE A 628 ? 1.0984 1.3219 1.5334 0.0296 -0.1877 0.1392 628 ILE A CG1 4863 C CG2 . ILE A 628 ? 1.1060 1.2839 1.5485 0.0311 -0.2083 0.1363 628 ILE A CG2 4864 C CD1 . ILE A 628 ? 1.1043 1.2764 1.5333 0.0128 -0.1915 0.1492 628 ILE A CD1 4865 N N . VAL A 629 ? 1.1746 1.2161 1.5521 0.0262 -0.2215 0.0859 629 VAL A N 4866 C CA . VAL A 629 ? 1.1894 1.1946 1.5615 0.0281 -0.2339 0.0758 629 VAL A CA 4867 C C . VAL A 629 ? 1.2319 1.2262 1.6164 0.0219 -0.2446 0.0921 629 VAL A C 4868 O O . VAL A 629 ? 1.2716 1.2506 1.6551 0.0092 -0.2461 0.1063 629 VAL A O 4869 C CB . VAL A 629 ? 1.2108 1.1599 1.5547 0.0192 -0.2376 0.0643 629 VAL A CB 4870 C CG1 . VAL A 629 ? 1.2353 1.1513 1.5773 0.0210 -0.2513 0.0569 629 VAL A CG1 4871 C CG2 . VAL A 629 ? 1.2170 1.1746 1.5496 0.0247 -0.2275 0.0482 629 VAL A CG2 4872 N N . LYS A 630 ? 1.2876 1.2910 1.6864 0.0313 -0.2524 0.0886 630 LYS A N 4873 C CA . LYS A 630 ? 1.2468 1.2374 1.6568 0.0262 -0.2640 0.1021 630 LYS A CA 4874 C C . LYS A 630 ? 1.3098 1.2550 1.7083 0.0246 -0.2771 0.0927 630 LYS A C 4875 O O . LYS A 630 ? 1.5241 1.4752 1.9314 0.0365 -0.2810 0.0799 630 LYS A O 4876 C CB . LYS A 630 ? 1.2026 1.2450 1.6428 0.0375 -0.2633 0.1104 630 LYS A CB 4877 C CG . LYS A 630 ? 1.2501 1.2816 1.7043 0.0329 -0.2755 0.1245 630 LYS A CG 4878 C CD . LYS A 630 ? 1.3896 1.4766 1.8747 0.0441 -0.2738 0.1335 630 LYS A CD 4879 C CE . LYS A 630 ? 1.4718 1.5474 1.9720 0.0393 -0.2862 0.1480 630 LYS A CE 4880 N NZ . LYS A 630 ? 1.3710 1.5025 1.9022 0.0500 -0.2846 0.1578 630 LYS A NZ 4881 N N . ALA A 631 ? 1.2296 1.1325 1.6110 0.0099 -0.2845 0.0991 631 ALA A N 4882 C CA . ALA A 631 ? 1.2502 1.1123 1.6199 0.0057 -0.2977 0.0947 631 ALA A CA 4883 C C . ALA A 631 ? 1.3384 1.1895 1.7152 -0.0020 -0.3097 0.1088 631 ALA A C 4884 O O . ALA A 631 ? 1.4311 1.2773 1.8045 -0.0132 -0.3095 0.1186 631 ALA A O 4885 C CB . ALA A 631 ? 1.2511 1.0754 1.5909 -0.0054 -0.2967 0.0883 631 ALA A CB 4886 N N . GLN A 632 ? 1.2692 1.1170 1.6587 0.0043 -0.3209 0.1088 632 GLN A N 4887 C CA . GLN A 632 ? 1.2984 1.1385 1.6963 -0.0019 -0.3331 0.1219 632 GLN A CA 4888 C C . GLN A 632 ? 1.2766 1.0866 1.6702 -0.0038 -0.3484 0.1212 632 GLN A C 4889 O O . GLN A 632 ? 1.3105 1.1176 1.7109 0.0059 -0.3510 0.1114 632 GLN A O 4890 C CB . GLN A 632 ? 1.3884 1.2698 1.8174 0.0084 -0.3315 0.1296 632 GLN A CB 4891 C CG . GLN A 632 ? 1.5328 1.4376 1.9817 0.0258 -0.3320 0.1194 632 GLN A CG 4892 C CD . GLN A 632 ? 1.5965 1.5477 2.0754 0.0355 -0.3295 0.1276 632 GLN A CD 4893 O OE1 . GLN A 632 ? 1.5816 1.5580 2.0678 0.0319 -0.3221 0.1397 632 GLN A OE1 4894 N NE2 . GLN A 632 ? 1.6038 1.5680 2.1033 0.0477 -0.3363 0.1218 632 GLN A NE2 4895 N N . ASN A 633 ? 1.2944 1.0838 1.6793 -0.0165 -0.3592 0.1316 633 ASN A N 4896 C CA . ASN A 633 ? 1.3797 1.1454 1.7631 -0.0197 -0.3753 0.1359 633 ASN A CA 4897 C C . ASN A 633 ? 1.2327 1.0104 1.6376 -0.0181 -0.3854 0.1471 633 ASN A C 4898 O O . ASN A 633 ? 1.2237 1.0011 1.6253 -0.0281 -0.3885 0.1556 633 ASN A O 4899 C CB . ASN A 633 ? 1.4467 1.1811 1.7993 -0.0369 -0.3809 0.1387 633 ASN A CB 4900 C CG . ASN A 633 ? 1.3085 1.0222 1.6596 -0.0418 -0.3982 0.1468 633 ASN A CG 4901 O OD1 . ASN A 633 ? 1.2900 1.0056 1.6627 -0.0313 -0.4054 0.1472 633 ASN A OD1 4902 N ND2 . ASN A 633 ? 1.2911 0.9878 1.6185 -0.0579 -0.4054 0.1531 633 ASN A ND2 4903 N N . GLN A 634 ? 1.4440 0.8893 1.9069 -0.1031 -0.4091 0.1910 634 GLN A N 4904 C CA . GLN A 634 ? 1.7111 1.1226 2.2543 -0.0979 -0.4249 0.1861 634 GLN A CA 4905 C C . GLN A 634 ? 1.8046 1.1878 2.3358 -0.1078 -0.4673 0.1737 634 GLN A C 4906 O O . GLN A 634 ? 1.9439 1.3333 2.5239 -0.1001 -0.4747 0.1605 634 GLN A O 4907 C CB . GLN A 634 ? 1.7101 1.1311 2.3003 -0.0946 -0.3954 0.1958 634 GLN A CB 4908 C CG . GLN A 634 ? 1.5167 0.9579 2.1206 -0.0836 -0.3550 0.2123 634 GLN A CG 4909 C CD . GLN A 634 ? 1.5475 0.9912 2.1947 -0.0693 -0.3485 0.2118 634 GLN A CD 4910 O OE1 . GLN A 634 ? 1.7882 1.2543 2.4114 -0.0608 -0.3265 0.2187 634 GLN A OE1 4911 N NE2 . GLN A 634 ? 1.5723 1.0191 2.2703 -0.0645 -0.3613 0.1964 634 GLN A NE2 4912 N N . GLY A 635 ? 1.5422 0.9294 1.9946 -0.1210 -0.4833 0.1736 635 GLY A N 4913 C CA . GLY A 635 ? 1.4218 0.7797 1.8510 -0.1307 -0.5249 0.1656 635 GLY A CA 4914 C C . GLY A 635 ? 1.5712 0.9342 1.9613 -0.1241 -0.5476 0.1524 635 GLY A C 4915 O O . GLY A 635 ? 1.3631 0.7415 1.7710 -0.1084 -0.5378 0.1444 635 GLY A O 4916 N N . GLU A 636 ? 1.6541 1.0041 1.9891 -0.1350 -0.5789 0.1502 636 GLU A N 4917 C CA . GLU A 636 ? 1.6084 0.9666 1.8958 -0.1271 -0.6016 0.1369 636 GLU A CA 4918 C C . GLU A 636 ? 1.5575 0.9662 1.7764 -0.1290 -0.5762 0.1423 636 GLU A C 4919 O O . GLU A 636 ? 1.4246 0.8590 1.6368 -0.1362 -0.5425 0.1558 636 GLU A O 4920 C CB . GLU A 636 ? 1.5372 0.8670 1.7824 -0.1377 -0.6417 0.1361 636 GLU A CB 4921 C CG . GLU A 636 ? 1.5294 0.8097 1.8416 -0.1300 -0.6758 0.1234 636 GLU A CG 4922 C CD . GLU A 636 ? 1.8985 1.1463 2.1695 -0.1429 -0.7134 0.1276 636 GLU A CD 4923 O OE1 . GLU A 636 ? 1.7861 0.9988 2.0839 -0.1322 -0.7518 0.1116 636 GLU A OE1 4924 O OE2 . GLU A 636 ? 2.2229 1.4785 2.4366 -0.1636 -0.7063 0.1472 636 GLU A OE2 4925 N N . GLY A 637 ? 1.3925 0.8174 1.5612 -0.1207 -0.5933 0.1301 637 GLY A N 4926 C CA . GLY A 637 ? 1.3787 0.8560 1.4875 -0.1188 -0.5712 0.1310 637 GLY A CA 4927 C C . GLY A 637 ? 1.5606 1.0661 1.6087 -0.1440 -0.5521 0.1535 637 GLY A C 4928 O O . GLY A 637 ? 1.6533 1.1404 1.6704 -0.1635 -0.5696 0.1661 637 GLY A O 4929 N N . ALA A 638 ? 1.6097 1.1586 1.6431 -0.1436 -0.5180 0.1586 638 ALA A N 4930 C CA . ALA A 638 ? 1.4017 0.9824 1.3833 -0.1669 -0.4991 0.1781 638 ALA A CA 4931 C C . ALA A 638 ? 1.4247 1.0620 1.3416 -0.1650 -0.4898 0.1747 638 ALA A C 4932 O O . ALA A 638 ? 1.4267 1.0975 1.3492 -0.1474 -0.4701 0.1633 638 ALA A O 4933 C CB . ALA A 638 ? 1.3828 0.9708 1.3994 -0.1689 -0.4674 0.1872 638 ALA A CB 4934 N N . TYR A 639 ? 1.4538 1.1027 1.3096 -0.1828 -0.5039 0.1854 639 TYR A N 4935 C CA . TYR A 639 ? 1.4926 1.2006 1.2845 -0.1820 -0.4950 0.1835 639 TYR A CA 4936 C C . TYR A 639 ? 1.4783 1.2361 1.2529 -0.1959 -0.4611 0.1963 639 TYR A C 4937 O O . TYR A 639 ? 1.4554 1.2031 1.2338 -0.2202 -0.4540 0.2164 639 TYR A O 4938 C CB . TYR A 639 ? 1.5845 1.2913 1.3154 -0.1985 -0.5183 0.1960 639 TYR A CB 4939 C CG . TYR A 639 ? 1.7068 1.3592 1.4513 -0.1874 -0.5563 0.1854 639 TYR A CG 4940 C CD1 . TYR A 639 ? 1.5284 1.1794 1.2807 -0.1559 -0.5729 0.1568 639 TYR A CD1 4941 C CD2 . TYR A 639 ? 1.8554 1.4566 1.6065 -0.2070 -0.5785 0.2020 639 TYR A CD2 4942 C CE1 . TYR A 639 ? 1.6953 1.2965 1.4628 -0.1446 -0.6105 0.1449 639 TYR A CE1 4943 C CE2 . TYR A 639 ? 1.7684 1.3201 1.5334 -0.1957 -0.6153 0.1909 639 TYR A CE2 4944 C CZ . TYR A 639 ? 1.8820 1.4344 1.6554 -0.1647 -0.6311 0.1622 639 TYR A CZ 4945 O OH . TYR A 639 ? 2.1680 1.6710 1.9580 -0.1523 -0.6706 0.1490 639 TYR A OH 4946 N N . GLU A 640 ? 1.5595 1.3705 1.3169 -0.1788 -0.4431 0.1823 640 GLU A N 4947 C CA . GLU A 640 ? 1.4648 1.3302 1.2049 -0.1884 -0.4125 0.1903 640 GLU A CA 4948 C C . GLU A 640 ? 1.4398 1.2831 1.2262 -0.1943 -0.3956 0.1989 640 GLU A C 4949 O O . GLU A 640 ? 1.4489 1.3067 1.2228 -0.2181 -0.3841 0.2166 640 GLU A O 4950 C CB . GLU A 640 ? 1.4788 1.3808 1.1602 -0.2188 -0.4109 0.2122 640 GLU A CB 4951 C CG . GLU A 640 ? 1.5896 1.5154 1.2176 -0.2136 -0.4268 0.2074 640 GLU A CG 4952 C CD . GLU A 640 ? 1.8270 1.7896 1.3987 -0.2462 -0.4230 0.2349 640 GLU A CD 4953 O OE1 . GLU A 640 ? 1.9163 1.8652 1.4497 -0.2538 -0.4444 0.2445 640 GLU A OE1 4954 O OE2 . GLU A 640 ? 1.9623 1.9677 1.5289 -0.2644 -0.3993 0.2479 640 GLU A OE2 4955 N N . ALA A 641 ? 1.4325 1.2414 1.2733 -0.1720 -0.3948 0.1864 641 ALA A N 4956 C CA . ALA A 641 ? 1.4167 1.2048 1.3016 -0.1725 -0.3779 0.1937 641 ALA A CA 4957 C C . ALA A 641 ? 1.4149 1.2523 1.2903 -0.1662 -0.3484 0.1922 641 ALA A C 4958 O O . ALA A 641 ? 1.4261 1.2974 1.2929 -0.1459 -0.3402 0.1773 641 ALA A O 4959 C CB . ALA A 641 ? 1.4709 1.2129 1.4177 -0.1507 -0.3837 0.1834 641 ALA A CB 4960 N N . GLU A 642 ? 1.4044 1.2446 1.2821 -0.1818 -0.3350 0.2058 642 GLU A N 4961 C CA . GLU A 642 ? 1.4073 1.2918 1.2769 -0.1758 -0.3093 0.2042 642 GLU A CA 4962 C C . GLU A 642 ? 1.4126 1.2737 1.3151 -0.1736 -0.2959 0.2111 642 GLU A C 4963 O O . GLU A 642 ? 1.3938 1.2183 1.3104 -0.1888 -0.3062 0.2213 642 GLU A O 4964 C CB . GLU A 642 ? 1.4092 1.3447 1.2306 -0.1996 -0.3060 0.2124 642 GLU A CB 4965 C CG . GLU A 642 ? 1.5372 1.5162 1.3202 -0.1959 -0.3101 0.2036 642 GLU A CG 4966 C CD . GLU A 642 ? 1.6840 1.7176 1.4243 -0.2222 -0.3041 0.2157 642 GLU A CD 4967 O OE1 . GLU A 642 ? 1.7202 1.7437 1.4605 -0.2492 -0.3056 0.2337 642 GLU A OE1 4968 O OE2 . GLU A 642 ? 1.8264 1.9142 1.5358 -0.2156 -0.2982 0.2068 642 GLU A OE2 4969 N N . LEU A 643 ? 1.4859 1.3690 1.3989 -0.1527 -0.2740 0.2047 643 LEU A N 4970 C CA . LEU A 643 ? 1.4110 1.2813 1.3462 -0.1469 -0.2585 0.2105 643 LEU A CA 4971 C C . LEU A 643 ? 1.4224 1.3330 1.3271 -0.1606 -0.2496 0.2137 643 LEU A C 4972 O O . LEU A 643 ? 1.4313 1.3889 1.3146 -0.1526 -0.2378 0.2064 643 LEU A O 4973 C CB . LEU A 643 ? 1.3710 1.2380 1.3353 -0.1150 -0.2402 0.2045 643 LEU A CB 4974 C CG . LEU A 643 ? 1.3534 1.2166 1.3320 -0.1037 -0.2201 0.2105 643 LEU A CG 4975 C CD1 . LEU A 643 ? 1.3533 1.1723 1.3615 -0.1116 -0.2258 0.2193 643 LEU A CD1 4976 C CD2 . LEU A 643 ? 1.3447 1.2106 1.3442 -0.0726 -0.2013 0.2079 643 LEU A CD2 4977 N N . ILE A 644 ? 1.3980 1.2897 1.3038 -0.1805 -0.2575 0.2231 644 ILE A N 4978 C CA . ILE A 644 ? 1.3930 1.3181 1.2764 -0.1959 -0.2539 0.2259 644 ILE A CA 4979 C C . ILE A 644 ? 1.4012 1.3240 1.2996 -0.1769 -0.2381 0.2220 644 ILE A C 4980 O O . ILE A 644 ? 1.4688 1.3526 1.3907 -0.1729 -0.2409 0.2249 644 ILE A O 4981 C CB . ILE A 644 ? 1.3828 1.2893 1.2572 -0.2304 -0.2759 0.2383 644 ILE A CB 4982 C CG1 . ILE A 644 ? 1.3751 1.2874 1.2267 -0.2489 -0.2908 0.2448 644 ILE A CG1 4983 C CG2 . ILE A 644 ? 1.3910 1.3298 1.2506 -0.2469 -0.2743 0.2409 644 ILE A CG2 4984 C CD1 . ILE A 644 ? 1.3658 1.3407 1.1863 -0.2488 -0.2796 0.2402 644 ILE A CD1 4985 N N . VAL A 645 ? 1.3990 1.3658 1.2824 -0.1632 -0.2220 0.2143 645 VAL A N 4986 C CA . VAL A 645 ? 1.4087 1.3791 1.2980 -0.1422 -0.2072 0.2098 645 VAL A CA 4987 C C . VAL A 645 ? 1.4595 1.4655 1.3288 -0.1574 -0.2111 0.2068 645 VAL A C 4988 O O . VAL A 645 ? 1.5374 1.5918 1.3871 -0.1621 -0.2074 0.2019 645 VAL A O 4989 C CB . VAL A 645 ? 1.4045 1.3926 1.2955 -0.1089 -0.1867 0.2030 645 VAL A CB 4990 C CG1 . VAL A 645 ? 1.4177 1.4141 1.3062 -0.0867 -0.1717 0.1995 645 VAL A CG1 4991 C CG2 . VAL A 645 ? 1.3935 1.3436 1.3132 -0.0940 -0.1840 0.2068 645 VAL A CG2 4992 N N . SER A 646 ? 1.4601 1.4430 1.3374 -0.1645 -0.2200 0.2082 646 SER A N 4993 C CA . SER A 646 ? 1.4419 1.4524 1.3072 -0.1799 -0.2285 0.2043 646 SER A CA 4994 C C . SER A 646 ? 1.4880 1.5173 1.3487 -0.1496 -0.2140 0.1920 646 SER A C 4995 O O . SER A 646 ? 1.6544 1.6543 1.5252 -0.1285 -0.2093 0.1893 646 SER A O 4996 C CB . SER A 646 ? 1.4446 1.4179 1.3214 -0.2044 -0.2520 0.2103 646 SER A CB 4997 O OG . SER A 646 ? 1.5234 1.4759 1.4014 -0.2311 -0.2669 0.2233 646 SER A OG 4998 N N . ILE A 647 ? 1.4281 1.5085 1.2725 -0.1462 -0.2071 0.1842 647 ILE A N 4999 C CA . ILE A 647 ? 1.5260 1.6270 1.3618 -0.1162 -0.1955 0.1717 647 ILE A CA 5000 C C . ILE A 647 ? 1.9025 2.0326 1.7337 -0.1317 -0.2102 0.1629 647 ILE A C 5001 O O . ILE A 647 ? 2.1364 2.3113 1.9624 -0.1516 -0.2143 0.1613 647 ILE A O 5002 C CB . ILE A 647 ? 1.6181 1.7535 1.4422 -0.0918 -0.1769 0.1662 647 ILE A CB 5003 C CG1 . ILE A 647 ? 1.5999 1.7807 1.4158 -0.1145 -0.1809 0.1654 647 ILE A CG1 5004 C CG2 . ILE A 647 ? 1.7309 1.8316 1.5657 -0.0704 -0.1634 0.1737 647 ILE A CG2 5005 C CD1 . ILE A 647 ? 1.5305 1.7521 1.3351 -0.0892 -0.1665 0.1547 647 ILE A CD1 5006 N N . PRO A 648 ? 2.0335 2.1392 1.8695 -0.1227 -0.2192 0.1563 648 PRO A N 5007 C CA . PRO A 648 ? 2.0082 2.1357 1.8451 -0.1357 -0.2377 0.1455 648 PRO A CA 5008 C C . PRO A 648 ? 1.8132 1.9871 1.6356 -0.1111 -0.2290 0.1295 648 PRO A C 5009 O O . PRO A 648 ? 1.4707 1.6423 1.2797 -0.0728 -0.2110 0.1242 648 PRO A O 5010 C CB . PRO A 648 ? 2.0297 2.1110 1.8753 -0.1256 -0.2504 0.1402 648 PRO A CB 5011 C CG . PRO A 648 ? 2.0564 2.1111 1.8979 -0.0905 -0.2276 0.1434 648 PRO A CG 5012 C CD . PRO A 648 ? 2.0785 2.1362 1.9221 -0.0996 -0.2139 0.1577 648 PRO A CD 5013 N N . LEU A 649 ? 1.9160 2.1318 1.7433 -0.1336 -0.2424 0.1232 649 LEU A N 5014 C CA . LEU A 649 ? 1.7553 2.0117 1.5751 -0.1130 -0.2434 0.1039 649 LEU A CA 5015 C C . LEU A 649 ? 1.7063 1.9897 1.5062 -0.0766 -0.2199 0.0976 649 LEU A C 5016 O O . LEU A 649 ? 1.6814 1.9965 1.4795 -0.0840 -0.2089 0.1023 649 LEU A O 5017 C CB . LEU A 649 ? 1.7135 1.9407 1.5323 -0.0923 -0.2576 0.0897 649 LEU A CB 5018 C CG . LEU A 649 ? 1.8386 2.0299 1.6790 -0.1235 -0.2845 0.0937 649 LEU A CG 5019 C CD1 . LEU A 649 ? 1.9267 2.0871 1.7638 -0.0958 -0.2982 0.0761 649 LEU A CD1 5020 C CD2 . LEU A 649 ? 1.7914 2.0169 1.6532 -0.1669 -0.3051 0.0959 649 LEU A CD2 5021 N N . GLN A 650 ? 1.6630 1.9335 1.4468 -0.0360 -0.2136 0.0867 650 GLN A N 5022 C CA . GLN A 650 ? 1.5950 1.8890 1.3579 0.0025 -0.1959 0.0792 650 GLN A CA 5023 C C . GLN A 650 ? 1.7629 2.0575 1.5228 0.0081 -0.1755 0.0918 650 GLN A C 5024 O O . GLN A 650 ? 1.8791 2.2122 1.6311 0.0212 -0.1682 0.0845 650 GLN A O 5025 C CB . GLN A 650 ? 1.5380 1.8018 1.2810 0.0449 -0.1892 0.0741 650 GLN A CB 5026 C CG . GLN A 650 ? 1.6919 1.9297 1.4398 0.0415 -0.2086 0.0656 650 GLN A CG 5027 C CD . GLN A 650 ? 1.5377 1.7257 1.3004 0.0258 -0.2083 0.0807 650 GLN A CD 5028 O OE1 . GLN A 650 ? 1.6880 1.8620 1.4603 0.0120 -0.1958 0.0981 650 GLN A OE1 5029 N NE2 . GLN A 650 ? 1.5339 1.6952 1.2998 0.0295 -0.2243 0.0718 650 GLN A NE2 5030 N N . ALA A 651 ? 1.6999 1.9516 1.4686 -0.0004 -0.1688 0.1085 651 ALA A N 5031 C CA . ALA A 651 ? 1.5046 1.7478 1.2740 0.0088 -0.1522 0.1192 651 ALA A CA 5032 C C . ALA A 651 ? 1.3539 1.6377 1.1280 -0.0150 -0.1550 0.1177 651 ALA A C 5033 O O . ALA A 651 ? 1.4214 1.7179 1.2052 -0.0517 -0.1677 0.1207 651 ALA A O 5034 C CB . ALA A 651 ? 1.6270 1.8154 1.4105 0.0031 -0.1479 0.1357 651 ALA A CB 5035 N N . ASP A 652 ? 1.3379 1.6426 1.1045 0.0073 -0.1434 0.1133 652 ASP A N 5036 C CA . ASP A 652 ? 1.5051 1.8475 1.2743 -0.0080 -0.1439 0.1102 652 ASP A CA 5037 C C . ASP A 652 ? 1.3457 1.6635 1.1170 0.0123 -0.1332 0.1156 652 ASP A C 5038 O O . ASP A 652 ? 1.2963 1.5929 1.0637 0.0459 -0.1232 0.1166 652 ASP A O 5039 C CB . ASP A 652 ? 1.6295 2.0377 1.3914 -0.0016 -0.1458 0.0918 652 ASP A CB 5040 C CG . ASP A 652 ? 1.8200 2.2300 1.5683 0.0412 -0.1390 0.0814 652 ASP A CG 5041 O OD1 . ASP A 652 ? 1.9414 2.3071 1.6836 0.0608 -0.1345 0.0886 652 ASP A OD1 5042 O OD2 . ASP A 652 ? 1.7887 2.2460 1.5315 0.0563 -0.1383 0.0661 652 ASP A OD2 5043 N N . PHE A 653 ? 1.3900 1.7104 1.1680 -0.0081 -0.1368 0.1198 653 PHE A N 5044 C CA . PHE A 653 ? 1.4610 1.7520 1.2468 0.0069 -0.1320 0.1241 653 PHE A CA 5045 C C . PHE A 653 ? 1.4144 1.7384 1.1937 0.0356 -0.1275 0.1093 653 PHE A C 5046 O O . PHE A 653 ? 1.6291 2.0103 1.3994 0.0299 -0.1307 0.0950 653 PHE A O 5047 C CB . PHE A 653 ? 1.5760 1.8590 1.3679 -0.0231 -0.1410 0.1309 653 PHE A CB 5048 C CG . PHE A 653 ? 1.4795 1.7276 1.2839 -0.0096 -0.1408 0.1338 653 PHE A CG 5049 C CD1 . PHE A 653 ? 1.5348 1.7250 1.3584 0.0048 -0.1357 0.1457 653 PHE A CD1 5050 C CD2 . PHE A 653 ? 1.4057 1.6806 1.2050 -0.0111 -0.1464 0.1239 653 PHE A CD2 5051 C CE1 . PHE A 653 ? 1.5205 1.6781 1.3628 0.0157 -0.1378 0.1483 653 PHE A CE1 5052 C CE2 . PHE A 653 ? 1.4231 1.6639 1.2368 0.0024 -0.1504 0.1237 653 PHE A CE2 5053 C CZ . PHE A 653 ? 1.4695 1.6503 1.3074 0.0146 -0.1469 0.1362 653 PHE A CZ 5054 N N . ILE A 654 ? 1.3133 1.6016 1.0995 0.0664 -0.1203 0.1134 654 ILE A N 5055 C CA . ILE A 654 ? 1.4200 1.7285 1.2033 0.0964 -0.1191 0.1002 654 ILE A CA 5056 C C . ILE A 654 ? 1.4768 1.7769 1.2724 0.0938 -0.1263 0.0965 654 ILE A C 5057 O O . ILE A 654 ? 1.5167 1.8639 1.3044 0.0937 -0.1324 0.0788 654 ILE A O 5058 C CB . ILE A 654 ? 1.6438 1.9165 1.4289 0.1320 -0.1094 0.1089 654 ILE A CB 5059 C CG1 . ILE A 654 ? 1.6428 1.9412 1.4068 0.1457 -0.1055 0.1031 654 ILE A CG1 5060 C CG2 . ILE A 654 ? 1.4908 1.7634 1.2823 0.1605 -0.1120 0.1002 654 ILE A CG2 5061 C CD1 . ILE A 654 ? 1.5395 1.8246 1.2990 0.1278 -0.1038 0.1122 654 ILE A CD1 5062 N N . GLY A 655 ? 1.4502 1.6927 1.2667 0.0933 -0.1261 0.1115 655 GLY A N 5063 C CA . GLY A 655 ? 1.5438 1.7713 1.3751 0.0926 -0.1364 0.1069 655 GLY A CA 5064 C C . GLY A 655 ? 1.5978 1.7581 1.4598 0.0950 -0.1356 0.1248 655 GLY A C 5065 O O . GLY A 655 ? 1.5785 1.7066 1.4491 0.0941 -0.1251 0.1425 655 GLY A O 5066 N N . VAL A 656 ? 1.6284 1.7700 1.5089 0.0990 -0.1476 0.1189 656 VAL A N 5067 C CA . VAL A 656 ? 1.5819 1.6618 1.5001 0.1019 -0.1492 0.1341 656 VAL A CA 5068 C C . VAL A 656 ? 1.5073 1.5623 1.4454 0.1337 -0.1414 0.1413 656 VAL A C 5069 O O . VAL A 656 ? 1.4482 1.5315 1.3662 0.1530 -0.1354 0.1345 656 VAL A O 5070 C CB . VAL A 656 ? 1.6333 1.7008 1.5662 0.0951 -0.1690 0.1232 656 VAL A CB 5071 C CG1 . VAL A 656 ? 1.5487 1.5619 1.5144 0.0793 -0.1722 0.1403 656 VAL A CG1 5072 C CG2 . VAL A 656 ? 1.6785 1.7978 1.5760 0.0764 -0.1779 0.1072 656 VAL A CG2 5073 N N . VAL A 657 ? 1.5396 1.5418 1.5189 0.1389 -0.1421 0.1560 657 VAL A N 5074 C CA . VAL A 657 ? 1.6225 1.5968 1.6254 0.1666 -0.1348 0.1680 657 VAL A CA 5075 C C . VAL A 657 ? 1.7063 1.6679 1.7345 0.1833 -0.1552 0.1528 657 VAL A C 5076 O O . VAL A 657 ? 1.7817 1.7099 1.8462 0.1761 -0.1686 0.1531 657 VAL A O 5077 C CB . VAL A 657 ? 1.5892 1.5147 1.6280 0.1631 -0.1192 0.1983 657 VAL A CB 5078 C CG1 . VAL A 657 ? 1.4885 1.4262 1.4998 0.1651 -0.0964 0.2131 657 VAL A CG1 5079 C CG2 . VAL A 657 ? 1.7665 1.6683 1.8311 0.1373 -0.1285 0.2003 657 VAL A CG2 5080 N N . ARG A 658 ? 1.6761 1.6647 1.6861 0.2073 -0.1600 0.1372 658 ARG A N 5081 C CA . ARG A 658 ? 1.7208 1.7008 1.7519 0.2278 -0.1824 0.1181 658 ARG A CA 5082 C C . ARG A 658 ? 1.8723 1.7966 1.9500 0.2468 -0.1820 0.1390 658 ARG A C 5083 O O . ARG A 658 ? 1.9163 1.8065 2.0358 0.2522 -0.2015 0.1337 658 ARG A O 5084 C CB . ARG A 658 ? 1.8693 1.9037 1.8638 0.2473 -0.1894 0.0904 658 ARG A CB 5085 C CG . ARG A 658 ? 1.8382 1.9352 1.7879 0.2281 -0.1851 0.0742 658 ARG A CG 5086 C CD . ARG A 658 ? 1.7664 1.8731 1.7155 0.2078 -0.1998 0.0600 658 ARG A CD 5087 N NE . ARG A 658 ? 1.7698 1.9401 1.6772 0.1897 -0.1956 0.0467 658 ARG A NE 5088 C CZ . ARG A 658 ? 1.8083 2.0021 1.7021 0.1720 -0.2059 0.0344 658 ARG A CZ 5089 N NH1 . ARG A 658 ? 1.7360 1.8937 1.6524 0.1721 -0.2233 0.0301 658 ARG A NH1 5090 N NH2 . ARG A 658 ? 1.6783 1.9319 1.5365 0.1542 -0.1995 0.0271 658 ARG A NH2 5091 N N . ASN A 659 ? 1.8995 1.8150 1.9701 0.2572 -0.1605 0.1634 659 ASN A N 5092 C CA . ASN A 659 ? 1.7365 1.6054 1.8445 0.2775 -0.1572 0.1873 659 ASN A CA 5093 C C . ASN A 659 ? 1.5287 1.3433 1.6970 0.2643 -0.1554 0.2120 659 ASN A C 5094 O O . ASN A 659 ? 1.6693 1.4462 1.8853 0.2755 -0.1716 0.2149 659 ASN A O 5095 C CB . ASN A 659 ? 1.6095 1.4851 1.6879 0.2906 -0.1318 0.2105 659 ASN A CB 5096 C CG . ASN A 659 ? 1.6586 1.5474 1.7139 0.2699 -0.1081 0.2252 659 ASN A CG 5097 O OD1 . ASN A 659 ? 1.6523 1.5847 1.6672 0.2585 -0.1079 0.2064 659 ASN A OD1 5098 N ND2 . ASN A 659 ? 1.6267 1.4789 1.7102 0.2652 -0.0885 0.2590 659 ASN A ND2 5099 N N . ASN A 660 ? 1.3708 1.1816 1.5409 0.2410 -0.1377 0.2286 660 ASN A N 5100 C CA . ASN A 660 ? 1.6155 1.3799 1.8456 0.2282 -0.1333 0.2528 660 ASN A CA 5101 C C . ASN A 660 ? 1.7156 1.4624 1.9833 0.2179 -0.1634 0.2311 660 ASN A C 5102 O O . ASN A 660 ? 1.7584 1.5325 1.9972 0.2053 -0.1773 0.2047 660 ASN A O 5103 C CB . ASN A 660 ? 1.8046 1.5738 2.0243 0.2084 -0.1084 0.2715 660 ASN A CB 5104 C CG . ASN A 660 ? 1.6134 1.3397 1.8950 0.2016 -0.0943 0.3042 660 ASN A CG 5105 O OD1 . ASN A 660 ? 1.3712 1.0637 1.7112 0.1989 -0.1108 0.3054 660 ASN A OD1 5106 N ND2 . ASN A 660 ? 1.5510 1.2808 1.8221 0.2000 -0.0642 0.3297 660 ASN A ND2 5107 N N . GLU A 661 ? 1.6868 1.3877 2.0196 0.2237 -0.1742 0.2433 661 GLU A N 5108 C CA . GLU A 661 ? 1.6066 1.2855 1.9813 0.2179 -0.2065 0.2217 661 GLU A CA 5109 C C . GLU A 661 ? 1.2952 0.9510 1.7098 0.1927 -0.2019 0.2355 661 GLU A C 5110 O O . GLU A 661 ? 1.4081 1.0474 1.8529 0.1847 -0.2286 0.2170 661 GLU A O 5111 C CB . GLU A 661 ? 1.7527 1.3920 2.1835 0.2380 -0.2270 0.2236 661 GLU A CB 5112 C CG . GLU A 661 ? 1.8145 1.4441 2.2675 0.2440 -0.2692 0.1860 661 GLU A CG 5113 C CD . GLU A 661 ? 2.0157 1.5983 2.5459 0.2308 -0.2850 0.1937 661 GLU A CD 5114 O OE1 . GLU A 661 ? 2.0817 1.6355 2.6602 0.2202 -0.2632 0.2313 661 GLU A OE1 5115 O OE2 . GLU A 661 ? 2.0393 1.6161 2.5824 0.2320 -0.3194 0.1614 661 GLU A OE2 5116 N N . ALA A 662 ? 1.2658 0.9216 1.6795 0.1825 -0.1693 0.2660 662 ALA A N 5117 C CA . ALA A 662 ? 1.5618 1.2000 2.0123 0.1602 -0.1626 0.2789 662 ALA A CA 5118 C C . ALA A 662 ? 1.7671 1.4377 2.1622 0.1422 -0.1600 0.2638 662 ALA A C 5119 O O . ALA A 662 ? 1.6205 1.2801 2.0365 0.1236 -0.1571 0.2702 662 ALA A O 5120 C CB . ALA A 662 ? 1.5069 1.1274 1.9939 0.1607 -0.1289 0.3205 662 ALA A CB 5121 N N . LEU A 663 ? 1.7143 1.4249 2.0419 0.1475 -0.1621 0.2442 663 LEU A N 5122 C CA . LEU A 663 ? 1.5046 1.2478 1.7796 0.1293 -0.1611 0.2311 663 LEU A CA 5123 C C . LEU A 663 ? 1.5939 1.3579 1.8409 0.1255 -0.1905 0.1978 663 LEU A C 5124 O O . LEU A 663 ? 1.7754 1.5454 2.0210 0.1436 -0.2064 0.1803 663 LEU A O 5125 C CB . LEU A 663 ? 1.4877 1.2666 1.7073 0.1353 -0.1370 0.2377 663 LEU A CB 5126 C CG . LEU A 663 ? 1.5719 1.3378 1.8049 0.1390 -0.1060 0.2694 663 LEU A CG 5127 C CD1 . LEU A 663 ? 1.5144 1.3155 1.6898 0.1505 -0.0873 0.2713 663 LEU A CD1 5128 C CD2 . LEU A 663 ? 1.4800 1.2315 1.7340 0.1173 -0.1011 0.2781 663 LEU A CD2 5129 N N . ALA A 664 ? 1.5184 1.2936 1.7423 0.1032 -0.1981 0.1892 664 ALA A N 5130 C CA . ALA A 664 ? 1.3813 1.1773 1.5761 0.0981 -0.2242 0.1611 664 ALA A CA 5131 C C . ALA A 664 ? 1.4286 1.2793 1.5631 0.1058 -0.2206 0.1445 664 ALA A C 5132 O O . ALA A 664 ? 1.4337 1.3092 1.5389 0.1053 -0.1990 0.1543 664 ALA A O 5133 C CB . ALA A 664 ? 1.4106 1.2012 1.5963 0.0713 -0.2326 0.1613 664 ALA A CB 5134 N N . ARG A 665 ? 1.5455 1.4165 1.6632 0.1144 -0.2429 0.1177 665 ARG A N 5135 C CA . ARG A 665 ? 1.7370 1.6647 1.8043 0.1246 -0.2418 0.0982 665 ARG A CA 5136 C C . ARG A 665 ? 1.7026 1.6733 1.7194 0.1004 -0.2413 0.0920 665 ARG A C 5137 O O . ARG A 665 ? 1.6691 1.6932 1.6455 0.1052 -0.2422 0.0742 665 ARG A O 5138 C CB . ARG A 665 ? 1.7887 1.7209 1.8647 0.1505 -0.2659 0.0704 665 ARG A CB 5139 C CG . ARG A 665 ? 1.8692 1.8466 1.9159 0.1734 -0.2607 0.0547 665 ARG A CG 5140 C CD . ARG A 665 ? 1.9834 1.9840 2.0210 0.1948 -0.2870 0.0193 665 ARG A CD 5141 N NE . ARG A 665 ? 2.0348 2.0729 2.0330 0.1784 -0.2955 0.0043 665 ARG A NE 5142 C CZ . ARG A 665 ? 1.9370 2.0102 1.9126 0.1945 -0.3151 -0.0276 665 ARG A CZ 5143 N NH1 . ARG A 665 ? 1.9785 2.0523 1.9697 0.2284 -0.3309 -0.0512 665 ARG A NH1 5144 N NH2 . ARG A 665 ? 1.7675 1.8753 1.7039 0.1779 -0.3196 -0.0357 665 ARG A NH2 5145 N N . LEU A 666 ? 1.5665 1.5141 1.5885 0.0745 -0.2404 0.1074 666 LEU A N 5146 C CA . LEU A 666 ? 1.5890 1.5630 1.5719 0.0490 -0.2474 0.1040 666 LEU A CA 5147 C C . LEU A 666 ? 1.5591 1.5974 1.4912 0.0420 -0.2350 0.0986 666 LEU A C 5148 O O . LEU A 666 ? 1.5317 1.5853 1.4574 0.0441 -0.2160 0.1074 666 LEU A O 5149 C CB . LEU A 666 ? 1.5329 1.4711 1.5305 0.0233 -0.2436 0.1260 666 LEU A CB 5150 C CG . LEU A 666 ? 1.6452 1.5223 1.6975 0.0244 -0.2545 0.1339 666 LEU A CG 5151 C CD1 . LEU A 666 ? 1.5122 1.3634 1.5756 0.0016 -0.2466 0.1546 666 LEU A CD1 5152 C CD2 . LEU A 666 ? 1.7976 1.6627 1.8532 0.0261 -0.2840 0.1161 666 LEU A CD2 5153 N N . SER A 667 ? 1.6171 1.6946 1.5137 0.0344 -0.2464 0.0841 667 SER A N 5154 C CA . SER A 667 ? 1.6349 1.7803 1.4876 0.0257 -0.2355 0.0787 667 SER A CA 5155 C C . SER A 667 ? 1.5371 1.6869 1.3755 -0.0072 -0.2243 0.1004 667 SER A C 5156 O O . SER A 667 ? 1.4953 1.6177 1.3332 -0.0306 -0.2334 0.1128 667 SER A O 5157 C CB . SER A 667 ? 1.6250 1.8133 1.4446 0.0266 -0.2493 0.0595 667 SER A CB 5158 O OG . SER A 667 ? 1.6729 1.8346 1.4858 0.0055 -0.2639 0.0681 667 SER A OG 5159 N N . CYS A 668 ? 1.5377 1.7202 1.3658 -0.0078 -0.2072 0.1036 668 CYS A N 5160 C CA . CYS A 668 ? 1.4879 1.6765 1.3050 -0.0367 -0.1991 0.1211 668 CYS A CA 5161 C C . CYS A 668 ? 1.5275 1.7884 1.3141 -0.0461 -0.1905 0.1146 668 CYS A C 5162 O O . CYS A 668 ? 1.7789 2.0822 1.5579 -0.0238 -0.1854 0.0969 668 CYS A O 5163 C CB . CYS A 668 ? 1.4655 1.6151 1.3075 -0.0292 -0.1875 0.1337 668 CYS A CB 5164 S SG . CYS A 668 ? 2.0052 2.0755 1.8919 -0.0200 -0.1935 0.1446 668 CYS A SG 5165 N N . ALA A 669 ? 1.4595 1.7343 1.2321 -0.0793 -0.1903 0.1287 669 ALA A N 5166 C CA . ALA A 669 ? 1.4474 1.7916 1.1981 -0.0937 -0.1825 0.1258 669 ALA A CA 5167 C C . ALA A 669 ? 1.4619 1.7988 1.2164 -0.1212 -0.1804 0.1427 669 ALA A C 5168 O O . ALA A 669 ? 1.3531 1.6433 1.1146 -0.1420 -0.1894 0.1590 669 ALA A O 5169 C CB . ALA A 669 ? 1.3977 1.7859 1.1217 -0.1096 -0.1880 0.1239 669 ALA A CB 5170 N N . PHE A 670 ? 1.5396 1.9224 1.2916 -0.1197 -0.1710 0.1367 670 PHE A N 5171 C CA . PHE A 670 ? 1.4587 1.8388 1.2163 -0.1434 -0.1720 0.1485 670 PHE A CA 5172 C C . PHE A 670 ? 1.4537 1.8740 1.1992 -0.1832 -0.1771 0.1606 670 PHE A C 5173 O O . PHE A 670 ? 1.5308 2.0185 1.2638 -0.1871 -0.1706 0.1535 670 PHE A O 5174 C CB . PHE A 670 ? 1.3063 1.7163 1.0685 -0.1231 -0.1627 0.1355 670 PHE A CB 5175 C CG . PHE A 670 ? 1.4064 1.8148 1.1761 -0.1436 -0.1669 0.1432 670 PHE A CG 5176 C CD1 . PHE A 670 ? 1.5882 1.9375 1.3693 -0.1381 -0.1705 0.1500 670 PHE A CD1 5177 C CD2 . PHE A 670 ? 1.3940 1.8617 1.1619 -0.1674 -0.1680 0.1425 670 PHE A CD2 5178 C CE1 . PHE A 670 ? 1.6480 1.9947 1.4359 -0.1538 -0.1779 0.1532 670 PHE A CE1 5179 C CE2 . PHE A 670 ? 1.5857 2.0492 1.3650 -0.1859 -0.1760 0.1476 670 PHE A CE2 5180 C CZ . PHE A 670 ? 1.6824 2.0839 1.4702 -0.1779 -0.1822 0.1516 670 PHE A CZ 5181 N N . LYS A 671 ? 1.3322 1.7119 1.0828 -0.2126 -0.1887 0.1799 671 LYS A N 5182 C CA . LYS A 671 ? 1.4172 1.8260 1.1584 -0.2538 -0.1953 0.1971 671 LYS A CA 5183 C C . LYS A 671 ? 1.5505 1.9533 1.3081 -0.2779 -0.2027 0.2066 671 LYS A C 5184 O O . LYS A 671 ? 1.3725 1.7232 1.1455 -0.2689 -0.2090 0.2055 671 LYS A O 5185 C CB . LYS A 671 ? 1.5935 1.9590 1.3241 -0.2717 -0.2082 0.2139 671 LYS A CB 5186 C CG . LYS A 671 ? 1.7114 2.0984 1.4200 -0.2576 -0.2051 0.2063 671 LYS A CG 5187 C CD . LYS A 671 ? 1.8134 2.1593 1.5086 -0.2780 -0.2210 0.2241 671 LYS A CD 5188 C CE . LYS A 671 ? 1.8618 2.2219 1.5484 -0.3230 -0.2281 0.2503 671 LYS A CE 5189 N NZ . LYS A 671 ? 1.7910 2.1049 1.4625 -0.3423 -0.2461 0.2694 671 LYS A NZ 5190 N N . THR A 672 ? 1.7302 2.1890 1.4866 -0.3079 -0.2023 0.2154 672 THR A N 5191 C CA . THR A 672 ? 1.6150 2.0662 1.3903 -0.3378 -0.2148 0.2271 672 THR A CA 5192 C C . THR A 672 ? 1.5108 1.9720 1.2800 -0.3839 -0.2243 0.2550 672 THR A C 5193 O O . THR A 672 ? 1.5502 2.0788 1.3102 -0.4010 -0.2143 0.2619 672 THR A O 5194 C CB . THR A 672 ? 1.5726 2.0828 1.3628 -0.3322 -0.2079 0.2119 672 THR A CB 5195 O OG1 . THR A 672 ? 1.7612 2.2823 1.5708 -0.3715 -0.2214 0.2268 672 THR A OG1 5196 C CG2 . THR A 672 ? 1.5212 2.1119 1.2995 -0.3219 -0.1896 0.2009 672 THR A CG2 5197 N N . GLU A 673 ? 1.5747 1.9693 1.3494 -0.4032 -0.2435 0.2718 673 GLU A N 5198 C CA . GLU A 673 ? 1.8358 2.2249 1.6028 -0.4463 -0.2561 0.3020 673 GLU A CA 5199 C C . GLU A 673 ? 1.8702 2.1950 1.6593 -0.4687 -0.2817 0.3145 673 GLU A C 5200 O O . GLU A 673 ? 1.8593 2.1273 1.6603 -0.4456 -0.2896 0.3008 673 GLU A O 5201 C CB . GLU A 673 ? 1.8059 2.1736 1.5431 -0.4412 -0.2557 0.3101 673 GLU A CB 5202 C CG . GLU A 673 ? 1.7152 2.1501 1.4269 -0.4243 -0.2348 0.3003 673 GLU A CG 5203 C CD . GLU A 673 ? 1.7887 2.3015 1.4912 -0.4570 -0.2254 0.3181 673 GLU A CD 5204 O OE1 . GLU A 673 ? 1.7762 2.3618 1.4818 -0.4450 -0.2070 0.3026 673 GLU A OE1 5205 O OE2 . GLU A 673 ? 1.8085 2.3109 1.5019 -0.4946 -0.2362 0.3486 673 GLU A OE2 5206 N N . ASN A 674 ? 1.8189 2.1538 1.6145 -0.5132 -0.2946 0.3410 674 ASN A N 5207 C CA . ASN A 674 ? 1.8937 2.1672 1.7119 -0.5379 -0.3234 0.3542 674 ASN A CA 5208 C C . ASN A 674 ? 1.7854 2.0405 1.6329 -0.5172 -0.3309 0.3293 674 ASN A C 5209 O O . ASN A 674 ? 1.8771 2.0652 1.7375 -0.5105 -0.3507 0.3244 674 ASN A O 5210 C CB . ASN A 674 ? 1.9879 2.1849 1.7928 -0.5349 -0.3393 0.3635 674 ASN A CB 5211 C CG . ASN A 674 ? 2.3958 2.5379 2.2166 -0.5712 -0.3713 0.3868 674 ASN A CG 5212 O OD1 . ASN A 674 ? 2.3309 2.4748 2.1801 -0.5906 -0.3855 0.3888 674 ASN A OD1 5213 N ND2 . ASN A 674 ? 2.9929 3.0835 2.7967 -0.5795 -0.3856 0.4033 674 ASN A ND2 5214 N N . GLN A 675 ? 1.5680 1.8853 1.4244 -0.5050 -0.3154 0.3122 675 GLN A N 5215 C CA . GLN A 675 ? 1.6081 1.9183 1.4862 -0.4803 -0.3203 0.2859 675 GLN A CA 5216 C C . GLN A 675 ? 1.6718 1.9267 1.5414 -0.4365 -0.3172 0.2658 675 GLN A C 5217 O O . GLN A 675 ? 1.6865 1.8978 1.5718 -0.4245 -0.3328 0.2540 675 GLN A O 5218 C CB . GLN A 675 ? 1.6492 1.9339 1.5595 -0.5110 -0.3504 0.2936 675 GLN A CB 5219 C CG . GLN A 675 ? 1.6383 1.9887 1.5711 -0.5476 -0.3523 0.3056 675 GLN A CG 5220 C CD . GLN A 675 ? 1.7331 2.1119 1.6544 -0.5891 -0.3466 0.3413 675 GLN A CD 5221 O OE1 . GLN A 675 ? 1.7205 2.0525 1.6219 -0.5993 -0.3534 0.3607 675 GLN A OE1 5222 N NE2 . GLN A 675 ? 1.6260 2.0840 1.5594 -0.6121 -0.3340 0.3504 675 GLN A NE2 5223 N N . THR A 676 ? 1.7337 1.9921 1.5801 -0.4121 -0.2972 0.2620 676 THR A N 5224 C CA . THR A 676 ? 1.6939 1.9063 1.5361 -0.3714 -0.2905 0.2460 676 THR A CA 5225 C C . THR A 676 ? 1.6246 1.8771 1.4522 -0.3355 -0.2642 0.2292 676 THR A C 5226 O O . THR A 676 ? 1.6956 1.9997 1.5096 -0.3418 -0.2518 0.2323 676 THR A O 5227 C CB . THR A 676 ? 1.6141 1.7670 1.4499 -0.3764 -0.2993 0.2597 676 THR A CB 5228 O OG1 . THR A 676 ? 1.6442 1.8253 1.4585 -0.3885 -0.2905 0.2724 676 THR A OG1 5229 C CG2 . THR A 676 ? 1.6787 1.7831 1.5297 -0.4077 -0.3285 0.2748 676 THR A CG2 5230 N N . ARG A 677 ? 1.4668 1.6961 1.2973 -0.2970 -0.2562 0.2118 677 ARG A N 5231 C CA . ARG A 677 ? 1.5674 1.8239 1.3862 -0.2606 -0.2339 0.1973 677 ARG A CA 5232 C C . ARG A 677 ? 1.7483 1.9547 1.5651 -0.2382 -0.2277 0.1990 677 ARG A C 5233 O O . ARG A 677 ? 1.8505 2.0089 1.6779 -0.2212 -0.2297 0.1965 677 ARG A O 5234 C CB . ARG A 677 ? 1.5100 1.7837 1.3323 -0.2319 -0.2279 0.1781 677 ARG A CB 5235 C CG . ARG A 677 ? 1.6221 1.9375 1.4548 -0.2534 -0.2393 0.1740 677 ARG A CG 5236 C CD . ARG A 677 ? 1.4479 1.7799 1.2809 -0.2207 -0.2356 0.1524 677 ARG A CD 5237 N NE . ARG A 677 ? 1.4250 1.8039 1.2453 -0.1936 -0.2163 0.1400 677 ARG A NE 5238 C CZ . ARG A 677 ? 1.4101 1.7711 1.2180 -0.1532 -0.2016 0.1318 677 ARG A CZ 5239 N NH1 . ARG A 677 ? 1.5207 1.8226 1.3281 -0.1355 -0.2010 0.1356 677 ARG A NH1 5240 N NH2 . ARG A 677 ? 1.2138 1.6172 1.0118 -0.1302 -0.1879 0.1205 677 ARG A NH2 5241 N N . GLN A 678 ? 1.7162 1.9362 1.5215 -0.2375 -0.2205 0.2023 678 GLN A N 5242 C CA . GLN A 678 ? 1.4968 1.6698 1.3057 -0.2204 -0.2185 0.2043 678 GLN A CA 5243 C C . GLN A 678 ? 1.3716 1.5716 1.1710 -0.1955 -0.2043 0.1941 678 GLN A C 5244 O O . GLN A 678 ? 1.3212 1.5787 1.1059 -0.1990 -0.1986 0.1883 678 GLN A O 5245 C CB . GLN A 678 ? 1.5469 1.6856 1.3553 -0.2502 -0.2359 0.2211 678 GLN A CB 5246 C CG . GLN A 678 ? 1.6683 1.7631 1.4911 -0.2704 -0.2540 0.2306 678 GLN A CG 5247 C CD . GLN A 678 ? 1.6521 1.7143 1.4716 -0.3005 -0.2735 0.2483 678 GLN A CD 5248 O OE1 . GLN A 678 ? 1.5645 1.6524 1.3647 -0.3155 -0.2740 0.2566 678 GLN A OE1 5249 N NE2 . GLN A 678 ? 1.6611 1.6673 1.4977 -0.3075 -0.2904 0.2535 678 GLN A NE2 5250 N N . VAL A 679 ? 1.4322 1.5909 1.2435 -0.1700 -0.1997 0.1914 679 VAL A N 5251 C CA . VAL A 679 ? 1.4692 1.6400 1.2771 -0.1473 -0.1924 0.1822 679 VAL A CA 5252 C C . VAL A 679 ? 1.3814 1.5036 1.2003 -0.1502 -0.2031 0.1889 679 VAL A C 5253 O O . VAL A 679 ? 1.3881 1.4576 1.2297 -0.1450 -0.2057 0.1951 679 VAL A O 5254 C CB . VAL A 679 ? 1.4943 1.6641 1.3113 -0.1091 -0.1770 0.1716 679 VAL A CB 5255 C CG1 . VAL A 679 ? 1.4528 1.5790 1.2867 -0.0998 -0.1731 0.1782 679 VAL A CG1 5256 C CG2 . VAL A 679 ? 1.4043 1.5603 1.2299 -0.0855 -0.1749 0.1653 679 VAL A CG2 5257 N N . VAL A 680 ? 1.3716 1.5145 1.1744 -0.1575 -0.2099 0.1864 680 VAL A N 5258 C CA . VAL A 680 ? 1.3842 1.4850 1.1935 -0.1622 -0.2246 0.1911 680 VAL A CA 5259 C C . VAL A 680 ? 1.4035 1.5033 1.2195 -0.1327 -0.2237 0.1762 680 VAL A C 5260 O O . VAL A 680 ? 1.4111 1.5599 1.2090 -0.1206 -0.2181 0.1629 680 VAL A O 5261 C CB . VAL A 680 ? 1.4251 1.5431 1.2072 -0.1952 -0.2383 0.2019 680 VAL A CB 5262 C CG1 . VAL A 680 ? 1.5361 1.7293 1.2898 -0.2031 -0.2286 0.1976 680 VAL A CG1 5263 C CG2 . VAL A 680 ? 1.5278 1.6179 1.3064 -0.1921 -0.2538 0.2004 680 VAL A CG2 5264 N N . CYS A 681 ? 1.4132 1.4575 1.2591 -0.1207 -0.2307 0.1774 681 CYS A N 5265 C CA . CYS A 681 ? 1.4539 1.4878 1.3155 -0.0932 -0.2339 0.1636 681 CYS A CA 5266 C C . CYS A 681 ? 1.5125 1.5131 1.3791 -0.0997 -0.2561 0.1627 681 CYS A C 5267 O O . CYS A 681 ? 1.5551 1.5136 1.4357 -0.1164 -0.2663 0.1750 681 CYS A O 5268 C CB . CYS A 681 ? 1.5177 1.5166 1.4187 -0.0690 -0.2222 0.1653 681 CYS A CB 5269 S SG . CYS A 681 ? 1.9037 1.9346 1.7964 -0.0566 -0.1981 0.1667 681 CYS A SG 5270 N N . ASP A 682 ? 1.5562 1.5758 1.4112 -0.0842 -0.2654 0.1461 682 ASP A N 5271 C CA . ASP A 682 ? 1.5131 1.5029 1.3703 -0.0855 -0.2892 0.1412 682 ASP A CA 5272 C C . ASP A 682 ? 1.4778 1.4055 1.3900 -0.0703 -0.2975 0.1405 682 ASP A C 5273 O O . ASP A 682 ? 1.4865 1.4075 1.4283 -0.0450 -0.2910 0.1317 682 ASP A O 5274 C CB . ASP A 682 ? 1.5286 1.5598 1.3566 -0.0686 -0.2979 0.1198 682 ASP A CB 5275 C CG . ASP A 682 ? 1.6722 1.7690 1.4469 -0.0863 -0.2902 0.1224 682 ASP A CG 5276 O OD1 . ASP A 682 ? 1.7292 1.8793 1.4826 -0.0689 -0.2847 0.1046 682 ASP A OD1 5277 O OD2 . ASP A 682 ? 1.8245 1.9204 1.5816 -0.1176 -0.2902 0.1426 682 ASP A OD2 5278 N N . LEU A 683 ? 1.5094 1.3921 1.4378 -0.0863 -0.3124 0.1509 683 LEU A N 5279 C CA . LEU A 683 ? 1.4622 1.2884 1.4479 -0.0747 -0.3219 0.1506 683 LEU A CA 5280 C C . LEU A 683 ? 1.4856 1.2925 1.4769 -0.0648 -0.3509 0.1343 683 LEU A C 5281 O O . LEU A 683 ? 1.4495 1.2096 1.4911 -0.0568 -0.3645 0.1319 683 LEU A O 5282 C CB . LEU A 683 ? 1.4125 1.2005 1.4205 -0.0946 -0.3217 0.1688 683 LEU A CB 5283 C CG . LEU A 683 ? 1.3713 1.1697 1.3846 -0.0973 -0.2949 0.1817 683 LEU A CG 5284 C CD1 . LEU A 683 ? 1.3315 1.0917 1.3688 -0.1131 -0.2978 0.1955 683 LEU A CD1 5285 C CD2 . LEU A 683 ? 1.3499 1.1488 1.3968 -0.0704 -0.2758 0.1788 683 LEU A CD2 5286 N N . GLY A 684 ? 1.5368 1.3826 1.4768 -0.0645 -0.3604 0.1226 684 GLY A N 5287 C CA . GLY A 684 ? 1.5922 1.4269 1.5258 -0.0521 -0.3894 0.1039 684 GLY A CA 5288 C C . GLY A 684 ? 1.5355 1.3631 1.4302 -0.0744 -0.4086 0.1121 684 GLY A C 5289 O O . GLY A 684 ? 1.5040 1.3085 1.4015 -0.0990 -0.4069 0.1326 684 GLY A O 5290 N N . ASN A 685 ? 1.5391 1.3862 1.3956 -0.0639 -0.4282 0.0954 685 ASN A N 5291 C CA . ASN A 685 ? 1.5318 1.3795 1.3394 -0.0827 -0.4462 0.1040 685 ASN A CA 5292 C C . ASN A 685 ? 1.5909 1.4129 1.3971 -0.0626 -0.4816 0.0822 685 ASN A C 5293 O O . ASN A 685 ? 1.7734 1.6333 1.5418 -0.0429 -0.4892 0.0617 685 ASN A O 5294 C CB . ASN A 685 ? 1.5325 1.4501 1.2720 -0.0951 -0.4294 0.1110 685 ASN A CB 5295 C CG . ASN A 685 ? 1.5584 1.4773 1.2458 -0.1203 -0.4433 0.1291 685 ASN A CG 5296 O OD1 . ASN A 685 ? 1.7471 1.6114 1.4491 -0.1325 -0.4638 0.1397 685 ASN A OD1 5297 N ND2 . ASN A 685 ? 1.5484 1.5311 1.1755 -0.1283 -0.4320 0.1341 685 ASN A ND2 5298 N N . PRO A 686 ? 1.5273 1.2865 1.3753 -0.0654 -0.5047 0.0843 686 PRO A N 5299 C CA . PRO A 686 ? 1.4899 1.2034 1.3849 -0.0855 -0.4993 0.1052 686 PRO A CA 5300 C C . PRO A 686 ? 1.5133 1.2092 1.4792 -0.0734 -0.4807 0.1034 686 PRO A C 5301 O O . PRO A 686 ? 1.5287 1.2334 1.5182 -0.0480 -0.4799 0.0845 686 PRO A O 5302 C CB . PRO A 686 ? 1.4769 1.1360 1.3892 -0.0849 -0.5369 0.1000 686 PRO A CB 5303 C CG . PRO A 686 ? 1.5872 1.2675 1.4473 -0.0678 -0.5611 0.0797 686 PRO A CG 5304 C CD . PRO A 686 ? 1.5470 1.2782 1.3955 -0.0463 -0.5428 0.0623 686 PRO A CD 5305 N N . MET A 687 ? 1.5139 1.1852 1.5123 -0.0908 -0.4667 0.1235 687 MET A N 5306 C CA . MET A 687 ? 1.4029 1.0493 1.4732 -0.0799 -0.4519 0.1252 687 MET A CA 5307 C C . MET A 687 ? 1.3680 0.9577 1.4974 -0.0764 -0.4783 0.1203 687 MET A C 5308 O O . MET A 687 ? 1.3574 0.9190 1.4919 -0.0941 -0.4886 0.1318 687 MET A O 5309 C CB . MET A 687 ? 1.3805 1.0352 1.4542 -0.0964 -0.4217 0.1471 687 MET A CB 5310 C CG . MET A 687 ? 1.4091 1.0421 1.5516 -0.0847 -0.4026 0.1523 687 MET A CG 5311 S SD . MET A 687 ? 1.4076 1.0534 1.5455 -0.0997 -0.3694 0.1744 687 MET A SD 5312 C CE . MET A 687 ? 1.2714 0.8943 1.4887 -0.0796 -0.3484 0.1794 687 MET A CE 5313 N N . LYS A 688 ? 1.5708 1.1435 1.7486 -0.0531 -0.4910 0.1024 688 LYS A N 5314 C CA . LYS A 688 ? 1.3803 0.9031 1.6159 -0.0474 -0.5219 0.0928 688 LYS A CA 5315 C C . LYS A 688 ? 1.2971 0.7872 1.6049 -0.0558 -0.5089 0.1090 688 LYS A C 5316 O O . LYS A 688 ? 1.4100 0.9151 1.7308 -0.0594 -0.4746 0.1252 688 LYS A O 5317 C CB . LYS A 688 ? 1.3331 0.8481 1.6047 -0.0198 -0.5414 0.0677 688 LYS A CB 5318 C CG . LYS A 688 ? 1.3823 0.9282 1.5851 -0.0064 -0.5601 0.0459 688 LYS A CG 5319 C CD . LYS A 688 ? 1.4201 0.9534 1.6640 0.0235 -0.5844 0.0174 688 LYS A CD 5320 C CE . LYS A 688 ? 1.5792 1.0578 1.8897 0.0283 -0.6206 0.0062 688 LYS A CE 5321 N NZ . LYS A 688 ? 1.6213 1.0841 1.9794 0.0573 -0.6479 -0.0228 688 LYS A NZ 5322 N N . ALA A 689 ? 1.3177 0.7655 1.6709 -0.0575 -0.5371 0.1036 689 ALA A N 5323 C CA . ALA A 689 ? 1.5263 0.9447 1.9529 -0.0642 -0.5281 0.1163 689 ALA A CA 5324 C C . ALA A 689 ? 1.6100 1.0289 2.1093 -0.0507 -0.5032 0.1214 689 ALA A C 5325 O O . ALA A 689 ? 1.4831 0.9026 2.0051 -0.0331 -0.5115 0.1080 689 ALA A O 5326 C CB . ALA A 689 ? 1.4758 0.8508 1.9421 -0.0646 -0.5680 0.1045 689 ALA A CB 5327 N N . GLY A 690 ? 1.5711 0.9900 2.1058 -0.0580 -0.4732 0.1413 690 GLY A N 5328 C CA . GLY A 690 ? 1.5996 1.0185 2.2047 -0.0470 -0.4466 0.1522 690 GLY A CA 5329 C C . GLY A 690 ? 1.6675 1.1204 2.2393 -0.0371 -0.4173 0.1585 690 GLY A C 5330 O O . GLY A 690 ? 1.8231 1.2770 2.4456 -0.0272 -0.3938 0.1706 690 GLY A O 5331 N N . THR A 691 ? 1.6895 1.1712 2.1769 -0.0397 -0.4187 0.1517 691 THR A N 5332 C CA . THR A 691 ? 1.4983 1.0154 1.9494 -0.0292 -0.3945 0.1542 691 THR A CA 5333 C C . THR A 691 ? 1.5688 1.1030 2.0205 -0.0325 -0.3537 0.1772 691 THR A C 5334 O O . THR A 691 ? 1.6149 1.1551 2.0387 -0.0475 -0.3446 0.1865 691 THR A O 5335 C CB . THR A 691 ? 1.2593 0.8100 1.6208 -0.0331 -0.4036 0.1421 691 THR A CB 5336 O OG1 . THR A 691 ? 1.3758 0.9165 1.7314 -0.0235 -0.4395 0.1187 691 THR A OG1 5337 C CG2 . THR A 691 ? 1.2640 0.8550 1.5898 -0.0229 -0.3767 0.1448 691 THR A CG2 5338 N N . GLN A 692 ? 1.5541 1.0946 2.0369 -0.0171 -0.3313 0.1859 692 GLN A N 5339 C CA . GLN A 692 ? 1.4160 0.9765 1.8911 -0.0153 -0.2923 0.2068 692 GLN A CA 5340 C C . GLN A 692 ? 1.3847 0.9757 1.8205 -0.0007 -0.2778 0.2050 692 GLN A C 5341 O O . GLN A 692 ? 1.6169 1.1995 2.0863 0.0154 -0.2810 0.2022 692 GLN A O 5342 C CB . GLN A 692 ? 1.6209 1.1594 2.1771 -0.0099 -0.2736 0.2259 692 GLN A CB 5343 C CG . GLN A 692 ? 1.7931 1.3047 2.3965 -0.0223 -0.2860 0.2272 692 GLN A CG 5344 C CD . GLN A 692 ? 1.8502 1.3499 2.5339 -0.0169 -0.2617 0.2480 692 GLN A CD 5345 O OE1 . GLN A 692 ? 1.6215 1.1345 2.3160 -0.0053 -0.2313 0.2658 692 GLN A OE1 5346 N NE2 . GLN A 692 ? 1.9682 1.4451 2.7083 -0.0248 -0.2746 0.2466 692 GLN A NE2 5347 N N . LEU A 693 ? 1.2514 0.8769 1.6193 -0.0061 -0.2639 0.2058 693 LEU A N 5348 C CA . LEU A 693 ? 1.3402 0.9990 1.6673 0.0078 -0.2514 0.2018 693 LEU A CA 5349 C C . LEU A 693 ? 1.4088 1.0842 1.7274 0.0145 -0.2159 0.2211 693 LEU A C 5350 O O . LEU A 693 ? 1.3845 1.0602 1.6975 0.0041 -0.2023 0.2324 693 LEU A O 5351 C CB . LEU A 693 ? 1.2574 0.9505 1.5123 -0.0014 -0.2647 0.1850 693 LEU A CB 5352 C CG . LEU A 693 ? 1.3433 1.0295 1.5912 -0.0021 -0.2988 0.1636 693 LEU A CG 5353 C CD1 . LEU A 693 ? 1.5143 1.2453 1.6882 -0.0081 -0.3043 0.1505 693 LEU A CD1 5354 C CD2 . LEU A 693 ? 1.3416 1.0092 1.6358 0.0204 -0.3114 0.1527 693 LEU A CD2 5355 N N . LEU A 694 ? 1.4212 1.1095 1.7376 0.0341 -0.2033 0.2234 694 LEU A N 5356 C CA . LEU A 694 ? 1.4121 1.1161 1.7160 0.0450 -0.1711 0.2414 694 LEU A CA 5357 C C . LEU A 694 ? 1.4492 1.1902 1.7000 0.0579 -0.1673 0.2307 694 LEU A C 5358 O O . LEU A 694 ? 1.7060 1.4460 1.9663 0.0734 -0.1773 0.2216 694 LEU A O 5359 C CB . LEU A 694 ? 1.6225 1.2985 1.9912 0.0588 -0.1549 0.2631 694 LEU A CB 5360 C CG . LEU A 694 ? 1.6939 1.3690 2.0761 0.0605 -0.1228 0.2883 694 LEU A CG 5361 C CD1 . LEU A 694 ? 1.7416 1.4513 2.0606 0.0695 -0.1021 0.2909 694 LEU A CD1 5362 C CD2 . LEU A 694 ? 1.6446 1.3067 2.0445 0.0417 -0.1283 0.2879 694 LEU A CD2 5363 N N . ALA A 695 ? 1.3589 1.1323 1.5570 0.0524 -0.1548 0.2302 695 ALA A N 5364 C CA . ALA A 695 ? 1.4817 1.2953 1.6303 0.0634 -0.1515 0.2187 695 ALA A CA 5365 C C . ALA A 695 ? 1.4430 1.2810 1.5563 0.0661 -0.1287 0.2279 695 ALA A C 5366 O O . ALA A 695 ? 1.4958 1.3313 1.6019 0.0512 -0.1237 0.2340 695 ALA A O 5367 C CB . ALA A 695 ? 1.4638 1.3048 1.5748 0.0499 -0.1736 0.1959 695 ALA A CB 5368 N N . GLY A 696 ? 1.3954 1.2556 1.4869 0.0870 -0.1176 0.2271 696 GLY A N 5369 C CA . GLY A 696 ? 1.4209 1.3068 1.4751 0.0934 -0.0993 0.2320 696 GLY A CA 5370 C C . GLY A 696 ? 1.4360 1.3688 1.4404 0.0841 -0.1085 0.2119 696 GLY A C 5371 O O . GLY A 696 ? 1.4029 1.3554 1.3972 0.0817 -0.1242 0.1948 696 GLY A O 5372 N N . LEU A 697 ? 1.5173 1.4701 1.4923 0.0799 -0.0990 0.2135 697 LEU A N 5373 C CA . LEU A 697 ? 1.4306 1.4305 1.3642 0.0696 -0.1063 0.1968 697 LEU A CA 5374 C C . LEU A 697 ? 1.4300 1.4534 1.3363 0.0885 -0.0921 0.1971 697 LEU A C 5375 O O . LEU A 697 ? 1.4230 1.4334 1.3272 0.0913 -0.0813 0.2074 697 LEU A O 5376 C CB . LEU A 697 ? 1.4199 1.4210 1.3462 0.0372 -0.1179 0.1950 697 LEU A CB 5377 C CG . LEU A 697 ? 1.4033 1.3857 1.3470 0.0167 -0.1355 0.1929 697 LEU A CG 5378 C CD1 . LEU A 697 ? 1.3987 1.3791 1.3323 -0.0145 -0.1469 0.1948 697 LEU A CD1 5379 C CD2 . LEU A 697 ? 1.4217 1.4347 1.3517 0.0198 -0.1465 0.1767 697 LEU A CD2 5380 N N . ARG A 698 ? 1.4560 1.5151 1.3408 0.1036 -0.0936 0.1838 698 ARG A N 5381 C CA . ARG A 698 ? 1.3922 1.4740 1.2504 0.1253 -0.0830 0.1820 698 ARG A CA 5382 C C . ARG A 698 ? 1.4057 1.5305 1.2351 0.1090 -0.0900 0.1675 698 ARG A C 5383 O O . ARG A 698 ? 1.3953 1.5543 1.2175 0.0903 -0.1022 0.1534 698 ARG A O 5384 C CB . ARG A 698 ? 1.4264 1.5222 1.2797 0.1536 -0.0827 0.1749 698 ARG A CB 5385 C CG . ARG A 698 ? 1.5272 1.5782 1.4074 0.1761 -0.0725 0.1945 698 ARG A CG 5386 C CD . ARG A 698 ? 1.3875 1.4492 1.2611 0.2058 -0.0747 0.1880 698 ARG A CD 5387 N NE . ARG A 698 ? 1.4912 1.5604 1.3801 0.2033 -0.0923 0.1710 698 ARG A NE 5388 C CZ . ARG A 698 ? 1.7167 1.7910 1.6076 0.2283 -0.0998 0.1616 698 ARG A CZ 5389 N NH1 . ARG A 698 ? 1.8855 1.9561 1.7635 0.2563 -0.0911 0.1703 698 ARG A NH1 5390 N NH2 . ARG A 698 ? 1.5539 1.6363 1.4582 0.2272 -0.1177 0.1428 698 ARG A NH2 5391 N N . PHE A 699 ? 1.4661 1.5902 1.2806 0.1169 -0.0826 0.1713 699 PHE A N 5392 C CA . PHE A 699 ? 1.6217 1.7824 1.4146 0.1028 -0.0913 0.1577 699 PHE A CA 5393 C C . PHE A 699 ? 1.7337 1.9134 1.5013 0.1322 -0.0849 0.1516 699 PHE A C 5394 O O . PHE A 699 ? 1.6817 1.8397 1.4453 0.1626 -0.0713 0.1626 699 PHE A O 5395 C CB . PHE A 699 ? 1.5534 1.6913 1.3549 0.0777 -0.0969 0.1639 699 PHE A CB 5396 C CG . PHE A 699 ? 1.4926 1.6180 1.3128 0.0452 -0.1082 0.1674 699 PHE A CG 5397 C CD1 . PHE A 699 ? 1.6113 1.7690 1.4240 0.0151 -0.1230 0.1584 699 PHE A CD1 5398 C CD2 . PHE A 699 ? 1.4657 1.5479 1.3119 0.0448 -0.1046 0.1806 699 PHE A CD2 5399 C CE1 . PHE A 699 ? 1.6536 1.7993 1.4780 -0.0134 -0.1337 0.1635 699 PHE A CE1 5400 C CE2 . PHE A 699 ? 1.4976 1.5669 1.3583 0.0172 -0.1176 0.1825 699 PHE A CE2 5401 C CZ . PHE A 699 ? 1.6315 1.7319 1.4781 -0.0112 -0.1321 0.1744 699 PHE A CZ 5402 N N . SER A 700 ? 1.6429 1.8633 1.3942 0.1229 -0.0956 0.1350 700 SER A N 5403 C CA . SER A 700 ? 1.6387 1.8789 1.3651 0.1499 -0.0942 0.1255 700 SER A CA 5404 C C . SER A 700 ? 1.5636 1.8108 1.2842 0.1348 -0.1053 0.1175 700 SER A C 5405 O O . SER A 700 ? 1.4222 1.6984 1.1502 0.1045 -0.1200 0.1070 700 SER A O 5406 C CB . SER A 700 ? 1.7935 2.0838 1.5093 0.1608 -0.1001 0.1074 700 SER A CB 5407 O OG . SER A 700 ? 1.8997 2.2079 1.5913 0.1888 -0.1013 0.0970 700 SER A OG 5408 N N . VAL A 701 ? 1.5710 1.7920 1.2791 0.1564 -0.0987 0.1229 701 VAL A N 5409 C CA . VAL A 701 ? 1.5105 1.7337 1.2132 0.1477 -0.1120 0.1123 701 VAL A CA 5410 C C . VAL A 701 ? 1.5928 1.8443 1.2674 0.1772 -0.1174 0.0951 701 VAL A C 5411 O O . VAL A 701 ? 1.6515 1.8962 1.3037 0.2151 -0.1038 0.1001 701 VAL A O 5412 C CB . VAL A 701 ? 1.4744 1.6512 1.1823 0.1527 -0.1041 0.1256 701 VAL A CB 5413 C CG1 . VAL A 701 ? 1.5406 1.7182 1.2455 0.1432 -0.1228 0.1109 701 VAL A CG1 5414 C CG2 . VAL A 701 ? 1.4852 1.6319 1.2229 0.1269 -0.0997 0.1421 701 VAL A CG2 5415 N N . HIS A 702 ? 1.6319 1.9145 1.3090 0.1599 -0.1384 0.0756 702 HIS A N 5416 C CA . HIS A 702 ? 1.8542 2.1648 1.5083 0.1870 -0.1484 0.0555 702 HIS A CA 5417 C C . HIS A 702 ? 1.9170 2.2069 1.5613 0.1966 -0.1594 0.0471 702 HIS A C 5418 O O . HIS A 702 ? 1.7667 2.0348 1.3841 0.2341 -0.1478 0.0512 702 HIS A O 5419 C CB . HIS A 702 ? 1.8481 2.2131 1.5162 0.1646 -0.1662 0.0365 702 HIS A CB 5420 C CG . HIS A 702 ? 1.8482 2.2357 1.5330 0.1439 -0.1587 0.0432 702 HIS A CG 5421 N ND1 . HIS A 702 ? 1.8482 2.2462 1.5216 0.1699 -0.1459 0.0448 702 HIS A ND1 5422 C CD2 . HIS A 702 ? 1.7455 2.1471 1.4557 0.1018 -0.1635 0.0481 702 HIS A CD2 5423 C CE1 . HIS A 702 ? 1.7893 2.2083 1.4809 0.1461 -0.1438 0.0473 702 HIS A CE1 5424 N NE2 . HIS A 702 ? 1.6717 2.0947 1.3837 0.1049 -0.1531 0.0502 702 HIS A NE2 5425 N N . GLN A 703 ? 1.9552 2.2518 1.6217 0.1627 -0.1819 0.0364 703 GLN A N 5426 C CA . GLN A 703 ? 1.9226 2.1966 1.5875 0.1660 -0.1982 0.0257 703 GLN A CA 5427 C C . GLN A 703 ? 1.9080 2.1944 1.6056 0.1211 -0.2264 0.0157 703 GLN A C 5428 O O . GLN A 703 ? 1.9034 2.2268 1.6194 0.0930 -0.2330 0.0138 703 GLN A O 5429 C CB . GLN A 703 ? 1.7823 2.0676 1.4137 0.2110 -0.2049 0.0057 703 GLN A CB 5430 C CG . GLN A 703 ? 1.6300 1.9651 1.2609 0.2132 -0.2216 -0.0158 703 GLN A CG 5431 C CD . GLN A 703 ? 1.9574 2.3001 1.5544 0.2585 -0.2331 -0.0382 703 GLN A CD 5432 O OE1 . GLN A 703 ? 2.0456 2.3606 1.6257 0.2794 -0.2380 -0.0440 703 GLN A OE1 5433 N NE2 . GLN A 703 ? 2.0618 2.4434 1.6474 0.2764 -0.2385 -0.0524 703 GLN A NE2 5434 N N . GLN A 704 ? 1.8570 2.1129 1.5627 0.1148 -0.2431 0.0099 704 GLN A N 5435 C CA . GLN A 704 ? 1.8905 2.1528 1.6274 0.0757 -0.2748 -0.0005 704 GLN A CA 5436 C C . GLN A 704 ? 1.9923 2.2450 1.7214 0.0991 -0.3001 -0.0264 704 GLN A C 5437 O O . GLN A 704 ? 1.9689 2.1834 1.6873 0.1189 -0.2999 -0.0280 704 GLN A O 5438 C CB . GLN A 704 ? 1.7640 1.9917 1.5268 0.0365 -0.2773 0.0188 704 GLN A CB 5439 C CG . GLN A 704 ? 1.6671 1.9206 1.4584 -0.0141 -0.2849 0.0301 704 GLN A CG 5440 C CD . GLN A 704 ? 1.7921 2.0626 1.6107 -0.0441 -0.3189 0.0167 704 GLN A CD 5441 O OE1 . GLN A 704 ? 2.0012 2.2616 1.8191 -0.0263 -0.3406 -0.0044 704 GLN A OE1 5442 N NE2 . GLN A 704 ? 1.6740 1.9711 1.5180 -0.0897 -0.3245 0.0294 704 GLN A NE2 5443 N N . SER A 705 ? 2.0774 2.3668 1.8144 0.0973 -0.3232 -0.0483 705 SER A N 5444 C CA . SER A 705 ? 2.1894 2.4749 1.9166 0.1257 -0.3503 -0.0781 705 SER A CA 5445 C C . SER A 705 ? 2.1936 2.4597 1.8720 0.1842 -0.3307 -0.0820 705 SER A C 5446 O O . SER A 705 ? 2.1379 2.4186 1.7877 0.2107 -0.3035 -0.0722 705 SER A O 5447 C CB . SER A 705 ? 2.1049 2.3577 1.8632 0.0980 -0.3822 -0.0852 705 SER A CB 5448 O OG . SER A 705 ? 1.9922 2.2624 1.7953 0.0423 -0.3995 -0.0769 705 SER A OG 5449 N N . GLU A 706 ? 2.0366 2.2703 1.7061 0.2044 -0.3448 -0.0956 706 GLU A N 5450 C CA . GLU A 706 ? 1.7790 1.9941 1.4028 0.2582 -0.3233 -0.0958 706 GLU A CA 5451 C C . GLU A 706 ? 1.8289 2.0008 1.4609 0.2578 -0.3264 -0.0940 706 GLU A C 5452 O O . GLU A 706 ? 1.7603 1.9143 1.4318 0.2173 -0.3494 -0.0948 706 GLU A O 5453 C CB . GLU A 706 ? 1.6631 1.8982 1.2520 0.3054 -0.3406 -0.1270 706 GLU A CB 5454 C CG . GLU A 706 ? 1.7015 1.9779 1.2742 0.3179 -0.3335 -0.1289 706 GLU A CG 5455 C CD . GLU A 706 ? 1.9450 2.2451 1.5015 0.3487 -0.3660 -0.1661 706 GLU A CD 5456 O OE1 . GLU A 706 ? 2.2447 2.5273 1.7974 0.3653 -0.3927 -0.1908 706 GLU A OE1 5457 O OE2 . GLU A 706 ? 1.6327 1.9689 1.1814 0.3578 -0.3669 -0.1727 706 GLU A OE2 5458 N N . MET A 707 ? 1.9812 2.1382 1.5763 0.3035 -0.3034 -0.0909 707 MET A N 5459 C CA . MET A 707 ? 2.0587 2.1803 1.6585 0.3122 -0.3035 -0.0921 707 MET A CA 5460 C C . MET A 707 ? 1.9210 2.0157 1.5633 0.2652 -0.2969 -0.0675 707 MET A C 5461 O O . MET A 707 ? 1.9556 2.0225 1.6229 0.2498 -0.3193 -0.0768 707 MET A O 5462 C CB . MET A 707 ? 2.0932 2.2064 1.6988 0.3218 -0.3482 -0.1303 707 MET A CB 5463 C CG . MET A 707 ? 2.2181 2.3598 1.7917 0.3585 -0.3680 -0.1607 707 MET A CG 5464 S SD . MET A 707 ? 2.5986 2.7277 2.1927 0.3611 -0.4291 -0.2077 707 MET A SD 5465 C CE . MET A 707 ? 1.9614 2.1309 1.5228 0.3980 -0.4487 -0.2383 707 MET A CE 5466 N N . ASP A 708 ? 1.8556 1.9571 1.5054 0.2444 -0.2688 -0.0380 708 ASP A N 5467 C CA . ASP A 708 ? 1.8452 1.9237 1.5333 0.1996 -0.2649 -0.0155 708 ASP A CA 5468 C C . ASP A 708 ? 1.8775 1.9295 1.5659 0.2139 -0.2334 0.0059 708 ASP A C 5469 O O . ASP A 708 ? 1.8687 1.8982 1.5886 0.1809 -0.2314 0.0228 708 ASP A O 5470 C CB . ASP A 708 ? 1.8451 1.9470 1.5462 0.1657 -0.2566 0.0018 708 ASP A CB 5471 C CG . ASP A 708 ? 1.8383 1.9574 1.5651 0.1257 -0.2909 -0.0107 708 ASP A CG 5472 O OD1 . ASP A 708 ? 2.0126 2.1382 1.7379 0.1353 -0.3201 -0.0372 708 ASP A OD1 5473 O OD2 . ASP A 708 ? 1.6602 1.7877 1.4097 0.0850 -0.2891 0.0061 708 ASP A OD2 5474 N N . THR A 709 ? 1.9058 1.9619 1.5602 0.2628 -0.2094 0.0058 709 THR A N 5475 C CA . THR A 709 ? 1.9387 1.9767 1.5954 0.2796 -0.1749 0.0286 709 THR A CA 5476 C C . THR A 709 ? 1.9650 1.9988 1.6442 0.2513 -0.1519 0.0599 709 THR A C 5477 O O . THR A 709 ? 2.1687 2.2233 1.8327 0.2550 -0.1386 0.0697 709 THR A O 5478 C CB . THR A 709 ? 2.0485 2.0565 1.7306 0.2744 -0.1884 0.0198 709 THR A CB 5479 O OG1 . THR A 709 ? 2.1852 2.1932 1.8594 0.2838 -0.2258 -0.0148 709 THR A OG1 5480 C CG2 . THR A 709 ? 2.0617 2.0638 1.7337 0.3120 -0.1532 0.0329 709 THR A CG2 5481 N N . SER A 710 ? 1.8775 1.8841 1.5935 0.2246 -0.1501 0.0733 710 SER A N 5482 C CA . SER A 710 ? 1.8406 1.8401 1.5799 0.2003 -0.1310 0.1005 710 SER A CA 5483 C C . SER A 710 ? 1.7973 1.8041 1.5531 0.1553 -0.1532 0.0996 710 SER A C 5484 O O . SER A 710 ? 1.8343 1.8524 1.5871 0.1402 -0.1822 0.0805 710 SER A O 5485 C CB . SER A 710 ? 2.0030 1.9712 1.7762 0.1929 -0.1204 0.1144 710 SER A CB 5486 O OG . SER A 710 ? 1.9139 1.8606 1.7105 0.1670 -0.1524 0.0998 710 SER A OG 5487 N N . VAL A 711 ? 1.7567 1.7584 1.5310 0.1348 -0.1395 0.1204 711 VAL A N 5488 C CA . VAL A 711 ? 1.7430 1.7537 1.5316 0.0934 -0.1565 0.1223 711 VAL A CA 5489 C C . VAL A 711 ? 1.8719 1.8553 1.6919 0.0686 -0.1510 0.1413 711 VAL A C 5490 O O . VAL A 711 ? 1.9546 1.9248 1.7837 0.0856 -0.1264 0.1568 711 VAL A O 5491 C CB . VAL A 711 ? 1.6950 1.7431 1.4631 0.0998 -0.1478 0.1222 711 VAL A CB 5492 C CG1 . VAL A 711 ? 1.6878 1.7339 1.4486 0.1285 -0.1155 0.1397 711 VAL A CG1 5493 C CG2 . VAL A 711 ? 1.6402 1.7040 1.4227 0.0585 -0.1623 0.1244 711 VAL A CG2 5494 N N . LYS A 712 ? 1.8176 1.7923 1.6552 0.0286 -0.1749 0.1408 712 LYS A N 5495 C CA . LYS A 712 ? 1.7728 1.7162 1.6393 0.0058 -0.1767 0.1552 712 LYS A CA 5496 C C . LYS A 712 ? 1.8148 1.7697 1.6854 -0.0162 -0.1729 0.1671 712 LYS A C 5497 O O . LYS A 712 ? 1.9214 1.9097 1.7768 -0.0285 -0.1786 0.1627 712 LYS A O 5498 C CB . LYS A 712 ? 1.8242 1.7421 1.7068 -0.0225 -0.2079 0.1488 712 LYS A CB 5499 C CG . LYS A 712 ? 1.8691 1.8048 1.7475 -0.0599 -0.2326 0.1462 712 LYS A CG 5500 C CD . LYS A 712 ? 1.8866 1.7883 1.7856 -0.0928 -0.2625 0.1484 712 LYS A CD 5501 C CE . LYS A 712 ? 1.8614 1.7819 1.7582 -0.1341 -0.2826 0.1539 712 LYS A CE 5502 N NZ . LYS A 712 ? 1.6487 1.5909 1.5388 -0.1461 -0.2666 0.1681 712 LYS A NZ 5503 N N . PHE A 713 ? 1.6948 1.6241 1.5880 -0.0189 -0.1636 0.1807 713 PHE A N 5504 C CA . PHE A 713 ? 1.5209 1.4534 1.4212 -0.0405 -0.1658 0.1897 713 PHE A CA 5505 C C . PHE A 713 ? 1.4850 1.3786 1.4123 -0.0636 -0.1810 0.1972 713 PHE A C 5506 O O . PHE A 713 ? 1.4570 1.3208 1.4084 -0.0503 -0.1735 0.2018 713 PHE A O 5507 C CB . PHE A 713 ? 1.4972 1.4374 1.3996 -0.0162 -0.1409 0.1976 713 PHE A CB 5508 C CG . PHE A 713 ? 1.5833 1.5636 1.4575 0.0018 -0.1305 0.1907 713 PHE A CG 5509 C CD1 . PHE A 713 ? 1.7045 1.6958 1.5606 0.0307 -0.1197 0.1850 713 PHE A CD1 5510 C CD2 . PHE A 713 ? 1.5803 1.5887 1.4453 -0.0078 -0.1325 0.1886 713 PHE A CD2 5511 C CE1 . PHE A 713 ? 1.6299 1.6567 1.4600 0.0487 -0.1126 0.1778 713 PHE A CE1 5512 C CE2 . PHE A 713 ? 1.5298 1.5761 1.3717 0.0102 -0.1246 0.1804 713 PHE A CE2 5513 C CZ . PHE A 713 ? 1.5369 1.5909 1.3618 0.0381 -0.1154 0.1753 713 PHE A CZ 5514 N N . ASP A 714 ? 1.4857 1.3812 1.4093 -0.0977 -0.2021 0.1990 714 ASP A N 5515 C CA . ASP A 714 ? 1.4851 1.3425 1.4295 -0.1205 -0.2207 0.2061 714 ASP A CA 5516 C C . ASP A 714 ? 1.4787 1.3341 1.4285 -0.1294 -0.2192 0.2144 714 ASP A C 5517 O O . ASP A 714 ? 1.5111 1.3983 1.4401 -0.1409 -0.2200 0.2145 714 ASP A O 5518 C CB . ASP A 714 ? 1.6027 1.4562 1.5390 -0.1533 -0.2494 0.2051 714 ASP A CB 5519 C CG . ASP A 714 ? 1.8414 1.6848 1.7803 -0.1444 -0.2586 0.1941 714 ASP A CG 5520 O OD1 . ASP A 714 ? 1.9953 1.8577 1.9207 -0.1596 -0.2733 0.1885 714 ASP A OD1 5521 O OD2 . ASP A 714 ? 1.7894 1.6076 1.7459 -0.1214 -0.2517 0.1902 714 ASP A OD2 5522 N N . LEU A 715 ? 1.4195 1.2394 1.3989 -0.1228 -0.2181 0.2196 715 LEU A N 5523 C CA . LEU A 715 ? 1.3446 1.1581 1.3338 -0.1262 -0.2188 0.2245 715 LEU A CA 5524 C C . LEU A 715 ? 1.3430 1.1162 1.3521 -0.1461 -0.2422 0.2290 715 LEU A C 5525 O O . LEU A 715 ? 1.3373 1.0781 1.3727 -0.1428 -0.2476 0.2293 715 LEU A O 5526 C CB . LEU A 715 ? 1.3103 1.1202 1.3233 -0.0955 -0.1947 0.2266 715 LEU A CB 5527 C CG . LEU A 715 ? 1.3295 1.1668 1.3297 -0.0680 -0.1695 0.2248 715 LEU A CG 5528 C CD1 . LEU A 715 ? 1.3005 1.1267 1.3296 -0.0425 -0.1488 0.2324 715 LEU A CD1 5529 C CD2 . LEU A 715 ? 1.4408 1.3220 1.4037 -0.0719 -0.1691 0.2181 715 LEU A CD2 5530 N N . GLN A 716 ? 1.3181 1.0951 1.3130 -0.1647 -0.2567 0.2316 716 GLN A N 5531 C CA . GLN A 716 ? 1.3429 1.0814 1.3540 -0.1797 -0.2796 0.2357 716 GLN A CA 5532 C C . GLN A 716 ? 1.3508 1.1014 1.3457 -0.1860 -0.2870 0.2357 716 GLN A C 5533 O O . GLN A 716 ? 1.3226 1.1151 1.2885 -0.1849 -0.2773 0.2329 716 GLN A O 5534 C CB . GLN A 716 ? 1.3470 1.0662 1.3473 -0.2071 -0.3046 0.2406 716 GLN A CB 5535 C CG . GLN A 716 ? 1.5032 1.2470 1.4634 -0.2359 -0.3184 0.2476 716 GLN A CG 5536 C CD . GLN A 716 ? 1.5575 1.2665 1.5143 -0.2648 -0.3494 0.2572 716 GLN A CD 5537 O OE1 . GLN A 716 ? 1.5217 1.2472 1.4486 -0.2919 -0.3615 0.2673 716 GLN A OE1 5538 N NE2 . GLN A 716 ? 1.4456 1.1068 1.4349 -0.2592 -0.3626 0.2553 716 GLN A NE2 5539 N N . ILE A 717 ? 1.3221 1.0373 1.3361 -0.1903 -0.3053 0.2367 717 ILE A N 5540 C CA . ILE A 717 ? 1.2916 1.0136 1.2900 -0.1931 -0.3165 0.2340 717 ILE A CA 5541 C C . ILE A 717 ? 1.3406 1.0500 1.3103 -0.2221 -0.3442 0.2421 717 ILE A C 5542 O O . ILE A 717 ? 1.3574 1.0292 1.3411 -0.2348 -0.3616 0.2480 717 ILE A O 5543 C CB . ILE A 717 ? 1.2717 0.9630 1.3145 -0.1731 -0.3191 0.2276 717 ILE A CB 5544 C CG1 . ILE A 717 ? 1.2573 0.9579 1.3311 -0.1460 -0.2910 0.2248 717 ILE A CG1 5545 C CG2 . ILE A 717 ? 1.2939 0.9926 1.3188 -0.1720 -0.3338 0.2206 717 ILE A CG2 5546 C CD1 . ILE A 717 ? 1.2383 0.9093 1.3648 -0.1280 -0.2922 0.2213 717 ILE A CD1 5547 N N . GLN A 718 ? 1.3369 1.0788 1.2659 -0.2317 -0.3484 0.2430 718 GLN A N 5548 C CA . GLN A 718 ? 1.3587 1.0926 1.2547 -0.2590 -0.3728 0.2545 718 GLN A CA 5549 C C . GLN A 718 ? 1.3871 1.1249 1.2642 -0.2522 -0.3851 0.2485 718 GLN A C 5550 O O . GLN A 718 ? 1.3976 1.1612 1.2763 -0.2300 -0.3725 0.2348 718 GLN A O 5551 C CB . GLN A 718 ? 1.4215 1.1984 1.2782 -0.2831 -0.3666 0.2661 718 GLN A CB 5552 C CG . GLN A 718 ? 1.5884 1.3568 1.4605 -0.2931 -0.3630 0.2713 718 GLN A CG 5553 C CD . GLN A 718 ? 1.7363 1.5469 1.5763 -0.3189 -0.3601 0.2828 718 GLN A CD 5554 O OE1 . GLN A 718 ? 1.7209 1.5734 1.5270 -0.3292 -0.3565 0.2879 718 GLN A OE1 5555 N NE2 . GLN A 718 ? 1.8132 1.6151 1.6661 -0.3290 -0.3623 0.2859 718 GLN A NE2 5556 N N . SER A 719 ? 1.4095 1.1204 1.2678 -0.2698 -0.4120 0.2578 719 SER A N 5557 C CA . SER A 719 ? 1.4295 1.1435 1.2627 -0.2628 -0.4275 0.2515 719 SER A CA 5558 C C . SER A 719 ? 1.4528 1.1600 1.2400 -0.2907 -0.4504 0.2703 719 SER A C 5559 O O . SER A 719 ? 1.4565 1.1522 1.2369 -0.3168 -0.4556 0.2888 719 SER A O 5560 C CB . SER A 719 ? 1.4151 1.0823 1.2947 -0.2398 -0.4422 0.2362 719 SER A CB 5561 O OG . SER A 719 ? 1.4115 1.0250 1.3241 -0.2492 -0.4592 0.2431 719 SER A OG 5562 N N . SER A 720 ? 1.4728 1.1859 1.2278 -0.2840 -0.4653 0.2656 720 SER A N 5563 C CA . SER A 720 ? 1.5001 1.2140 1.2019 -0.3083 -0.4845 0.2857 720 SER A CA 5564 C C . SER A 720 ? 1.5388 1.1858 1.2503 -0.3117 -0.5204 0.2896 720 SER A C 5565 O O . SER A 720 ? 1.6863 1.3241 1.3537 -0.3311 -0.5404 0.3084 720 SER A O 5566 C CB . SER A 720 ? 1.5154 1.2831 1.1653 -0.2980 -0.4793 0.2792 720 SER A CB 5567 O OG . SER A 720 ? 1.5335 1.3664 1.1737 -0.2959 -0.4476 0.2756 720 SER A OG 5568 N N . ASN A 721 ? 1.5619 1.1637 1.3319 -0.2927 -0.5285 0.2729 721 ASN A N 5569 C CA . ASN A 721 ? 1.7007 1.2397 1.4891 -0.2921 -0.5636 0.2722 721 ASN A CA 5570 C C . ASN A 721 ? 1.8467 1.3507 1.6276 -0.3222 -0.5807 0.2962 721 ASN A C 5571 O O . ASN A 721 ? 1.8783 1.3923 1.6698 -0.3376 -0.5646 0.3067 721 ASN A O 5572 C CB . ASN A 721 ? 1.6206 1.1254 1.4830 -0.2669 -0.5644 0.2503 721 ASN A CB 5573 C CG . ASN A 721 ? 1.5424 1.0718 1.4183 -0.2372 -0.5544 0.2269 721 ASN A CG 5574 O OD1 . ASN A 721 ? 1.5739 1.1557 1.4220 -0.2321 -0.5308 0.2240 721 ASN A OD1 5575 N ND2 . ASN A 721 ? 1.6595 1.1509 1.5813 -0.2171 -0.5746 0.2091 721 ASN A ND2 5576 N N . LEU A 722 ? 1.9360 1.3970 1.6989 -0.3289 -0.6160 0.3036 722 LEU A N 5577 C CA . LEU A 722 ? 1.7406 1.1633 1.4916 -0.3576 -0.6385 0.3278 722 LEU A CA 5578 C C . LEU A 722 ? 1.5479 0.9281 1.3643 -0.3561 -0.6426 0.3209 722 LEU A C 5579 O O . LEU A 722 ? 1.6489 1.0149 1.4652 -0.3789 -0.6471 0.3376 722 LEU A O 5580 C CB . LEU A 722 ? 1.9014 1.2848 1.6169 -0.3608 -0.6779 0.3358 722 LEU A CB 5581 C CG . LEU A 722 ? 1.8512 1.2676 1.4844 -0.3779 -0.6809 0.3595 722 LEU A CG 5582 C CD1 . LEU A 722 ? 2.1758 1.6587 1.7805 -0.3594 -0.6537 0.3453 722 LEU A CD1 5583 C CD2 . LEU A 722 ? 1.7990 1.1670 1.3999 -0.3784 -0.7234 0.3674 722 LEU A CD2 5584 N N . PHE A 723 ? 1.5241 0.8857 1.3982 -0.3287 -0.6414 0.2961 723 PHE A N 5585 C CA . PHE A 723 ? 1.4747 0.8008 1.4137 -0.3229 -0.6434 0.2875 723 PHE A CA 5586 C C . PHE A 723 ? 1.4639 0.8177 1.4530 -0.2996 -0.6081 0.2694 723 PHE A C 5587 O O . PHE A 723 ? 1.4319 0.8077 1.4281 -0.2799 -0.5962 0.2558 723 PHE A O 5588 C CB . PHE A 723 ? 1.6388 0.9065 1.6105 -0.3137 -0.6811 0.2781 723 PHE A CB 5589 C CG . PHE A 723 ? 1.8046 1.0376 1.7277 -0.3347 -0.7193 0.2969 723 PHE A CG 5590 C CD1 . PHE A 723 ? 1.8402 1.0393 1.7633 -0.3562 -0.7376 0.3127 723 PHE A CD1 5591 C CD2 . PHE A 723 ? 1.7391 0.9717 1.6155 -0.3314 -0.7387 0.2988 723 PHE A CD2 5592 C CE1 . PHE A 723 ? 2.0042 1.1678 1.8826 -0.3762 -0.7741 0.3334 723 PHE A CE1 5593 C CE2 . PHE A 723 ? 1.8136 1.0138 1.6408 -0.3500 -0.7735 0.3193 723 PHE A CE2 5594 C CZ . PHE A 723 ? 2.1524 1.3168 1.9811 -0.3735 -0.7910 0.3382 723 PHE A CZ 5595 N N . ASP A 724 ? 1.5956 0.9468 1.6185 -0.3008 -0.5934 0.2693 724 ASP A N 5596 C CA . ASP A 724 ? 1.6279 1.0041 1.6957 -0.2792 -0.5587 0.2561 724 ASP A CA 5597 C C . ASP A 724 ? 1.4941 0.9256 1.5304 -0.2732 -0.5288 0.2554 724 ASP A C 5598 O O . ASP A 724 ? 1.4262 0.8722 1.4899 -0.2507 -0.5125 0.2424 724 ASP A O 5599 C CB . ASP A 724 ? 1.6840 1.0332 1.8174 -0.2552 -0.5640 0.2390 724 ASP A CB 5600 C CG . ASP A 724 ? 2.0230 1.3225 2.1935 -0.2576 -0.5927 0.2362 724 ASP A CG 5601 O OD1 . ASP A 724 ? 2.1567 1.4696 2.3683 -0.2439 -0.5734 0.2275 724 ASP A OD1 5602 O OD2 . ASP A 724 ? 2.1773 1.4554 2.3295 -0.2621 -0.6242 0.2362 724 ASP A OD2 5603 N N . LYS A 725 ? 1.5057 0.9681 1.4878 -0.2938 -0.5229 0.2698 725 LYS A N 5604 C CA . LYS A 725 ? 1.4772 0.9955 1.4234 -0.2901 -0.4983 0.2691 725 LYS A CA 5605 C C . LYS A 725 ? 1.4106 0.9635 1.3763 -0.2776 -0.4630 0.2632 725 LYS A C 5606 O O . LYS A 725 ? 1.3633 0.9618 1.3088 -0.2689 -0.4414 0.2588 725 LYS A O 5607 C CB . LYS A 725 ? 1.4355 0.9783 1.3183 -0.3185 -0.5056 0.2885 725 LYS A CB 5608 C CG . LYS A 725 ? 1.5204 1.0652 1.3973 -0.3423 -0.5032 0.3034 725 LYS A CG 5609 C CD . LYS A 725 ? 1.6819 1.2546 1.5016 -0.3727 -0.5089 0.3259 725 LYS A CD 5610 C CE . LYS A 725 ? 1.6877 1.2212 1.4808 -0.3884 -0.5436 0.3406 725 LYS A CE 5611 N NZ . LYS A 725 ? 1.9710 1.5371 1.7055 -0.4176 -0.5457 0.3662 725 LYS A NZ 5612 N N . VAL A 726 ? 1.3181 0.8503 1.3210 -0.2746 -0.4580 0.2619 726 VAL A N 5613 C CA . VAL A 726 ? 1.2914 0.8554 1.3057 -0.2626 -0.4263 0.2577 726 VAL A CA 5614 C C . VAL A 726 ? 1.2885 0.8325 1.3608 -0.2384 -0.4130 0.2477 726 VAL A C 5615 O O . VAL A 726 ? 1.4415 0.9443 1.5505 -0.2355 -0.4304 0.2446 726 VAL A O 5616 C CB . VAL A 726 ? 1.2808 0.8558 1.2708 -0.2842 -0.4276 0.2678 726 VAL A CB 5617 C CG1 . VAL A 726 ? 1.3071 0.9194 1.2428 -0.3070 -0.4293 0.2798 726 VAL A CG1 5618 C CG2 . VAL A 726 ? 1.4714 0.9957 1.4788 -0.2977 -0.4566 0.2723 726 VAL A CG2 5619 N N . SER A 727 ? 1.3173 0.8934 1.3975 -0.2204 -0.3814 0.2434 727 SER A N 5620 C CA . SER A 727 ? 1.3229 0.8895 1.4519 -0.1975 -0.3624 0.2379 727 SER A CA 5621 C C . SER A 727 ? 1.5264 1.0920 1.6528 -0.2012 -0.3594 0.2386 727 SER A C 5622 O O . SER A 727 ? 1.4156 0.9977 1.5027 -0.2189 -0.3654 0.2429 727 SER A O 5623 C CB . SER A 727 ? 1.3422 0.9415 1.4784 -0.1745 -0.3307 0.2349 727 SER A CB 5624 O OG . SER A 727 ? 1.2778 0.9174 1.3740 -0.1762 -0.3139 0.2364 727 SER A OG 5625 N N . PRO A 728 ? 1.5889 1.1368 1.7593 -0.1838 -0.3511 0.2338 728 PRO A N 5626 C CA . PRO A 728 ? 1.4426 0.9942 1.6091 -0.1806 -0.3465 0.2304 728 PRO A CA 5627 C C . PRO A 728 ? 1.5569 1.1525 1.6954 -0.1691 -0.3179 0.2301 728 PRO A C 5628 O O . PRO A 728 ? 1.5912 1.2076 1.7384 -0.1501 -0.2920 0.2312 728 PRO A O 5629 C CB . PRO A 728 ? 1.5029 1.0339 1.7247 -0.1589 -0.3385 0.2244 728 PRO A CB 5630 C CG . PRO A 728 ? 1.4637 0.9946 1.7189 -0.1466 -0.3253 0.2271 728 PRO A CG 5631 C CD . PRO A 728 ? 1.6343 1.1599 1.8615 -0.1664 -0.3469 0.2304 728 PRO A CD 5632 N N . VAL A 729 ? 1.4460 1.0542 1.5536 -0.1802 -0.3249 0.2285 729 VAL A N 5633 C CA . VAL A 729 ? 1.3755 1.0263 1.4547 -0.1702 -0.3021 0.2265 729 VAL A CA 5634 C C . VAL A 729 ? 1.4734 1.1336 1.5729 -0.1366 -0.2740 0.2207 729 VAL A C 5635 O O . VAL A 729 ? 1.7311 1.3738 1.8496 -0.1267 -0.2782 0.2139 729 VAL A O 5636 C CB . VAL A 729 ? 1.3472 1.0081 1.3949 -0.1912 -0.3198 0.2251 729 VAL A CB 5637 C CG1 . VAL A 729 ? 1.4034 1.1106 1.4239 -0.1803 -0.2981 0.2212 729 VAL A CG1 5638 C CG2 . VAL A 729 ? 1.4032 1.0557 1.4303 -0.2262 -0.3460 0.2356 729 VAL A CG2 5639 N N . VAL A 730 ? 1.3668 1.0554 1.4611 -0.1178 -0.2457 0.2236 730 VAL A N 5640 C CA . VAL A 730 ? 1.3863 1.0870 1.4950 -0.0853 -0.2158 0.2228 730 VAL A CA 5641 C C . VAL A 730 ? 1.5420 1.2809 1.6116 -0.0735 -0.2003 0.2192 730 VAL A C 5642 O O . VAL A 730 ? 1.6022 1.3658 1.6503 -0.0761 -0.1934 0.2220 730 VAL A O 5643 C CB . VAL A 730 ? 1.4609 1.1576 1.6039 -0.0692 -0.1948 0.2321 730 VAL A CB 5644 C CG1 . VAL A 730 ? 1.5634 1.2751 1.7181 -0.0366 -0.1613 0.2363 730 VAL A CG1 5645 C CG2 . VAL A 730 ? 1.5839 1.2435 1.7711 -0.0791 -0.2117 0.2336 730 VAL A CG2 5646 N N . SER A 731 ? 1.6018 1.3464 1.6627 -0.0586 -0.1968 0.2108 731 SER A N 5647 C CA . SER A 731 ? 1.4953 1.2746 1.5197 -0.0451 -0.1857 0.2046 731 SER A CA 5648 C C . SER A 731 ? 1.4554 1.2502 1.4815 -0.0076 -0.1513 0.2090 731 SER A C 5649 O O . SER A 731 ? 1.4527 1.2333 1.5051 0.0108 -0.1384 0.2117 731 SER A O 5650 C CB . SER A 731 ? 1.5156 1.2925 1.5250 -0.0512 -0.2078 0.1902 731 SER A CB 5651 O OG . SER A 731 ? 1.6729 1.4835 1.6491 -0.0375 -0.2003 0.1819 731 SER A OG 5652 N N . HIS A 732 ? 1.5155 1.3408 1.5137 0.0041 -0.1362 0.2106 732 HIS A N 5653 C CA . HIS A 732 ? 1.6112 1.4518 1.6036 0.0398 -0.1044 0.2174 732 HIS A CA 5654 C C . HIS A 732 ? 1.5712 1.4438 1.5195 0.0550 -0.1022 0.2065 732 HIS A C 5655 O O . HIS A 732 ? 1.5301 1.4224 1.4565 0.0390 -0.1155 0.1998 732 HIS A O 5656 C CB . HIS A 732 ? 1.6204 1.4612 1.6295 0.0445 -0.0866 0.2332 732 HIS A CB 5657 C CG . HIS A 732 ? 1.5467 1.4024 1.5474 0.0789 -0.0550 0.2444 732 HIS A CG 5658 N ND1 . HIS A 732 ? 1.4486 1.3291 1.4193 0.0906 -0.0469 0.2450 732 HIS A ND1 5659 C CD2 . HIS A 732 ? 1.5727 1.4230 1.5907 0.1047 -0.0294 0.2568 732 HIS A CD2 5660 C CE1 . HIS A 732 ? 1.5369 1.4225 1.5046 0.1217 -0.0191 0.2586 732 HIS A CE1 5661 N NE2 . HIS A 732 ? 1.5699 1.4391 1.5655 0.1304 -0.0065 0.2672 732 HIS A NE2 5662 N N . LYS A 733 ? 1.5822 1.4624 1.5178 0.0872 -0.0855 0.2041 733 LYS A N 5663 C CA . LYS A 733 ? 1.5735 1.4822 1.4666 0.1059 -0.0859 0.1913 733 LYS A CA 5664 C C . LYS A 733 ? 1.5791 1.5041 1.4538 0.1439 -0.0535 0.2031 733 LYS A C 5665 O O . LYS A 733 ? 1.6279 1.5411 1.5238 0.1602 -0.0289 0.2206 733 LYS A O 5666 C CB . LYS A 733 ? 1.6114 1.5158 1.4955 0.1122 -0.1035 0.1718 733 LYS A CB 5667 C CG . LYS A 733 ? 1.6661 1.5597 1.5614 0.1423 -0.0844 0.1746 733 LYS A CG 5668 C CD . LYS A 733 ? 1.8644 1.7560 1.7471 0.1530 -0.1054 0.1502 733 LYS A CD 5669 C CE . LYS A 733 ? 1.9026 1.7908 1.7937 0.1873 -0.0840 0.1512 733 LYS A CE 5670 N NZ . LYS A 733 ? 1.8798 1.7925 1.7438 0.2260 -0.0469 0.1648 733 LYS A NZ 5671 N N . VAL A 734 ? 1.5957 1.5482 1.4324 0.1572 -0.0542 0.1947 734 VAL A N 5672 C CA . VAL A 734 ? 1.6267 1.5947 1.4366 0.1961 -0.0275 0.2044 734 VAL A CA 5673 C C . VAL A 734 ? 1.6538 1.6427 1.4216 0.2202 -0.0362 0.1836 734 VAL A C 5674 O O . VAL A 734 ? 1.6701 1.6727 1.4254 0.2043 -0.0631 0.1628 734 VAL A O 5675 C CB . VAL A 734 ? 1.6540 1.6349 1.4571 0.1961 -0.0197 0.2146 734 VAL A CB 5676 C CG1 . VAL A 734 ? 1.6770 1.6350 1.5209 0.1857 -0.0055 0.2374 734 VAL A CG1 5677 C CG2 . VAL A 734 ? 1.6299 1.6305 1.4230 0.1694 -0.0466 0.1964 734 VAL A CG2 5678 N N . ASP A 735 ? 1.6530 1.6454 1.4004 0.2589 -0.0140 0.1894 735 ASP A N 5679 C CA . ASP A 735 ? 1.7231 1.7332 1.4292 0.2874 -0.0232 0.1674 735 ASP A CA 5680 C C . ASP A 735 ? 1.8347 1.8712 1.4999 0.3063 -0.0240 0.1621 735 ASP A C 5681 O O . ASP A 735 ? 1.8905 1.9308 1.5508 0.3156 -0.0037 0.1825 735 ASP A O 5682 C CB . ASP A 735 ? 1.8572 1.8649 1.5528 0.3251 0.0020 0.1752 735 ASP A CB 5683 C CG . ASP A 735 ? 1.9255 1.9104 1.6638 0.3100 0.0015 0.1770 735 ASP A CG 5684 O OD1 . ASP A 735 ? 1.9451 1.9161 1.7066 0.2773 -0.0291 0.1604 735 ASP A OD1 5685 O OD2 . ASP A 735 ? 1.9754 1.9572 1.7256 0.3306 0.0318 0.1961 735 ASP A OD2 5686 N N . LEU A 736 ? 1.8154 1.8692 1.4545 0.3122 -0.0499 0.1335 736 LEU A N 5687 C CA . LEU A 736 ? 1.7320 1.8131 1.3325 0.3333 -0.0542 0.1239 736 LEU A CA 5688 C C . LEU A 736 ? 1.7566 1.8456 1.3112 0.3862 -0.0350 0.1260 736 LEU A C 5689 O O . LEU A 736 ? 1.8073 1.8943 1.3475 0.4064 -0.0405 0.1108 736 LEU A O 5690 C CB . LEU A 736 ? 1.7358 1.8343 1.3343 0.3144 -0.0926 0.0919 736 LEU A CB 5691 C CG . LEU A 736 ? 1.6922 1.8027 1.3173 0.2709 -0.1097 0.0898 736 LEU A CG 5692 C CD1 . LEU A 736 ? 1.7394 1.8253 1.4066 0.2331 -0.1051 0.1078 736 LEU A CD1 5693 C CD2 . LEU A 736 ? 1.6916 1.8196 1.3193 0.2533 -0.1466 0.0602 736 LEU A CD2 5694 N N . ALA A 737 ? 1.7230 1.8206 1.2531 0.4099 -0.0134 0.1448 737 ALA A N 5695 C CA . ALA A 737 ? 1.7364 1.8426 1.2167 0.4614 0.0065 0.1515 737 ALA A CA 5696 C C . ALA A 737 ? 1.7390 1.8705 1.1751 0.4845 -0.0140 0.1280 737 ALA A C 5697 O O . ALA A 737 ? 1.6997 1.8434 1.1449 0.4651 -0.0295 0.1208 737 ALA A O 5698 C CB . ALA A 737 ? 1.6928 1.7877 1.1748 0.4753 0.0450 0.1926 737 ALA A CB 5699 N N . VAL A 738 ? 1.3692 1.4864 1.3981 0.2982 -0.2590 0.0218 738 VAL A N 5700 C CA . VAL A 738 ? 1.3437 1.3979 1.3510 0.2904 -0.2274 0.0184 738 VAL A CA 5701 C C . VAL A 738 ? 1.3343 1.3938 1.3704 0.2660 -0.2070 -0.0088 738 VAL A C 5702 O O . VAL A 738 ? 1.3030 1.3907 1.3915 0.2700 -0.2004 -0.0140 738 VAL A O 5703 C CB . VAL A 738 ? 1.2937 1.3088 1.3121 0.3187 -0.2166 0.0369 738 VAL A CB 5704 C CG1 . VAL A 738 ? 1.2555 1.2150 1.2598 0.3070 -0.1862 0.0297 738 VAL A CG1 5705 C CG2 . VAL A 738 ? 1.4078 1.3987 1.3906 0.3401 -0.2365 0.0674 738 VAL A CG2 5706 N N . LEU A 739 ? 1.3963 1.4297 1.3971 0.2423 -0.1967 -0.0247 739 LEU A N 5707 C CA . LEU A 739 ? 1.3785 1.4039 1.3999 0.2197 -0.1788 -0.0482 739 LEU A CA 5708 C C . LEU A 739 ? 1.3565 1.3255 1.3429 0.2147 -0.1535 -0.0520 739 LEU A C 5709 O O . LEU A 739 ? 1.3988 1.3512 1.3380 0.2093 -0.1540 -0.0555 739 LEU A O 5710 C CB . LEU A 739 ? 1.5126 1.5681 1.5340 0.1941 -0.1973 -0.0715 739 LEU A CB 5711 C CG . LEU A 739 ? 1.4801 1.5322 1.5332 0.1675 -0.1869 -0.0935 739 LEU A CG 5712 C CD1 . LEU A 739 ? 1.4989 1.4943 1.5115 0.1555 -0.1692 -0.1112 739 LEU A CD1 5713 C CD2 . LEU A 739 ? 1.4280 1.4917 1.5348 0.1745 -0.1682 -0.0823 739 LEU A CD2 5714 N N . ALA A 740 ? 1.2927 1.2383 1.3026 0.2178 -0.1314 -0.0510 740 ALA A N 5715 C CA . ALA A 740 ? 1.2641 1.1632 1.2494 0.2136 -0.1089 -0.0543 740 ALA A CA 5716 C C . ALA A 740 ? 1.2853 1.1742 1.2965 0.1999 -0.0926 -0.0699 740 ALA A C 5717 O O . ALA A 740 ? 1.2871 1.1841 1.3331 0.2051 -0.0842 -0.0651 740 ALA A O 5718 C CB . ALA A 740 ? 1.1966 1.0670 1.1746 0.2317 -0.1003 -0.0334 740 ALA A CB 5719 N N . ALA A 741 ? 1.3453 1.2152 1.3366 0.1844 -0.0879 -0.0882 741 ALA A N 5720 C CA . ALA A 741 ? 1.3013 1.1505 1.3112 0.1717 -0.0736 -0.0999 741 ALA A CA 5721 C C . ALA A 741 ? 1.1995 1.0126 1.1972 0.1819 -0.0523 -0.0928 741 ALA A C 5722 O O . ALA A 741 ? 1.5117 1.3060 1.4771 0.1860 -0.0467 -0.0953 741 ALA A O 5723 C CB . ALA A 741 ? 1.2904 1.1266 1.2841 0.1533 -0.0812 -0.1245 741 ALA A CB 5724 N N . VAL A 742 ? 1.0988 0.9082 1.1225 0.1861 -0.0404 -0.0839 742 VAL A N 5725 C CA . VAL A 742 ? 1.0465 0.8257 1.0602 0.1956 -0.0241 -0.0768 742 VAL A CA 5726 C C . VAL A 742 ? 1.0555 0.8187 1.0849 0.1878 -0.0107 -0.0806 742 VAL A C 5727 O O . VAL A 742 ? 1.1136 0.8953 1.1706 0.1842 -0.0077 -0.0761 742 VAL A O 5728 C CB . VAL A 742 ? 1.0727 0.8546 1.0912 0.2130 -0.0239 -0.0609 742 VAL A CB 5729 C CG1 . VAL A 742 ? 0.9702 0.7200 0.9710 0.2189 -0.0134 -0.0551 742 VAL A CG1 5730 C CG2 . VAL A 742 ? 1.0503 0.8491 1.0594 0.2209 -0.0407 -0.0525 742 VAL A CG2 5731 N N . GLU A 743 ? 1.0542 0.7867 1.0664 0.1865 -0.0022 -0.0868 743 GLU A N 5732 C CA . GLU A 743 ? 1.1816 0.8918 1.2032 0.1810 0.0089 -0.0868 743 GLU A CA 5733 C C . GLU A 743 ? 1.0976 0.7886 1.1077 0.1942 0.0199 -0.0786 743 GLU A C 5734 O O . GLU A 743 ? 0.9547 0.6450 0.9489 0.2030 0.0190 -0.0767 743 GLU A O 5735 C CB . GLU A 743 ? 1.2102 0.8953 1.2238 0.1692 0.0057 -0.1031 743 GLU A CB 5736 C CG . GLU A 743 ? 1.3240 0.9912 1.3086 0.1805 0.0075 -0.1140 743 GLU A CG 5737 C CD . GLU A 743 ? 1.7422 1.3769 1.7154 0.1748 0.0041 -0.1346 743 GLU A CD 5738 O OE1 . GLU A 743 ? 1.9974 1.6223 1.9842 0.1562 -0.0044 -0.1408 743 GLU A OE1 5739 O OE2 . GLU A 743 ? 1.7667 1.3858 1.7185 0.1889 0.0095 -0.1449 743 GLU A OE2 5740 N N . ILE A 744 ? 0.9708 0.6495 0.9890 0.1935 0.0292 -0.0717 744 ILE A N 5741 C CA . ILE A 744 ? 0.8715 0.5335 0.8782 0.2049 0.0364 -0.0648 744 ILE A CA 5742 C C . ILE A 744 ? 0.9654 0.5986 0.9687 0.2028 0.0418 -0.0656 744 ILE A C 5743 O O . ILE A 744 ? 1.2270 0.8505 1.2400 0.1913 0.0443 -0.0628 744 ILE A O 5744 C CB . ILE A 744 ? 0.9168 0.5890 0.9273 0.2123 0.0412 -0.0544 744 ILE A CB 5745 C CG1 . ILE A 744 ? 0.9630 0.6176 0.9587 0.2218 0.0446 -0.0491 744 ILE A CG1 5746 C CG2 . ILE A 744 ? 0.8928 0.5786 0.9207 0.2036 0.0483 -0.0490 744 ILE A CG2 5747 C CD1 . ILE A 744 ? 0.8812 0.5409 0.8712 0.2315 0.0471 -0.0441 744 ILE A CD1 5748 N N . ARG A 745 ? 1.0789 0.6996 1.0701 0.2137 0.0428 -0.0678 745 ARG A N 5749 C CA . ARG A 745 ? 0.9061 0.4970 0.8933 0.2181 0.0457 -0.0692 745 ARG A CA 5750 C C . ARG A 745 ? 1.1455 0.7340 1.1277 0.2314 0.0486 -0.0579 745 ARG A C 5751 O O . ARG A 745 ? 1.0732 0.6822 1.0536 0.2360 0.0468 -0.0540 745 ARG A O 5752 C CB . ARG A 745 ? 0.8915 0.4731 0.8703 0.2239 0.0432 -0.0867 745 ARG A CB 5753 C CG . ARG A 745 ? 0.9608 0.5400 0.9390 0.2102 0.0365 -0.1014 745 ARG A CG 5754 C CD . ARG A 745 ? 1.1186 0.6843 1.0802 0.2201 0.0346 -0.1227 745 ARG A CD 5755 N NE . ARG A 745 ? 1.5420 1.0738 1.4999 0.2357 0.0388 -0.1251 745 ARG A NE 5756 C CZ . ARG A 745 ? 1.6433 1.1272 1.6015 0.2307 0.0349 -0.1287 745 ARG A CZ 5757 N NH1 . ARG A 745 ? 1.6406 1.1101 1.6058 0.2060 0.0275 -0.1303 745 ARG A NH1 5758 N NH2 . ARG A 745 ? 1.2863 0.7373 1.2401 0.2499 0.0373 -0.1289 745 ARG A NH2 5759 N N . GLY A 746 ? 1.3651 0.9260 1.3447 0.2365 0.0504 -0.0520 746 GLY A N 5760 C CA . GLY A 746 ? 0.9958 0.5566 0.9699 0.2500 0.0499 -0.0406 746 GLY A CA 5761 C C . GLY A 746 ? 0.9375 0.4660 0.9084 0.2627 0.0490 -0.0371 746 GLY A C 5762 O O . GLY A 746 ? 1.3206 0.8140 1.2909 0.2568 0.0493 -0.0395 746 GLY A O 5763 N N . VAL A 747 ? 0.9133 0.4522 0.8835 0.2799 0.0455 -0.0310 747 VAL A N 5764 C CA . VAL A 747 ? 1.1749 0.6858 1.1432 0.2984 0.0425 -0.0253 747 VAL A CA 5765 C C . VAL A 747 ? 1.1416 0.6668 1.1052 0.3099 0.0362 -0.0079 747 VAL A C 5766 O O . VAL A 747 ? 1.1026 0.6612 1.0655 0.3041 0.0332 -0.0056 747 VAL A O 5767 C CB . VAL A 747 ? 1.0917 0.6077 1.0687 0.3180 0.0429 -0.0428 747 VAL A CB 5768 C CG1 . VAL A 747 ? 1.1623 0.6459 1.1347 0.3114 0.0455 -0.0616 747 VAL A CG1 5769 C CG2 . VAL A 747 ? 1.2430 0.8155 1.2313 0.3192 0.0441 -0.0485 747 VAL A CG2 5770 N N . SER A 748 ? 1.2573 0.7532 1.2158 0.3264 0.0317 0.0039 748 SER A N 5771 C CA . SER A 748 ? 1.1642 0.6750 1.1170 0.3409 0.0221 0.0209 748 SER A CA 5772 C C . SER A 748 ? 1.2807 0.7920 1.2473 0.3714 0.0154 0.0195 748 SER A C 5773 O O . SER A 748 ? 1.2416 0.7063 1.2055 0.3849 0.0157 0.0198 748 SER A O 5774 C CB . SER A 748 ? 1.1554 0.6342 1.0836 0.3342 0.0217 0.0444 748 SER A CB 5775 O OG . SER A 748 ? 1.2276 0.7197 1.1449 0.3503 0.0099 0.0611 748 SER A OG 5776 N N . SER A 749 ? 1.0239 0.5886 1.0074 0.3823 0.0086 0.0174 749 SER A N 5777 C CA . SER A 749 ? 1.0201 0.6027 1.0238 0.4147 0.0026 0.0169 749 SER A CA 5778 C C . SER A 749 ? 1.2270 0.8362 1.2314 0.4275 -0.0143 0.0367 749 SER A C 5779 O O . SER A 749 ? 1.1845 0.8454 1.1986 0.4162 -0.0220 0.0372 749 SER A O 5780 C CB . SER A 749 ? 1.1556 0.7932 1.1871 0.4180 0.0098 -0.0018 749 SER A CB 5781 O OG . SER A 749 ? 1.5121 1.1280 1.5373 0.4070 0.0233 -0.0204 749 SER A OG 5782 N N . PRO A 750 ? 1.2982 0.8693 1.2911 0.4505 -0.0227 0.0537 750 PRO A N 5783 C CA . PRO A 750 ? 1.1702 0.6665 1.1481 0.4603 -0.0173 0.0565 750 PRO A CA 5784 C C . PRO A 750 ? 1.1444 0.5933 1.0917 0.4288 -0.0105 0.0677 750 PRO A C 5785 O O . PRO A 750 ? 1.1331 0.6060 1.0656 0.4086 -0.0114 0.0767 750 PRO A O 5786 C CB . PRO A 750 ? 1.1856 0.6743 1.1663 0.4882 -0.0329 0.0765 750 PRO A CB 5787 C CG . PRO A 750 ? 1.1690 0.7033 1.1419 0.4907 -0.0472 0.0934 750 PRO A CG 5788 C CD . PRO A 750 ? 1.3298 0.9295 1.3236 0.4689 -0.0420 0.0733 750 PRO A CD 5789 N N . ASP A 751 ? 1.5998 0.9876 1.5404 0.4223 -0.0043 0.0656 751 ASP A N 5790 C CA . ASP A 751 ? 1.4449 0.7914 1.3623 0.3924 0.0035 0.0787 751 ASP A CA 5791 C C . ASP A 751 ? 1.4470 0.7588 1.3379 0.3953 -0.0038 0.1150 751 ASP A C 5792 O O . ASP A 751 ? 1.4729 0.7645 1.3447 0.3686 0.0039 0.1327 751 ASP A O 5793 C CB . ASP A 751 ? 1.3820 0.6771 1.3045 0.3795 0.0100 0.0625 751 ASP A CB 5794 C CG . ASP A 751 ? 1.8048 1.0558 1.7362 0.3931 -0.0001 0.0637 751 ASP A CG 5795 O OD1 . ASP A 751 ? 2.1105 1.2980 2.0344 0.3759 -0.0003 0.0680 751 ASP A OD1 5796 O OD2 . ASP A 751 ? 1.8558 1.1341 1.8032 0.4215 -0.0082 0.0608 751 ASP A OD2 5797 N N . HIS A 752 ? 1.3956 0.7081 1.2869 0.4271 -0.0184 0.1276 752 HIS A N 5798 C CA . HIS A 752 ? 1.5630 0.8443 1.4247 0.4346 -0.0281 0.1656 752 HIS A CA 5799 C C . HIS A 752 ? 1.5158 0.8417 1.3821 0.4658 -0.0469 0.1748 752 HIS A C 5800 O O . HIS A 752 ? 1.6646 1.0315 1.5668 0.4851 -0.0529 0.1539 752 HIS A O 5801 C CB . HIS A 752 ? 1.7803 0.9901 1.6428 0.4290 -0.0312 0.1781 752 HIS A CB 5802 C CG . HIS A 752 ? 2.0378 1.2452 1.9377 0.4478 -0.0383 0.1527 752 HIS A CG 5803 N ND1 . HIS A 752 ? 2.0877 1.3338 2.0077 0.4818 -0.0509 0.1505 752 HIS A ND1 5804 C CD2 . HIS A 752 ? 2.1857 1.3580 2.1044 0.4398 -0.0336 0.1279 752 HIS A CD2 5805 C CE1 . HIS A 752 ? 2.0710 1.3069 2.0205 0.4956 -0.0504 0.1261 752 HIS A CE1 5806 N NE2 . HIS A 752 ? 2.2308 1.4202 2.1776 0.4708 -0.0405 0.1109 752 HIS A NE2 5807 N N . VAL A 753 ? 1.3799 0.7059 1.2108 0.4680 -0.0558 0.2066 753 VAL A N 5808 C CA . VAL A 753 ? 1.4958 0.8591 1.3247 0.4987 -0.0783 0.2206 753 VAL A CA 5809 C C . VAL A 753 ? 1.7763 1.0931 1.5748 0.5079 -0.0901 0.2610 753 VAL A C 5810 O O . VAL A 753 ? 1.8064 1.0910 1.5596 0.4907 -0.0832 0.2890 753 VAL A O 5811 C CB . VAL A 753 ? 1.3499 0.7855 1.1673 0.4838 -0.0840 0.2143 753 VAL A CB 5812 C CG1 . VAL A 753 ? 1.3799 0.8516 1.1904 0.5120 -0.1114 0.2324 753 VAL A CG1 5813 C CG2 . VAL A 753 ? 1.2714 0.7587 1.1255 0.4707 -0.0761 0.1764 753 VAL A CG2 5814 N N . PHE A 754 ? 1.5173 0.8359 1.3425 0.5335 -0.1066 0.2650 754 PHE A N 5815 C CA . PHE A 754 ? 1.6044 0.8767 1.4068 0.5426 -0.1202 0.3034 754 PHE A CA 5816 C C . PHE A 754 ? 1.6272 0.9440 1.4043 0.5641 -0.1435 0.3290 754 PHE A C 5817 O O . PHE A 754 ? 1.6033 0.9810 1.4116 0.5895 -0.1599 0.3161 754 PHE A O 5818 C CB . PHE A 754 ? 1.6463 0.8859 1.4902 0.5611 -0.1264 0.2949 754 PHE A CB 5819 C CG . PHE A 754 ? 1.6599 0.8339 1.5143 0.5379 -0.1097 0.2800 754 PHE A CG 5820 C CD1 . PHE A 754 ? 1.7883 0.9817 1.6769 0.5332 -0.0958 0.2370 754 PHE A CD1 5821 C CD2 . PHE A 754 ? 1.7359 0.8303 1.5650 0.5191 -0.1095 0.3108 754 PHE A CD2 5822 C CE1 . PHE A 754 ? 1.8279 0.9629 1.7237 0.5117 -0.0840 0.2218 754 PHE A CE1 5823 C CE2 . PHE A 754 ? 1.7541 0.7884 1.5950 0.4955 -0.0979 0.2969 754 PHE A CE2 5824 C CZ . PHE A 754 ? 1.7734 0.8281 1.6469 0.4926 -0.0860 0.2508 754 PHE A CZ 5825 N N . LEU A 755 ? 1.7663 1.0569 1.4860 0.5526 -0.1450 0.3663 755 LEU A N 5826 C CA . LEU A 755 ? 1.7146 1.0420 1.3989 0.5706 -0.1690 0.3939 755 LEU A CA 5827 C C . LEU A 755 ? 1.8557 1.1487 1.5444 0.5897 -0.1882 0.4259 755 LEU A C 5828 O O . LEU A 755 ? 2.1166 1.3390 1.8126 0.5800 -0.1798 0.4382 755 LEU A O 5829 C CB . LEU A 755 ? 1.7706 1.0932 1.3831 0.5504 -0.1593 0.4184 755 LEU A CB 5830 C CG . LEU A 755 ? 1.7492 1.1242 1.3600 0.5263 -0.1443 0.3829 755 LEU A CG 5831 C CD1 . LEU A 755 ? 1.8293 1.2076 1.3797 0.4972 -0.1285 0.4009 755 LEU A CD1 5832 C CD2 . LEU A 755 ? 1.6057 1.0602 1.2387 0.5415 -0.1682 0.3566 755 LEU A CD2 5833 N N . PRO A 756 ? 1.8262 1.1678 1.5119 0.6166 -0.2167 0.4396 756 PRO A N 5834 C CA . PRO A 756 ? 1.7793 1.2064 1.4605 0.6278 -0.2342 0.4250 756 PRO A CA 5835 C C . PRO A 756 ? 1.7930 1.2790 1.5444 0.6430 -0.2370 0.3837 756 PRO A C 5836 O O . PRO A 756 ? 1.7657 1.2372 1.5688 0.6577 -0.2331 0.3724 756 PRO A O 5837 C CB . PRO A 756 ? 1.8545 1.3006 1.5119 0.6496 -0.2662 0.4606 756 PRO A CB 5838 C CG . PRO A 756 ? 2.0295 1.4192 1.7185 0.6646 -0.2688 0.4779 756 PRO A CG 5839 C CD . PRO A 756 ? 1.9165 1.2270 1.6034 0.6375 -0.2378 0.4740 756 PRO A CD 5840 N N . ILE A 757 ? 1.7264 1.2784 1.4775 0.6393 -0.2439 0.3620 757 ILE A N 5841 C CA . ILE A 757 ? 1.7188 1.3381 1.5361 0.6509 -0.2480 0.3278 757 ILE A CA 5842 C C . ILE A 757 ? 1.6939 1.3715 1.5497 0.6827 -0.2783 0.3382 757 ILE A C 5843 O O . ILE A 757 ? 1.7692 1.4727 1.5926 0.6905 -0.3062 0.3619 757 ILE A O 5844 C CB . ILE A 757 ? 1.6923 1.3664 1.5025 0.6279 -0.2493 0.3017 757 ILE A CB 5845 C CG1 . ILE A 757 ? 1.5251 1.1775 1.3571 0.5982 -0.2145 0.2699 757 ILE A CG1 5846 C CG2 . ILE A 757 ? 1.7587 1.5303 1.6210 0.6394 -0.2756 0.2861 757 ILE A CG2 5847 C CD1 . ILE A 757 ? 1.5702 1.1349 1.3645 0.5830 -0.1880 0.2822 757 ILE A CD1 5848 N N . PRO A 758 ? 1.6657 1.3656 1.5891 0.7019 -0.2724 0.3205 758 PRO A N 5849 C CA . PRO A 758 ? 1.7843 1.5483 1.7562 0.7351 -0.2977 0.3275 758 PRO A CA 5850 C C . PRO A 758 ? 1.7412 1.6091 1.7299 0.7354 -0.3259 0.3215 758 PRO A C 5851 O O . PRO A 758 ? 1.5056 1.4131 1.5079 0.7173 -0.3187 0.2961 758 PRO A O 5852 C CB . PRO A 758 ? 1.8562 1.6263 1.8928 0.7501 -0.2760 0.3003 758 PRO A CB 5853 C CG . PRO A 758 ? 1.8279 1.5069 1.8379 0.7273 -0.2444 0.2898 758 PRO A CG 5854 C CD . PRO A 758 ? 1.6233 1.2868 1.5780 0.6939 -0.2401 0.2931 758 PRO A CD 5855 N N . ASN A 759 ? 1.7664 1.6768 1.7550 0.7542 -0.3599 0.3449 759 ASN A N 5856 C CA . ASN A 759 ? 1.8208 1.8330 1.8259 0.7516 -0.3942 0.3409 759 ASN A CA 5857 C C . ASN A 759 ? 1.9708 1.9826 1.9189 0.7192 -0.3995 0.3301 759 ASN A C 5858 O O . ASN A 759 ? 1.8977 1.9629 1.8756 0.7021 -0.3998 0.3027 759 ASN A O 5859 C CB . ASN A 759 ? 1.6637 1.7699 1.7601 0.7620 -0.3932 0.3162 759 ASN A CB 5860 C CG . ASN A 759 ? 1.8913 2.0079 2.0442 0.7990 -0.3900 0.3234 759 ASN A CG 5861 O OD1 . ASN A 759 ? 2.0001 2.0904 2.1359 0.8203 -0.4081 0.3510 759 ASN A OD1 5862 N ND2 . ASN A 759 ? 1.8534 2.0080 2.0715 0.8081 -0.3670 0.2985 759 ASN A ND2 5863 N N . TRP A 760 ? 2.1388 2.0905 2.0042 0.7094 -0.4033 0.3516 760 TRP A N 5864 C CA . TRP A 760 ? 2.1278 2.0719 1.9312 0.6767 -0.4048 0.3386 760 TRP A CA 5865 C C . TRP A 760 ? 2.0854 2.0744 1.8403 0.6740 -0.4470 0.3505 760 TRP A C 5866 O O . TRP A 760 ? 1.9747 1.9320 1.6751 0.6882 -0.4583 0.3840 760 TRP A O 5867 C CB . TRP A 760 ? 2.1283 1.9734 1.8689 0.6599 -0.3689 0.3481 760 TRP A CB 5868 C CG . TRP A 760 ? 2.0748 1.9134 1.7466 0.6218 -0.3664 0.3372 760 TRP A CG 5869 C CD1 . TRP A 760 ? 2.0618 1.8600 1.6491 0.6200 -0.3674 0.3641 760 TRP A CD1 5870 C CD2 . TRP A 760 ? 1.8272 1.7008 1.5065 0.5829 -0.3624 0.2964 760 TRP A CD2 5871 N NE1 . TRP A 760 ? 1.7991 1.6084 1.3406 0.5856 -0.3627 0.3388 760 TRP A NE1 5872 C CE2 . TRP A 760 ? 1.7923 1.6424 1.3889 0.5630 -0.3612 0.2966 760 TRP A CE2 5873 C CE3 . TRP A 760 ? 1.6782 1.5987 1.4242 0.5635 -0.3594 0.2612 760 TRP A CE3 5874 C CZ2 . TRP A 760 ? 1.8486 1.7143 1.4276 0.5282 -0.3588 0.2594 760 TRP A CZ2 5875 C CZ3 . TRP A 760 ? 1.8748 1.8074 1.6035 0.5248 -0.3583 0.2287 760 TRP A CZ3 5876 C CH2 . TRP A 760 ? 1.9476 1.8498 1.5936 0.5092 -0.3588 0.2262 760 TRP A CH2 5877 N N . GLU A 761 ? 2.0027 2.0644 1.7810 0.6457 -0.4676 0.3207 761 GLU A N 5878 C CA . GLU A 761 ? 1.9096 2.0117 1.6367 0.6349 -0.5089 0.3218 761 GLU A CA 5879 C C . GLU A 761 ? 1.8801 1.9686 1.5656 0.5858 -0.4994 0.2851 761 GLU A C 5880 O O . GLU A 761 ? 1.7916 1.9064 1.5288 0.5566 -0.4905 0.2519 761 GLU A O 5881 C CB . GLU A 761 ? 1.7395 1.9467 1.5330 0.6476 -0.5544 0.3204 761 GLU A CB 5882 C CG . GLU A 761 ? 1.8670 2.0923 1.6937 0.6934 -0.5682 0.3571 761 GLU A CG 5883 C CD . GLU A 761 ? 2.0011 2.3381 1.8919 0.6973 -0.6126 0.3561 761 GLU A CD 5884 O OE1 . GLU A 761 ? 2.0509 2.4068 1.9712 0.7249 -0.6246 0.3833 761 GLU A OE1 5885 O OE2 . GLU A 761 ? 1.9893 2.3948 1.9030 0.6709 -0.6375 0.3281 761 GLU A OE2 5886 N N . HIS A 762 ? 1.9337 1.9804 1.5239 0.5789 -0.5007 0.2921 762 HIS A N 5887 C CA . HIS A 762 ? 2.0388 2.0638 1.5797 0.5400 -0.4895 0.2567 762 HIS A CA 5888 C C . HIS A 762 ? 1.9767 2.0593 1.4997 0.5208 -0.5375 0.2313 762 HIS A C 5889 O O . HIS A 762 ? 2.0022 2.1193 1.4907 0.5386 -0.5778 0.2498 762 HIS A O 5890 C CB . HIS A 762 ? 2.0686 2.0248 1.5149 0.5427 -0.4624 0.2741 762 HIS A CB 5891 C CG . HIS A 762 ? 2.1193 2.0819 1.4757 0.5295 -0.4838 0.2584 762 HIS A CG 5892 N ND1 . HIS A 762 ? 2.0609 2.0147 1.3944 0.4978 -0.4763 0.2134 762 HIS A ND1 5893 C CD2 . HIS A 762 ? 2.2956 2.2703 1.5747 0.5462 -0.5132 0.2807 762 HIS A CD2 5894 C CE1 . HIS A 762 ? 2.1639 2.1230 1.4092 0.4967 -0.4996 0.2050 762 HIS A CE1 5895 N NE2 . HIS A 762 ? 2.3570 2.3316 1.5663 0.5247 -0.5220 0.2458 762 HIS A NE2 5896 N N . LYS A 763 ? 1.8092 1.8993 1.3557 0.4835 -0.5354 0.1892 763 LYS A N 5897 C CA . LYS A 763 ? 1.9604 2.0888 1.4847 0.4573 -0.5800 0.1584 763 LYS A CA 5898 C C . LYS A 763 ? 2.1412 2.2130 1.6039 0.4284 -0.5613 0.1202 763 LYS A C 5899 O O . LYS A 763 ? 2.2030 2.2334 1.6888 0.4161 -0.5196 0.1078 763 LYS A O 5900 C CB . LYS A 763 ? 1.9787 2.1806 1.6042 0.4376 -0.6064 0.1443 763 LYS A CB 5901 C CG . LYS A 763 ? 2.2028 2.4778 1.8909 0.4697 -0.6323 0.1781 763 LYS A CG 5902 C CD . LYS A 763 ? 2.1650 2.5292 1.9507 0.4457 -0.6619 0.1633 763 LYS A CD 5903 C CE . LYS A 763 ? 2.0714 2.5206 1.9205 0.4824 -0.6904 0.1960 763 LYS A CE 5904 N NZ . LYS A 763 ? 1.9320 2.4836 1.8803 0.4567 -0.7201 0.1839 763 LYS A NZ 5905 N N . GLU A 764 ? 2.1539 2.2246 1.5363 0.4206 -0.5935 0.1005 764 GLU A N 5906 C CA . GLU A 764 ? 2.1852 2.2005 1.4964 0.4018 -0.5780 0.0625 764 GLU A CA 5907 C C . GLU A 764 ? 2.2174 2.2206 1.5852 0.3649 -0.5739 0.0230 764 GLU A C 5908 O O . GLU A 764 ? 2.2155 2.1632 1.5553 0.3552 -0.5418 -0.0008 764 GLU A O 5909 C CB . GLU A 764 ? 2.1732 2.1957 1.3876 0.4025 -0.6206 0.0443 764 GLU A CB 5910 C CG . GLU A 764 ? 2.3113 2.3389 1.4506 0.4383 -0.6222 0.0847 764 GLU A CG 5911 C CD . GLU A 764 ? 2.6385 2.6720 1.6704 0.4396 -0.6616 0.0633 764 GLU A CD 5912 O OE1 . GLU A 764 ? 2.7389 2.7677 1.7558 0.4127 -0.6897 0.0135 764 GLU A OE1 5913 O OE2 . GLU A 764 ? 2.7727 2.8121 1.7313 0.4674 -0.6656 0.0965 764 GLU A OE2 5914 N N . ASN A 765 ? 2.2179 2.2764 1.6668 0.3446 -0.6067 0.0187 765 ASN A N 5915 C CA . ASN A 765 ? 2.1304 2.1821 1.6395 0.3061 -0.6051 -0.0113 765 ASN A CA 5916 C C . ASN A 765 ? 1.9916 2.0865 1.6120 0.3046 -0.5852 0.0121 765 ASN A C 5917 O O . ASN A 765 ? 2.1253 2.2907 1.8163 0.2901 -0.6173 0.0169 765 ASN A O 5918 C CB . ASN A 765 ? 2.1885 2.2678 1.6939 0.2719 -0.6640 -0.0429 765 ASN A CB 5919 C CG . ASN A 765 ? 2.2958 2.3231 1.6865 0.2710 -0.6835 -0.0773 765 ASN A CG 5920 O OD1 . ASN A 765 ? 2.3986 2.3923 1.7088 0.3020 -0.6596 -0.0688 765 ASN A OD1 5921 N ND2 . ASN A 765 ? 2.3038 2.3245 1.6855 0.2348 -0.7271 -0.1165 765 ASN A ND2 5922 N N . PRO A 766 ? 1.7843 1.8417 1.4207 0.3199 -0.5324 0.0260 766 PRO A N 5923 C CA . PRO A 766 ? 1.7519 1.8460 1.4840 0.3242 -0.5100 0.0461 766 PRO A CA 5924 C C . PRO A 766 ? 1.7180 1.8407 1.5217 0.2835 -0.5184 0.0263 766 PRO A C 5925 O O . PRO A 766 ? 1.7136 1.7856 1.4973 0.2563 -0.5084 -0.0005 766 PRO A O 5926 C CB . PRO A 766 ? 1.6923 1.7229 1.4059 0.3416 -0.4548 0.0549 766 PRO A CB 5927 C CG . PRO A 766 ? 1.7461 1.7266 1.3598 0.3568 -0.4504 0.0545 766 PRO A CG 5928 C CD . PRO A 766 ? 1.7844 1.7685 1.3500 0.3347 -0.4916 0.0237 766 PRO A CD 5929 N N . GLU A 767 ? 1.8452 2.0508 1.7325 0.2807 -0.5365 0.0416 767 GLU A N 5930 C CA . GLU A 767 ? 1.8133 2.0591 1.7773 0.2405 -0.5420 0.0310 767 GLU A CA 5931 C C . GLU A 767 ? 1.6421 1.8787 1.6581 0.2443 -0.4919 0.0396 767 GLU A C 5932 O O . GLU A 767 ? 1.6043 1.8205 1.6410 0.2100 -0.4799 0.0248 767 GLU A O 5933 C CB . GLU A 767 ? 1.9006 2.2543 1.9363 0.2337 -0.5833 0.0445 767 GLU A CB 5934 C CG . GLU A 767 ? 1.9328 2.3036 1.9212 0.2244 -0.6400 0.0337 767 GLU A CG 5935 C CD . GLU A 767 ? 1.8766 2.3629 1.9458 0.2106 -0.6843 0.0457 767 GLU A CD 5936 O OE1 . GLU A 767 ? 1.8159 2.3355 1.8552 0.2182 -0.7306 0.0469 767 GLU A OE1 5937 O OE2 . GLU A 767 ? 1.8870 2.4364 2.0498 0.1921 -0.6728 0.0547 767 GLU A OE2 5938 N N . THR A 768 ? 1.6272 1.8752 1.6607 0.2866 -0.4647 0.0635 768 THR A N 5939 C CA . THR A 768 ? 1.5965 1.8511 1.6854 0.2945 -0.4223 0.0716 768 THR A CA 5940 C C . THR A 768 ? 1.5597 1.7456 1.6076 0.3301 -0.3824 0.0804 768 THR A C 5941 O O . THR A 768 ? 1.5319 1.6748 1.5154 0.3516 -0.3866 0.0871 768 THR A O 5942 C CB . THR A 768 ? 1.5376 1.8950 1.7161 0.3106 -0.4289 0.0911 768 THR A CB 5943 O OG1 . THR A 768 ? 1.5402 1.9178 1.7072 0.3562 -0.4437 0.1115 768 THR A OG1 5944 C CG2 . THR A 768 ? 1.5386 1.9761 1.7723 0.2687 -0.4660 0.0856 768 THR A CG2 5945 N N . GLU A 769 ? 1.5534 1.7305 1.6378 0.3333 -0.3444 0.0811 769 GLU A N 5946 C CA . GLU A 769 ? 1.4147 1.5303 1.4716 0.3625 -0.3072 0.0884 769 GLU A CA 5947 C C . GLU A 769 ? 1.3696 1.4915 1.4199 0.4080 -0.3135 0.1125 769 GLU A C 5948 O O . GLU A 769 ? 1.3683 1.4254 1.3688 0.4279 -0.2971 0.1220 769 GLU A O 5949 C CB . GLU A 769 ? 1.3379 1.4610 1.4446 0.3604 -0.2723 0.0846 769 GLU A CB 5950 C CG . GLU A 769 ? 1.4174 1.5460 1.5427 0.3164 -0.2683 0.0674 769 GLU A CG 5951 C CD . GLU A 769 ? 1.4620 1.6096 1.6350 0.3166 -0.2353 0.0672 769 GLU A CD 5952 O OE1 . GLU A 769 ? 1.2490 1.3707 1.4182 0.3479 -0.2090 0.0718 769 GLU A OE1 5953 O OE2 . GLU A 769 ? 1.6662 1.8530 1.8780 0.2843 -0.2367 0.0628 769 GLU A OE2 5954 N N . GLU A 770 ? 1.3498 1.5519 1.4536 0.4239 -0.3377 0.1244 770 GLU A N 5955 C CA . GLU A 770 ? 1.4014 1.6158 1.5065 0.4715 -0.3485 0.1491 770 GLU A CA 5956 C C . GLU A 770 ? 1.4877 1.6596 1.5146 0.4790 -0.3716 0.1607 770 GLU A C 5957 O O . GLU A 770 ? 1.5075 1.6401 1.5035 0.5145 -0.3673 0.1833 770 GLU A O 5958 C CB . GLU A 770 ? 1.5476 1.8710 1.7299 0.4851 -0.3746 0.1578 770 GLU A CB 5959 C CG . GLU A 770 ? 1.6718 2.0129 1.8732 0.5430 -0.3802 0.1826 770 GLU A CG 5960 C CD . GLU A 770 ? 1.6987 2.0198 1.9343 0.5734 -0.3407 0.1817 770 GLU A CD 5961 O OE1 . GLU A 770 ? 1.7190 2.0335 1.9735 0.5479 -0.3110 0.1627 770 GLU A OE1 5962 O OE2 . GLU A 770 ? 1.5599 1.8686 1.8005 0.6240 -0.3409 0.1994 770 GLU A OE2 5963 N N . ASP A 771 ? 1.4931 1.6701 1.4850 0.4451 -0.3963 0.1453 771 ASP A N 5964 C CA . ASP A 771 ? 1.4933 1.6403 1.4054 0.4504 -0.4203 0.1527 771 ASP A CA 5965 C C . ASP A 771 ? 1.5054 1.5613 1.3416 0.4444 -0.3893 0.1479 771 ASP A C 5966 O O . ASP A 771 ? 1.5705 1.5962 1.3329 0.4520 -0.3999 0.1569 771 ASP A O 5967 C CB . ASP A 771 ? 1.5822 1.7739 1.4853 0.4182 -0.4634 0.1337 771 ASP A CB 5968 C CG . ASP A 771 ? 1.8689 2.1629 1.8561 0.4163 -0.4952 0.1384 771 ASP A CG 5969 O OD1 . ASP A 771 ? 2.0641 2.4059 2.0553 0.4436 -0.5275 0.1590 771 ASP A OD1 5970 O OD2 . ASP A 771 ? 1.8416 2.1725 1.8923 0.3873 -0.4880 0.1238 771 ASP A OD2 5971 N N . VAL A 772 ? 1.5284 1.5470 1.3830 0.4310 -0.3510 0.1348 772 VAL A N 5972 C CA . VAL A 772 ? 1.5232 1.4665 1.3177 0.4232 -0.3202 0.1292 772 VAL A CA 5973 C C . VAL A 772 ? 1.4504 1.3476 1.2446 0.4489 -0.2879 0.1522 772 VAL A C 5974 O O . VAL A 772 ? 1.5521 1.4089 1.2906 0.4635 -0.2829 0.1733 772 VAL A O 5975 C CB . VAL A 772 ? 1.4519 1.3783 1.2598 0.3889 -0.3018 0.0985 772 VAL A CB 5976 C CG1 . VAL A 772 ? 1.4585 1.3170 1.2108 0.3848 -0.2698 0.0935 772 VAL A CG1 5977 C CG2 . VAL A 772 ? 1.4954 1.4525 1.2991 0.3601 -0.3359 0.0749 772 VAL A CG2 5978 N N . GLY A 773 ? 1.3654 1.2675 1.2198 0.4527 -0.2667 0.1482 773 GLY A N 5979 C CA . GLY A 773 ? 1.3328 1.1865 1.1909 0.4752 -0.2392 0.1648 773 GLY A CA 5980 C C . GLY A 773 ? 1.2739 1.1362 1.1931 0.4742 -0.2160 0.1500 773 GLY A C 5981 O O . GLY A 773 ? 1.2556 1.1677 1.2169 0.4560 -0.2202 0.1311 773 GLY A O 5982 N N . PRO A 774 ? 1.3955 1.2074 1.3170 0.4921 -0.1922 0.1589 774 PRO A N 5983 C CA . PRO A 774 ? 1.3320 1.1455 1.3018 0.4951 -0.1691 0.1433 774 PRO A CA 5984 C C . PRO A 774 ? 1.2194 1.0282 1.1903 0.4582 -0.1497 0.1186 774 PRO A C 5985 O O . PRO A 774 ? 1.2526 1.0368 1.1814 0.4347 -0.1484 0.1146 774 PRO A O 5986 C CB . PRO A 774 ? 1.3745 1.1151 1.3259 0.5174 -0.1525 0.1580 774 PRO A CB 5987 C CG . PRO A 774 ? 1.4101 1.1040 1.2983 0.5077 -0.1557 0.1781 774 PRO A CG 5988 C CD . PRO A 774 ? 1.5077 1.2535 1.3807 0.5074 -0.1862 0.1847 774 PRO A CD 5989 N N . VAL A 775 ? 1.2401 1.0729 1.2562 0.4559 -0.1346 0.1027 775 VAL A N 5990 C CA . VAL A 775 ? 1.1845 1.0144 1.2032 0.4228 -0.1184 0.0824 775 VAL A CA 5991 C C . VAL A 775 ? 1.2465 1.0129 1.2459 0.4201 -0.0911 0.0771 775 VAL A C 5992 O O . VAL A 775 ? 1.3529 1.1077 1.3733 0.4379 -0.0773 0.0735 775 VAL A O 5993 C CB . VAL A 775 ? 1.1014 0.9971 1.1762 0.4166 -0.1161 0.0706 775 VAL A CB 5994 C CG1 . VAL A 775 ? 1.1111 0.9977 1.1833 0.3821 -0.1017 0.0541 775 VAL A CG1 5995 C CG2 . VAL A 775 ? 1.3301 1.2972 1.4331 0.4149 -0.1450 0.0770 775 VAL A CG2 5996 N N . VAL A 776 ? 1.2239 0.9521 1.1838 0.3985 -0.0844 0.0751 776 VAL A N 5997 C CA . VAL A 776 ? 1.1215 0.7995 1.0675 0.3895 -0.0606 0.0699 776 VAL A CA 5998 C C . VAL A 776 ? 1.2885 0.9802 1.2471 0.3644 -0.0500 0.0494 776 VAL A C 5999 O O . VAL A 776 ? 1.2573 0.9625 1.2037 0.3461 -0.0579 0.0429 776 VAL A O 6000 C CB . VAL A 776 ? 1.1755 0.8096 1.0737 0.3831 -0.0564 0.0838 776 VAL A CB 6001 C CG1 . VAL A 776 ? 1.1945 0.7900 1.0870 0.3677 -0.0331 0.0774 776 VAL A CG1 6002 C CG2 . VAL A 776 ? 1.3245 0.9359 1.2061 0.4072 -0.0660 0.1095 776 VAL A CG2 6003 N N . GLN A 777 ? 1.4918 1.1764 1.4716 0.3651 -0.0337 0.0389 777 GLN A N 6004 C CA . GLN A 777 ? 1.3554 1.0561 1.3480 0.3440 -0.0249 0.0230 777 GLN A CA 6005 C C . GLN A 777 ? 1.1931 0.8528 1.1711 0.3332 -0.0074 0.0158 777 GLN A C 6006 O O . GLN A 777 ? 1.1026 0.7356 1.0835 0.3433 0.0024 0.0141 777 GLN A O 6007 C CB . GLN A 777 ? 1.3213 1.0670 1.3530 0.3521 -0.0220 0.0161 777 GLN A CB 6008 C CG . GLN A 777 ? 1.4886 1.2550 1.5320 0.3295 -0.0140 0.0050 777 GLN A CG 6009 C CD . GLN A 777 ? 1.7183 1.5417 1.7992 0.3362 -0.0097 0.0025 777 GLN A CD 6010 O OE1 . GLN A 777 ? 1.6785 1.5369 1.7824 0.3572 -0.0158 0.0084 777 GLN A OE1 6011 N NE2 . GLN A 777 ? 1.7323 1.5701 1.8197 0.3197 0.0013 -0.0044 777 GLN A NE2 6012 N N . HIS A 778 ? 1.0205 0.6750 0.9834 0.3132 -0.0055 0.0105 778 HIS A N 6013 C CA . HIS A 778 ? 1.1317 0.7608 1.0875 0.3017 0.0090 0.0036 778 HIS A CA 6014 C C . HIS A 778 ? 1.1385 0.7876 1.1109 0.2898 0.0126 -0.0092 778 HIS A C 6015 O O . HIS A 778 ? 1.2816 0.9527 1.2582 0.2802 0.0038 -0.0113 778 HIS A O 6016 C CB . HIS A 778 ? 1.0589 0.6720 0.9870 0.2927 0.0109 0.0074 778 HIS A CB 6017 C CG . HIS A 778 ? 1.2937 0.8831 1.2011 0.3003 0.0137 0.0238 778 HIS A CG 6018 N ND1 . HIS A 778 ? 1.3228 0.8997 1.2081 0.2926 0.0234 0.0302 778 HIS A ND1 6019 C CD2 . HIS A 778 ? 1.3837 0.9609 1.2889 0.3155 0.0083 0.0380 778 HIS A CD2 6020 C CE1 . HIS A 778 ? 1.2987 0.8564 1.1674 0.2990 0.0248 0.0498 778 HIS A CE1 6021 N NE2 . HIS A 778 ? 1.4345 0.9875 1.3136 0.3136 0.0142 0.0551 778 HIS A NE2 6022 N N . ILE A 779 ? 1.0854 0.7241 1.0648 0.2890 0.0237 -0.0170 779 ILE A N 6023 C CA . ILE A 779 ? 0.9242 0.5815 0.9136 0.2787 0.0276 -0.0267 779 ILE A CA 6024 C C . ILE A 779 ? 0.9953 0.6325 0.9756 0.2673 0.0343 -0.0325 779 ILE A C 6025 O O . ILE A 779 ? 0.8444 0.4580 0.8216 0.2687 0.0401 -0.0350 779 ILE A O 6026 C CB . ILE A 779 ? 0.8988 0.5747 0.9038 0.2904 0.0337 -0.0337 779 ILE A CB 6027 C CG1 . ILE A 779 ? 1.2422 0.9518 1.2648 0.3038 0.0274 -0.0269 779 ILE A CG1 6028 C CG2 . ILE A 779 ? 0.9130 0.6103 0.9215 0.2786 0.0387 -0.0406 779 ILE A CG2 6029 C CD1 . ILE A 779 ? 1.5173 1.2550 1.5572 0.3211 0.0362 -0.0347 779 ILE A CD1 6030 N N . TYR A 780 ? 1.0208 0.6665 0.9984 0.2557 0.0314 -0.0340 780 TYR A N 6031 C CA . TYR A 780 ? 0.8192 0.4560 0.7932 0.2475 0.0357 -0.0388 780 TYR A CA 6032 C C . TYR A 780 ? 0.8296 0.4826 0.8083 0.2410 0.0349 -0.0435 780 TYR A C 6033 O O . TYR A 780 ? 0.9987 0.6658 0.9794 0.2365 0.0292 -0.0389 780 TYR A O 6034 C CB . TYR A 780 ? 0.8183 0.4485 0.7818 0.2452 0.0331 -0.0360 780 TYR A CB 6035 C CG . TYR A 780 ? 0.9325 0.5504 0.8858 0.2501 0.0378 -0.0296 780 TYR A CG 6036 C CD1 . TYR A 780 ? 1.0153 0.6311 0.9558 0.2570 0.0318 -0.0238 780 TYR A CD1 6037 C CD2 . TYR A 780 ? 1.0680 0.6796 1.0238 0.2456 0.0473 -0.0274 780 TYR A CD2 6038 C CE1 . TYR A 780 ? 1.3123 0.9184 1.2374 0.2616 0.0365 -0.0145 780 TYR A CE1 6039 C CE2 . TYR A 780 ? 1.0749 0.6780 1.0202 0.2471 0.0535 -0.0164 780 TYR A CE2 6040 C CZ . TYR A 780 ? 1.2646 0.8641 1.1917 0.2563 0.0488 -0.0094 780 TYR A CZ 6041 O OH . TYR A 780 ? 1.2069 0.7993 1.1177 0.2581 0.0553 0.0047 780 TYR A OH 6042 N N . GLU A 781 ? 0.8026 0.4531 0.7816 0.2383 0.0391 -0.0512 781 GLU A N 6043 C CA . GLU A 781 ? 0.8601 0.5273 0.8371 0.2331 0.0379 -0.0545 781 GLU A CA 6044 C C . GLU A 781 ? 1.0589 0.7238 1.0341 0.2265 0.0346 -0.0573 781 GLU A C 6045 O O . GLU A 781 ? 0.8502 0.5064 0.8289 0.2239 0.0364 -0.0639 781 GLU A O 6046 C CB . GLU A 781 ? 0.9850 0.6605 0.9598 0.2394 0.0439 -0.0646 781 GLU A CB 6047 C CG . GLU A 781 ? 1.0863 0.7835 1.0518 0.2346 0.0440 -0.0672 781 GLU A CG 6048 C CD . GLU A 781 ? 1.6418 1.3475 1.5982 0.2444 0.0512 -0.0824 781 GLU A CD 6049 O OE1 . GLU A 781 ? 1.9251 1.6107 1.8838 0.2554 0.0544 -0.0930 781 GLU A OE1 6050 O OE2 . GLU A 781 ? 1.6333 1.3637 1.5771 0.2427 0.0535 -0.0836 781 GLU A OE2 6051 N N . LEU A 782 ? 1.0980 0.7713 1.0700 0.2230 0.0282 -0.0507 782 LEU A N 6052 C CA . LEU A 782 ? 0.9824 0.6609 0.9546 0.2205 0.0225 -0.0518 782 LEU A CA 6053 C C . LEU A 782 ? 0.8729 0.5673 0.8342 0.2166 0.0192 -0.0521 782 LEU A C 6054 O O . LEU A 782 ? 1.0657 0.7659 1.0190 0.2142 0.0165 -0.0410 782 LEU A O 6055 C CB . LEU A 782 ? 1.0478 0.7190 1.0208 0.2247 0.0157 -0.0438 782 LEU A CB 6056 C CG . LEU A 782 ? 0.8883 0.5694 0.8663 0.2280 0.0087 -0.0433 782 LEU A CG 6057 C CD1 . LEU A 782 ? 1.0860 0.7806 1.0797 0.2263 0.0138 -0.0512 782 LEU A CD1 6058 C CD2 . LEU A 782 ? 0.8377 0.5044 0.8135 0.2384 0.0016 -0.0375 782 LEU A CD2 6059 N N . ARG A 783 ? 0.8951 0.5959 0.8537 0.2141 0.0185 -0.0643 783 ARG A N 6060 C CA . ARG A 783 ? 1.0056 0.7233 0.9459 0.2121 0.0156 -0.0679 783 ARG A CA 6061 C C . ARG A 783 ? 1.0159 0.7454 0.9544 0.2083 0.0029 -0.0700 783 ARG A C 6062 O O . ARG A 783 ? 0.9850 0.7131 0.9378 0.2041 -0.0011 -0.0794 783 ARG A O 6063 C CB . ARG A 783 ? 1.2683 0.9836 1.1988 0.2155 0.0233 -0.0858 783 ARG A CB 6064 C CG . ARG A 783 ? 1.0379 0.7740 0.9420 0.2165 0.0227 -0.0930 783 ARG A CG 6065 C CD . ARG A 783 ? 1.0564 0.7906 0.9487 0.2271 0.0336 -0.1117 783 ARG A CD 6066 N NE . ARG A 783 ? 1.2513 1.0118 1.1126 0.2312 0.0362 -0.1192 783 ARG A NE 6067 C CZ . ARG A 783 ? 1.3652 1.1586 1.2167 0.2344 0.0469 -0.1049 783 ARG A CZ 6068 N NH1 . ARG A 783 ? 1.2131 1.0143 1.0869 0.2317 0.0531 -0.0837 783 ARG A NH1 6069 N NH2 . ARG A 783 ? 1.5677 1.3889 1.3863 0.2385 0.0511 -0.1112 783 ARG A NH2 6070 N N . ASN A 784 ? 1.0236 0.7675 0.9458 0.2084 -0.0044 -0.0585 784 ASN A N 6071 C CA . ASN A 784 ? 1.0722 0.8329 0.9892 0.2070 -0.0195 -0.0588 784 ASN A CA 6072 C C . ASN A 784 ? 1.1414 0.9159 1.0330 0.2031 -0.0220 -0.0756 784 ASN A C 6073 O O . ASN A 784 ? 1.1768 0.9597 1.0421 0.2050 -0.0147 -0.0735 784 ASN A O 6074 C CB . ASN A 784 ? 1.2644 1.0282 1.1722 0.2111 -0.0291 -0.0351 784 ASN A CB 6075 C CG . ASN A 784 ? 1.1675 0.9516 1.0724 0.2139 -0.0477 -0.0325 784 ASN A CG 6076 O OD1 . ASN A 784 ? 1.1813 0.9805 1.1006 0.2109 -0.0543 -0.0482 784 ASN A OD1 6077 N ND2 . ASN A 784 ? 1.1820 0.9670 1.0696 0.2182 -0.0580 -0.0105 784 ASN A ND2 6078 N N . ASN A 785 ? 1.1967 0.9754 1.0960 0.1970 -0.0322 -0.0932 785 ASN A N 6079 C CA . ASN A 785 ? 1.4089 1.1938 1.2811 0.1927 -0.0387 -0.1156 785 ASN A CA 6080 C C . ASN A 785 ? 1.5210 1.3347 1.3784 0.1899 -0.0599 -0.1127 785 ASN A C 6081 O O . ASN A 785 ? 1.4838 1.3123 1.3021 0.1933 -0.0629 -0.1128 785 ASN A O 6082 C CB . ASN A 785 ? 1.3114 1.0739 1.1991 0.1835 -0.0397 -0.1396 785 ASN A CB 6083 C CG . ASN A 785 ? 1.4374 1.1694 1.3265 0.1902 -0.0210 -0.1458 785 ASN A CG 6084 O OD1 . ASN A 785 ? 1.3988 1.1118 1.3154 0.1870 -0.0151 -0.1412 785 ASN A OD1 6085 N ND2 . ASN A 785 ? 1.6114 1.3435 1.4706 0.2015 -0.0113 -0.1551 785 ASN A ND2 6086 N N . GLY A 786 ? 1.5816 1.4087 1.4707 0.1845 -0.0744 -0.1094 786 GLY A N 6087 C CA . GLY A 786 ? 1.4601 1.3204 1.3439 0.1827 -0.0985 -0.1067 786 GLY A CA 6088 C C . GLY A 786 ? 1.6806 1.5539 1.5331 0.1944 -0.1039 -0.0830 786 GLY A C 6089 O O . GLY A 786 ? 1.9930 1.8510 1.8454 0.2028 -0.0914 -0.0614 786 GLY A O 6090 N N . PRO A 787 ? 1.5414 1.4416 1.3654 0.1931 -0.1246 -0.0859 787 PRO A N 6091 C CA . PRO A 787 ? 1.5487 1.4623 1.3290 0.2015 -0.1312 -0.0638 787 PRO A CA 6092 C C . PRO A 787 ? 1.4867 1.3909 1.2800 0.2133 -0.1307 -0.0269 787 PRO A C 6093 O O . PRO A 787 ? 1.4931 1.3870 1.2562 0.2156 -0.1214 -0.0049 787 PRO A O 6094 C CB . PRO A 787 ? 1.5934 1.5424 1.3591 0.1983 -0.1616 -0.0731 787 PRO A CB 6095 C CG . PRO A 787 ? 1.5834 1.5422 1.4021 0.1886 -0.1723 -0.0911 787 PRO A CG 6096 C CD . PRO A 787 ? 1.5755 1.4988 1.4126 0.1811 -0.1472 -0.1080 787 PRO A CD 6097 N N . SER A 788 ? 1.4302 1.3375 1.2680 0.2206 -0.1402 -0.0204 788 SER A N 6098 C CA . SER A 788 ? 1.3821 1.2719 1.2312 0.2360 -0.1427 0.0099 788 SER A CA 6099 C C . SER A 788 ? 1.3226 1.1723 1.1809 0.2350 -0.1189 0.0148 788 SER A C 6100 O O . SER A 788 ? 1.2884 1.1301 1.1635 0.2270 -0.1021 -0.0055 788 SER A O 6101 C CB . SER A 788 ? 1.3507 1.2617 1.2453 0.2497 -0.1588 0.0111 788 SER A CB 6102 O OG . SER A 788 ? 1.4155 1.3707 1.3066 0.2498 -0.1846 0.0078 788 SER A OG 6103 N N . SER A 789 ? 1.3203 1.1425 1.1665 0.2420 -0.1200 0.0429 789 SER A N 6104 C CA . SER A 789 ? 1.2929 1.0767 1.1490 0.2397 -0.1031 0.0485 789 SER A CA 6105 C C . SER A 789 ? 1.2153 0.9780 1.1048 0.2571 -0.1088 0.0501 789 SER A C 6106 O O . SER A 789 ? 1.2468 1.0300 1.1547 0.2725 -0.1239 0.0491 789 SER A O 6107 C CB . SER A 789 ? 1.3368 1.0994 1.1600 0.2316 -0.1012 0.0779 789 SER A CB 6108 O OG . SER A 789 ? 1.4117 1.2040 1.1992 0.2203 -0.0959 0.0786 789 SER A OG 6109 N N . PHE A 790 ? 1.1572 0.8830 1.0543 0.2561 -0.0972 0.0514 790 PHE A N 6110 C CA . PHE A 790 ? 1.1294 0.8280 1.0480 0.2759 -0.1024 0.0518 790 PHE A CA 6111 C C . PHE A 790 ? 1.1246 0.7683 1.0289 0.2718 -0.1019 0.0667 790 PHE A C 6112 O O . PHE A 790 ? 1.1294 0.7652 1.0242 0.2517 -0.0894 0.0675 790 PHE A O 6113 C CB . PHE A 790 ? 1.0764 0.7927 1.0271 0.2806 -0.0891 0.0265 790 PHE A CB 6114 C CG . PHE A 790 ? 1.0728 0.7793 1.0222 0.2636 -0.0695 0.0142 790 PHE A CG 6115 C CD1 . PHE A 790 ? 1.1893 0.8576 1.1365 0.2647 -0.0634 0.0149 790 PHE A CD1 6116 C CD2 . PHE A 790 ? 1.2220 0.9554 1.1720 0.2484 -0.0597 0.0004 790 PHE A CD2 6117 C CE1 . PHE A 790 ? 1.0973 0.7618 1.0450 0.2513 -0.0481 0.0053 790 PHE A CE1 6118 C CE2 . PHE A 790 ? 1.2061 0.9295 1.1561 0.2377 -0.0433 -0.0095 790 PHE A CE2 6119 C CZ . PHE A 790 ? 1.0653 0.7579 1.0154 0.2395 -0.0376 -0.0057 790 PHE A CZ 6120 N N . SER A 791 ? 1.2332 0.8392 1.1376 0.2916 -0.1172 0.0780 791 SER A N 6121 C CA . SER A 791 ? 1.1494 0.6929 1.0371 0.2857 -0.1237 0.0944 791 SER A CA 6122 C C . SER A 791 ? 1.1084 0.6224 1.0067 0.2854 -0.1140 0.0748 791 SER A C 6123 O O . SER A 791 ? 1.2471 0.7255 1.1341 0.2658 -0.1140 0.0831 791 SER A O 6124 C CB . SER A 791 ? 1.2208 0.7237 1.1002 0.3097 -0.1475 0.1132 791 SER A CB 6125 O OG . SER A 791 ? 1.6486 1.1698 1.5526 0.3437 -0.1515 0.0952 791 SER A OG 6126 N N . LYS A 792 ? 1.0761 0.6086 0.9957 0.3057 -0.1065 0.0503 792 LYS A N 6127 C CA . LYS A 792 ? 1.0783 0.5859 1.0018 0.3090 -0.0977 0.0309 792 LYS A CA 6128 C C . LYS A 792 ? 1.0393 0.5953 0.9847 0.3151 -0.0791 0.0083 792 LYS A C 6129 O O . LYS A 792 ? 1.0927 0.6922 1.0572 0.3279 -0.0773 0.0041 792 LYS A O 6130 C CB . LYS A 792 ? 1.0912 0.5425 1.0073 0.3365 -0.1126 0.0273 792 LYS A CB 6131 C CG . LYS A 792 ? 1.3067 0.6880 1.1986 0.3244 -0.1317 0.0476 792 LYS A CG 6132 C CD . LYS A 792 ? 1.7608 1.0774 1.6432 0.3567 -0.1488 0.0395 792 LYS A CD 6133 C CE . LYS A 792 ? 2.0673 1.3029 1.9252 0.3403 -0.1711 0.0616 792 LYS A CE 6134 N NZ . LYS A 792 ? 2.1715 1.3856 2.0218 0.3034 -0.1681 0.0595 792 LYS A NZ 6135 N N . ALA A 793 ? 1.0550 0.6042 0.9984 0.3042 -0.0668 -0.0040 793 ALA A N 6136 C CA . ALA A 793 ? 1.0359 0.6223 0.9958 0.3083 -0.0491 -0.0212 793 ALA A CA 6137 C C . ALA A 793 ? 1.1993 0.7591 1.1480 0.3096 -0.0429 -0.0339 793 ALA A C 6138 O O . ALA A 793 ? 1.1916 0.7139 1.1238 0.2966 -0.0506 -0.0301 793 ALA A O 6139 C CB . ALA A 793 ? 0.8955 0.5209 0.8640 0.2864 -0.0385 -0.0200 793 ALA A CB 6140 N N . MET A 794 ? 1.1425 0.7262 1.1002 0.3238 -0.0294 -0.0477 794 MET A N 6141 C CA . MET A 794 ? 1.1635 0.7290 1.1055 0.3272 -0.0228 -0.0602 794 MET A CA 6142 C C . MET A 794 ? 1.0232 0.6213 0.9729 0.3111 -0.0060 -0.0607 794 MET A C 6143 O O . MET A 794 ? 1.0435 0.6822 1.0141 0.3077 0.0048 -0.0580 794 MET A O 6144 C CB . MET A 794 ? 1.0041 0.5684 0.9419 0.3601 -0.0192 -0.0750 794 MET A CB 6145 C CG . MET A 794 ? 1.0167 0.5324 0.9410 0.3818 -0.0383 -0.0782 794 MET A CG 6146 S SD . MET A 794 ? 1.6117 1.0502 1.5027 0.3644 -0.0587 -0.0797 794 MET A SD 6147 C CE . MET A 794 ? 1.0962 0.5391 0.9667 0.3685 -0.0469 -0.1016 794 MET A CE 6148 N N . LEU A 795 ? 1.1570 0.7349 1.0902 0.3008 -0.0063 -0.0632 795 LEU A N 6149 C CA . LEU A 795 ? 0.9900 0.5899 0.9269 0.2888 0.0070 -0.0616 795 LEU A CA 6150 C C . LEU A 795 ? 1.1159 0.7042 1.0305 0.2979 0.0105 -0.0705 795 LEU A C 6151 O O . LEU A 795 ? 1.4969 1.0525 1.3913 0.2974 -0.0029 -0.0762 795 LEU A O 6152 C CB . LEU A 795 ? 0.8549 0.4524 0.7954 0.2674 0.0027 -0.0528 795 LEU A CB 6153 C CG . LEU A 795 ? 0.9780 0.5924 0.9237 0.2583 0.0139 -0.0503 795 LEU A CG 6154 C CD1 . LEU A 795 ? 0.9233 0.5520 0.8824 0.2456 0.0156 -0.0450 795 LEU A CD1 6155 C CD2 . LEU A 795 ? 1.0736 0.6735 1.0048 0.2556 0.0086 -0.0509 795 LEU A CD2 6156 N N . HIS A 796 ? 0.9927 0.6087 0.9097 0.3039 0.0274 -0.0706 796 HIS A N 6157 C CA . HIS A 796 ? 1.0703 0.6819 0.9604 0.3144 0.0329 -0.0773 796 HIS A CA 6158 C C . HIS A 796 ? 1.2211 0.8436 1.1093 0.3006 0.0410 -0.0661 796 HIS A C 6159 O O . HIS A 796 ? 1.1090 0.7555 1.0170 0.2917 0.0539 -0.0554 796 HIS A O 6160 C CB . HIS A 796 ? 0.9304 0.5685 0.8191 0.3367 0.0481 -0.0839 796 HIS A CB 6161 C CG . HIS A 796 ? 1.0043 0.6267 0.8905 0.3590 0.0390 -0.0973 796 HIS A CG 6162 N ND1 . HIS A 796 ? 1.1128 0.7050 0.9650 0.3818 0.0324 -0.1161 796 HIS A ND1 6163 C CD2 . HIS A 796 ? 1.1143 0.7429 1.0251 0.3643 0.0332 -0.0950 796 HIS A CD2 6164 C CE1 . HIS A 796 ? 1.2798 0.8556 1.1373 0.4016 0.0234 -0.1247 796 HIS A CE1 6165 N NE2 . HIS A 796 ? 1.4815 1.0811 1.3751 0.3916 0.0236 -0.1103 796 HIS A NE2 6166 N N . LEU A 797 ? 1.1857 0.7882 1.0504 0.2986 0.0309 -0.0684 797 LEU A N 6167 C CA . LEU A 797 ? 1.0332 0.6428 0.8932 0.2905 0.0354 -0.0564 797 LEU A CA 6168 C C . LEU A 797 ? 1.1742 0.7870 0.9990 0.3029 0.0411 -0.0580 797 LEU A C 6169 O O . LEU A 797 ? 1.3147 0.9098 1.1099 0.3124 0.0286 -0.0720 797 LEU A O 6170 C CB . LEU A 797 ? 1.0094 0.6057 0.8738 0.2789 0.0186 -0.0540 797 LEU A CB 6171 C CG . LEU A 797 ? 1.1084 0.7101 0.9669 0.2765 0.0188 -0.0423 797 LEU A CG 6172 C CD1 . LEU A 797 ? 0.9341 0.5457 0.8112 0.2720 0.0346 -0.0291 797 LEU A CD1 6173 C CD2 . LEU A 797 ? 1.3536 0.9538 1.2220 0.2682 0.0014 -0.0413 797 LEU A CD2 6174 N N . GLN A 798 ? 1.0449 0.6785 0.8702 0.3015 0.0590 -0.0431 798 GLN A N 6175 C CA . GLN A 798 ? 1.0613 0.7025 0.8492 0.3116 0.0667 -0.0386 798 GLN A CA 6176 C C . GLN A 798 ? 1.1490 0.7798 0.9267 0.3040 0.0584 -0.0228 798 GLN A C 6177 O O . GLN A 798 ? 1.3325 0.9622 1.1344 0.2921 0.0629 -0.0065 798 GLN A O 6178 C CB . GLN A 798 ? 1.0911 0.7664 0.8843 0.3137 0.0930 -0.0269 798 GLN A CB 6179 C CG . GLN A 798 ? 1.1392 0.8354 0.9480 0.3260 0.1017 -0.0414 798 GLN A CG 6180 C CD . GLN A 798 ? 1.2066 0.9500 1.0195 0.3304 0.1291 -0.0299 798 GLN A CD 6181 O OE1 . GLN A 798 ? 1.2395 0.9960 1.0310 0.3262 0.1420 -0.0121 798 GLN A OE1 6182 N NE2 . GLN A 798 ? 1.4409 1.2148 1.2829 0.3386 0.1380 -0.0374 798 GLN A NE2 6183 N N . TRP A 799 ? 1.1585 0.7799 0.8994 0.3124 0.0442 -0.0292 799 TRP A N 6184 C CA . TRP A 799 ? 1.1794 0.7945 0.9119 0.3090 0.0312 -0.0151 799 TRP A CA 6185 C C . TRP A 799 ? 1.4107 1.0331 1.0941 0.3198 0.0344 -0.0053 799 TRP A C 6186 O O . TRP A 799 ? 1.4642 1.0907 1.1100 0.3321 0.0355 -0.0211 799 TRP A O 6187 C CB . TRP A 799 ? 1.1341 0.7374 0.8733 0.3050 0.0041 -0.0291 799 TRP A CB 6188 C CG . TRP A 799 ? 1.2260 0.8330 0.9717 0.3026 -0.0104 -0.0148 799 TRP A CG 6189 C CD1 . TRP A 799 ? 1.4081 1.0188 1.1214 0.3095 -0.0264 -0.0106 799 TRP A CD1 6190 C CD2 . TRP A 799 ? 1.2829 0.8935 1.0695 0.2962 -0.0113 -0.0040 799 TRP A CD2 6191 N NE1 . TRP A 799 ? 1.3780 0.9970 1.1146 0.3088 -0.0377 0.0042 799 TRP A NE1 6192 C CE2 . TRP A 799 ? 1.2133 0.8317 0.9945 0.3020 -0.0274 0.0073 799 TRP A CE2 6193 C CE3 . TRP A 799 ? 1.3395 0.9492 1.1641 0.2885 -0.0008 -0.0042 799 TRP A CE3 6194 C CZ2 . TRP A 799 ? 1.0917 0.7179 0.9074 0.3036 -0.0313 0.0176 799 TRP A CZ2 6195 C CZ3 . TRP A 799 ? 1.1192 0.7338 0.9721 0.2886 -0.0042 0.0040 799 TRP A CZ3 6196 C CH2 . TRP A 799 ? 1.0342 0.6574 0.8841 0.2976 -0.0183 0.0145 799 TRP A CH2 6197 N N . PRO A 800 ? 1.4157 1.0376 1.0958 0.3173 0.0354 0.0209 800 PRO A N 6198 C CA . PRO A 800 ? 1.3702 0.9989 1.0008 0.3266 0.0374 0.0375 800 PRO A CA 6199 C C . PRO A 800 ? 1.4216 1.0467 1.0211 0.3349 0.0079 0.0282 800 PRO A C 6200 O O . PRO A 800 ? 1.6032 1.2251 1.2070 0.3356 -0.0065 0.0461 800 PRO A O 6201 C CB . PRO A 800 ? 1.3477 0.9676 0.9946 0.3189 0.0466 0.0718 800 PRO A CB 6202 C CG . PRO A 800 ? 1.2623 0.8723 0.9654 0.3061 0.0523 0.0675 800 PRO A CG 6203 C CD . PRO A 800 ? 1.2251 0.8368 0.9463 0.3070 0.0374 0.0376 800 PRO A CD 6204 N N . TYR A 801 ? 1.4514 1.0761 1.0211 0.3419 -0.0029 -0.0004 801 TYR A N 6205 C CA . TYR A 801 ? 1.5965 1.2174 1.1382 0.3452 -0.0354 -0.0135 801 TYR A CA 6206 C C . TYR A 801 ? 1.6471 1.2792 1.1373 0.3559 -0.0414 0.0066 801 TYR A C 6207 O O . TYR A 801 ? 1.5830 1.2192 1.0790 0.3553 -0.0638 0.0204 801 TYR A O 6208 C CB . TYR A 801 ? 1.6233 1.2308 1.1376 0.3500 -0.0464 -0.0511 801 TYR A CB 6209 C CG . TYR A 801 ? 1.7581 1.3577 1.2500 0.3466 -0.0850 -0.0685 801 TYR A CG 6210 C CD1 . TYR A 801 ? 1.7840 1.3886 1.3207 0.3310 -0.1085 -0.0619 801 TYR A CD1 6211 C CD2 . TYR A 801 ? 1.8162 1.4071 1.2426 0.3588 -0.0984 -0.0926 801 TYR A CD2 6212 C CE1 . TYR A 801 ? 1.8847 1.4899 1.4080 0.3237 -0.1456 -0.0761 801 TYR A CE1 6213 C CE2 . TYR A 801 ? 2.0635 1.6462 1.4698 0.3518 -0.1379 -0.1102 801 TYR A CE2 6214 C CZ . TYR A 801 ? 2.1492 1.7412 1.6074 0.3323 -0.1621 -0.1005 801 TYR A CZ 6215 O OH . TYR A 801 ? 2.2863 1.8779 1.7314 0.3213 -0.2032 -0.1164 801 TYR A OH 6216 N N . LYS A 802 ? 1.6703 1.3121 1.1099 0.3673 -0.0210 0.0098 802 LYS A N 6217 C CA . LYS A 802 ? 1.7205 1.3745 1.1003 0.3781 -0.0256 0.0303 802 LYS A CA 6218 C C . LYS A 802 ? 1.7452 1.4156 1.1009 0.3816 0.0113 0.0595 802 LYS A C 6219 O O . LYS A 802 ? 1.7455 1.4261 1.1160 0.3803 0.0399 0.0525 802 LYS A O 6220 C CB . LYS A 802 ? 1.7925 1.4469 1.1084 0.3905 -0.0481 -0.0020 802 LYS A CB 6221 C CG . LYS A 802 ? 1.7935 1.4369 1.1239 0.3827 -0.0915 -0.0224 802 LYS A CG 6222 C CD . LYS A 802 ? 1.8662 1.5075 1.1237 0.3932 -0.1178 -0.0513 802 LYS A CD 6223 C CE . LYS A 802 ? 1.8854 1.5218 1.1616 0.3800 -0.1644 -0.0677 802 LYS A CE 6224 N NZ . LYS A 802 ? 2.0007 1.6332 1.2022 0.3877 -0.1956 -0.0961 802 LYS A NZ 6225 N N . TYR A 803 ? 1.8668 1.5427 1.1872 0.3853 0.0093 0.0948 803 TYR A N 6226 C CA . TYR A 803 ? 1.8604 1.5547 1.1472 0.3859 0.0423 0.1282 803 TYR A CA 6227 C C . TYR A 803 ? 1.8794 1.5899 1.0800 0.4022 0.0327 0.1369 803 TYR A C 6228 O O . TYR A 803 ? 1.9089 1.6100 1.0905 0.4058 0.0064 0.1580 803 TYR A O 6229 C CB . TYR A 803 ? 1.7889 1.4661 1.1173 0.3706 0.0527 0.1734 803 TYR A CB 6230 C CG . TYR A 803 ? 1.8816 1.5754 1.1821 0.3636 0.0863 0.2145 803 TYR A CG 6231 C CD1 . TYR A 803 ? 1.9793 1.6621 1.2438 0.3639 0.0817 0.2609 803 TYR A CD1 6232 C CD2 . TYR A 803 ? 1.9719 1.6955 1.2842 0.3563 0.1221 0.2098 803 TYR A CD2 6233 C CE1 . TYR A 803 ? 1.9752 1.6728 1.2142 0.3529 0.1130 0.3037 803 TYR A CE1 6234 C CE2 . TYR A 803 ? 2.0195 1.7673 1.3116 0.3457 0.1543 0.2506 803 TYR A CE2 6235 C CZ . TYR A 803 ? 1.9639 1.6969 1.2184 0.3420 0.1502 0.2985 803 TYR A CZ 6236 O OH . TYR A 803 ? 1.9478 1.7044 1.1820 0.3270 0.1829 0.3441 803 TYR A OH 6237 N N . ASN A 804 ? 1.9172 1.6549 1.0647 0.4146 0.0540 0.1202 804 ASN A N 6238 C CA . ASN A 804 ? 1.9759 1.7326 1.0306 0.4331 0.0463 0.1197 804 ASN A CA 6239 C C . ASN A 804 ? 1.9876 1.7261 1.0165 0.4408 -0.0035 0.0929 804 ASN A C 6240 O O . ASN A 804 ? 2.1982 1.9368 1.1954 0.4437 -0.0267 0.1200 804 ASN A O 6241 C CB . ASN A 804 ? 2.0037 1.7742 1.0235 0.4292 0.0627 0.1796 804 ASN A CB 6242 C CG . ASN A 804 ? 2.0112 1.8028 1.0609 0.4147 0.1104 0.2108 804 ASN A CG 6243 O OD1 . ASN A 804 ? 1.9600 1.7484 1.0782 0.4032 0.1253 0.1958 804 ASN A OD1 6244 N ND2 . ASN A 804 ? 2.1007 1.9172 1.0992 0.4133 0.1337 0.2565 804 ASN A ND2 6245 N N . ASN A 805 ? 1.9806 1.7034 1.0270 0.4425 -0.0215 0.0417 805 ASN A N 6246 C CA . ASN A 805 ? 2.0267 1.7341 1.0512 0.4449 -0.0699 0.0096 805 ASN A CA 6247 C C . ASN A 805 ? 2.1782 1.8763 1.2588 0.4308 -0.1030 0.0299 805 ASN A C 6248 O O . ASN A 805 ? 2.2154 1.9085 1.2933 0.4278 -0.1446 0.0067 805 ASN A O 6249 C CB . ASN A 805 ? 2.2747 1.9988 1.1956 0.4638 -0.0833 0.0034 805 ASN A CB 6250 C CG . ASN A 805 ? 2.4373 2.1748 1.2966 0.4836 -0.0524 -0.0250 805 ASN A CG 6251 O OD1 . ASN A 805 ? 2.3260 2.0504 1.2150 0.4861 -0.0383 -0.0595 805 ASN A OD1 6252 N ND2 . ASN A 805 ? 2.4805 2.2466 1.2521 0.5005 -0.0413 -0.0100 805 ASN A ND2 6253 N N . ASN A 806 ? 2.1837 1.8808 1.3157 0.4224 -0.0853 0.0721 806 ASN A N 6254 C CA . ASN A 806 ? 1.8735 1.5648 1.0593 0.4155 -0.1125 0.0920 806 ASN A CA 6255 C C . ASN A 806 ? 1.7874 1.4635 1.0637 0.4005 -0.1028 0.0857 806 ASN A C 6256 O O . ASN A 806 ? 1.7559 1.4241 1.0601 0.3942 -0.0682 0.0966 806 ASN A O 6257 C CB . ASN A 806 ? 1.8823 1.5764 1.0485 0.4227 -0.1076 0.1464 806 ASN A CB 6258 C CG . ASN A 806 ? 1.9834 1.6958 1.0569 0.4382 -0.1225 0.1572 806 ASN A CG 6259 O OD1 . ASN A 806 ? 2.2542 1.9771 1.3085 0.4452 -0.1638 0.1520 806 ASN A OD1 6260 N ND2 . ASN A 806 ? 2.0043 1.7266 1.0195 0.4433 -0.0892 0.1729 806 ASN A ND2 6261 N N . THR A 807 ? 1.7532 1.4303 1.0744 0.3936 -0.1341 0.0689 807 THR A N 6262 C CA . THR A 807 ? 1.6824 1.3504 1.0837 0.3798 -0.1279 0.0596 807 THR A CA 6263 C C . THR A 807 ? 1.6479 1.3074 1.0948 0.3803 -0.1092 0.0955 807 THR A C 6264 O O . THR A 807 ? 1.9992 1.6613 1.4382 0.3910 -0.1202 0.1266 807 THR A O 6265 C CB . THR A 807 ? 1.6672 1.3480 1.1053 0.3711 -0.1660 0.0394 807 THR A CB 6266 O OG1 . THR A 807 ? 1.7373 1.4175 1.1288 0.3683 -0.1896 0.0055 807 THR A OG1 6267 C CG2 . THR A 807 ? 1.5951 1.2697 1.1071 0.3560 -0.1564 0.0276 807 THR A CG2 6268 N N . LEU A 808 ? 1.5664 1.2123 1.0587 0.3697 -0.0833 0.0903 808 LEU A N 6269 C CA . LEU A 808 ? 1.5018 1.1323 1.0388 0.3680 -0.0677 0.1167 808 LEU A CA 6270 C C . LEU A 808 ? 1.4380 1.0722 1.0408 0.3635 -0.0801 0.1035 808 LEU A C 6271 O O . LEU A 808 ? 1.5028 1.1442 1.1279 0.3736 -0.0982 0.1173 808 LEU A O 6272 C CB . LEU A 808 ? 1.4853 1.1025 1.0279 0.3578 -0.0312 0.1218 808 LEU A CB 6273 C CG . LEU A 808 ? 1.5663 1.1909 1.0499 0.3605 -0.0110 0.1360 808 LEU A CG 6274 C CD1 . LEU A 808 ? 1.5731 1.1943 1.0789 0.3472 0.0242 0.1439 808 LEU A CD1 6275 C CD2 . LEU A 808 ? 1.6162 1.2364 1.0585 0.3706 -0.0194 0.1746 808 LEU A CD2 6276 N N . LEU A 809 ? 1.4400 1.0728 1.0731 0.3503 -0.0697 0.0779 809 LEU A N 6277 C CA . LEU A 809 ? 1.3307 0.9730 1.0210 0.3436 -0.0790 0.0646 809 LEU A CA 6278 C C . LEU A 809 ? 1.3743 1.0312 1.0639 0.3331 -0.0993 0.0360 809 LEU A C 6279 O O . LEU A 809 ? 1.5881 1.2327 1.2652 0.3247 -0.0905 0.0157 809 LEU A O 6280 C CB . LEU A 809 ? 1.2907 0.9170 1.0184 0.3348 -0.0533 0.0616 809 LEU A CB 6281 C CG . LEU A 809 ? 1.3234 0.9280 1.0634 0.3410 -0.0382 0.0866 809 LEU A CG 6282 C CD1 . LEU A 809 ? 1.4746 1.0647 1.2474 0.3290 -0.0167 0.0782 809 LEU A CD1 6283 C CD2 . LEU A 809 ? 1.3102 0.9213 1.0742 0.3565 -0.0559 0.0989 809 LEU A CD2 6284 N N . TYR A 810 ? 1.3782 1.0609 1.0836 0.3334 -0.1280 0.0352 810 TYR A N 6285 C CA . TYR A 810 ? 1.3910 1.0854 1.0959 0.3185 -0.1532 0.0108 810 TYR A CA 6286 C C . TYR A 810 ? 1.3312 1.0374 1.0962 0.3018 -0.1519 0.0019 810 TYR A C 6287 O O . TYR A 810 ? 1.3014 1.0393 1.1124 0.3036 -0.1579 0.0134 810 TYR A O 6288 C CB . TYR A 810 ? 1.4471 1.1710 1.1383 0.3235 -0.1883 0.0161 810 TYR A CB 6289 C CG . TYR A 810 ? 1.4956 1.2321 1.1890 0.3033 -0.2206 -0.0083 810 TYR A CG 6290 C CD1 . TYR A 810 ? 1.5807 1.2950 1.2136 0.3001 -0.2358 -0.0306 810 TYR A CD1 6291 C CD2 . TYR A 810 ? 1.4712 1.2424 1.2262 0.2869 -0.2363 -0.0090 810 TYR A CD2 6292 C CE1 . TYR A 810 ? 1.6384 1.3544 1.2714 0.2790 -0.2692 -0.0548 810 TYR A CE1 6293 C CE2 . TYR A 810 ? 1.5286 1.3094 1.2888 0.2624 -0.2678 -0.0284 810 TYR A CE2 6294 C CZ . TYR A 810 ? 1.6112 1.3594 1.3100 0.2575 -0.2860 -0.0520 810 TYR A CZ 6295 O OH . TYR A 810 ? 1.6715 1.4200 1.3741 0.2303 -0.3210 -0.0732 810 TYR A OH 6296 N N . ILE A 811 ? 1.3241 1.0071 1.0872 0.2878 -0.1437 -0.0175 811 ILE A N 6297 C CA . ILE A 811 ? 1.2846 0.9752 1.0978 0.2710 -0.1396 -0.0223 811 ILE A CA 6298 C C . ILE A 811 ? 1.3363 1.0557 1.1761 0.2516 -0.1702 -0.0277 811 ILE A C 6299 O O . ILE A 811 ? 1.4229 1.1292 1.2346 0.2404 -0.1946 -0.0437 811 ILE A O 6300 C CB . ILE A 811 ? 1.2881 0.9425 1.0895 0.2633 -0.1245 -0.0385 811 ILE A CB 6301 C CG1 . ILE A 811 ? 1.2070 0.8445 0.9927 0.2786 -0.0938 -0.0315 811 ILE A CG1 6302 C CG2 . ILE A 811 ? 1.2077 0.8698 1.0555 0.2447 -0.1226 -0.0397 811 ILE A CG2 6303 C CD1 . ILE A 811 ? 1.1947 0.8064 0.9746 0.2753 -0.0789 -0.0457 811 ILE A CD1 6304 N N . LEU A 812 ? 1.2892 1.0497 1.1838 0.2474 -0.1688 -0.0149 812 LEU A N 6305 C CA . LEU A 812 ? 1.3343 1.1372 1.2671 0.2259 -0.1947 -0.0147 812 LEU A CA 6306 C C . LEU A 812 ? 1.3392 1.1303 1.2942 0.1976 -0.1921 -0.0224 812 LEU A C 6307 O O . LEU A 812 ? 1.4130 1.1856 1.3566 0.1737 -0.2157 -0.0351 812 LEU A O 6308 C CB . LEU A 812 ? 1.4948 1.3585 1.4785 0.2390 -0.1922 0.0044 812 LEU A CB 6309 C CG . LEU A 812 ? 1.4062 1.3210 1.4042 0.2409 -0.2246 0.0115 812 LEU A CG 6310 C CD1 . LEU A 812 ? 1.4943 1.3784 1.4302 0.2542 -0.2410 0.0071 812 LEU A CD1 6311 C CD2 . LEU A 812 ? 1.2949 1.2639 1.3398 0.2660 -0.2159 0.0303 812 LEU A CD2 6312 N N . HIS A 813 ? 1.2728 1.0708 1.2563 0.2004 -0.1648 -0.0143 813 HIS A N 6313 C CA . HIS A 813 ? 1.2850 1.0760 1.2897 0.1756 -0.1596 -0.0153 813 HIS A CA 6314 C C . HIS A 813 ? 1.2181 0.9900 1.2216 0.1889 -0.1269 -0.0132 813 HIS A C 6315 O O . HIS A 813 ? 1.4016 1.1860 1.4099 0.2123 -0.1091 -0.0072 813 HIS A O 6316 C CB . HIS A 813 ? 1.4218 1.2782 1.4831 0.1548 -0.1690 -0.0016 813 HIS A CB 6317 C CG . HIS A 813 ? 1.6296 1.4815 1.7111 0.1242 -0.1659 0.0030 813 HIS A CG 6318 N ND1 . HIS A 813 ? 1.8218 1.6249 1.8827 0.0971 -0.1864 -0.0062 813 HIS A ND1 6319 C CD2 . HIS A 813 ? 1.5660 1.4537 1.6829 0.1171 -0.1453 0.0168 813 HIS A CD2 6320 C CE1 . HIS A 813 ? 1.8790 1.6854 1.9632 0.0730 -0.1793 0.0056 813 HIS A CE1 6321 N NE2 . HIS A 813 ? 1.7778 1.6392 1.8952 0.0841 -0.1535 0.0201 813 HIS A NE2 6322 N N . TYR A 814 ? 1.2131 0.9516 1.2092 0.1743 -0.1217 -0.0181 814 TYR A N 6323 C CA . TYR A 814 ? 1.1470 0.8736 1.1439 0.1844 -0.0945 -0.0161 814 TYR A CA 6324 C C . TYR A 814 ? 1.1521 0.8896 1.1734 0.1621 -0.0908 -0.0076 814 TYR A C 6325 O O . TYR A 814 ? 1.2382 0.9552 1.2570 0.1384 -0.1081 -0.0077 814 TYR A O 6326 C CB . TYR A 814 ? 1.0983 0.7721 1.0543 0.1976 -0.0870 -0.0286 814 TYR A CB 6327 C CG . TYR A 814 ? 1.2845 0.9141 1.2190 0.1847 -0.1005 -0.0395 814 TYR A CG 6328 C CD1 . TYR A 814 ? 1.4812 1.0851 1.3878 0.1812 -0.1236 -0.0528 814 TYR A CD1 6329 C CD2 . TYR A 814 ? 1.2887 0.8982 1.2270 0.1786 -0.0919 -0.0377 814 TYR A CD2 6330 C CE1 . TYR A 814 ? 1.4226 0.9762 1.3063 0.1732 -0.1373 -0.0662 814 TYR A CE1 6331 C CE2 . TYR A 814 ? 1.1335 0.6953 1.0516 0.1711 -0.1057 -0.0470 814 TYR A CE2 6332 C CZ . TYR A 814 ? 1.1977 0.7286 1.0887 0.1692 -0.1282 -0.0624 814 TYR A CZ 6333 O OH . TYR A 814 ? 1.2183 0.6925 1.0862 0.1652 -0.1434 -0.0749 814 TYR A OH 6334 N N . ASP A 815 ? 1.1024 0.8694 1.1437 0.1698 -0.0690 0.0002 815 ASP A N 6335 C CA . ASP A 815 ? 1.1396 0.9278 1.2014 0.1508 -0.0619 0.0119 815 ASP A CA 6336 C C . ASP A 815 ? 1.0825 0.8427 1.1260 0.1592 -0.0443 0.0089 815 ASP A C 6337 O O . ASP A 815 ? 1.0161 0.7588 1.0438 0.1810 -0.0326 -0.0009 815 ASP A O 6338 C CB . ASP A 815 ? 1.1656 1.0257 1.2667 0.1528 -0.0516 0.0232 815 ASP A CB 6339 C CG . ASP A 815 ? 1.3230 1.2246 1.4521 0.1397 -0.0718 0.0298 815 ASP A CG 6340 O OD1 . ASP A 815 ? 1.4567 1.4056 1.6086 0.1588 -0.0680 0.0314 815 ASP A OD1 6341 O OD2 . ASP A 815 ? 1.3368 1.2222 1.4657 0.1107 -0.0936 0.0329 815 ASP A OD2 6342 N N . ILE A 816 ? 1.1043 0.8619 1.1507 0.1396 -0.0441 0.0197 816 ILE A N 6343 C CA . ILE A 816 ? 1.0705 0.8024 1.0982 0.1457 -0.0328 0.0186 816 ILE A CA 6344 C C . ILE A 816 ? 1.1066 0.8792 1.1470 0.1372 -0.0182 0.0330 816 ILE A C 6345 O O . ILE A 816 ? 1.1916 0.9919 1.2496 0.1135 -0.0224 0.0508 816 ILE A O 6346 C CB . ILE A 816 ? 1.0907 0.7652 1.0967 0.1356 -0.0491 0.0179 816 ILE A CB 6347 C CG1 . ILE A 816 ? 1.0985 0.7355 1.0856 0.1472 -0.0617 0.0005 816 ILE A CG1 6348 C CG2 . ILE A 816 ? 1.0575 0.7123 1.0475 0.1450 -0.0396 0.0183 816 ILE A CG2 6349 C CD1 . ILE A 816 ? 1.2362 0.8157 1.2023 0.1393 -0.0811 -0.0040 816 ILE A CD1 6350 N N . ASP A 817 ? 1.0667 0.8447 1.0966 0.1551 -0.0014 0.0256 817 ASP A N 6351 C CA . ASP A 817 ? 1.1414 0.9534 1.1714 0.1506 0.0127 0.0358 817 ASP A CA 6352 C C . ASP A 817 ? 1.1302 0.9075 1.1339 0.1521 0.0116 0.0357 817 ASP A C 6353 O O . ASP A 817 ? 1.3076 1.0589 1.2985 0.1689 0.0127 0.0197 817 ASP A O 6354 C CB . ASP A 817 ? 1.4829 1.3359 1.5206 0.1720 0.0315 0.0245 817 ASP A CB 6355 C CG . ASP A 817 ? 1.7008 1.6197 1.7673 0.1663 0.0399 0.0363 817 ASP A CG 6356 O OD1 . ASP A 817 ? 1.8239 1.7656 1.9013 0.1400 0.0362 0.0579 817 ASP A OD1 6357 O OD2 . ASP A 817 ? 1.5523 1.5012 1.6325 0.1883 0.0500 0.0254 817 ASP A OD2 6358 N N . GLY A 818 ? 1.1716 0.9519 1.1692 0.1334 0.0084 0.0561 818 GLY A N 6359 C CA . GLY A 818 ? 1.1570 0.9074 1.1301 0.1356 0.0040 0.0601 818 GLY A CA 6360 C C . GLY A 818 ? 1.1751 0.8706 1.1407 0.1250 -0.0169 0.0698 818 GLY A C 6361 O O . GLY A 818 ? 1.1870 0.8645 1.1636 0.1126 -0.0288 0.0718 818 GLY A O 6362 N N . PRO A 819 ? 1.2448 0.9117 1.1906 0.1315 -0.0235 0.0743 819 PRO A N 6363 C CA . PRO A 819 ? 1.1708 0.7795 1.1061 0.1276 -0.0441 0.0834 819 PRO A CA 6364 C C . PRO A 819 ? 1.0972 0.6669 1.0319 0.1468 -0.0525 0.0595 819 PRO A C 6365 O O . PRO A 819 ? 1.0697 0.6189 0.9948 0.1669 -0.0561 0.0512 819 PRO A O 6366 C CB . PRO A 819 ? 1.1747 0.7799 1.0906 0.1354 -0.0459 0.0952 819 PRO A CB 6367 C CG . PRO A 819 ? 1.1334 0.7812 1.0493 0.1519 -0.0297 0.0768 819 PRO A CG 6368 C CD . PRO A 819 ? 1.2090 0.8982 1.1405 0.1453 -0.0138 0.0696 819 PRO A CD 6369 N N . MET A 820 ? 1.0890 0.6548 1.0337 0.1416 -0.0554 0.0492 820 MET A N 6370 C CA . MET A 820 ? 1.0473 0.5826 0.9858 0.1604 -0.0609 0.0264 820 MET A CA 6371 C C . MET A 820 ? 1.0882 0.5933 1.0256 0.1471 -0.0777 0.0223 820 MET A C 6372 O O . MET A 820 ? 1.4352 0.9678 1.3883 0.1268 -0.0785 0.0299 820 MET A O 6373 C CB . MET A 820 ? 1.1170 0.6886 1.0630 0.1766 -0.0433 0.0100 820 MET A CB 6374 C CG . MET A 820 ? 1.1619 0.7125 1.0994 0.1959 -0.0443 -0.0099 820 MET A CG 6375 S SD . MET A 820 ? 1.4482 1.0349 1.3936 0.2113 -0.0236 -0.0214 820 MET A SD 6376 C CE . MET A 820 ? 0.9013 0.5256 0.8622 0.1984 -0.0163 -0.0146 820 MET A CE 6377 N N . ASN A 821 ? 1.0892 0.5401 1.0080 0.1601 -0.0920 0.0086 821 ASN A N 6378 C CA . ASN A 821 ? 1.1261 0.5428 1.0357 0.1526 -0.1099 -0.0040 821 ASN A CA 6379 C C . ASN A 821 ? 1.0924 0.5120 0.9888 0.1796 -0.1026 -0.0297 821 ASN A C 6380 O O . ASN A 821 ? 1.1889 0.6118 1.0791 0.2052 -0.0903 -0.0381 821 ASN A O 6381 C CB . ASN A 821 ? 1.1986 0.5416 1.0896 0.1475 -0.1343 -0.0029 821 ASN A CB 6382 C CG . ASN A 821 ? 1.5182 0.8533 1.4203 0.1144 -0.1438 0.0280 821 ASN A CG 6383 O OD1 . ASN A 821 ? 1.6809 1.0689 1.6060 0.0896 -0.1351 0.0460 821 ASN A OD1 6384 N ND2 . ASN A 821 ? 1.9875 1.2571 1.8729 0.1154 -0.1611 0.0359 821 ASN A ND2 6385 N N . CYS A 822 ? 1.2108 0.6340 1.1032 0.1730 -0.1107 -0.0400 822 CYS A N 6386 C CA . CYS A 822 ? 1.2512 0.6815 1.1265 0.1969 -0.1027 -0.0601 822 CYS A CA 6387 C C . CYS A 822 ? 1.3965 0.7888 1.2446 0.1962 -0.1245 -0.0793 822 CYS A C 6388 O O . CYS A 822 ? 1.5532 0.9266 1.4048 0.1702 -0.1468 -0.0759 822 CYS A O 6389 C CB . CYS A 822 ? 1.0438 0.5322 0.9379 0.1965 -0.0853 -0.0530 822 CYS A CB 6390 S SG . CYS A 822 ? 2.1477 1.6749 2.0634 0.2037 -0.0597 -0.0405 822 CYS A SG 6391 N N . THR A 823 ? 1.3253 0.7098 1.1456 0.2236 -0.1179 -0.0994 823 THR A N 6392 C CA . THR A 823 ? 1.4515 0.7994 1.2353 0.2293 -0.1373 -0.1229 823 THR A CA 6393 C C . THR A 823 ? 1.3537 0.7325 1.1159 0.2521 -0.1216 -0.1333 823 THR A C 6394 O O . THR A 823 ? 1.4267 0.8333 1.1940 0.2715 -0.0960 -0.1291 823 THR A O 6395 C CB . THR A 823 ? 1.2232 0.5034 0.9786 0.2460 -0.1506 -0.1424 823 THR A CB 6396 O OG1 . THR A 823 ? 1.3182 0.5666 1.0931 0.2249 -0.1639 -0.1264 823 THR A OG1 6397 C CG2 . THR A 823 ? 1.2970 0.5308 1.0099 0.2489 -0.1755 -0.1709 823 THR A CG2 6398 N N . SER A 824 ? 1.2339 0.6093 0.9719 0.2473 -0.1382 -0.1448 824 SER A N 6399 C CA . SER A 824 ? 1.2363 0.6380 0.9459 0.2679 -0.1257 -0.1518 824 SER A CA 6400 C C . SER A 824 ? 1.3111 0.6716 0.9649 0.2900 -0.1365 -0.1833 824 SER A C 6401 O O . SER A 824 ? 1.5384 0.8509 1.1721 0.2798 -0.1661 -0.2018 824 SER A O 6402 C CB . SER A 824 ? 1.2626 0.7008 0.9820 0.2513 -0.1356 -0.1392 824 SER A CB 6403 O OG . SER A 824 ? 1.3419 0.7975 1.0251 0.2704 -0.1286 -0.1445 824 SER A OG 6404 N N . ASP A 825 ? 1.2964 0.6762 0.9247 0.3197 -0.1123 -0.1899 825 ASP A N 6405 C CA . ASP A 825 ? 1.3623 0.7121 0.9331 0.3474 -0.1167 -0.2218 825 ASP A CA 6406 C C . ASP A 825 ? 1.6316 0.9783 1.1599 0.3413 -0.1389 -0.2342 825 ASP A C 6407 O O . ASP A 825 ? 1.7528 1.0647 1.2261 0.3591 -0.1524 -0.2659 825 ASP A O 6408 C CB . ASP A 825 ? 1.3430 0.7298 0.9029 0.3795 -0.0804 -0.2210 825 ASP A CB 6409 C CG . ASP A 825 ? 1.7410 1.1853 1.3046 0.3754 -0.0596 -0.1962 825 ASP A CG 6410 O OD1 . ASP A 825 ? 1.8259 1.2856 1.4170 0.3502 -0.0682 -0.1748 825 ASP A OD1 6411 O OD2 . ASP A 825 ? 1.6737 1.1484 1.2131 0.3982 -0.0343 -0.1968 825 ASP A OD2 6412 N N . MET A 826 ? 1.6450 1.0292 1.1975 0.3188 -0.1438 -0.2103 826 MET A N 6413 C CA . MET A 826 ? 1.5310 0.9191 1.0522 0.3093 -0.1704 -0.2174 826 MET A CA 6414 C C . MET A 826 ? 1.5454 0.9370 1.1114 0.2723 -0.1981 -0.2043 826 MET A C 6415 O O . MET A 826 ? 1.5929 0.9993 1.2135 0.2567 -0.1881 -0.1826 826 MET A O 6416 C CB . MET A 826 ? 1.5428 0.9823 1.0477 0.3220 -0.1513 -0.1982 826 MET A CB 6417 C CG . MET A 826 ? 1.5940 1.0432 1.0562 0.3550 -0.1208 -0.2058 826 MET A CG 6418 S SD . MET A 826 ? 1.7298 1.2337 1.1701 0.3638 -0.1007 -0.1759 826 MET A SD 6419 C CE . MET A 826 ? 1.6720 1.1902 1.0693 0.3981 -0.0621 -0.1856 826 MET A CE 6420 N N . GLU A 827 ? 1.6360 1.0195 1.1786 0.2580 -0.2330 -0.2175 827 GLU A N 6421 C CA . GLU A 827 ? 1.6731 1.0719 1.2619 0.2210 -0.2606 -0.2042 827 GLU A CA 6422 C C . GLU A 827 ? 1.6433 1.1120 1.2730 0.2179 -0.2478 -0.1709 827 GLU A C 6423 O O . GLU A 827 ? 1.6833 1.1803 1.2852 0.2340 -0.2463 -0.1663 827 GLU A O 6424 C CB . GLU A 827 ? 1.8437 1.2159 1.3970 0.2046 -0.3057 -0.2300 827 GLU A CB 6425 C CG . GLU A 827 ? 1.9407 1.3462 1.5464 0.1642 -0.3355 -0.2134 827 GLU A CG 6426 C CD . GLU A 827 ? 2.0823 1.4752 1.6529 0.1477 -0.3823 -0.2373 827 GLU A CD 6427 O OE1 . GLU A 827 ? 2.1470 1.4961 1.6456 0.1687 -0.3922 -0.2703 827 GLU A OE1 6428 O OE2 . GLU A 827 ? 2.1262 1.5575 1.7413 0.1141 -0.4095 -0.2239 827 GLU A OE2 6429 N N . ILE A 828 ? 1.6019 1.0965 1.2942 0.1995 -0.2388 -0.1474 828 ILE A N 6430 C CA . ILE A 828 ? 1.6388 1.1955 1.3722 0.2002 -0.2271 -0.1189 828 ILE A CA 6431 C C . ILE A 828 ? 1.7025 1.2957 1.4532 0.1804 -0.2616 -0.1149 828 ILE A C 6432 O O . ILE A 828 ? 1.7237 1.3040 1.4871 0.1511 -0.2906 -0.1246 828 ILE A O 6433 C CB . ILE A 828 ? 1.4490 1.0250 1.2394 0.1914 -0.2036 -0.0982 828 ILE A CB 6434 C CG1 . ILE A 828 ? 1.8208 1.3824 1.6419 0.1583 -0.2219 -0.0993 828 ILE A CG1 6435 C CG2 . ILE A 828 ? 1.3438 0.8967 1.1209 0.2127 -0.1703 -0.0990 828 ILE A CG2 6436 C CD1 . ILE A 828 ? 1.8957 1.5171 1.7736 0.1344 -0.2326 -0.0786 828 ILE A CD1 6437 N N . ASN A 829 ? 1.6526 1.2907 1.4044 0.1961 -0.2601 -0.0994 829 ASN A N 6438 C CA . ASN A 829 ? 1.6841 1.3692 1.4552 0.1834 -0.2929 -0.0928 829 ASN A CA 6439 C C . ASN A 829 ? 1.7902 1.4486 1.5187 0.1674 -0.3345 -0.1199 829 ASN A C 6440 O O . ASN A 829 ? 2.0700 1.7417 1.8312 0.1343 -0.3650 -0.1233 829 ASN A O 6441 C CB . ASN A 829 ? 1.6370 1.3695 1.4854 0.1586 -0.2951 -0.0746 829 ASN A CB 6442 C CG . ASN A 829 ? 1.6090 1.4153 1.4959 0.1631 -0.3089 -0.0549 829 ASN A CG 6443 O OD1 . ASN A 829 ? 1.6220 1.4415 1.4839 0.1913 -0.3066 -0.0469 829 ASN A OD1 6444 N ND2 . ASN A 829 ? 1.6077 1.4654 1.5574 0.1361 -0.3229 -0.0444 829 ASN A ND2 6445 N N . PRO A 830 ? 1.8133 1.4358 1.4677 0.1895 -0.3361 -0.1395 830 PRO A N 6446 C CA . PRO A 830 ? 1.8830 1.4708 1.4853 0.1779 -0.3758 -0.1720 830 PRO A CA 6447 C C . PRO A 830 ? 1.9357 1.5733 1.5450 0.1642 -0.4176 -0.1679 830 PRO A C 6448 O O . PRO A 830 ? 2.0845 1.7031 1.6783 0.1387 -0.4592 -0.1919 830 PRO A O 6449 C CB . PRO A 830 ? 1.9056 1.4574 1.4267 0.2133 -0.3575 -0.1895 830 PRO A CB 6450 C CG . PRO A 830 ? 1.8593 1.4508 1.3925 0.2388 -0.3211 -0.1569 830 PRO A CG 6451 C CD . PRO A 830 ? 1.7933 1.4080 1.4069 0.2254 -0.3013 -0.1325 830 PRO A CD 6452 N N . LEU A 831 ? 1.8526 1.5509 1.4846 0.1816 -0.4087 -0.1381 831 LEU A N 6453 C CA . LEU A 831 ? 1.8518 1.6087 1.4970 0.1746 -0.4472 -0.1290 831 LEU A CA 6454 C C . LEU A 831 ? 1.8199 1.6368 1.5601 0.1466 -0.4568 -0.1088 831 LEU A C 6455 O O . LEU A 831 ? 1.8030 1.6860 1.5770 0.1406 -0.4857 -0.0955 831 LEU A O 6456 C CB . LEU A 831 ? 1.8185 1.6075 1.4367 0.2124 -0.4341 -0.1048 831 LEU A CB 6457 C CG . LEU A 831 ? 1.8370 1.5779 1.3767 0.2433 -0.4038 -0.1112 831 LEU A CG 6458 C CD1 . LEU A 831 ? 1.8825 1.6550 1.4073 0.2753 -0.3886 -0.0777 831 LEU A CD1 6459 C CD2 . LEU A 831 ? 1.9749 1.6736 1.4311 0.2420 -0.4299 -0.1491 831 LEU A CD2 6460 N N . ARG A 832 ? 1.9005 1.6980 1.6825 0.1312 -0.4315 -0.1056 832 ARG A N 6461 C CA . ARG A 832 ? 2.0004 1.8563 1.8710 0.1122 -0.4229 -0.0813 832 ARG A CA 6462 C C . ARG A 832 ? 2.0042 1.9261 1.9104 0.1438 -0.4041 -0.0515 832 ARG A C 6463 O O . ARG A 832 ? 2.1645 2.0668 2.0292 0.1798 -0.3833 -0.0458 832 ARG A O 6464 C CB . ARG A 832 ? 1.8670 1.7608 1.7803 0.0673 -0.4676 -0.0853 832 ARG A CB 6465 C CG . ARG A 832 ? 1.8992 1.7189 1.7790 0.0320 -0.4934 -0.1153 832 ARG A CG 6466 C CD . ARG A 832 ? 2.0030 1.7813 1.9086 0.0147 -0.4657 -0.1110 832 ARG A CD 6467 N NE . ARG A 832 ? 2.2580 1.9640 2.1071 0.0470 -0.4319 -0.1239 832 ARG A NE 6468 C CZ . ARG A 832 ? 2.2735 1.9387 2.1334 0.0427 -0.4047 -0.1207 832 ARG A CZ 6469 N NH1 . ARG A 832 ? 2.2673 1.9529 2.1873 0.0071 -0.4058 -0.1034 832 ARG A NH1 6470 N NH2 . ARG A 832 ? 2.2136 1.8232 2.0252 0.0739 -0.3765 -0.1326 832 ARG A NH2 6471 N N . ILE A 833 ? 1.6779 1.6785 1.6602 0.1302 -0.4137 -0.0326 833 ILE A N 6472 C CA . ILE A 833 ? 1.5945 1.6612 1.6204 0.1622 -0.3979 -0.0057 833 ILE A CA 6473 C C . ILE A 833 ? 1.6298 1.7847 1.7463 0.1386 -0.4064 0.0096 833 ILE A C 6474 O O . ILE A 833 ? 1.8733 2.0287 2.0162 0.0957 -0.4169 0.0031 833 ILE A O 6475 C CB . ILE A 833 ? 1.5322 1.5634 1.5487 0.1941 -0.3482 0.0036 833 ILE A CB 6476 C CG1 . ILE A 833 ? 1.5826 1.6333 1.5891 0.2384 -0.3413 0.0223 833 ILE A CG1 6477 C CG2 . ILE A 833 ? 1.5570 1.6148 1.6364 0.1813 -0.3206 0.0126 833 ILE A CG2 6478 C CD1 . ILE A 833 ? 1.5106 1.5265 1.4415 0.2532 -0.3614 0.0169 833 ILE A CD1 6479 N N . LYS A 834 ? 1.5551 1.7853 1.7198 0.1668 -0.4018 0.0312 834 LYS A N 6480 C CA . LYS A 834 ? 1.6753 1.9982 1.9304 0.1518 -0.3983 0.0474 834 LYS A CA 6481 C C . LYS A 834 ? 1.6083 1.9541 1.8958 0.1902 -0.3541 0.0626 834 LYS A C 6482 O O . LYS A 834 ? 1.5395 1.8697 1.8419 0.1795 -0.3221 0.0622 834 LYS A O 6483 C CB . LYS A 834 ? 1.7876 2.2046 2.0881 0.1471 -0.4409 0.0572 834 LYS A CB 6484 C CG . LYS A 834 ? 1.7905 2.2569 2.1409 0.0878 -0.4722 0.0547 834 LYS A CG 6485 C CD . LYS A 834 ? 1.7881 2.3053 2.2104 0.0665 -0.4408 0.0694 834 LYS A CD 6486 C CE . LYS A 834 ? 1.7732 2.2131 2.1702 0.0200 -0.4341 0.0573 834 LYS A CE 6487 N NZ . LYS A 834 ? 1.6282 2.1170 2.0879 -0.0002 -0.4019 0.0756 834 LYS A NZ 6488 N N . ILE A 835 ? 1.6902 2.0670 1.9835 0.2362 -0.3544 0.0751 835 ILE A N 6489 C CA . ILE A 835 ? 1.6328 2.0253 1.9533 0.2780 -0.3170 0.0863 835 ILE A CA 6490 C C . ILE A 835 ? 1.6349 1.9993 1.9192 0.3291 -0.3191 0.0954 835 ILE A C 6491 O O . ILE A 835 ? 1.5177 1.9433 1.8441 0.3653 -0.3228 0.1102 835 ILE A O 6492 C CB . ILE A 835 ? 1.6468 2.1562 2.0596 0.2803 -0.3132 0.0999 835 ILE A CB 6493 C CG1 . ILE A 835 ? 1.5437 2.1401 1.9989 0.2606 -0.3594 0.1074 835 ILE A CG1 6494 C CG2 . ILE A 835 ? 1.5290 2.0508 1.9731 0.2460 -0.2857 0.0971 835 ILE A CG2 6495 C CD1 . ILE A 835 ? 1.3388 2.0663 1.8922 0.2630 -0.3562 0.1231 835 ILE A CD1 6496 N N . ASP A 868 ? 2.6370 1.8319 2.1202 0.0855 0.1606 0.7180 868 ASP A N 6497 C CA . ASP A 868 ? 2.6078 1.7465 2.0799 0.1317 0.1247 0.6966 868 ASP A CA 6498 C C . ASP A 868 ? 2.4525 1.6364 1.9565 0.1607 0.1162 0.6244 868 ASP A C 6499 O O . ASP A 868 ? 2.4328 1.6605 1.9063 0.1962 0.1073 0.6040 868 ASP A O 6500 C CB . ASP A 868 ? 2.6218 1.6425 2.1182 0.1235 0.1012 0.7142 868 ASP A CB 6501 C CG . ASP A 868 ? 2.5866 1.5825 2.1416 0.0767 0.1117 0.7027 868 ASP A CG 6502 O OD1 . ASP A 868 ? 2.6314 1.5337 2.1951 0.0514 0.1012 0.7360 868 ASP A OD1 6503 O OD2 . ASP A 868 ? 2.3564 1.4237 1.9481 0.0651 0.1281 0.6604 868 ASP A OD2 6504 N N . ILE A 869 ? 2.3272 1.4995 1.8908 0.1433 0.1175 0.5871 869 ILE A N 6505 C CA . ILE A 869 ? 2.1663 1.3790 1.7616 0.1662 0.1109 0.5229 869 ILE A CA 6506 C C . ILE A 869 ? 2.1289 1.4395 1.7257 0.1569 0.1375 0.5015 869 ILE A C 6507 O O . ILE A 869 ? 2.1451 1.4869 1.7608 0.1212 0.1622 0.5159 869 ILE A O 6508 C CB . ILE A 869 ? 2.0661 1.2265 1.7186 0.1548 0.0999 0.4904 869 ILE A CB 6509 C CG1 . ILE A 869 ? 1.7318 0.9428 1.4151 0.1737 0.0970 0.4290 869 ILE A CG1 6510 C CG2 . ILE A 869 ? 2.2354 1.3819 1.9180 0.1028 0.1170 0.5110 869 ILE A CG2 6511 C CD1 . ILE A 869 ? 1.6726 0.8914 1.3384 0.2197 0.0760 0.4068 869 ILE A CD1 6512 N N . HIS A 870 ? 2.0170 1.3764 1.5952 0.1899 0.1311 0.4674 870 HIS A N 6513 C CA . HIS A 870 ? 1.9434 1.3874 1.5146 0.1897 0.1532 0.4443 870 HIS A CA 6514 C C . HIS A 870 ? 1.8229 1.2906 1.4274 0.2074 0.1428 0.3847 870 HIS A C 6515 O O . HIS A 870 ? 1.6661 1.1163 1.2659 0.2349 0.1183 0.3625 870 HIS A O 6516 C CB . HIS A 870 ? 2.1210 1.6036 1.6227 0.2102 0.1571 0.4630 870 HIS A CB 6517 C CG . HIS A 870 ? 2.2887 1.8525 1.7733 0.2058 0.1874 0.4538 870 HIS A CG 6518 N ND1 . HIS A 870 ? 2.3484 1.9556 1.7658 0.2250 0.1948 0.4627 870 HIS A ND1 6519 C CD2 . HIS A 870 ? 2.2570 1.8686 1.7819 0.1876 0.2117 0.4352 870 HIS A CD2 6520 C CE1 . HIS A 870 ? 2.3350 2.0116 1.7513 0.2211 0.2243 0.4481 870 HIS A CE1 6521 N NE2 . HIS A 870 ? 2.3159 1.9984 1.7997 0.1990 0.2348 0.4325 870 HIS A NE2 6522 N N . THR A 871 ? 1.8782 1.3889 1.5181 0.1910 0.1613 0.3617 871 THR A N 6523 C CA . THR A 871 ? 1.6351 1.1676 1.3056 0.2048 0.1531 0.3098 871 THR A CA 6524 C C . THR A 871 ? 1.6096 1.1975 1.2450 0.2285 0.1577 0.2865 871 THR A C 6525 O O . THR A 871 ? 1.6590 1.2945 1.2692 0.2253 0.1810 0.2987 871 THR A O 6526 C CB . THR A 871 ? 1.5822 1.1331 1.3079 0.1786 0.1667 0.2951 871 THR A CB 6527 O OG1 . THR A 871 ? 1.7900 1.2827 1.5451 0.1544 0.1594 0.3127 871 THR A OG1 6528 C CG2 . THR A 871 ? 1.4951 1.0633 1.2483 0.1938 0.1563 0.2456 871 THR A CG2 6529 N N . LEU A 872 ? 1.5692 1.1510 1.2024 0.2519 0.1353 0.2526 872 LEU A N 6530 C CA . LEU A 872 ? 1.5670 1.1900 1.1709 0.2721 0.1348 0.2232 872 LEU A CA 6531 C C . LEU A 872 ? 1.5123 1.1468 1.1585 0.2734 0.1313 0.1812 872 LEU A C 6532 O O . LEU A 872 ? 1.4343 1.0442 1.1045 0.2785 0.1103 0.1617 872 LEU A O 6533 C CB . LEU A 872 ? 1.5694 1.1792 1.1311 0.2952 0.1087 0.2202 872 LEU A CB 6534 C CG . LEU A 872 ? 1.6428 1.2407 1.1549 0.2987 0.1073 0.2633 872 LEU A CG 6535 C CD1 . LEU A 872 ? 1.6373 1.2294 1.1136 0.3227 0.0762 0.2559 872 LEU A CD1 6536 C CD2 . LEU A 872 ? 1.7814 1.4207 1.2510 0.2937 0.1366 0.2830 872 LEU A CD2 6537 N N . GLY A 873 ? 1.6028 1.2785 1.2580 0.2699 0.1528 0.1698 873 GLY A N 6538 C CA . GLY A 873 ? 1.4730 1.1610 1.1645 0.2729 0.1500 0.1338 873 GLY A CA 6539 C C . GLY A 873 ? 1.5924 1.3033 1.2500 0.2970 0.1477 0.1041 873 GLY A C 6540 O O . GLY A 873 ? 1.5923 1.3101 1.1964 0.3112 0.1467 0.1081 873 GLY A O 6541 N N . CYS A 874 ? 1.7887 1.5076 1.4737 0.3024 0.1451 0.0738 874 CYS A N 6542 C CA . CYS A 874 ? 1.5365 1.2662 1.1910 0.3262 0.1408 0.0423 874 CYS A CA 6543 C C . CYS A 874 ? 1.5373 1.3151 1.1666 0.3387 0.1698 0.0454 874 CYS A C 6544 O O . CYS A 874 ? 1.7615 1.5480 1.3509 0.3634 0.1695 0.0204 874 CYS A O 6545 C CB . CYS A 874 ? 1.3341 1.0525 1.0256 0.3285 0.1289 0.0135 874 CYS A CB 6546 S SG . CYS A 874 ? 2.5100 2.1967 2.1676 0.3476 0.1001 -0.0232 874 CYS A SG 6547 N N . GLY A 875 ? 1.5465 1.3564 1.1998 0.3211 0.1947 0.0756 875 GLY A N 6548 C CA . GLY A 875 ? 1.6250 1.4939 1.2608 0.3298 0.2268 0.0853 875 GLY A CA 6549 C C . GLY A 875 ? 1.7106 1.5877 1.2786 0.3384 0.2349 0.1043 875 GLY A C 6550 O O . GLY A 875 ? 1.7722 1.6839 1.2952 0.3637 0.2496 0.0899 875 GLY A O 6551 N N . VAL A 876 ? 1.7557 1.6001 1.3132 0.3201 0.2247 0.1362 876 VAL A N 6552 C CA . VAL A 876 ? 1.8096 1.6599 1.3012 0.3262 0.2302 0.1617 876 VAL A CA 6553 C C . VAL A 876 ? 1.8523 1.6651 1.2930 0.3470 0.1975 0.1389 876 VAL A C 6554 O O . VAL A 876 ? 1.8281 1.6479 1.2039 0.3586 0.1967 0.1509 876 VAL A O 6555 C CB . VAL A 876 ? 1.7700 1.6016 1.2735 0.2965 0.2349 0.2140 876 VAL A CB 6556 C CG1 . VAL A 876 ? 1.7283 1.4937 1.2437 0.2919 0.2000 0.2152 876 VAL A CG1 6557 C CG2 . VAL A 876 ? 1.8925 1.7518 1.3316 0.2994 0.2538 0.2501 876 VAL A CG2 6558 N N . ALA A 877 ? 1.7889 1.5661 1.2589 0.3501 0.1699 0.1070 877 ALA A N 6559 C CA . ALA A 877 ? 1.7541 1.4994 1.1878 0.3638 0.1357 0.0857 877 ALA A CA 6560 C C . ALA A 877 ? 1.7388 1.4758 1.1729 0.3799 0.1219 0.0366 877 ALA A C 6561 O O . ALA A 877 ? 1.9210 1.6693 1.3935 0.3805 0.1352 0.0207 877 ALA A O 6562 C CB . ALA A 877 ? 1.6810 1.3871 1.1491 0.3492 0.1105 0.1008 877 ALA A CB 6563 N N . GLN A 878 ? 1.7494 1.4650 1.1405 0.3921 0.0928 0.0138 878 GLN A N 6564 C CA . GLN A 878 ? 1.7145 1.4087 1.1029 0.4036 0.0736 -0.0318 878 GLN A CA 6565 C C . GLN A 878 ? 1.6063 1.2765 1.0652 0.3868 0.0612 -0.0381 878 GLN A C 6566 O O . GLN A 878 ? 1.5672 1.2235 1.0570 0.3705 0.0456 -0.0209 878 GLN A O 6567 C CB . GLN A 878 ? 1.8584 1.5314 1.1911 0.4122 0.0393 -0.0518 878 GLN A CB 6568 C CG . GLN A 878 ? 2.0098 1.6506 1.3350 0.4204 0.0156 -0.0988 878 GLN A CG 6569 C CD . GLN A 878 ? 2.1828 1.8028 1.4541 0.4237 -0.0222 -0.1194 878 GLN A CD 6570 O OE1 . GLN A 878 ? 2.3738 2.0084 1.6129 0.4224 -0.0313 -0.0978 878 GLN A OE1 6571 N NE2 . GLN A 878 ? 2.1653 1.7488 1.4262 0.4271 -0.0468 -0.1604 878 GLN A NE2 6572 N N . CYS A 879 ? 1.7044 1.3720 1.1866 0.3936 0.0684 -0.0624 879 CYS A N 6573 C CA . CYS A 879 ? 1.5877 1.2384 1.1332 0.3783 0.0610 -0.0650 879 CYS A CA 6574 C C . CYS A 879 ? 1.4320 1.0434 0.9780 0.3765 0.0280 -0.0933 879 CYS A C 6575 O O . CYS A 879 ? 1.5757 1.1685 1.0818 0.3925 0.0165 -0.1231 879 CYS A O 6576 C CB . CYS A 879 ? 1.5936 1.2675 1.1711 0.3847 0.0868 -0.0687 879 CYS A CB 6577 S SG . CYS A 879 ? 2.1928 1.8513 1.8422 0.3669 0.0789 -0.0692 879 CYS A SG 6578 N N . LEU A 880 ? 1.3438 0.9423 0.9346 0.3563 0.0128 -0.0837 880 LEU A N 6579 C CA . LEU A 880 ? 1.3843 0.9516 0.9886 0.3475 -0.0153 -0.1037 880 LEU A CA 6580 C C . LEU A 880 ? 1.4061 0.9694 1.0624 0.3388 -0.0075 -0.1020 880 LEU A C 6581 O O . LEU A 880 ? 1.4078 0.9846 1.1045 0.3248 -0.0005 -0.0818 880 LEU A O 6582 C CB . LEU A 880 ? 1.3399 0.9057 0.9525 0.3315 -0.0404 -0.0932 880 LEU A CB 6583 C CG . LEU A 880 ? 1.3316 0.8728 0.9557 0.3169 -0.0724 -0.1104 880 LEU A CG 6584 C CD1 . LEU A 880 ? 1.4074 0.9560 1.0117 0.3107 -0.0998 -0.1086 880 LEU A CD1 6585 C CD2 . LEU A 880 ? 1.2475 0.7917 0.9313 0.2988 -0.0713 -0.0988 880 LEU A CD2 6586 N N . LYS A 881 ? 1.2367 0.7789 0.8883 0.3494 -0.0102 -0.1241 881 LYS A N 6587 C CA . LYS A 881 ? 1.2098 0.7506 0.9044 0.3453 -0.0030 -0.1214 881 LYS A CA 6588 C C . LYS A 881 ? 1.3063 0.8184 1.0250 0.3258 -0.0272 -0.1231 881 LYS A C 6589 O O . LYS A 881 ? 1.6542 1.1322 1.3514 0.3225 -0.0516 -0.1394 881 LYS A O 6590 C CB . LYS A 881 ? 1.1743 0.7103 0.8552 0.3710 0.0075 -0.1407 881 LYS A CB 6591 C CG . LYS A 881 ? 1.3188 0.8950 0.9793 0.3907 0.0357 -0.1379 881 LYS A CG 6592 C CD . LYS A 881 ? 1.2521 0.8305 0.9023 0.4215 0.0462 -0.1596 881 LYS A CD 6593 C CE . LYS A 881 ? 1.6937 1.3187 1.3157 0.4428 0.0748 -0.1588 881 LYS A CE 6594 N NZ . LYS A 881 ? 1.9032 1.5171 1.4656 0.4469 0.0672 -0.1665 881 LYS A NZ 6595 N N . ILE A 882 ? 1.0838 0.6107 0.8459 0.3111 -0.0206 -0.1059 882 ILE A N 6596 C CA . ILE A 882 ? 1.0616 0.5703 0.8485 0.2926 -0.0379 -0.1033 882 ILE A CA 6597 C C . ILE A 882 ? 1.1154 0.6219 0.9254 0.2963 -0.0295 -0.1012 882 ILE A C 6598 O O . ILE A 882 ? 1.3631 0.8988 1.1981 0.2947 -0.0123 -0.0888 882 ILE A O 6599 C CB . ILE A 882 ? 1.1169 0.6498 0.9316 0.2731 -0.0396 -0.0848 882 ILE A CB 6600 C CG1 . ILE A 882 ? 1.2118 0.7501 1.0063 0.2711 -0.0525 -0.0852 882 ILE A CG1 6601 C CG2 . ILE A 882 ? 1.0702 0.5954 0.9117 0.2536 -0.0523 -0.0792 882 ILE A CG2 6602 C CD1 . ILE A 882 ? 1.2964 0.8614 1.1209 0.2572 -0.0567 -0.0686 882 ILE A CD1 6603 N N . VAL A 883 ? 1.2299 0.6983 1.0299 0.3013 -0.0444 -0.1135 883 VAL A N 6604 C CA . VAL A 883 ? 1.2175 0.6804 1.0353 0.3092 -0.0405 -0.1109 883 VAL A CA 6605 C C . VAL A 883 ? 1.3283 0.7760 1.1670 0.2857 -0.0548 -0.0968 883 VAL A C 6606 O O . VAL A 883 ? 1.7300 1.1440 1.5595 0.2705 -0.0757 -0.0986 883 VAL A O 6607 C CB . VAL A 883 ? 1.0880 0.5148 0.8797 0.3368 -0.0468 -0.1322 883 VAL A CB 6608 C CG1 . VAL A 883 ? 1.2221 0.6378 1.0336 0.3452 -0.0493 -0.1266 883 VAL A CG1 6609 C CG2 . VAL A 883 ? 1.3384 0.7951 1.1122 0.3631 -0.0261 -0.1438 883 VAL A CG2 6610 N N . CYS A 884 ? 1.0472 0.5221 0.9128 0.2809 -0.0439 -0.0822 884 CYS A N 6611 C CA . CYS A 884 ? 1.1745 0.6446 1.0566 0.2594 -0.0533 -0.0659 884 CYS A CA 6612 C C . CYS A 884 ? 1.1909 0.6501 1.0793 0.2685 -0.0559 -0.0598 884 CYS A C 6613 O O . CYS A 884 ? 1.0803 0.5638 0.9775 0.2860 -0.0437 -0.0624 884 CYS A O 6614 C CB . CYS A 884 ? 0.9256 0.4399 0.8292 0.2439 -0.0405 -0.0531 884 CYS A CB 6615 S SG . CYS A 884 ? 1.5031 1.0337 1.4039 0.2359 -0.0402 -0.0554 884 CYS A SG 6616 N N . GLN A 885 ? 1.3356 0.7602 1.2209 0.2551 -0.0732 -0.0491 885 GLN A N 6617 C CA . GLN A 885 ? 1.3818 0.7933 1.2705 0.2625 -0.0789 -0.0377 885 GLN A CA 6618 C C . GLN A 885 ? 1.3312 0.7765 1.2353 0.2406 -0.0737 -0.0155 885 GLN A C 6619 O O . GLN A 885 ? 1.5477 0.9893 1.4534 0.2147 -0.0797 -0.0015 885 GLN A O 6620 C CB . GLN A 885 ? 1.3744 0.7163 1.2443 0.2637 -0.1030 -0.0373 885 GLN A CB 6621 C CG . GLN A 885 ? 1.6072 0.9085 1.4545 0.2904 -0.1099 -0.0644 885 GLN A CG 6622 C CD . GLN A 885 ? 1.8771 1.1612 1.7093 0.2747 -0.1177 -0.0777 885 GLN A CD 6623 O OE1 . GLN A 885 ? 1.9984 1.3051 1.8428 0.2441 -0.1182 -0.0650 885 GLN A OE1 6624 N NE2 . GLN A 885 ? 1.8050 1.0530 1.6097 0.2979 -0.1246 -0.1043 885 GLN A NE2 6625 N N . VAL A 886 ? 1.1483 0.6306 1.0634 0.2508 -0.0626 -0.0130 886 VAL A N 6626 C CA . VAL A 886 ? 1.0911 0.6074 1.0139 0.2344 -0.0570 0.0033 886 VAL A CA 6627 C C . VAL A 886 ? 1.2618 0.7643 1.1779 0.2395 -0.0691 0.0195 886 VAL A C 6628 O O . VAL A 886 ? 1.4193 0.9051 1.3345 0.2630 -0.0766 0.0143 886 VAL A O 6629 C CB . VAL A 886 ? 0.9143 0.4795 0.8505 0.2385 -0.0395 -0.0064 886 VAL A CB 6630 C CG1 . VAL A 886 ? 0.9312 0.5277 0.8685 0.2224 -0.0336 0.0043 886 VAL A CG1 6631 C CG2 . VAL A 886 ? 1.1071 0.6789 1.0472 0.2394 -0.0291 -0.0204 886 VAL A CG2 6632 N N . GLY A 887 ? 1.0490 0.5622 0.9598 0.2195 -0.0707 0.0405 887 GLY A N 6633 C CA . GLY A 887 ? 1.0750 0.5798 0.9750 0.2233 -0.0823 0.0603 887 GLY A CA 6634 C C . GLY A 887 ? 1.2864 0.8305 1.1787 0.2055 -0.0756 0.0782 887 GLY A C 6635 O O . GLY A 887 ? 1.9015 1.4694 1.7959 0.1856 -0.0639 0.0815 887 GLY A O 6636 N N . ARG A 888 ? 1.1883 0.7421 1.0704 0.2154 -0.0838 0.0895 888 ARG A N 6637 C CA . ARG A 888 ? 1.1907 0.7821 1.0560 0.2031 -0.0797 0.1059 888 ARG A CA 6638 C C . ARG A 888 ? 1.1815 0.8228 1.0507 0.1934 -0.0589 0.0898 888 ARG A C 6639 O O . ARG A 888 ? 1.2224 0.8806 1.0860 0.1748 -0.0482 0.1005 888 ARG A O 6640 C CB . ARG A 888 ? 1.4286 0.9957 1.2749 0.1822 -0.0871 0.1411 888 ARG A CB 6641 C CG . ARG A 888 ? 1.3849 0.9826 1.2043 0.1773 -0.0887 0.1643 888 ARG A CG 6642 C CD . ARG A 888 ? 1.3487 0.9583 1.1648 0.2032 -0.1011 0.1548 888 ARG A CD 6643 N NE . ARG A 888 ? 1.3862 1.0319 1.1722 0.2000 -0.1040 0.1717 888 ARG A NE 6644 C CZ . ARG A 888 ? 1.4070 1.0387 1.1728 0.2100 -0.1245 0.1970 888 ARG A CZ 6645 N NH1 . ARG A 888 ? 1.3890 0.9679 1.1644 0.2264 -0.1437 0.2071 888 ARG A NH1 6646 N NH2 . ARG A 888 ? 1.4559 1.1254 1.1891 0.2065 -0.1270 0.2114 888 ARG A NH2 6647 N N . LEU A 889 ? 1.1393 0.8043 1.0201 0.2062 -0.0536 0.0643 889 LEU A N 6648 C CA . LEU A 889 ? 1.1396 0.8435 1.0187 0.2009 -0.0380 0.0476 889 LEU A CA 6649 C C . LEU A 889 ? 1.2128 0.9460 1.0727 0.2045 -0.0441 0.0461 889 LEU A C 6650 O O . LEU A 889 ? 1.2150 0.9530 1.0835 0.2157 -0.0554 0.0371 889 LEU A O 6651 C CB . LEU A 889 ? 1.0682 0.7724 0.9706 0.2078 -0.0291 0.0211 889 LEU A CB 6652 C CG . LEU A 889 ? 1.0293 0.7179 0.9451 0.2032 -0.0199 0.0175 889 LEU A CG 6653 C CD1 . LEU A 889 ? 0.9739 0.6670 0.9058 0.2099 -0.0107 -0.0051 889 LEU A CD1 6654 C CD2 . LEU A 889 ? 1.0749 0.7815 0.9835 0.1892 -0.0101 0.0280 889 LEU A CD2 6655 N N . ASP A 890 ? 1.2880 1.0464 1.1219 0.1951 -0.0369 0.0549 890 ASP A N 6656 C CA . ASP A 890 ? 1.3265 1.1139 1.1326 0.1980 -0.0438 0.0523 890 ASP A CA 6657 C C . ASP A 890 ? 1.3212 1.1295 1.1284 0.2011 -0.0362 0.0173 890 ASP A C 6658 O O . ASP A 890 ? 1.2584 1.0551 1.0911 0.2025 -0.0270 -0.0016 890 ASP A O 6659 C CB . ASP A 890 ? 1.4172 1.2245 1.1875 0.1876 -0.0383 0.0780 890 ASP A CB 6660 C CG . ASP A 890 ? 1.4734 1.2513 1.2409 0.1799 -0.0484 0.1165 890 ASP A CG 6661 O OD1 . ASP A 890 ? 1.4951 1.2579 1.2519 0.1878 -0.0688 0.1326 890 ASP A OD1 6662 O OD2 . ASP A 890 ? 1.6374 1.4058 1.4147 0.1658 -0.0378 0.1311 890 ASP A OD2 6663 N N . ARG A 891 ? 1.3990 1.2337 1.1750 0.2020 -0.0419 0.0091 891 ARG A N 6664 C CA . ARG A 891 ? 1.4182 1.2636 1.1907 0.2039 -0.0408 -0.0266 891 ARG A CA 6665 C C . ARG A 891 ? 1.4599 1.3037 1.2331 0.2050 -0.0182 -0.0457 891 ARG A C 6666 O O . ARG A 891 ? 1.6403 1.4694 1.4305 0.2068 -0.0160 -0.0720 891 ARG A O 6667 C CB . ARG A 891 ? 1.5245 1.3976 1.2544 0.2046 -0.0538 -0.0326 891 ARG A CB 6668 C CG . ARG A 891 ? 1.5704 1.4471 1.2910 0.2045 -0.0570 -0.0731 891 ARG A CG 6669 C CD . ARG A 891 ? 1.7007 1.6040 1.3771 0.2045 -0.0759 -0.0815 891 ARG A CD 6670 N NE . ARG A 891 ? 1.8484 1.7759 1.4729 0.2086 -0.0638 -0.0700 891 ARG A NE 6671 C CZ . ARG A 891 ? 1.8530 1.7990 1.4518 0.2081 -0.0704 -0.0343 891 ARG A CZ 6672 N NH1 . ARG A 891 ? 1.8660 1.8040 1.4867 0.2075 -0.0908 -0.0091 891 ARG A NH1 6673 N NH2 . ARG A 891 ? 1.9145 1.8877 1.4651 0.2096 -0.0559 -0.0224 891 ARG A NH2 6674 N N . GLY A 892 ? 1.4703 1.3309 1.2274 0.2040 -0.0019 -0.0302 892 GLY A N 6675 C CA . GLY A 892 ? 1.5639 1.4334 1.3228 0.2100 0.0196 -0.0474 892 GLY A CA 6676 C C . GLY A 892 ? 1.5456 1.4056 1.3400 0.2070 0.0313 -0.0335 892 GLY A C 6677 O O . GLY A 892 ? 1.7934 1.6714 1.5922 0.2128 0.0492 -0.0399 892 GLY A O 6678 N N . LYS A 893 ? 1.3236 1.1572 1.1429 0.2002 0.0201 -0.0164 893 LYS A N 6679 C CA . LYS A 893 ? 1.2499 1.0721 1.0980 0.1952 0.0265 -0.0034 893 LYS A CA 6680 C C . LYS A 893 ? 1.1736 0.9641 1.0502 0.2005 0.0225 -0.0187 893 LYS A C 6681 O O . LYS A 893 ? 1.1401 0.9190 1.0184 0.2057 0.0163 -0.0372 893 LYS A O 6682 C CB . LYS A 893 ? 1.2901 1.1024 1.1378 0.1824 0.0172 0.0303 893 LYS A CB 6683 C CG . LYS A 893 ? 1.4669 1.3122 1.2872 0.1726 0.0234 0.0542 893 LYS A CG 6684 C CD . LYS A 893 ? 1.5990 1.4882 1.4204 0.1733 0.0465 0.0484 893 LYS A CD 6685 C CE . LYS A 893 ? 1.6303 1.5626 1.4237 0.1627 0.0568 0.0748 893 LYS A CE 6686 N NZ . LYS A 893 ? 1.5788 1.4990 1.3819 0.1391 0.0496 0.1155 893 LYS A NZ 6687 N N . SER A 894 ? 1.1732 0.9521 1.0714 0.1969 0.0251 -0.0090 894 SER A N 6688 C CA . SER A 894 ? 1.0400 0.7947 0.9600 0.2027 0.0246 -0.0216 894 SER A CA 6689 C C . SER A 894 ? 1.0432 0.7880 0.9794 0.1967 0.0233 -0.0083 894 SER A C 6690 O O . SER A 894 ? 1.3873 1.1481 1.3237 0.1858 0.0247 0.0090 894 SER A O 6691 C CB . SER A 894 ? 1.0429 0.8031 0.9652 0.2128 0.0355 -0.0437 894 SER A CB 6692 O OG . SER A 894 ? 1.3942 1.1314 1.3347 0.2172 0.0355 -0.0500 894 SER A OG 6693 N N . ALA A 895 ? 0.9509 0.6715 0.8997 0.2019 0.0200 -0.0160 895 ALA A N 6694 C CA . ALA A 895 ? 0.9414 0.6495 0.9012 0.1972 0.0153 -0.0083 895 ALA A CA 6695 C C . ALA A 895 ? 1.0488 0.7539 1.0192 0.2064 0.0208 -0.0203 895 ALA A C 6696 O O . ALA A 895 ? 1.1889 0.8822 1.1585 0.2151 0.0239 -0.0320 895 ALA A O 6697 C CB . ALA A 895 ? 0.9275 0.6023 0.8829 0.1965 0.0017 -0.0031 895 ALA A CB 6698 N N . ILE A 896 ? 0.9173 0.6350 0.8987 0.2030 0.0207 -0.0149 896 ILE A N 6699 C CA . ILE A 896 ? 0.9160 0.6340 0.9060 0.2139 0.0242 -0.0227 896 ILE A CA 6700 C C . ILE A 896 ? 0.9419 0.6501 0.9362 0.2093 0.0127 -0.0176 896 ILE A C 6701 O O . ILE A 896 ? 0.9579 0.6765 0.9593 0.1950 0.0042 -0.0072 896 ILE A O 6702 C CB . ILE A 896 ? 0.8980 0.6511 0.8992 0.2219 0.0352 -0.0250 896 ILE A CB 6703 C CG1 . ILE A 896 ? 0.9255 0.6886 0.9153 0.2266 0.0453 -0.0335 896 ILE A CG1 6704 C CG2 . ILE A 896 ? 0.9811 0.7260 0.9887 0.2379 0.0370 -0.0322 896 ILE A CG2 6705 C CD1 . ILE A 896 ? 1.2661 1.0635 1.2530 0.2157 0.0492 -0.0218 896 ILE A CD1 6706 N N . LEU A 897 ? 1.1737 0.8619 1.1619 0.2195 0.0114 -0.0243 897 LEU A N 6707 C CA . LEU A 897 ? 1.1975 0.8773 1.1828 0.2183 -0.0005 -0.0227 897 LEU A CA 6708 C C . LEU A 897 ? 1.1786 0.8735 1.1716 0.2300 0.0016 -0.0222 897 LEU A C 6709 O O . LEU A 897 ? 1.3613 1.0426 1.3472 0.2425 0.0094 -0.0255 897 LEU A O 6710 C CB . LEU A 897 ? 1.0009 0.6475 0.9656 0.2232 -0.0044 -0.0293 897 LEU A CB 6711 C CG . LEU A 897 ? 0.8838 0.5183 0.8345 0.2261 -0.0160 -0.0321 897 LEU A CG 6712 C CD1 . LEU A 897 ? 0.9397 0.5749 0.8948 0.2102 -0.0343 -0.0294 897 LEU A CD1 6713 C CD2 . LEU A 897 ? 0.8737 0.4823 0.8009 0.2362 -0.0141 -0.0407 897 LEU A CD2 6714 N N . TYR A 898 ? 0.9337 0.6575 0.9433 0.2251 -0.0068 -0.0158 898 TYR A N 6715 C CA . TYR A 898 ? 0.9149 0.6573 0.9345 0.2395 -0.0085 -0.0133 898 TYR A CA 6716 C C . TYR A 898 ? 0.9416 0.6717 0.9471 0.2383 -0.0257 -0.0125 898 TYR A C 6717 O O . TYR A 898 ? 1.0376 0.7721 1.0446 0.2219 -0.0414 -0.0117 898 TYR A O 6718 C CB . TYR A 898 ? 0.9434 0.7387 0.9949 0.2384 -0.0074 -0.0066 898 TYR A CB 6719 C CG . TYR A 898 ? 0.9456 0.7600 1.0054 0.2401 0.0100 -0.0086 898 TYR A CG 6720 C CD1 . TYR A 898 ? 1.0102 0.8380 1.0732 0.2193 0.0111 -0.0023 898 TYR A CD1 6721 C CD2 . TYR A 898 ? 0.9483 0.7634 1.0086 0.2628 0.0238 -0.0168 898 TYR A CD2 6722 C CE1 . TYR A 898 ? 1.1376 0.9864 1.2014 0.2216 0.0270 -0.0034 898 TYR A CE1 6723 C CE2 . TYR A 898 ? 1.0172 0.8494 1.0782 0.2660 0.0386 -0.0227 898 TYR A CE2 6724 C CZ . TYR A 898 ? 1.2739 1.1268 1.3355 0.2457 0.0408 -0.0156 898 TYR A CZ 6725 O OH . TYR A 898 ? 1.4262 1.2992 1.4818 0.2497 0.0555 -0.0206 898 TYR A OH 6726 N N . VAL A 899 ? 0.9671 0.6794 0.9558 0.2544 -0.0239 -0.0122 899 VAL A N 6727 C CA . VAL A 899 ? 0.9673 0.6704 0.9345 0.2562 -0.0397 -0.0114 899 VAL A CA 6728 C C . VAL A 899 ? 1.1138 0.8411 1.0909 0.2712 -0.0478 -0.0019 899 VAL A C 6729 O O . VAL A 899 ? 1.2501 0.9661 1.2233 0.2890 -0.0382 0.0042 899 VAL A O 6730 C CB . VAL A 899 ? 0.9520 0.6182 0.8843 0.2627 -0.0318 -0.0149 899 VAL A CB 6731 C CG1 . VAL A 899 ? 1.0583 0.7173 0.9601 0.2653 -0.0477 -0.0166 899 VAL A CG1 6732 C CG2 . VAL A 899 ? 0.9237 0.5715 0.8514 0.2536 -0.0234 -0.0238 899 VAL A CG2 6733 N N . LYS A 900 ? 1.0355 0.7950 1.0270 0.2635 -0.0678 0.0004 900 LYS A N 6734 C CA . LYS A 900 ? 1.0763 0.8685 1.0821 0.2792 -0.0797 0.0105 900 LYS A CA 6735 C C . LYS A 900 ? 1.1285 0.9059 1.0981 0.2829 -0.0989 0.0119 900 LYS A C 6736 O O . LYS A 900 ? 1.2720 1.0504 1.2295 0.2657 -0.1183 0.0039 900 LYS A O 6737 C CB . LYS A 900 ? 1.0842 0.9364 1.1355 0.2682 -0.0908 0.0143 900 LYS A CB 6738 C CG . LYS A 900 ? 1.1006 0.9997 1.1768 0.2881 -0.1036 0.0252 900 LYS A CG 6739 C CD . LYS A 900 ? 1.1233 1.0950 1.2547 0.2784 -0.1069 0.0303 900 LYS A CD 6740 C CE . LYS A 900 ? 1.1325 1.1613 1.2957 0.3021 -0.1207 0.0412 900 LYS A CE 6741 N NZ . LYS A 900 ? 1.1890 1.2255 1.3381 0.2934 -0.1538 0.0442 900 LYS A NZ 6742 N N . SER A 901 ? 1.2268 0.9870 1.1756 0.3049 -0.0943 0.0221 901 SER A N 6743 C CA . SER A 901 ? 1.2238 0.9712 1.1301 0.3108 -0.1097 0.0264 901 SER A CA 6744 C C . SER A 901 ? 1.2366 1.0007 1.1457 0.3351 -0.1202 0.0453 901 SER A C 6745 O O . SER A 901 ? 1.2231 0.9929 1.1608 0.3520 -0.1098 0.0544 901 SER A O 6746 C CB . SER A 901 ? 1.2067 0.9079 1.0691 0.3116 -0.0919 0.0244 901 SER A CB 6747 O OG . SER A 901 ? 1.1103 0.7908 0.9739 0.3256 -0.0725 0.0386 901 SER A OG 6748 N N . LEU A 902 ? 1.2219 0.9918 1.0979 0.3390 -0.1423 0.0503 902 LEU A N 6749 C CA . LEU A 902 ? 1.2389 1.0217 1.1096 0.3640 -0.1558 0.0716 902 LEU A CA 6750 C C . LEU A 902 ? 1.2802 1.0182 1.0944 0.3748 -0.1459 0.0866 902 LEU A C 6751 O O . LEU A 902 ? 1.4698 1.1870 1.2402 0.3630 -0.1412 0.0775 902 LEU A O 6752 C CB . LEU A 902 ? 1.2897 1.1196 1.1635 0.3612 -0.1921 0.0707 902 LEU A CB 6753 C CG . LEU A 902 ? 1.3405 1.2247 1.2712 0.3431 -0.2061 0.0592 902 LEU A CG 6754 C CD1 . LEU A 902 ? 1.3895 1.3165 1.3168 0.3358 -0.2459 0.0583 902 LEU A CD1 6755 C CD2 . LEU A 902 ? 1.3213 1.2402 1.3115 0.3609 -0.1934 0.0691 902 LEU A CD2 6756 N N . LEU A 903 ? 1.4132 1.1364 1.2283 0.3981 -0.1421 0.1104 903 LEU A N 6757 C CA . LEU A 903 ? 1.4670 1.1518 1.2286 0.4066 -0.1354 0.1325 903 LEU A CA 6758 C C . LEU A 903 ? 1.5065 1.2148 1.2267 0.4139 -0.1641 0.1414 903 LEU A C 6759 O O . LEU A 903 ? 1.5875 1.3294 1.3274 0.4300 -0.1900 0.1506 903 LEU A O 6760 C CB . LEU A 903 ? 1.4374 1.0891 1.2116 0.4279 -0.1260 0.1574 903 LEU A CB 6761 C CG . LEU A 903 ? 1.3421 0.9512 1.0629 0.4336 -0.1193 0.1882 903 LEU A CG 6762 C CD1 . LEU A 903 ? 1.3408 0.9187 1.0414 0.4103 -0.0892 0.1837 903 LEU A CD1 6763 C CD2 . LEU A 903 ? 1.4257 1.0006 1.1585 0.4592 -0.1225 0.2160 903 LEU A CD2 6764 N N . TRP A 904 ? 1.4959 1.1909 1.1579 0.4040 -0.1605 0.1378 904 TRP A N 6765 C CA . TRP A 904 ? 1.5554 1.2713 1.1678 0.4111 -0.1887 0.1432 904 TRP A CA 6766 C C . TRP A 904 ? 1.6513 1.3491 1.2316 0.4336 -0.1900 0.1835 904 TRP A C 6767 O O . TRP A 904 ? 1.9515 1.6131 1.4982 0.4322 -0.1647 0.2021 904 TRP A O 6768 C CB . TRP A 904 ? 1.5619 1.2696 1.1175 0.3968 -0.1831 0.1215 904 TRP A CB 6769 C CG . TRP A 904 ? 1.6087 1.3430 1.1209 0.3978 -0.2186 0.1092 904 TRP A CG 6770 C CD1 . TRP A 904 ? 1.6714 1.4098 1.1170 0.4119 -0.2327 0.1270 904 TRP A CD1 6771 C CD2 . TRP A 904 ? 1.6204 1.3785 1.1494 0.3817 -0.2466 0.0764 904 TRP A CD2 6772 N NE1 . TRP A 904 ? 1.7483 1.5129 1.1668 0.4070 -0.2693 0.1037 904 TRP A NE1 6773 C CE2 . TRP A 904 ? 1.6883 1.4631 1.1591 0.3868 -0.2791 0.0723 904 TRP A CE2 6774 C CE3 . TRP A 904 ? 1.5862 1.3518 1.1720 0.3613 -0.2484 0.0518 904 TRP A CE3 6775 C CZ2 . TRP A 904 ? 1.7204 1.5156 1.1908 0.3703 -0.3153 0.0418 904 TRP A CZ2 6776 C CZ3 . TRP A 904 ? 1.6258 1.4113 1.2128 0.3438 -0.2824 0.0258 904 TRP A CZ3 6777 C CH2 . TRP A 904 ? 1.6909 1.4892 1.2218 0.3475 -0.3164 0.0196 904 TRP A CH2 6778 N N . THR A 905 ? 1.5371 1.2623 1.1294 0.4535 -0.2207 0.1994 905 THR A N 6779 C CA . THR A 905 ? 1.5592 1.2627 1.1280 0.4789 -0.2258 0.2414 905 THR A CA 6780 C C . THR A 905 ? 1.6416 1.3442 1.1264 0.4824 -0.2370 0.2599 905 THR A C 6781 O O . THR A 905 ? 1.8457 1.5123 1.2901 0.4915 -0.2246 0.2964 905 THR A O 6782 C CB . THR A 905 ? 1.5978 1.3348 1.2162 0.5055 -0.2552 0.2528 905 THR A CB 6783 O OG1 . THR A 905 ? 1.4807 1.2323 1.1743 0.5020 -0.2446 0.2305 905 THR A OG1 6784 C CG2 . THR A 905 ? 1.7596 1.4572 1.3618 0.5351 -0.2566 0.2969 905 THR A CG2 6785 N N . GLU A 906 ? 1.6625 1.4033 1.1192 0.4737 -0.2610 0.2349 906 GLU A N 6786 C CA . GLU A 906 ? 1.7574 1.5052 1.1279 0.4788 -0.2759 0.2457 906 GLU A CA 6787 C C . GLU A 906 ? 1.8443 1.5553 1.1547 0.4715 -0.2380 0.2591 906 GLU A C 6788 O O . GLU A 906 ? 2.0378 1.7434 1.2798 0.4826 -0.2398 0.2905 906 GLU A O 6789 C CB . GLU A 906 ? 1.9923 1.7773 1.3440 0.4651 -0.3047 0.2045 906 GLU A CB 6790 C CG . GLU A 906 ? 2.2068 2.0416 1.6131 0.4681 -0.3473 0.1951 906 GLU A CG 6791 C CD . GLU A 906 ? 2.2725 2.1354 1.6630 0.4469 -0.3767 0.1527 906 GLU A CD 6792 O OE1 . GLU A 906 ? 2.3147 2.2152 1.6805 0.4525 -0.4198 0.1533 906 GLU A OE1 6793 O OE2 . GLU A 906 ? 2.1580 2.0024 1.5601 0.4244 -0.3591 0.1188 906 GLU A OE2 6794 N N . THR A 907 ? 1.8652 1.5568 1.2021 0.4528 -0.2039 0.2373 907 THR A N 6795 C CA . THR A 907 ? 1.9263 1.5934 1.2217 0.4439 -0.1645 0.2491 907 THR A CA 6796 C C . THR A 907 ? 1.8523 1.4861 1.1396 0.4515 -0.1493 0.3023 907 THR A C 6797 O O . THR A 907 ? 2.0658 1.6939 1.2888 0.4525 -0.1353 0.3319 907 THR A O 6798 C CB . THR A 907 ? 1.8148 1.4702 1.1568 0.4243 -0.1339 0.2189 907 THR A CB 6799 O OG1 . THR A 907 ? 1.7626 1.4391 1.1065 0.4165 -0.1482 0.1721 907 THR A OG1 6800 C CG2 . THR A 907 ? 1.8690 1.5104 1.1768 0.4152 -0.0934 0.2336 907 THR A CG2 6801 N N . PHE A 908 ? 1.7418 1.3522 1.0931 0.4569 -0.1519 0.3141 908 PHE A N 6802 C CA . PHE A 908 ? 1.8790 1.4442 1.2298 0.4651 -0.1429 0.3624 908 PHE A CA 6803 C C . PHE A 908 ? 2.0278 1.5977 1.3326 0.4904 -0.1746 0.3999 908 PHE A C 6804 O O . PHE A 908 ? 2.2659 1.8793 1.5552 0.5023 -0.2072 0.3840 908 PHE A O 6805 C CB . PHE A 908 ? 1.8597 1.3954 1.2893 0.4679 -0.1392 0.3560 908 PHE A CB 6806 C CG . PHE A 908 ? 1.7707 1.3029 1.2427 0.4436 -0.1107 0.3216 908 PHE A CG 6807 C CD1 . PHE A 908 ? 1.8738 1.3697 1.3454 0.4238 -0.0778 0.3359 908 PHE A CD1 6808 C CD2 . PHE A 908 ? 1.7880 1.3553 1.3002 0.4387 -0.1185 0.2773 908 PHE A CD2 6809 C CE1 . PHE A 908 ? 1.8052 1.3028 1.3158 0.4030 -0.0547 0.3049 908 PHE A CE1 6810 C CE2 . PHE A 908 ? 1.5936 1.1570 1.1409 0.4183 -0.0944 0.2486 908 PHE A CE2 6811 C CZ . PHE A 908 ? 1.5639 1.0940 1.1103 0.4021 -0.0633 0.2616 908 PHE A CZ 6812 N N . MET A 909 ? 1.8725 1.3960 1.1551 0.4967 -0.1667 0.4507 909 MET A N 6813 C CA . MET A 909 ? 2.2245 1.7443 1.4448 0.5178 -0.1900 0.4977 909 MET A CA 6814 C C . MET A 909 ? 2.3116 1.8674 1.4447 0.5090 -0.1841 0.5001 909 MET A C 6815 O O . MET A 909 ? 2.1016 1.6559 1.2118 0.4859 -0.1474 0.4967 909 MET A O 6816 C CB . MET A 909 ? 2.3563 1.9037 1.6015 0.5499 -0.2364 0.4946 909 MET A CB 6817 C CG . MET A 909 ? 2.4506 1.9706 1.7786 0.5671 -0.2431 0.4915 909 MET A CG 6818 S SD . MET A 909 ? 2.1826 1.7535 1.5943 0.5584 -0.2454 0.4254 909 MET A SD 6819 C CE . MET A 909 ? 1.7825 1.3256 1.2726 0.5908 -0.2557 0.4341 909 MET A CE 6820 N N . ASN A 910 ? 2.6018 2.1936 1.6863 0.5292 -0.2205 0.5054 910 ASN A N 6821 C CA . ASN A 910 ? 2.6643 2.2908 1.6547 0.5265 -0.2199 0.5063 910 ASN A CA 6822 C C . ASN A 910 ? 2.6789 2.2801 1.6058 0.5151 -0.1836 0.5558 910 ASN A C 6823 O O . ASN A 910 ? 2.6893 2.2435 1.6193 0.5185 -0.1790 0.6099 910 ASN A O 6824 C CB . ASN A 910 ? 2.4302 2.0938 1.4223 0.5101 -0.2102 0.4427 910 ASN A CB 6825 C CG . ASN A 910 ? 2.3814 2.0710 1.4373 0.5137 -0.2439 0.3958 910 ASN A CG 6826 O OD1 . ASN A 910 ? 2.5711 2.2757 1.6455 0.5328 -0.2834 0.4068 910 ASN A OD1 6827 N ND2 . ASN A 910 ? 2.0691 1.7673 1.1608 0.4951 -0.2286 0.3455 910 ASN A ND2 6828 N N . LYS A 911 ? 2.5658 2.1989 1.4358 0.5018 -0.1576 0.5370 911 LYS A N 6829 C CA . LYS A 911 ? 2.6238 2.2497 1.4392 0.4867 -0.1158 0.5792 911 LYS A CA 6830 C C . LYS A 911 ? 2.5657 2.1785 1.4424 0.4589 -0.0709 0.5616 911 LYS A C 6831 O O . LYS A 911 ? 2.7340 2.3521 1.5834 0.4405 -0.0305 0.5879 911 LYS A O 6832 C CB . LYS A 911 ? 2.7099 2.3873 1.4218 0.4933 -0.1115 0.5708 911 LYS A CB 6833 C CG . LYS A 911 ? 2.6808 2.3584 1.3174 0.4860 -0.0800 0.6345 911 LYS A CG 6834 C CD . LYS A 911 ? 2.7803 2.5164 1.3191 0.4923 -0.0751 0.6177 911 LYS A CD 6835 C CE . LYS A 911 ? 2.9030 2.6506 1.3939 0.4720 -0.0428 0.6744 911 LYS A CE 6836 N NZ . LYS A 911 ? 2.9017 2.6381 1.4293 0.4462 0.0111 0.6995 911 LYS A NZ 6837 N N . GLU A 912 ? 2.3808 1.9821 1.3421 0.4557 -0.0794 0.5184 912 GLU A N 6838 C CA . GLU A 912 ? 2.3651 1.9555 1.3930 0.4320 -0.0451 0.4942 912 GLU A CA 6839 C C . GLU A 912 ? 2.4267 1.9671 1.4850 0.4127 -0.0203 0.5441 912 GLU A C 6840 O O . GLU A 912 ? 2.3416 1.8693 1.4589 0.3913 0.0046 0.5284 912 GLU A O 6841 C CB . GLU A 912 ? 2.1659 1.7537 1.2717 0.4356 -0.0657 0.4425 912 GLU A CB 6842 C CG . GLU A 912 ? 1.9976 1.6008 1.1455 0.4174 -0.0385 0.3959 912 GLU A CG 6843 C CD . GLU A 912 ? 2.0921 1.6574 1.3183 0.4001 -0.0205 0.3999 912 GLU A CD 6844 O OE1 . GLU A 912 ? 2.4120 1.9349 1.6642 0.4051 -0.0331 0.4306 912 GLU A OE1 6845 O OE2 . GLU A 912 ? 1.9628 1.5395 1.2226 0.3837 0.0043 0.3710 912 GLU A OE2 6846 N N . ASN A 913 ? 2.7253 2.2348 1.7421 0.4203 -0.0313 0.6035 913 ASN A N 6847 C CA . ASN A 913 ? 2.9369 2.3815 1.9744 0.4053 -0.0200 0.6592 913 ASN A CA 6848 C C . ASN A 913 ? 2.9719 2.3601 2.0669 0.4247 -0.0532 0.6592 913 ASN A C 6849 O O . ASN A 913 ? 3.0794 2.4000 2.1913 0.4189 -0.0526 0.7016 913 ASN A O 6850 C CB . ASN A 913 ? 2.7638 2.2018 1.8438 0.3677 0.0233 0.6576 913 ASN A CB 6851 C CG . ASN A 913 ? 2.9121 2.2882 1.9928 0.3442 0.0375 0.7231 913 ASN A CG 6852 O OD1 . ASN A 913 ? 2.9708 2.3662 2.0110 0.3204 0.0683 0.7629 913 ASN A OD1 6853 N ND2 . ASN A 913 ? 2.9517 2.2530 2.0792 0.3503 0.0156 0.7343 913 ASN A ND2 6854 N N . GLN A 914 ? 2.7309 2.1473 1.8552 0.4479 -0.0823 0.6119 914 GLN A N 6855 C CA . GLN A 914 ? 2.3979 1.7798 1.5705 0.4750 -0.1164 0.6112 914 GLN A CA 6856 C C . GLN A 914 ? 2.3504 1.6675 1.5909 0.4624 -0.1015 0.6122 914 GLN A C 6857 O O . GLN A 914 ? 2.4595 1.7874 1.7514 0.4446 -0.0831 0.5691 914 GLN A O 6858 C CB . GLN A 914 ? 2.5167 1.8808 1.6415 0.4997 -0.1465 0.6628 914 GLN A CB 6859 C CG . GLN A 914 ? 2.5514 1.9262 1.7272 0.5301 -0.1889 0.6445 914 GLN A CG 6860 C CD . GLN A 914 ? 2.6186 2.0093 1.7560 0.5452 -0.2217 0.6793 914 GLN A CD 6861 O OE1 . GLN A 914 ? 2.6026 2.0065 1.6651 0.5345 -0.2155 0.7102 914 GLN A OE1 6862 N NE2 . GLN A 914 ? 2.5729 1.9669 1.7618 0.5708 -0.2560 0.6745 914 GLN A NE2 6863 N N . ASN A 915 ? 2.4753 1.7262 1.7189 0.4692 -0.1122 0.6567 915 ASN A N 6864 C CA . ASN A 915 ? 2.4295 1.6133 1.7332 0.4517 -0.1001 0.6552 915 ASN A CA 6865 C C . ASN A 915 ? 2.3156 1.4890 1.6113 0.4117 -0.0583 0.6621 915 ASN A C 6866 O O . ASN A 915 ? 2.4299 1.6049 1.6743 0.3896 -0.0394 0.7054 915 ASN A O 6867 C CB . ASN A 915 ? 2.5441 1.6675 1.8568 0.4511 -0.1201 0.6963 915 ASN A CB 6868 C CG . ASN A 915 ? 2.5134 1.6568 1.8414 0.4901 -0.1608 0.6917 915 ASN A CG 6869 O OD1 . ASN A 915 ? 2.5923 1.8024 1.9007 0.5122 -0.1759 0.6731 915 ASN A OD1 6870 N ND2 . ASN A 915 ? 2.4570 1.5437 1.8219 0.4989 -0.1801 0.7084 915 ASN A ND2 6871 N N . HIS A 916 ? 2.2755 1.4515 1.6333 0.3972 -0.0450 0.6149 916 HIS A N 6872 C CA . HIS A 916 ? 2.3670 1.5569 1.7421 0.3547 -0.0091 0.6041 916 HIS A CA 6873 C C . HIS A 916 ? 2.1645 1.3608 1.6087 0.3521 -0.0068 0.5455 916 HIS A C 6874 O O . HIS A 916 ? 2.1993 1.4089 1.6693 0.3816 -0.0287 0.5118 916 HIS A O 6875 C CB . HIS A 916 ? 2.2944 1.5643 1.6230 0.3424 0.0120 0.6006 916 HIS A CB 6876 C CG . HIS A 916 ? 2.3806 1.6525 1.6893 0.3033 0.0470 0.6381 916 HIS A CG 6877 N ND1 . HIS A 916 ? 2.3624 1.5817 1.6389 0.2894 0.0500 0.7035 916 HIS A ND1 6878 C CD2 . HIS A 916 ? 2.3750 1.6995 1.6947 0.2750 0.0806 0.6216 916 HIS A CD2 6879 C CE1 . HIS A 916 ? 2.2665 1.5106 1.5367 0.2504 0.0854 0.7266 916 HIS A CE1 6880 N NE2 . HIS A 916 ? 2.3886 1.6999 1.6862 0.2430 0.1047 0.6767 916 HIS A NE2 6881 N N . SER A 917 ? 1.8940 1.0870 1.3684 0.3163 0.0195 0.5350 917 SER A N 6882 C CA . SER A 917 ? 1.8363 1.0316 1.3718 0.3120 0.0216 0.4834 917 SER A CA 6883 C C . SER A 917 ? 1.9547 1.2235 1.5016 0.2932 0.0442 0.4478 917 SER A C 6884 O O . SER A 917 ? 2.0323 1.3212 1.5720 0.2627 0.0702 0.4638 917 SER A O 6885 C CB . SER A 917 ? 2.1189 1.2366 1.6886 0.2891 0.0256 0.4944 917 SER A CB 6886 O OG . SER A 917 ? 2.4212 1.5221 1.9700 0.2517 0.0458 0.5399 917 SER A OG 6887 N N . TYR A 918 ? 1.9432 1.2534 1.5099 0.3123 0.0339 0.4012 918 TYR A N 6888 C CA . TYR A 918 ? 1.6060 0.9754 1.1875 0.2994 0.0510 0.3636 918 TYR A CA 6889 C C . TYR A 918 ? 1.5276 0.8885 1.1676 0.2957 0.0489 0.3228 918 TYR A C 6890 O O . TYR A 918 ? 1.4880 0.8248 1.1508 0.3160 0.0294 0.3086 918 TYR A O 6891 C CB . TYR A 918 ? 1.5950 1.0200 1.1436 0.3204 0.0405 0.3432 918 TYR A CB 6892 C CG . TYR A 918 ? 1.6714 1.1146 1.1531 0.3259 0.0426 0.3774 918 TYR A CG 6893 C CD1 . TYR A 918 ? 1.7238 1.1976 1.1761 0.3068 0.0717 0.3927 918 TYR A CD1 6894 C CD2 . TYR A 918 ? 1.7175 1.1542 1.1644 0.3519 0.0155 0.3943 918 TYR A CD2 6895 C CE1 . TYR A 918 ? 1.9377 1.4328 1.3223 0.3131 0.0759 0.4239 918 TYR A CE1 6896 C CE2 . TYR A 918 ? 1.9687 1.4236 1.3475 0.3577 0.0158 0.4258 918 TYR A CE2 6897 C CZ . TYR A 918 ? 1.8642 1.3473 1.2092 0.3382 0.0471 0.4404 918 TYR A CZ 6898 O OH . TYR A 918 ? 1.8970 1.4023 1.1679 0.3453 0.0496 0.4719 918 TYR A OH 6899 N N . SER A 919 ? 1.7305 1.1165 1.3943 0.2716 0.0694 0.3048 919 SER A N 6900 C CA . SER A 919 ? 1.6410 1.0291 1.3531 0.2682 0.0676 0.2649 919 SER A CA 6901 C C . SER A 919 ? 1.4227 0.8713 1.1359 0.2721 0.0726 0.2312 919 SER A C 6902 O O . SER A 919 ? 1.4325 0.9164 1.1396 0.2577 0.0921 0.2306 919 SER A O 6903 C CB . SER A 919 ? 1.6959 1.0580 1.4397 0.2370 0.0818 0.2695 919 SER A CB 6904 O OG . SER A 919 ? 1.9613 1.3699 1.7031 0.2142 0.1051 0.2754 919 SER A OG 6905 N N . LEU A 920 ? 1.5172 0.9779 1.2398 0.2921 0.0547 0.2040 920 LEU A N 6906 C CA . LEU A 920 ? 1.3095 0.8157 1.0311 0.2958 0.0544 0.1728 920 LEU A CA 6907 C C . LEU A 920 ? 1.4397 0.9540 1.2019 0.2812 0.0646 0.1471 920 LEU A C 6908 O O . LEU A 920 ? 1.5382 1.0332 1.3333 0.2812 0.0577 0.1345 920 LEU A O 6909 C CB . LEU A 920 ? 1.2791 0.7965 0.9990 0.3167 0.0297 0.1574 920 LEU A CB 6910 C CG . LEU A 920 ? 1.3316 0.8421 1.0153 0.3340 0.0136 0.1835 920 LEU A CG 6911 C CD1 . LEU A 920 ? 1.3984 0.9307 1.0904 0.3518 -0.0129 0.1670 920 LEU A CD1 6912 C CD2 . LEU A 920 ? 1.4028 0.9311 1.0326 0.3315 0.0233 0.1999 920 LEU A CD2 6913 N N . LYS A 921 ? 1.4014 0.9473 1.1594 0.2715 0.0808 0.1390 921 LYS A N 6914 C CA . LYS A 921 ? 1.2240 0.7810 1.0194 0.2571 0.0909 0.1206 921 LYS A CA 6915 C C . LYS A 921 ? 1.2889 0.8775 1.0860 0.2652 0.0889 0.0905 921 LYS A C 6916 O O . LYS A 921 ? 1.6274 1.2423 1.3984 0.2718 0.0971 0.0874 921 LYS A O 6917 C CB . LYS A 921 ? 1.2801 0.8479 1.0813 0.2361 0.1129 0.1413 921 LYS A CB 6918 C CG . LYS A 921 ? 1.2742 0.8712 1.1108 0.2232 0.1235 0.1231 921 LYS A CG 6919 C CD . LYS A 921 ? 1.4694 1.0835 1.3199 0.1985 0.1438 0.1475 921 LYS A CD 6920 C CE . LYS A 921 ? 1.6220 1.2883 1.5007 0.1930 0.1566 0.1315 921 LYS A CE 6921 N NZ . LYS A 921 ? 1.7899 1.4972 1.6405 0.2165 0.1655 0.1198 921 LYS A NZ 6922 N N . SER A 922 ? 1.3360 0.9193 1.1612 0.2658 0.0779 0.0689 922 SER A N 6923 C CA . SER A 922 ? 1.2055 0.8091 1.0369 0.2700 0.0745 0.0433 922 SER A CA 6924 C C . SER A 922 ? 1.0831 0.6948 0.9494 0.2574 0.0830 0.0345 922 SER A C 6925 O O . SER A 922 ? 1.1371 0.7326 1.0261 0.2463 0.0832 0.0392 922 SER A O 6926 C CB . SER A 922 ? 1.1738 0.7710 1.0081 0.2782 0.0539 0.0289 922 SER A CB 6927 O OG . SER A 922 ? 1.2640 0.8483 1.1277 0.2740 0.0493 0.0281 922 SER A OG 6928 N N . SER A 923 ? 1.1302 0.7655 0.9991 0.2610 0.0880 0.0205 923 SER A N 6929 C CA . SER A 923 ? 1.0599 0.7101 0.9617 0.2512 0.0936 0.0132 923 SER A CA 6930 C C . SER A 923 ? 0.9860 0.6392 0.8940 0.2597 0.0825 -0.0078 923 SER A C 6931 O O . SER A 923 ? 1.1538 0.8028 1.0391 0.2730 0.0752 -0.0178 923 SER A O 6932 C CB . SER A 923 ? 1.1086 0.7929 1.0159 0.2471 0.1131 0.0228 923 SER A CB 6933 O OG . SER A 923 ? 1.2086 0.9122 1.0889 0.2662 0.1188 0.0152 923 SER A OG 6934 N N . ALA A 924 ? 1.0100 0.6666 0.9458 0.2508 0.0793 -0.0140 924 ALA A N 6935 C CA . ALA A 924 ? 0.9212 0.5794 0.8629 0.2571 0.0689 -0.0286 924 ALA A CA 6936 C C . ALA A 924 ? 0.8750 0.5569 0.8437 0.2520 0.0724 -0.0313 924 ALA A C 6937 O O . ALA A 924 ? 0.9088 0.5948 0.8970 0.2369 0.0740 -0.0274 924 ALA A O 6938 C CB . ALA A 924 ? 1.0736 0.7123 1.0163 0.2531 0.0555 -0.0323 924 ALA A CB 6939 N N . SER A 925 ? 0.8782 0.5740 0.8472 0.2660 0.0713 -0.0393 925 SER A N 6940 C CA . SER A 925 ? 0.8815 0.6061 0.8779 0.2657 0.0714 -0.0414 925 SER A CA 6941 C C . SER A 925 ? 0.9898 0.6994 0.9838 0.2745 0.0553 -0.0497 925 SER A C 6942 O O . SER A 925 ? 1.0382 0.7184 1.0099 0.2829 0.0466 -0.0546 925 SER A O 6943 C CB . SER A 925 ? 0.9212 0.6842 0.9257 0.2790 0.0860 -0.0404 925 SER A CB 6944 O OG . SER A 925 ? 1.2066 0.9569 1.1849 0.3040 0.0845 -0.0511 925 SER A OG 6945 N N . PHE A 926 ? 0.8587 0.5881 0.8751 0.2703 0.0495 -0.0496 926 PHE A N 6946 C CA . PHE A 926 ? 0.8939 0.6099 0.9064 0.2784 0.0338 -0.0523 926 PHE A CA 6947 C C . PHE A 926 ? 1.1113 0.8617 1.1469 0.2909 0.0306 -0.0526 926 PHE A C 6948 O O . PHE A 926 ? 1.2385 1.0298 1.3008 0.2832 0.0376 -0.0502 926 PHE A O 6949 C CB . PHE A 926 ? 1.0247 0.7274 1.0337 0.2610 0.0251 -0.0497 926 PHE A CB 6950 C CG . PHE A 926 ? 0.9484 0.6787 0.9773 0.2488 0.0227 -0.0497 926 PHE A CG 6951 C CD1 . PHE A 926 ? 0.8852 0.6287 0.9193 0.2526 0.0097 -0.0483 926 PHE A CD1 6952 C CD2 . PHE A 926 ? 0.9209 0.6598 0.9606 0.2326 0.0307 -0.0508 926 PHE A CD2 6953 C CE1 . PHE A 926 ? 1.0449 0.8156 1.0942 0.2404 0.0039 -0.0505 926 PHE A CE1 6954 C CE2 . PHE A 926 ? 0.9066 0.6659 0.9627 0.2186 0.0247 -0.0541 926 PHE A CE2 6955 C CZ . PHE A 926 ? 0.9377 0.7157 0.9981 0.2223 0.0109 -0.0552 926 PHE A CZ 6956 N N . ASN A 927 ? 1.1171 0.8502 1.1441 0.3097 0.0184 -0.0543 927 ASN A N 6957 C CA . ASN A 927 ? 0.9447 0.7087 0.9936 0.3273 0.0115 -0.0533 927 ASN A CA 6958 C C . ASN A 927 ? 0.9757 0.7099 1.0120 0.3320 -0.0092 -0.0473 927 ASN A C 6959 O O . ASN A 927 ? 1.2745 0.9592 1.2850 0.3375 -0.0172 -0.0471 927 ASN A O 6960 C CB . ASN A 927 ? 0.9894 0.7663 1.0412 0.3581 0.0205 -0.0614 927 ASN A CB 6961 C CG . ASN A 927 ? 1.1324 0.9598 1.2177 0.3790 0.0173 -0.0601 927 ASN A CG 6962 O OD1 . ASN A 927 ? 1.1682 1.0362 1.2815 0.3639 0.0123 -0.0529 927 ASN A OD1 6963 N ND2 . ASN A 927 ? 1.2497 1.0758 1.3321 0.4157 0.0187 -0.0687 927 ASN A ND2 6964 N N . VAL A 928 ? 0.8931 0.6574 0.9465 0.3274 -0.0195 -0.0407 928 VAL A N 6965 C CA . VAL A 928 ? 0.9101 0.6508 0.9486 0.3311 -0.0393 -0.0301 928 VAL A CA 6966 C C . VAL A 928 ? 0.9732 0.7155 1.0209 0.3651 -0.0506 -0.0280 928 VAL A C 6967 O O . VAL A 928 ? 1.0881 0.8834 1.1669 0.3780 -0.0518 -0.0288 928 VAL A O 6968 C CB . VAL A 928 ? 0.9346 0.7054 0.9783 0.3112 -0.0476 -0.0245 928 VAL A CB 6969 C CG1 . VAL A 928 ? 0.9844 0.7362 1.0090 0.3172 -0.0677 -0.0095 928 VAL A CG1 6970 C CG2 . VAL A 928 ? 0.9247 0.6865 0.9558 0.2835 -0.0371 -0.0293 928 VAL A CG2 6971 N N . ILE A 929 ? 0.9499 0.6339 0.9724 0.3798 -0.0603 -0.0253 929 ILE A N 6972 C CA . ILE A 929 ? 1.0767 0.7474 1.1034 0.4189 -0.0697 -0.0280 929 ILE A CA 6973 C C . ILE A 929 ? 1.1482 0.8081 1.1731 0.4328 -0.0939 -0.0103 929 ILE A C 6974 O O . ILE A 929 ? 1.5279 1.1872 1.5634 0.4703 -0.1031 -0.0118 929 ILE A O 6975 C CB . ILE A 929 ? 1.0360 0.6381 1.0331 0.4310 -0.0704 -0.0384 929 ILE A CB 6976 C CG1 . ILE A 929 ? 1.3637 0.9024 1.3302 0.4061 -0.0848 -0.0244 929 ILE A CG1 6977 C CG2 . ILE A 929 ? 1.0044 0.6215 1.0001 0.4236 -0.0482 -0.0552 929 ILE A CG2 6978 C CD1 . ILE A 929 ? 1.3209 0.7906 1.2592 0.4094 -0.0894 -0.0354 929 ILE A CD1 6979 N N . GLU A 930 ? 1.0641 0.7193 1.0748 0.4059 -0.1036 0.0067 930 GLU A N 6980 C CA . GLU A 930 ? 1.5230 1.1693 1.5253 0.4161 -0.1273 0.0282 930 GLU A CA 6981 C C . GLU A 930 ? 1.4101 1.0629 1.3916 0.3824 -0.1322 0.0449 930 GLU A C 6982 O O . GLU A 930 ? 1.1190 0.7693 1.0892 0.3529 -0.1181 0.0402 930 GLU A O 6983 C CB . GLU A 930 ? 1.7141 1.2813 1.6924 0.4383 -0.1435 0.0376 930 GLU A CB 6984 C CG . GLU A 930 ? 1.6944 1.1946 1.6398 0.4103 -0.1429 0.0441 930 GLU A CG 6985 C CD . GLU A 930 ? 1.9656 1.3801 1.8877 0.4281 -0.1634 0.0544 930 GLU A CD 6986 O OE1 . GLU A 930 ? 1.8894 1.2915 1.8214 0.4587 -0.1639 0.0382 930 GLU A OE1 6987 O OE2 . GLU A 930 ? 2.0071 1.3758 1.9040 0.4043 -0.1756 0.0792 930 GLU A OE2 6988 N N . PHE A 931 ? 1.4700 1.1335 1.4445 0.3905 -0.1527 0.0646 931 PHE A N 6989 C CA . PHE A 931 ? 1.1824 0.8625 1.1327 0.3637 -0.1581 0.0801 931 PHE A CA 6990 C C . PHE A 931 ? 1.3419 0.9770 1.2594 0.3692 -0.1795 0.1128 931 PHE A C 6991 O O . PHE A 931 ? 1.5407 1.1438 1.4620 0.3998 -0.1961 0.1228 931 PHE A O 6992 C CB . PHE A 931 ? 1.1603 0.9155 1.1320 0.3624 -0.1633 0.0715 931 PHE A CB 6993 C CG . PHE A 931 ? 1.1165 0.9133 1.1207 0.3517 -0.1438 0.0441 931 PHE A CG 6994 C CD1 . PHE A 931 ? 1.1202 0.9293 1.1143 0.3206 -0.1303 0.0324 931 PHE A CD1 6995 C CD2 . PHE A 931 ? 1.0976 0.9210 1.1414 0.3741 -0.1385 0.0315 931 PHE A CD2 6996 C CE1 . PHE A 931 ? 1.0951 0.9333 1.1170 0.3095 -0.1144 0.0111 931 PHE A CE1 6997 C CE2 . PHE A 931 ? 1.1779 1.0396 1.2503 0.3606 -0.1200 0.0119 931 PHE A CE2 6998 C CZ . PHE A 931 ? 1.0768 0.9414 1.1378 0.3270 -0.1092 0.0029 931 PHE A CZ 6999 N N . PRO A 932 ? 1.2854 0.9173 1.1695 0.3409 -0.1786 0.1307 932 PRO A N 7000 C CA . PRO A 932 ? 1.3953 0.9882 1.2444 0.3404 -0.1975 0.1681 932 PRO A CA 7001 C C . PRO A 932 ? 1.4465 1.0694 1.2927 0.3641 -0.2227 0.1840 932 PRO A C 7002 O O . PRO A 932 ? 1.6704 1.2539 1.4909 0.3732 -0.2428 0.2175 932 PRO A O 7003 C CB . PRO A 932 ? 1.3782 0.9847 1.1962 0.3032 -0.1834 0.1787 932 PRO A CB 7004 C CG . PRO A 932 ? 1.3093 0.9757 1.1442 0.2934 -0.1662 0.1460 932 PRO A CG 7005 C CD . PRO A 932 ? 1.2460 0.9095 1.1215 0.3093 -0.1585 0.1181 932 PRO A CD 7006 N N . TYR A 933 ? 1.3482 1.0400 1.2214 0.3722 -0.2236 0.1622 933 TYR A N 7007 C CA . TYR A 933 ? 1.3973 1.1316 1.2716 0.3922 -0.2499 0.1751 933 TYR A CA 7008 C C . TYR A 933 ? 1.3591 1.0924 1.2719 0.4356 -0.2648 0.1729 933 TYR A C 7009 O O . TYR A 933 ? 1.4960 1.2639 1.4532 0.4470 -0.2531 0.1450 933 TYR A O 7010 C CB . TYR A 933 ? 1.4080 1.2204 1.2928 0.3752 -0.2474 0.1524 933 TYR A CB 7011 C CG . TYR A 933 ? 1.3597 1.1737 1.2182 0.3381 -0.2245 0.1395 933 TYR A CG 7012 C CD1 . TYR A 933 ? 1.4266 1.2323 1.2328 0.3200 -0.2259 0.1608 933 TYR A CD1 7013 C CD2 . TYR A 933 ? 1.3188 1.1445 1.2041 0.3237 -0.2009 0.1076 933 TYR A CD2 7014 C CE1 . TYR A 933 ? 1.4648 1.2778 1.2490 0.2919 -0.2033 0.1472 933 TYR A CE1 7015 C CE2 . TYR A 933 ? 1.3930 1.2186 1.2560 0.2957 -0.1812 0.0953 933 TYR A CE2 7016 C CZ . TYR A 933 ? 1.4515 1.2728 1.2655 0.2816 -0.1820 0.1135 933 TYR A CZ 7017 O OH . TYR A 933 ? 1.5362 1.3632 1.3298 0.2591 -0.1607 0.0994 933 TYR A OH 7018 N N . LYS A 934 ? 1.4426 1.1373 1.3372 0.4614 -0.2901 0.2042 934 LYS A N 7019 C CA . LYS A 934 ? 1.7296 1.4144 1.6564 0.5103 -0.3060 0.2041 934 LYS A CA 7020 C C . LYS A 934 ? 1.7858 1.5473 1.7365 0.5358 -0.3316 0.2106 934 LYS A C 7021 O O . LYS A 934 ? 1.8336 1.6228 1.7550 0.5213 -0.3486 0.2307 934 LYS A O 7022 C CB . LYS A 934 ? 1.9194 1.5024 1.8141 0.5281 -0.3212 0.2335 934 LYS A CB 7023 C CG . LYS A 934 ? 1.9475 1.4547 1.8250 0.5039 -0.3005 0.2256 934 LYS A CG 7024 C CD . LYS A 934 ? 1.7280 1.2569 1.6445 0.5111 -0.2758 0.1827 934 LYS A CD 7025 C CE . LYS A 934 ? 1.7097 1.1737 1.6077 0.4832 -0.2571 0.1732 934 LYS A CE 7026 N NZ . LYS A 934 ? 1.7792 1.2673 1.7086 0.4897 -0.2333 0.1337 934 LYS A NZ 7027 N N . ASN A 935 ? 1.7183 1.5197 1.7224 0.5741 -0.3338 0.1930 935 ASN A N 7028 C CA . ASN A 935 ? 1.7839 1.6729 1.8266 0.6013 -0.3576 0.1957 935 ASN A CA 7029 C C . ASN A 935 ? 1.6947 1.6748 1.7527 0.5634 -0.3544 0.1789 935 ASN A C 7030 O O . ASN A 935 ? 1.6372 1.6800 1.7012 0.5677 -0.3816 0.1895 935 ASN A O 7031 C CB . ASN A 935 ? 1.8195 1.6808 1.8304 0.6281 -0.3951 0.2361 935 ASN A CB 7032 C CG . ASN A 935 ? 1.9086 1.6763 1.9098 0.6591 -0.3977 0.2515 935 ASN A CG 7033 O OD1 . ASN A 935 ? 2.0170 1.6937 1.9696 0.6387 -0.3942 0.2709 935 ASN A OD1 7034 N ND2 . ASN A 935 ? 1.8659 1.6636 1.9198 0.6937 -0.3961 0.2407 935 ASN A ND2 7035 N N . LEU A 936 ? 1.6645 1.6472 1.7268 0.5267 -0.3235 0.1523 936 LEU A N 7036 C CA . LEU A 936 ? 1.5151 1.5743 1.5981 0.4916 -0.3182 0.1302 936 LEU A CA 7037 C C . LEU A 936 ? 1.3001 1.3947 1.4381 0.4884 -0.2908 0.1007 936 LEU A C 7038 O O . LEU A 936 ? 1.2316 1.2734 1.3672 0.4949 -0.2668 0.0928 936 LEU A O 7039 C CB . LEU A 936 ? 1.4481 1.4759 1.4756 0.4463 -0.3079 0.1284 936 LEU A CB 7040 C CG . LEU A 936 ? 1.5880 1.6232 1.5641 0.4367 -0.3342 0.1504 936 LEU A CG 7041 C CD1 . LEU A 936 ? 1.8225 1.7875 1.7540 0.4574 -0.3466 0.1888 936 LEU A CD1 7042 C CD2 . LEU A 936 ? 1.6671 1.7020 1.6036 0.3927 -0.3195 0.1345 936 LEU A CD2 7043 N N . PRO A 937 ? 1.4068 1.5921 1.5936 0.4764 -0.2956 0.0856 937 PRO A N 7044 C CA . PRO A 937 ? 1.4821 1.7092 1.7227 0.4693 -0.2689 0.0625 937 PRO A CA 7045 C C . PRO A 937 ? 1.5846 1.7602 1.7982 0.4319 -0.2380 0.0462 937 PRO A C 7046 O O . PRO A 937 ? 1.3063 1.4671 1.4857 0.3957 -0.2400 0.0413 937 PRO A O 7047 C CB . PRO A 937 ? 1.3914 1.7218 1.6812 0.4512 -0.2865 0.0548 937 PRO A CB 7048 C CG . PRO A 937 ? 1.4541 1.7793 1.6975 0.4334 -0.3165 0.0644 937 PRO A CG 7049 C CD . PRO A 937 ? 1.5040 1.7581 1.6967 0.4653 -0.3274 0.0903 937 PRO A CD 7050 N N . ILE A 938 ? 1.6968 1.8474 1.9244 0.4436 -0.2105 0.0368 938 ILE A N 7051 C CA . ILE A 938 ? 1.5819 1.6808 1.7833 0.4139 -0.1830 0.0240 938 ILE A CA 7052 C C . ILE A 938 ? 1.5790 1.7136 1.8232 0.4102 -0.1557 0.0080 938 ILE A C 7053 O O . ILE A 938 ? 1.7218 1.8651 1.9887 0.4443 -0.1451 0.0064 938 ILE A O 7054 C CB . ILE A 938 ? 1.5204 1.5256 1.6725 0.4272 -0.1772 0.0330 938 ILE A CB 7055 C CG1 . ILE A 938 ? 1.2636 1.2514 1.4255 0.4770 -0.1870 0.0425 938 ILE A CG1 7056 C CG2 . ILE A 938 ? 1.6068 1.5722 1.7068 0.4081 -0.1926 0.0481 938 ILE A CG2 7057 C CD1 . ILE A 938 ? 1.1291 1.0847 1.2973 0.4969 -0.1633 0.0282 938 ILE A CD1 7058 N N . GLU A 939 ? 1.4930 1.6467 1.7451 0.3696 -0.1444 -0.0037 939 GLU A N 7059 C CA . GLU A 939 ? 1.5582 1.7423 1.8456 0.3588 -0.1178 -0.0141 939 GLU A CA 7060 C C . GLU A 939 ? 1.5472 1.6582 1.7967 0.3532 -0.0932 -0.0199 939 GLU A C 7061 O O . GLU A 939 ? 1.4345 1.4859 1.6390 0.3364 -0.0955 -0.0201 939 GLU A O 7062 C CB . GLU A 939 ? 1.6001 1.8352 1.9166 0.3159 -0.1208 -0.0214 939 GLU A CB 7063 C CG . GLU A 939 ? 1.5910 1.9080 1.9504 0.3164 -0.1482 -0.0171 939 GLU A CG 7064 C CD . GLU A 939 ? 1.6759 2.0388 2.0662 0.2692 -0.1535 -0.0262 939 GLU A CD 7065 O OE1 . GLU A 939 ? 1.6290 2.0534 2.0475 0.2604 -0.1813 -0.0254 939 GLU A OE1 7066 O OE2 . GLU A 939 ? 1.7514 2.0862 2.1370 0.2403 -0.1322 -0.0336 939 GLU A OE2 7067 N N . ASP A 940 ? 1.5929 1.7149 1.8607 0.3681 -0.0699 -0.0245 940 ASP A N 7068 C CA . ASP A 940 ? 1.6087 1.6666 1.8407 0.3665 -0.0493 -0.0302 940 ASP A CA 7069 C C . ASP A 940 ? 1.2991 1.3414 1.5206 0.3241 -0.0378 -0.0348 940 ASP A C 7070 O O . ASP A 940 ? 1.1115 1.2023 1.3666 0.3012 -0.0303 -0.0359 940 ASP A O 7071 C CB . ASP A 940 ? 1.7598 1.8397 2.0095 0.3958 -0.0279 -0.0354 940 ASP A CB 7072 C CG . ASP A 940 ? 1.8095 1.8123 2.0134 0.4159 -0.0209 -0.0415 940 ASP A CG 7073 O OD1 . ASP A 940 ? 1.7150 1.6571 1.8812 0.3936 -0.0225 -0.0414 940 ASP A OD1 7074 O OD2 . ASP A 940 ? 1.7559 1.7607 1.9622 0.4548 -0.0148 -0.0478 940 ASP A OD2 7075 N N . ILE A 941 ? 1.1515 1.1259 1.3281 0.3137 -0.0373 -0.0363 941 ILE A N 7076 C CA . ILE A 941 ? 1.0225 0.9745 1.1853 0.2801 -0.0283 -0.0413 941 ILE A CA 7077 C C . ILE A 941 ? 1.1341 1.0517 1.2805 0.2813 -0.0066 -0.0438 941 ILE A C 7078 O O . ILE A 941 ? 1.3524 1.2237 1.4688 0.2962 -0.0059 -0.0439 941 ILE A O 7079 C CB . ILE A 941 ? 1.0164 0.9281 1.1424 0.2673 -0.0419 -0.0415 941 ILE A CB 7080 C CG1 . ILE A 941 ? 1.0623 1.0087 1.1963 0.2655 -0.0652 -0.0388 941 ILE A CG1 7081 C CG2 . ILE A 941 ? 1.0185 0.9061 1.1308 0.2395 -0.0320 -0.0495 941 ILE A CG2 7082 C CD1 . ILE A 941 ? 1.0764 0.9901 1.1685 0.2579 -0.0774 -0.0366 941 ILE A CD1 7083 N N . THR A 942 ? 1.2276 1.1675 1.3931 0.2635 0.0090 -0.0444 942 THR A N 7084 C CA . THR A 942 ? 1.2613 1.1733 1.4090 0.2636 0.0286 -0.0444 942 THR A CA 7085 C C . THR A 942 ? 1.2575 1.1676 1.4120 0.2319 0.0378 -0.0420 942 THR A C 7086 O O . THR A 942 ? 1.4766 1.4203 1.6605 0.2102 0.0330 -0.0406 942 THR A O 7087 C CB . THR A 942 ? 1.2981 1.2425 1.4588 0.2891 0.0441 -0.0433 942 THR A CB 7088 O OG1 . THR A 942 ? 1.4693 1.3880 1.6064 0.2875 0.0617 -0.0428 942 THR A OG1 7089 C CG2 . THR A 942 ? 1.1510 1.1724 1.3615 0.2821 0.0506 -0.0374 942 THR A CG2 7090 N N . ASN A 943 ? 1.1280 0.9964 1.2553 0.2292 0.0487 -0.0410 943 ASN A N 7091 C CA . ASN A 943 ? 1.0262 0.8781 1.1533 0.2035 0.0563 -0.0367 943 ASN A CA 7092 C C . ASN A 943 ? 1.0052 0.8146 1.0993 0.2110 0.0662 -0.0341 943 ASN A C 7093 O O . ASN A 943 ? 1.0853 0.8736 1.1559 0.2306 0.0631 -0.0387 943 ASN A O 7094 C CB . ASN A 943 ? 1.0524 0.8828 1.1771 0.1832 0.0411 -0.0447 943 ASN A CB 7095 C CG . ASN A 943 ? 1.3660 1.1966 1.5093 0.1531 0.0433 -0.0414 943 ASN A CG 7096 O OD1 . ASN A 943 ? 1.5669 1.3600 1.6958 0.1446 0.0513 -0.0368 943 ASN A OD1 7097 N ND2 . ASN A 943 ? 1.7256 1.5968 1.9019 0.1357 0.0337 -0.0427 943 ASN A ND2 7098 N N . SER A 944 ? 1.0608 0.8561 1.1534 0.1940 0.0756 -0.0254 944 SER A N 7099 C CA . SER A 944 ? 1.0674 0.8290 1.1298 0.2019 0.0836 -0.0201 944 SER A CA 7100 C C . SER A 944 ? 1.0508 0.7739 1.1062 0.1841 0.0828 -0.0145 944 SER A C 7101 O O . SER A 944 ? 1.3495 1.0707 1.4238 0.1624 0.0789 -0.0139 944 SER A O 7102 C CB . SER A 944 ? 1.1788 0.9693 1.2387 0.2114 0.1014 -0.0096 944 SER A CB 7103 O OG . SER A 944 ? 1.4849 1.2448 1.5121 0.2177 0.1067 -0.0032 944 SER A OG 7104 N N . THR A 945 ? 0.9808 0.6714 1.0088 0.1943 0.0840 -0.0113 945 THR A N 7105 C CA . THR A 945 ? 1.0635 0.7140 1.0825 0.1850 0.0829 -0.0045 945 THR A CA 7106 C C . THR A 945 ? 1.0841 0.7185 1.0758 0.1988 0.0878 0.0066 945 THR A C 7107 O O . THR A 945 ? 1.3551 1.0034 1.3317 0.2151 0.0884 0.0030 945 THR A O 7108 C CB . THR A 945 ? 1.0812 0.7041 1.0973 0.1865 0.0698 -0.0201 945 THR A CB 7109 O OG1 . THR A 945 ? 1.4257 1.0076 1.4373 0.1790 0.0683 -0.0159 945 THR A OG1 7110 C CG2 . THR A 945 ? 0.9592 0.5790 0.9576 0.2064 0.0649 -0.0267 945 THR A CG2 7111 N N . LEU A 946 ? 1.0293 0.6308 1.0126 0.1926 0.0888 0.0198 946 LEU A N 7112 C CA . LEU A 946 ? 1.1836 0.7712 1.1394 0.2059 0.0907 0.0333 946 LEU A CA 7113 C C . LEU A 946 ? 1.1954 0.7408 1.1430 0.2136 0.0802 0.0338 946 LEU A C 7114 O O . LEU A 946 ? 1.1908 0.7081 1.1509 0.2051 0.0757 0.0292 946 LEU A O 7115 C CB . LEU A 946 ? 1.3067 0.9032 1.2553 0.1950 0.1053 0.0583 946 LEU A CB 7116 C CG . LEU A 946 ? 1.2254 0.8051 1.1937 0.1677 0.1100 0.0742 946 LEU A CG 7117 C CD1 . LEU A 946 ? 1.4597 0.9810 1.4130 0.1671 0.1026 0.0888 946 LEU A CD1 7118 C CD2 . LEU A 946 ? 1.2645 0.8856 1.2387 0.1529 0.1290 0.0954 946 LEU A CD2 7119 N N . VAL A 947 ? 1.1443 0.6871 1.0711 0.2316 0.0748 0.0377 947 VAL A N 7120 C CA . VAL A 947 ? 1.0333 0.5463 0.9553 0.2447 0.0647 0.0401 947 VAL A CA 7121 C C . VAL A 947 ? 1.0753 0.5733 0.9725 0.2522 0.0645 0.0649 947 VAL A C 7122 O O . VAL A 947 ? 1.1213 0.6421 0.9972 0.2588 0.0650 0.0704 947 VAL A O 7123 C CB . VAL A 947 ? 0.9448 0.4764 0.8703 0.2599 0.0544 0.0234 947 VAL A CB 7124 C CG1 . VAL A 947 ? 0.9659 0.4812 0.8888 0.2781 0.0448 0.0290 947 VAL A CG1 7125 C CG2 . VAL A 947 ? 0.9162 0.4575 0.8617 0.2536 0.0542 0.0031 947 VAL A CG2 7126 N N . THR A 948 ? 1.1357 0.5913 1.0318 0.2521 0.0621 0.0796 948 THR A N 7127 C CA . THR A 948 ? 1.2371 0.6725 1.1073 0.2578 0.0612 0.1091 948 THR A CA 7128 C C . THR A 948 ? 1.5118 0.9250 1.3762 0.2841 0.0454 0.1129 948 THR A C 7129 O O . THR A 948 ? 1.6094 0.9943 1.4910 0.2934 0.0391 0.1015 948 THR A O 7130 C CB . THR A 948 ? 1.4122 0.8103 1.2829 0.2355 0.0697 0.1325 948 THR A CB 7131 O OG1 . THR A 948 ? 1.8854 1.2521 1.7292 0.2440 0.0656 0.1645 948 THR A OG1 7132 C CG2 . THR A 948 ? 1.3255 0.6816 1.2209 0.2276 0.0641 0.1172 948 THR A CG2 7133 N N . THR A 949 ? 1.5580 0.9877 1.3973 0.2981 0.0386 0.1274 949 THR A N 7134 C CA . THR A 949 ? 1.5074 0.9231 1.3416 0.3245 0.0218 0.1369 949 THR A CA 7135 C C . THR A 949 ? 1.4598 0.8445 1.2612 0.3273 0.0200 0.1745 949 THR A C 7136 O O . THR A 949 ? 1.6228 1.0319 1.3926 0.3242 0.0222 0.1891 949 THR A O 7137 C CB . THR A 949 ? 1.4064 0.8716 1.2404 0.3392 0.0088 0.1233 949 THR A CB 7138 O OG1 . THR A 949 ? 1.5366 1.0274 1.4008 0.3350 0.0106 0.0936 949 THR A OG1 7139 C CG2 . THR A 949 ? 1.1690 0.6305 1.0031 0.3673 -0.0100 0.1355 949 THR A CG2 7140 N N . ASN A 950 ? 1.3797 0.7074 1.1849 0.3341 0.0153 0.1902 950 ASN A N 7141 C CA . ASN A 950 ? 1.3685 0.6560 1.1422 0.3333 0.0136 0.2315 950 ASN A CA 7142 C C . ASN A 950 ? 1.5277 0.8100 1.2853 0.3679 -0.0076 0.2487 950 ASN A C 7143 O O . ASN A 950 ? 1.9032 1.1583 1.6808 0.3933 -0.0206 0.2416 950 ASN A O 7144 C CB . ASN A 950 ? 1.4347 0.6506 1.2187 0.3173 0.0181 0.2434 950 ASN A CB 7145 C CG . ASN A 950 ? 1.6275 0.8538 1.4289 0.2797 0.0366 0.2315 950 ASN A CG 7146 O OD1 . ASN A 950 ? 1.7123 0.9967 1.5235 0.2718 0.0457 0.2086 950 ASN A OD1 7147 N ND2 . ASN A 950 ? 2.0478 1.2161 1.8544 0.2561 0.0400 0.2478 950 ASN A ND2 7148 N N . VAL A 951 ? 1.4789 0.7905 1.1989 0.3710 -0.0115 0.2703 951 VAL A N 7149 C CA . VAL A 951 ? 1.4644 0.7778 1.1649 0.4025 -0.0346 0.2904 951 VAL A CA 7150 C C . VAL A 951 ? 1.5556 0.8180 1.2155 0.4014 -0.0357 0.3402 951 VAL A C 7151 O O . VAL A 951 ? 1.5769 0.8454 1.2036 0.3771 -0.0197 0.3616 951 VAL A O 7152 C CB . VAL A 951 ? 1.4305 0.8141 1.1127 0.4089 -0.0449 0.2780 951 VAL A CB 7153 C CG1 . VAL A 951 ? 1.6361 1.0465 1.2870 0.3820 -0.0255 0.2765 951 VAL A CG1 7154 C CG2 . VAL A 951 ? 1.5372 0.9256 1.1898 0.4367 -0.0700 0.3058 951 VAL A CG2 7155 N N . THR A 952 ? 1.6727 0.8857 1.3355 0.4291 -0.0540 0.3601 952 THR A N 7156 C CA . THR A 952 ? 1.7131 0.8630 1.3389 0.4284 -0.0574 0.4113 952 THR A CA 7157 C C . THR A 952 ? 1.8751 1.0104 1.5045 0.4644 -0.0868 0.4278 952 THR A C 7158 O O . THR A 952 ? 2.0652 1.2334 1.7366 0.4893 -0.1016 0.3968 952 THR A O 7159 C CB . THR A 952 ? 1.7984 0.8720 1.4392 0.4013 -0.0428 0.4197 952 THR A CB 7160 O OG1 . THR A 952 ? 2.3219 1.3376 1.9346 0.3942 -0.0497 0.4697 952 THR A OG1 7161 C CG2 . THR A 952 ? 1.7240 0.7770 1.4210 0.4128 -0.0519 0.3789 952 THR A CG2 7162 N N . TRP A 953 ? 1.8553 0.9554 1.4485 0.4610 -0.0944 0.4752 953 TRP A N 7163 C CA . TRP A 953 ? 2.0334 1.1229 1.6363 0.4885 -0.1233 0.4932 953 TRP A CA 7164 C C . TRP A 953 ? 2.1950 1.2090 1.8356 0.4835 -0.1279 0.4960 953 TRP A C 7165 O O . TRP A 953 ? 2.2487 1.2029 1.8790 0.4506 -0.1141 0.5152 953 TRP A O 7166 C CB . TRP A 953 ? 2.1703 1.2633 1.7106 0.4890 -0.1327 0.5448 953 TRP A CB 7167 C CG . TRP A 953 ? 2.1840 1.3511 1.6815 0.4988 -0.1342 0.5407 953 TRP A CG 7168 C CD1 . TRP A 953 ? 2.0303 1.2248 1.4915 0.4805 -0.1100 0.5345 953 TRP A CD1 7169 C CD2 . TRP A 953 ? 2.2304 1.4538 1.7162 0.5298 -0.1637 0.5416 953 TRP A CD2 7170 N NE1 . TRP A 953 ? 1.9582 1.2245 1.3884 0.4937 -0.1239 0.5247 953 TRP A NE1 7171 C CE2 . TRP A 953 ? 2.0144 1.2938 1.4531 0.5270 -0.1581 0.5328 953 TRP A CE2 7172 C CE3 . TRP A 953 ? 2.2907 1.5247 1.8027 0.5603 -0.1952 0.5483 953 TRP A CE3 7173 C CZ2 . TRP A 953 ? 1.9607 1.3033 1.3761 0.5499 -0.1862 0.5287 953 TRP A CZ2 7174 C CZ3 . TRP A 953 ? 2.2152 1.5176 1.7083 0.5830 -0.2211 0.5474 953 TRP A CZ3 7175 C CH2 . TRP A 953 ? 2.1124 1.4674 1.5571 0.5759 -0.2179 0.5368 953 TRP A CH2 7176 N N . GLY A 954 ? 2.2417 1.2606 1.9269 0.5162 -0.1472 0.4769 954 GLY A N 7177 C CA . GLY A 954 ? 2.1393 1.0876 1.8603 0.5192 -0.1534 0.4760 954 GLY A CA 7178 C C . GLY A 954 ? 2.3513 1.2485 2.0528 0.5280 -0.1733 0.5273 954 GLY A C 7179 O O . GLY A 954 ? 2.5657 1.3846 2.2808 0.5171 -0.1752 0.5423 954 GLY A O 7180 N N . ILE A 955 ? 2.4828 1.4240 2.1522 0.5471 -0.1896 0.5549 955 ILE A N 7181 C CA . ILE A 955 ? 2.7054 1.6075 2.3541 0.5591 -0.2119 0.6060 955 ILE A CA 7182 C C . ILE A 955 ? 2.8070 1.6802 2.3904 0.5220 -0.2036 0.6585 955 ILE A C 7183 O O . ILE A 955 ? 2.8815 1.7271 2.4353 0.5256 -0.2208 0.7082 955 ILE A O 7184 C CB . ILE A 955 ? 2.6069 1.5761 2.2568 0.6016 -0.2382 0.6096 955 ILE A CB 7185 C CG1 . ILE A 955 ? 2.4792 1.5163 2.1827 0.6284 -0.2374 0.5533 955 ILE A CG1 7186 C CG2 . ILE A 955 ? 2.5266 1.4483 2.1865 0.6276 -0.2640 0.6467 955 ILE A CG2 7187 C CD1 . ILE A 955 ? 2.2896 1.3988 2.0054 0.6685 -0.2644 0.5551 955 ILE A CD1 7188 N N . GLN A 956 ? 2.6597 1.5438 2.2210 0.4868 -0.1758 0.6484 956 GLN A N 7189 C CA . GLN A 956 ? 2.5754 1.4457 2.0750 0.4492 -0.1600 0.6953 956 GLN A CA 7190 C C . GLN A 956 ? 2.8347 1.6171 2.3292 0.4249 -0.1667 0.7456 956 GLN A C 7191 O O . GLN A 956 ? 2.8615 1.5818 2.4064 0.4278 -0.1753 0.7351 956 GLN A O 7192 C CB . GLN A 956 ? 2.3092 1.1987 1.8030 0.4161 -0.1253 0.6719 956 GLN A CB 7193 C CG . GLN A 956 ? 2.4625 1.2907 2.0047 0.3909 -0.1141 0.6494 956 GLN A CG 7194 C CD . GLN A 956 ? 2.7895 1.6413 2.3273 0.3587 -0.0807 0.6293 956 GLN A CD 7195 O OE1 . GLN A 956 ? 2.8509 1.7706 2.3600 0.3640 -0.0654 0.6206 956 GLN A OE1 7196 N NE2 . GLN A 956 ? 2.8004 1.5965 2.3684 0.3257 -0.0702 0.6220 956 GLN A NE2 7197 N N . GLY B 1 ? 1.6508 2.7763 2.4372 -0.2137 -0.6035 -0.4158 1 GLY B N 7198 C CA . GLY B 1 ? 1.7100 2.8788 2.5168 -0.2155 -0.5640 -0.4215 1 GLY B CA 7199 C C . GLY B 1 ? 1.7891 2.7681 2.4985 -0.1617 -0.5708 -0.3347 1 GLY B C 7200 O O . GLY B 1 ? 1.7221 2.6074 2.3163 -0.1997 -0.5314 -0.2558 1 GLY B O 7201 N N . PRO B 2 ? 1.8698 2.7897 2.6296 -0.0764 -0.6277 -0.3514 2 PRO B N 7202 C CA . PRO B 2 ? 1.8523 2.6001 2.5220 -0.0282 -0.6387 -0.2769 2 PRO B CA 7203 C C . PRO B 2 ? 1.7626 2.5316 2.4187 -0.0439 -0.5799 -0.2590 2 PRO B C 7204 O O . PRO B 2 ? 1.6495 2.5805 2.3903 -0.0801 -0.5434 -0.3196 2 PRO B O 7205 C CB . PRO B 2 ? 1.8874 2.6099 2.6459 0.0520 -0.7249 -0.3185 2 PRO B CB 7206 C CG . PRO B 2 ? 1.8698 2.7012 2.7356 0.0506 -0.7694 -0.3955 2 PRO B CG 7207 C CD . PRO B 2 ? 1.8353 2.8443 2.7455 -0.0246 -0.6963 -0.4448 2 PRO B CD 7208 N N . ASN B 3 ? 1.8436 2.4575 2.3932 -0.0228 -0.5699 -0.1815 3 ASN B N 7209 C CA . ASN B 3 ? 1.8044 2.4195 2.3372 -0.0308 -0.5205 -0.1592 3 ASN B CA 7210 C C . ASN B 3 ? 1.7992 2.2653 2.2741 0.0291 -0.5413 -0.1109 3 ASN B C 7211 O O . ASN B 3 ? 1.7973 2.1720 2.2524 0.0729 -0.6006 -0.1007 3 ASN B O 7212 C CB . ASN B 3 ? 1.8188 2.4140 2.2623 -0.1063 -0.4625 -0.1049 3 ASN B CB 7213 C CG . ASN B 3 ? 1.9376 2.3704 2.2647 -0.1097 -0.4699 -0.0349 3 ASN B CG 7214 O OD1 . ASN B 3 ? 1.8845 2.1886 2.1439 -0.0772 -0.4681 0.0109 3 ASN B OD1 7215 N ND2 . ASN B 3 ? 2.0746 2.5216 2.3832 -0.1533 -0.4763 -0.0339 3 ASN B ND2 7216 N N . ILE B 4 ? 1.8109 2.2534 2.2532 0.0227 -0.4954 -0.0800 4 ILE B N 7217 C CA . ILE B 4 ? 1.8593 2.1781 2.2514 0.0722 -0.5066 -0.0397 4 ILE B CA 7218 C C . ILE B 4 ? 1.8802 2.0336 2.1423 0.0721 -0.5164 0.0249 4 ILE B C 7219 O O . ILE B 4 ? 1.9312 1.9858 2.1517 0.1096 -0.5581 0.0444 4 ILE B O 7220 C CB . ILE B 4 ? 1.7071 2.0417 2.0907 0.0582 -0.4489 -0.0211 4 ILE B CB 7221 C CG1 . ILE B 4 ? 1.7182 2.2341 2.2265 0.0457 -0.4316 -0.0937 4 ILE B CG1 7222 C CG2 . ILE B 4 ? 1.6244 1.8384 1.9605 0.1083 -0.4595 0.0155 4 ILE B CG2 7223 C CD1 . ILE B 4 ? 1.6872 2.3151 2.1944 -0.0402 -0.3829 -0.1031 4 ILE B CD1 7224 N N . CYS B 5 ? 1.8627 1.9900 2.0628 0.0231 -0.4819 0.0538 5 CYS B N 7225 C CA . CYS B 5 ? 1.9392 1.9317 2.0313 0.0157 -0.4826 0.0979 5 CYS B CA 7226 C C . CYS B 5 ? 1.9855 1.9414 2.0539 0.0284 -0.5394 0.0892 5 CYS B C 7227 O O . CYS B 5 ? 2.0363 1.8821 2.0149 0.0325 -0.5547 0.1173 5 CYS B O 7228 C CB . CYS B 5 ? 1.9690 1.9509 2.0293 -0.0380 -0.4445 0.1188 5 CYS B CB 7229 S SG . CYS B 5 ? 2.3206 2.3184 2.3926 -0.0657 -0.3930 0.1419 5 CYS B SG 7230 N N . THR B 6 ? 1.9440 1.9982 2.0920 0.0276 -0.5709 0.0466 6 THR B N 7231 C CA . THR B 6 ? 2.0125 2.0385 2.1482 0.0367 -0.6321 0.0363 6 THR B CA 7232 C C . THR B 6 ? 2.0499 2.0026 2.1744 0.0817 -0.7004 0.0426 6 THR B C 7233 O O . THR B 6 ? 2.1844 2.0312 2.2142 0.0747 -0.7379 0.0739 6 THR B O 7234 C CB . THR B 6 ? 2.0386 2.2006 2.2830 0.0282 -0.6533 -0.0220 6 THR B CB 7235 O OG1 . THR B 6 ? 2.0497 2.3127 2.4181 0.0643 -0.6764 -0.0767 6 THR B OG1 7236 C CG2 . THR B 6 ? 2.0175 2.2529 2.2656 -0.0301 -0.5939 -0.0231 6 THR B CG2 7237 N N . THR B 7 ? 1.9465 1.9566 2.1674 0.1210 -0.7210 0.0115 7 THR B N 7238 C CA . THR B 7 ? 1.8373 1.7822 2.0749 0.1654 -0.8061 0.0121 7 THR B CA 7239 C C . THR B 7 ? 1.8910 1.6888 1.9951 0.1616 -0.8044 0.0774 7 THR B C 7240 O O . THR B 7 ? 1.9705 1.6585 1.9898 0.1554 -0.8697 0.1107 7 THR B O 7241 C CB . THR B 7 ? 1.6517 1.7073 2.0502 0.2106 -0.8287 -0.0509 7 THR B CB 7242 O OG1 . THR B 7 ? 1.6078 1.6951 2.0037 0.2055 -0.7511 -0.0416 7 THR B OG1 7243 C CG2 . THR B 7 ? 1.5651 1.7856 2.1056 0.2074 -0.8331 -0.1324 7 THR B CG2 7244 N N . ARG B 8 ? 1.9482 1.7466 2.0299 0.1576 -0.7315 0.0946 8 ARG B N 7245 C CA . ARG B 8 ? 2.0227 1.7018 1.9961 0.1552 -0.7238 0.1446 8 ARG B CA 7246 C C . ARG B 8 ? 2.1795 1.7692 2.0076 0.1052 -0.6834 0.1834 8 ARG B C 7247 O O . ARG B 8 ? 2.2991 1.7880 2.0195 0.0888 -0.6891 0.2188 8 ARG B O 7248 C CB . ARG B 8 ? 1.7435 1.4635 1.7619 0.1734 -0.6638 0.1408 8 ARG B CB 7249 C CG . ARG B 8 ? 1.6941 1.5008 1.8555 0.2220 -0.7033 0.0945 8 ARG B CG 7250 C CD . ARG B 8 ? 1.7361 1.6108 1.9459 0.2285 -0.6315 0.0837 8 ARG B CD 7251 N NE . ARG B 8 ? 1.8268 1.7945 2.1799 0.2730 -0.6663 0.0280 8 ARG B NE 7252 C CZ . ARG B 8 ? 1.9232 2.0448 2.4140 0.2771 -0.6688 -0.0449 8 ARG B CZ 7253 N NH1 . ARG B 8 ? 1.9355 2.1261 2.4264 0.2363 -0.6404 -0.0604 8 ARG B NH1 7254 N NH2 . ARG B 8 ? 2.0460 2.2595 2.6800 0.3182 -0.7001 -0.1093 8 ARG B NH2 7255 N N . GLY B 9 ? 2.1540 1.7866 1.9831 0.0763 -0.6440 0.1705 9 GLY B N 7256 C CA . GLY B 9 ? 2.2366 1.8038 1.9581 0.0316 -0.6018 0.1892 9 GLY B CA 7257 C C . GLY B 9 ? 2.3188 1.8469 1.9713 0.0004 -0.6445 0.1912 9 GLY B C 7258 O O . GLY B 9 ? 2.3610 1.8681 1.9554 -0.0380 -0.6071 0.1881 9 GLY B O 7259 N N . VAL B 10 ? 2.2471 1.7656 1.9147 0.0169 -0.7285 0.1920 10 VAL B N 7260 C CA . VAL B 10 ? 2.3000 1.7783 1.9019 -0.0139 -0.7829 0.1973 10 VAL B CA 7261 C C . VAL B 10 ? 2.4710 1.8493 1.9095 -0.0719 -0.7727 0.2267 10 VAL B C 7262 O O . VAL B 10 ? 2.5716 1.9516 1.9585 -0.1127 -0.7356 0.2145 10 VAL B O 7263 C CB . VAL B 10 ? 2.3669 1.8328 2.0179 0.0160 -0.8943 0.1963 10 VAL B CB 7264 C CG1 . VAL B 10 ? 2.4458 1.8539 2.0115 -0.0232 -0.9584 0.2104 10 VAL B CG1 7265 C CG2 . VAL B 10 ? 2.2421 1.8334 2.0683 0.0649 -0.9034 0.1447 10 VAL B CG2 7266 N N . SER B 11 ? 2.5401 1.8381 1.9004 -0.0810 -0.8068 0.2600 11 SER B N 7267 C CA . SER B 11 ? 2.7077 1.9128 1.8976 -0.1521 -0.8209 0.2887 11 SER B CA 7268 C C . SER B 11 ? 2.7513 1.9666 1.8698 -0.2029 -0.7231 0.2648 11 SER B C 7269 O O . SER B 11 ? 2.9189 2.1236 1.9570 -0.2584 -0.7214 0.2538 11 SER B O 7270 C CB . SER B 11 ? 2.7372 1.8604 1.8613 -0.1573 -0.8651 0.3295 11 SER B CB 7271 O OG . SER B 11 ? 2.9084 1.9472 1.8513 -0.2438 -0.8784 0.3585 11 SER B OG 7272 N N . SER B 12 ? 2.6227 1.8616 1.7800 -0.1844 -0.6460 0.2500 12 SER B N 7273 C CA . SER B 12 ? 2.6202 1.8663 1.7292 -0.2289 -0.5624 0.2157 12 SER B CA 7274 C C . SER B 12 ? 2.5212 1.8250 1.7521 -0.1869 -0.4919 0.1854 12 SER B C 7275 O O . SER B 12 ? 2.4443 1.7824 1.7758 -0.1319 -0.4987 0.1974 12 SER B O 7276 C CB . SER B 12 ? 2.8048 1.9908 1.7862 -0.2806 -0.5471 0.2283 12 SER B CB 7277 O OG . SER B 12 ? 2.8198 1.9931 1.8436 -0.2362 -0.5394 0.2496 12 SER B OG 7278 N N . CYS B 13 ? 2.6005 1.9165 1.8252 -0.2189 -0.4299 0.1417 13 CYS B N 7279 C CA . CYS B 13 ? 2.6117 1.9640 1.9486 -0.1885 -0.3773 0.1140 13 CYS B CA 7280 C C . CYS B 13 ? 2.5758 1.9159 1.9412 -0.1557 -0.3509 0.1302 13 CYS B C 7281 O O . CYS B 13 ? 2.4298 1.7987 1.8948 -0.1166 -0.3371 0.1354 13 CYS B O 7282 C CB . CYS B 13 ? 2.6677 2.0278 2.0033 -0.2295 -0.3295 0.0524 13 CYS B CB 7283 S SG . CYS B 13 ? 2.6296 2.0127 2.1134 -0.1969 -0.2899 0.0186 13 CYS B SG 7284 N N . GLN B 14 ? 2.6117 1.9089 1.8818 -0.1799 -0.3460 0.1399 14 GLN B N 7285 C CA . GLN B 14 ? 2.4468 1.7283 1.7344 -0.1512 -0.3226 0.1560 14 GLN B CA 7286 C C . GLN B 14 ? 2.2591 1.5508 1.6032 -0.0960 -0.3684 0.2009 14 GLN B C 7287 O O . GLN B 14 ? 2.1420 1.4604 1.5716 -0.0549 -0.3453 0.2049 14 GLN B O 7288 C CB . GLN B 14 ? 2.5981 1.8314 1.7577 -0.2015 -0.3116 0.1570 14 GLN B CB 7289 C CG . GLN B 14 ? 2.6026 1.8496 1.7281 -0.2569 -0.2480 0.0909 14 GLN B CG 7290 C CD . GLN B 14 ? 2.7061 1.9220 1.7150 -0.3106 -0.2242 0.0866 14 GLN B CD 7291 O OE1 . GLN B 14 ? 2.6318 1.8426 1.6724 -0.2870 -0.1902 0.0837 14 GLN B OE1 7292 N NE2 . GLN B 14 ? 2.8727 2.0683 1.7385 -0.3914 -0.2439 0.0877 14 GLN B NE2 7293 N N . GLN B 15 ? 2.3944 1.6684 1.6973 -0.0982 -0.4374 0.2287 15 GLN B N 7294 C CA . GLN B 15 ? 2.4272 1.7234 1.8060 -0.0450 -0.4904 0.2529 15 GLN B CA 7295 C C . GLN B 15 ? 2.3149 1.6970 1.8224 -0.0108 -0.4749 0.2328 15 GLN B C 7296 O O . GLN B 15 ? 2.2452 1.6764 1.8421 0.0313 -0.4869 0.2344 15 GLN B O 7297 C CB . GLN B 15 ? 2.4593 1.7160 1.7857 -0.0559 -0.5818 0.2767 15 GLN B CB 7298 C CG . GLN B 15 ? 2.4924 1.6547 1.6794 -0.1009 -0.6177 0.3104 15 GLN B CG 7299 C CD . GLN B 15 ? 2.6066 1.7150 1.7536 -0.1098 -0.7309 0.3426 15 GLN B CD 7300 O OE1 . GLN B 15 ? 2.6210 1.7706 1.8759 -0.0622 -0.7847 0.3332 15 GLN B OE1 7301 N NE2 . GLN B 15 ? 2.7647 1.7819 1.7572 -0.1773 -0.7726 0.3777 15 GLN B NE2 7302 N N . CYS B 16 ? 2.2783 1.6826 1.7932 -0.0366 -0.4495 0.2105 16 CYS B N 7303 C CA . CYS B 16 ? 2.2625 1.7404 1.8803 -0.0232 -0.4352 0.1960 16 CYS B CA 7304 C C . CYS B 16 ? 2.1426 1.6313 1.8111 -0.0155 -0.3804 0.1934 16 CYS B C 7305 O O . CYS B 16 ? 1.9638 1.5068 1.7067 0.0068 -0.3762 0.1997 16 CYS B O 7306 C CB . CYS B 16 ? 2.3505 1.8363 1.9567 -0.0567 -0.4377 0.1764 16 CYS B CB 7307 S SG . CYS B 16 ? 2.2026 1.7779 1.9190 -0.0540 -0.4401 0.1661 16 CYS B SG 7308 N N . LEU B 17 ? 2.2609 1.7033 1.8939 -0.0388 -0.3416 0.1778 17 LEU B N 7309 C CA . LEU B 17 ? 2.1956 1.6328 1.8814 -0.0334 -0.3001 0.1716 17 LEU B CA 7310 C C . LEU B 17 ? 1.9922 1.4407 1.7041 -0.0004 -0.2906 0.1954 17 LEU B C 7311 O O . LEU B 17 ? 1.8636 1.3378 1.6412 0.0061 -0.2752 0.2029 17 LEU B O 7312 C CB . LEU B 17 ? 2.2469 1.6336 1.8949 -0.0572 -0.2650 0.1366 17 LEU B CB 7313 C CG . LEU B 17 ? 2.2242 1.6096 1.9344 -0.0770 -0.2563 0.1012 17 LEU B CG 7314 C CD1 . LEU B 17 ? 2.3682 1.7748 2.0675 -0.0992 -0.2854 0.0926 17 LEU B CD1 7315 C CD2 . LEU B 17 ? 2.2615 1.6136 1.9672 -0.0941 -0.2195 0.0472 17 LEU B CD2 7316 N N . ALA B 18 ? 1.9000 1.3260 1.5589 0.0153 -0.3055 0.2093 18 ALA B N 7317 C CA . ALA B 18 ? 1.7703 1.2211 1.4711 0.0512 -0.3070 0.2277 18 ALA B CA 7318 C C . ALA B 18 ? 1.7565 1.2612 1.4970 0.0737 -0.3588 0.2312 18 ALA B C 7319 O O . ALA B 18 ? 2.0304 1.5019 1.7278 0.0823 -0.4047 0.2399 18 ALA B O 7320 C CB . ALA B 18 ? 1.8575 1.2469 1.4936 0.0573 -0.2937 0.2377 18 ALA B CB 7321 N N . VAL B 19 ? 1.6956 1.2853 1.5227 0.0771 -0.3561 0.2208 19 VAL B N 7322 C CA . VAL B 19 ? 1.8046 1.4803 1.7108 0.1023 -0.3900 0.2050 19 VAL B CA 7323 C C . VAL B 19 ? 1.7800 1.5323 1.7566 0.0971 -0.3506 0.1996 19 VAL B C 7324 O O . VAL B 19 ? 1.7051 1.4872 1.7211 0.1226 -0.3428 0.1958 19 VAL B O 7325 C CB . VAL B 19 ? 1.9746 1.7031 1.9099 0.0899 -0.4283 0.1837 19 VAL B CB 7326 C CG1 . VAL B 19 ? 1.9446 1.7858 1.9892 0.1144 -0.4573 0.1476 19 VAL B CG1 7327 C CG2 . VAL B 19 ? 2.1754 1.8237 2.0309 0.0867 -0.4734 0.1934 19 VAL B CG2 7328 N N . SER B 20 ? 1.7204 1.5009 1.7074 0.0563 -0.3311 0.2008 20 SER B N 7329 C CA . SER B 20 ? 1.6651 1.4924 1.6885 0.0265 -0.2985 0.2093 20 SER B CA 7330 C C . SER B 20 ? 1.6691 1.4170 1.6534 -0.0071 -0.2856 0.2309 20 SER B C 7331 O O . SER B 20 ? 1.7384 1.4461 1.6927 -0.0174 -0.3008 0.2252 20 SER B O 7332 C CB . SER B 20 ? 1.7182 1.6782 1.8087 -0.0046 -0.3058 0.1835 20 SER B CB 7333 O OG . SER B 20 ? 1.7352 1.7317 1.8361 -0.0573 -0.2810 0.2006 20 SER B OG 7334 N N . PRO B 21 ? 1.7106 1.4337 1.7033 -0.0239 -0.2636 0.2512 21 PRO B N 7335 C CA . PRO B 21 ? 1.7570 1.3983 1.7383 -0.0511 -0.2651 0.2640 21 PRO B CA 7336 C C . PRO B 21 ? 1.7923 1.4527 1.7861 -0.1005 -0.2920 0.2666 21 PRO B C 7337 O O . PRO B 21 ? 1.8185 1.4064 1.8133 -0.1174 -0.3059 0.2671 21 PRO B O 7338 C CB . PRO B 21 ? 1.7411 1.3692 1.7437 -0.0633 -0.2511 0.2879 21 PRO B CB 7339 C CG . PRO B 21 ? 1.6483 1.3805 1.6730 -0.0619 -0.2389 0.2872 21 PRO B CG 7340 C CD . PRO B 21 ? 1.6372 1.4011 1.6573 -0.0156 -0.2426 0.2593 21 PRO B CD 7341 N N . MET B 22 ? 1.8353 1.5969 1.8477 -0.1246 -0.3012 0.2612 22 MET B N 7342 C CA . MET B 22 ? 1.9822 1.7715 2.0019 -0.1791 -0.3263 0.2647 22 MET B CA 7343 C C . MET B 22 ? 2.0286 1.8070 2.0327 -0.1610 -0.3426 0.2401 22 MET B C 7344 O O . MET B 22 ? 2.1849 1.9704 2.1924 -0.2004 -0.3646 0.2406 22 MET B O 7345 C CB . MET B 22 ? 1.9675 1.8883 2.0146 -0.2269 -0.3238 0.2609 22 MET B CB 7346 C CG . MET B 22 ? 1.9503 1.9764 2.0297 -0.1911 -0.3180 0.2163 22 MET B CG 7347 S SD . MET B 22 ? 2.1888 2.3998 2.3201 -0.2572 -0.3075 0.1860 22 MET B SD 7348 C CE . MET B 22 ? 2.1005 2.3040 2.2007 -0.3473 -0.3321 0.2124 22 MET B CE 7349 N N . CYS B 23 ? 1.9664 1.7234 1.9475 -0.1080 -0.3368 0.2220 23 CYS B N 7350 C CA . CYS B 23 ? 2.0343 1.7772 1.9884 -0.0960 -0.3574 0.2022 23 CYS B CA 7351 C C . CYS B 23 ? 2.0993 1.7531 2.0239 -0.1097 -0.3590 0.1980 23 CYS B C 7352 O O . CYS B 23 ? 2.0496 1.6362 1.9698 -0.1044 -0.3415 0.1997 23 CYS B O 7353 C CB . CYS B 23 ? 2.1044 1.8363 2.0308 -0.0478 -0.3637 0.1921 23 CYS B CB 7354 S SG . CYS B 23 ? 2.3332 2.1772 2.3252 -0.0208 -0.3776 0.1746 23 CYS B SG 7355 N N . ALA B 24 ? 2.2686 1.9293 2.1839 -0.1268 -0.3807 0.1837 24 ALA B N 7356 C CA . ALA B 24 ? 2.3369 1.9279 2.2327 -0.1393 -0.3830 0.1648 24 ALA B CA 7357 C C . ALA B 24 ? 2.3892 1.9727 2.2274 -0.1290 -0.3930 0.1442 24 ALA B C 7358 O O . ALA B 24 ? 2.4676 2.0899 2.2889 -0.1107 -0.4095 0.1501 24 ALA B O 7359 C CB . ALA B 24 ? 2.3481 1.9426 2.2862 -0.1817 -0.4063 0.1680 24 ALA B CB 7360 N N . TRP B 25 ? 2.4375 1.9731 2.2518 -0.1447 -0.3892 0.1159 25 TRP B N 7361 C CA . TRP B 25 ? 2.5287 2.0535 2.2719 -0.1502 -0.3991 0.0976 25 TRP B CA 7362 C C . TRP B 25 ? 2.5945 2.1171 2.3480 -0.1804 -0.4116 0.0683 25 TRP B C 7363 O O . TRP B 25 ? 2.5851 2.0927 2.4001 -0.1943 -0.4093 0.0529 25 TRP B O 7364 C CB . TRP B 25 ? 2.5491 2.0245 2.2250 -0.1492 -0.3717 0.0817 25 TRP B CB 7365 C CG . TRP B 25 ? 2.6068 2.0658 2.1912 -0.1761 -0.3830 0.0637 25 TRP B CG 7366 C CD1 . TRP B 25 ? 2.7025 2.1448 2.2546 -0.2129 -0.3628 0.0153 25 TRP B CD1 7367 C CD2 . TRP B 25 ? 2.6058 2.0655 2.1224 -0.1753 -0.4242 0.0904 25 TRP B CD2 7368 N NE1 . TRP B 25 ? 2.7606 2.1945 2.2104 -0.2436 -0.3836 0.0163 25 TRP B NE1 7369 C CE2 . TRP B 25 ? 2.6940 2.1289 2.1198 -0.2198 -0.4279 0.0670 25 TRP B CE2 7370 C CE3 . TRP B 25 ? 2.6452 2.1263 2.1781 -0.1431 -0.4640 0.1255 25 TRP B CE3 7371 C CZ2 . TRP B 25 ? 2.8180 2.2333 2.1557 -0.2370 -0.4777 0.0907 25 TRP B CZ2 7372 C CZ3 . TRP B 25 ? 2.7145 2.1763 2.1809 -0.1502 -0.5175 0.1408 25 TRP B CZ3 7373 C CH2 . TRP B 25 ? 2.8137 2.2355 2.1768 -0.1987 -0.5276 0.1300 25 TRP B CH2 7374 N N . CYS B 26 ? 2.6842 2.2164 2.3814 -0.1917 -0.4330 0.0607 26 CYS B N 7375 C CA . CYS B 26 ? 2.6700 2.2048 2.3738 -0.2208 -0.4446 0.0302 26 CYS B CA 7376 C C . CYS B 26 ? 2.7127 2.2232 2.3286 -0.2479 -0.4380 -0.0035 26 CYS B C 7377 O O . CYS B 26 ? 2.8337 2.3360 2.3647 -0.2517 -0.4558 0.0151 26 CYS B O 7378 C CB . CYS B 26 ? 2.6940 2.2805 2.4245 -0.2225 -0.4818 0.0487 26 CYS B CB 7379 S SG . CYS B 26 ? 2.8005 2.3943 2.5787 -0.2568 -0.4974 0.0206 26 CYS B SG 7380 N N . SER B 27 ? 2.6471 2.1468 2.2895 -0.2725 -0.4178 -0.0565 27 SER B N 7381 C CA . SER B 27 ? 2.7027 2.2026 2.2811 -0.3140 -0.4088 -0.1064 27 SER B CA 7382 C C . SER B 27 ? 2.7602 2.2842 2.3439 -0.3258 -0.4460 -0.1017 27 SER B C 7383 O O . SER B 27 ? 2.7195 2.2613 2.3121 -0.3046 -0.4796 -0.0535 27 SER B O 7384 C CB . SER B 27 ? 2.6585 2.1545 2.2941 -0.3323 -0.3719 -0.1838 27 SER B CB 7385 O OG . SER B 27 ? 2.6183 2.0967 2.2538 -0.3212 -0.3372 -0.1926 27 SER B OG 7386 N N . ASP B 28 ? 2.8491 2.3823 2.4333 -0.3609 -0.4386 -0.1600 28 ASP B N 7387 C CA . ASP B 28 ? 2.9503 2.5045 2.5065 -0.3846 -0.4687 -0.1661 28 ASP B CA 7388 C C . ASP B 28 ? 3.0374 2.5858 2.4544 -0.4164 -0.4848 -0.1491 28 ASP B C 7389 O O . ASP B 28 ? 3.1383 2.6776 2.4749 -0.4561 -0.4555 -0.1813 28 ASP B O 7390 C CB . ASP B 28 ? 2.9241 2.4974 2.5457 -0.3575 -0.5079 -0.1200 28 ASP B CB 7391 C CG . ASP B 28 ? 2.8998 2.4688 2.6415 -0.3444 -0.5068 -0.1257 28 ASP B CG 7392 O OD1 . ASP B 28 ? 2.8949 2.4447 2.6908 -0.3549 -0.4892 -0.1797 28 ASP B OD1 7393 O OD2 . ASP B 28 ? 2.8972 2.4842 2.6823 -0.3294 -0.5288 -0.0800 28 ASP B OD2 7394 N N . GLU B 29 ? 2.9879 2.5399 2.3759 -0.4037 -0.5348 -0.0993 29 GLU B N 7395 C CA . GLU B 29 ? 3.0037 2.5566 2.3046 -0.4416 -0.5726 -0.0991 29 GLU B CA 7396 C C . GLU B 29 ? 2.9298 2.5183 2.3083 -0.4346 -0.5933 -0.1129 29 GLU B C 7397 O O . GLU B 29 ? 2.9892 2.5845 2.3166 -0.4627 -0.6245 -0.1183 29 GLU B O 7398 C CB . GLU B 29 ? 3.0928 2.6388 2.2889 -0.5107 -0.5439 -0.1485 29 GLU B CB 7399 C CG . GLU B 29 ? 3.1211 2.7049 2.3827 -0.5360 -0.5069 -0.2291 29 GLU B CG 7400 C CD . GLU B 29 ? 3.1919 2.7914 2.3966 -0.5955 -0.4529 -0.3022 29 GLU B CD 7401 O OE1 . GLU B 29 ? 3.2286 2.8660 2.5139 -0.6107 -0.4203 -0.3856 29 GLU B OE1 7402 O OE2 . GLU B 29 ? 3.2055 2.7838 2.2910 -0.6308 -0.4458 -0.2818 29 GLU B OE2 7403 N N . ALA B 30 ? 2.7780 2.3854 2.2745 -0.4026 -0.5805 -0.1139 30 ALA B N 7404 C CA . ALA B 30 ? 2.7225 2.3646 2.2979 -0.3932 -0.6075 -0.1080 30 ALA B CA 7405 C C . ALA B 30 ? 2.7520 2.4209 2.3161 -0.3716 -0.6542 -0.0651 30 ALA B C 7406 O O . ALA B 30 ? 2.7793 2.4917 2.4089 -0.3650 -0.6756 -0.0595 30 ALA B O 7407 C CB . ALA B 30 ? 2.6508 2.2975 2.3360 -0.3765 -0.5922 -0.1053 30 ALA B CB 7408 N N . LEU B 31 ? 2.7204 2.3646 2.2120 -0.3622 -0.6725 -0.0392 31 LEU B N 7409 C CA . LEU B 31 ? 2.6925 2.3483 2.1704 -0.3424 -0.7329 -0.0104 31 LEU B CA 7410 C C . LEU B 31 ? 2.6309 2.3492 2.2172 -0.3008 -0.7479 0.0016 31 LEU B C 7411 O O . LEU B 31 ? 2.6225 2.3931 2.2610 -0.2972 -0.7795 -0.0082 31 LEU B O 7412 C CB . LEU B 31 ? 2.8606 2.5183 2.2937 -0.3717 -0.7758 -0.0227 31 LEU B CB 7413 C CG . LEU B 31 ? 2.7859 2.4783 2.2553 -0.3945 -0.7720 -0.0542 31 LEU B CG 7414 C CD1 . LEU B 31 ? 2.7264 2.4794 2.2786 -0.3706 -0.8130 -0.0501 31 LEU B CD1 7415 C CD2 . LEU B 31 ? 2.8337 2.4928 2.1944 -0.4441 -0.7878 -0.0710 31 LEU B CD2 7416 N N . PRO B 32 ? 2.7030 2.4251 2.3240 -0.2741 -0.7229 0.0168 32 PRO B N 7417 C CA . PRO B 32 ? 2.6894 2.4790 2.3990 -0.2392 -0.7430 0.0213 32 PRO B CA 7418 C C . PRO B 32 ? 2.7027 2.4695 2.3900 -0.2093 -0.7995 0.0342 32 PRO B C 7419 O O . PRO B 32 ? 2.7078 2.4569 2.3971 -0.1857 -0.7903 0.0495 32 PRO B O 7420 C CB . PRO B 32 ? 2.5688 2.3691 2.3207 -0.2320 -0.6895 0.0305 32 PRO B CB 7421 C CG . PRO B 32 ? 2.5559 2.2887 2.2542 -0.2576 -0.6481 0.0277 32 PRO B CG 7422 C CD . PRO B 32 ? 2.6983 2.3800 2.3000 -0.2776 -0.6696 0.0198 32 PRO B CD 7423 N N . LEU B 33 ? 2.6281 2.3873 2.2967 -0.2112 -0.8651 0.0294 33 LEU B N 7424 C CA . LEU B 33 ? 2.6625 2.3873 2.3226 -0.1841 -0.9424 0.0426 33 LEU B CA 7425 C C . LEU B 33 ? 2.6739 2.4963 2.4824 -0.1369 -0.9671 0.0114 33 LEU B C 7426 O O . LEU B 33 ? 2.6989 2.6077 2.5930 -0.1351 -0.9767 -0.0246 33 LEU B O 7427 C CB . LEU B 33 ? 2.6401 2.3130 2.2281 -0.2086 -1.0167 0.0499 33 LEU B CB 7428 C CG . LEU B 33 ? 2.6309 2.2101 2.1452 -0.2074 -1.1050 0.0845 33 LEU B CG 7429 C CD1 . LEU B 33 ? 2.6930 2.1823 2.0571 -0.2531 -1.0685 0.1205 33 LEU B CD1 7430 C CD2 . LEU B 33 ? 2.6087 2.1552 2.0932 -0.2244 -1.2006 0.0872 33 LEU B CD2 7431 N N . GLY B 34 ? 2.6221 2.4397 2.4651 -0.1025 -0.9755 0.0177 34 GLY B N 7432 C CA . GLY B 34 ? 2.5258 2.4579 2.5169 -0.0653 -0.9712 -0.0244 34 GLY B CA 7433 C C . GLY B 34 ? 2.4917 2.4819 2.4982 -0.0890 -0.8743 -0.0254 34 GLY B C 7434 O O . GLY B 34 ? 2.5630 2.4969 2.4827 -0.1240 -0.8276 0.0018 34 GLY B O 7435 N N . SER B 35 ? 2.4423 2.5454 2.5612 -0.0759 -0.8493 -0.0605 35 SER B N 7436 C CA . SER B 35 ? 2.4027 2.5515 2.5268 -0.1087 -0.7691 -0.0524 35 SER B CA 7437 C C . SER B 35 ? 2.3379 2.3757 2.3643 -0.1114 -0.7297 -0.0022 35 SER B C 7438 O O . SER B 35 ? 2.3121 2.2877 2.2665 -0.1431 -0.6997 0.0213 35 SER B O 7439 C CB . SER B 35 ? 2.4261 2.6129 2.5451 -0.1586 -0.7452 -0.0578 35 SER B CB 7440 O OG . SER B 35 ? 2.5003 2.5802 2.5190 -0.1749 -0.7492 -0.0274 35 SER B OG 7441 N N . PRO B 36 ? 2.3449 2.3642 2.3811 -0.0776 -0.7314 0.0057 36 PRO B N 7442 C CA . PRO B 36 ? 2.4523 2.3588 2.3954 -0.0690 -0.7170 0.0466 36 PRO B CA 7443 C C . PRO B 36 ? 2.4819 2.3347 2.3588 -0.1035 -0.6535 0.0712 36 PRO B C 7444 O O . PRO B 36 ? 2.4308 2.3321 2.3474 -0.1291 -0.6155 0.0668 36 PRO B O 7445 C CB . PRO B 36 ? 2.3621 2.3090 2.3719 -0.0327 -0.7128 0.0385 36 PRO B CB 7446 C CG . PRO B 36 ? 2.2964 2.3891 2.4277 -0.0379 -0.7000 -0.0083 36 PRO B CG 7447 C CD . PRO B 36 ? 2.2949 2.4261 2.4507 -0.0508 -0.7394 -0.0355 36 PRO B CD 7448 N N . ARG B 37 ? 2.5002 2.2523 2.2785 -0.1093 -0.6493 0.0935 37 ARG B N 7449 C CA . ARG B 37 ? 2.4703 2.1689 2.1944 -0.1408 -0.6001 0.0987 37 ARG B CA 7450 C C . ARG B 37 ? 2.5638 2.2526 2.3095 -0.1334 -0.5499 0.1094 37 ARG B C 7451 O O . ARG B 37 ? 2.6523 2.2977 2.3765 -0.1536 -0.5139 0.1054 37 ARG B O 7452 C CB . ARG B 37 ? 2.4986 2.1133 2.1089 -0.1615 -0.6121 0.1036 37 ARG B CB 7453 C CG . ARG B 37 ? 2.6370 2.2458 2.2088 -0.1736 -0.6726 0.1009 37 ARG B CG 7454 C CD . ARG B 37 ? 2.8057 2.3305 2.2452 -0.2062 -0.6929 0.1149 37 ARG B CD 7455 N NE . ARG B 37 ? 2.8654 2.3455 2.2703 -0.1870 -0.7238 0.1444 37 ARG B NE 7456 C CZ . ARG B 37 ? 2.9165 2.3704 2.3097 -0.1733 -0.8075 0.1646 37 ARG B CZ 7457 N NH1 . ARG B 37 ? 2.9029 2.3754 2.3170 -0.1752 -0.8657 0.1559 37 ARG B NH1 7458 N NH2 . ARG B 37 ? 2.9346 2.3391 2.3021 -0.1572 -0.8405 0.1921 37 ARG B NH2 7459 N N . CYS B 38 ? 2.5149 2.2466 2.3127 -0.1043 -0.5508 0.1163 38 CYS B N 7460 C CA . CYS B 38 ? 2.2955 2.0154 2.1087 -0.0969 -0.5074 0.1295 38 CYS B CA 7461 C C . CYS B 38 ? 2.2317 2.0248 2.1218 -0.1155 -0.4863 0.1287 38 CYS B C 7462 O O . CYS B 38 ? 2.2531 2.0197 2.1458 -0.1452 -0.4653 0.1357 38 CYS B O 7463 C CB . CYS B 38 ? 2.2089 1.9212 2.0199 -0.0585 -0.5202 0.1392 38 CYS B CB 7464 S SG . CYS B 38 ? 2.3631 2.0653 2.1940 -0.0453 -0.4689 0.1552 38 CYS B SG 7465 N N . ASP B 39 ? 2.2016 2.0883 2.1571 -0.1040 -0.4977 0.1160 39 ASP B N 7466 C CA . ASP B 39 ? 2.1935 2.1713 2.2114 -0.1383 -0.4781 0.1117 39 ASP B CA 7467 C C . ASP B 39 ? 2.1531 2.0877 2.1589 -0.1600 -0.4428 0.1419 39 ASP B C 7468 O O . ASP B 39 ? 2.2423 2.1142 2.2220 -0.1307 -0.4261 0.1556 39 ASP B O 7469 C CB . ASP B 39 ? 2.2931 2.3140 2.3253 -0.1825 -0.4926 0.1006 39 ASP B CB 7470 C CG . ASP B 39 ? 2.3434 2.4783 2.4382 -0.1766 -0.5197 0.0583 39 ASP B CG 7471 O OD1 . ASP B 39 ? 2.2823 2.5105 2.4415 -0.1647 -0.5144 0.0314 39 ASP B OD1 7472 O OD2 . ASP B 39 ? 2.4545 2.5918 2.5439 -0.1835 -0.5473 0.0442 39 ASP B OD2 7473 N N . LEU B 40 ? 2.1309 2.0946 2.1546 -0.2161 -0.4384 0.1539 40 LEU B N 7474 C CA . LEU B 40 ? 2.1689 2.0731 2.1837 -0.2440 -0.4238 0.1871 40 LEU B CA 7475 C C . LEU B 40 ? 2.2014 2.0645 2.2145 -0.3007 -0.4461 0.2048 40 LEU B C 7476 O O . LEU B 40 ? 2.1535 2.0887 2.1816 -0.3553 -0.4596 0.2070 40 LEU B O 7477 C CB . LEU B 40 ? 2.1585 2.1432 2.2020 -0.2663 -0.4045 0.1954 40 LEU B CB 7478 C CG . LEU B 40 ? 2.0104 2.1429 2.0943 -0.3125 -0.4053 0.1700 40 LEU B CG 7479 C CD1 . LEU B 40 ? 1.9697 2.1268 2.0431 -0.4049 -0.4084 0.2018 40 LEU B CD1 7480 C CD2 . LEU B 40 ? 1.9324 2.1656 2.0639 -0.2777 -0.3867 0.1336 40 LEU B CD2 7481 N N . LYS B 41 ? 2.2508 2.0030 2.2527 -0.2907 -0.4529 0.2109 41 LYS B N 7482 C CA . LYS B 41 ? 2.2219 1.9118 2.2427 -0.3403 -0.4854 0.2298 41 LYS B CA 7483 C C . LYS B 41 ? 2.3272 2.0645 2.3533 -0.3950 -0.5152 0.2324 41 LYS B C 7484 O O . LYS B 41 ? 2.3940 2.1462 2.4127 -0.3788 -0.5193 0.2047 41 LYS B O 7485 C CB . LYS B 41 ? 2.1709 1.8353 2.2052 -0.3749 -0.4929 0.2690 41 LYS B CB 7486 C CG . LYS B 41 ? 2.2419 1.7917 2.3083 -0.4010 -0.5382 0.2840 41 LYS B CG 7487 C CD . LYS B 41 ? 2.0758 1.5512 2.1634 -0.3466 -0.5329 0.2366 41 LYS B CD 7488 C CE . LYS B 41 ? 1.9779 1.3580 2.1252 -0.3729 -0.5900 0.2305 41 LYS B CE 7489 N NZ . LYS B 41 ? 1.8748 1.1819 2.0612 -0.3949 -0.6268 0.2638 41 LYS B NZ 7490 N N . GLU B 42 ? 2.3672 2.1248 2.3993 -0.4675 -0.5389 0.2684 42 GLU B N 7491 C CA . GLU B 42 ? 2.2992 2.0992 2.3299 -0.5366 -0.5704 0.2772 42 GLU B CA 7492 C C . GLU B 42 ? 2.1134 2.0427 2.1421 -0.5297 -0.5472 0.2408 42 GLU B C 7493 O O . GLU B 42 ? 2.0559 2.0153 2.0864 -0.5642 -0.5681 0.2318 42 GLU B O 7494 C CB . GLU B 42 ? 2.3576 2.1667 2.3756 -0.6319 -0.5987 0.3282 42 GLU B CB 7495 C CG . GLU B 42 ? 2.3463 2.3092 2.3455 -0.7022 -0.5806 0.3243 42 GLU B CG 7496 C CD . GLU B 42 ? 2.2660 2.3349 2.2711 -0.6743 -0.5277 0.3003 42 GLU B CD 7497 O OE1 . GLU B 42 ? 2.1566 2.1642 2.1664 -0.6155 -0.5111 0.3063 42 GLU B OE1 7498 O OE2 . GLU B 42 ? 2.2612 2.4806 2.2753 -0.7118 -0.5035 0.2681 42 GLU B OE2 7499 N N . ASN B 43 ? 2.1422 2.1457 2.1774 -0.4837 -0.5105 0.2161 43 ASN B N 7500 C CA . ASN B 43 ? 2.1355 2.2547 2.1922 -0.4640 -0.5001 0.1705 43 ASN B CA 7501 C C . ASN B 43 ? 2.0919 2.1546 2.1386 -0.4007 -0.5115 0.1463 43 ASN B C 7502 O O . ASN B 43 ? 2.0779 2.2058 2.1405 -0.3950 -0.5232 0.1144 43 ASN B O 7503 C CB . ASN B 43 ? 2.1288 2.3427 2.2143 -0.4349 -0.4700 0.1455 43 ASN B CB 7504 C CG . ASN B 43 ? 2.0620 2.3824 2.1943 -0.3985 -0.4731 0.0874 43 ASN B CG 7505 O OD1 . ASN B 43 ? 2.0532 2.3402 2.1915 -0.3244 -0.4794 0.0697 43 ASN B OD1 7506 N ND2 . ASN B 43 ? 2.0918 2.5390 2.2590 -0.4556 -0.4751 0.0559 43 ASN B ND2 7507 N N . LEU B 44 ? 2.1552 2.1011 2.1749 -0.3600 -0.5090 0.1577 44 LEU B N 7508 C CA . LEU B 44 ? 2.2051 2.0928 2.1983 -0.3196 -0.5183 0.1361 44 LEU B CA 7509 C C . LEU B 44 ? 2.2826 2.1411 2.2783 -0.3582 -0.5443 0.1331 44 LEU B C 7510 O O . LEU B 44 ? 2.3637 2.1899 2.3383 -0.3394 -0.5536 0.1105 44 LEU B O 7511 C CB . LEU B 44 ? 2.2572 2.0469 2.2207 -0.2795 -0.5007 0.1382 44 LEU B CB 7512 C CG . LEU B 44 ? 2.3028 2.0694 2.2206 -0.2306 -0.4952 0.1199 44 LEU B CG 7513 C CD1 . LEU B 44 ? 2.3517 2.0274 2.2378 -0.2147 -0.4734 0.1154 44 LEU B CD1 7514 C CD2 . LEU B 44 ? 2.4332 2.2120 2.3282 -0.2330 -0.5211 0.0985 44 LEU B CD2 7515 N N . LEU B 45 ? 2.2739 2.1421 2.2914 -0.4193 -0.5603 0.1575 45 LEU B N 7516 C CA . LEU B 45 ? 2.2781 2.1077 2.3054 -0.4616 -0.5945 0.1599 45 LEU B CA 7517 C C . LEU B 45 ? 2.2072 2.1339 2.2392 -0.4961 -0.6065 0.1463 45 LEU B C 7518 O O . LEU B 45 ? 2.1399 2.0485 2.1795 -0.5414 -0.6370 0.1519 45 LEU B O 7519 C CB . LEU B 45 ? 2.2665 2.0345 2.3122 -0.5183 -0.6237 0.2002 45 LEU B CB 7520 C CG . LEU B 45 ? 2.1817 1.8503 2.2413 -0.4862 -0.6206 0.2078 45 LEU B CG 7521 C CD1 . LEU B 45 ? 2.2430 1.8328 2.3323 -0.5455 -0.6731 0.2473 45 LEU B CD1 7522 C CD2 . LEU B 45 ? 2.2001 1.8060 2.2651 -0.4273 -0.6086 0.1618 45 LEU B CD2 7523 N N . LYS B 46 ? 2.2475 2.2785 2.2859 -0.4751 -0.5871 0.1233 46 LYS B N 7524 C CA . LYS B 46 ? 2.2380 2.3694 2.2957 -0.4945 -0.5983 0.0932 46 LYS B CA 7525 C C . LYS B 46 ? 2.3524 2.4229 2.3929 -0.4711 -0.6201 0.0772 46 LYS B C 7526 O O . LYS B 46 ? 2.5028 2.5827 2.5496 -0.5148 -0.6419 0.0760 46 LYS B O 7527 C CB . LYS B 46 ? 2.1738 2.4127 2.2640 -0.4549 -0.5840 0.0550 46 LYS B CB 7528 C CG . LYS B 46 ? 2.2027 2.5341 2.3212 -0.4859 -0.5583 0.0546 46 LYS B CG 7529 C CD . LYS B 46 ? 2.1333 2.5685 2.3082 -0.4355 -0.5515 0.0022 46 LYS B CD 7530 C CE . LYS B 46 ? 2.0648 2.4038 2.2186 -0.3496 -0.5603 0.0069 46 LYS B CE 7531 N NZ . LYS B 46 ? 1.9970 2.4205 2.2165 -0.2987 -0.5713 -0.0416 46 LYS B NZ 7532 N N . ASP B 47 ? 2.3088 2.3190 2.3216 -0.4096 -0.6149 0.0650 47 ASP B N 7533 C CA . ASP B 47 ? 2.4340 2.3645 2.4167 -0.3976 -0.6279 0.0527 47 ASP B CA 7534 C C . ASP B 47 ? 2.4365 2.2730 2.4231 -0.4112 -0.6230 0.0680 47 ASP B C 7535 O O . ASP B 47 ? 2.4463 2.2549 2.4337 -0.3967 -0.6041 0.0844 47 ASP B O 7536 C CB . ASP B 47 ? 2.4907 2.3947 2.4280 -0.3456 -0.6267 0.0352 47 ASP B CB 7537 C CG . ASP B 47 ? 2.6105 2.4381 2.5049 -0.3459 -0.6304 0.0171 47 ASP B CG 7538 O OD1 . ASP B 47 ? 2.6348 2.4572 2.5475 -0.3766 -0.6450 0.0057 47 ASP B OD1 7539 O OD2 . ASP B 47 ? 2.6758 2.4540 2.5175 -0.3218 -0.6187 0.0105 47 ASP B OD2 7540 N N . ASN B 48 ? 2.4584 2.2472 2.4592 -0.4365 -0.6450 0.0572 48 ASN B N 7541 C CA . ASN B 48 ? 2.4837 2.1879 2.5210 -0.4557 -0.6595 0.0645 48 ASN B CA 7542 C C . ASN B 48 ? 2.5709 2.2158 2.6050 -0.4169 -0.6331 0.0558 48 ASN B C 7543 O O . ASN B 48 ? 2.6448 2.2726 2.6962 -0.4231 -0.6310 0.0858 48 ASN B O 7544 C CB . ASN B 48 ? 2.4953 2.1551 2.5585 -0.4707 -0.6875 0.0322 48 ASN B CB 7545 C CG . ASN B 48 ? 2.5041 2.2078 2.5794 -0.5199 -0.7208 0.0470 48 ASN B CG 7546 O OD1 . ASN B 48 ? 2.4556 2.2438 2.5125 -0.5380 -0.7144 0.0669 48 ASN B OD1 7547 N ND2 . ASN B 48 ? 2.5101 2.1631 2.6251 -0.5437 -0.7574 0.0295 48 ASN B ND2 7548 N N . CYS B 49 ? 2.5623 2.1814 2.5690 -0.3850 -0.6128 0.0136 49 CYS B N 7549 C CA . CYS B 49 ? 2.5619 2.1414 2.5528 -0.3526 -0.5801 -0.0026 49 CYS B CA 7550 C C . CYS B 49 ? 2.6088 2.1253 2.6692 -0.3582 -0.5911 -0.0010 49 CYS B C 7551 O O . CYS B 49 ? 2.6353 2.1315 2.6926 -0.3358 -0.5674 0.0057 49 CYS B O 7552 C CB . CYS B 49 ? 2.5399 2.1604 2.4795 -0.3253 -0.5560 0.0274 49 CYS B CB 7553 S SG . CYS B 49 ? 2.9819 2.5663 2.8606 -0.2904 -0.5164 0.0054 49 CYS B SG 7554 N N . ALA B 50 ? 2.6698 2.1500 2.7969 -0.3890 -0.6354 -0.0066 50 ALA B N 7555 C CA . ALA B 50 ? 2.5943 2.0006 2.8022 -0.4008 -0.6715 -0.0007 50 ALA B CA 7556 C C . ALA B 50 ? 2.5116 1.8662 2.7742 -0.3681 -0.6562 -0.0657 50 ALA B C 7557 O O . ALA B 50 ? 2.3026 1.6118 2.6067 -0.3595 -0.6652 -0.0529 50 ALA B O 7558 C CB . ALA B 50 ? 2.5613 1.9317 2.8297 -0.4460 -0.7386 0.0081 50 ALA B CB 7559 N N . PRO B 51 ? 2.5986 1.9675 2.8639 -0.3557 -0.6327 -0.1413 51 PRO B N 7560 C CA . PRO B 51 ? 2.5436 1.8835 2.8751 -0.3349 -0.6151 -0.2220 51 PRO B CA 7561 C C . PRO B 51 ? 2.3726 1.7167 2.6605 -0.3081 -0.5653 -0.2146 51 PRO B C 7562 O O . PRO B 51 ? 2.2905 1.6645 2.4858 -0.3012 -0.5396 -0.1518 51 PRO B O 7563 C CB . PRO B 51 ? 2.5473 1.9326 2.8521 -0.3421 -0.5851 -0.2998 51 PRO B CB 7564 C CG . PRO B 51 ? 2.5150 1.9478 2.7096 -0.3544 -0.5767 -0.2445 51 PRO B CG 7565 C CD . PRO B 51 ? 2.5762 1.9922 2.7933 -0.3679 -0.6243 -0.1658 51 PRO B CD 7566 N N . GLU B 52 ? 2.4245 1.7430 2.7905 -0.2929 -0.5546 -0.2869 52 GLU B N 7567 C CA . GLU B 52 ? 2.4499 1.7652 2.7945 -0.2693 -0.5118 -0.2891 52 GLU B CA 7568 C C . GLU B 52 ? 2.5025 1.8709 2.7020 -0.2670 -0.4492 -0.2684 52 GLU B C 7569 O O . GLU B 52 ? 2.4952 1.8617 2.6547 -0.2497 -0.4157 -0.2502 52 GLU B O 7570 C CB . GLU B 52 ? 2.4163 1.7191 2.8737 -0.2591 -0.5031 -0.4001 52 GLU B CB 7571 C CG . GLU B 52 ? 2.4634 1.6933 3.0864 -0.2522 -0.5803 -0.4211 52 GLU B CG 7572 C CD . GLU B 52 ? 2.5250 1.7502 3.2782 -0.2331 -0.5718 -0.5391 52 GLU B CD 7573 O OE1 . GLU B 52 ? 2.4208 1.7065 3.1196 -0.2316 -0.4957 -0.5986 52 GLU B OE1 7574 O OE2 . GLU B 52 ? 2.5792 1.7528 3.4817 -0.2200 -0.6383 -0.5674 52 GLU B OE2 7575 N N . SER B 53 ? 2.5534 1.9619 2.6774 -0.2867 -0.4416 -0.2715 53 SER B N 7576 C CA . SER B 53 ? 2.7227 2.1674 2.7078 -0.2914 -0.4061 -0.2425 53 SER B CA 7577 C C . SER B 53 ? 2.8086 2.2500 2.7448 -0.2670 -0.4063 -0.1556 53 SER B C 7578 O O . SER B 53 ? 2.7607 2.2123 2.6065 -0.2613 -0.3794 -0.1376 53 SER B O 7579 C CB . SER B 53 ? 2.7230 2.1988 2.6537 -0.3149 -0.4235 -0.2386 53 SER B CB 7580 O OG . SER B 53 ? 2.6980 2.1734 2.6619 -0.3105 -0.4668 -0.1796 53 SER B OG 7581 N N . ILE B 54 ? 2.7991 2.2277 2.7951 -0.2593 -0.4400 -0.1047 54 ILE B N 7582 C CA . ILE B 54 ? 2.5735 2.0122 2.5432 -0.2410 -0.4365 -0.0370 54 ILE B CA 7583 C C . ILE B 54 ? 2.3650 1.7699 2.3591 -0.2203 -0.4111 -0.0448 54 ILE B C 7584 O O . ILE B 54 ? 2.2558 1.6194 2.3360 -0.2212 -0.4230 -0.0787 54 ILE B O 7585 C CB . ILE B 54 ? 2.4503 1.8997 2.4666 -0.2580 -0.4770 0.0151 54 ILE B CB 7586 C CG1 . ILE B 54 ? 2.3894 1.8624 2.3899 -0.2462 -0.4670 0.0700 54 ILE B CG1 7587 C CG2 . ILE B 54 ? 2.4770 1.8703 2.5901 -0.2776 -0.5161 -0.0015 54 ILE B CG2 7588 C CD1 . ILE B 54 ? 2.4343 1.9326 2.4672 -0.2813 -0.5004 0.1170 54 ILE B CD1 7589 N N . GLU B 55 ? 2.4311 1.8507 2.3578 -0.2003 -0.3826 -0.0168 55 GLU B N 7590 C CA . GLU B 55 ? 2.5168 1.9086 2.4566 -0.1803 -0.3546 -0.0223 55 GLU B CA 7591 C C . GLU B 55 ? 2.3703 1.7675 2.3288 -0.1653 -0.3633 0.0406 55 GLU B C 7592 O O . GLU B 55 ? 2.2968 1.7338 2.2059 -0.1545 -0.3600 0.0800 55 GLU B O 7593 C CB . GLU B 55 ? 2.5691 1.9675 2.4145 -0.1764 -0.3160 -0.0402 55 GLU B CB 7594 C CG . GLU B 55 ? 2.5996 1.9985 2.4241 -0.2050 -0.2937 -0.1172 55 GLU B CG 7595 C CD . GLU B 55 ? 2.5036 1.8826 2.4165 -0.2031 -0.2722 -0.1862 55 GLU B CD 7596 O OE1 . GLU B 55 ? 2.3561 1.7090 2.3231 -0.1770 -0.2726 -0.1642 55 GLU B OE1 7597 O OE2 . GLU B 55 ? 2.5353 1.9301 2.4711 -0.2291 -0.2566 -0.2695 55 GLU B OE2 7598 N N . PHE B 56 ? 2.3239 1.6826 2.3603 -0.1678 -0.3799 0.0448 56 PHE B N 7599 C CA . PHE B 56 ? 2.2783 1.6426 2.3273 -0.1658 -0.3874 0.1021 56 PHE B CA 7600 C C . PHE B 56 ? 2.2618 1.5683 2.3695 -0.1537 -0.3865 0.0914 56 PHE B C 7601 O O . PHE B 56 ? 2.2209 1.4818 2.3994 -0.1745 -0.4314 0.1030 56 PHE B O 7602 C CB . PHE B 56 ? 2.2322 1.6154 2.3069 -0.2054 -0.4319 0.1440 56 PHE B CB 7603 C CG . PHE B 56 ? 2.1565 1.5723 2.2257 -0.2204 -0.4341 0.1996 56 PHE B CG 7604 C CD1 . PHE B 56 ? 2.0901 1.5813 2.1132 -0.2035 -0.4039 0.2152 56 PHE B CD1 7605 C CD2 . PHE B 56 ? 2.1335 1.5053 2.2474 -0.2566 -0.4730 0.2324 56 PHE B CD2 7606 C CE1 . PHE B 56 ? 2.0502 1.5895 2.0760 -0.2221 -0.4006 0.2524 56 PHE B CE1 7607 C CE2 . PHE B 56 ? 2.0708 1.4821 2.1680 -0.2841 -0.4722 0.2814 56 PHE B CE2 7608 C CZ . PHE B 56 ? 2.0280 1.5318 2.0831 -0.2668 -0.4302 0.2862 56 PHE B CZ 7609 N N . PRO B 57 ? 2.1191 1.4220 2.1976 -0.1238 -0.3424 0.0700 57 PRO B N 7610 C CA . PRO B 57 ? 1.9748 1.2298 2.1107 -0.1080 -0.3373 0.0548 57 PRO B CA 7611 C C . PRO B 57 ? 1.8376 1.0866 1.9882 -0.1144 -0.3581 0.1218 57 PRO B C 7612 O O . PRO B 57 ? 1.8723 1.1748 1.9655 -0.1132 -0.3416 0.1666 57 PRO B O 7613 C CB . PRO B 57 ? 1.9245 1.1950 1.9973 -0.0833 -0.2799 0.0259 57 PRO B CB 7614 C CG . PRO B 57 ? 2.0127 1.3199 2.0068 -0.0951 -0.2663 0.0098 57 PRO B CG 7615 C CD . PRO B 57 ? 2.0355 1.3724 2.0237 -0.1090 -0.3022 0.0579 57 PRO B CD 7616 N N . VAL B 58 ? 1.6648 0.8511 1.8967 -0.1247 -0.3992 0.1233 58 VAL B N 7617 C CA . VAL B 58 ? 1.6676 0.8417 1.9051 -0.1459 -0.4258 0.1895 58 VAL B CA 7618 C C . VAL B 58 ? 1.7037 0.8375 1.9741 -0.1165 -0.4100 0.1796 58 VAL B C 7619 O O . VAL B 58 ? 1.6750 0.7458 2.0293 -0.1024 -0.4318 0.1296 58 VAL B O 7620 C CB . VAL B 58 ? 1.7881 0.9078 2.0813 -0.1978 -0.5070 0.2210 58 VAL B CB 7621 C CG1 . VAL B 58 ? 1.5757 0.6788 1.8603 -0.2356 -0.5380 0.2916 58 VAL B CG1 7622 C CG2 . VAL B 58 ? 1.9104 1.0770 2.1669 -0.2327 -0.5213 0.2353 58 VAL B CG2 7623 N N . SER B 59 ? 1.4372 0.6129 1.6526 -0.1060 -0.3735 0.2192 59 SER B N 7624 C CA . SER B 59 ? 1.4113 0.5537 1.6509 -0.0802 -0.3573 0.2175 59 SER B CA 7625 C C . SER B 59 ? 1.6166 0.7393 1.9140 -0.1052 -0.4062 0.2323 59 SER B C 7626 O O . SER B 59 ? 1.7349 0.8714 2.0204 -0.1545 -0.4502 0.2801 59 SER B O 7627 C CB . SER B 59 ? 1.4896 0.6972 1.6602 -0.0669 -0.3113 0.2565 59 SER B CB 7628 O OG . SER B 59 ? 1.5601 0.8179 1.6705 -0.0370 -0.2635 0.2317 59 SER B OG 7629 N N . GLU B 60 ? 1.5303 0.8214 1.1887 -0.5578 -0.0811 -0.0214 60 GLU B N 7630 C CA . GLU B 60 ? 1.5244 0.7874 1.1819 -0.5389 -0.0523 -0.0299 60 GLU B CA 7631 C C . GLU B 60 ? 1.8176 1.0772 1.4549 -0.5047 -0.0267 -0.0404 60 GLU B C 7632 O O . GLU B 60 ? 1.9893 1.2500 1.5935 -0.5001 -0.0281 -0.0520 60 GLU B O 7633 C CB . GLU B 60 ? 1.5915 0.7961 1.2115 -0.5619 -0.0538 -0.0513 60 GLU B CB 7634 C CG . GLU B 60 ? 1.7960 0.9617 1.3484 -0.5730 -0.0536 -0.0811 60 GLU B CG 7635 C CD . GLU B 60 ? 2.2853 1.3929 1.8052 -0.5918 -0.0472 -0.1063 60 GLU B CD 7636 O OE1 . GLU B 60 ? 2.3617 1.4596 1.9142 -0.5927 -0.0439 -0.0989 60 GLU B OE1 7637 O OE2 . GLU B 60 ? 2.3849 1.4686 1.8539 -0.5983 -0.0427 -0.1324 60 GLU B OE2 7638 N N . ALA B 61 ? 1.7555 1.0103 1.4128 -0.4831 -0.0049 -0.0345 61 ALA B N 7639 C CA . ALA B 61 ? 1.4990 0.7420 1.1393 -0.4534 0.0170 -0.0441 61 ALA B CA 7640 C C . ALA B 61 ? 1.5815 0.7775 1.2193 -0.4495 0.0304 -0.0519 61 ALA B C 7641 O O . ALA B 61 ? 1.8473 1.0444 1.5135 -0.4489 0.0341 -0.0343 61 ALA B O 7642 C CB . ALA B 61 ? 1.4008 0.6879 1.0702 -0.4294 0.0276 -0.0244 61 ALA B CB 7643 N N . ARG B 62 ? 1.5267 0.6802 1.1331 -0.4482 0.0391 -0.0781 62 ARG B N 7644 C CA . ARG B 62 ? 1.6459 0.7513 1.2590 -0.4440 0.0521 -0.0871 62 ARG B CA 7645 C C . ARG B 62 ? 1.7065 0.8007 1.3223 -0.4132 0.0710 -0.0942 62 ARG B C 7646 O O . ARG B 62 ? 1.7442 0.8479 1.3389 -0.4031 0.0772 -0.1081 62 ARG B O 7647 C CB . ARG B 62 ? 1.6909 0.7474 1.2757 -0.4714 0.0502 -0.1149 62 ARG B CB 7648 C CG . ARG B 62 ? 1.7393 0.7802 1.2772 -0.4779 0.0561 -0.1449 62 ARG B CG 7649 C CD . ARG B 62 ? 1.7229 0.7184 1.2365 -0.4981 0.0617 -0.1747 62 ARG B CD 7650 N NE . ARG B 62 ? 1.7507 0.7510 1.2613 -0.5284 0.0384 -0.1673 62 ARG B NE 7651 C CZ . ARG B 62 ? 2.4574 1.4309 1.9505 -0.5467 0.0380 -0.1878 62 ARG B CZ 7652 N NH1 . ARG B 62 ? 2.4517 1.3923 1.9311 -0.5376 0.0626 -0.2182 62 ARG B NH1 7653 N NH2 . ARG B 62 ? 2.3701 1.3508 1.8635 -0.5743 0.0142 -0.1780 62 ARG B NH2 7654 N N . VAL B 63 ? 1.5504 0.6248 1.1951 -0.3998 0.0782 -0.0823 63 VAL B N 7655 C CA . VAL B 63 ? 1.5398 0.6022 1.1981 -0.3717 0.0920 -0.0848 63 VAL B CA 7656 C C . VAL B 63 ? 1.5881 0.5991 1.2425 -0.3726 0.1075 -0.1181 63 VAL B C 7657 O O . VAL B 63 ? 1.8303 0.7995 1.4972 -0.3852 0.1100 -0.1262 63 VAL B O 7658 C CB . VAL B 63 ? 1.5324 0.5908 1.2246 -0.3597 0.0895 -0.0552 63 VAL B CB 7659 C CG1 . VAL B 63 ? 1.5302 0.5709 1.2440 -0.3333 0.0990 -0.0566 63 VAL B CG1 7660 C CG2 . VAL B 63 ? 1.6331 0.7401 1.3246 -0.3595 0.0815 -0.0261 63 VAL B CG2 7661 N N . LEU B 64 ? 1.6192 0.6322 1.2581 -0.3603 0.1206 -0.1388 64 LEU B N 7662 C CA . LEU B 64 ? 1.7722 0.7368 1.4102 -0.3605 0.1427 -0.1741 64 LEU B CA 7663 C C . LEU B 64 ? 1.7333 0.6748 1.4269 -0.3341 0.1539 -0.1673 64 LEU B C 7664 O O . LEU B 64 ? 1.8684 0.7750 1.5925 -0.3325 0.1650 -0.1830 64 LEU B O 7665 C CB . LEU B 64 ? 1.6256 0.6004 1.2250 -0.3604 0.1547 -0.1992 64 LEU B CB 7666 C CG . LEU B 64 ? 1.7239 0.7074 1.2654 -0.3927 0.1429 -0.2109 64 LEU B CG 7667 C CD1 . LEU B 64 ? 1.7882 0.7852 1.2921 -0.3910 0.1534 -0.2309 64 LEU B CD1 7668 C CD2 . LEU B 64 ? 1.7039 0.6628 1.2375 -0.4145 0.1420 -0.2281 64 LEU B CD2 7669 N N . GLU B 65 ? 1.5800 0.5558 1.2950 -0.3097 0.1468 -0.1406 65 GLU B N 7670 C CA . GLU B 65 ? 1.6666 0.6255 1.4375 -0.2861 0.1491 -0.1254 65 GLU B CA 7671 C C . GLU B 65 ? 1.6285 0.6213 1.4108 -0.2766 0.1276 -0.0816 65 GLU B C 7672 O O . GLU B 65 ? 1.5756 0.6118 1.3350 -0.2696 0.1220 -0.0703 65 GLU B O 7673 C CB . GLU B 65 ? 1.6644 0.6197 1.4530 -0.2647 0.1689 -0.1462 65 GLU B CB 7674 C CG . GLU B 65 ? 1.8826 0.8276 1.7375 -0.2389 0.1666 -0.1260 65 GLU B CG 7675 C CD . GLU B 65 ? 2.1034 1.0530 1.9804 -0.2175 0.1853 -0.1443 65 GLU B CD 7676 O OE1 . GLU B 65 ? 2.0557 0.9906 1.9983 -0.1971 0.1862 -0.1335 65 GLU B OE1 7677 O OE2 . GLU B 65 ? 2.2902 1.2582 2.1222 -0.2221 0.1980 -0.1677 65 GLU B OE2 7678 N N . ASP B 66 ? 1.7034 0.6738 1.5182 -0.2786 0.1163 -0.0573 66 ASP B N 7679 C CA . ASP B 66 ? 1.7541 0.7465 1.5792 -0.2710 0.0978 -0.0159 66 ASP B CA 7680 C C . ASP B 66 ? 1.5663 0.5224 1.4492 -0.2589 0.0904 0.0028 66 ASP B C 7681 O O . ASP B 66 ? 1.6065 0.5251 1.5146 -0.2692 0.0873 0.0070 66 ASP B O 7682 C CB . ASP B 66 ? 1.8450 0.8557 1.6420 -0.2931 0.0853 0.0065 66 ASP B CB 7683 C CG . ASP B 66 ? 1.7994 0.7715 1.6101 -0.3122 0.0832 0.0048 66 ASP B CG 7684 O OD1 . ASP B 66 ? 2.0108 0.9490 1.8322 -0.3153 0.0954 -0.0259 66 ASP B OD1 7685 O OD2 . ASP B 66 ? 1.6363 0.6102 1.4451 -0.3263 0.0710 0.0333 66 ASP B OD2 7686 N N . ARG B 67 ? 1.7259 0.6930 1.6337 -0.2378 0.0857 0.0157 67 ARG B N 7687 C CA . ARG B 67 ? 1.6925 0.6307 1.6612 -0.2265 0.0715 0.0419 67 ARG B CA 7688 C C . ARG B 67 ? 1.5969 0.5508 1.5467 -0.2364 0.0440 0.0896 67 ARG B C 7689 O O . ARG B 67 ? 1.6170 0.6106 1.5146 -0.2428 0.0413 0.0980 67 ARG B O 7690 C CB . ARG B 67 ? 1.8137 0.7536 1.8271 -0.2004 0.0788 0.0323 67 ARG B CB 7691 C CG . ARG B 67 ? 1.6699 0.5900 1.7009 -0.1930 0.1114 -0.0172 67 ARG B CG 7692 C CD . ARG B 67 ? 1.6019 0.5200 1.6923 -0.1672 0.1204 -0.0241 67 ARG B CD 7693 N NE . ARG B 67 ? 1.6749 0.6387 1.7410 -0.1567 0.1077 -0.0058 67 ARG B NE 7694 C CZ . ARG B 67 ? 1.5851 0.5795 1.6095 -0.1528 0.1242 -0.0304 67 ARG B CZ 7695 N NH1 . ARG B 67 ? 1.7223 0.7064 1.7200 -0.1605 0.1523 -0.0730 67 ARG B NH1 7696 N NH2 . ARG B 67 ? 1.4444 0.4777 1.4511 -0.1437 0.1115 -0.0118 67 ARG B NH2 7697 N N . PRO B 68 ? 1.6077 0.5284 1.5991 -0.2399 0.0244 0.1210 68 PRO B N 7698 C CA . PRO B 68 ? 1.7170 0.6481 1.6837 -0.2534 -0.0028 0.1684 68 PRO B CA 7699 C C . PRO B 68 ? 1.6537 0.6137 1.6137 -0.2402 -0.0144 0.1847 68 PRO B C 7700 O O . PRO B 68 ? 1.5713 0.5335 1.5707 -0.2172 -0.0065 0.1666 68 PRO B O 7701 C CB . PRO B 68 ? 1.6677 0.5512 1.6920 -0.2575 -0.0229 0.1972 68 PRO B CB 7702 C CG . PRO B 68 ? 1.6775 0.5316 1.7752 -0.2357 -0.0071 0.1670 68 PRO B CG 7703 C CD . PRO B 68 ? 1.6508 0.5211 1.7133 -0.2340 0.0262 0.1155 68 PRO B CD 7704 N N . LEU B 69 ? 1.5883 0.5685 1.4982 -0.2565 -0.0308 0.2169 69 LEU B N 7705 C CA . LEU B 69 ? 1.5691 0.5742 1.4661 -0.2483 -0.0437 0.2335 69 LEU B CA 7706 C C . LEU B 69 ? 1.6011 0.5778 1.5620 -0.2390 -0.0735 0.2663 69 LEU B C 7707 O O . LEU B 69 ? 2.2535 1.1918 2.2719 -0.2374 -0.0816 0.2745 69 LEU B O 7708 C CB . LEU B 69 ? 1.5705 0.6000 1.3913 -0.2731 -0.0499 0.2564 69 LEU B CB 7709 C CG . LEU B 69 ? 1.5377 0.5996 1.3060 -0.2823 -0.0217 0.2278 69 LEU B CG 7710 C CD1 . LEU B 69 ? 1.5483 0.6289 1.2511 -0.3085 -0.0236 0.2506 69 LEU B CD1 7711 C CD2 . LEU B 69 ? 1.4856 0.5785 1.2562 -0.2597 -0.0017 0.1910 69 LEU B CD2 7712 N N . SER B 70 ? 1.5911 0.5862 1.5471 -0.2334 -0.0910 0.2857 70 SER B N 7713 C CA . SER B 70 ? 1.6202 0.5924 1.6444 -0.2245 -0.1237 0.3198 70 SER B CA 7714 C C . SER B 70 ? 1.6536 0.6373 1.6329 -0.2467 -0.1572 0.3669 70 SER B C 7715 O O . SER B 70 ? 1.7535 0.7568 1.6555 -0.2642 -0.1574 0.3730 70 SER B O 7716 C CB . SER B 70 ? 1.9042 0.8953 1.9773 -0.1948 -0.1157 0.2991 70 SER B CB 7717 O OG . SER B 70 ? 1.7528 0.7416 1.8607 -0.1746 -0.0786 0.2497 70 SER B OG 7718 N N . ASP B 71 ? 1.6980 0.6722 1.7223 -0.2469 -0.1830 0.3967 71 ASP B N 7719 C CA . ASP B 71 ? 1.8751 0.8620 1.8619 -0.2680 -0.2184 0.4403 71 ASP B CA 7720 C C . ASP B 71 ? 1.8827 0.8884 1.8990 -0.2549 -0.2424 0.4547 71 ASP B C 7721 O O . ASP B 71 ? 1.9141 0.9376 1.8703 -0.2746 -0.2631 0.4779 71 ASP B O 7722 C CB . ASP B 71 ? 2.0726 1.0409 2.0949 -0.2760 -0.2410 0.4684 71 ASP B CB 7723 C CG . ASP B 71 ? 2.3061 1.2565 2.4394 -0.2462 -0.2404 0.4581 71 ASP B CG 7724 O OD1 . ASP B 71 ? 2.3357 1.2809 2.5071 -0.2232 -0.2095 0.4186 71 ASP B OD1 7725 O OD2 . ASP B 71 ? 2.2710 1.2130 2.4532 -0.2472 -0.2698 0.4880 71 ASP B OD2 7726 N N . LYS B 72 ? 1.8584 0.8609 1.9672 -0.2228 -0.2373 0.4381 72 LYS B N 7727 C CA . LYS B 72 ? 1.9256 0.9478 2.0805 -0.2074 -0.2592 0.4502 72 LYS B CA 7728 C C . LYS B 72 ? 1.9044 0.9325 2.1016 -0.1782 -0.2276 0.4094 72 LYS B C 7729 O O . LYS B 72 ? 1.7928 0.8062 1.9972 -0.1683 -0.1910 0.3715 72 LYS B O 7730 C CB . LYS B 72 ? 1.9301 0.9485 2.1775 -0.1976 -0.2921 0.4785 72 LYS B CB 7731 C CG . LYS B 72 ? 2.0818 1.0933 2.2936 -0.2273 -0.3279 0.5212 72 LYS B CG 7732 C CD . LYS B 72 ? 2.2383 1.2688 2.3561 -0.2578 -0.3541 0.5486 72 LYS B CD 7733 C CE . LYS B 72 ? 2.2697 1.3234 2.4283 -0.2484 -0.3838 0.5645 72 LYS B CE 7734 N NZ . LYS B 72 ? 2.2440 1.3136 2.3043 -0.2813 -0.4081 0.5876 72 LYS B NZ 7735 N N . GLY B 73 ? 1.9056 0.9556 2.1294 -0.1666 -0.2424 0.4168 73 GLY B N 7736 C CA . GLY B 73 ? 1.5731 0.6323 1.8367 -0.1400 -0.2134 0.3798 73 GLY B CA 7737 C C . GLY B 73 ? 1.7358 0.7999 2.1212 -0.1094 -0.2122 0.3714 73 GLY B C 7738 O O . GLY B 73 ? 1.7056 0.7852 2.1307 -0.0884 -0.1951 0.3481 73 GLY B O 7739 N N . SER B 74 ? 1.7898 0.8426 2.2370 -0.1076 -0.2290 0.3894 74 SER B N 7740 C CA . SER B 74 ? 1.8939 0.9540 2.4644 -0.0808 -0.2290 0.3837 74 SER B CA 7741 C C . SER B 74 ? 2.0730 1.1204 2.6895 -0.0575 -0.1754 0.3282 74 SER B C 7742 O O . SER B 74 ? 2.1426 1.1749 2.6946 -0.0629 -0.1419 0.2955 74 SER B O 7743 C CB . SER B 74 ? 2.0864 1.1387 2.7105 -0.0884 -0.2655 0.4220 74 SER B CB 7744 O OG . SER B 74 ? 2.2825 1.3498 2.8698 -0.1114 -0.3172 0.4722 74 SER B OG 7745 N N . GLY B 75 ? 2.0959 1.1513 2.8241 -0.0343 -0.1673 0.3170 75 GLY B N 7746 C CA . GLY B 75 ? 2.0302 1.0788 2.8024 -0.0138 -0.1141 0.2616 75 GLY B CA 7747 C C . GLY B 75 ? 2.0017 1.0196 2.7953 -0.0142 -0.0908 0.2397 75 GLY B C 7748 O O . GLY B 75 ? 2.1615 1.1670 2.9434 -0.0080 -0.0441 0.1897 75 GLY B O 7749 N N . ASP B 76 ? 1.7740 0.7796 2.5960 -0.0234 -0.1235 0.2763 76 ASP B N 7750 C CA . ASP B 76 ? 1.8960 0.8725 2.7523 -0.0226 -0.1038 0.2582 76 ASP B CA 7751 C C . ASP B 76 ? 1.9464 0.8933 2.7011 -0.0417 -0.0837 0.2379 76 ASP B C 7752 O O . ASP B 76 ? 1.7760 0.6967 2.5450 -0.0424 -0.0602 0.2132 76 ASP B O 7753 C CB . ASP B 76 ? 2.1413 1.1148 3.0651 -0.0269 -0.1470 0.3056 76 ASP B CB 7754 C CG . ASP B 76 ? 2.2056 1.1997 3.2688 -0.0043 -0.1495 0.3074 76 ASP B CG 7755 O OD1 . ASP B 76 ? 1.8217 0.8041 2.9638 -0.0013 -0.1580 0.3188 76 ASP B OD1 7756 O OD2 . ASP B 76 ? 2.0258 1.0487 3.1241 0.0099 -0.1421 0.2975 76 ASP B OD2 7757 N N . SER B 77 ? 2.1850 1.1371 2.8405 -0.0586 -0.0931 0.2486 77 SER B N 7758 C CA . SER B 77 ? 2.2770 1.2083 2.8424 -0.0761 -0.0693 0.2237 77 SER B CA 7759 C C . SER B 77 ? 2.3607 1.2882 2.9324 -0.0629 -0.0187 0.1629 77 SER B C 7760 O O . SER B 77 ? 2.3912 1.3398 3.0068 -0.0438 -0.0039 0.1447 77 SER B O 7761 C CB . SER B 77 ? 2.0594 1.0039 2.5285 -0.0960 -0.0865 0.2456 77 SER B CB 7762 O OG . SER B 77 ? 1.7831 0.7555 2.2552 -0.0841 -0.0873 0.2432 77 SER B OG 7763 N N . SER B 78 ? 2.3453 1.2481 2.8728 -0.0752 0.0071 0.1318 78 SER B N 7764 C CA . SER B 78 ? 2.2213 1.1201 2.7431 -0.0684 0.0540 0.0730 78 SER B CA 7765 C C . SER B 78 ? 1.9919 0.9181 2.4794 -0.0621 0.0682 0.0557 78 SER B C 7766 O O . SER B 78 ? 2.0201 0.9615 2.5507 -0.0444 0.0930 0.0273 78 SER B O 7767 C CB . SER B 78 ? 2.1151 0.9876 2.5717 -0.0899 0.0710 0.0486 78 SER B CB 7768 O OG . SER B 78 ? 2.1485 1.0189 2.5928 -0.0875 0.1135 -0.0073 78 SER B OG 7769 N N . GLN B 79 ? 1.5754 0.5089 1.9874 -0.0780 0.0536 0.0736 79 GLN B N 7770 C CA . GLN B 79 ? 1.6384 0.5997 2.0225 -0.0730 0.0543 0.0744 79 GLN B CA 7771 C C . GLN B 79 ? 1.7576 0.7255 2.0887 -0.0913 0.0170 0.1218 79 GLN B C 7772 O O . GLN B 79 ? 2.0525 1.0037 2.3668 -0.1080 -0.0047 0.1493 79 GLN B O 7773 C CB . GLN B 79 ? 1.8157 0.7820 2.1430 -0.0768 0.0957 0.0240 79 GLN B CB 7774 C CG . GLN B 79 ? 2.0374 1.0086 2.4054 -0.0604 0.1324 -0.0224 79 GLN B CG 7775 C CD . GLN B 79 ? 2.1211 1.1158 2.5636 -0.0365 0.1269 -0.0118 79 GLN B CD 7776 O OE1 . GLN B 79 ? 2.1937 1.2085 2.6286 -0.0327 0.1063 0.0144 79 GLN B OE1 7777 N NE2 . GLN B 79 ? 1.9149 0.9082 2.4326 -0.0219 0.1461 -0.0319 79 GLN B NE2 7778 N N . VAL B 80 ? 1.4785 0.4873 1.7638 -0.0887 0.0100 0.1280 80 VAL B N 7779 C CA . VAL B 80 ? 1.6159 0.6483 1.8243 -0.1079 -0.0198 0.1639 80 VAL B CA 7780 C C . VAL B 80 ? 1.8266 0.8808 1.9393 -0.1226 0.0022 0.1376 80 VAL B C 7781 O O . VAL B 80 ? 1.9196 0.9989 2.0037 -0.1148 0.0273 0.1044 80 VAL B O 7782 C CB . VAL B 80 ? 1.6791 0.7419 1.8876 -0.1007 -0.0418 0.1874 80 VAL B CB 7783 C CG1 . VAL B 80 ? 1.8802 0.9707 1.9890 -0.1227 -0.0572 0.2077 80 VAL B CG1 7784 C CG2 . VAL B 80 ? 1.5667 0.6080 1.8645 -0.0941 -0.0782 0.2294 80 VAL B CG2 7785 N N . THR B 81 ? 1.4667 0.5111 1.5349 -0.1448 -0.0080 0.1542 81 THR B N 7786 C CA . THR B 81 ? 1.4466 0.5122 1.4354 -0.1604 0.0097 0.1342 81 THR B CA 7787 C C . THR B 81 ? 1.4412 0.5315 1.3637 -0.1795 -0.0089 0.1651 81 THR B C 7788 O O . THR B 81 ? 1.4754 0.5486 1.3857 -0.1984 -0.0292 0.1976 81 THR B O 7789 C CB . THR B 81 ? 1.8210 0.8567 1.8104 -0.1734 0.0206 0.1209 81 THR B CB 7790 O OG1 . THR B 81 ? 1.7936 0.8026 1.8386 -0.1589 0.0429 0.0871 81 THR B OG1 7791 C CG2 . THR B 81 ? 1.8278 0.8879 1.7449 -0.1899 0.0358 0.1027 81 THR B CG2 7792 N N . GLN B 82 ? 1.4707 0.5992 1.3496 -0.1764 0.0002 0.1540 82 GLN B N 7793 C CA . GLN B 82 ? 1.4699 0.6223 1.2832 -0.1956 -0.0089 0.1752 82 GLN B CA 7794 C C . GLN B 82 ? 1.3840 0.5568 1.1461 -0.2088 0.0137 0.1537 82 GLN B C 7795 O O . GLN B 82 ? 1.3792 0.5711 1.0906 -0.2263 0.0139 0.1659 82 GLN B O 7796 C CB . GLN B 82 ? 1.3798 0.5603 1.1812 -0.1858 -0.0145 0.1795 82 GLN B CB 7797 C CG . GLN B 82 ? 1.4878 0.6518 1.3308 -0.1812 -0.0462 0.2134 82 GLN B CG 7798 C CD . GLN B 82 ? 1.5871 0.7793 1.4122 -0.1757 -0.0538 0.2190 82 GLN B CD 7799 O OE1 . GLN B 82 ? 1.8613 1.0484 1.6753 -0.1883 -0.0836 0.2547 82 GLN B OE1 7800 N NE2 . GLN B 82 ? 1.5482 0.7683 1.3678 -0.1593 -0.0287 0.1847 82 GLN B NE2 7801 N N . VAL B 83 ? 1.3774 0.5447 1.1550 -0.2023 0.0330 0.1217 83 VAL B N 7802 C CA . VAL B 83 ? 1.3606 0.5483 1.1000 -0.2142 0.0507 0.1018 83 VAL B CA 7803 C C . VAL B 83 ? 1.3793 0.5399 1.1349 -0.2222 0.0578 0.0864 83 VAL B C 7804 O O . VAL B 83 ? 1.3880 0.5261 1.1775 -0.2105 0.0653 0.0652 83 VAL B O 7805 C CB . VAL B 83 ? 1.3726 0.5927 1.0981 -0.2011 0.0675 0.0729 83 VAL B CB 7806 C CG1 . VAL B 83 ? 1.4177 0.6527 1.1189 -0.2131 0.0815 0.0523 83 VAL B CG1 7807 C CG2 . VAL B 83 ? 1.3052 0.5562 1.0056 -0.1979 0.0635 0.0859 83 VAL B CG2 7808 N N . SER B 84 ? 1.4477 0.6097 1.1791 -0.2437 0.0577 0.0954 84 SER B N 7809 C CA . SER B 84 ? 1.5155 0.6543 1.2575 -0.2547 0.0634 0.0808 84 SER B CA 7810 C C . SER B 84 ? 1.4915 0.6577 1.2015 -0.2725 0.0721 0.0736 84 SER B C 7811 O O . SER B 84 ? 1.4815 0.6716 1.1675 -0.2835 0.0718 0.0916 84 SER B O 7812 C CB . SER B 84 ? 1.4549 0.5547 1.2205 -0.2650 0.0490 0.1059 84 SER B CB 7813 O OG . SER B 84 ? 1.4788 0.5550 1.2540 -0.2772 0.0548 0.0913 84 SER B OG 7814 N N . PRO B 85 ? 1.5338 0.6953 1.2450 -0.2777 0.0802 0.0472 85 PRO B N 7815 C CA . PRO B 85 ? 1.5337 0.6651 1.2639 -0.2694 0.0867 0.0196 85 PRO B CA 7816 C C . PRO B 85 ? 1.3862 0.5325 1.1138 -0.2499 0.0961 -0.0010 85 PRO B C 7817 O O . PRO B 85 ? 1.3589 0.5379 1.0739 -0.2404 0.0948 0.0087 85 PRO B O 7818 C CB . PRO B 85 ? 1.4255 0.5545 1.1407 -0.2899 0.0902 0.0017 85 PRO B CB 7819 C CG . PRO B 85 ? 1.3931 0.5668 1.0861 -0.2995 0.0884 0.0129 85 PRO B CG 7820 C CD . PRO B 85 ? 1.3865 0.5707 1.0800 -0.2971 0.0837 0.0439 85 PRO B CD 7821 N N . GLN B 86 ? 1.4060 0.5263 1.1436 -0.2462 0.1079 -0.0307 86 GLN B N 7822 C CA . GLN B 86 ? 1.3887 0.5179 1.1240 -0.2302 0.1205 -0.0529 86 GLN B CA 7823 C C . GLN B 86 ? 1.4588 0.5981 1.1557 -0.2435 0.1294 -0.0808 86 GLN B C 7824 O O . GLN B 86 ? 1.7676 0.9425 1.4409 -0.2401 0.1293 -0.0821 86 GLN B O 7825 C CB . GLN B 86 ? 1.4502 0.5399 1.2299 -0.2159 0.1315 -0.0668 86 GLN B CB 7826 C CG . GLN B 86 ? 1.4457 0.5291 1.2703 -0.2002 0.1180 -0.0360 86 GLN B CG 7827 C CD . GLN B 86 ? 1.5198 0.5769 1.3631 -0.2121 0.1031 -0.0116 86 GLN B CD 7828 O OE1 . GLN B 86 ? 1.4876 0.5049 1.3569 -0.2177 0.1101 -0.0251 86 GLN B OE1 7829 N NE2 . GLN B 86 ? 1.4806 0.5574 1.3087 -0.2182 0.0842 0.0237 86 GLN B NE2 7830 N N . ARG B 87 ? 1.4299 0.5356 1.1200 -0.2607 0.1357 -0.1024 87 ARG B N 7831 C CA . ARG B 87 ? 1.5048 0.6141 1.1523 -0.2798 0.1395 -0.1266 87 ARG B CA 7832 C C . ARG B 87 ? 1.4919 0.6082 1.1226 -0.3053 0.1239 -0.1165 87 ARG B C 7833 O O . ARG B 87 ? 1.4774 0.5692 1.1260 -0.3144 0.1196 -0.1088 87 ARG B O 7834 C CB . ARG B 87 ? 1.6747 0.7381 1.3169 -0.2862 0.1606 -0.1640 87 ARG B CB 7835 C CG . ARG B 87 ? 1.7449 0.7978 1.4174 -0.2612 0.1799 -0.1761 87 ARG B CG 7836 C CD . ARG B 87 ? 1.8635 0.8764 1.5201 -0.2719 0.2074 -0.2191 87 ARG B CD 7837 N NE . ARG B 87 ? 2.0155 1.0427 1.6080 -0.2926 0.2077 -0.2359 87 ARG B NE 7838 C CZ . ARG B 87 ? 2.0358 1.0921 1.6091 -0.2833 0.2116 -0.2383 87 ARG B CZ 7839 N NH1 . ARG B 87 ? 1.6630 0.7384 1.2764 -0.2535 0.2167 -0.2267 87 ARG B NH1 7840 N NH2 . ARG B 87 ? 2.2194 1.2852 1.7341 -0.3057 0.2080 -0.2503 87 ARG B NH2 7841 N N . ILE B 88 ? 1.6297 0.7799 1.2317 -0.3169 0.1144 -0.1149 88 ILE B N 7842 C CA . ILE B 88 ? 1.6900 0.8512 1.2839 -0.3420 0.0981 -0.1051 88 ILE B CA 7843 C C . ILE B 88 ? 1.6309 0.7949 1.1858 -0.3648 0.0908 -0.1229 88 ILE B C 7844 O O . ILE B 88 ? 1.4337 0.6243 0.9718 -0.3591 0.0897 -0.1248 88 ILE B O 7845 C CB . ILE B 88 ? 1.6685 0.8766 1.2814 -0.3366 0.0880 -0.0738 88 ILE B CB 7846 C CG1 . ILE B 88 ? 1.7712 0.9720 1.4119 -0.3230 0.0918 -0.0531 88 ILE B CG1 7847 C CG2 . ILE B 88 ? 1.3980 0.6216 1.0124 -0.3626 0.0725 -0.0648 88 ILE B CG2 7848 C CD1 . ILE B 88 ? 1.7971 1.0375 1.4498 -0.3228 0.0876 -0.0257 88 ILE B CD1 7849 N N . ALA B 89 ? 1.6920 0.8267 1.2309 -0.3929 0.0838 -0.1344 89 ALA B N 7850 C CA . ALA B 89 ? 1.6868 0.8204 1.1834 -0.4219 0.0707 -0.1475 89 ALA B CA 7851 C C . ALA B 89 ? 1.7154 0.8917 1.2276 -0.4362 0.0442 -0.1207 89 ALA B C 7852 O O . ALA B 89 ? 1.9463 1.1226 1.4843 -0.4468 0.0352 -0.1068 89 ALA B O 7853 C CB . ALA B 89 ? 1.8532 0.9308 1.3202 -0.4494 0.0758 -0.1752 89 ALA B CB 7854 N N . LEU B 90 ? 1.6024 0.8150 1.1049 -0.4367 0.0325 -0.1129 90 LEU B N 7855 C CA . LEU B 90 ? 1.6414 0.8987 1.1729 -0.4473 0.0087 -0.0865 90 LEU B CA 7856 C C . LEU B 90 ? 1.4951 0.7502 0.9938 -0.4821 -0.0183 -0.0896 90 LEU B C 7857 O O . LEU B 90 ? 1.5089 0.7597 0.9669 -0.4869 -0.0203 -0.1012 90 LEU B O 7858 C CB . LEU B 90 ? 1.6934 0.9990 1.2545 -0.4197 0.0139 -0.0689 90 LEU B CB 7859 C CG . LEU B 90 ? 1.6115 0.9665 1.2184 -0.4254 -0.0037 -0.0421 90 LEU B CG 7860 C CD1 . LEU B 90 ? 1.5278 0.8869 1.1758 -0.4311 -0.0025 -0.0274 90 LEU B CD1 7861 C CD2 . LEU B 90 ? 1.4875 0.8828 1.1168 -0.3987 0.0064 -0.0315 90 LEU B CD2 7862 N N . ARG B 91 ? 1.5169 0.7740 1.0327 -0.5086 -0.0406 -0.0777 91 ARG B N 7863 C CA . ARG B 91 ? 1.5585 0.8148 1.0477 -0.5463 -0.0737 -0.0746 91 ARG B CA 7864 C C . ARG B 91 ? 1.6716 0.9809 1.2248 -0.5513 -0.1000 -0.0406 91 ARG B C 7865 O O . ARG B 91 ? 1.6526 0.9766 1.2581 -0.5475 -0.0974 -0.0265 91 ARG B O 7866 C CB . ARG B 91 ? 1.9064 1.1107 1.3559 -0.5810 -0.0803 -0.0936 91 ARG B CB 7867 C CG . ARG B 91 ? 2.1097 1.2594 1.5173 -0.5724 -0.0466 -0.1282 91 ARG B CG 7868 C CD . ARG B 91 ? 2.2778 1.3868 1.6490 -0.6009 -0.0503 -0.1485 91 ARG B CD 7869 N NE . ARG B 91 ? 2.4101 1.5150 1.7206 -0.6267 -0.0660 -0.1585 91 ARG B NE 7870 C CZ . ARG B 91 ? 2.4691 1.5886 1.7695 -0.6589 -0.1034 -0.1423 91 ARG B CZ 7871 N NH1 . ARG B 91 ? 2.3665 1.5087 1.7214 -0.6675 -0.1271 -0.1171 91 ARG B NH1 7872 N NH2 . ARG B 91 ? 2.5268 1.6385 1.7643 -0.6833 -0.1167 -0.1495 91 ARG B NH2 7873 N N . LEU B 92 ? 1.7340 1.0714 1.2875 -0.5607 -0.1243 -0.0271 92 LEU B N 7874 C CA . LEU B 92 ? 1.5949 0.9864 1.2237 -0.5611 -0.1466 0.0056 92 LEU B CA 7875 C C . LEU B 92 ? 1.8052 1.2043 1.4281 -0.5996 -0.1935 0.0219 92 LEU B C 7876 O O . LEU B 92 ? 1.9764 1.3595 1.5399 -0.6143 -0.2074 0.0147 92 LEU B O 7877 C CB . LEU B 92 ? 1.4067 0.8394 1.0726 -0.5245 -0.1283 0.0151 92 LEU B CB 7878 C CG . LEU B 92 ? 1.3692 0.8101 1.0642 -0.4891 -0.0893 0.0115 92 LEU B CG 7879 C CD1 . LEU B 92 ? 1.5034 0.9753 1.2137 -0.4579 -0.0724 0.0151 92 LEU B CD1 7880 C CD2 . LEU B 92 ? 1.3491 0.8138 1.1135 -0.4926 -0.0884 0.0299 92 LEU B CD2 7881 N N . ARG B 93 ? 1.5728 0.9957 1.2582 -0.6178 -0.2188 0.0453 93 ARG B N 7882 C CA . ARG B 93 ? 1.6064 1.0490 1.3122 -0.6514 -0.2690 0.0707 93 ARG B CA 7883 C C . ARG B 93 ? 2.0346 1.5361 1.8228 -0.6272 -0.2726 0.0973 93 ARG B C 7884 O O . ARG B 93 ? 2.1303 1.6582 1.9710 -0.5913 -0.2372 0.0973 93 ARG B O 7885 C CB . ARG B 93 ? 1.7745 1.2160 1.5183 -0.6833 -0.2961 0.0845 93 ARG B CB 7886 C CG . ARG B 93 ? 1.8926 1.3742 1.7395 -0.6625 -0.2785 0.1011 93 ARG B CG 7887 C CD . ARG B 93 ? 1.6676 1.1474 1.5485 -0.6937 -0.3049 0.1130 93 ARG B CD 7888 N NE . ARG B 93 ? 1.5832 1.0878 1.4829 -0.7161 -0.3550 0.1364 93 ARG B NE 7889 C CZ . ARG B 93 ? 1.8721 1.3771 1.7831 -0.7398 -0.3841 0.1458 93 ARG B CZ 7890 N NH1 . ARG B 93 ? 2.0179 1.5007 1.9251 -0.7440 -0.3668 0.1321 93 ARG B NH1 7891 N NH2 . ARG B 93 ? 2.0424 1.5687 1.9678 -0.7599 -0.4319 0.1707 93 ARG B NH2 7892 N N . PRO B 94 ? 2.1081 1.6275 1.9059 -0.6486 -0.3151 0.1199 94 PRO B N 7893 C CA . PRO B 94 ? 1.9538 1.5245 1.8277 -0.6257 -0.3188 0.1435 94 PRO B CA 7894 C C . PRO B 94 ? 1.7111 1.3307 1.7064 -0.6023 -0.3007 0.1607 94 PRO B C 7895 O O . PRO B 94 ? 1.6559 1.2831 1.7020 -0.6195 -0.3130 0.1720 94 PRO B O 7896 C CB . PRO B 94 ? 1.9837 1.5606 1.8586 -0.6650 -0.3797 0.1716 94 PRO B CB 7897 C CG . PRO B 94 ? 2.0289 1.5471 1.7825 -0.7018 -0.3950 0.1507 94 PRO B CG 7898 C CD . PRO B 94 ? 1.9857 1.4739 1.7180 -0.6982 -0.3629 0.1245 94 PRO B CD 7899 N N . ASP B 95 ? 1.4977 1.1481 1.5360 -0.5653 -0.2696 0.1609 95 ASP B N 7900 C CA . ASP B 95 ? 1.4869 1.1824 1.6362 -0.5427 -0.2440 0.1730 95 ASP B CA 7901 C C . ASP B 95 ? 1.6273 1.3106 1.7815 -0.5377 -0.2105 0.1592 95 ASP B C 7902 O O . ASP B 95 ? 1.9086 1.6215 2.1531 -0.5398 -0.2045 0.1734 95 ASP B O 7903 C CB . ASP B 95 ? 1.6515 1.3888 1.9101 -0.5616 -0.2845 0.2087 95 ASP B CB 7904 C CG . ASP B 95 ? 1.8490 1.6058 2.1252 -0.5618 -0.3148 0.2279 95 ASP B CG 7905 O OD1 . ASP B 95 ? 1.6946 1.4526 1.9425 -0.5340 -0.2878 0.2151 95 ASP B OD1 7906 O OD2 . ASP B 95 ? 2.0358 1.8064 2.3556 -0.5911 -0.3680 0.2577 95 ASP B OD2 7907 N N . ASP B 96 ? 1.5189 1.1581 1.5803 -0.5316 -0.1878 0.1323 96 ASP B N 7908 C CA . ASP B 96 ? 1.5122 1.1344 1.5704 -0.5275 -0.1579 0.1205 96 ASP B CA 7909 C C . ASP B 96 ? 1.6309 1.2347 1.6382 -0.4959 -0.1135 0.0984 96 ASP B C 7910 O O . ASP B 96 ? 1.6004 1.1930 1.5548 -0.4817 -0.1091 0.0867 96 ASP B O 7911 C CB . ASP B 96 ? 1.4045 0.9841 1.4084 -0.5595 -0.1815 0.1128 96 ASP B CB 7912 C CG . ASP B 96 ? 1.7166 1.2837 1.7375 -0.5608 -0.1584 0.1082 96 ASP B CG 7913 O OD1 . ASP B 96 ? 1.7288 1.3268 1.8163 -0.5443 -0.1307 0.1167 96 ASP B OD1 7914 O OD2 . ASP B 96 ? 2.1359 1.6604 2.1027 -0.5803 -0.1665 0.0954 96 ASP B OD2 7915 N N . SER B 97 ? 1.5951 1.1954 1.6191 -0.4871 -0.0823 0.0946 97 SER B N 7916 C CA . SER B 97 ? 1.6012 1.1851 1.5833 -0.4603 -0.0440 0.0788 97 SER B CA 7917 C C . SER B 97 ? 1.5828 1.1333 1.5396 -0.4652 -0.0274 0.0713 97 SER B C 7918 O O . SER B 97 ? 1.7734 1.3316 1.7752 -0.4810 -0.0277 0.0820 97 SER B O 7919 C CB . SER B 97 ? 1.7457 1.3696 1.7835 -0.4385 -0.0148 0.0860 97 SER B CB 7920 O OG . SER B 97 ? 1.8736 1.5241 1.9886 -0.4487 -0.0048 0.0998 97 SER B OG 7921 N N . LYS B 98 ? 1.4140 0.9272 1.3040 -0.4518 -0.0134 0.0542 98 LYS B N 7922 C CA . LYS B 98 ? 1.5788 1.0592 1.4474 -0.4520 0.0040 0.0493 98 LYS B CA 7923 C C . LYS B 98 ? 1.5719 1.0504 1.4210 -0.4252 0.0341 0.0460 98 LYS B C 7924 O O . LYS B 98 ? 1.2607 0.7438 1.0855 -0.4068 0.0379 0.0382 98 LYS B O 7925 C CB . LYS B 98 ? 1.6550 1.0851 1.4676 -0.4649 -0.0103 0.0328 98 LYS B CB 7926 C CG . LYS B 98 ? 1.7292 1.1547 1.5466 -0.4965 -0.0432 0.0345 98 LYS B CG 7927 C CD . LYS B 98 ? 1.6777 1.1217 1.5555 -0.5155 -0.0489 0.0524 98 LYS B CD 7928 C CE . LYS B 98 ? 1.6685 1.0787 1.5352 -0.5178 -0.0315 0.0490 98 LYS B CE 7929 N NZ . LYS B 98 ? 1.6391 1.0658 1.5634 -0.5388 -0.0361 0.0657 98 LYS B NZ 7930 N N . ASN B 99 ? 1.8206 1.2915 1.6784 -0.4257 0.0540 0.0532 99 ASN B N 7931 C CA . ASN B 99 ? 1.6969 1.1647 1.5335 -0.4059 0.0790 0.0538 99 ASN B CA 7932 C C . ASN B 99 ? 1.3945 0.8155 1.1891 -0.4030 0.0822 0.0502 99 ASN B C 7933 O O . ASN B 99 ? 1.4981 0.8962 1.2972 -0.4191 0.0789 0.0549 99 ASN B O 7934 C CB . ASN B 99 ? 1.8917 1.3898 1.7689 -0.4100 0.1030 0.0672 99 ASN B CB 7935 C CG . ASN B 99 ? 2.0624 1.5562 1.9706 -0.4337 0.1043 0.0776 99 ASN B CG 7936 O OD1 . ASN B 99 ? 2.0661 1.5755 2.0159 -0.4492 0.0881 0.0811 99 ASN B OD1 7937 N ND2 . ASN B 99 ? 2.4604 1.9325 2.3491 -0.4385 0.1219 0.0846 99 ASN B ND2 7938 N N . PHE B 100 ? 1.2745 0.6817 1.0345 -0.3823 0.0878 0.0430 100 PHE B N 7939 C CA . PHE B 100 ? 1.2984 0.6627 1.0293 -0.3764 0.0895 0.0416 100 PHE B CA 7940 C C . PHE B 100 ? 1.3092 0.6765 1.0271 -0.3635 0.1050 0.0533 100 PHE B C 7941 O O . PHE B 100 ? 1.3543 0.7551 1.0809 -0.3603 0.1177 0.0587 100 PHE B O 7942 C CB . PHE B 100 ? 1.3121 0.6495 1.0169 -0.3662 0.0798 0.0217 100 PHE B CB 7943 C CG . PHE B 100 ? 1.3139 0.6736 1.0068 -0.3476 0.0823 0.0127 100 PHE B CG 7944 C CD1 . PHE B 100 ? 1.5493 0.9037 1.2272 -0.3265 0.0918 0.0132 100 PHE B CD1 7945 C CD2 . PHE B 100 ? 1.5226 0.9075 1.2207 -0.3529 0.0726 0.0060 100 PHE B CD2 7946 C CE1 . PHE B 100 ? 1.5822 0.9568 1.2505 -0.3101 0.0945 0.0049 100 PHE B CE1 7947 C CE2 . PHE B 100 ? 1.5226 0.9266 1.2098 -0.3369 0.0746 -0.0010 100 PHE B CE2 7948 C CZ . PHE B 100 ? 1.3506 0.7495 1.0226 -0.3150 0.0870 -0.0026 100 PHE B CZ 7949 N N . SER B 101 ? 1.4302 0.7609 1.1290 -0.3579 0.1031 0.0575 101 SER B N 7950 C CA . SER B 101 ? 1.3485 0.6765 1.0303 -0.3510 0.1117 0.0727 101 SER B CA 7951 C C . SER B 101 ? 1.3891 0.6911 1.0557 -0.3311 0.1042 0.0689 101 SER B C 7952 O O . SER B 101 ? 1.6092 0.8848 1.2807 -0.3255 0.0960 0.0552 101 SER B O 7953 C CB . SER B 101 ? 1.5208 0.8303 1.2016 -0.3710 0.1151 0.0933 101 SER B CB 7954 O OG . SER B 101 ? 1.6873 0.9882 1.3429 -0.3693 0.1192 0.1103 101 SER B OG 7955 N N . ILE B 102 ? 1.3093 0.6180 0.9596 -0.3221 0.1083 0.0801 102 ILE B N 7956 C CA . ILE B 102 ? 1.4388 0.7262 1.0833 -0.3035 0.0997 0.0807 102 ILE B CA 7957 C C . ILE B 102 ? 1.3627 0.6401 0.9886 -0.3086 0.0963 0.1068 102 ILE B C 7958 O O . ILE B 102 ? 1.3296 0.6295 0.9352 -0.3187 0.1070 0.1158 102 ILE B O 7959 C CB . ILE B 102 ? 1.3743 0.6856 1.0163 -0.2832 0.1033 0.0623 102 ILE B CB 7960 C CG1 . ILE B 102 ? 1.4901 0.7831 1.1330 -0.2642 0.0961 0.0648 102 ILE B CG1 7961 C CG2 . ILE B 102 ? 1.4143 0.7664 1.0461 -0.2854 0.1154 0.0644 102 ILE B CG2 7962 C CD1 . ILE B 102 ? 1.6112 0.9278 1.2507 -0.2454 0.1010 0.0486 102 ILE B CD1 7963 N N . GLN B 103 ? 1.4266 0.6683 1.0606 -0.3038 0.0813 0.1194 103 GLN B N 7964 C CA . GLN B 103 ? 1.3923 0.6202 1.0076 -0.3107 0.0706 0.1483 103 GLN B CA 7965 C C . GLN B 103 ? 1.3779 0.6065 0.9987 -0.2889 0.0607 0.1484 103 GLN B C 7966 O O . GLN B 103 ? 1.3659 0.5846 1.0179 -0.2688 0.0576 0.1321 103 GLN B O 7967 C CB . GLN B 103 ? 1.4419 0.6283 1.0691 -0.3239 0.0554 0.1706 103 GLN B CB 7968 C CG . GLN B 103 ? 1.8027 0.9870 1.4134 -0.3524 0.0634 0.1823 103 GLN B CG 7969 C CD . GLN B 103 ? 2.0432 1.2390 1.6740 -0.3550 0.0759 0.1585 103 GLN B CD 7970 O OE1 . GLN B 103 ? 2.1802 1.3766 1.8328 -0.3383 0.0757 0.1344 103 GLN B OE1 7971 N NE2 . GLN B 103 ? 1.9861 1.1899 1.6084 -0.3789 0.0868 0.1656 103 GLN B NE2 7972 N N . VAL B 104 ? 1.3831 0.6223 0.9731 -0.2952 0.0574 0.1657 104 VAL B N 7973 C CA . VAL B 104 ? 1.3797 0.6212 0.9747 -0.2775 0.0453 0.1696 104 VAL B CA 7974 C C . VAL B 104 ? 1.4180 0.6378 0.9914 -0.2934 0.0229 0.2063 104 VAL B C 7975 O O . VAL B 104 ? 1.4443 0.6667 0.9709 -0.3192 0.0271 0.2219 104 VAL B O 7976 C CB . VAL B 104 ? 1.3290 0.6099 0.9043 -0.2685 0.0616 0.1509 104 VAL B CB 7977 C CG1 . VAL B 104 ? 1.3410 0.6235 0.9197 -0.2534 0.0477 0.1579 104 VAL B CG1 7978 C CG2 . VAL B 104 ? 1.3131 0.6136 0.9098 -0.2540 0.0777 0.1186 104 VAL B CG2 7979 N N . ARG B 105 ? 1.6426 0.8396 1.2517 -0.2798 -0.0009 0.2205 105 ARG B N 7980 C CA . ARG B 105 ? 1.6978 0.8720 1.2931 -0.2953 -0.0304 0.2602 105 ARG B CA 7981 C C . ARG B 105 ? 1.5641 0.7421 1.1886 -0.2750 -0.0489 0.2659 105 ARG B C 7982 O O . ARG B 105 ? 1.5001 0.6777 1.1819 -0.2473 -0.0463 0.2474 105 ARG B O 7983 C CB . ARG B 105 ? 1.5269 0.6604 1.1513 -0.3053 -0.0499 0.2847 105 ARG B CB 7984 C CG . ARG B 105 ? 1.5813 0.6866 1.2044 -0.3201 -0.0884 0.3306 105 ARG B CG 7985 C CD . ARG B 105 ? 1.7387 0.8029 1.4078 -0.3244 -0.1083 0.3531 105 ARG B CD 7986 N NE . ARG B 105 ? 1.8032 0.8577 1.4388 -0.3486 -0.0938 0.3535 105 ARG B NE 7987 C CZ . ARG B 105 ? 1.6717 0.6985 1.3460 -0.3506 -0.1001 0.3609 105 ARG B CZ 7988 N NH1 . ARG B 105 ? 1.6792 0.6838 1.4294 -0.3292 -0.1183 0.3671 105 ARG B NH1 7989 N NH2 . ARG B 105 ? 1.6877 0.7160 1.3332 -0.3711 -0.0847 0.3586 105 ARG B NH2 7990 N N . GLN B 106 ? 1.4920 0.6723 1.0761 -0.2911 -0.0665 0.2909 106 GLN B N 7991 C CA . GLN B 106 ? 1.5743 0.7555 1.1896 -0.2759 -0.0908 0.3036 106 GLN B CA 7992 C C . GLN B 106 ? 1.6253 0.7686 1.2758 -0.2849 -0.1314 0.3464 106 GLN B C 7993 O O . GLN B 106 ? 1.5989 0.7235 1.2009 -0.3174 -0.1535 0.3819 106 GLN B O 7994 C CB . GLN B 106 ? 1.6474 0.8502 1.2012 -0.2900 -0.0912 0.3078 106 GLN B CB 7995 C CG . GLN B 106 ? 1.6944 0.9356 1.2305 -0.2758 -0.0546 0.2670 106 GLN B CG 7996 C CD . GLN B 106 ? 1.8419 1.0992 1.3056 -0.2986 -0.0467 0.2692 106 GLN B CD 7997 O OE1 . GLN B 106 ? 2.0757 1.3159 1.4828 -0.3329 -0.0541 0.2927 106 GLN B OE1 7998 N NE2 . GLN B 106 ? 1.5244 0.8123 0.9876 -0.2818 -0.0298 0.2439 106 GLN B NE2 7999 N N . VAL B 107 ? 1.5313 0.6618 1.2679 -0.2577 -0.1404 0.3432 107 VAL B N 8000 C CA . VAL B 107 ? 1.6387 0.7316 1.4288 -0.2625 -0.1775 0.3825 107 VAL B CA 8001 C C . VAL B 107 ? 1.7834 0.8741 1.5805 -0.2700 -0.2192 0.4216 107 VAL B C 8002 O O . VAL B 107 ? 1.7435 0.8587 1.5412 -0.2575 -0.2176 0.4109 107 VAL B O 8003 C CB . VAL B 107 ? 1.7085 0.7865 1.5985 -0.2305 -0.1682 0.3624 107 VAL B CB 8004 C CG1 . VAL B 107 ? 1.8648 0.9421 1.7424 -0.2279 -0.1310 0.3254 107 VAL B CG1 8005 C CG2 . VAL B 107 ? 1.6532 0.7536 1.5957 -0.1990 -0.1583 0.3382 107 VAL B CG2 8006 N N . GLU B 108 ? 1.6632 0.7497 1.4694 -0.2844 -0.2506 0.4558 108 GLU B N 8007 C CA . GLU B 108 ? 1.8224 0.9211 1.6431 -0.2899 -0.2921 0.4885 108 GLU B CA 8008 C C . GLU B 108 ? 1.9151 1.0137 1.8544 -0.2550 -0.3060 0.4892 108 GLU B C 8009 O O . GLU B 108 ? 1.8875 0.9716 1.8978 -0.2305 -0.2857 0.4684 108 GLU B O 8010 C CB . GLU B 108 ? 1.7652 0.8571 1.5568 -0.3195 -0.3233 0.5244 108 GLU B CB 8011 C CG . GLU B 108 ? 1.7908 0.8842 1.4709 -0.3550 -0.3048 0.5208 108 GLU B CG 8012 C CD . GLU B 108 ? 2.3629 1.4471 2.0131 -0.3860 -0.3354 0.5550 108 GLU B CD 8013 O OE1 . GLU B 108 ? 2.5669 1.6474 2.2721 -0.3841 -0.3781 0.5861 108 GLU B OE1 8014 O OE2 . GLU B 108 ? 2.2467 1.3283 1.8216 -0.4131 -0.3167 0.5506 108 GLU B OE2 8015 N N . ASP B 109 ? 1.9590 1.0748 1.9200 -0.2541 -0.3381 0.5103 109 ASP B N 8016 C CA . ASP B 109 ? 1.8475 0.9704 1.9268 -0.2222 -0.3517 0.5119 109 ASP B CA 8017 C C . ASP B 109 ? 1.7370 0.8597 1.8620 -0.1891 -0.3093 0.4681 109 ASP B C 8018 O O . ASP B 109 ? 1.7655 0.8827 1.9911 -0.1603 -0.2972 0.4524 109 ASP B O 8019 C CB . ASP B 109 ? 1.7063 0.8158 1.8708 -0.2150 -0.3717 0.5310 109 ASP B CB 8020 C CG . ASP B 109 ? 1.9208 1.0454 2.2016 -0.1931 -0.3997 0.5459 109 ASP B CG 8021 O OD1 . ASP B 109 ? 1.6753 0.8196 1.9796 -0.1787 -0.3973 0.5359 109 ASP B OD1 8022 O OD2 . ASP B 109 ? 2.0997 1.2178 2.4528 -0.1908 -0.4238 0.5677 109 ASP B OD2 8023 N N . TYR B 110 ? 1.5682 0.6968 1.6174 -0.1952 -0.2851 0.4464 110 TYR B N 8024 C CA . TYR B 110 ? 1.6447 0.7813 1.7246 -0.1666 -0.2441 0.4008 110 TYR B CA 8025 C C . TYR B 110 ? 1.6648 0.8235 1.7997 -0.1472 -0.2545 0.4010 110 TYR B C 8026 O O . TYR B 110 ? 1.5920 0.7654 1.6779 -0.1640 -0.2791 0.4227 110 TYR B O 8027 C CB . TYR B 110 ? 1.4933 0.6542 1.4695 -0.1759 -0.2051 0.3646 110 TYR B CB 8028 C CG . TYR B 110 ? 1.4214 0.5989 1.4187 -0.1485 -0.1560 0.3096 110 TYR B CG 8029 C CD1 . TYR B 110 ? 1.4230 0.5787 1.4676 -0.1369 -0.1358 0.2896 110 TYR B CD1 8030 C CD2 . TYR B 110 ? 1.7226 0.9351 1.6878 -0.1377 -0.1308 0.2782 110 TYR B CD2 8031 C CE1 . TYR B 110 ? 1.3856 0.5526 1.4390 -0.1178 -0.0928 0.2402 110 TYR B CE1 8032 C CE2 . TYR B 110 ? 1.7518 0.9769 1.7294 -0.1173 -0.0893 0.2312 110 TYR B CE2 8033 C CZ . TYR B 110 ? 1.6828 0.8844 1.7011 -0.1089 -0.0709 0.2125 110 TYR B CZ 8034 O OH . TYR B 110 ? 1.8519 1.0622 1.8731 -0.0941 -0.0315 0.1665 110 TYR B OH 8035 N N . PRO B 111 ? 1.5984 0.7582 1.8352 -0.1138 -0.2338 0.3755 111 PRO B N 8036 C CA . PRO B 111 ? 1.5587 0.7388 1.8665 -0.0929 -0.2402 0.3741 111 PRO B CA 8037 C C . PRO B 111 ? 1.4850 0.7028 1.7153 -0.0947 -0.2231 0.3515 111 PRO B C 8038 O O . PRO B 111 ? 1.4165 0.6487 1.5755 -0.0950 -0.1842 0.3137 111 PRO B O 8039 C CB . PRO B 111 ? 1.4081 0.5806 1.8156 -0.0600 -0.2007 0.3347 111 PRO B CB 8040 C CG . PRO B 111 ? 1.4046 0.5634 1.7583 -0.0648 -0.1649 0.3028 111 PRO B CG 8041 C CD . PRO B 111 ? 1.5185 0.6597 1.8044 -0.0961 -0.1977 0.3418 111 PRO B CD 8042 N N . VAL B 112 ? 1.5250 0.7581 1.7736 -0.0969 -0.2541 0.3763 112 VAL B N 8043 C CA . VAL B 112 ? 1.3661 0.6321 1.5412 -0.1020 -0.2436 0.3603 112 VAL B CA 8044 C C . VAL B 112 ? 1.3401 0.6297 1.5941 -0.0751 -0.2349 0.3445 112 VAL B C 8045 O O . VAL B 112 ? 1.3778 0.6611 1.7305 -0.0660 -0.2655 0.3722 112 VAL B O 8046 C CB . VAL B 112 ? 1.4108 0.6741 1.5059 -0.1388 -0.2885 0.4036 112 VAL B CB 8047 C CG1 . VAL B 112 ? 1.8268 1.1219 1.8543 -0.1436 -0.2764 0.3855 112 VAL B CG1 8048 C CG2 . VAL B 112 ? 1.4490 0.6900 1.4566 -0.1688 -0.2907 0.4159 112 VAL B CG2 8049 N N . ASP B 113 ? 1.3218 0.6385 1.5368 -0.0629 -0.1934 0.3011 113 ASP B N 8050 C CA . ASP B 113 ? 1.2696 0.6116 1.5409 -0.0418 -0.1830 0.2853 113 ASP B CA 8051 C C . ASP B 113 ? 1.4256 0.7929 1.6175 -0.0581 -0.1959 0.2917 113 ASP B C 8052 O O . ASP B 113 ? 1.5987 0.9742 1.6890 -0.0729 -0.1783 0.2759 113 ASP B O 8053 C CB . ASP B 113 ? 1.2104 0.5618 1.5026 -0.0168 -0.1257 0.2309 113 ASP B CB 8054 C CG . ASP B 113 ? 1.3032 0.6278 1.6862 0.0001 -0.1087 0.2195 113 ASP B CG 8055 O OD1 . ASP B 113 ? 1.2102 0.5315 1.5820 0.0102 -0.0630 0.1765 113 ASP B OD1 8056 O OD2 . ASP B 113 ? 1.6464 0.9517 2.1127 0.0016 -0.1417 0.2539 113 ASP B OD2 8057 N N . ILE B 114 ? 1.4662 0.8452 1.7094 -0.0561 -0.2264 0.3149 114 ILE B N 8058 C CA . ILE B 114 ? 1.3536 0.7542 1.5268 -0.0725 -0.2399 0.3209 114 ILE B CA 8059 C C . ILE B 114 ? 1.2663 0.6941 1.5060 -0.0498 -0.2287 0.3044 114 ILE B C 8060 O O . ILE B 114 ? 1.3052 0.7326 1.6509 -0.0377 -0.2524 0.3253 114 ILE B O 8061 C CB . ILE B 114 ? 1.3752 0.7608 1.5175 -0.1061 -0.3005 0.3752 114 ILE B CB 8062 C CG1 . ILE B 114 ? 1.5384 0.8973 1.5972 -0.1341 -0.3082 0.3904 114 ILE B CG1 8063 C CG2 . ILE B 114 ? 1.3004 0.7062 1.3765 -0.1238 -0.3130 0.3782 114 ILE B CG2 8064 C CD1 . ILE B 114 ? 1.4809 0.8204 1.4877 -0.1745 -0.3653 0.4427 114 ILE B CD1 8065 N N . TYR B 115 ? 1.1938 0.6454 1.3763 -0.0445 -0.1924 0.2678 115 TYR B N 8066 C CA . TYR B 115 ? 1.1656 0.6438 1.3982 -0.0261 -0.1794 0.2509 115 TYR B CA 8067 C C . TYR B 115 ? 1.2783 0.7744 1.4341 -0.0461 -0.1960 0.2588 115 TYR B C 8068 O O . TYR B 115 ? 1.4520 0.9525 1.5083 -0.0595 -0.1768 0.2412 115 TYR B O 8069 C CB . TYR B 115 ? 1.1486 0.6380 1.3894 -0.0020 -0.1209 0.1999 115 TYR B CB 8070 C CG . TYR B 115 ? 1.1650 0.6775 1.4739 0.0185 -0.1031 0.1817 115 TYR B CG 8071 C CD1 . TYR B 115 ? 1.4460 0.9545 1.8791 0.0383 -0.1030 0.1855 115 TYR B CD1 8072 C CD2 . TYR B 115 ? 1.1376 0.6752 1.3919 0.0178 -0.0845 0.1605 115 TYR B CD2 8073 C CE1 . TYR B 115 ? 1.4083 0.9380 1.9066 0.0558 -0.0831 0.1678 115 TYR B CE1 8074 C CE2 . TYR B 115 ? 1.1191 0.6772 1.4341 0.0349 -0.0674 0.1445 115 TYR B CE2 8075 C CZ . TYR B 115 ? 1.3127 0.8671 1.7483 0.0534 -0.0659 0.1478 115 TYR B CZ 8076 O OH . TYR B 115 ? 1.2972 0.8721 1.7961 0.0692 -0.0454 0.1308 115 TYR B OH 8077 N N . TYR B 116 ? 1.2072 0.7125 1.4145 -0.0489 -0.2316 0.2851 116 TYR B N 8078 C CA . TYR B 116 ? 1.2417 0.7600 1.3797 -0.0714 -0.2525 0.2956 116 TYR B CA 8079 C C . TYR B 116 ? 1.3757 0.9240 1.5218 -0.0532 -0.2180 0.2606 116 TYR B C 8080 O O . TYR B 116 ? 1.5478 1.1094 1.7908 -0.0279 -0.2060 0.2506 116 TYR B O 8081 C CB . TYR B 116 ? 1.3534 0.8645 1.5358 -0.0897 -0.3158 0.3466 116 TYR B CB 8082 C CG . TYR B 116 ? 1.5126 1.0071 1.5854 -0.1336 -0.3542 0.3767 116 TYR B CG 8083 C CD1 . TYR B 116 ? 1.5605 1.0247 1.6133 -0.1577 -0.3914 0.4146 116 TYR B CD1 8084 C CD2 . TYR B 116 ? 1.5605 1.0669 1.5481 -0.1534 -0.3516 0.3664 116 TYR B CD2 8085 C CE1 . TYR B 116 ? 1.6175 1.0628 1.5615 -0.2027 -0.4237 0.4409 116 TYR B CE1 8086 C CE2 . TYR B 116 ? 1.6703 1.1574 1.5521 -0.1974 -0.3818 0.3900 116 TYR B CE2 8087 C CZ . TYR B 116 ? 1.7048 1.1609 1.5619 -0.2232 -0.4173 0.4271 116 TYR B CZ 8088 O OH . TYR B 116 ? 1.6257 1.0591 1.3691 -0.2718 -0.4447 0.4496 116 TYR B OH 8089 N N . LEU B 117 ? 1.4498 1.0076 1.4969 -0.0670 -0.2003 0.2415 117 LEU B N 8090 C CA . LEU B 117 ? 1.2302 0.8149 1.2770 -0.0546 -0.1739 0.2135 117 LEU B CA 8091 C C . LEU B 117 ? 1.2624 0.8535 1.2693 -0.0791 -0.2077 0.2339 117 LEU B C 8092 O O . LEU B 117 ? 1.2762 0.8579 1.1845 -0.1071 -0.2139 0.2372 117 LEU B O 8093 C CB . LEU B 117 ? 1.2125 0.8044 1.1894 -0.0490 -0.1249 0.1735 117 LEU B CB 8094 C CG . LEU B 117 ? 1.3665 0.9589 1.3874 -0.0223 -0.0844 0.1441 117 LEU B CG 8095 C CD1 . LEU B 117 ? 1.2800 0.8815 1.2310 -0.0208 -0.0440 0.1099 117 LEU B CD1 8096 C CD2 . LEU B 117 ? 1.3727 0.9787 1.4938 0.0021 -0.0744 0.1354 117 LEU B CD2 8097 N N . MET B 118 ? 1.3596 0.9657 1.4452 -0.0701 -0.2275 0.2461 118 MET B N 8098 C CA . MET B 118 ? 1.3204 0.9305 1.3805 -0.0953 -0.2678 0.2707 118 MET B CA 8099 C C . MET B 118 ? 1.2580 0.8930 1.2996 -0.0887 -0.2414 0.2420 118 MET B C 8100 O O . MET B 118 ? 1.2215 0.8760 1.3247 -0.0593 -0.2072 0.2160 118 MET B O 8101 C CB . MET B 118 ? 1.2208 0.8305 1.3870 -0.0943 -0.3177 0.3114 118 MET B CB 8102 C CG . MET B 118 ? 1.4158 1.0003 1.6180 -0.0985 -0.3464 0.3430 118 MET B CG 8103 S SD . MET B 118 ? 1.7698 1.3572 2.1310 -0.0884 -0.3985 0.3879 118 MET B SD 8104 C CE . MET B 118 ? 1.7359 1.2888 2.1147 -0.0949 -0.4228 0.4187 118 MET B CE 8105 N N . ASP B 119 ? 1.2694 0.9011 1.2237 -0.1184 -0.2561 0.2464 119 ASP B N 8106 C CA . ASP B 119 ? 1.2711 0.9236 1.2080 -0.1161 -0.2374 0.2236 119 ASP B CA 8107 C C . ASP B 119 ? 1.2755 0.9379 1.2730 -0.1242 -0.2816 0.2518 119 ASP B C 8108 O O . ASP B 119 ? 1.2977 0.9446 1.2573 -0.1579 -0.3293 0.2844 119 ASP B O 8109 C CB . ASP B 119 ? 1.3617 1.0039 1.1755 -0.1441 -0.2238 0.2084 119 ASP B CB 8110 C CG . ASP B 119 ? 1.5054 1.1671 1.3025 -0.1411 -0.2015 0.1830 119 ASP B CG 8111 O OD1 . ASP B 119 ? 1.4537 1.1056 1.1636 -0.1693 -0.2010 0.1768 119 ASP B OD1 8112 O OD2 . ASP B 119 ? 1.7820 1.4668 1.6527 -0.1121 -0.1826 0.1684 119 ASP B OD2 8113 N N . LEU B 120 ? 1.3240 1.0111 1.4162 -0.0954 -0.2663 0.2403 120 LEU B N 8114 C CA . LEU B 120 ? 1.4252 1.1255 1.5965 -0.0990 -0.3066 0.2672 120 LEU B CA 8115 C C . LEU B 120 ? 1.2755 0.9920 1.4119 -0.1093 -0.3022 0.2533 120 LEU B C 8116 O O . LEU B 120 ? 1.2912 1.0225 1.4953 -0.1109 -0.3309 0.2712 120 LEU B O 8117 C CB . LEU B 120 ? 1.4367 1.1536 1.7489 -0.0633 -0.2940 0.2658 120 LEU B CB 8118 C CG . LEU B 120 ? 1.1982 0.8975 1.5703 -0.0559 -0.3111 0.2886 120 LEU B CG 8119 C CD1 . LEU B 120 ? 1.3497 1.0644 1.8786 -0.0278 -0.3115 0.2962 120 LEU B CD1 8120 C CD2 . LEU B 120 ? 1.1990 0.8741 1.5232 -0.0924 -0.3731 0.3344 120 LEU B CD2 8121 N N . SER B 121 ? 1.2842 0.9979 1.3223 -0.1158 -0.2661 0.2218 121 SER B N 8122 C CA . SER B 121 ? 1.3059 1.0308 1.3033 -0.1273 -0.2592 0.2066 121 SER B CA 8123 C C . SER B 121 ? 1.3427 1.0535 1.2952 -0.1688 -0.3145 0.2385 121 SER B C 8124 O O . SER B 121 ? 1.4096 1.0967 1.3258 -0.1942 -0.3512 0.2675 121 SER B O 8125 C CB . SER B 121 ? 1.3070 1.0279 1.2118 -0.1277 -0.2111 0.1691 121 SER B CB 8126 O OG . SER B 121 ? 1.3203 1.0145 1.1347 -0.1530 -0.2169 0.1744 121 SER B OG 8127 N N . TYR B 122 ? 1.3587 1.0822 1.3103 -0.1781 -0.3212 0.2338 122 TYR B N 8128 C CA . TYR B 122 ? 1.3937 1.1061 1.3167 -0.2181 -0.3778 0.2654 122 TYR B CA 8129 C C . TYR B 122 ? 1.4281 1.1051 1.2176 -0.2635 -0.3937 0.2721 122 TYR B C 8130 O O . TYR B 122 ? 1.6200 1.2785 1.3801 -0.3020 -0.4496 0.3080 122 TYR B O 8131 C CB . TYR B 122 ? 1.5547 1.2857 1.4887 -0.2199 -0.3722 0.2507 122 TYR B CB 8132 C CG . TYR B 122 ? 1.7045 1.4312 1.6478 -0.2549 -0.4364 0.2878 122 TYR B CG 8133 C CD1 . TYR B 122 ? 1.5824 1.3294 1.6523 -0.2420 -0.4744 0.3193 122 TYR B CD1 8134 C CD2 . TYR B 122 ? 1.7252 1.4263 1.5527 -0.3030 -0.4587 0.2912 122 TYR B CD2 8135 C CE1 . TYR B 122 ? 1.4535 1.1975 1.5375 -0.2756 -0.5383 0.3568 122 TYR B CE1 8136 C CE2 . TYR B 122 ? 1.7372 1.4318 1.5666 -0.3396 -0.5212 0.3265 122 TYR B CE2 8137 C CZ . TYR B 122 ? 1.6148 1.3320 1.5742 -0.3255 -0.5635 0.3611 122 TYR B CZ 8138 O OH . TYR B 122 ? 1.8756 1.5875 1.8426 -0.3634 -0.6307 0.3998 122 TYR B OH 8139 N N . SER B 123 ? 1.4099 1.0767 1.1199 -0.2612 -0.3448 0.2382 123 SER B N 8140 C CA . SER B 123 ? 1.4630 1.0955 1.0472 -0.3034 -0.3484 0.2384 123 SER B CA 8141 C C . SER B 123 ? 1.5702 1.1800 1.1462 -0.3212 -0.3884 0.2763 123 SER B C 8142 O O . SER B 123 ? 1.4419 1.0196 0.9191 -0.3669 -0.4110 0.2908 123 SER B O 8143 C CB . SER B 123 ? 1.4548 1.0853 0.9805 -0.2907 -0.2840 0.1945 123 SER B CB 8144 O OG . SER B 123 ? 1.4027 1.0454 0.9857 -0.2522 -0.2570 0.1866 123 SER B OG 8145 N N . MET B 124 ? 1.5981 1.2225 1.2777 -0.2868 -0.3952 0.2915 124 MET B N 8146 C CA . MET B 124 ? 1.6226 1.2268 1.3114 -0.2973 -0.4302 0.3271 124 MET B CA 8147 C C . MET B 124 ? 1.7554 1.3577 1.5111 -0.3141 -0.5022 0.3791 124 MET B C 8148 O O . MET B 124 ? 1.8807 1.4671 1.6618 -0.3222 -0.5390 0.4152 124 MET B O 8149 C CB . MET B 124 ? 1.4823 1.0990 1.2460 -0.2520 -0.3948 0.3131 124 MET B CB 8150 C CG . MET B 124 ? 1.4409 1.0527 1.1335 -0.2424 -0.3353 0.2726 124 MET B CG 8151 S SD . MET B 124 ? 1.7438 1.3174 1.3394 -0.2764 -0.3452 0.2888 124 MET B SD 8152 C CE . MET B 124 ? 1.6411 1.2136 1.3480 -0.2527 -0.3767 0.3240 124 MET B CE 8153 N N . LYS B 125 ? 1.7007 1.3194 1.4906 -0.3195 -0.5236 0.3844 125 LYS B N 8154 C CA . LYS B 125 ? 1.6071 1.2262 1.4654 -0.3383 -0.5961 0.4356 125 LYS B CA 8155 C C . LYS B 125 ? 1.6682 1.2475 1.4257 -0.3967 -0.6525 0.4756 125 LYS B C 8156 O O . LYS B 125 ? 1.5900 1.1607 1.4034 -0.4111 -0.7154 0.5270 125 LYS B O 8157 C CB . LYS B 125 ? 1.5005 1.1418 1.3911 -0.3410 -0.6062 0.4302 125 LYS B CB 8158 C CG . LYS B 125 ? 1.7684 1.4166 1.7514 -0.3561 -0.6809 0.4830 125 LYS B CG 8159 C CD . LYS B 125 ? 1.8559 1.5247 1.8592 -0.3625 -0.6887 0.4750 125 LYS B CD 8160 C CE . LYS B 125 ? 1.7301 1.4094 1.8398 -0.3761 -0.7646 0.5290 125 LYS B CE 8161 N NZ . LYS B 125 ? 1.6870 1.3949 1.9724 -0.3269 -0.7613 0.5415 125 LYS B NZ 8162 N N . ASP B 126 ? 1.8670 1.4206 1.4769 -0.4316 -0.6282 0.4517 126 ASP B N 8163 C CA . ASP B 126 ? 1.7559 1.2666 1.2449 -0.4930 -0.6704 0.4817 126 ASP B CA 8164 C C . ASP B 126 ? 1.7788 1.2689 1.2533 -0.4918 -0.6693 0.4970 126 ASP B C 8165 O O . ASP B 126 ? 1.9529 1.4214 1.3952 -0.5314 -0.7064 0.5238 126 ASP B O 8166 C CB . ASP B 126 ? 1.7977 1.2869 1.1373 -0.5303 -0.6339 0.4437 126 ASP B CB 8167 C CG . ASP B 126 ? 2.3440 1.8447 1.6613 -0.4946 -0.5494 0.3861 126 ASP B CG 8168 O OD1 . ASP B 126 ? 2.4008 1.9345 1.8240 -0.4381 -0.5170 0.3685 126 ASP B OD1 8169 O OD2 . ASP B 126 ? 2.5126 1.9881 1.7080 -0.5249 -0.5149 0.3586 126 ASP B OD2 8170 N N . ASP B 127 ? 1.6152 1.1227 1.1350 -0.4432 -0.6103 0.4627 127 ASP B N 8171 C CA . ASP B 127 ? 1.7547 1.2430 1.2513 -0.4406 -0.5976 0.4679 127 ASP B CA 8172 C C . ASP B 127 ? 1.7484 1.2468 1.3797 -0.4076 -0.6264 0.5012 127 ASP B C 8173 O O . ASP B 127 ? 1.7218 1.2064 1.3514 -0.3997 -0.6151 0.5051 127 ASP B O 8174 C CB . ASP B 127 ? 1.8571 1.3545 1.3156 -0.4120 -0.5170 0.4112 127 ASP B CB 8175 C CG . ASP B 127 ? 1.9459 1.4348 1.2886 -0.4395 -0.4818 0.3746 127 ASP B CG 8176 O OD1 . ASP B 127 ? 1.8304 1.3452 1.2043 -0.4163 -0.4529 0.3441 127 ASP B OD1 8177 O OD2 . ASP B 127 ? 2.1997 1.6546 1.4214 -0.4857 -0.4812 0.3758 127 ASP B OD2 8178 N N . LEU B 128 ? 1.7918 1.3136 1.5445 -0.3887 -0.6615 0.5240 128 LEU B N 8179 C CA . LEU B 128 ? 1.7569 1.2901 1.6568 -0.3543 -0.6839 0.5520 128 LEU B CA 8180 C C . LEU B 128 ? 1.7930 1.3044 1.6971 -0.3882 -0.7441 0.6009 128 LEU B C 8181 O O . LEU B 128 ? 1.6019 1.1236 1.6261 -0.3632 -0.7583 0.6192 128 LEU B O 8182 C CB . LEU B 128 ? 1.8288 1.3968 1.8656 -0.3261 -0.6988 0.5581 128 LEU B CB 8183 C CG . LEU B 128 ? 1.6285 1.2287 1.7854 -0.2641 -0.6408 0.5206 128 LEU B CG 8184 C CD1 . LEU B 128 ? 1.3531 0.9591 1.4255 -0.2466 -0.5638 0.4604 128 LEU B CD1 8185 C CD2 . LEU B 128 ? 1.6662 1.2993 1.9442 -0.2440 -0.6536 0.5252 128 LEU B CD2 8186 N N . TRP B 129 ? 1.9617 1.4529 1.7442 -0.4450 -0.7650 0.6055 129 TRP B N 8187 C CA . TRP B 129 ? 1.9388 1.4158 1.7167 -0.4839 -0.8108 0.6372 129 TRP B CA 8188 C C . TRP B 129 ? 1.7750 1.2399 1.5573 -0.4689 -0.7922 0.6372 129 TRP B C 8189 O O . TRP B 129 ? 1.8262 1.2912 1.6791 -0.4747 -0.8296 0.6680 129 TRP B O 8190 C CB . TRP B 129 ? 1.9620 1.4120 1.5927 -0.5496 -0.8230 0.6334 129 TRP B CB 8191 C CG . TRP B 129 ? 2.1691 1.5997 1.6603 -0.5588 -0.7634 0.5910 129 TRP B CG 8192 C CD1 . TRP B 129 ? 2.4285 1.8622 1.8544 -0.5519 -0.7198 0.5540 129 TRP B CD1 8193 C CD2 . TRP B 129 ? 2.3155 1.7225 1.7245 -0.5760 -0.7383 0.5797 129 TRP B CD2 8194 N NE1 . TRP B 129 ? 2.4222 1.8368 1.7358 -0.5636 -0.6672 0.5190 129 TRP B NE1 8195 C CE2 . TRP B 129 ? 2.3983 1.7966 1.7001 -0.5783 -0.6771 0.5340 129 TRP B CE2 8196 C CE3 . TRP B 129 ? 2.4943 1.8879 1.9145 -0.5900 -0.7610 0.6033 129 TRP B CE3 8197 C CZ2 . TRP B 129 ? 2.4285 1.8067 1.6412 -0.5932 -0.6367 0.5106 129 TRP B CZ2 8198 C CZ3 . TRP B 129 ? 2.4639 1.8360 1.7878 -0.6054 -0.7230 0.5814 129 TRP B CZ3 8199 C CH2 . TRP B 129 ? 2.4100 1.7752 1.6342 -0.6066 -0.6608 0.5352 129 TRP B CH2 8200 N N . SER B 130 ? 1.7351 1.1891 1.4444 -0.4509 -0.7344 0.6030 130 SER B N 8201 C CA . SER B 130 ? 2.1191 1.5580 1.8147 -0.4413 -0.7121 0.5993 130 SER B CA 8202 C C . SER B 130 ? 2.0477 1.5009 1.8841 -0.3838 -0.6986 0.6024 130 SER B C 8203 O O . SER B 130 ? 1.6576 1.1003 1.5124 -0.3738 -0.6896 0.6058 130 SER B O 8204 C CB . SER B 130 ? 2.0343 1.4553 1.5959 -0.4496 -0.6533 0.5598 130 SER B CB 8205 O OG . SER B 130 ? 1.7420 1.1734 1.3100 -0.4152 -0.6106 0.5313 130 SER B OG 8206 N N . ILE B 131 ? 2.1048 1.5807 2.0424 -0.3471 -0.6939 0.5984 131 ILE B N 8207 C CA . ILE B 131 ? 1.8915 1.3801 1.9691 -0.2926 -0.6716 0.5926 131 ILE B CA 8208 C C . ILE B 131 ? 1.8974 1.4045 2.1147 -0.2876 -0.7179 0.6255 131 ILE B C 8209 O O . ILE B 131 ? 1.8165 1.3318 2.1496 -0.2495 -0.7008 0.6214 131 ILE B O 8210 C CB . ILE B 131 ? 1.9408 1.4596 2.0745 -0.2529 -0.6264 0.5533 131 ILE B CB 8211 C CG1 . ILE B 131 ? 1.7799 1.3104 1.9712 -0.2045 -0.5606 0.5099 131 ILE B CG1 8212 C CG2 . ILE B 131 ? 2.0726 1.6132 2.3316 -0.2437 -0.6684 0.5812 131 ILE B CG2 8213 C CD1 . ILE B 131 ? 1.8746 1.3861 1.9517 -0.2131 -0.5206 0.4836 131 ILE B CD1 8214 N N . GLN B 132 ? 1.8256 1.3374 2.0307 -0.3294 -0.7744 0.6564 132 GLN B N 8215 C CA . GLN B 132 ? 1.6637 1.1896 1.9896 -0.3357 -0.8249 0.6925 132 GLN B CA 8216 C C . GLN B 132 ? 1.6862 1.1921 1.9930 -0.3451 -0.8296 0.7040 132 GLN B C 8217 O O . GLN B 132 ? 1.6997 1.1803 1.8795 -0.3596 -0.8032 0.6880 132 GLN B O 8218 C CB . GLN B 132 ? 1.7420 1.2701 2.0414 -0.3865 -0.8852 0.7233 132 GLN B CB 8219 C CG . GLN B 132 ? 1.8803 1.4223 2.1636 -0.3863 -0.8804 0.7103 132 GLN B CG 8220 C CD . GLN B 132 ? 1.9362 1.5123 2.3784 -0.3328 -0.8604 0.6999 132 GLN B CD 8221 O OE1 . GLN B 132 ? 1.9187 1.5006 2.3527 -0.2985 -0.8116 0.6671 132 GLN B OE1 8222 N NE2 . GLN B 132 ? 1.9162 1.5141 2.5066 -0.3275 -0.8959 0.7268 132 GLN B NE2 8223 N N . ASN B 133 ? 1.7030 1.2208 2.1373 -0.3380 -0.8613 0.7308 133 ASN B N 8224 C CA . ASN B 133 ? 1.9406 1.4414 2.3752 -0.3394 -0.8618 0.7401 133 ASN B CA 8225 C C . ASN B 133 ? 2.0292 1.5206 2.4531 -0.2954 -0.7938 0.7011 133 ASN B C 8226 O O . ASN B 133 ? 2.1766 1.6849 2.7237 -0.2485 -0.7633 0.6839 133 ASN B O 8227 C CB . ASN B 133 ? 2.0543 1.5267 2.3464 -0.3986 -0.8945 0.7599 133 ASN B CB 8228 C CG . ASN B 133 ? 2.1458 1.6217 2.4593 -0.4462 -0.9655 0.8017 133 ASN B CG 8229 O OD1 . ASN B 133 ? 1.8933 1.3883 2.2604 -0.4480 -0.9861 0.8090 133 ASN B OD1 8230 N ND2 . ASN B 133 ? 2.1985 1.6546 2.4730 -0.4866 -1.0038 0.8304 133 ASN B ND2 8231 N N . LEU B 134 ? 1.9690 1.4329 2.2503 -0.3130 -0.7685 0.6858 134 LEU B N 8232 C CA . LEU B 134 ? 1.9163 1.3666 2.1780 -0.2783 -0.7068 0.6510 134 LEU B CA 8233 C C . LEU B 134 ? 1.8561 1.3044 2.2217 -0.2533 -0.7025 0.6568 134 LEU B C 8234 O O . LEU B 134 ? 1.9702 1.4026 2.2983 -0.2792 -0.7263 0.6776 134 LEU B O 8235 C CB . LEU B 134 ? 1.5348 0.9978 1.8323 -0.2388 -0.6608 0.6169 134 LEU B CB 8236 C CG . LEU B 134 ? 1.5979 1.0401 1.8170 -0.2209 -0.5991 0.5787 134 LEU B CG 8237 C CD1 . LEU B 134 ? 1.5960 1.0155 1.6451 -0.2644 -0.5974 0.5776 134 LEU B CD1 8238 C CD2 . LEU B 134 ? 1.5296 0.9869 1.7756 -0.1903 -0.5599 0.5461 134 LEU B CD2 8239 N N . GLY B 135 ? 1.7075 1.1699 2.1980 -0.2052 -0.6688 0.6357 135 GLY B N 8240 C CA . GLY B 135 ? 1.5339 0.9895 2.1078 -0.1793 -0.6491 0.6295 135 GLY B CA 8241 C C . GLY B 135 ? 1.8225 1.2751 2.4355 -0.2029 -0.6989 0.6686 135 GLY B C 8242 O O . GLY B 135 ? 1.9442 1.3800 2.5665 -0.1951 -0.6843 0.6656 135 GLY B O 8243 N N . THR B 136 ? 1.8104 1.2779 2.4475 -0.2335 -0.7586 0.7057 136 THR B N 8244 C CA . THR B 136 ? 1.9110 1.3704 2.5531 -0.2684 -0.8130 0.7468 136 THR B CA 8245 C C . THR B 136 ? 1.9718 1.4003 2.4412 -0.3099 -0.8182 0.7516 136 THR B C 8246 O O . THR B 136 ? 1.8121 1.2218 2.2611 -0.3187 -0.8208 0.7609 136 THR B O 8247 C CB . THR B 136 ? 1.9799 1.4605 2.6867 -0.2972 -0.8783 0.7860 136 THR B CB 8248 O OG1 . THR B 136 ? 1.8507 1.3618 2.7343 -0.2606 -0.8733 0.7834 136 THR B OG1 8249 C CG2 . THR B 136 ? 1.8694 1.3363 2.5605 -0.3411 -0.9370 0.8296 136 THR B CG2 8250 N N . LYS B 137 ? 2.2172 1.6409 2.5648 -0.3363 -0.8170 0.7434 137 LYS B N 8251 C CA . LYS B 137 ? 2.3521 1.7484 2.5306 -0.3764 -0.8101 0.7386 137 LYS B CA 8252 C C . LYS B 137 ? 2.2155 1.5941 2.3437 -0.3508 -0.7484 0.7044 137 LYS B C 8253 O O . LYS B 137 ? 2.1441 1.5003 2.1781 -0.3762 -0.7424 0.7051 137 LYS B O 8254 C CB . LYS B 137 ? 2.4570 1.8541 2.5275 -0.4055 -0.8115 0.7287 137 LYS B CB 8255 C CG . LYS B 137 ? 2.5731 1.9734 2.6305 -0.4544 -0.8758 0.7638 137 LYS B CG 8256 C CD . LYS B 137 ? 2.6119 2.0079 2.5492 -0.4834 -0.8667 0.7462 137 LYS B CD 8257 C CE . LYS B 137 ? 2.6320 2.0235 2.5394 -0.5398 -0.9286 0.7787 137 LYS B CE 8258 N NZ . LYS B 137 ? 2.6246 2.0117 2.4261 -0.5658 -0.9165 0.7584 137 LYS B NZ 8259 N N . LEU B 138 ? 1.7072 1.0951 1.8988 -0.3030 -0.7020 0.6734 138 LEU B N 8260 C CA . LEU B 138 ? 1.6612 1.0314 1.8174 -0.2785 -0.6438 0.6401 138 LEU B CA 8261 C C . LEU B 138 ? 2.0301 1.3862 2.2316 -0.2730 -0.6469 0.6512 138 LEU B C 8262 O O . LEU B 138 ? 2.2126 1.5475 2.3474 -0.2739 -0.6137 0.6345 138 LEU B O 8263 C CB . LEU B 138 ? 1.5773 0.9590 1.8120 -0.2297 -0.5981 0.6062 138 LEU B CB 8264 C CG . LEU B 138 ? 1.8266 1.2128 1.9893 -0.2291 -0.5719 0.5819 138 LEU B CG 8265 C CD1 . LEU B 138 ? 1.4832 0.8781 1.7354 -0.1805 -0.5260 0.5482 138 LEU B CD1 8266 C CD2 . LEU B 138 ? 1.9299 1.2941 1.9361 -0.2566 -0.5452 0.5659 138 LEU B CD2 8267 N N . ALA B 139 ? 1.8827 1.2516 2.2020 -0.2683 -0.6870 0.6797 139 ALA B N 8268 C CA . ALA B 139 ? 1.7361 1.0928 2.1077 -0.2655 -0.6965 0.6946 139 ALA B CA 8269 C C . ALA B 139 ? 1.8601 1.1990 2.1289 -0.3168 -0.7356 0.7251 139 ALA B C 8270 O O . ALA B 139 ? 1.9226 1.2408 2.1580 -0.3221 -0.7238 0.7251 139 ALA B O 8271 C CB . ALA B 139 ? 2.0530 1.4316 2.5952 -0.2430 -0.7232 0.7129 139 ALA B CB 8272 N N . THR B 140 ? 1.9698 1.3153 2.1861 -0.3569 -0.7806 0.7492 140 THR B N 8273 C CA . THR B 140 ? 2.2463 1.5742 2.3692 -0.4111 -0.8210 0.7783 140 THR B CA 8274 C C . THR B 140 ? 2.2367 1.5409 2.2017 -0.4334 -0.7815 0.7539 140 THR B C 8275 O O . THR B 140 ? 2.2413 1.5268 2.1253 -0.4746 -0.8009 0.7703 140 THR B O 8276 C CB . THR B 140 ? 2.2672 1.6049 2.3687 -0.4533 -0.8776 0.8068 140 THR B CB 8277 O OG1 . THR B 140 ? 2.2466 1.5709 2.3319 -0.4980 -0.9318 0.8463 140 THR B OG1 8278 C CG2 . THR B 140 ? 2.1299 1.4606 2.0861 -0.4810 -0.8564 0.7835 140 THR B CG2 8279 N N . GLN B 141 ? 1.9068 1.2122 1.8327 -0.4074 -0.7251 0.7142 141 GLN B N 8280 C CA . GLN B 141 ? 2.1007 1.3875 1.8950 -0.4233 -0.6802 0.6867 141 GLN B CA 8281 C C . GLN B 141 ? 2.1446 1.4196 1.9736 -0.3899 -0.6376 0.6679 141 GLN B C 8282 O O . GLN B 141 ? 2.2150 1.4720 1.9960 -0.4085 -0.6339 0.6733 141 GLN B O 8283 C CB . GLN B 141 ? 2.1029 1.3972 1.8207 -0.4232 -0.6452 0.6547 141 GLN B CB 8284 C CG . GLN B 141 ? 2.2459 1.5600 2.0583 -0.3780 -0.6301 0.6401 141 GLN B CG 8285 C CD . GLN B 141 ? 2.2026 1.5210 1.9345 -0.3766 -0.5900 0.6065 141 GLN B CD 8286 O OE1 . GLN B 141 ? 2.1738 1.5081 1.9242 -0.3739 -0.6029 0.6068 141 GLN B OE1 8287 N NE2 . GLN B 141 ? 2.0052 1.3106 1.6522 -0.3788 -0.5410 0.5772 141 GLN B NE2 8288 N N . MET B 142 ? 1.8672 1.1511 1.7796 -0.3425 -0.6049 0.6448 142 MET B N 8289 C CA . MET B 142 ? 1.7374 1.0077 1.6762 -0.3120 -0.5587 0.6197 142 MET B CA 8290 C C . MET B 142 ? 1.9251 1.1850 1.9463 -0.3032 -0.5762 0.6394 142 MET B C 8291 O O . MET B 142 ? 1.7380 0.9824 1.7697 -0.2855 -0.5411 0.6206 142 MET B O 8292 C CB . MET B 142 ? 1.6562 0.9368 1.6694 -0.2667 -0.5219 0.5888 142 MET B CB 8293 C CG . MET B 142 ? 1.6234 0.9106 1.5541 -0.2712 -0.4948 0.5640 142 MET B CG 8294 S SD . MET B 142 ? 2.2727 1.5414 2.0648 -0.2899 -0.4440 0.5338 142 MET B SD 8295 C CE . MET B 142 ? 1.5695 0.8232 1.4428 -0.2483 -0.4022 0.5074 142 MET B CE 8296 N N . ARG B 143 ? 2.0777 1.3458 2.1588 -0.3173 -0.6311 0.6771 143 ARG B N 8297 C CA . ARG B 143 ? 1.8437 1.1034 2.0101 -0.3107 -0.6519 0.6988 143 ARG B CA 8298 C C . ARG B 143 ? 1.9419 1.1760 2.0183 -0.3361 -0.6423 0.7017 143 ARG B C 8299 O O . ARG B 143 ? 2.1089 1.3297 2.2401 -0.3199 -0.6315 0.7012 143 ARG B O 8300 C CB . ARG B 143 ? 1.9016 1.1757 2.1374 -0.3300 -0.7184 0.7426 143 ARG B CB 8301 C CG . ARG B 143 ? 2.0700 1.3379 2.4062 -0.3237 -0.7438 0.7677 143 ARG B CG 8302 C CD . ARG B 143 ? 2.1357 1.4220 2.5593 -0.3408 -0.8103 0.8108 143 ARG B CD 8303 N NE . ARG B 143 ? 2.1353 1.4500 2.6816 -0.3073 -0.8084 0.8024 143 ARG B NE 8304 C CZ . ARG B 143 ? 2.1602 1.4941 2.6917 -0.3178 -0.8262 0.8056 143 ARG B CZ 8305 N NH1 . ARG B 143 ? 2.2274 1.5533 2.6235 -0.3618 -0.8467 0.8157 143 ARG B NH1 8306 N NH2 . ARG B 143 ? 2.0769 1.4373 2.7296 -0.2857 -0.8210 0.7969 143 ARG B NH2 8307 N N . LYS B 144 ? 2.0581 1.2854 1.9980 -0.3768 -0.6433 0.7023 144 LYS B N 8308 C CA . LYS B 144 ? 2.2467 1.4520 2.0957 -0.4052 -0.6322 0.7038 144 LYS B CA 8309 C C . LYS B 144 ? 2.1600 1.3536 1.9964 -0.3788 -0.5714 0.6670 144 LYS B C 8310 O O . LYS B 144 ? 2.3191 1.4957 2.1640 -0.3787 -0.5633 0.6703 144 LYS B O 8311 C CB . LYS B 144 ? 2.3966 1.5990 2.1041 -0.4556 -0.6395 0.7054 144 LYS B CB 8312 C CG . LYS B 144 ? 2.4162 1.6287 2.0522 -0.4518 -0.5984 0.6695 144 LYS B CG 8313 C CD . LYS B 144 ? 2.5611 1.7704 2.0669 -0.5030 -0.6051 0.6683 144 LYS B CD 8314 C CE . LYS B 144 ? 2.6355 1.8553 2.1565 -0.5246 -0.6591 0.6947 144 LYS B CE 8315 N NZ . LYS B 144 ? 2.6691 1.8840 2.0616 -0.5724 -0.6564 0.6839 144 LYS B NZ 8316 N N . LEU B 145 ? 1.9209 1.1231 1.7378 -0.3584 -0.5306 0.6328 145 LEU B N 8317 C CA . LEU B 145 ? 1.9270 1.1187 1.7233 -0.3390 -0.4745 0.5968 145 LEU B CA 8318 C C . LEU B 145 ? 1.8540 1.0419 1.7700 -0.2925 -0.4542 0.5802 145 LEU B C 8319 O O . LEU B 145 ? 1.8315 1.0051 1.7428 -0.2797 -0.4151 0.5550 145 LEU B O 8320 C CB . LEU B 145 ? 1.8365 1.0379 1.5487 -0.3434 -0.4389 0.5662 145 LEU B CB 8321 C CG . LEU B 145 ? 2.0725 1.2697 1.6527 -0.3807 -0.4151 0.5538 145 LEU B CG 8322 C CD1 . LEU B 145 ? 2.2242 1.4172 1.7468 -0.4246 -0.4551 0.5844 145 LEU B CD1 8323 C CD2 . LEU B 145 ? 1.7495 0.9609 1.2660 -0.3821 -0.3837 0.5245 145 LEU B CD2 8324 N N . THR B 146 ? 1.8247 1.0255 1.8494 -0.2690 -0.4786 0.5915 146 THR B N 8325 C CA . THR B 146 ? 1.6955 0.8957 1.8319 -0.2244 -0.4499 0.5659 146 THR B CA 8326 C C . THR B 146 ? 1.9441 1.1564 2.2174 -0.2043 -0.4818 0.5860 146 THR B C 8327 O O . THR B 146 ? 2.0077 1.2377 2.3007 -0.2182 -0.5265 0.6161 146 THR B O 8328 C CB . THR B 146 ? 1.8632 1.0741 1.9881 -0.2044 -0.4145 0.5314 146 THR B CB 8329 O OG1 . THR B 146 ? 2.4081 1.6104 2.4113 -0.2242 -0.3850 0.5127 146 THR B OG1 8330 C CG2 . THR B 146 ? 1.5523 0.7598 1.7796 -0.1621 -0.3769 0.4971 146 THR B CG2 8331 N N . SER B 147 ? 1.9518 1.1551 2.3206 -0.1736 -0.4571 0.5672 147 SER B N 8332 C CA . SER B 147 ? 1.7919 1.0102 2.3058 -0.1465 -0.4697 0.5720 147 SER B CA 8333 C C . SER B 147 ? 1.8458 1.0666 2.4188 -0.1081 -0.4148 0.5229 147 SER B C 8334 O O . SER B 147 ? 1.6564 0.8612 2.1638 -0.1044 -0.3724 0.4897 147 SER B O 8335 C CB . SER B 147 ? 1.7042 0.9094 2.2852 -0.1477 -0.4887 0.5925 147 SER B CB 8336 O OG . SER B 147 ? 1.6893 0.8684 2.2592 -0.1358 -0.4448 0.5621 147 SER B OG 8337 N N . ASN B 148 ? 2.0398 1.2819 2.7363 -0.0822 -0.4151 0.5173 148 ASN B N 8338 C CA . ASN B 148 ? 2.0703 1.3201 2.8210 -0.0489 -0.3630 0.4694 148 ASN B CA 8339 C C . ASN B 148 ? 1.9457 1.2028 2.6091 -0.0529 -0.3480 0.4535 148 ASN B C 8340 O O . ASN B 148 ? 1.8054 1.0506 2.4268 -0.0422 -0.3009 0.4134 148 ASN B O 8341 C CB . ASN B 148 ? 2.0219 1.2456 2.7820 -0.0330 -0.3119 0.4291 148 ASN B CB 8342 C CG . ASN B 148 ? 1.9283 1.1613 2.7652 -0.0004 -0.2592 0.3792 148 ASN B CG 8343 O OD1 . ASN B 148 ? 1.6489 0.9067 2.5147 0.0110 -0.2537 0.3702 148 ASN B OD1 8344 N ND2 . ASN B 148 ? 1.9606 1.1735 2.8258 0.0121 -0.2185 0.3449 148 ASN B ND2 8345 N N . LEU B 149 ? 1.9065 1.1827 2.5416 -0.0711 -0.3903 0.4858 149 LEU B N 8346 C CA . LEU B 149 ? 1.6201 0.9063 2.1830 -0.0756 -0.3813 0.4745 149 LEU B CA 8347 C C . LEU B 149 ? 1.4175 0.7284 2.0778 -0.0443 -0.3586 0.4493 149 LEU B C 8348 O O . LEU B 149 ? 1.5173 0.8474 2.2959 -0.0302 -0.3726 0.4588 149 LEU B O 8349 C CB . LEU B 149 ? 1.5014 0.7966 1.9870 -0.1120 -0.4348 0.5171 149 LEU B CB 8350 C CG . LEU B 149 ? 1.4774 0.7855 1.8918 -0.1211 -0.4345 0.5118 149 LEU B CG 8351 C CD1 . LEU B 149 ? 1.7479 1.0370 2.0501 -0.1270 -0.3931 0.4822 149 LEU B CD1 8352 C CD2 . LEU B 149 ? 1.5309 0.8492 1.8879 -0.1590 -0.4910 0.5539 149 LEU B CD2 8353 N N . ARG B 150 ? 1.3710 0.6828 1.9844 -0.0350 -0.3224 0.4168 150 ARG B N 8354 C CA . ARG B 150 ? 1.3294 0.6648 2.0235 -0.0071 -0.2949 0.3887 150 ARG B CA 8355 C C . ARG B 150 ? 1.5048 0.8512 2.1289 -0.0155 -0.2991 0.3884 150 ARG B C 8356 O O . ARG B 150 ? 1.8184 1.1662 2.3270 -0.0265 -0.2748 0.3654 150 ARG B O 8357 C CB . ARG B 150 ? 1.3355 0.6601 2.0640 0.0192 -0.2303 0.3347 150 ARG B CB 8358 C CG . ARG B 150 ? 1.5206 0.8371 2.3341 0.0306 -0.2201 0.3288 150 ARG B CG 8359 C CD . ARG B 150 ? 1.7372 1.0797 2.6827 0.0565 -0.1971 0.3076 150 ARG B CD 8360 N NE . ARG B 150 ? 1.8835 1.2274 2.8257 0.0752 -0.1335 0.2513 150 ARG B NE 8361 C CZ . ARG B 150 ? 1.8754 1.2045 2.8359 0.0862 -0.0841 0.2094 150 ARG B CZ 8362 N NH1 . ARG B 150 ? 1.7460 1.0569 2.7366 0.0833 -0.0905 0.2178 150 ARG B NH1 8363 N NH2 . ARG B 150 ? 1.7863 1.1188 2.7307 0.0975 -0.0287 0.1590 150 ARG B NH2 8364 N N . ILE B 151 ? 1.4412 0.8165 2.1261 -0.0114 -0.3234 0.4038 151 ILE B N 8365 C CA . ILE B 151 ? 1.5126 0.9005 2.1364 -0.0204 -0.3309 0.4054 151 ILE B CA 8366 C C . ILE B 151 ? 1.3536 0.7693 2.0645 0.0085 -0.3000 0.3755 151 ILE B C 8367 O O . ILE B 151 ? 1.4959 0.9204 2.3173 0.0337 -0.2731 0.3549 151 ILE B O 8368 C CB . ILE B 151 ? 1.3257 0.7231 1.9135 -0.0528 -0.3964 0.4561 151 ILE B CB 8369 C CG1 . ILE B 151 ? 1.3468 0.7708 2.0679 -0.0449 -0.4299 0.4800 151 ILE B CG1 8370 C CG2 . ILE B 151 ? 1.4957 0.8684 1.9766 -0.0869 -0.4215 0.4812 151 ILE B CG2 8371 C CD1 . ILE B 151 ? 1.3985 0.8338 2.0917 -0.0799 -0.4972 0.5287 151 ILE B CD1 8372 N N . GLY B 152 ? 1.2310 0.6738 1.8796 0.0016 -0.2978 0.3657 152 GLY B N 8373 C CA . GLY B 152 ? 1.3454 0.8164 2.0562 0.0251 -0.2660 0.3356 152 GLY B CA 8374 C C . GLY B 152 ? 1.1639 0.6588 1.7600 0.0117 -0.2566 0.3187 152 GLY B C 8375 O O . GLY B 152 ? 1.1780 0.6659 1.6531 -0.0132 -0.2671 0.3249 152 GLY B O 8376 N N . PHE B 153 ? 1.2225 0.7444 1.8579 0.0272 -0.2349 0.2969 153 PHE B N 8377 C CA . PHE B 153 ? 1.2775 0.8214 1.8128 0.0149 -0.2276 0.2823 153 PHE B CA 8378 C C . PHE B 153 ? 1.2175 0.7880 1.7879 0.0372 -0.1824 0.2427 153 PHE B C 8379 O O . PHE B 153 ? 1.1965 0.7690 1.8704 0.0616 -0.1535 0.2243 153 PHE B O 8380 C CB . PHE B 153 ? 1.2288 0.7764 1.7425 -0.0122 -0.2899 0.3287 153 PHE B CB 8381 C CG . PHE B 153 ? 1.2149 0.7781 1.8546 -0.0019 -0.3188 0.3523 153 PHE B CG 8382 C CD1 . PHE B 153 ? 1.2983 0.8897 1.9414 0.0012 -0.3118 0.3397 153 PHE B CD1 8383 C CD2 . PHE B 153 ? 1.2696 0.8196 2.0306 0.0042 -0.3541 0.3884 153 PHE B CD2 8384 C CE1 . PHE B 153 ? 1.4559 1.0634 2.2204 0.0099 -0.3388 0.3622 153 PHE B CE1 8385 C CE2 . PHE B 153 ? 1.3575 0.9238 2.2464 0.0138 -0.3819 0.4119 153 PHE B CE2 8386 C CZ . PHE B 153 ? 1.5277 1.1236 2.4179 0.0164 -0.3740 0.3985 153 PHE B CZ 8387 N N . GLY B 154 ? 1.1706 0.7595 1.6526 0.0264 -0.1750 0.2293 154 GLY B N 8388 C CA . GLY B 154 ? 1.1538 0.7683 1.6523 0.0420 -0.1378 0.1962 154 GLY B CA 8389 C C . GLY B 154 ? 1.2134 0.8444 1.6315 0.0223 -0.1580 0.2042 154 GLY B C 8390 O O . GLY B 154 ? 1.1557 0.7755 1.4958 -0.0038 -0.1923 0.2287 154 GLY B O 8391 N N . ALA B 155 ? 1.1544 0.8096 1.5886 0.0324 -0.1352 0.1828 155 ALA B N 8392 C CA . ALA B 155 ? 1.1147 0.7848 1.4833 0.0142 -0.1540 0.1895 155 ALA B CA 8393 C C . ALA B 155 ? 1.1268 0.8143 1.4427 0.0223 -0.1069 0.1489 155 ALA B C 8394 O O . ALA B 155 ? 1.0781 0.7722 1.4353 0.0436 -0.0640 0.1191 155 ALA B O 8395 C CB . ALA B 155 ? 1.1830 0.8668 1.6384 0.0120 -0.1941 0.2195 155 ALA B CB 8396 N N . PHE B 156 ? 1.2278 0.9201 1.4513 0.0028 -0.1150 0.1484 156 PHE B N 8397 C CA . PHE B 156 ? 1.1562 0.8650 1.3325 0.0079 -0.0775 0.1156 156 PHE B CA 8398 C C . PHE B 156 ? 1.1881 0.9092 1.3340 -0.0093 -0.1013 0.1262 156 PHE B C 8399 O O . PHE B 156 ? 1.2010 0.9124 1.3214 -0.0327 -0.1445 0.1558 156 PHE B O 8400 C CB . PHE B 156 ? 1.1625 0.8610 1.2452 0.0026 -0.0500 0.0942 156 PHE B CB 8401 C CG . PHE B 156 ? 1.1989 0.8833 1.1953 -0.0251 -0.0757 0.1114 156 PHE B CG 8402 C CD1 . PHE B 156 ? 1.2211 0.9120 1.1488 -0.0420 -0.0756 0.1053 156 PHE B CD1 8403 C CD2 . PHE B 156 ? 1.2218 0.8841 1.2054 -0.0361 -0.0973 0.1323 156 PHE B CD2 8404 C CE1 . PHE B 156 ? 1.2265 0.9011 1.0725 -0.0706 -0.0933 0.1173 156 PHE B CE1 8405 C CE2 . PHE B 156 ? 1.3206 0.9674 1.2199 -0.0652 -0.1173 0.1469 156 PHE B CE2 8406 C CZ . PHE B 156 ? 1.2310 0.8835 1.0602 -0.0831 -0.1136 0.1381 156 PHE B CZ 8407 N N . VAL B 157 ? 1.2443 0.9847 1.3895 -0.0004 -0.0736 0.1025 157 VAL B N 8408 C CA . VAL B 157 ? 1.2027 0.9530 1.3081 -0.0173 -0.0894 0.1065 157 VAL B CA 8409 C C . VAL B 157 ? 1.2083 0.9638 1.2394 -0.0173 -0.0518 0.0756 157 VAL B C 8410 O O . VAL B 157 ? 1.2467 0.9918 1.1950 -0.0369 -0.0558 0.0746 157 VAL B O 8411 C CB . VAL B 157 ? 1.1807 0.9519 1.3732 -0.0087 -0.1000 0.1136 157 VAL B CB 8412 C CG1 . VAL B 157 ? 1.3124 1.0910 1.4578 -0.0294 -0.1186 0.1180 157 VAL B CG1 8413 C CG2 . VAL B 157 ? 1.1634 0.9312 1.4476 -0.0071 -0.1385 0.1464 157 VAL B CG2 8414 N N . ASP B 158 ? 1.1685 0.9384 1.2322 0.0033 -0.0146 0.0508 158 ASP B N 8415 C CA . ASP B 158 ? 1.1551 0.9305 1.1620 0.0055 0.0204 0.0238 158 ASP B CA 8416 C C . ASP B 158 ? 1.0937 0.8822 1.1525 0.0262 0.0548 0.0032 158 ASP B C 8417 O O . ASP B 158 ? 1.0685 0.8622 1.2064 0.0376 0.0535 0.0082 158 ASP B O 8418 C CB . ASP B 158 ? 1.1917 0.9731 1.1513 -0.0112 0.0107 0.0237 158 ASP B CB 8419 C CG . ASP B 158 ? 1.1658 0.9443 1.0534 -0.0158 0.0375 0.0030 158 ASP B CG 8420 O OD1 . ASP B 158 ? 1.1071 0.8880 0.9949 -0.0017 0.0677 -0.0144 158 ASP B OD1 8421 O OD2 . ASP B 158 ? 1.1706 0.9431 1.0031 -0.0351 0.0282 0.0044 158 ASP B OD2 8422 N N . LYS B 159 ? 1.0498 0.8422 1.0667 0.0292 0.0859 -0.0191 159 LYS B N 8423 C CA . LYS B 159 ? 0.9690 0.7702 1.0200 0.0431 0.1198 -0.0388 159 LYS B CA 8424 C C . LYS B 159 ? 1.0000 0.8191 1.1076 0.0466 0.1172 -0.0363 159 LYS B C 8425 O O . LYS B 159 ? 0.9937 0.8222 1.0778 0.0380 0.1077 -0.0337 159 LYS B O 8426 C CB . LYS B 159 ? 0.9491 0.7501 0.9389 0.0410 0.1460 -0.0575 159 LYS B CB 8427 C CG . LYS B 159 ? 1.0925 0.8778 1.0383 0.0392 0.1535 -0.0624 159 LYS B CG 8428 C CD . LYS B 159 ? 1.0499 0.8365 0.9496 0.0371 0.1770 -0.0781 159 LYS B CD 8429 C CE . LYS B 159 ? 1.0163 0.7883 0.8808 0.0347 0.1832 -0.0821 159 LYS B CE 8430 N NZ . LYS B 159 ? 1.1347 0.8943 1.0312 0.0415 0.1929 -0.0871 159 LYS B NZ 8431 N N . PRO B 160 ? 1.0072 0.8304 1.1940 0.0587 0.1279 -0.0383 160 PRO B N 8432 C CA . PRO B 160 ? 0.9243 0.7657 1.1818 0.0629 0.1263 -0.0348 160 PRO B CA 8433 C C . PRO B 160 ? 1.0892 0.9418 1.3284 0.0635 0.1579 -0.0548 160 PRO B C 8434 O O . PRO B 160 ? 1.4771 1.3356 1.7674 0.0718 0.1876 -0.0687 160 PRO B O 8435 C CB . PRO B 160 ? 0.8815 0.7201 1.2296 0.0764 0.1385 -0.0362 160 PRO B CB 8436 C CG . PRO B 160 ? 0.8916 0.7112 1.2003 0.0799 0.1668 -0.0544 160 PRO B CG 8437 C CD . PRO B 160 ? 1.0755 0.8848 1.2930 0.0686 0.1467 -0.0467 160 PRO B CD 8438 N N . VAL B 161 ? 0.9832 0.8371 1.1517 0.0535 0.1528 -0.0564 161 VAL B N 8439 C CA . VAL B 161 ? 0.8623 0.7248 1.0082 0.0523 0.1785 -0.0719 161 VAL B CA 8440 C C . VAL B 161 ? 0.8948 0.7612 0.9904 0.0406 0.1601 -0.0660 161 VAL B C 8441 O O . VAL B 161 ? 0.9122 0.7710 0.9740 0.0317 0.1342 -0.0546 161 VAL B O 8442 C CB . VAL B 161 ? 0.8232 0.6739 0.9235 0.0538 0.2111 -0.0904 161 VAL B CB 8443 C CG1 . VAL B 161 ? 0.7234 0.5653 0.7471 0.0458 0.2019 -0.0889 161 VAL B CG1 8444 C CG2 . VAL B 161 ? 1.2971 1.1549 1.4033 0.0534 0.2424 -0.1054 161 VAL B CG2 8445 N N . SER B 162 ? 0.8119 0.6883 0.9028 0.0389 0.1755 -0.0747 162 SER B N 8446 C CA . SER B 162 ? 0.8265 0.7051 0.8757 0.0281 0.1638 -0.0727 162 SER B CA 8447 C C . SER B 162 ? 0.8444 0.7099 0.8242 0.0232 0.1686 -0.0781 162 SER B C 8448 O O . SER B 162 ? 1.0840 0.9428 1.0457 0.0282 0.1874 -0.0861 162 SER B O 8449 C CB . SER B 162 ? 1.1141 1.0052 1.1812 0.0284 0.1818 -0.0806 162 SER B CB 8450 O OG . SER B 162 ? 1.1597 1.0517 1.1942 0.0182 0.1719 -0.0798 162 SER B OG 8451 N N . PRO B 163 ? 0.7925 0.6536 0.7353 0.0114 0.1527 -0.0746 163 PRO B N 8452 C CA . PRO B 163 ? 1.0545 0.9185 1.0085 0.0002 0.1260 -0.0642 163 PRO B CA 8453 C C . PRO B 163 ? 1.0186 0.8716 0.9617 -0.0087 0.0976 -0.0497 163 PRO B C 8454 O O . PRO B 163 ? 1.1562 1.0008 1.0640 -0.0266 0.0779 -0.0444 163 PRO B O 8455 C CB . PRO B 163 ? 1.2912 1.1507 1.2009 -0.0113 0.1304 -0.0724 163 PRO B CB 8456 C CG . PRO B 163 ? 0.9999 0.8488 0.8677 -0.0089 0.1469 -0.0804 163 PRO B CG 8457 C CD . PRO B 163 ? 0.7228 0.5750 0.6122 0.0060 0.1622 -0.0821 163 PRO B CD 8458 N N . TYR B 164 ? 1.0531 0.9036 1.0233 0.0010 0.0958 -0.0436 164 TYR B N 8459 C CA . TYR B 164 ? 1.1180 0.9578 1.0873 -0.0076 0.0652 -0.0255 164 TYR B CA 8460 C C . TYR B 164 ? 1.1598 1.0095 1.1958 -0.0088 0.0372 -0.0071 164 TYR B C 8461 O O . TYR B 164 ? 1.2143 1.0572 1.2402 -0.0262 0.0013 0.0117 164 TYR B O 8462 C CB . TYR B 164 ? 1.1233 0.9533 1.0920 0.0026 0.0751 -0.0265 164 TYR B CB 8463 C CG . TYR B 164 ? 1.0012 0.8241 0.9148 0.0041 0.1013 -0.0430 164 TYR B CG 8464 C CD1 . TYR B 164 ? 0.9014 0.7274 0.8264 0.0180 0.1304 -0.0569 164 TYR B CD1 8465 C CD2 . TYR B 164 ? 0.9877 0.7998 0.8393 -0.0107 0.0973 -0.0446 164 TYR B CD2 8466 C CE1 . TYR B 164 ? 0.9253 0.7455 0.8048 0.0175 0.1488 -0.0680 164 TYR B CE1 8467 C CE2 . TYR B 164 ? 0.8831 0.6909 0.6976 -0.0088 0.1201 -0.0577 164 TYR B CE2 8468 C CZ . TYR B 164 ? 0.9097 0.7223 0.7400 0.0056 0.1428 -0.0675 164 TYR B CZ 8469 O OH . TYR B 164 ? 1.0478 0.8567 0.8458 0.0057 0.1600 -0.0768 164 TYR B OH 8470 N N . MET B 165 ? 1.1038 0.9689 1.2089 0.0077 0.0543 -0.0124 165 MET B N 8471 C CA . MET B 165 ? 1.1120 0.9892 1.3034 0.0114 0.0335 0.0042 165 MET B CA 8472 C C . MET B 165 ? 1.2779 1.1707 1.4935 0.0038 0.0235 0.0069 165 MET B C 8473 O O . MET B 165 ? 1.4078 1.3063 1.5980 0.0049 0.0485 -0.0103 165 MET B O 8474 C CB . MET B 165 ? 1.0322 0.9157 1.2927 0.0327 0.0639 -0.0062 165 MET B CB 8475 C CG . MET B 165 ? 1.1112 1.0078 1.4795 0.0399 0.0486 0.0090 165 MET B CG 8476 S SD . MET B 165 ? 1.1685 1.0658 1.6121 0.0625 0.0939 -0.0097 165 MET B SD 8477 C CE . MET B 165 ? 1.3870 1.2890 1.7813 0.0645 0.1443 -0.0412 165 MET B CE 8478 N N . TYR B 166 ? 1.2554 1.1546 1.5224 -0.0051 -0.0151 0.0305 166 TYR B N 8479 C CA . TYR B 166 ? 1.1688 1.0844 1.4703 -0.0122 -0.0255 0.0339 166 TYR B CA 8480 C C . TYR B 166 ? 1.1031 1.0392 1.4976 0.0086 0.0044 0.0246 166 TYR B C 8481 O O . TYR B 166 ? 1.0689 1.0123 1.5502 0.0189 -0.0029 0.0365 166 TYR B O 8482 C CB . TYR B 166 ? 1.2018 1.1171 1.5281 -0.0324 -0.0814 0.0650 166 TYR B CB 8483 C CG . TYR B 166 ? 1.2507 1.1436 1.4775 -0.0610 -0.1108 0.0731 166 TYR B CG 8484 C CD1 . TYR B 166 ? 1.3045 1.1952 1.4920 -0.0851 -0.1306 0.0751 166 TYR B CD1 8485 C CD2 . TYR B 166 ? 1.2691 1.1410 1.4400 -0.0663 -0.1165 0.0775 166 TYR B CD2 8486 C CE1 . TYR B 166 ? 1.3150 1.1814 1.4070 -0.1151 -0.1522 0.0788 166 TYR B CE1 8487 C CE2 . TYR B 166 ? 1.3124 1.1616 1.3897 -0.0955 -0.1384 0.0828 166 TYR B CE2 8488 C CZ . TYR B 166 ? 1.3356 1.1812 1.3724 -0.1206 -0.1548 0.0824 166 TYR B CZ 8489 O OH . TYR B 166 ? 1.4704 1.2898 1.4095 -0.1533 -0.1716 0.0840 166 TYR B OH 8490 N N . ILE B 167 ? 1.1894 1.1331 1.5676 0.0133 0.0397 0.0032 167 ILE B N 8491 C CA . ILE B 167 ? 1.1315 1.0930 1.5880 0.0277 0.0720 -0.0078 167 ILE B CA 8492 C C . ILE B 167 ? 1.2313 1.2118 1.7321 0.0200 0.0609 -0.0021 167 ILE B C 8493 O O . ILE B 167 ? 1.2359 1.2329 1.8103 0.0295 0.0859 -0.0093 167 ILE B O 8494 C CB . ILE B 167 ? 0.9789 0.9345 1.3889 0.0364 0.1220 -0.0348 167 ILE B CB 8495 C CG1 . ILE B 167 ? 1.0096 0.9591 1.3342 0.0248 0.1235 -0.0426 167 ILE B CG1 8496 C CG2 . ILE B 167 ? 0.8691 0.8076 1.2504 0.0447 0.1359 -0.0415 167 ILE B CG2 8497 C CD1 . ILE B 167 ? 1.1310 1.0719 1.4024 0.0300 0.1631 -0.0631 167 ILE B CD1 8498 N N . SER B 168 ? 1.3791 1.3554 1.8336 0.0006 0.0255 0.0095 168 SER B N 8499 C CA . SER B 168 ? 1.3095 1.2982 1.7738 -0.0093 0.0228 0.0076 168 SER B CA 8500 C C . SER B 168 ? 1.1392 1.1525 1.7186 -0.0070 0.0095 0.0217 168 SER B C 8501 O O . SER B 168 ? 1.3382 1.3667 1.9618 0.0012 0.0419 0.0088 168 SER B O 8502 C CB . SER B 168 ? 1.6813 1.6551 2.0643 -0.0338 -0.0103 0.0140 168 SER B CB 8503 O OG . SER B 168 ? 1.8063 1.7636 2.1539 -0.0442 -0.0432 0.0297 168 SER B OG 8504 N N . PRO B 169 ? 1.1038 1.1213 1.7357 -0.0155 -0.0383 0.0495 169 PRO B N 8505 C CA . PRO B 169 ? 1.0153 1.0585 1.7782 -0.0060 -0.0393 0.0599 169 PRO B CA 8506 C C . PRO B 169 ? 0.9546 1.0009 1.7888 0.0177 -0.0074 0.0530 169 PRO B C 8507 O O . PRO B 169 ? 1.1822 1.2100 1.9682 0.0231 -0.0028 0.0497 169 PRO B O 8508 C CB . PRO B 169 ? 1.0291 1.0756 1.8290 -0.0257 -0.1064 0.0957 169 PRO B CB 8509 C CG . PRO B 169 ? 1.1022 1.1243 1.7749 -0.0504 -0.1340 0.0980 169 PRO B CG 8510 C CD . PRO B 169 ? 1.1308 1.1338 1.7179 -0.0386 -0.0943 0.0738 169 PRO B CD 8511 N N . PRO B 170 ? 0.8168 1.3694 1.9537 -0.4969 0.1143 0.0838 170 PRO B N 8512 C CA . PRO B 170 ? 0.8015 1.3992 2.0367 -0.4416 0.1521 0.0835 170 PRO B CA 8513 C C . PRO B 170 ? 0.7554 1.4052 2.0797 -0.4178 0.0922 0.1089 170 PRO B C 8514 O O . PRO B 170 ? 0.7035 1.3598 2.0740 -0.3703 0.1116 0.1081 170 PRO B O 8515 C CB . PRO B 170 ? 0.7882 1.4471 2.1119 -0.4447 0.1963 0.0851 170 PRO B CB 8516 C CG . PRO B 170 ? 1.0913 1.7703 2.4061 -0.5039 0.1539 0.0966 170 PRO B CG 8517 C CD . PRO B 170 ? 0.8382 1.4237 2.0010 -0.5364 0.1272 0.0857 170 PRO B CD 8518 N N . GLU B 171 ? 0.8413 1.5180 2.1779 -0.4515 0.0190 0.1308 171 GLU B N 8519 C CA . GLU B 171 ? 0.8374 1.5535 2.2403 -0.4323 -0.0465 0.1583 171 GLU B CA 8520 C C . GLU B 171 ? 0.8717 1.5177 2.1771 -0.4227 -0.0794 0.1595 171 GLU B C 8521 O O . GLU B 171 ? 1.0001 1.6648 2.3467 -0.3997 -0.1259 0.1811 171 GLU B O 8522 C CB . GLU B 171 ? 0.8102 1.5675 2.2432 -0.4735 -0.1161 0.1805 171 GLU B CB 8523 C CG . GLU B 171 ? 1.0399 1.8840 2.5989 -0.4808 -0.0938 0.1874 171 GLU B CG 8524 C CD . GLU B 171 ? 1.2423 2.0637 2.7457 -0.5232 -0.0485 0.1652 171 GLU B CD 8525 O OE1 . GLU B 171 ? 1.3827 2.1170 2.7459 -0.5486 -0.0412 0.1459 171 GLU B OE1 8526 O OE2 . GLU B 171 ? 1.2798 2.1674 2.8788 -0.5307 -0.0191 0.1691 171 GLU B OE2 8527 N N . ALA B 172 ? 0.7874 1.3412 1.9378 -0.4328 -0.0528 0.1344 172 ALA B N 8528 C CA . ALA B 172 ? 0.9083 1.3797 1.9271 -0.4106 -0.0695 0.1284 172 ALA B CA 8529 C C . ALA B 172 ? 0.8126 1.2828 1.8633 -0.3533 -0.0296 0.1193 172 ALA B C 8530 O O . ALA B 172 ? 0.7270 1.1629 1.7332 -0.3283 -0.0540 0.1255 172 ALA B O 8531 C CB . ALA B 172 ? 1.1292 1.5058 1.9803 -0.4316 -0.0476 0.1056 172 ALA B CB 8532 N N . LEU B 173 ? 0.8746 1.3746 1.9948 -0.3349 0.0341 0.1040 173 LEU B N 8533 C CA . LEU B 173 ? 1.1050 1.6053 2.2689 -0.2830 0.0723 0.0958 173 LEU B CA 8534 C C . LEU B 173 ? 1.2301 1.8148 2.5559 -0.2615 0.0437 0.1243 173 LEU B C 8535 O O . LEU B 173 ? 1.1427 1.8067 2.5849 -0.2837 0.0272 0.1434 173 LEU B O 8536 C CB . LEU B 173 ? 1.1699 1.6568 2.3324 -0.2719 0.1539 0.0684 173 LEU B CB 8537 C CG . LEU B 173 ? 1.1363 1.5354 2.1389 -0.2868 0.1827 0.0422 173 LEU B CG 8538 C CD1 . LEU B 173 ? 1.2220 1.6047 2.2214 -0.2775 0.2604 0.0179 173 LEU B CD1 8539 C CD2 . LEU B 173 ? 1.0419 1.3706 1.9353 -0.2649 0.1629 0.0366 173 LEU B CD2 8540 N N . GLU B 174 ? 1.0354 1.6017 2.3683 -0.2202 0.0341 0.1297 174 GLU B N 8541 C CA . GLU B 174 ? 1.1576 1.7887 2.6296 -0.1919 0.0015 0.1596 174 GLU B CA 8542 C C . GLU B 174 ? 1.0744 1.7252 2.5449 -0.2200 -0.0884 0.1928 174 GLU B C 8543 O O . GLU B 174 ? 1.0268 1.7056 2.5684 -0.1973 -0.1321 0.2207 174 GLU B O 8544 C CB . GLU B 174 ? 1.1061 1.8281 2.7501 -0.1800 0.0427 0.1669 174 GLU B CB 8545 C CG . GLU B 174 ? 1.0945 1.8854 2.8813 -0.1483 0.0077 0.2011 174 GLU B CG 8546 C CD . GLU B 174 ? 1.2254 1.9934 3.0528 -0.0907 0.0375 0.1988 174 GLU B CD 8547 O OE1 . GLU B 174 ? 1.1721 1.9773 3.0948 -0.0587 0.0110 0.2261 174 GLU B OE1 8548 O OE2 . GLU B 174 ? 1.2825 1.9680 2.9989 -0.0756 0.0850 0.1662 174 GLU B OE2 8549 N N . ASN B 175 ? 0.9829 1.6073 2.3592 -0.2693 -0.1156 0.1894 175 ASN B N 8550 C CA . ASN B 175 ? 0.8325 1.4467 2.1625 -0.3017 -0.1983 0.2153 175 ASN B CA 8551 C C . ASN B 175 ? 0.8959 1.4185 2.0423 -0.3368 -0.2034 0.1970 175 ASN B C 8552 O O . ASN B 175 ? 0.9373 1.4599 2.0528 -0.3831 -0.2161 0.1947 175 ASN B O 8553 C CB . ASN B 175 ? 0.8899 1.5930 2.3435 -0.3339 -0.2440 0.2428 175 ASN B CB 8554 C CG . ASN B 175 ? 1.1852 1.8705 2.5863 -0.3620 -0.3356 0.2718 175 ASN B CG 8555 O OD1 . ASN B 175 ? 0.9947 1.6257 2.3202 -0.3509 -0.3684 0.2812 175 ASN B OD1 8556 N ND2 . ASN B 175 ? 1.3572 2.0764 2.7798 -0.3971 -0.3738 0.2841 175 ASN B ND2 8557 N N . PRO B 176 ? 0.9071 1.3501 1.9349 -0.3146 -0.1907 0.1850 176 PRO B N 8558 C CA . PRO B 176 ? 0.8077 1.1613 1.6661 -0.3383 -0.1873 0.1694 176 PRO B CA 8559 C C . PRO B 176 ? 0.8518 1.1810 1.6427 -0.3856 -0.2498 0.1866 176 PRO B C 8560 O O . PRO B 176 ? 0.8898 1.1528 1.5560 -0.4136 -0.2403 0.1721 176 PRO B O 8561 C CB . PRO B 176 ? 0.8394 1.1371 1.6302 -0.3024 -0.1807 0.1683 176 PRO B CB 8562 C CG . PRO B 176 ? 0.8903 1.2326 1.7928 -0.2598 -0.1480 0.1647 176 PRO B CG 8563 C CD . PRO B 176 ? 0.9809 1.4141 2.0355 -0.2641 -0.1729 0.1854 176 PRO B CD 8564 N N . CYS B 177 ? 0.8519 1.2277 1.7191 -0.3943 -0.3139 0.2179 177 CYS B N 8565 C CA . CYS B 177 ? 1.0205 1.3746 1.8287 -0.4457 -0.3799 0.2351 177 CYS B CA 8566 C C . CYS B 177 ? 1.2767 1.7185 2.2121 -0.4806 -0.4009 0.2454 177 CYS B C 8567 O O . CYS B 177 ? 1.5217 2.0541 2.6122 -0.4680 -0.4296 0.2704 177 CYS B O 8568 C CB . CYS B 177 ? 0.9626 1.2986 1.7505 -0.4405 -0.4488 0.2670 177 CYS B CB 8569 S SG . CYS B 177 ? 1.4926 1.7178 2.1179 -0.4111 -0.4288 0.2599 177 CYS B SG 8570 N N . TYR B 178 ? 1.0581 1.4709 1.9285 -0.5234 -0.3842 0.2272 178 TYR B N 8571 C CA . TYR B 178 ? 0.9778 1.4516 1.9280 -0.5563 -0.3974 0.2314 178 TYR B CA 8572 C C . TYR B 178 ? 1.4972 1.8928 2.3043 -0.6095 -0.4473 0.2323 178 TYR B C 8573 O O . TYR B 178 ? 1.6699 2.0854 2.4969 -0.6305 -0.5110 0.2548 178 TYR B O 8574 C CB . TYR B 178 ? 0.9318 1.4349 1.9305 -0.5540 -0.3191 0.2047 178 TYR B CB 8575 C CG . TYR B 178 ? 1.2620 1.8421 2.3672 -0.5742 -0.3200 0.2086 178 TYR B CG 8576 C CD1 . TYR B 178 ? 1.2654 1.9475 2.5369 -0.5453 -0.3282 0.2295 178 TYR B CD1 8577 C CD2 . TYR B 178 ? 1.2469 1.7944 2.2867 -0.6214 -0.3105 0.1926 178 TYR B CD2 8578 C CE1 . TYR B 178 ? 1.2521 2.0080 2.6262 -0.5647 -0.3273 0.2356 178 TYR B CE1 8579 C CE2 . TYR B 178 ? 1.2476 1.8675 2.3900 -0.6433 -0.3110 0.1972 178 TYR B CE2 8580 C CZ . TYR B 178 ? 1.2104 1.9377 2.5217 -0.6156 -0.3195 0.2193 178 TYR B CZ 8581 O OH . TYR B 178 ? 1.0497 1.8526 2.4678 -0.6381 -0.3184 0.2262 178 TYR B OH 8582 N N . ASP B 179 ? 1.5619 1.8613 2.2190 -0.6298 -0.4154 0.2081 179 ASP B N 8583 C CA . ASP B 179 ? 1.5364 1.7288 2.0193 -0.6709 -0.4552 0.2069 179 ASP B CA 8584 C C . ASP B 179 ? 1.5657 1.7211 1.9945 -0.6629 -0.5140 0.2312 179 ASP B C 8585 O O . ASP B 179 ? 1.3516 1.5317 1.8300 -0.6178 -0.5000 0.2379 179 ASP B O 8586 C CB . ASP B 179 ? 1.5307 1.6203 1.8627 -0.6802 -0.3987 0.1771 179 ASP B CB 8587 C CG . ASP B 179 ? 1.6940 1.7826 2.0327 -0.6203 -0.3307 0.1616 179 ASP B CG 8588 O OD1 . ASP B 179 ? 1.6808 1.7069 1.9266 -0.5916 -0.3281 0.1626 179 ASP B OD1 8589 O OD2 . ASP B 179 ? 1.7017 1.8487 2.1343 -0.6008 -0.2780 0.1485 179 ASP B OD2 8590 N N . MET B 180 ? 1.7254 1.8143 2.0429 -0.7000 -0.5732 0.2430 180 MET B N 8591 C CA . MET B 180 ? 1.8589 1.9073 2.1166 -0.7003 -0.6393 0.2705 180 MET B CA 8592 C C . MET B 180 ? 1.7920 1.9523 2.2219 -0.6783 -0.6881 0.3041 180 MET B C 8593 O O . MET B 180 ? 1.8401 1.9766 2.2379 -0.6776 -0.7488 0.3322 180 MET B O 8594 C CB . MET B 180 ? 1.7987 1.7787 1.9649 -0.6669 -0.6083 0.2642 180 MET B CB 8595 C CG . MET B 180 ? 1.9103 1.7578 1.8770 -0.6756 -0.5597 0.2366 180 MET B CG 8596 S SD . MET B 180 ? 2.6425 2.5013 2.6291 -0.6537 -0.4605 0.1989 180 MET B SD 8597 C CE . MET B 180 ? 1.9883 1.6830 1.7359 -0.6588 -0.4195 0.1783 180 MET B CE 8598 N N . LYS B 181 ? 1.6908 1.9653 2.2966 -0.6587 -0.6568 0.3014 181 LYS B N 8599 C CA . LYS B 181 ? 1.6213 2.0049 2.4001 -0.6391 -0.6937 0.3315 181 LYS B CA 8600 C C . LYS B 181 ? 1.6238 2.0226 2.4472 -0.5987 -0.7273 0.3601 181 LYS B C 8601 O O . LYS B 181 ? 1.7947 2.1775 2.5959 -0.6095 -0.7983 0.3912 181 LYS B O 8602 C CB . LYS B 181 ? 1.4841 1.8644 2.2436 -0.6858 -0.7588 0.3498 181 LYS B CB 8603 C CG . LYS B 181 ? 1.4930 1.8780 2.2451 -0.7241 -0.7284 0.3257 181 LYS B CG 8604 C CD . LYS B 181 ? 1.6691 2.0578 2.4174 -0.7710 -0.7969 0.3468 181 LYS B CD 8605 C CE . LYS B 181 ? 1.5770 1.9731 2.3274 -0.8094 -0.7654 0.3233 181 LYS B CE 8606 N NZ . LYS B 181 ? 1.6968 2.0988 2.4498 -0.8584 -0.8343 0.3449 181 LYS B NZ 8607 N N . THR B 182 ? 1.2908 1.7149 2.1734 -0.5527 -0.6759 0.3502 182 THR B N 8608 C CA . THR B 182 ? 1.2894 1.7334 2.2317 -0.5084 -0.6983 0.3757 182 THR B CA 8609 C C . THR B 182 ? 1.3438 1.8666 2.4368 -0.4550 -0.6305 0.3644 182 THR B C 8610 O O . THR B 182 ? 1.3794 1.9460 2.5342 -0.4552 -0.5731 0.3408 182 THR B O 8611 C CB . THR B 182 ? 1.4652 1.8031 2.2471 -0.5128 -0.7163 0.3766 182 THR B CB 8612 O OG1 . THR B 182 ? 1.5927 1.8312 2.1948 -0.5658 -0.7326 0.3632 182 THR B OG1 8613 C CG2 . THR B 182 ? 1.5676 1.8975 2.3578 -0.4932 -0.7811 0.4157 182 THR B CG2 8614 N N . THR B 183 ? 1.3425 1.8751 2.4869 -0.4094 -0.6347 0.3809 183 THR B N 8615 C CA . THR B 183 ? 1.0882 1.6794 2.3617 -0.3565 -0.5685 0.3692 183 THR B CA 8616 C C . THR B 183 ? 1.1774 1.6915 2.3548 -0.3186 -0.5246 0.3514 183 THR B C 8617 O O . THR B 183 ? 1.2027 1.6778 2.3414 -0.2995 -0.5596 0.3726 183 THR B O 8618 C CB . THR B 183 ? 1.0382 1.7055 2.4676 -0.3153 -0.5862 0.3987 183 THR B CB 8619 O OG1 . THR B 183 ? 1.1056 1.8347 2.6087 -0.3390 -0.6033 0.4076 183 THR B OG1 8620 C CG2 . THR B 183 ? 0.8601 1.5675 2.4019 -0.2585 -0.5121 0.3840 183 THR B CG2 8621 N N . CYS B 184 ? 1.1799 1.6668 2.3112 -0.3080 -0.4464 0.3126 184 CYS B N 8622 C CA . CYS B 184 ? 0.8682 1.2910 1.9243 -0.2701 -0.3961 0.2928 184 CYS B CA 8623 C C . CYS B 184 ? 0.8026 1.2756 1.9824 -0.2241 -0.3369 0.2795 184 CYS B C 8624 O O . CYS B 184 ? 1.0413 1.5989 2.3667 -0.2182 -0.3327 0.2882 184 CYS B O 8625 C CB . CYS B 184 ? 0.9026 1.2465 1.8026 -0.2911 -0.3553 0.2609 184 CYS B CB 8626 S SG . CYS B 184 ? 1.7965 2.0548 2.5234 -0.3398 -0.4099 0.2720 184 CYS B SG 8627 N N . LEU B 185 ? 0.8209 1.2391 1.9423 -0.1929 -0.2900 0.2593 185 LEU B N 8628 C CA . LEU B 185 ? 0.7882 1.2301 1.9942 -0.1526 -0.2282 0.2406 185 LEU B CA 8629 C C . LEU B 185 ? 0.7986 1.1937 1.9125 -0.1589 -0.1646 0.2010 185 LEU B C 8630 O O . LEU B 185 ? 0.9047 1.2351 1.8870 -0.1767 -0.1673 0.1917 185 LEU B O 8631 C CB . LEU B 185 ? 0.8787 1.2922 2.1031 -0.1096 -0.2317 0.2524 185 LEU B CB 8632 C CG . LEU B 185 ? 1.1136 1.5825 2.4708 -0.0841 -0.2752 0.2898 185 LEU B CG 8633 C CD1 . LEU B 185 ? 1.2736 1.7497 2.6066 -0.1148 -0.3593 0.3262 185 LEU B CD1 8634 C CD2 . LEU B 185 ? 1.0467 1.4731 2.4131 -0.0382 -0.2591 0.2927 185 LEU B CD2 8635 N N . PRO B 186 ? 0.7516 1.1766 1.9335 -0.1432 -0.1061 0.1794 186 PRO B N 8636 C CA . PRO B 186 ? 0.7777 1.1571 1.8740 -0.1489 -0.0472 0.1434 186 PRO B CA 8637 C C . PRO B 186 ? 0.8066 1.1064 1.7915 -0.1344 -0.0366 0.1307 186 PRO B C 8638 O O . PRO B 186 ? 1.0084 1.2922 2.0190 -0.1036 -0.0387 0.1369 186 PRO B O 8639 C CB . PRO B 186 ? 0.7746 1.1925 1.9742 -0.1232 0.0113 0.1286 186 PRO B CB 8640 C CG . PRO B 186 ? 0.7954 1.2676 2.1306 -0.0923 -0.0119 0.1560 186 PRO B CG 8641 C CD . PRO B 186 ? 0.7104 1.2113 2.0545 -0.1176 -0.0900 0.1899 186 PRO B CD 8642 N N . MET B 187 ? 0.7988 1.0497 1.6661 -0.1569 -0.0255 0.1150 187 MET B N 8643 C CA . MET B 187 ? 0.8721 1.0565 1.6407 -0.1485 -0.0226 0.1092 187 MET B CA 8644 C C . MET B 187 ? 0.8435 0.9989 1.6104 -0.1226 0.0232 0.0860 187 MET B C 8645 O O . MET B 187 ? 0.8430 1.0146 1.6517 -0.1153 0.0639 0.0675 187 MET B O 8646 C CB . MET B 187 ? 0.8128 0.9568 1.4662 -0.1768 -0.0217 0.1022 187 MET B CB 8647 C CG . MET B 187 ? 0.7981 0.9245 1.4103 -0.1827 0.0266 0.0743 187 MET B CG 8648 S SD . MET B 187 ? 0.9892 1.0570 1.4649 -0.2047 0.0282 0.0706 187 MET B SD 8649 C CE . MET B 187 ? 0.8107 0.8395 1.2456 -0.1851 0.0114 0.0842 187 MET B CE 8650 N N . PHE B 188 ? 0.8570 0.9645 1.5703 -0.1113 0.0162 0.0879 188 PHE B N 8651 C CA . PHE B 188 ? 0.9218 0.9899 1.6217 -0.0911 0.0485 0.0683 188 PHE B CA 8652 C C . PHE B 188 ? 1.0935 1.1098 1.7017 -0.0982 0.0399 0.0690 188 PHE B C 8653 O O . PHE B 188 ? 1.0896 1.1002 1.6704 -0.1061 0.0079 0.0908 188 PHE B O 8654 C CB . PHE B 188 ? 0.9290 1.0040 1.7117 -0.0608 0.0451 0.0768 188 PHE B CB 8655 C CG . PHE B 188 ? 0.9382 1.0253 1.7475 -0.0573 -0.0047 0.1098 188 PHE B CG 8656 C CD1 . PHE B 188 ? 0.9440 0.9845 1.6980 -0.0560 -0.0244 0.1209 188 PHE B CD1 8657 C CD2 . PHE B 188 ? 1.0341 1.1781 1.9233 -0.0575 -0.0335 0.1319 188 PHE B CD2 8658 C CE1 . PHE B 188 ? 0.9659 1.0084 1.7327 -0.0537 -0.0678 0.1523 188 PHE B CE1 8659 C CE2 . PHE B 188 ? 1.0789 1.2260 1.9809 -0.0556 -0.0838 0.1641 188 PHE B CE2 8660 C CZ . PHE B 188 ? 0.9878 1.0801 1.8230 -0.0532 -0.0989 0.1737 188 PHE B CZ 8661 N N . GLY B 189 ? 1.1086 1.0862 1.6690 -0.0968 0.0681 0.0469 189 GLY B N 8662 C CA . GLY B 189 ? 1.2051 1.1429 1.6950 -0.1042 0.0587 0.0504 189 GLY B CA 8663 C C . GLY B 189 ? 0.9631 0.8809 1.4709 -0.0927 0.0362 0.0667 189 GLY B C 8664 O O . GLY B 189 ? 0.8544 0.7685 1.3392 -0.0998 0.0123 0.0890 189 GLY B O 8665 N N . TYR B 190 ? 0.9156 0.8134 1.4595 -0.0748 0.0480 0.0556 190 TYR B N 8666 C CA . TYR B 190 ? 0.9251 0.7991 1.4932 -0.0621 0.0285 0.0709 190 TYR B CA 8667 C C . TYR B 190 ? 0.9799 0.8461 1.6114 -0.0358 0.0459 0.0606 190 TYR B C 8668 O O . TYR B 190 ? 1.0137 0.8652 1.6429 -0.0295 0.0813 0.0339 190 TYR B O 8669 C CB . TYR B 190 ? 0.9081 0.7335 1.4197 -0.0730 0.0244 0.0684 190 TYR B CB 8670 C CG . TYR B 190 ? 1.1375 0.9237 1.6691 -0.0620 0.0120 0.0774 190 TYR B CG 8671 C CD1 . TYR B 190 ? 1.1198 0.9124 1.6732 -0.0587 -0.0155 0.1081 190 TYR B CD1 8672 C CD2 . TYR B 190 ? 1.2437 0.9759 1.7614 -0.0566 0.0283 0.0551 190 TYR B CD2 8673 C CE1 . TYR B 190 ? 1.0066 0.7570 1.5748 -0.0494 -0.0259 0.1177 190 TYR B CE1 8674 C CE2 . TYR B 190 ? 0.9932 0.6797 1.5231 -0.0483 0.0178 0.0626 190 TYR B CE2 8675 C CZ . TYR B 190 ? 1.0338 0.7317 1.5924 -0.0443 -0.0090 0.0946 190 TYR B CZ 8676 O OH . TYR B 190 ? 1.1288 0.7754 1.6965 -0.0368 -0.0186 0.1035 190 TYR B OH 8677 N N . LYS B 191 ? 0.9935 0.8635 1.6778 -0.0189 0.0240 0.0828 191 LYS B N 8678 C CA . LYS B 191 ? 1.0762 0.9312 1.8238 0.0116 0.0424 0.0762 191 LYS B CA 8679 C C . LYS B 191 ? 1.0953 0.9096 1.8538 0.0249 0.0187 0.0963 191 LYS B C 8680 O O . LYS B 191 ? 1.0514 0.8792 1.8103 0.0182 -0.0184 0.1263 191 LYS B O 8681 C CB . LYS B 191 ? 1.0733 0.9952 1.9138 0.0278 0.0463 0.0852 191 LYS B CB 8682 C CG . LYS B 191 ? 1.0676 1.0374 1.9502 0.0249 -0.0020 0.1223 191 LYS B CG 8683 C CD . LYS B 191 ? 1.0753 1.1154 2.0637 0.0393 -0.0009 0.1320 191 LYS B CD 8684 C CE . LYS B 191 ? 1.0848 1.1676 2.1102 0.0333 -0.0578 0.1707 191 LYS B CE 8685 N NZ . LYS B 191 ? 1.1336 1.1827 2.1748 0.0544 -0.0872 0.1965 191 LYS B NZ 8686 N N . HIS B 192 ? 1.0639 0.8185 1.8211 0.0423 0.0426 0.0788 192 HIS B N 8687 C CA . HIS B 192 ? 1.0731 0.7766 1.8387 0.0560 0.0256 0.0950 192 HIS B CA 8688 C C . HIS B 192 ? 1.0859 0.8146 1.9491 0.0937 0.0231 0.1141 192 HIS B C 8689 O O . HIS B 192 ? 1.1244 0.8562 2.0390 0.1204 0.0600 0.0974 192 HIS B O 8690 C CB . HIS B 192 ? 1.1278 0.7428 1.8370 0.0543 0.0506 0.0667 192 HIS B CB 8691 C CG . HIS B 192 ? 1.2675 0.8181 1.9839 0.0689 0.0387 0.0800 192 HIS B CG 8692 N ND1 . HIS B 192 ? 1.3450 0.8861 2.0453 0.0536 0.0004 0.1100 192 HIS B ND1 8693 C CD2 . HIS B 192 ? 1.2701 0.7553 2.0036 0.0978 0.0636 0.0679 192 HIS B CD2 8694 C CE1 . HIS B 192 ? 1.5230 0.9968 2.2309 0.0703 -0.0008 0.1164 192 HIS B CE1 8695 N NE2 . HIS B 192 ? 1.4465 0.8835 2.1739 0.0982 0.0367 0.0908 192 HIS B NE2 8696 N N . VAL B 193 ? 1.0675 0.8126 1.9565 0.0968 -0.0193 0.1512 193 VAL B N 8697 C CA . VAL B 193 ? 1.1053 0.8830 2.0925 0.1314 -0.0334 0.1773 193 VAL B CA 8698 C C . VAL B 193 ? 1.2957 1.0008 2.2995 0.1612 -0.0289 0.1846 193 VAL B C 8699 O O . VAL B 193 ? 1.3761 1.0632 2.4352 0.1963 0.0066 0.1715 193 VAL B O 8700 C CB . VAL B 193 ? 1.0403 0.8697 2.0407 0.1185 -0.0878 0.2169 193 VAL B CB 8701 C CG1 . VAL B 193 ? 1.1713 1.0483 2.2845 0.1523 -0.1083 0.2456 193 VAL B CG1 8702 C CG2 . VAL B 193 ? 1.0303 0.9127 1.9930 0.0846 -0.0922 0.2085 193 VAL B CG2 8703 N N . LEU B 194 ? 1.3658 1.0241 2.3192 0.1476 -0.0609 0.2062 194 LEU B N 8704 C CA . LEU B 194 ? 1.4324 1.0137 2.3936 0.1723 -0.0612 0.2171 194 LEU B CA 8705 C C . LEU B 194 ? 1.3574 0.8512 2.2250 0.1454 -0.0511 0.1985 194 LEU B C 8706 O O . LEU B 194 ? 1.1434 0.6362 1.9506 0.1093 -0.0741 0.2091 194 LEU B O 8707 C CB . LEU B 194 ? 1.3084 0.9018 2.3005 0.1822 -0.1113 0.2660 194 LEU B CB 8708 C CG . LEU B 194 ? 1.4691 0.9808 2.4712 0.2096 -0.1163 0.2842 194 LEU B CG 8709 C CD1 . LEU B 194 ? 1.5944 1.0860 2.6712 0.2575 -0.0758 0.2674 194 LEU B CD1 8710 C CD2 . LEU B 194 ? 1.5425 1.0690 2.5677 0.2172 -0.1702 0.3358 194 LEU B CD2 8711 N N . THR B 195 ? 1.3863 0.8047 2.2431 0.1624 -0.0155 0.1715 195 THR B N 8712 C CA . THR B 195 ? 1.3768 0.7035 2.1475 0.1347 -0.0102 0.1538 195 THR B CA 8713 C C . THR B 195 ? 1.5659 0.8417 2.3253 0.1314 -0.0426 0.1884 195 THR B C 8714 O O . THR B 195 ? 1.4812 0.7723 2.2987 0.1615 -0.0616 0.2212 195 THR B O 8715 C CB . THR B 195 ? 1.3713 0.6138 2.1195 0.1526 0.0363 0.1143 195 THR B CB 8716 O OG1 . THR B 195 ? 1.4214 0.5791 2.0765 0.1148 0.0337 0.0955 195 THR B OG1 8717 C CG2 . THR B 195 ? 1.7324 0.9267 2.5406 0.2030 0.0500 0.1272 195 THR B CG2 8718 N N . LEU B 196 ? 1.6952 0.9119 2.3820 0.0933 -0.0509 0.1838 196 LEU B N 8719 C CA . LEU B 196 ? 1.5457 0.7124 2.2147 0.0826 -0.0788 0.2177 196 LEU B CA 8720 C C . LEU B 196 ? 1.5017 0.6025 2.1836 0.1207 -0.0692 0.2214 196 LEU B C 8721 O O . LEU B 196 ? 1.5736 0.6025 2.2286 0.1310 -0.0390 0.1894 196 LEU B O 8722 C CB . LEU B 196 ? 1.4796 0.6006 2.0735 0.0320 -0.0839 0.2081 196 LEU B CB 8723 C CG . LEU B 196 ? 1.3875 0.5803 1.9604 -0.0074 -0.0962 0.2128 196 LEU B CG 8724 C CD1 . LEU B 196 ? 1.3658 0.5145 1.8826 -0.0542 -0.1003 0.2035 196 LEU B CD1 8725 C CD2 . LEU B 196 ? 1.2943 0.5432 1.8847 -0.0081 -0.1212 0.2555 196 LEU B CD2 8726 N N . THR B 197 ? 1.5131 0.6349 2.2248 0.1405 -0.0952 0.2603 197 THR B N 8727 C CA . THR B 197 ? 1.7174 0.7863 2.4445 0.1799 -0.0903 0.2703 197 THR B CA 8728 C C . THR B 197 ? 1.7387 0.7917 2.4382 0.1712 -0.1249 0.3118 197 THR B C 8729 O O . THR B 197 ? 1.5984 0.6971 2.2806 0.1423 -0.1515 0.3353 197 THR B O 8730 C CB . THR B 197 ? 1.8207 0.9481 2.6446 0.2329 -0.0810 0.2755 197 THR B CB 8731 O OG1 . THR B 197 ? 1.9010 1.1277 2.7755 0.2296 -0.1147 0.3048 197 THR B OG1 8732 C CG2 . THR B 197 ? 1.8113 0.9356 2.6563 0.2484 -0.0334 0.2318 197 THR B CG2 8733 N N . ASP B 198 ? 1.7559 0.7378 2.4444 0.1970 -0.1211 0.3203 198 ASP B N 8734 C CA . ASP B 198 ? 1.8419 0.7944 2.4970 0.1914 -0.1496 0.3589 198 ASP B CA 8735 C C . ASP B 198 ? 1.9759 0.9860 2.6947 0.2296 -0.1783 0.3956 198 ASP B C 8736 O O . ASP B 198 ? 2.0675 1.0532 2.7601 0.2314 -0.2040 0.4301 198 ASP B O 8737 C CB . ASP B 198 ? 2.0286 0.8632 2.6282 0.1959 -0.1327 0.3511 198 ASP B CB 8738 C CG . ASP B 198 ? 2.1367 0.9324 2.7770 0.2507 -0.1076 0.3363 198 ASP B CG 8739 O OD1 . ASP B 198 ? 2.1568 1.0000 2.8526 0.2726 -0.0860 0.3127 198 ASP B OD1 8740 O OD2 . ASP B 198 ? 2.1871 0.9030 2.8029 0.2728 -0.1061 0.3488 198 ASP B OD2 8741 N N . GLN B 199 ? 1.8906 0.9772 2.6922 0.2580 -0.1745 0.3887 199 GLN B N 8742 C CA . GLN B 199 ? 1.7908 0.9426 2.6653 0.2925 -0.2051 0.4227 199 GLN B CA 8743 C C . GLN B 199 ? 1.6980 0.9351 2.5782 0.2657 -0.2433 0.4450 199 GLN B C 8744 O O . GLN B 199 ? 1.7058 1.0056 2.6178 0.2546 -0.2353 0.4273 199 GLN B O 8745 C CB . GLN B 199 ? 1.7649 0.9558 2.7363 0.3397 -0.1773 0.4054 199 GLN B CB 8746 C CG . GLN B 199 ? 1.9560 1.0545 2.9129 0.3692 -0.1329 0.3794 199 GLN B CG 8747 C CD . GLN B 199 ? 1.9793 1.1074 3.0023 0.3991 -0.0858 0.3452 199 GLN B CD 8748 O OE1 . GLN B 199 ? 1.8722 1.0638 2.9197 0.3820 -0.0754 0.3266 199 GLN B OE1 8749 N NE2 . GLN B 199 ? 1.9038 0.9817 2.9515 0.4445 -0.0537 0.3368 199 GLN B NE2 8750 N N . VAL B 200 ? 1.7572 0.9878 2.5972 0.2549 -0.2833 0.4833 200 VAL B N 8751 C CA . VAL B 200 ? 1.6972 0.9930 2.5248 0.2298 -0.3217 0.5064 200 VAL B CA 8752 C C . VAL B 200 ? 1.7409 1.1156 2.6584 0.2601 -0.3544 0.5276 200 VAL B C 8753 O O . VAL B 200 ? 1.7537 1.1931 2.6780 0.2416 -0.3846 0.5398 200 VAL B O 8754 C CB . VAL B 200 ? 1.7210 0.9681 2.4511 0.2017 -0.3473 0.5374 200 VAL B CB 8755 C CG1 . VAL B 200 ? 1.6947 0.8745 2.3470 0.1681 -0.3142 0.5188 200 VAL B CG1 8756 C CG2 . VAL B 200 ? 1.9796 1.1885 2.7147 0.2328 -0.3721 0.5696 200 VAL B CG2 8757 N N . THR B 201 ? 1.7610 1.1288 2.7468 0.3053 -0.3479 0.5323 201 THR B N 8758 C CA . THR B 201 ? 1.7266 1.1749 2.8130 0.3358 -0.3771 0.5541 201 THR B CA 8759 C C . THR B 201 ? 1.7984 1.3327 2.9702 0.3391 -0.3556 0.5286 201 THR B C 8760 O O . THR B 201 ? 1.8949 1.5137 3.1184 0.3323 -0.3901 0.5450 201 THR B O 8761 C CB . THR B 201 ? 1.7684 1.1862 2.9112 0.3871 -0.3677 0.5652 201 THR B CB 8762 O OG1 . THR B 201 ? 1.7734 1.1521 2.9385 0.4098 -0.3060 0.5262 201 THR B OG1 8763 C CG2 . THR B 201 ? 2.1928 1.5220 3.2501 0.3851 -0.3901 0.5931 201 THR B CG2 8764 N N . ARG B 202 ? 1.7081 1.2151 2.8878 0.3471 -0.2984 0.4879 202 ARG B N 8765 C CA . ARG B 202 ? 1.6669 1.2426 2.9141 0.3487 -0.2683 0.4594 202 ARG B CA 8766 C C . ARG B 202 ? 1.5693 1.1805 2.7691 0.3024 -0.2880 0.4563 202 ARG B C 8767 O O . ARG B 202 ? 1.5546 1.2487 2.8150 0.2979 -0.2943 0.4539 202 ARG B O 8768 C CB . ARG B 202 ? 1.7398 1.2568 2.9795 0.3643 -0.2010 0.4145 202 ARG B CB 8769 C CG . ARG B 202 ? 1.8055 1.3773 3.0919 0.3612 -0.1625 0.3806 202 ARG B CG 8770 C CD . ARG B 202 ? 1.8316 1.3327 3.0977 0.3782 -0.0953 0.3359 202 ARG B CD 8771 N NE . ARG B 202 ? 1.8085 1.3521 3.1029 0.3720 -0.0556 0.3020 202 ARG B NE 8772 C CZ . ARG B 202 ? 1.7658 1.3836 3.1606 0.4001 -0.0284 0.2968 202 ARG B CZ 8773 N NH1 . ARG B 202 ? 1.7669 1.4293 3.2502 0.4362 -0.0395 0.3247 202 ARG B NH1 8774 N NH2 . ARG B 202 ? 1.6007 1.2485 3.0072 0.3906 0.0110 0.2647 202 ARG B NH2 8775 N N . PHE B 203 ? 1.4007 0.9481 2.4916 0.2675 -0.2958 0.4577 203 PHE B N 8776 C CA . PHE B 203 ? 1.3769 0.9432 2.4085 0.2239 -0.3072 0.4544 203 PHE B CA 8777 C C . PHE B 203 ? 1.5098 1.1461 2.5558 0.2107 -0.3601 0.4858 203 PHE B C 8778 O O . PHE B 203 ? 1.2408 0.9346 2.3085 0.1955 -0.3623 0.4769 203 PHE B O 8779 C CB . PHE B 203 ? 1.4742 0.9615 2.3902 0.1904 -0.3054 0.4571 203 PHE B CB 8780 C CG . PHE B 203 ? 1.3899 0.8902 2.2407 0.1470 -0.3075 0.4528 203 PHE B CG 8781 C CD1 . PHE B 203 ? 1.2533 0.7519 2.0818 0.1278 -0.2658 0.4129 203 PHE B CD1 8782 C CD2 . PHE B 203 ? 1.3108 0.8259 2.1060 0.1228 -0.3464 0.4833 203 PHE B CD2 8783 C CE1 . PHE B 203 ? 1.2035 0.7265 1.9634 0.0877 -0.2606 0.4028 203 PHE B CE1 8784 C CE2 . PHE B 203 ? 1.2665 0.7932 1.9907 0.0840 -0.3388 0.4748 203 PHE B CE2 8785 C CZ . PHE B 203 ? 1.2094 0.7464 1.9193 0.0675 -0.2939 0.4333 203 PHE B CZ 8786 N N . ASN B 204 ? 1.5851 1.2097 2.6107 0.2143 -0.4039 0.5219 204 ASN B N 8787 C CA . ASN B 204 ? 1.5411 1.2167 2.5607 0.1966 -0.4607 0.5526 204 ASN B CA 8788 C C . ASN B 204 ? 1.5157 1.2906 2.6572 0.2137 -0.4727 0.5520 204 ASN B C 8789 O O . ASN B 204 ? 1.5040 1.3321 2.6433 0.1881 -0.5053 0.5606 204 ASN B O 8790 C CB . ASN B 204 ? 1.4810 1.1160 2.4561 0.2009 -0.5035 0.5901 204 ASN B CB 8791 C CG . ASN B 204 ? 1.5727 1.1135 2.4253 0.1800 -0.4907 0.5936 204 ASN B CG 8792 O OD1 . ASN B 204 ? 1.7127 1.1969 2.5483 0.1982 -0.4893 0.6064 204 ASN B OD1 8793 N ND2 . ASN B 204 ? 1.6221 1.1460 2.3903 0.1416 -0.4783 0.5832 204 ASN B ND2 8794 N N . GLU B 205 ? 1.4560 1.2529 2.7002 0.2555 -0.4430 0.5416 205 GLU B N 8795 C CA . GLU B 205 ? 1.4315 1.3263 2.8037 0.2742 -0.4443 0.5414 205 GLU B CA 8796 C C . GLU B 205 ? 1.3466 1.2868 2.7524 0.2641 -0.4028 0.5058 205 GLU B C 8797 O O . GLU B 205 ? 1.3888 1.4164 2.8907 0.2687 -0.4018 0.5034 205 GLU B O 8798 C CB . GLU B 205 ? 1.3729 1.2690 2.8380 0.3249 -0.4174 0.5428 205 GLU B CB 8799 C CG . GLU B 205 ? 1.5114 1.3667 2.9546 0.3402 -0.4593 0.5803 205 GLU B CG 8800 C CD . GLU B 205 ? 1.7869 1.6321 3.3143 0.3938 -0.4271 0.5810 205 GLU B CD 8801 O OE1 . GLU B 205 ? 1.8490 1.6587 3.3661 0.4125 -0.4576 0.6116 205 GLU B OE1 8802 O OE2 . GLU B 205 ? 1.8720 1.7393 3.4699 0.4181 -0.3690 0.5508 205 GLU B OE2 8803 N N . GLU B 206 ? 1.1932 1.0729 2.5191 0.2484 -0.3681 0.4788 206 GLU B N 8804 C CA . GLU B 206 ? 1.3734 1.2856 2.6949 0.2303 -0.3250 0.4384 206 GLU B CA 8805 C C . GLU B 206 ? 1.3236 1.2652 2.5619 0.1793 -0.3558 0.4395 206 GLU B C 8806 O O . GLU B 206 ? 1.3469 1.3641 2.6287 0.1655 -0.3606 0.4326 206 GLU B O 8807 C CB . GLU B 206 ? 1.3516 1.1861 2.5995 0.2272 -0.2662 0.3976 206 GLU B CB 8808 C CG . GLU B 206 ? 1.5490 1.3475 2.8677 0.2745 -0.2205 0.3830 206 GLU B CG 8809 C CD . GLU B 206 ? 1.4610 1.3358 2.8963 0.3011 -0.1860 0.3675 206 GLU B CD 8810 O OE1 . GLU B 206 ? 1.2463 1.1216 2.7580 0.3425 -0.1636 0.3710 206 GLU B OE1 8811 O OE2 . GLU B 206 ? 1.5005 1.4354 2.9294 0.2736 -0.1744 0.3467 206 GLU B OE2 8812 N N . VAL B 207 ? 1.2842 1.1605 2.4012 0.1513 -0.3719 0.4480 207 VAL B N 8813 C CA . VAL B 207 ? 1.1542 1.0366 2.1725 0.1052 -0.3944 0.4497 207 VAL B CA 8814 C C . VAL B 207 ? 1.1970 1.1424 2.2526 0.0937 -0.4523 0.4784 207 VAL B C 8815 O O . VAL B 207 ? 1.1857 1.1641 2.2011 0.0602 -0.4562 0.4654 207 VAL B O 8816 C CB . VAL B 207 ? 1.3555 1.1541 2.2543 0.0857 -0.4084 0.4688 207 VAL B CB 8817 C CG1 . VAL B 207 ? 1.2499 1.0459 2.0409 0.0416 -0.4178 0.4664 207 VAL B CG1 8818 C CG2 . VAL B 207 ? 1.4425 1.1805 2.3120 0.0923 -0.3587 0.4446 207 VAL B CG2 8819 N N . LYS B 208 ? 1.3824 1.3409 2.5140 0.1204 -0.4997 0.5186 208 LYS B N 8820 C CA . LYS B 208 ? 1.2233 1.2441 2.4039 0.1094 -0.5653 0.5514 208 LYS B CA 8821 C C . LYS B 208 ? 1.1159 1.2340 2.3957 0.1049 -0.5469 0.5286 208 LYS B C 8822 O O . LYS B 208 ? 1.1956 1.3588 2.4682 0.0719 -0.5878 0.5383 208 LYS B O 8823 C CB . LYS B 208 ? 1.2556 1.2790 2.4975 0.1381 -0.5995 0.5839 208 LYS B CB 8824 C CG . LYS B 208 ? 1.5378 1.6238 2.8207 0.1206 -0.6630 0.6118 208 LYS B CG 8825 C CD . LYS B 208 ? 1.6817 1.7241 2.8241 0.0715 -0.7177 0.6298 208 LYS B CD 8826 C CE . LYS B 208 ? 1.5666 1.6598 2.7397 0.0495 -0.7849 0.6566 208 LYS B CE 8827 N NZ . LYS B 208 ? 1.5262 1.5612 2.5438 -0.0006 -0.8358 0.6709 208 LYS B NZ 8828 N N . LYS B 209 ? 1.0656 1.2079 2.4300 0.1357 -0.4837 0.4981 209 LYS B N 8829 C CA . LYS B 209 ? 1.0672 1.2968 2.5292 0.1347 -0.4542 0.4756 209 LYS B CA 8830 C C . LYS B 209 ? 1.0573 1.2851 2.4202 0.0891 -0.4267 0.4385 209 LYS B C 8831 O O . LYS B 209 ? 1.1979 1.4953 2.6140 0.0719 -0.4221 0.4281 209 LYS B O 8832 C CB . LYS B 209 ? 0.9821 1.2194 2.5428 0.1819 -0.3861 0.4520 209 LYS B CB 8833 C CG . LYS B 209 ? 1.1123 1.3510 2.7664 0.2276 -0.3960 0.4798 209 LYS B CG 8834 C CD . LYS B 209 ? 1.1172 1.3351 2.8287 0.2708 -0.3174 0.4490 209 LYS B CD 8835 C CE . LYS B 209 ? 1.0671 1.3568 2.8598 0.2715 -0.2653 0.4200 209 LYS B CE 8836 N NZ . LYS B 209 ? 1.2759 1.6648 3.1760 0.2672 -0.2916 0.4433 209 LYS B NZ 8837 N N . GLN B 210 ? 1.0200 1.1689 2.2442 0.0701 -0.4075 0.4207 210 GLN B N 8838 C CA . GLN B 210 ? 1.0620 1.2007 2.1915 0.0335 -0.3748 0.3857 210 GLN B CA 8839 C C . GLN B 210 ? 1.0756 1.2438 2.1628 -0.0083 -0.4199 0.3978 210 GLN B C 8840 O O . GLN B 210 ? 1.0615 1.2115 2.1098 -0.0220 -0.4805 0.4326 210 GLN B O 8841 C CB . GLN B 210 ? 1.0543 1.1068 2.0565 0.0236 -0.3517 0.3733 210 GLN B CB 8842 C CG . GLN B 210 ? 1.0860 1.0976 2.1124 0.0561 -0.3083 0.3574 210 GLN B CG 8843 C CD . GLN B 210 ? 1.0591 1.1024 2.1474 0.0708 -0.2514 0.3192 210 GLN B CD 8844 O OE1 . GLN B 210 ? 1.0269 1.0903 2.0801 0.0474 -0.2257 0.2922 210 GLN B OE1 8845 N NE2 . GLN B 210 ? 0.9990 1.0391 2.1734 0.1109 -0.2290 0.3174 210 GLN B NE2 8846 N N . SER B 211 ? 1.0763 1.2808 2.1618 -0.0302 -0.3904 0.3689 211 SER B N 8847 C CA . SER B 211 ? 1.1004 1.3275 2.1439 -0.0730 -0.4279 0.3755 211 SER B CA 8848 C C . SER B 211 ? 1.1204 1.3090 2.0451 -0.1030 -0.3878 0.3416 211 SER B C 8849 O O . SER B 211 ? 1.0613 1.2256 1.9619 -0.0900 -0.3309 0.3122 211 SER B O 8850 C CB . SER B 211 ? 1.0387 1.3623 2.2225 -0.0735 -0.4413 0.3819 211 SER B CB 8851 O OG . SER B 211 ? 1.2960 1.6611 2.5993 -0.0440 -0.4832 0.4191 211 SER B OG 8852 N N . VAL B 212 ? 1.3659 1.5439 2.2133 -0.1435 -0.4201 0.3471 212 VAL B N 8853 C CA . VAL B 212 ? 1.1388 1.2718 1.8658 -0.1708 -0.3856 0.3199 212 VAL B CA 8854 C C . VAL B 212 ? 1.0466 1.2279 1.8197 -0.1807 -0.3457 0.2894 212 VAL B C 8855 O O . VAL B 212 ? 1.1428 1.3934 2.0193 -0.1861 -0.3628 0.2955 212 VAL B O 8856 C CB . VAL B 212 ? 1.2818 1.3647 1.8878 -0.2104 -0.4317 0.3368 212 VAL B CB 8857 C CG1 . VAL B 212 ? 1.2560 1.2612 1.7193 -0.2213 -0.3917 0.3190 212 VAL B CG1 8858 C CG2 . VAL B 212 ? 1.6686 1.7305 2.2696 -0.2063 -0.4947 0.3774 212 VAL B CG2 8859 N N . SER B 213 ? 1.0298 1.1751 1.7292 -0.1835 -0.2928 0.2593 213 SER B N 8860 C CA . SER B 213 ? 0.9688 1.1429 1.6843 -0.1960 -0.2529 0.2305 213 SER B CA 8861 C C . SER B 213 ? 1.0385 1.1602 1.6233 -0.2298 -0.2469 0.2195 213 SER B C 8862 O O . SER B 213 ? 1.2119 1.2776 1.6995 -0.2421 -0.2716 0.2343 213 SER B O 8863 C CB . SER B 213 ? 0.9245 1.0994 1.6719 -0.1666 -0.1929 0.2036 213 SER B CB 8864 O OG . SER B 213 ? 0.8764 1.0796 1.6457 -0.1772 -0.1550 0.1786 213 SER B OG 8865 N N . ARG B 214 ? 0.9854 1.1180 1.5623 -0.2436 -0.2107 0.1945 214 ARG B N 8866 C CA . ARG B 214 ? 0.9802 1.0588 1.4354 -0.2734 -0.2018 0.1840 214 ARG B CA 8867 C C . ARG B 214 ? 0.9348 0.9999 1.3593 -0.2691 -0.1430 0.1540 214 ARG B C 8868 O O . ARG B 214 ? 1.0037 1.1135 1.5033 -0.2635 -0.1160 0.1387 214 ARG B O 8869 C CB . ARG B 214 ? 1.1086 1.2036 1.5632 -0.3137 -0.2423 0.1931 214 ARG B CB 8870 C CG . ARG B 214 ? 1.0977 1.1230 1.4156 -0.3466 -0.2351 0.1826 214 ARG B CG 8871 C CD . ARG B 214 ? 1.0791 1.1248 1.4088 -0.3909 -0.2693 0.1858 214 ARG B CD 8872 N NE . ARG B 214 ? 1.1537 1.1158 1.3376 -0.4242 -0.2671 0.1772 214 ARG B NE 8873 C CZ . ARG B 214 ? 1.3201 1.2752 1.4798 -0.4695 -0.2923 0.1757 214 ARG B CZ 8874 N NH1 . ARG B 214 ? 1.4276 1.4657 1.7117 -0.4881 -0.3228 0.1845 214 ARG B NH1 8875 N NH2 . ARG B 214 ? 1.6051 1.4686 1.6189 -0.4967 -0.2853 0.1662 214 ARG B NH2 8876 N N . ASN B 215 ? 0.9504 0.9517 1.2638 -0.2709 -0.1223 0.1479 215 ASN B N 8877 C CA . ASN B 215 ? 0.9237 0.9029 1.1900 -0.2720 -0.0754 0.1244 215 ASN B CA 8878 C C . ASN B 215 ? 0.9729 0.8905 1.1214 -0.2978 -0.0756 0.1245 215 ASN B C 8879 O O . ASN B 215 ? 1.0317 0.9197 1.1300 -0.3151 -0.1104 0.1410 215 ASN B O 8880 C CB . ASN B 215 ? 0.8935 0.8562 1.1513 -0.2418 -0.0431 0.1171 215 ASN B CB 8881 C CG . ASN B 215 ? 0.9553 0.8654 1.1322 -0.2361 -0.0459 0.1318 215 ASN B CG 8882 O OD1 . ASN B 215 ? 1.0064 0.8827 1.1243 -0.2304 -0.0160 0.1256 215 ASN B OD1 8883 N ND2 . ASN B 215 ? 1.0031 0.9063 1.1799 -0.2366 -0.0805 0.1538 215 ASN B ND2 8884 N N . ARG B 216 ? 0.9555 0.8457 1.0526 -0.3005 -0.0369 0.1068 216 ARG B N 8885 C CA . ARG B 216 ? 0.9923 0.8170 0.9769 -0.3236 -0.0315 0.1051 216 ARG B CA 8886 C C . ARG B 216 ? 1.0226 0.7820 0.9126 -0.3087 -0.0160 0.1146 216 ARG B C 8887 O O . ARG B 216 ? 1.1748 0.8758 0.9749 -0.3262 -0.0283 0.1233 216 ARG B O 8888 C CB . ARG B 216 ? 1.0533 0.8695 1.0192 -0.3331 0.0041 0.0846 216 ARG B CB 8889 C CG . ARG B 216 ? 1.0853 0.8266 0.9344 -0.3579 0.0111 0.0818 216 ARG B CG 8890 C CD . ARG B 216 ? 1.1270 0.8626 0.9664 -0.3752 0.0377 0.0639 216 ARG B CD 8891 N NE . ARG B 216 ? 1.3127 1.0931 1.2146 -0.4095 0.0122 0.0617 216 ARG B NE 8892 C CZ . ARG B 216 ? 1.2192 1.0732 1.2318 -0.4062 0.0191 0.0557 216 ARG B CZ 8893 N NH1 . ARG B 216 ? 0.9588 0.8386 1.0160 -0.3716 0.0487 0.0484 216 ARG B NH1 8894 N NH2 . ARG B 216 ? 1.0656 0.9645 1.1431 -0.4386 -0.0026 0.0576 216 ARG B NH2 8895 N N . ASP B 217 ? 1.0290 0.7956 0.9379 -0.2780 0.0116 0.1140 217 ASP B N 8896 C CA . ASP B 217 ? 1.0232 0.7358 0.8555 -0.2628 0.0363 0.1238 217 ASP B CA 8897 C C . ASP B 217 ? 1.0423 0.7568 0.8902 -0.2463 0.0243 0.1441 217 ASP B C 8898 O O . ASP B 217 ? 1.1387 0.9013 1.0696 -0.2346 0.0087 0.1469 217 ASP B O 8899 C CB . ASP B 217 ? 1.0203 0.7342 0.8555 -0.2432 0.0752 0.1136 217 ASP B CB 8900 C CG . ASP B 217 ? 1.3295 1.0951 1.2511 -0.2221 0.0752 0.1118 217 ASP B CG 8901 O OD1 . ASP B 217 ? 1.6770 1.4828 1.6670 -0.2230 0.0506 0.1120 217 ASP B OD1 8902 O OD2 . ASP B 217 ? 1.3275 1.0899 1.2474 -0.2049 0.0984 0.1111 217 ASP B OD2 8903 N N . ALA B 218 ? 1.1360 0.7907 0.8982 -0.2452 0.0365 0.1583 218 ALA B N 8904 C CA . ALA B 218 ? 1.2554 0.8970 1.0114 -0.2358 0.0268 0.1807 218 ALA B CA 8905 C C . ALA B 218 ? 1.1490 0.8328 0.9832 -0.2101 0.0382 0.1878 218 ALA B C 8906 O O . ALA B 218 ? 1.2267 0.9315 1.1075 -0.2065 0.0133 0.1994 218 ALA B O 8907 C CB . ALA B 218 ? 1.1501 0.7103 0.7891 -0.2377 0.0522 0.1929 218 ALA B CB 8908 N N . PRO B 219 ? 0.9450 0.6370 0.7918 -0.1937 0.0725 0.1830 219 PRO B N 8909 C CA . PRO B 219 ? 1.0416 0.7740 0.9655 -0.1766 0.0731 0.1893 219 PRO B CA 8910 C C . PRO B 219 ? 1.0665 0.8472 1.0699 -0.1783 0.0470 0.1740 219 PRO B C 8911 O O . PRO B 219 ? 0.9099 0.7071 0.9258 -0.1841 0.0488 0.1537 219 PRO B O 8912 C CB . PRO B 219 ? 1.1886 0.9229 1.1113 -0.1628 0.1067 0.1871 219 PRO B CB 8913 C CG . PRO B 219 ? 1.1585 0.8646 1.0216 -0.1712 0.1205 0.1722 219 PRO B CG 8914 C CD . PRO B 219 ? 1.1805 0.8446 0.9767 -0.1895 0.1075 0.1751 219 PRO B CD 8915 N N . GLU B 220 ? 1.0331 0.8307 1.0868 -0.1726 0.0269 0.1844 220 GLU B N 8916 C CA . GLU B 220 ? 1.0071 0.8413 1.1327 -0.1711 0.0044 0.1723 220 GLU B CA 8917 C C . GLU B 220 ? 0.9478 0.8041 1.1300 -0.1589 0.0131 0.1603 220 GLU B C 8918 O O . GLU B 220 ? 1.1144 0.9930 1.3507 -0.1546 0.0039 0.1471 220 GLU B O 8919 C CB . GLU B 220 ? 0.9001 0.7314 1.0433 -0.1718 -0.0273 0.1910 220 GLU B CB 8920 C CG . GLU B 220 ? 0.9372 0.7837 1.0931 -0.1840 -0.0563 0.1886 220 GLU B CG 8921 C CD . GLU B 220 ? 1.1222 0.9481 1.2096 -0.2039 -0.0504 0.1813 220 GLU B CD 8922 O OE1 . GLU B 220 ? 1.2807 1.0643 1.2946 -0.2170 -0.0627 0.1964 220 GLU B OE1 8923 O OE2 . GLU B 220 ? 1.3156 1.1593 1.4144 -0.2079 -0.0329 0.1603 220 GLU B OE2 8924 N N . GLY B 221 ? 0.8419 0.6895 1.0112 -0.1537 0.0311 0.1656 221 GLY B N 8925 C CA . GLY B 221 ? 1.3154 1.1750 1.5247 -0.1479 0.0336 0.1547 221 GLY B CA 8926 C C . GLY B 221 ? 1.2907 1.1537 1.5520 -0.1431 0.0151 0.1561 221 GLY B C 8927 O O . GLY B 221 ? 0.7596 0.6285 1.0524 -0.1393 0.0134 0.1360 221 GLY B O 8928 N N . GLY B 222 ? 1.1601 1.0119 1.4250 -0.1424 0.0050 0.1800 222 GLY B N 8929 C CA . GLY B 222 ? 1.0052 0.8508 1.3140 -0.1375 -0.0123 0.1847 222 GLY B CA 8930 C C . GLY B 222 ? 1.1031 0.9414 1.4331 -0.1398 -0.0100 0.1819 222 GLY B C 8931 O O . GLY B 222 ? 1.0993 0.9229 1.4608 -0.1372 -0.0220 0.1806 222 GLY B O 8932 N N . PHE B 223 ? 1.1544 0.9997 1.4664 -0.1454 0.0031 0.1823 223 PHE B N 8933 C CA . PHE B 223 ? 0.9009 0.7427 1.2324 -0.1529 -0.0015 0.1831 223 PHE B CA 8934 C C . PHE B 223 ? 0.7940 0.6208 1.1328 -0.1536 -0.0085 0.1534 223 PHE B C 8935 O O . PHE B 223 ? 0.8191 0.6272 1.1718 -0.1624 -0.0208 0.1514 223 PHE B O 8936 C CB . PHE B 223 ? 1.0415 0.9001 1.3585 -0.1562 0.0115 0.1936 223 PHE B CB 8937 C CG . PHE B 223 ? 0.9524 0.8181 1.2694 -0.1553 0.0248 0.2264 223 PHE B CG 8938 C CD1 . PHE B 223 ? 0.8885 0.7402 1.2109 -0.1560 0.0216 0.2445 223 PHE B CD1 8939 C CD2 . PHE B 223 ? 0.7494 0.6311 1.0592 -0.1521 0.0436 0.2407 223 PHE B CD2 8940 C CE1 . PHE B 223 ? 0.8236 0.6734 1.1366 -0.1556 0.0405 0.2747 223 PHE B CE1 8941 C CE2 . PHE B 223 ? 0.6626 0.5467 0.9724 -0.1485 0.0650 0.2711 223 PHE B CE2 8942 C CZ . PHE B 223 ? 0.7263 0.5925 1.0340 -0.1513 0.0652 0.2874 223 PHE B CZ 8943 N N . ASP B 224 ? 0.7449 0.5749 1.0703 -0.1465 0.0012 0.1304 224 ASP B N 8944 C CA . ASP B 224 ? 0.8476 0.6563 1.1747 -0.1440 0.0039 0.1014 224 ASP B CA 8945 C C . ASP B 224 ? 1.0757 0.8622 1.4371 -0.1368 -0.0058 0.1011 224 ASP B C 8946 O O . ASP B 224 ? 0.9861 0.7362 1.3446 -0.1394 -0.0083 0.0857 224 ASP B O 8947 C CB . ASP B 224 ? 0.9798 0.8015 1.2961 -0.1374 0.0222 0.0812 224 ASP B CB 8948 C CG . ASP B 224 ? 0.9766 0.7966 1.2482 -0.1449 0.0343 0.0698 224 ASP B CG 8949 O OD1 . ASP B 224 ? 0.8108 0.6134 1.0625 -0.1535 0.0260 0.0700 224 ASP B OD1 8950 O OD2 . ASP B 224 ? 1.2649 1.0994 1.5215 -0.1438 0.0495 0.0622 224 ASP B OD2 8951 N N . ALA B 225 ? 1.0885 0.8894 1.4752 -0.1280 -0.0124 0.1191 225 ALA B N 8952 C CA . ALA B 225 ? 1.0587 0.8386 1.4807 -0.1172 -0.0229 0.1242 225 ALA B CA 8953 C C . ALA B 225 ? 0.8971 0.6452 1.3194 -0.1281 -0.0362 0.1386 225 ALA B C 8954 O O . ALA B 225 ? 1.0771 0.7862 1.5121 -0.1243 -0.0401 0.1296 225 ALA B O 8955 C CB . ALA B 225 ? 1.1006 0.9028 1.5429 -0.1078 -0.0337 0.1451 225 ALA B CB 8956 N N . ILE B 226 ? 0.7639 0.5261 1.1733 -0.1418 -0.0401 0.1617 226 ILE B N 8957 C CA . ILE B 226 ? 0.8070 0.5483 1.2253 -0.1570 -0.0512 0.1799 226 ILE B CA 8958 C C . ILE B 226 ? 0.9946 0.7073 1.4053 -0.1708 -0.0576 0.1589 226 ILE B C 8959 O O . ILE B 226 ? 1.2880 0.9611 1.7074 -0.1805 -0.0701 0.1605 226 ILE B O 8960 C CB . ILE B 226 ? 0.7361 0.5061 1.1493 -0.1679 -0.0457 0.2087 226 ILE B CB 8961 C CG1 . ILE B 226 ? 0.7373 0.5123 1.1413 -0.1589 -0.0415 0.2325 226 ILE B CG1 8962 C CG2 . ILE B 226 ? 0.7566 0.5159 1.1913 -0.1882 -0.0553 0.2266 226 ILE B CG2 8963 C CD1 . ILE B 226 ? 0.7340 0.5244 1.1263 -0.1669 -0.0269 0.2620 226 ILE B CD1 8964 N N . MET B 227 ? 0.8159 0.5408 1.2020 -0.1735 -0.0506 0.1393 227 MET B N 8965 C CA . MET B 227 ? 0.9109 0.6015 1.2725 -0.1890 -0.0600 0.1184 227 MET B CA 8966 C C . MET B 227 ? 0.9888 0.6210 1.3382 -0.1815 -0.0566 0.0911 227 MET B C 8967 O O . MET B 227 ? 1.1933 0.7752 1.5314 -0.1972 -0.0715 0.0859 227 MET B O 8968 C CB . MET B 227 ? 1.1281 0.8374 1.4562 -0.1901 -0.0515 0.1037 227 MET B CB 8969 C CG . MET B 227 ? 1.1721 0.8365 1.4579 -0.2070 -0.0636 0.0808 227 MET B CG 8970 S SD . MET B 227 ? 1.0836 0.7363 1.3841 -0.2400 -0.1012 0.1026 227 MET B SD 8971 C CE . MET B 227 ? 0.8196 0.5511 1.1586 -0.2399 -0.1009 0.1399 227 MET B CE 8972 N N . GLN B 228 ? 1.0066 0.6438 1.3603 -0.1578 -0.0354 0.0747 228 GLN B N 8973 C CA . GLN B 228 ? 1.0482 0.6326 1.3958 -0.1438 -0.0216 0.0482 228 GLN B CA 8974 C C . GLN B 228 ? 1.1835 0.7328 1.5611 -0.1364 -0.0312 0.0608 228 GLN B C 8975 O O . GLN B 228 ? 1.0470 0.5289 1.4060 -0.1347 -0.0268 0.0419 228 GLN B O 8976 C CB . GLN B 228 ? 0.9756 0.5886 1.3401 -0.1193 0.0057 0.0338 228 GLN B CB 8977 C CG . GLN B 228 ? 0.9854 0.6151 1.3101 -0.1265 0.0206 0.0163 228 GLN B CG 8978 C CD . GLN B 228 ? 1.1067 0.6737 1.3663 -0.1428 0.0218 -0.0089 228 GLN B CD 8979 O OE1 . GLN B 228 ? 1.1121 0.6146 1.3526 -0.1389 0.0303 -0.0284 228 GLN B OE1 8980 N NE2 . GLN B 228 ? 1.2559 0.8346 1.4752 -0.1612 0.0121 -0.0077 228 GLN B NE2 8981 N N . ALA B 229 ? 1.1168 0.7022 1.5316 -0.1322 -0.0429 0.0927 229 ALA B N 8982 C CA . ALA B 229 ? 0.9903 0.5407 1.4299 -0.1258 -0.0539 0.1099 229 ALA B CA 8983 C C . ALA B 229 ? 1.1663 0.6677 1.5849 -0.1547 -0.0714 0.1147 229 ALA B C 8984 O O . ALA B 229 ? 1.3495 0.7964 1.7737 -0.1538 -0.0781 0.1196 229 ALA B O 8985 C CB . ALA B 229 ? 0.9112 0.5055 1.3804 -0.1184 -0.0635 0.1446 229 ALA B CB 8986 N N . THR B 230 ? 1.1590 0.6800 1.5565 -0.1812 -0.0805 0.1151 230 THR B N 8987 C CA . THR B 230 ? 1.1582 0.6452 1.5445 -0.2149 -0.1029 0.1227 230 THR B CA 8988 C C . THR B 230 ? 1.1696 0.5852 1.5039 -0.2281 -0.1070 0.0873 230 THR B C 8989 O O . THR B 230 ? 1.3131 0.6549 1.6304 -0.2379 -0.1152 0.0796 230 THR B O 8990 C CB . THR B 230 ? 1.1870 0.7356 1.5876 -0.2370 -0.1139 0.1463 230 THR B CB 8991 O OG1 . THR B 230 ? 0.9375 0.5379 1.3716 -0.2251 -0.1043 0.1777 230 THR B OG1 8992 C CG2 . THR B 230 ? 1.2321 0.7558 1.6383 -0.2750 -0.1410 0.1591 230 THR B CG2 8993 N N . VAL B 231 ? 1.2261 0.6547 1.5255 -0.2294 -0.1006 0.0659 231 VAL B N 8994 C CA . VAL B 231 ? 1.3473 0.7032 1.5787 -0.2469 -0.1064 0.0333 231 VAL B CA 8995 C C . VAL B 231 ? 1.3286 0.6036 1.5258 -0.2247 -0.0795 0.0006 231 VAL B C 8996 O O . VAL B 231 ? 1.7011 0.8891 1.8301 -0.2412 -0.0832 -0.0264 231 VAL B O 8997 C CB . VAL B 231 ? 1.4447 0.8312 1.6403 -0.2508 -0.1031 0.0206 231 VAL B CB 8998 C CG1 . VAL B 231 ? 1.3809 0.8377 1.6091 -0.2719 -0.1292 0.0529 231 VAL B CG1 8999 C CG2 . VAL B 231 ? 1.3452 0.7707 1.5532 -0.2151 -0.0657 0.0095 231 VAL B CG2 9000 N N . CYS B 232 ? 1.2084 0.5080 1.4512 -0.1872 -0.0527 0.0039 232 CYS B N 9001 C CA . CYS B 232 ? 1.4396 0.6686 1.6676 -0.1602 -0.0229 -0.0222 232 CYS B CA 9002 C C . CYS B 232 ? 1.5842 0.7730 1.8440 -0.1534 -0.0322 -0.0048 232 CYS B C 9003 O O . CYS B 232 ? 1.7889 1.0296 2.1128 -0.1332 -0.0339 0.0229 232 CYS B O 9004 C CB . CYS B 232 ? 1.6860 0.9675 1.9531 -0.1215 0.0130 -0.0292 232 CYS B CB 9005 S SG . CYS B 232 ? 1.3280 0.6480 1.5535 -0.1283 0.0303 -0.0499 232 CYS B SG 9006 N N . ASP B 233 ? 1.5758 0.6633 1.7815 -0.1725 -0.0399 -0.0211 233 ASP B N 9007 C CA . ASP B 233 ? 1.6107 0.6423 1.8336 -0.1720 -0.0502 -0.0057 233 ASP B CA 9008 C C . ASP B 233 ? 1.7526 0.7333 1.9933 -0.1249 -0.0144 -0.0181 233 ASP B C 9009 O O . ASP B 233 ? 1.8622 0.8512 2.1572 -0.1037 -0.0177 0.0079 233 ASP B O 9010 C CB . ASP B 233 ? 1.9078 0.8457 2.0622 -0.2180 -0.0772 -0.0170 233 ASP B CB 9011 C CG . ASP B 233 ? 1.9424 0.9344 2.0898 -0.2640 -0.1147 -0.0028 233 ASP B CG 9012 O OD1 . ASP B 233 ? 1.4830 0.5805 1.6913 -0.2612 -0.1220 0.0269 233 ASP B OD1 9013 O OD2 . ASP B 233 ? 2.2936 1.2246 2.3731 -0.3014 -0.1356 -0.0208 233 ASP B OD2 9014 N N . GLU B 234 ? 1.8980 0.8245 2.0930 -0.1072 0.0215 -0.0558 234 GLU B N 9015 C CA . GLU B 234 ? 1.8787 0.7443 2.0891 -0.0610 0.0628 -0.0702 234 GLU B CA 9016 C C . GLU B 234 ? 1.8503 0.8154 2.1629 -0.0145 0.0815 -0.0496 234 GLU B C 9017 O O . GLU B 234 ? 2.0098 0.9564 2.3756 0.0239 0.0961 -0.0381 234 GLU B O 9018 C CB . GLU B 234 ? 1.9935 0.7649 2.1174 -0.0567 0.1032 -0.1175 234 GLU B CB 9019 C CG . GLU B 234 ? 2.3397 1.1747 2.4575 -0.0504 0.1286 -0.1343 234 GLU B CG 9020 C CD . GLU B 234 ? 2.3177 1.2033 2.3971 -0.0975 0.0888 -0.1289 234 GLU B CD 9021 O OE1 . GLU B 234 ? 2.5190 1.3667 2.5566 -0.1391 0.0465 -0.1218 234 GLU B OE1 9022 O OE2 . GLU B 234 ? 1.8476 0.8116 1.9438 -0.0927 0.0998 -0.1298 234 GLU B OE2 9023 N N . LYS B 235 ? 1.6476 0.7153 1.9873 -0.0190 0.0783 -0.0435 235 LYS B N 9024 C CA . LYS B 235 ? 1.5414 0.7070 1.9739 0.0163 0.0888 -0.0234 235 LYS B CA 9025 C C . LYS B 235 ? 1.4326 0.6451 1.9245 0.0190 0.0518 0.0203 235 LYS B C 9026 O O . LYS B 235 ? 1.4467 0.6743 2.0068 0.0555 0.0561 0.0389 235 LYS B O 9027 C CB . LYS B 235 ? 1.4913 0.7421 1.9233 0.0039 0.0927 -0.0290 235 LYS B CB 9028 C CG . LYS B 235 ? 1.5371 0.7565 1.9294 0.0135 0.1391 -0.0676 235 LYS B CG 9029 C CD . LYS B 235 ? 1.5650 0.7918 2.0298 0.0629 0.1829 -0.0716 235 LYS B CD 9030 C CE . LYS B 235 ? 1.6489 0.8389 2.0716 0.0729 0.2386 -0.1096 235 LYS B CE 9031 N NZ . LYS B 235 ? 1.6769 0.8842 2.1873 0.1234 0.2873 -0.1103 235 LYS B NZ 9032 N N . ILE B 236 ? 1.3774 0.6116 1.8433 -0.0193 0.0161 0.0387 236 ILE B N 9033 C CA . ILE B 236 ? 1.3862 0.6555 1.8912 -0.0219 -0.0154 0.0805 236 ILE B CA 9034 C C . ILE B 236 ? 1.4562 0.6397 1.9613 -0.0124 -0.0213 0.0912 236 ILE B C 9035 O O . ILE B 236 ? 1.4357 0.6323 1.9893 0.0111 -0.0327 0.1213 236 ILE B O 9036 C CB . ILE B 236 ? 1.3824 0.6893 1.8594 -0.0647 -0.0427 0.0973 236 ILE B CB 9037 C CG1 . ILE B 236 ? 1.2284 0.6081 1.6973 -0.0732 -0.0351 0.0856 236 ILE B CG1 9038 C CG2 . ILE B 236 ? 1.2849 0.6232 1.7937 -0.0659 -0.0672 0.1406 236 ILE B CG2 9039 C CD1 . ILE B 236 ? 1.2799 0.7329 1.8002 -0.0446 -0.0263 0.0943 236 ILE B CD1 9040 N N . GLY B 237 ? 1.4201 0.5086 1.8646 -0.0317 -0.0153 0.0668 237 GLY B N 9041 C CA . GLY B 237 ? 1.6611 0.6518 2.0940 -0.0258 -0.0183 0.0732 237 GLY B CA 9042 C C . GLY B 237 ? 1.8745 0.8465 2.2869 -0.0668 -0.0531 0.1007 237 GLY B C 9043 O O . GLY B 237 ? 1.9786 0.9090 2.3867 -0.0580 -0.0593 0.1192 237 GLY B O 9044 N N . TRP B 238 ? 1.8635 0.8814 2.2563 -0.1094 -0.0722 0.1039 238 TRP B N 9045 C CA . TRP B 238 ? 1.4809 0.5056 1.8525 -0.1495 -0.0974 0.1286 238 TRP B CA 9046 C C . TRP B 238 ? 1.6015 0.5225 1.9151 -0.1670 -0.0980 0.1157 238 TRP B C 9047 O O . TRP B 238 ? 1.6805 0.5253 1.9410 -0.1725 -0.0867 0.0796 238 TRP B O 9048 C CB . TRP B 238 ? 1.4648 0.5502 1.8262 -0.1897 -0.1123 0.1281 238 TRP B CB 9049 C CG . TRP B 238 ? 1.4429 0.6270 1.8513 -0.1796 -0.1119 0.1457 238 TRP B CG 9050 C CD1 . TRP B 238 ? 1.3358 0.5716 1.7363 -0.1723 -0.1000 0.1236 238 TRP B CD1 9051 C CD2 . TRP B 238 ? 1.3856 0.6347 1.8301 -0.1739 -0.1178 0.1846 238 TRP B CD2 9052 N NE1 . TRP B 238 ? 1.2218 0.5475 1.6554 -0.1634 -0.0995 0.1463 238 TRP B NE1 9053 C CE2 . TRP B 238 ? 1.1768 0.5086 1.6352 -0.1645 -0.1104 0.1835 238 TRP B CE2 9054 C CE3 . TRP B 238 ? 1.4868 0.7328 1.9357 -0.1745 -0.1246 0.2167 238 TRP B CE3 9055 C CZ2 . TRP B 238 ? 1.1142 0.5092 1.5940 -0.1590 -0.1126 0.2151 238 TRP B CZ2 9056 C CZ3 . TRP B 238 ? 1.2131 0.5220 1.6829 -0.1688 -0.1264 0.2488 238 TRP B CZ3 9057 C CH2 . TRP B 238 ? 1.1344 0.5087 1.6220 -0.1628 -0.1219 0.2496 238 TRP B CH2 9058 N N . ARG B 239 ? 1.7311 0.6423 2.0473 -0.1770 -0.1087 0.1447 239 ARG B N 9059 C CA . ARG B 239 ? 1.8145 0.6284 2.0778 -0.1980 -0.1088 0.1363 239 ARG B CA 9060 C C . ARG B 239 ? 1.7454 0.5843 1.9945 -0.2541 -0.1292 0.1454 239 ARG B C 9061 O O . ARG B 239 ? 1.6755 0.5942 1.9633 -0.2675 -0.1402 0.1777 239 ARG B O 9062 C CB . ARG B 239 ? 1.8486 0.6233 2.1234 -0.1708 -0.1045 0.1620 239 ARG B CB 9063 C CG . ARG B 239 ? 1.9396 0.6916 2.2404 -0.1111 -0.0864 0.1572 239 ARG B CG 9064 C CD . ARG B 239 ? 1.8645 0.5823 2.1752 -0.0867 -0.0886 0.1879 239 ARG B CD 9065 N NE . ARG B 239 ? 1.7945 0.5901 2.1364 -0.0989 -0.1080 0.2288 239 ARG B NE 9066 C CZ . ARG B 239 ? 1.9129 0.6847 2.2517 -0.0914 -0.1148 0.2607 239 ARG B CZ 9067 N NH1 . ARG B 239 ? 2.0374 0.7129 2.3492 -0.0707 -0.1054 0.2579 239 ARG B NH1 9068 N NH2 . ARG B 239 ? 1.8125 0.6494 2.1673 -0.1041 -0.1282 0.2952 239 ARG B NH2 9069 N N . ASN B 240 ? 1.8287 0.6008 2.0250 -0.2859 -0.1326 0.1172 240 ASN B N 9070 C CA . ASN B 240 ? 1.9012 0.6939 2.0945 -0.3386 -0.1552 0.1273 240 ASN B CA 9071 C C . ASN B 240 ? 2.0582 0.8217 2.2604 -0.3464 -0.1547 0.1554 240 ASN B C 9072 O O . ASN B 240 ? 2.2571 0.9496 2.4437 -0.3155 -0.1376 0.1562 240 ASN B O 9073 C CB . ASN B 240 ? 1.9542 0.6783 2.0879 -0.3705 -0.1638 0.0900 240 ASN B CB 9074 C CG . ASN B 240 ? 2.2585 0.8535 2.3367 -0.3499 -0.1393 0.0599 240 ASN B CG 9075 O OD1 . ASN B 240 ? 2.3869 0.9494 2.4697 -0.3017 -0.1122 0.0579 240 ASN B OD1 9076 N ND2 . ASN B 240 ? 2.4126 0.9350 2.4418 -0.3845 -0.1499 0.0376 240 ASN B ND2 9077 N N . ASP B 241 ? 2.0263 0.8445 2.2558 -0.3858 -0.1718 0.1797 241 ASP B N 9078 C CA . ASP B 241 ? 2.1218 0.9259 2.3649 -0.3964 -0.1692 0.2109 241 ASP B CA 9079 C C . ASP B 241 ? 1.9499 0.7803 2.2175 -0.3540 -0.1545 0.2390 241 ASP B C 9080 O O . ASP B 241 ? 1.9319 0.6978 2.1830 -0.3374 -0.1447 0.2511 241 ASP B O 9081 C CB . ASP B 241 ? 2.1716 0.8540 2.3650 -0.4086 -0.1645 0.1943 241 ASP B CB 9082 C CG . ASP B 241 ? 2.2936 0.9535 2.4650 -0.4596 -0.1860 0.1735 241 ASP B CG 9083 O OD1 . ASP B 241 ? 2.1411 0.7694 2.2754 -0.4604 -0.1905 0.1380 241 ASP B OD1 9084 O OD2 . ASP B 241 ? 2.4052 1.0784 2.5955 -0.4994 -0.1995 0.1935 241 ASP B OD2 9085 N N . ALA B 242 ? 1.7531 0.6762 2.0577 -0.3369 -0.1545 0.2496 242 ALA B N 9086 C CA . ALA B 242 ? 1.7021 0.6620 2.0301 -0.3012 -0.1455 0.2776 242 ALA B CA 9087 C C . ALA B 242 ? 1.5913 0.6619 1.9586 -0.3059 -0.1459 0.2953 242 ALA B C 9088 O O . ALA B 242 ? 1.6030 0.7210 1.9825 -0.3218 -0.1522 0.2800 242 ALA B O 9089 C CB . ALA B 242 ? 1.7066 0.6298 2.0283 -0.2525 -0.1386 0.2618 242 ALA B CB 9090 N N . SER B 243 ? 1.5627 0.6677 1.9429 -0.2915 -0.1379 0.3278 243 SER B N 9091 C CA . SER B 243 ? 1.4716 0.6698 1.8791 -0.2925 -0.1315 0.3449 243 SER B CA 9092 C C . SER B 243 ? 1.4506 0.6838 1.8682 -0.2609 -0.1322 0.3304 243 SER B C 9093 O O . SER B 243 ? 1.5969 0.8050 2.0097 -0.2271 -0.1333 0.3322 243 SER B O 9094 C CB . SER B 243 ? 1.4837 0.6922 1.8850 -0.2891 -0.1190 0.3825 243 SER B CB 9095 O OG . SER B 243 ? 1.6360 0.8252 2.0362 -0.3228 -0.1136 0.3977 243 SER B OG 9096 N N . HIS B 244 ? 1.3343 0.6271 1.7697 -0.2719 -0.1326 0.3179 244 HIS B N 9097 C CA . HIS B 244 ? 1.2700 0.5951 1.7146 -0.2470 -0.1315 0.3020 244 HIS B CA 9098 C C . HIS B 244 ? 1.2010 0.5965 1.6574 -0.2380 -0.1207 0.3253 244 HIS B C 9099 O O . HIS B 244 ? 1.4265 0.8755 1.8947 -0.2570 -0.1129 0.3354 244 HIS B O 9100 C CB . HIS B 244 ? 1.3178 0.6515 1.7619 -0.2635 -0.1382 0.2710 244 HIS B CB 9101 C CG . HIS B 244 ? 1.3364 0.5889 1.7512 -0.2759 -0.1471 0.2445 244 HIS B CG 9102 N ND1 . HIS B 244 ? 1.5059 0.7501 1.9045 -0.3057 -0.1590 0.2224 244 HIS B ND1 9103 C CD2 . HIS B 244 ? 1.4160 0.5854 1.8081 -0.2623 -0.1453 0.2367 244 HIS B CD2 9104 C CE1 . HIS B 244 ? 1.4495 0.6037 1.8090 -0.3123 -0.1628 0.2000 244 HIS B CE1 9105 N NE2 . HIS B 244 ? 1.4864 0.5931 1.8428 -0.2848 -0.1520 0.2079 244 HIS B NE2 9106 N N . LEU B 245 ? 1.1909 0.5834 1.6434 -0.2083 -0.1204 0.3346 245 LEU B N 9107 C CA . LEU B 245 ? 1.1446 0.5873 1.5914 -0.2003 -0.1112 0.3558 245 LEU B CA 9108 C C . LEU B 245 ? 1.2770 0.7462 1.7358 -0.1784 -0.1146 0.3415 245 LEU B C 9109 O O . LEU B 245 ? 1.4498 0.8928 1.9194 -0.1537 -0.1257 0.3362 245 LEU B O 9110 C CB . LEU B 245 ? 1.1949 0.6084 1.6144 -0.1906 -0.1118 0.3863 245 LEU B CB 9111 C CG . LEU B 245 ? 1.2564 0.6392 1.6607 -0.2123 -0.1038 0.4044 245 LEU B CG 9112 C CD1 . LEU B 245 ? 1.3116 0.6611 1.6765 -0.2013 -0.1029 0.4349 245 LEU B CD1 9113 C CD2 . LEU B 245 ? 1.2266 0.6588 1.6434 -0.2397 -0.0850 0.4095 245 LEU B CD2 9114 N N . LEU B 246 ? 1.2700 0.7923 1.7319 -0.1867 -0.1039 0.3366 246 LEU B N 9115 C CA . LEU B 246 ? 1.1168 0.6688 1.5837 -0.1694 -0.1036 0.3234 246 LEU B CA 9116 C C . LEU B 246 ? 1.0899 0.6721 1.5280 -0.1661 -0.0950 0.3470 246 LEU B C 9117 O O . LEU B 246 ? 1.2709 0.8818 1.6983 -0.1806 -0.0771 0.3575 246 LEU B O 9118 C CB . LEU B 246 ? 0.9505 0.5346 1.4243 -0.1781 -0.0965 0.2926 246 LEU B CB 9119 C CG . LEU B 246 ? 0.8969 0.5176 1.3645 -0.1584 -0.0907 0.2660 246 LEU B CG 9120 C CD1 . LEU B 246 ? 0.9194 0.5149 1.4023 -0.1331 -0.0974 0.2481 246 LEU B CD1 9121 C CD2 . LEU B 246 ? 0.9802 0.6245 1.4442 -0.1708 -0.0836 0.2414 246 LEU B CD2 9122 N N . VAL B 247 ? 0.9834 0.5567 1.4068 -0.1462 -0.1078 0.3551 247 VAL B N 9123 C CA . VAL B 247 ? 1.2173 0.8009 1.5955 -0.1458 -0.1047 0.3774 247 VAL B CA 9124 C C . VAL B 247 ? 1.2249 0.8527 1.5944 -0.1359 -0.1042 0.3554 247 VAL B C 9125 O O . VAL B 247 ? 1.2045 0.8461 1.6031 -0.1195 -0.1185 0.3354 247 VAL B O 9126 C CB . VAL B 247 ? 1.1987 0.7379 1.5544 -0.1362 -0.1269 0.4064 247 VAL B CB 9127 C CG1 . VAL B 247 ? 1.3222 0.8491 1.7230 -0.1133 -0.1510 0.3937 247 VAL B CG1 9128 C CG2 . VAL B 247 ? 1.5175 1.0615 1.8153 -0.1348 -0.1325 0.4220 247 VAL B CG2 9129 N N . PHE B 248 ? 1.1785 0.8259 1.5095 -0.1458 -0.0842 0.3603 248 PHE B N 9130 C CA . PHE B 248 ? 0.9575 0.6414 1.2740 -0.1416 -0.0788 0.3389 248 PHE B CA 9131 C C . PHE B 248 ? 1.0538 0.7237 1.3055 -0.1430 -0.0834 0.3559 248 PHE B C 9132 O O . PHE B 248 ? 1.3543 0.9973 1.5544 -0.1524 -0.0657 0.3797 248 PHE B O 9133 C CB . PHE B 248 ? 0.8473 0.5593 1.1687 -0.1511 -0.0511 0.3270 248 PHE B CB 9134 C CG . PHE B 248 ? 0.9717 0.7149 1.2771 -0.1471 -0.0429 0.3038 248 PHE B CG 9135 C CD1 . PHE B 248 ? 0.9691 0.7348 1.3080 -0.1407 -0.0490 0.2727 248 PHE B CD1 9136 C CD2 . PHE B 248 ? 1.1192 0.8610 1.3695 -0.1505 -0.0251 0.3129 248 PHE B CD2 9137 C CE1 . PHE B 248 ? 0.8350 0.6254 1.1569 -0.1393 -0.0395 0.2528 248 PHE B CE1 9138 C CE2 . PHE B 248 ? 0.9078 0.6706 1.1391 -0.1486 -0.0172 0.2919 248 PHE B CE2 9139 C CZ . PHE B 248 ? 0.9363 0.7257 1.2058 -0.1439 -0.0253 0.2626 248 PHE B CZ 9140 N N . THR B 249 ? 0.9438 0.6287 1.1961 -0.1355 -0.1062 0.3443 249 THR B N 9141 C CA . THR B 249 ? 1.1218 0.7874 1.3064 -0.1418 -0.1201 0.3590 249 THR B CA 9142 C C . THR B 249 ? 1.0629 0.7584 1.2310 -0.1461 -0.1155 0.3357 249 THR B C 9143 O O . THR B 249 ? 1.1344 0.8702 1.3595 -0.1389 -0.1227 0.3118 249 THR B O 9144 C CB . THR B 249 ? 1.2549 0.9045 1.4505 -0.1342 -0.1645 0.3768 249 THR B CB 9145 O OG1 . THR B 249 ? 1.4330 1.1237 1.7147 -0.1183 -0.1807 0.3567 249 THR B OG1 9146 C CG2 . THR B 249 ? 1.0654 0.6678 1.2508 -0.1329 -0.1686 0.4062 249 THR B CG2 9147 N N . THR B 250 ? 0.9786 0.6474 1.0638 -0.1581 -0.0997 0.3429 250 THR B N 9148 C CA . THR B 250 ? 1.0731 0.7565 1.1279 -0.1655 -0.0945 0.3227 250 THR B CA 9149 C C . THR B 250 ? 1.2791 0.9077 1.2225 -0.1806 -0.0940 0.3372 250 THR B C 9150 O O . THR B 250 ? 1.0979 0.6768 0.9792 -0.1835 -0.0779 0.3605 250 THR B O 9151 C CB . THR B 250 ? 1.0131 0.7230 1.0865 -0.1621 -0.0549 0.3017 250 THR B CB 9152 O OG1 . THR B 250 ? 1.0861 0.8001 1.1209 -0.1699 -0.0488 0.2840 250 THR B OG1 9153 C CG2 . THR B 250 ? 0.9230 0.6070 0.9623 -0.1621 -0.0177 0.3197 250 THR B CG2 9154 N N . ASP B 251 ? 1.5420 1.1744 1.4557 -0.1921 -0.1099 0.3232 251 ASP B N 9155 C CA . ASP B 251 ? 1.3944 0.9644 1.1891 -0.2108 -0.1125 0.3318 251 ASP B CA 9156 C C . ASP B 251 ? 1.4409 0.9810 1.1703 -0.2106 -0.0572 0.3231 251 ASP B C 9157 O O . ASP B 251 ? 1.4864 0.9574 1.1126 -0.2168 -0.0347 0.3380 251 ASP B O 9158 C CB . ASP B 251 ? 1.4113 0.9967 1.2044 -0.2281 -0.1561 0.3209 251 ASP B CB 9159 C CG . ASP B 251 ? 2.0147 1.5294 1.6935 -0.2516 -0.1899 0.3399 251 ASP B CG 9160 O OD1 . ASP B 251 ? 2.1150 1.6062 1.7304 -0.2736 -0.1997 0.3284 251 ASP B OD1 9161 O OD2 . ASP B 251 ? 2.3129 1.7894 1.9589 -0.2504 -0.2090 0.3667 251 ASP B OD2 9162 N N . ALA B 252 ? 1.3601 0.9480 1.1478 -0.2018 -0.0336 0.3000 252 ALA B N 9163 C CA . ALA B 252 ? 1.5740 1.1401 1.3103 -0.1994 0.0135 0.2903 252 ALA B CA 9164 C C . ALA B 252 ? 1.3909 1.0017 1.2024 -0.1803 0.0481 0.2866 252 ALA B C 9165 O O . ALA B 252 ? 1.2907 0.9376 1.1796 -0.1723 0.0380 0.2926 252 ALA B O 9166 C CB . ALA B 252 ? 1.6153 1.1839 1.3271 -0.2130 0.0033 0.2665 252 ALA B CB 9167 N N . LYS B 253 ? 1.3239 0.9272 1.1090 -0.1741 0.0864 0.2780 253 LYS B N 9168 C CA . LYS B 253 ? 1.2904 0.9352 1.1430 -0.1577 0.1145 0.2777 253 LYS B CA 9169 C C . LYS B 253 ? 1.0975 0.8014 1.0344 -0.1566 0.0905 0.2554 253 LYS B C 9170 O O . LYS B 253 ? 1.0612 0.7780 1.0127 -0.1656 0.0583 0.2409 253 LYS B O 9171 C CB . LYS B 253 ? 1.4080 1.0260 1.2095 -0.1484 0.1600 0.2773 253 LYS B CB 9172 C CG . LYS B 253 ? 1.3227 0.8953 1.0377 -0.1601 0.1595 0.2597 253 LYS B CG 9173 C CD . LYS B 253 ? 1.4514 0.9865 1.1123 -0.1462 0.2105 0.2621 253 LYS B CD 9174 C CE . LYS B 253 ? 1.4653 0.9272 1.0108 -0.1611 0.2153 0.2490 253 LYS B CE 9175 N NZ . LYS B 253 ? 1.1807 0.6648 0.7399 -0.1787 0.1823 0.2229 253 LYS B NZ 9176 N N . THR B 254 ? 1.0443 0.7821 1.0361 -0.1458 0.1064 0.2541 254 THR B N 9177 C CA . THR B 254 ? 0.9576 0.7389 1.0187 -0.1455 0.0857 0.2344 254 THR B CA 9178 C C . THR B 254 ? 0.9713 0.7686 1.0389 -0.1397 0.1024 0.2209 254 THR B C 9179 O O . THR B 254 ? 1.3036 1.0895 1.3460 -0.1312 0.1311 0.2328 254 THR B O 9180 C CB . THR B 254 ? 0.9133 0.7159 1.0405 -0.1436 0.0731 0.2461 254 THR B CB 9181 O OG1 . THR B 254 ? 0.7892 0.6200 0.9671 -0.1435 0.0585 0.2250 254 THR B OG1 9182 C CG2 . THR B 254 ? 0.7420 0.5465 0.8803 -0.1381 0.0997 0.2717 254 THR B CG2 9183 N N . HIS B 255 ? 0.8535 0.6733 0.9531 -0.1428 0.0864 0.1974 255 HIS B N 9184 C CA . HIS B 255 ? 1.0015 0.8326 1.1059 -0.1387 0.0966 0.1854 255 HIS B CA 9185 C C . HIS B 255 ? 0.9949 0.8473 1.1496 -0.1345 0.0920 0.1980 255 HIS B C 9186 O O . HIS B 255 ? 1.1029 0.9651 1.2996 -0.1391 0.0727 0.1991 255 HIS B O 9187 C CB . HIS B 255 ? 0.9088 0.7482 1.0207 -0.1452 0.0854 0.1561 255 HIS B CB 9188 C CG . HIS B 255 ? 0.9276 0.7512 0.9925 -0.1527 0.0939 0.1435 255 HIS B CG 9189 N ND1 . HIS B 255 ? 1.1253 0.9243 1.1351 -0.1510 0.1164 0.1455 255 HIS B ND1 9190 C CD2 . HIS B 255 ? 0.8888 0.7175 0.9576 -0.1633 0.0819 0.1301 255 HIS B CD2 9191 C CE1 . HIS B 255 ? 1.3523 1.1362 1.3263 -0.1638 0.1171 0.1321 255 HIS B CE1 9192 N NE2 . HIS B 255 ? 1.0848 0.8913 1.0986 -0.1725 0.0949 0.1236 255 HIS B NE2 9193 N N . ILE B 256 ? 0.8912 0.7488 1.0430 -0.1265 0.1080 0.2094 256 ILE B N 9194 C CA . ILE B 256 ? 0.7382 0.6215 0.9429 -0.1262 0.0972 0.2230 256 ILE B CA 9195 C C . ILE B 256 ? 0.9246 0.8096 1.1227 -0.1292 0.0840 0.2030 256 ILE B C 9196 O O . ILE B 256 ? 0.7042 0.5713 0.8607 -0.1308 0.0886 0.1792 256 ILE B O 9197 C CB . ILE B 256 ? 0.7029 0.5983 0.9243 -0.1137 0.1217 0.2560 256 ILE B CB 9198 C CG1 . ILE B 256 ? 0.6804 0.5603 0.8568 -0.0996 0.1464 0.2546 256 ILE B CG1 9199 C CG2 . ILE B 256 ? 0.6787 0.5608 0.8915 -0.1115 0.1412 0.2756 256 ILE B CG2 9200 C CD1 . ILE B 256 ? 0.8516 0.7379 1.0431 -0.0808 0.1799 0.2876 256 ILE B CD1 9201 N N . ALA B 257 ? 0.9269 0.8305 1.1632 -0.1327 0.0665 0.2140 257 ALA B N 9202 C CA . ALA B 257 ? 0.7241 0.6196 0.9412 -0.1375 0.0506 0.1977 257 ALA B CA 9203 C C . ALA B 257 ? 0.8579 0.7441 1.0344 -0.1239 0.0716 0.2009 257 ALA B C 9204 O O . ALA B 257 ? 1.0174 0.9083 1.1939 -0.1093 0.0971 0.2217 257 ALA B O 9205 C CB . ALA B 257 ? 0.7607 0.6748 1.0238 -0.1482 0.0198 0.2127 257 ALA B CB 9206 N N . LEU B 258 ? 0.8941 0.7585 1.0287 -0.1285 0.0641 0.1799 258 LEU B N 9207 C CA . LEU B 258 ? 0.8250 0.6701 0.9117 -0.1178 0.0813 0.1802 258 LEU B CA 9208 C C . LEU B 258 ? 0.8780 0.6989 0.9168 -0.1141 0.1126 0.1666 258 LEU B C 9209 O O . LEU B 258 ? 0.8757 0.6704 0.8652 -0.1086 0.1292 0.1625 258 LEU B O 9210 C CB . LEU B 258 ? 0.8188 0.6858 0.9380 -0.1007 0.0843 0.2165 258 LEU B CB 9211 C CG . LEU B 258 ? 0.8514 0.7434 1.0160 -0.1072 0.0462 0.2340 258 LEU B CG 9212 C CD1 . LEU B 258 ? 0.9154 0.8388 1.1281 -0.0863 0.0527 0.2748 258 LEU B CD1 9213 C CD2 . LEU B 258 ? 0.9814 0.8393 1.0899 -0.1199 0.0229 0.2112 258 LEU B CD2 9214 N N . ASP B 259 ? 0.8760 0.7018 0.9262 -0.1195 0.1173 0.1608 259 ASP B N 9215 C CA . ASP B 259 ? 0.7676 0.5705 0.7734 -0.1231 0.1370 0.1472 259 ASP B CA 9216 C C . ASP B 259 ? 0.7816 0.5710 0.7611 -0.1363 0.1354 0.1169 259 ASP B C 9217 O O . ASP B 259 ? 0.8752 0.6424 0.8112 -0.1419 0.1520 0.1060 259 ASP B O 9218 C CB . ASP B 259 ? 0.7990 0.6104 0.8243 -0.1273 0.1342 0.1521 259 ASP B CB 9219 C CG . ASP B 259 ? 1.0725 0.8783 1.0937 -0.1151 0.1523 0.1801 259 ASP B CG 9220 O OD1 . ASP B 259 ? 1.3848 1.1776 1.3845 -0.1013 0.1734 0.1933 259 ASP B OD1 9221 O OD2 . ASP B 259 ? 1.1605 0.9707 1.1976 -0.1178 0.1484 0.1899 259 ASP B OD2 9222 N N . GLY B 260 ? 0.7966 0.5950 0.8004 -0.1426 0.1179 0.1037 260 GLY B N 9223 C CA . GLY B 260 ? 0.8131 0.5985 0.7986 -0.1533 0.1231 0.0753 260 GLY B CA 9224 C C . GLY B 260 ? 0.8418 0.5965 0.7694 -0.1557 0.1375 0.0661 260 GLY B C 9225 O O . GLY B 260 ? 0.8569 0.5973 0.7638 -0.1657 0.1501 0.0435 260 GLY B O 9226 N N . ARG B 261 ? 0.8907 0.6343 0.7946 -0.1454 0.1381 0.0855 261 ARG B N 9227 C CA . ARG B 261 ? 0.9721 0.6800 0.8157 -0.1456 0.1496 0.0812 261 ARG B CA 9228 C C . ARG B 261 ? 1.0096 0.6949 0.8123 -0.1536 0.1773 0.0690 261 ARG B C 9229 O O . ARG B 261 ? 0.9836 0.6376 0.7382 -0.1623 0.1913 0.0549 261 ARG B O 9230 C CB . ARG B 261 ? 0.9097 0.6146 0.7487 -0.1283 0.1427 0.1103 261 ARG B CB 9231 C CG . ARG B 261 ? 0.9592 0.6228 0.7345 -0.1261 0.1485 0.1102 261 ARG B CG 9232 C CD . ARG B 261 ? 0.9883 0.6561 0.7743 -0.1049 0.1378 0.1439 261 ARG B CD 9233 N NE . ARG B 261 ? 1.3450 0.9666 1.0646 -0.1000 0.1447 0.1469 261 ARG B NE 9234 C CZ . ARG B 261 ? 1.3833 1.0008 1.1047 -0.0793 0.1356 0.1772 261 ARG B CZ 9235 N NH1 . ARG B 261 ? 1.4728 1.1365 1.2680 -0.0623 0.1217 0.2074 261 ARG B NH1 9236 N NH2 . ARG B 261 ? 1.2240 0.7923 0.8780 -0.0751 0.1414 0.1797 261 ARG B NH2 9237 N N . LEU B 262 ? 1.0700 0.7662 0.8869 -0.1538 0.1842 0.0749 262 LEU B N 9238 C CA . LEU B 262 ? 0.8512 0.5254 0.6313 -0.1678 0.2034 0.0638 262 LEU B CA 9239 C C . LEU B 262 ? 0.9429 0.6306 0.7413 -0.1874 0.2059 0.0390 262 LEU B C 9240 O O . LEU B 262 ? 1.2058 0.8729 0.9715 -0.2033 0.2235 0.0268 262 LEU B O 9241 C CB . LEU B 262 ? 0.8221 0.4998 0.6074 -0.1677 0.2032 0.0752 262 LEU B CB 9242 C CG . LEU B 262 ? 0.9911 0.6321 0.7299 -0.1527 0.2206 0.0950 262 LEU B CG 9243 C CD1 . LEU B 262 ? 1.0905 0.7449 0.8554 -0.1271 0.2178 0.1178 262 LEU B CD1 9244 C CD2 . LEU B 262 ? 1.3336 0.9662 1.0621 -0.1579 0.2215 0.1016 262 LEU B CD2 9245 N N . ALA B 263 ? 0.9583 0.6792 0.8124 -0.1858 0.1910 0.0327 263 ALA B N 9246 C CA . ALA B 263 ? 0.8294 0.5659 0.7133 -0.1980 0.1984 0.0112 263 ALA B CA 9247 C C . ALA B 263 ? 0.8841 0.5923 0.7325 -0.1991 0.2121 -0.0035 263 ALA B C 9248 O O . ALA B 263 ? 0.8863 0.5981 0.7509 -0.2066 0.2278 -0.0224 263 ALA B O 9249 C CB . ALA B 263 ? 0.8135 0.5878 0.7677 -0.1924 0.1801 0.0116 263 ALA B CB 9250 N N . GLY B 264 ? 1.1350 0.8124 0.9337 -0.1908 0.2070 0.0070 264 GLY B N 9251 C CA . GLY B 264 ? 1.3735 1.0131 1.1218 -0.1931 0.2132 -0.0036 264 GLY B CA 9252 C C . GLY B 264 ? 1.0477 0.6906 0.8177 -0.1891 0.1939 -0.0096 264 GLY B C 9253 O O . GLY B 264 ? 1.2370 0.8472 0.9716 -0.1956 0.2043 -0.0279 264 GLY B O 9254 N N . ILE B 265 ? 0.9560 0.6307 0.7773 -0.1801 0.1679 0.0056 265 ILE B N 9255 C CA . ILE B 265 ? 0.9894 0.6625 0.8308 -0.1794 0.1461 0.0015 265 ILE B CA 9256 C C . ILE B 265 ? 1.0150 0.6857 0.8493 -0.1746 0.1139 0.0249 265 ILE B C 9257 O O . ILE B 265 ? 0.9681 0.6730 0.8474 -0.1660 0.1007 0.0484 265 ILE B O 9258 C CB . ILE B 265 ? 0.9534 0.6650 0.8684 -0.1756 0.1398 0.0014 265 ILE B CB 9259 C CG1 . ILE B 265 ? 0.9561 0.6834 0.8963 -0.1792 0.1666 -0.0148 265 ILE B CG1 9260 C CG2 . ILE B 265 ? 1.0239 0.7208 0.9508 -0.1769 0.1216 -0.0064 265 ILE B CG2 9261 C CD1 . ILE B 265 ? 0.9197 0.6869 0.9330 -0.1739 0.1563 -0.0089 265 ILE B CD1 9262 N N . VAL B 266 ? 1.0832 0.7123 0.8609 -0.1813 0.1015 0.0200 266 VAL B N 9263 C CA . VAL B 266 ? 1.1302 0.7591 0.9041 -0.1796 0.0647 0.0449 266 VAL B CA 9264 C C . VAL B 266 ? 1.2490 0.8718 1.0395 -0.1907 0.0292 0.0437 266 VAL B C 9265 O O . VAL B 266 ? 1.4571 1.0873 1.2579 -0.1935 -0.0078 0.0670 266 VAL B O 9266 C CB . VAL B 266 ? 1.2947 0.8765 0.9875 -0.1821 0.0627 0.0474 266 VAL B CB 9267 C CG1 . VAL B 266 ? 1.1493 0.7359 0.8299 -0.1699 0.0903 0.0582 266 VAL B CG1 9268 C CG2 . VAL B 266 ? 1.6932 1.2152 1.3111 -0.1969 0.0791 0.0149 266 VAL B CG2 9269 N N . GLN B 267 ? 1.1770 0.7849 0.9728 -0.1973 0.0397 0.0182 267 GLN B N 9270 C CA . GLN B 267 ? 1.2322 0.8153 1.0260 -0.2108 0.0089 0.0123 267 GLN B CA 9271 C C . GLN B 267 ? 1.1446 0.7767 1.0259 -0.2081 -0.0093 0.0305 267 GLN B C 9272 O O . GLN B 267 ? 1.1012 0.7601 1.0297 -0.1985 0.0126 0.0256 267 GLN B O 9273 C CB . GLN B 267 ? 1.3743 0.9016 1.1202 -0.2171 0.0339 -0.0250 267 GLN B CB 9274 C CG . GLN B 267 ? 1.4541 0.9280 1.1649 -0.2345 0.0035 -0.0360 267 GLN B CG 9275 C CD . GLN B 267 ? 1.5797 0.9888 1.2390 -0.2362 0.0378 -0.0737 267 GLN B CD 9276 O OE1 . GLN B 267 ? 1.7992 1.2257 1.4874 -0.2214 0.0827 -0.0879 267 GLN B OE1 9277 N NE2 . GLN B 267 ? 1.5436 0.8754 1.1266 -0.2546 0.0172 -0.0892 267 GLN B NE2 9278 N N . PRO B 268 ? 1.1449 0.7884 1.0491 -0.2183 -0.0514 0.0540 268 PRO B N 9279 C CA . PRO B 268 ? 1.0843 0.7715 1.0706 -0.2195 -0.0690 0.0752 268 PRO B CA 9280 C C . PRO B 268 ? 1.0870 0.7445 1.0792 -0.2281 -0.0689 0.0532 268 PRO B C 9281 O O . PRO B 268 ? 1.1514 0.7462 1.0795 -0.2391 -0.0694 0.0250 268 PRO B O 9282 C CB . PRO B 268 ? 1.1039 0.8025 1.1052 -0.2340 -0.1162 0.1035 268 PRO B CB 9283 C CG . PRO B 268 ? 1.1667 0.8428 1.1047 -0.2315 -0.1201 0.1050 268 PRO B CG 9284 C CD . PRO B 268 ? 1.2102 0.8280 1.0665 -0.2308 -0.0868 0.0657 268 PRO B CD 9285 N N . ASN B 269 ? 1.0254 0.7201 1.0874 -0.2221 -0.0655 0.0665 269 ASN B N 9286 C CA . ASN B 269 ? 1.0243 0.6907 1.0994 -0.2273 -0.0665 0.0508 269 ASN B CA 9287 C C . ASN B 269 ? 1.1248 0.7449 1.1746 -0.2538 -0.1057 0.0476 269 ASN B C 9288 O O . ASN B 269 ? 1.1867 0.8326 1.2669 -0.2689 -0.1406 0.0751 269 ASN B O 9289 C CB . ASN B 269 ? 0.9470 0.6602 1.0977 -0.2175 -0.0608 0.0728 269 ASN B CB 9290 C CG . ASN B 269 ? 1.2697 0.9554 1.4333 -0.2127 -0.0503 0.0553 269 ASN B CG 9291 O OD1 . ASN B 269 ? 1.5571 1.2013 1.7140 -0.2268 -0.0690 0.0479 269 ASN B OD1 9292 N ND2 . ASN B 269 ? 1.3164 1.0227 1.4991 -0.1932 -0.0223 0.0502 269 ASN B ND2 9293 N N . ASP B 270 ? 1.1405 0.6899 1.1351 -0.2602 -0.0992 0.0149 270 ASP B N 9294 C CA . ASP B 270 ? 1.2009 0.6861 1.1499 -0.2894 -0.1365 0.0064 270 ASP B CA 9295 C C . ASP B 270 ? 1.2820 0.7614 1.2819 -0.2987 -0.1511 0.0142 270 ASP B C 9296 O O . ASP B 270 ? 1.4807 0.9117 1.4548 -0.3279 -0.1879 0.0128 270 ASP B O 9297 C CB . ASP B 270 ? 1.2933 0.6856 1.1381 -0.2929 -0.1178 -0.0346 270 ASP B CB 9298 C CG . ASP B 270 ? 1.3341 0.7119 1.1881 -0.2661 -0.0648 -0.0599 270 ASP B CG 9299 O OD1 . ASP B 270 ? 1.3820 0.8132 1.3185 -0.2488 -0.0526 -0.0460 270 ASP B OD1 9300 O OD2 . ASP B 270 ? 1.3710 0.6827 1.1500 -0.2623 -0.0350 -0.0920 270 ASP B OD2 9301 N N . GLY B 271 ? 1.1200 0.6430 1.1863 -0.2761 -0.1247 0.0233 271 GLY B N 9302 C CA . GLY B 271 ? 1.1111 0.6277 1.2253 -0.2820 -0.1349 0.0339 271 GLY B CA 9303 C C . GLY B 271 ? 1.3206 0.7456 1.3838 -0.2865 -0.1289 0.0015 271 GLY B C 9304 O O . GLY B 271 ? 1.4962 0.8863 1.5706 -0.3044 -0.1508 0.0068 271 GLY B O 9305 N N . GLN B 272 ? 1.2528 0.6340 1.2588 -0.2701 -0.0956 -0.0315 272 GLN B N 9306 C CA . GLN B 272 ? 1.3939 0.6825 1.3496 -0.2667 -0.0770 -0.0641 272 GLN B CA 9307 C C . GLN B 272 ? 1.6019 0.9128 1.6150 -0.2295 -0.0355 -0.0681 272 GLN B C 9308 O O . GLN B 272 ? 1.4427 0.8363 1.5225 -0.2114 -0.0260 -0.0473 272 GLN B O 9309 C CB . GLN B 272 ? 1.4014 0.6151 1.2507 -0.2730 -0.0617 -0.0983 272 GLN B CB 9310 C CG . GLN B 272 ? 1.4283 0.6271 1.2175 -0.3079 -0.1070 -0.0910 272 GLN B CG 9311 C CD . GLN B 272 ? 2.1544 1.2995 1.9206 -0.3463 -0.1587 -0.0850 272 GLN B CD 9312 O OE1 . GLN B 272 ? 2.3259 1.4133 2.0889 -0.3486 -0.1542 -0.0967 272 GLN B OE1 9313 N NE2 . GLN B 272 ? 2.3741 1.5375 2.1275 -0.3775 -0.2097 -0.0647 272 GLN B NE2 9314 N N . CYS B 273 ? 1.7502 0.9839 1.7356 -0.2179 -0.0117 -0.0937 273 CYS B N 9315 C CA . CYS B 273 ? 1.6136 0.8692 1.6620 -0.1800 0.0256 -0.0950 273 CYS B CA 9316 C C . CYS B 273 ? 1.6400 0.8914 1.6675 -0.1566 0.0749 -0.1208 273 CYS B C 9317 O O . CYS B 273 ? 1.9265 1.0908 1.8821 -0.1549 0.1024 -0.1528 273 CYS B O 9318 C CB . CYS B 273 ? 1.7906 0.9686 1.8372 -0.1741 0.0283 -0.1033 273 CYS B CB 9319 S SG . CYS B 273 ? 2.2018 1.3973 2.3288 -0.1229 0.0730 -0.1038 273 CYS B SG 9320 N N . HIS B 274 ? 1.5207 0.8615 1.6073 -0.1405 0.0879 -0.1064 274 HIS B N 9321 C CA . HIS B 274 ? 1.6099 0.9617 1.6922 -0.1215 0.1345 -0.1257 274 HIS B CA 9322 C C . HIS B 274 ? 1.6748 1.0601 1.8443 -0.0856 0.1674 -0.1234 274 HIS B C 9323 O O . HIS B 274 ? 1.7909 1.1983 1.9796 -0.0688 0.2081 -0.1352 274 HIS B O 9324 C CB . HIS B 274 ? 1.5024 0.9236 1.5847 -0.1318 0.1275 -0.1132 274 HIS B CB 9325 C CG . HIS B 274 ? 1.6170 1.0062 1.6169 -0.1620 0.0995 -0.1150 274 HIS B CG 9326 N ND1 . HIS B 274 ? 1.6334 0.9361 1.5332 -0.1750 0.1112 -0.1433 274 HIS B ND1 9327 C CD2 . HIS B 274 ? 1.7433 1.1736 1.7470 -0.1810 0.0596 -0.0899 274 HIS B CD2 9328 C CE1 . HIS B 274 ? 1.8295 1.1247 1.6768 -0.2022 0.0728 -0.1339 274 HIS B CE1 9329 N NE2 . HIS B 274 ? 1.9014 1.2775 1.8178 -0.2045 0.0428 -0.1009 274 HIS B NE2 9330 N N . VAL B 275 ? 1.6486 1.0391 1.8750 -0.0745 0.1485 -0.1054 275 VAL B N 9331 C CA . VAL B 275 ? 1.4730 0.8973 1.7900 -0.0390 0.1708 -0.0970 275 VAL B CA 9332 C C . VAL B 275 ? 1.5746 0.9185 1.8741 -0.0149 0.2179 -0.1259 275 VAL B C 9333 O O . VAL B 275 ? 1.6767 0.9292 1.9207 -0.0204 0.2143 -0.1391 275 VAL B O 9334 C CB . VAL B 275 ? 1.2264 0.6756 1.6030 -0.0342 0.1334 -0.0649 275 VAL B CB 9335 C CG1 . VAL B 275 ? 1.2122 0.6961 1.6839 0.0036 0.1503 -0.0528 275 VAL B CG1 9336 C CG2 . VAL B 275 ? 1.1394 0.6593 1.5266 -0.0559 0.0953 -0.0366 275 VAL B CG2 9337 N N . GLY B 276 ? 1.5169 0.8925 1.8645 0.0111 0.2644 -0.1349 276 GLY B N 9338 C CA . GLY B 276 ? 1.5470 0.8487 1.8808 0.0382 0.3222 -0.1626 276 GLY B CA 9339 C C . GLY B 276 ? 1.6063 0.9280 2.0492 0.0810 0.3389 -0.1476 276 GLY B C 9340 O O . GLY B 276 ? 1.4582 0.8299 1.9693 0.0858 0.2966 -0.1162 276 GLY B O 9341 N N . SER B 277 ? 1.6994 0.9790 2.1578 0.1136 0.4029 -0.1685 277 SER B N 9342 C CA . SER B 277 ? 1.5757 0.8692 2.1443 0.1608 0.4259 -0.1541 277 SER B CA 9343 C C . SER B 277 ? 1.4277 0.8607 2.1408 0.1774 0.4127 -0.1198 277 SER B C 9344 O O . SER B 277 ? 1.4461 0.9145 2.2679 0.2128 0.4099 -0.0957 277 SER B O 9345 C CB . SER B 277 ? 1.6544 0.8624 2.2002 0.1935 0.5072 -0.1862 277 SER B CB 9346 O OG . SER B 277 ? 1.7504 0.9937 2.2949 0.1909 0.5556 -0.2016 277 SER B OG 9347 N N . ASP B 278 ? 1.3428 0.8502 2.0540 0.1504 0.4017 -0.1165 278 ASP B N 9348 C CA . ASP B 278 ? 1.2919 0.9260 2.1244 0.1557 0.3814 -0.0850 278 ASP B CA 9349 C C . ASP B 278 ? 1.3013 0.9807 2.1422 0.1347 0.3056 -0.0527 278 ASP B C 9350 O O . ASP B 278 ? 1.1954 0.9686 2.1171 0.1325 0.2756 -0.0244 278 ASP B O 9351 C CB . ASP B 278 ? 1.4643 1.1481 2.2853 0.1345 0.4073 -0.0966 278 ASP B CB 9352 C CG . ASP B 278 ? 1.6920 1.3457 2.3872 0.0903 0.3796 -0.1091 278 ASP B CG 9353 O OD1 . ASP B 278 ? 1.9033 1.4705 2.4999 0.0779 0.3656 -0.1233 278 ASP B OD1 9354 O OD2 . ASP B 278 ? 1.5462 1.2620 2.2439 0.0675 0.3707 -0.1031 278 ASP B OD2 9355 N N . ASN B 279 ? 1.3818 0.9895 2.1347 0.1172 0.2761 -0.0568 279 ASN B N 9356 C CA . ASN B 279 ? 1.3032 0.9375 2.0520 0.0975 0.2126 -0.0272 279 ASN B CA 9357 C C . ASN B 279 ? 1.2577 0.9669 1.9962 0.0667 0.1838 -0.0144 279 ASN B C 9358 O O . ASN B 279 ? 1.3143 1.0768 2.0909 0.0611 0.1412 0.0165 279 ASN B O 9359 C CB . ASN B 279 ? 1.1966 0.8615 2.0447 0.1278 0.1893 0.0058 279 ASN B CB 9360 C CG . ASN B 279 ? 1.2338 0.8091 2.0775 0.1560 0.2085 -0.0021 279 ASN B CG 9361 O OD1 . ASN B 279 ? 1.3819 0.8766 2.1642 0.1600 0.2520 -0.0360 279 ASN B OD1 9362 N ND2 . ASN B 279 ? 1.2837 0.8631 2.1829 0.1748 0.1761 0.0292 279 ASN B ND2 9363 N N . HIS B 280 ? 1.1969 0.9006 1.8748 0.0469 0.2082 -0.0383 280 HIS B N 9364 C CA . HIS B 280 ? 1.1724 0.9298 1.8239 0.0174 0.1855 -0.0295 280 HIS B CA 9365 C C . HIS B 280 ? 1.1832 0.8872 1.7232 -0.0112 0.1815 -0.0470 280 HIS B C 9366 O O . HIS B 280 ? 1.4551 1.0847 1.9347 -0.0111 0.2052 -0.0727 280 HIS B O 9367 C CB . HIS B 280 ? 1.3537 1.1717 2.0535 0.0196 0.2158 -0.0348 280 HIS B CB 9368 C CG . HIS B 280 ? 1.4256 1.3203 2.2448 0.0380 0.2030 -0.0084 280 HIS B CG 9369 N ND1 . HIS B 280 ? 1.1773 1.1273 2.0229 0.0243 0.1529 0.0218 280 HIS B ND1 9370 C CD2 . HIS B 280 ? 1.5239 1.4484 2.4440 0.0687 0.2324 -0.0058 280 HIS B CD2 9371 C CE1 . HIS B 280 ? 1.1449 1.1555 2.0995 0.0427 0.1448 0.0426 280 HIS B CE1 9372 N NE2 . HIS B 280 ? 1.4012 1.4039 2.4122 0.0712 0.1927 0.0279 280 HIS B NE2 9373 N N . TYR B 281 ? 1.0911 0.8293 1.6018 -0.0354 0.1509 -0.0321 281 TYR B N 9374 C CA . TYR B 281 ? 1.0799 0.7812 1.4994 -0.0608 0.1441 -0.0430 281 TYR B CA 9375 C C . TYR B 281 ? 1.0999 0.7997 1.4822 -0.0669 0.1799 -0.0657 281 TYR B C 9376 O O . TYR B 281 ? 1.0755 0.8307 1.4849 -0.0706 0.1858 -0.0588 281 TYR B O 9377 C CB . TYR B 281 ? 1.0078 0.7458 1.4170 -0.0790 0.1056 -0.0162 281 TYR B CB 9378 C CG . TYR B 281 ? 1.0028 0.7148 1.3366 -0.1022 0.0942 -0.0198 281 TYR B CG 9379 C CD1 . TYR B 281 ? 1.1746 0.8218 1.4485 -0.1105 0.1012 -0.0418 281 TYR B CD1 9380 C CD2 . TYR B 281 ? 0.9878 0.7368 1.3090 -0.1155 0.0756 0.0004 281 TYR B CD2 9381 C CE1 . TYR B 281 ? 1.1983 0.8275 1.4114 -0.1325 0.0832 -0.0404 281 TYR B CE1 9382 C CE2 . TYR B 281 ? 0.9346 0.6671 1.2014 -0.1327 0.0648 0.0018 281 TYR B CE2 9383 C CZ . TYR B 281 ? 1.1099 0.7871 1.3275 -0.1416 0.0653 -0.0172 281 TYR B CZ 9384 O OH . TYR B 281 ? 1.3212 0.9870 1.4920 -0.1595 0.0472 -0.0116 281 TYR B OH 9385 N N . SER B 282 ? 1.1525 0.7808 1.4644 -0.0708 0.2030 -0.0926 282 SER B N 9386 C CA . SER B 282 ? 1.1910 0.8016 1.4584 -0.0746 0.2445 -0.1160 282 SER B CA 9387 C C . SER B 282 ? 1.2662 0.8815 1.4642 -0.1002 0.2289 -0.1133 282 SER B C 9388 O O . SER B 282 ? 1.4797 1.1129 1.6646 -0.1051 0.2549 -0.1200 282 SER B O 9389 C CB . SER B 282 ? 1.2704 0.7867 1.4733 -0.0685 0.2782 -0.1467 282 SER B CB 9390 O OG . SER B 282 ? 1.2986 0.7496 1.4192 -0.0885 0.2448 -0.1509 282 SER B OG 9391 N N . ALA B 283 ? 1.1480 0.7479 1.3070 -0.1159 0.1875 -0.1010 283 ALA B N 9392 C CA . ALA B 283 ? 1.1724 0.7707 1.2677 -0.1364 0.1705 -0.0957 283 ALA B CA 9393 C C . ALA B 283 ? 1.1736 0.8437 1.3109 -0.1388 0.1525 -0.0690 283 ALA B C 9394 O O . ALA B 283 ? 1.2809 0.9558 1.3776 -0.1514 0.1376 -0.0588 283 ALA B O 9395 C CB . ALA B 283 ? 1.2554 0.8049 1.2961 -0.1527 0.1350 -0.0931 283 ALA B CB 9396 N N . SER B 284 ? 1.1831 0.9030 1.3977 -0.1263 0.1530 -0.0568 284 SER B N 9397 C CA . SER B 284 ? 1.0651 0.8409 1.3098 -0.1300 0.1356 -0.0327 284 SER B CA 9398 C C . SER B 284 ? 1.0347 0.8206 1.2386 -0.1414 0.1507 -0.0360 284 SER B C 9399 O O . SER B 284 ? 0.9609 0.7587 1.1403 -0.1493 0.1348 -0.0194 284 SER B O 9400 C CB . SER B 284 ? 0.9535 0.7733 1.2796 -0.1170 0.1349 -0.0227 284 SER B CB 9401 O OG . SER B 284 ? 1.0881 0.9475 1.4276 -0.1238 0.1128 0.0009 284 SER B OG 9402 N N . THR B 285 ? 1.1800 0.9568 1.3758 -0.1412 0.1855 -0.0565 285 THR B N 9403 C CA . THR B 285 ? 1.0843 0.8613 1.2359 -0.1538 0.2038 -0.0610 285 THR B CA 9404 C C . THR B 285 ? 1.0757 0.7982 1.1362 -0.1627 0.2037 -0.0691 285 THR B C 9405 O O . THR B 285 ? 1.2277 0.9469 1.2434 -0.1721 0.2038 -0.0628 285 THR B O 9406 C CB . THR B 285 ? 0.9964 0.7860 1.1780 -0.1529 0.2451 -0.0775 285 THR B CB 9407 O OG1 . THR B 285 ? 1.0740 0.8145 1.2301 -0.1449 0.2746 -0.1007 285 THR B OG1 9408 C CG2 . THR B 285 ? 0.9616 0.8124 1.2444 -0.1449 0.2391 -0.0656 285 THR B CG2 9409 N N . THR B 286 ? 1.1128 0.7871 1.1418 -0.1605 0.2014 -0.0822 286 THR B N 9410 C CA . THR B 286 ? 1.1093 0.7241 1.0450 -0.1718 0.1985 -0.0913 286 THR B CA 9411 C C . THR B 286 ? 1.1852 0.7946 1.0985 -0.1789 0.1529 -0.0713 286 THR B C 9412 O O . THR B 286 ? 1.1498 0.7195 0.9917 -0.1893 0.1417 -0.0719 286 THR B O 9413 C CB . THR B 286 ? 1.1903 0.7377 1.0810 -0.1709 0.2212 -0.1191 286 THR B CB 9414 O OG1 . THR B 286 ? 1.2953 0.8286 1.2113 -0.1664 0.1968 -0.1178 286 THR B OG1 9415 C CG2 . THR B 286 ? 1.2152 0.7716 1.1410 -0.1604 0.2736 -0.1368 286 THR B CG2 9416 N N . MET B 287 ? 1.0802 0.7296 1.0556 -0.1740 0.1265 -0.0510 287 MET B N 9417 C CA . MET B 287 ? 1.0545 0.7079 1.0240 -0.1808 0.0880 -0.0284 287 MET B CA 9418 C C . MET B 287 ? 0.9724 0.6829 1.0030 -0.1740 0.0752 0.0002 287 MET B C 9419 O O . MET B 287 ? 0.9323 0.6724 1.0107 -0.1658 0.0853 0.0022 287 MET B O 9420 C CB . MET B 287 ? 1.1954 0.8090 1.1555 -0.1891 0.0641 -0.0346 287 MET B CB 9421 C CG . MET B 287 ? 1.3642 0.9943 1.3901 -0.1815 0.0592 -0.0307 287 MET B CG 9422 S SD . MET B 287 ? 1.5490 1.1289 1.5583 -0.1980 0.0228 -0.0313 287 MET B SD 9423 C CE . MET B 287 ? 1.1971 0.6885 1.0984 -0.2101 0.0347 -0.0656 287 MET B CE 9424 N N . ASP B 288 ? 0.9594 0.6821 0.9857 -0.1773 0.0531 0.0238 288 ASP B N 9425 C CA . ASP B 288 ? 0.9048 0.6711 0.9707 -0.1698 0.0500 0.0520 288 ASP B CA 9426 C C . ASP B 288 ? 0.9784 0.7664 1.1027 -0.1683 0.0355 0.0671 288 ASP B C 9427 O O . ASP B 288 ? 1.3622 1.1315 1.4992 -0.1748 0.0200 0.0601 288 ASP B O 9428 C CB . ASP B 288 ? 0.9961 0.7679 1.0459 -0.1700 0.0365 0.0745 288 ASP B CB 9429 C CG . ASP B 288 ? 1.0926 0.8945 1.1592 -0.1579 0.0508 0.0982 288 ASP B CG 9430 O OD1 . ASP B 288 ? 1.0573 0.8759 1.1494 -0.1536 0.0618 0.1013 288 ASP B OD1 9431 O OD2 . ASP B 288 ? 0.9946 0.7978 1.0443 -0.1521 0.0508 0.1147 288 ASP B OD2 9432 N N . TYR B 289 ? 0.8110 0.6291 0.9612 -0.1607 0.0422 0.0876 289 TYR B N 9433 C CA . TYR B 289 ? 0.7669 0.6024 0.9638 -0.1597 0.0306 0.1084 289 TYR B CA 9434 C C . TYR B 289 ? 0.7665 0.6063 0.9853 -0.1682 0.0082 0.1271 289 TYR B C 9435 O O . TYR B 289 ? 0.7845 0.6295 0.9902 -0.1696 0.0034 0.1366 289 TYR B O 9436 C CB . TYR B 289 ? 0.7302 0.5851 0.9296 -0.1516 0.0450 0.1288 289 TYR B CB 9437 C CG . TYR B 289 ? 0.9495 0.8018 1.1261 -0.1491 0.0604 0.1142 289 TYR B CG 9438 C CD1 . TYR B 289 ? 1.0452 0.8903 1.1787 -0.1486 0.0777 0.1076 289 TYR B CD1 9439 C CD2 . TYR B 289 ? 1.0927 0.9494 1.2941 -0.1485 0.0548 0.1095 289 TYR B CD2 9440 C CE1 . TYR B 289 ? 0.8649 0.7081 0.9808 -0.1521 0.0886 0.0955 289 TYR B CE1 9441 C CE2 . TYR B 289 ? 1.0810 0.9425 1.2722 -0.1499 0.0627 0.0997 289 TYR B CE2 9442 C CZ . TYR B 289 ? 0.9578 0.8130 1.1064 -0.1539 0.0793 0.0922 289 TYR B CZ 9443 O OH . TYR B 289 ? 0.7665 0.6267 0.9078 -0.1609 0.0842 0.0834 289 TYR B OH 9444 N N . PRO B 290 ? 0.7965 0.6343 1.0525 -0.1750 -0.0076 0.1348 290 PRO B N 9445 C CA . PRO B 290 ? 0.8487 0.6924 1.1337 -0.1892 -0.0326 0.1537 290 PRO B CA 9446 C C . PRO B 290 ? 0.8068 0.6916 1.1310 -0.1846 -0.0261 0.1912 290 PRO B C 9447 O O . PRO B 290 ? 0.7536 0.6505 1.0840 -0.1729 -0.0038 0.2039 290 PRO B O 9448 C CB . PRO B 290 ? 0.7524 0.5737 1.0607 -0.1978 -0.0457 0.1490 290 PRO B CB 9449 C CG . PRO B 290 ? 0.7955 0.6205 1.1080 -0.1822 -0.0256 0.1464 290 PRO B CG 9450 C CD . PRO B 290 ? 0.9350 0.7635 1.2102 -0.1710 -0.0054 0.1282 290 PRO B CD 9451 N N . SER B 291 ? 0.7170 0.6206 1.0664 -0.1939 -0.0451 0.2100 291 SER B N 9452 C CA . SER B 291 ? 0.6923 0.6402 1.0955 -0.1882 -0.0356 0.2494 291 SER B CA 9453 C C . SER B 291 ? 0.9035 0.8623 1.3602 -0.1998 -0.0401 0.2700 291 SER B C 9454 O O . SER B 291 ? 0.7352 0.6663 1.1905 -0.2161 -0.0613 0.2554 291 SER B O 9455 C CB . SER B 291 ? 0.7113 0.6836 1.1391 -0.1942 -0.0590 0.2672 291 SER B CB 9456 O OG . SER B 291 ? 0.8246 0.7847 1.2668 -0.2220 -0.1022 0.2630 291 SER B OG 9457 N N . LEU B 292 ? 1.0961 0.9721 1.2476 -0.0510 0.0664 0.1961 292 LEU B N 9458 C CA . LEU B 292 ? 0.9562 0.8379 1.1093 -0.0814 0.0453 0.2182 292 LEU B CA 9459 C C . LEU B 292 ? 1.0985 0.9934 1.2527 -0.1196 0.0136 0.2348 292 LEU B C 9460 O O . LEU B 292 ? 0.9199 0.7776 1.0636 -0.1498 -0.0132 0.2367 292 LEU B O 9461 C CB . LEU B 292 ? 0.8105 0.7569 0.9865 -0.0770 0.0703 0.2459 292 LEU B CB 9462 C CG . LEU B 292 ? 0.7819 0.7194 0.9540 -0.0500 0.1011 0.2287 292 LEU B CG 9463 C CD1 . LEU B 292 ? 0.7751 0.7805 0.9675 -0.0574 0.1249 0.2526 292 LEU B CD1 9464 C CD2 . LEU B 292 ? 0.7911 0.6568 0.9322 -0.0548 0.0802 0.2076 292 LEU B CD2 9465 N N . GLY B 293 ? 1.1849 1.1321 1.3526 -0.1190 0.0156 0.2475 293 GLY B N 9466 C CA . GLY B 293 ? 1.0951 1.0683 1.2644 -0.1573 -0.0137 0.2613 293 GLY B CA 9467 C C . GLY B 293 ? 1.0533 0.9562 1.1929 -0.1802 -0.0388 0.2270 293 GLY B C 9468 O O . GLY B 293 ? 1.2740 1.1633 1.4115 -0.2195 -0.0647 0.2296 293 GLY B O 9469 N N . LEU B 294 ? 0.9828 0.8407 1.1026 -0.1577 -0.0283 0.1914 294 LEU B N 9470 C CA . LEU B 294 ? 1.0125 0.8074 1.1102 -0.1774 -0.0459 0.1490 294 LEU B CA 9471 C C . LEU B 294 ? 1.0102 0.7341 1.1123 -0.1857 -0.0616 0.1320 294 LEU B C 9472 O O . LEU B 294 ? 1.3368 1.0228 1.4375 -0.2182 -0.0860 0.1159 294 LEU B O 9473 C CB . LEU B 294 ? 1.0096 0.7781 1.0871 -0.1521 -0.0253 0.1121 294 LEU B CB 9474 C CG . LEU B 294 ? 1.0348 0.7461 1.0929 -0.1733 -0.0368 0.0591 294 LEU B CG 9475 C CD1 . LEU B 294 ? 1.1052 0.8506 1.1472 -0.2160 -0.0570 0.0625 294 LEU B CD1 9476 C CD2 . LEU B 294 ? 1.0930 0.7761 1.1335 -0.1479 -0.0105 0.0190 294 LEU B CD2 9477 N N . MET B 295 ? 0.9433 0.6483 1.0517 -0.1570 -0.0486 0.1360 295 MET B N 9478 C CA . MET B 295 ? 1.1947 0.8329 1.3072 -0.1607 -0.0679 0.1270 295 MET B CA 9479 C C . MET B 295 ? 1.2337 0.8818 1.3506 -0.1957 -0.0890 0.1694 295 MET B C 9480 O O . MET B 295 ? 1.5454 1.1311 1.6642 -0.2113 -0.1142 0.1686 295 MET B O 9481 C CB . MET B 295 ? 1.3602 0.9837 1.4736 -0.1225 -0.0500 0.1191 295 MET B CB 9482 C CG . MET B 295 ? 1.5294 1.2181 1.6441 -0.1096 -0.0246 0.1551 295 MET B CG 9483 S SD . MET B 295 ? 1.3560 1.0398 1.4692 -0.0641 0.0078 0.1294 295 MET B SD 9484 C CE . MET B 295 ? 0.9091 0.5159 1.0206 -0.0629 -0.0240 0.1108 295 MET B CE 9485 N N . THR B 296 ? 1.2931 1.0194 1.4153 -0.2085 -0.0787 0.2065 296 THR B N 9486 C CA . THR B 296 ? 1.0698 0.8165 1.1968 -0.2502 -0.0957 0.2435 296 THR B CA 9487 C C . THR B 296 ? 0.9817 0.7031 1.1089 -0.2901 -0.1223 0.2295 296 THR B C 9488 O O . THR B 296 ? 1.1138 0.7868 1.2403 -0.3236 -0.1456 0.2378 296 THR B O 9489 C CB . THR B 296 ? 0.9464 0.7956 1.0902 -0.2533 -0.0751 0.2804 296 THR B CB 9490 O OG1 . THR B 296 ? 0.9781 0.8440 1.1214 -0.2348 -0.0538 0.2974 296 THR B OG1 9491 C CG2 . THR B 296 ? 0.9728 0.8578 1.1262 -0.3045 -0.0934 0.3081 296 THR B CG2 9492 N N . GLU B 297 ? 1.0098 0.7619 1.1353 -0.2888 -0.1182 0.2079 297 GLU B N 9493 C CA . GLU B 297 ? 1.0503 0.7902 1.1722 -0.3297 -0.1398 0.1875 297 GLU B CA 9494 C C . GLU B 297 ? 1.2233 0.8588 1.3432 -0.3380 -0.1567 0.1460 297 GLU B C 9495 O O . GLU B 297 ? 1.3915 0.9907 1.5171 -0.3789 -0.1784 0.1427 297 GLU B O 9496 C CB . GLU B 297 ? 1.0879 0.8796 1.1989 -0.3240 -0.1315 0.1709 297 GLU B CB 9497 C CG . GLU B 297 ? 1.2869 1.0756 1.3873 -0.3705 -0.1519 0.1440 297 GLU B CG 9498 C CD . GLU B 297 ? 1.4928 1.3244 1.5702 -0.3662 -0.1450 0.1260 297 GLU B CD 9499 O OE1 . GLU B 297 ? 1.2398 1.0400 1.3021 -0.3326 -0.1267 0.0997 297 GLU B OE1 9500 O OE2 . GLU B 297 ? 1.7494 1.6487 1.8219 -0.3990 -0.1588 0.1395 297 GLU B OE2 9501 N N . LYS B 298 ? 1.3199 0.9078 1.4376 -0.2990 -0.1457 0.1124 298 LYS B N 9502 C CA . LYS B 298 ? 1.3457 0.8400 1.4741 -0.2989 -0.1597 0.0657 298 LYS B CA 9503 C C . LYS B 298 ? 1.4360 0.8625 1.5801 -0.3015 -0.1818 0.0878 298 LYS B C 9504 O O . LYS B 298 ? 1.6097 0.9604 1.7716 -0.3197 -0.2034 0.0642 298 LYS B O 9505 C CB . LYS B 298 ? 1.0362 0.5107 1.1633 -0.2564 -0.1398 0.0216 298 LYS B CB 9506 C CG . LYS B 298 ? 1.0270 0.5358 1.1344 -0.2646 -0.1239 -0.0149 298 LYS B CG 9507 C CD . LYS B 298 ? 1.1881 0.6655 1.2980 -0.3092 -0.1404 -0.0537 298 LYS B CD 9508 C CE . LYS B 298 ? 1.3894 0.9054 1.4697 -0.3246 -0.1252 -0.0904 298 LYS B CE 9509 N NZ . LYS B 298 ? 1.5058 1.1146 1.5596 -0.3341 -0.1214 -0.0430 298 LYS B NZ 9510 N N . LEU B 299 ? 1.0857 0.5378 1.2231 -0.2849 -0.1764 0.1330 299 LEU B N 9511 C CA . LEU B 299 ? 1.3718 0.7668 1.5130 -0.2929 -0.1995 0.1648 299 LEU B CA 9512 C C . LEU B 299 ? 1.3413 0.7238 1.4828 -0.3480 -0.2199 0.1924 299 LEU B C 9513 O O . LEU B 299 ? 1.2593 0.5836 1.4052 -0.3521 -0.2369 0.1913 299 LEU B O 9514 C CB . LEU B 299 ? 1.0981 0.5379 1.2232 -0.2723 -0.1852 0.2063 299 LEU B CB 9515 C CG . LEU B 299 ? 1.0650 0.4872 1.1912 -0.2226 -0.1754 0.1857 299 LEU B CG 9516 C CD1 . LEU B 299 ? 1.0387 0.5136 1.1451 -0.2134 -0.1591 0.2260 299 LEU B CD1 9517 C CD2 . LEU B 299 ? 1.6053 0.9296 1.7507 -0.2113 -0.2071 0.1656 299 LEU B CD2 9518 N N . SER B 300 ? 1.1732 0.6385 1.3075 -0.3758 -0.2077 0.2093 300 SER B N 9519 C CA . SER B 300 ? 1.2270 0.6976 1.3628 -0.4329 -0.2231 0.2336 300 SER B CA 9520 C C . SER B 300 ? 1.4134 0.8290 1.5609 -0.4560 -0.2372 0.1868 300 SER B C 9521 O O . SER B 300 ? 1.5364 0.9173 1.6862 -0.4797 -0.2472 0.1900 300 SER B O 9522 C CB . SER B 300 ? 1.2926 0.8824 1.4265 -0.4510 -0.2056 0.2589 300 SER B CB 9523 O OG . SER B 300 ? 1.7066 1.3104 1.8450 -0.5097 -0.2194 0.2786 300 SER B OG 9524 N N . GLN B 301 ? 1.3516 0.7682 1.5033 -0.4446 -0.2309 0.1384 301 GLN B N 9525 C CA . GLN B 301 ? 1.5180 0.9003 1.6784 -0.4633 -0.2339 0.0827 301 GLN B CA 9526 C C . GLN B 301 ? 1.5572 0.8525 1.7365 -0.4332 -0.2343 0.0503 301 GLN B C 9527 O O . GLN B 301 ? 1.4279 0.6871 1.6200 -0.4557 -0.2363 0.0255 301 GLN B O 9528 C CB . GLN B 301 ? 1.4758 0.8889 1.6274 -0.4598 -0.2233 0.0381 301 GLN B CB 9529 C CG . GLN B 301 ? 1.6892 1.2178 1.8196 -0.4784 -0.2138 0.0613 301 GLN B CG 9530 C CD . GLN B 301 ? 1.7841 1.3495 1.8944 -0.4681 -0.1991 0.0194 301 GLN B CD 9531 O OE1 . GLN B 301 ? 1.8912 1.3980 2.0030 -0.4512 -0.1920 -0.0333 301 GLN B OE1 9532 N NE2 . GLN B 301 ? 1.6873 1.3521 1.7799 -0.4793 -0.1951 0.0433 301 GLN B NE2 9533 N N . LYS B 302 ? 1.5497 0.8170 1.7332 -0.3832 -0.2313 0.0511 302 LYS B N 9534 C CA . LYS B 302 ? 1.4532 0.6520 1.6569 -0.3506 -0.2333 0.0245 302 LYS B CA 9535 C C . LYS B 302 ? 1.5347 0.6970 1.7371 -0.3523 -0.2537 0.0770 302 LYS B C 9536 O O . LYS B 302 ? 1.7307 0.8370 1.9506 -0.3264 -0.2630 0.0689 302 LYS B O 9537 C CB . LYS B 302 ? 1.3309 0.5290 1.5403 -0.2973 -0.2210 -0.0038 302 LYS B CB 9538 C CG . LYS B 302 ? 1.2924 0.5203 1.4973 -0.2947 -0.1975 -0.0598 302 LYS B CG 9539 C CD . LYS B 302 ? 1.3531 0.5537 1.5660 -0.3134 -0.1862 -0.1169 302 LYS B CD 9540 C CE . LYS B 302 ? 1.6167 0.8489 1.8106 -0.3150 -0.1611 -0.1719 302 LYS B CE 9541 N NZ . LYS B 302 ? 1.8160 1.0195 2.0009 -0.3370 -0.1485 -0.2270 302 LYS B NZ 9542 N N . ASN B 303 ? 1.4278 0.6276 1.6082 -0.3852 -0.2603 0.1320 303 ASN B N 9543 C CA . ASN B 303 ? 1.4809 0.6570 1.6484 -0.3960 -0.2766 0.1861 303 ASN B CA 9544 C C . ASN B 303 ? 1.4892 0.6393 1.6539 -0.3510 -0.2866 0.2034 303 ASN B C 9545 O O . ASN B 303 ? 1.7979 0.8923 1.9680 -0.3438 -0.3057 0.2187 303 ASN B O 9546 C CB . ASN B 303 ? 1.5792 0.6944 1.7609 -0.4225 -0.2870 0.1776 303 ASN B CB 9547 C CG . ASN B 303 ? 1.5947 0.7434 1.7752 -0.4762 -0.2790 0.1684 303 ASN B CG 9548 O OD1 . ASN B 303 ? 1.5582 0.7772 1.7196 -0.5057 -0.2748 0.2013 303 ASN B OD1 9549 N ND2 . ASN B 303 ? 1.6513 0.7569 1.8551 -0.4903 -0.2750 0.1211 303 ASN B ND2 9550 N N . ILE B 304 ? 1.4790 0.6708 1.6362 -0.3227 -0.2747 0.2016 304 ILE B N 9551 C CA . ILE B 304 ? 1.5306 0.7090 1.6852 -0.2816 -0.2825 0.2125 304 ILE B CA 9552 C C . ILE B 304 ? 1.3547 0.5833 1.4743 -0.2915 -0.2773 0.2665 304 ILE B C 9553 O O . ILE B 304 ? 1.2915 0.5800 1.4016 -0.3005 -0.2555 0.2729 304 ILE B O 9554 C CB . ILE B 304 ? 1.5680 0.7519 1.7439 -0.2366 -0.2678 0.1582 304 ILE B CB 9555 C CG1 . ILE B 304 ? 1.7836 0.9275 1.9922 -0.2274 -0.2659 0.1001 304 ILE B CG1 9556 C CG2 . ILE B 304 ? 1.4655 0.6452 1.6401 -0.1974 -0.2763 0.1690 304 ILE B CG2 9557 C CD1 . ILE B 304 ? 1.7869 0.9446 2.0128 -0.1874 -0.2461 0.0429 304 ILE B CD1 9558 N N . ASN B 305 ? 1.4058 0.6133 1.5068 -0.2914 -0.2961 0.3056 305 ASN B N 9559 C CA . ASN B 305 ? 1.3874 0.6452 1.4504 -0.3025 -0.2878 0.3527 305 ASN B CA 9560 C C . ASN B 305 ? 1.5737 0.8410 1.6358 -0.2600 -0.2837 0.3416 305 ASN B C 9561 O O . ASN B 305 ? 1.6059 0.8286 1.6807 -0.2304 -0.3066 0.3305 305 ASN B O 9562 C CB . ASN B 305 ? 1.4768 0.7127 1.5104 -0.3319 -0.3090 0.4019 305 ASN B CB 9563 C CG . ASN B 305 ? 1.6359 0.8750 1.6648 -0.3805 -0.3069 0.4174 305 ASN B CG 9564 O OD1 . ASN B 305 ? 1.9153 1.0922 1.9610 -0.3892 -0.3258 0.4092 305 ASN B OD1 9565 N ND2 . ASN B 305 ? 1.6476 0.9630 1.6580 -0.4125 -0.2817 0.4380 305 ASN B ND2 9566 N N . LEU B 306 ? 1.4711 0.7994 1.5226 -0.2574 -0.2540 0.3444 306 LEU B N 9567 C CA . LEU B 306 ? 1.2194 0.5588 1.2692 -0.2206 -0.2450 0.3324 306 LEU B CA 9568 C C . LEU B 306 ? 1.3351 0.6996 1.3421 -0.2342 -0.2487 0.3804 306 LEU B C 9569 O O . LEU B 306 ? 1.4333 0.8475 1.4103 -0.2725 -0.2335 0.4184 306 LEU B O 9570 C CB . LEU B 306 ? 1.2860 0.6953 1.3457 -0.2031 -0.2014 0.3016 306 LEU B CB 9571 C CG . LEU B 306 ? 1.0712 0.5183 1.1287 -0.1605 -0.1762 0.2741 306 LEU B CG 9572 C CD1 . LEU B 306 ? 1.0808 0.4624 1.1654 -0.1242 -0.1994 0.2337 306 LEU B CD1 9573 C CD2 . LEU B 306 ? 0.9923 0.5127 1.0584 -0.1451 -0.1292 0.2475 306 LEU B CD2 9574 N N . ILE B 307 ? 1.5204 0.8575 1.5251 -0.2046 -0.2680 0.3753 307 ILE B N 9575 C CA . ILE B 307 ? 1.4483 0.8089 1.4055 -0.2195 -0.2753 0.4194 307 ILE B CA 9576 C C . ILE B 307 ? 1.3964 0.8095 1.3523 -0.1812 -0.2496 0.3849 307 ILE B C 9577 O O . ILE B 307 ? 1.2139 0.5959 1.2039 -0.1396 -0.2615 0.3439 307 ILE B O 9578 C CB . ILE B 307 ? 1.3913 0.6975 1.3401 -0.2205 -0.3229 0.4421 307 ILE B CB 9579 C CG1 . ILE B 307 ? 1.5480 0.8271 1.4980 -0.2538 -0.3349 0.4602 307 ILE B CG1 9580 C CG2 . ILE B 307 ? 1.4339 0.7695 1.3259 -0.2387 -0.3323 0.4873 307 ILE B CG2 9581 C CD1 . ILE B 307 ? 1.6570 0.8772 1.6024 -0.2567 -0.3807 0.4870 307 ILE B CD1 9582 N N . PHE B 308 ? 1.4269 0.9244 1.3480 -0.1966 -0.2107 0.3957 308 PHE B N 9583 C CA . PHE B 308 ? 1.2250 0.7771 1.1417 -0.1663 -0.1813 0.3613 308 PHE B CA 9584 C C . PHE B 308 ? 1.3833 0.9384 1.2543 -0.1786 -0.2078 0.3923 308 PHE B C 9585 O O . PHE B 308 ? 1.4776 1.0691 1.2982 -0.2215 -0.2025 0.4356 308 PHE B O 9586 C CB . PHE B 308 ? 1.1357 0.7799 1.0493 -0.1721 -0.1188 0.3462 308 PHE B CB 9587 C CG . PHE B 308 ? 1.2640 0.9166 1.2230 -0.1487 -0.0910 0.3090 308 PHE B CG 9588 C CD1 . PHE B 308 ? 1.3533 1.0002 1.3418 -0.1047 -0.0743 0.2562 308 PHE B CD1 9589 C CD2 . PHE B 308 ? 1.5321 1.2022 1.5015 -0.1742 -0.0820 0.3279 308 PHE B CD2 9590 C CE1 . PHE B 308 ? 1.3042 0.9580 1.3250 -0.0877 -0.0504 0.2270 308 PHE B CE1 9591 C CE2 . PHE B 308 ? 1.4128 1.0952 1.4186 -0.1550 -0.0611 0.2981 308 PHE B CE2 9592 C CZ . PHE B 308 ? 1.1516 0.8237 1.1796 -0.1123 -0.0457 0.2497 308 PHE B CZ 9593 N N . ALA B 309 ? 1.3807 0.9029 1.2693 -0.1432 -0.2367 0.3692 309 ALA B N 9594 C CA . ALA B 309 ? 1.3761 0.9147 1.2230 -0.1500 -0.2617 0.3922 309 ALA B CA 9595 C C . ALA B 309 ? 1.4976 1.1018 1.3525 -0.1200 -0.2218 0.3362 309 ALA B C 9596 O O . ALA B 309 ? 1.6444 1.2279 1.5467 -0.0771 -0.2262 0.2880 309 ALA B O 9597 C CB . ALA B 309 ? 1.3502 0.8037 1.2150 -0.1345 -0.3334 0.4148 309 ALA B CB 9598 N N . VAL B 310 ? 1.4728 1.1569 1.2833 -0.1454 -0.1802 0.3392 310 VAL B N 9599 C CA . VAL B 310 ? 1.3423 1.0902 1.1640 -0.1214 -0.1299 0.2814 310 VAL B CA 9600 C C . VAL B 310 ? 1.4177 1.2296 1.1822 -0.1470 -0.1229 0.2893 310 VAL B C 9601 O O . VAL B 310 ? 1.4338 1.2553 1.1409 -0.1912 -0.1455 0.3433 310 VAL B O 9602 C CB . VAL B 310 ? 1.2781 1.0708 1.1224 -0.1194 -0.0634 0.2542 310 VAL B CB 9603 C CG1 . VAL B 310 ? 1.2054 0.9464 1.1060 -0.0880 -0.0648 0.2300 310 VAL B CG1 9604 C CG2 . VAL B 310 ? 1.2453 1.0744 1.0544 -0.1675 -0.0474 0.2999 310 VAL B CG2 9605 N N . THR B 311 ? 1.4615 1.3182 1.2389 -0.1234 -0.0898 0.2338 311 THR B N 9606 C CA . THR B 311 ? 1.5251 1.4495 1.2507 -0.1476 -0.0788 0.2288 311 THR B CA 9607 C C . THR B 311 ? 1.4718 1.4681 1.1582 -0.1904 -0.0217 0.2364 311 THR B C 9608 O O . THR B 311 ? 1.3992 1.4027 1.1152 -0.1885 0.0200 0.2297 311 THR B O 9609 C CB . THR B 311 ? 1.5885 1.5425 1.3448 -0.1127 -0.0527 0.1591 311 THR B CB 9610 O OG1 . THR B 311 ? 1.7201 1.6876 1.5211 -0.0900 0.0132 0.1103 311 THR B OG1 9611 C CG2 . THR B 311 ? 1.6357 1.5313 1.4341 -0.0735 -0.1099 0.1478 311 THR B CG2 9612 N N . GLU B 312 ? 1.5028 1.5570 1.1247 -0.2300 -0.0205 0.2487 312 GLU B N 9613 C CA . GLU B 312 ? 1.5160 1.6429 1.0941 -0.2798 0.0297 0.2580 312 GLU B CA 9614 C C . GLU B 312 ? 1.6045 1.7868 1.2284 -0.2630 0.1141 0.1948 312 GLU B C 9615 O O . GLU B 312 ? 1.6572 1.8896 1.2771 -0.2917 0.1616 0.1976 312 GLU B O 9616 C CB . GLU B 312 ? 1.5895 1.7710 1.0844 -0.3271 0.0138 0.2756 312 GLU B CB 9617 C CG . GLU B 312 ? 1.8326 2.0446 1.2560 -0.3945 0.0131 0.3331 312 GLU B CG 9618 C CD . GLU B 312 ? 1.8995 2.1856 1.3353 -0.4187 0.0966 0.3021 312 GLU B CD 9619 O OE1 . GLU B 312 ? 1.9482 2.2319 1.3788 -0.4482 0.1028 0.3404 312 GLU B OE1 9620 O OE2 . GLU B 312 ? 1.8167 2.1645 1.2727 -0.4083 0.1567 0.2375 312 GLU B OE2 9621 N N . ASN B 313 ? 1.5495 1.7225 1.2210 -0.2170 0.1331 0.1376 313 ASN B N 9622 C CA . ASN B 313 ? 1.2426 1.4560 0.9608 -0.1977 0.2106 0.0795 313 ASN B CA 9623 C C . ASN B 313 ? 1.1847 1.3644 0.9633 -0.1707 0.2291 0.0857 313 ASN B C 9624 O O . ASN B 313 ? 1.3038 1.5275 1.1089 -0.1755 0.2854 0.0719 313 ASN B O 9625 C CB . ASN B 313 ? 1.1863 1.3976 0.9307 -0.1627 0.2257 0.0175 313 ASN B CB 9626 C CG . ASN B 313 ? 1.2644 1.3985 1.0494 -0.1178 0.1799 0.0150 313 ASN B CG 9627 O OD1 . ASN B 313 ? 1.4021 1.5047 1.1677 -0.1170 0.1158 0.0391 313 ASN B OD1 9628 N ND2 . ASN B 313 ? 1.2122 1.3166 1.0557 -0.0808 0.2127 -0.0146 313 ASN B ND2 9629 N N . VAL B 314 ? 1.2051 1.3104 1.0082 -0.1430 0.1807 0.1052 314 VAL B N 9630 C CA . VAL B 314 ? 1.1550 1.2272 1.0116 -0.1173 0.1923 0.1081 314 VAL B CA 9631 C C . VAL B 314 ? 1.2399 1.2958 1.0834 -0.1464 0.1610 0.1677 314 VAL B C 9632 O O . VAL B 314 ? 1.1165 1.1501 0.9992 -0.1324 0.1636 0.1762 314 VAL B O 9633 C CB . VAL B 314 ? 1.1749 1.1790 1.0691 -0.0724 0.1665 0.0829 314 VAL B CB 9634 C CG1 . VAL B 314 ? 1.2652 1.2038 1.1476 -0.0758 0.0939 0.1227 314 VAL B CG1 9635 C CG2 . VAL B 314 ? 1.2880 1.2800 1.2356 -0.0431 0.2029 0.0631 314 VAL B CG2 9636 N N . VAL B 315 ? 1.3092 1.3784 1.0944 -0.1907 0.1317 0.2094 315 VAL B N 9637 C CA . VAL B 315 ? 1.2795 1.3254 1.0458 -0.2245 0.0983 0.2683 315 VAL B CA 9638 C C . VAL B 315 ? 1.3612 1.4626 1.1541 -0.2420 0.1468 0.2725 315 VAL B C 9639 O O . VAL B 315 ? 1.3783 1.4549 1.1876 -0.2520 0.1281 0.3044 315 VAL B O 9640 C CB . VAL B 315 ? 1.6218 1.6713 1.3112 -0.2743 0.0588 0.3163 315 VAL B CB 9641 C CG1 . VAL B 315 ? 1.6857 1.8288 1.3333 -0.3142 0.1091 0.3043 315 VAL B CG1 9642 C CG2 . VAL B 315 ? 1.5260 1.5306 1.1974 -0.3079 0.0174 0.3790 315 VAL B CG2 9643 N N . ASN B 316 ? 1.3471 1.5256 1.1509 -0.2450 0.2095 0.2368 316 ASN B N 9644 C CA . ASN B 316 ? 1.2104 1.4514 1.0532 -0.2566 0.2586 0.2350 316 ASN B CA 9645 C C . ASN B 316 ? 1.2448 1.4610 1.1609 -0.2102 0.2679 0.2203 316 ASN B C 9646 O O . ASN B 316 ? 1.2738 1.5159 1.2245 -0.2187 0.2775 0.2391 316 ASN B O 9647 C CB . ASN B 316 ? 1.0331 1.3600 0.8786 -0.2677 0.3258 0.1931 316 ASN B CB 9648 C CG . ASN B 316 ? 1.1386 1.5390 0.9526 -0.3279 0.3491 0.2158 316 ASN B CG 9649 O OD1 . ASN B 316 ? 1.4349 1.8871 1.3009 -0.3300 0.3879 0.2095 316 ASN B OD1 9650 N ND2 . ASN B 316 ? 1.3405 1.7456 1.0714 -0.3761 0.3230 0.2419 316 ASN B ND2 9651 N N . LEU B 317 ? 1.0764 1.2461 1.0139 -0.1642 0.2638 0.1871 317 LEU B N 9652 C CA . LEU B 317 ? 1.0069 1.1469 1.0020 -0.1226 0.2689 0.1742 317 LEU B CA 9653 C C . LEU B 317 ? 0.9752 1.0614 0.9704 -0.1296 0.2161 0.2124 317 LEU B C 9654 O O . LEU B 317 ? 1.1630 1.2655 1.1953 -0.1280 0.2222 0.2263 317 LEU B O 9655 C CB . LEU B 317 ? 1.0654 1.1646 1.0729 -0.0800 0.2757 0.1294 317 LEU B CB 9656 C CG . LEU B 317 ? 0.8463 0.9027 0.8982 -0.0418 0.2730 0.1187 317 LEU B CG 9657 C CD1 . LEU B 317 ? 0.8369 0.9420 0.9415 -0.0271 0.3205 0.1145 317 LEU B CD1 9658 C CD2 . LEU B 317 ? 0.8198 0.8306 0.8730 -0.0092 0.2740 0.0760 317 LEU B CD2 9659 N N . TYR B 318 ? 1.0123 1.0357 0.9698 -0.1375 0.1636 0.2279 318 TYR B N 9660 C CA . TYR B 318 ? 1.0117 0.9720 0.9727 -0.1425 0.1137 0.2558 318 TYR B CA 9661 C C . TYR B 318 ? 1.0257 1.0067 0.9716 -0.1900 0.1003 0.3042 318 TYR B C 9662 O O . TYR B 318 ? 1.0497 0.9968 1.0111 -0.1975 0.0733 0.3234 318 TYR B O 9663 C CB . TYR B 318 ? 1.0548 0.9408 0.9908 -0.1345 0.0624 0.2560 318 TYR B CB 9664 C CG . TYR B 318 ? 1.0604 0.9144 1.0245 -0.0876 0.0681 0.2063 318 TYR B CG 9665 C CD1 . TYR B 318 ? 1.0954 0.9724 1.0513 -0.0705 0.0910 0.1711 318 TYR B CD1 9666 C CD2 . TYR B 318 ? 1.0622 0.8670 1.0590 -0.0653 0.0535 0.1913 318 TYR B CD2 9667 C CE1 . TYR B 318 ? 1.0889 0.9388 1.0711 -0.0320 0.0991 0.1237 318 TYR B CE1 9668 C CE2 . TYR B 318 ? 1.1264 0.9049 1.1458 -0.0281 0.0624 0.1441 318 TYR B CE2 9669 C CZ . TYR B 318 ? 1.1519 0.9526 1.1653 -0.0113 0.0855 0.1110 318 TYR B CZ 9670 O OH . TYR B 318 ? 1.0807 0.8575 1.1171 0.0217 0.0970 0.0621 318 TYR B OH 9671 N N . GLN B 319 ? 1.1002 1.1392 1.0142 -0.2262 0.1213 0.3206 319 GLN B N 9672 C CA . GLN B 319 ? 1.2930 1.3677 1.1960 -0.2758 0.1209 0.3613 319 GLN B CA 9673 C C . GLN B 319 ? 1.1812 1.3100 1.1472 -0.2640 0.1548 0.3509 319 GLN B C 9674 O O . GLN B 319 ? 1.3168 1.4389 1.2981 -0.2840 0.1348 0.3769 319 GLN B O 9675 C CB . GLN B 319 ? 1.1487 1.2866 1.0042 -0.3194 0.1460 0.3731 319 GLN B CB 9676 C CG . GLN B 319 ? 1.2594 1.3475 1.0405 -0.3541 0.0978 0.4112 319 GLN B CG 9677 C CD . GLN B 319 ? 1.5493 1.7062 1.2740 -0.4117 0.1219 0.4311 319 GLN B CD 9678 O OE1 . GLN B 319 ? 1.7607 2.0047 1.5086 -0.4281 0.1770 0.4139 319 GLN B OE1 9679 N NE2 . GLN B 319 ? 1.6355 1.7557 1.2873 -0.4438 0.0804 0.4676 319 GLN B NE2 9680 N N . ASN B 320 ? 1.1057 1.2879 1.1110 -0.2313 0.2050 0.3129 320 ASN B N 9681 C CA . ASN B 320 ? 0.9475 1.1822 1.0208 -0.2113 0.2358 0.3035 320 ASN B CA 9682 C C . ASN B 320 ? 0.8752 1.0529 0.9755 -0.1793 0.2056 0.3015 320 ASN B C 9683 O O . ASN B 320 ? 0.9763 1.1846 1.1195 -0.1779 0.2063 0.3126 320 ASN B O 9684 C CB . ASN B 320 ? 0.7954 1.0880 0.9065 -0.1809 0.2957 0.2631 320 ASN B CB 9685 C CG . ASN B 320 ? 1.0687 1.4496 1.1797 -0.2173 0.3385 0.2617 320 ASN B CG 9686 O OD1 . ASN B 320 ? 1.2854 1.6856 1.3608 -0.2687 0.3232 0.2937 320 ASN B OD1 9687 N ND2 . ASN B 320 ? 1.4408 1.8747 1.5922 -0.1939 0.3950 0.2226 320 ASN B ND2 9688 N N . TYR B 321 ? 0.9699 1.0704 1.0454 -0.1561 0.1792 0.2854 321 TYR B N 9689 C CA . TYR B 321 ? 0.9707 1.0118 1.0615 -0.1333 0.1493 0.2792 321 TYR B CA 9690 C C . TYR B 321 ? 0.8796 0.8890 0.9576 -0.1697 0.1045 0.3134 321 TYR B C 9691 O O . TYR B 321 ? 1.1315 1.1354 1.2351 -0.1670 0.0915 0.3162 321 TYR B O 9692 C CB . TYR B 321 ? 1.1865 1.1578 1.2571 -0.1042 0.1342 0.2486 321 TYR B CB 9693 C CG . TYR B 321 ? 1.1032 1.0801 1.2018 -0.0599 0.1701 0.2087 321 TYR B CG 9694 C CD1 . TYR B 321 ? 0.9168 0.9240 1.0567 -0.0418 0.1918 0.2075 321 TYR B CD1 9695 C CD2 . TYR B 321 ? 1.2785 1.2302 1.3624 -0.0380 0.1806 0.1743 321 TYR B CD2 9696 C CE1 . TYR B 321 ? 1.1245 1.1283 1.2866 -0.0037 0.2239 0.1765 321 TYR B CE1 9697 C CE2 . TYR B 321 ? 1.1440 1.0957 1.2517 -0.0021 0.2159 0.1378 321 TYR B CE2 9698 C CZ . TYR B 321 ? 1.0744 1.0479 1.2194 0.0147 0.2378 0.1408 321 TYR B CZ 9699 O OH . TYR B 321 ? 1.0468 1.0122 1.2121 0.0482 0.2721 0.1099 321 TYR B OH 9700 N N . SER B 322 ? 1.0064 0.9944 1.0423 -0.2066 0.0807 0.3401 322 SER B N 9701 C CA . SER B 322 ? 1.1630 1.1072 1.1833 -0.2450 0.0376 0.3737 322 SER B CA 9702 C C . SER B 322 ? 1.1240 1.1347 1.1700 -0.2782 0.0500 0.3968 322 SER B C 9703 O O . SER B 322 ? 1.2004 1.1825 1.2514 -0.3023 0.0204 0.4132 322 SER B O 9704 C CB . SER B 322 ? 1.1081 1.0121 1.0742 -0.2778 0.0098 0.4031 322 SER B CB 9705 O OG . SER B 322 ? 1.4194 1.3966 1.3633 -0.3050 0.0425 0.4170 322 SER B OG 9706 N N . GLU B 323 ? 1.0827 1.1851 1.1501 -0.2801 0.0950 0.3943 323 GLU B N 9707 C CA . GLU B 323 ? 1.0158 1.1974 1.1192 -0.3094 0.1106 0.4125 323 GLU B CA 9708 C C . GLU B 323 ? 0.9497 1.1429 1.1035 -0.2853 0.1029 0.4031 323 GLU B C 9709 O O . GLU B 323 ? 0.8693 1.1105 1.0514 -0.3130 0.0975 0.4208 323 GLU B O 9710 C CB . GLU B 323 ? 0.8850 1.1659 1.0131 -0.3096 0.1649 0.4028 323 GLU B CB 9711 C CG . GLU B 323 ? 1.2553 1.5413 1.3267 -0.3441 0.1761 0.4123 323 GLU B CG 9712 C CD . GLU B 323 ? 1.6214 2.0136 1.7212 -0.3515 0.2351 0.3958 323 GLU B CD 9713 O OE1 . GLU B 323 ? 1.7552 2.2218 1.9255 -0.3391 0.2623 0.3869 323 GLU B OE1 9714 O OE2 . GLU B 323 ? 1.6558 2.0598 1.7103 -0.3701 0.2540 0.3902 323 GLU B OE2 9715 N N . LEU B 324 ? 1.0057 1.1587 1.1682 -0.2371 0.1021 0.3752 324 LEU B N 9716 C CA . LEU B 324 ? 1.0537 1.2118 1.2518 -0.2159 0.0921 0.3673 324 LEU B CA 9717 C C . LEU B 324 ? 0.9569 1.0322 1.1279 -0.2319 0.0457 0.3670 324 LEU B C 9718 O O . LEU B 324 ? 1.1318 1.2105 1.3216 -0.2293 0.0310 0.3625 324 LEU B O 9719 C CB . LEU B 324 ? 0.7985 0.9567 1.0173 -0.1605 0.1190 0.3378 324 LEU B CB 9720 C CG . LEU B 324 ? 0.7688 1.0093 1.0318 -0.1383 0.1683 0.3327 324 LEU B CG 9721 C CD1 . LEU B 324 ? 1.0718 1.2917 1.3494 -0.0860 0.1929 0.3039 324 LEU B CD1 9722 C CD2 . LEU B 324 ? 0.7394 1.0690 1.0594 -0.1500 0.1736 0.3544 324 LEU B CD2 9723 N N . ILE B 325 ? 0.8668 0.8689 0.9953 -0.2495 0.0220 0.3713 325 ILE B N 9724 C CA . ILE B 325 ? 0.9761 0.8927 1.0867 -0.2655 -0.0208 0.3682 325 ILE B CA 9725 C C . ILE B 325 ? 1.0758 0.9639 1.1599 -0.3176 -0.0457 0.4030 325 ILE B C 9726 O O . ILE B 325 ? 1.4463 1.2778 1.4969 -0.3219 -0.0606 0.4124 325 ILE B O 9727 C CB . ILE B 325 ? 1.1895 1.0242 1.2830 -0.2295 -0.0326 0.3363 325 ILE B CB 9728 C CG1 . ILE B 325 ? 1.0446 0.9085 1.1562 -0.1811 0.0001 0.3044 325 ILE B CG1 9729 C CG2 . ILE B 325 ? 1.2898 1.0446 1.3814 -0.2401 -0.0705 0.3218 325 ILE B CG2 9730 C CD1 . ILE B 325 ? 1.0431 0.8388 1.1421 -0.1477 -0.0057 0.2685 325 ILE B CD1 9731 N N . PRO B 326 ? 1.0175 0.9464 1.1166 -0.3594 -0.0513 0.4242 326 PRO B N 9732 C CA . PRO B 326 ? 1.2423 1.1502 1.3173 -0.4172 -0.0705 0.4603 326 PRO B CA 9733 C C . PRO B 326 ? 1.4306 1.2159 1.4760 -0.4281 -0.1130 0.4638 326 PRO B C 9734 O O . PRO B 326 ? 1.6354 1.3619 1.6931 -0.4037 -0.1313 0.4332 326 PRO B O 9735 C CB . PRO B 326 ? 1.3201 1.2885 1.4282 -0.4514 -0.0717 0.4671 326 PRO B CB 9736 C CG . PRO B 326 ? 1.0841 1.1399 1.2349 -0.4112 -0.0429 0.4471 326 PRO B CG 9737 C CD . PRO B 326 ? 0.9568 0.9591 1.0982 -0.3552 -0.0403 0.4161 326 PRO B CD 9738 N N . GLY B 327 ? 1.3048 1.0604 1.3135 -0.4531 -0.1255 0.4875 327 GLY B N 9739 C CA . GLY B 327 ? 1.6965 1.3449 1.6842 -0.4516 -0.1648 0.4860 327 GLY B CA 9740 C C . GLY B 327 ? 1.7884 1.3838 1.7586 -0.4130 -0.1762 0.4803 327 GLY B C 9741 O O . GLY B 327 ? 1.8665 1.3792 1.8272 -0.4041 -0.2097 0.4792 327 GLY B O 9742 N N . THR B 328 ? 1.3268 0.9735 1.2977 -0.3896 -0.1477 0.4762 328 THR B N 9743 C CA . THR B 328 ? 1.4090 1.0162 1.3639 -0.3548 -0.1562 0.4689 328 THR B CA 9744 C C . THR B 328 ? 1.4818 1.1376 1.3934 -0.3719 -0.1400 0.4975 328 THR B C 9745 O O . THR B 328 ? 1.4397 1.1866 1.3500 -0.3902 -0.1005 0.5042 328 THR B O 9746 C CB . THR B 328 ? 1.2684 0.9055 1.2550 -0.2985 -0.1293 0.4161 328 THR B CB 9747 O OG1 . THR B 328 ? 1.3499 1.0897 1.3448 -0.2941 -0.0817 0.4116 328 THR B OG1 9748 C CG2 . THR B 328 ? 1.2565 0.8599 1.2787 -0.2873 -0.1401 0.3847 328 THR B CG2 9749 N N . THR B 329 ? 1.4189 1.0205 1.2987 -0.3646 -0.1700 0.5093 329 THR B N 9750 C CA . THR B 329 ? 1.3248 0.9686 1.1537 -0.3854 -0.1601 0.5358 329 THR B CA 9751 C C . THR B 329 ? 1.3016 0.9363 1.1191 -0.3490 -0.1632 0.5207 329 THR B C 9752 O O . THR B 329 ? 1.2810 0.8582 1.1292 -0.3053 -0.1859 0.4903 329 THR B O 9753 C CB . THR B 329 ? 1.4323 1.0354 1.2237 -0.4179 -0.1956 0.5696 329 THR B CB 9754 O OG1 . THR B 329 ? 1.6339 1.2738 1.3702 -0.4373 -0.1906 0.5932 329 THR B OG1 9755 C CG2 . THR B 329 ? 1.4785 0.9770 1.2881 -0.3914 -0.2475 0.5654 329 THR B CG2 9756 N N . VAL B 330 ? 1.3041 1.0084 1.0826 -0.3631 -0.1353 0.5272 330 VAL B N 9757 C CA . VAL B 330 ? 1.2785 0.9985 1.0475 -0.3271 -0.1293 0.4978 330 VAL B CA 9758 C C . VAL B 330 ? 1.3699 1.0832 1.0697 -0.3609 -0.1580 0.5416 330 VAL B C 9759 O O . VAL B 330 ? 1.4370 1.1694 1.0903 -0.4167 -0.1582 0.5874 330 VAL B O 9760 C CB . VAL B 330 ? 1.2239 1.0419 1.0128 -0.3085 -0.0626 0.4529 330 VAL B CB 9761 C CG1 . VAL B 330 ? 1.2205 1.0435 1.0132 -0.2652 -0.0551 0.4103 330 VAL B CG1 9762 C CG2 . VAL B 330 ? 1.1204 0.9554 0.9691 -0.2874 -0.0356 0.4259 330 VAL B CG2 9763 N N . GLY B 331 ? 1.3769 1.0677 1.0692 -0.3294 -0.1827 0.5270 331 GLY B N 9764 C CA . GLY B 331 ? 1.6607 1.3509 1.2853 -0.3586 -0.2149 0.5685 331 GLY B CA 9765 C C . GLY B 331 ? 1.4358 1.1615 1.0572 -0.3241 -0.2093 0.5289 331 GLY B C 9766 O O . GLY B 331 ? 1.3635 1.0833 1.0415 -0.2712 -0.1965 0.4735 331 GLY B O 9767 N N . VAL B 332 ? 1.5037 1.2688 1.0553 -0.3586 -0.2186 0.5569 332 VAL B N 9768 C CA . VAL B 332 ? 1.4850 1.3026 1.0247 -0.3373 -0.2070 0.5176 332 VAL B CA 9769 C C . VAL B 332 ? 1.6990 1.4537 1.2493 -0.3036 -0.2768 0.5272 332 VAL B C 9770 O O . VAL B 332 ? 1.9670 1.6651 1.4819 -0.3253 -0.3401 0.5906 332 VAL B O 9771 C CB . VAL B 332 ? 1.7106 1.6140 1.1666 -0.3952 -0.1807 0.5366 332 VAL B CB 9772 C CG1 . VAL B 332 ? 1.7267 1.6861 1.1686 -0.3774 -0.1701 0.4927 332 VAL B CG1 9773 C CG2 . VAL B 332 ? 1.7834 1.7594 1.2432 -0.4247 -0.1067 0.5179 332 VAL B CG2 9774 N N . LEU B 333 ? 1.7064 1.4713 1.3100 -0.2504 -0.2652 0.4643 333 LEU B N 9775 C CA . LEU B 333 ? 1.6108 1.3346 1.2367 -0.2144 -0.3256 0.4614 333 LEU B CA 9776 C C . LEU B 333 ? 1.6741 1.4780 1.2569 -0.2229 -0.3175 0.4407 333 LEU B C 9777 O O . LEU B 333 ? 1.7530 1.6165 1.3581 -0.2035 -0.2623 0.3743 333 LEU B O 9778 C CB . LEU B 333 ? 1.5427 1.2237 1.2610 -0.1526 -0.3205 0.4013 333 LEU B CB 9779 C CG . LEU B 333 ? 1.5426 1.1492 1.3122 -0.1123 -0.3912 0.4051 333 LEU B CG 9780 C CD1 . LEU B 333 ? 1.7537 1.2648 1.5326 -0.1241 -0.4412 0.4631 333 LEU B CD1 9781 C CD2 . LEU B 333 ? 1.5142 1.1147 1.3658 -0.0569 -0.3671 0.3261 333 LEU B CD2 9782 N N . SER B 334 ? 1.7834 1.5875 1.3023 -0.2544 -0.3734 0.4988 334 SER B N 9783 C CA . SER B 334 ? 1.9998 1.8861 1.4665 -0.2718 -0.3716 0.4845 334 SER B CA 9784 C C . SER B 334 ? 2.0429 1.9018 1.4637 -0.2862 -0.4610 0.5525 334 SER B C 9785 O O . SER B 334 ? 1.9745 1.7541 1.3840 -0.2984 -0.5164 0.6231 334 SER B O 9786 C CB . SER B 334 ? 2.0179 1.9940 1.4127 -0.3299 -0.3037 0.4791 334 SER B CB 9787 O OG . SER B 334 ? 1.9201 1.8751 1.2528 -0.3853 -0.3181 0.5518 334 SER B OG 9788 N N . MET B 335 ? 2.0011 1.9259 1.3965 -0.2860 -0.4759 0.5321 335 MET B N 9789 C CA . MET B 335 ? 2.1559 2.0670 1.5087 -0.2973 -0.5653 0.5965 335 MET B CA 9790 C C . MET B 335 ? 2.3365 2.2647 1.5700 -0.3754 -0.5811 0.6783 335 MET B C 9791 O O . MET B 335 ? 2.4028 2.2796 1.6168 -0.3849 -0.6500 0.7459 335 MET B O 9792 C CB . MET B 335 ? 2.0933 2.0841 1.4516 -0.2791 -0.5744 0.5469 335 MET B CB 9793 C CG . MET B 335 ? 1.9135 1.8704 1.3889 -0.2022 -0.5950 0.4896 335 MET B CG 9794 S SD . MET B 335 ? 2.4795 2.5385 1.9652 -0.1854 -0.6049 0.4280 335 MET B SD 9795 C CE . MET B 335 ? 1.9966 2.0810 1.3785 -0.2352 -0.6986 0.5272 335 MET B CE 9796 N N . ASP B 336 ? 2.3282 2.3312 1.5031 -0.4262 -0.5033 0.6559 336 ASP B N 9797 C CA . ASP B 336 ? 2.5022 2.5201 1.5853 -0.4996 -0.4987 0.7168 336 ASP B CA 9798 C C . ASP B 336 ? 2.4660 2.4347 1.5788 -0.5085 -0.4571 0.7248 336 ASP B C 9799 O O . ASP B 336 ? 2.2562 2.2750 1.3691 -0.5211 -0.3822 0.6835 336 ASP B O 9800 C CB . ASP B 336 ? 2.4080 2.5510 1.4109 -0.5562 -0.4394 0.6824 336 ASP B CB 9801 C CG . ASP B 336 ? 2.4233 2.5866 1.3624 -0.6205 -0.4405 0.7253 336 ASP B CG 9802 O OD1 . ASP B 336 ? 2.4019 2.6473 1.2792 -0.6592 -0.4340 0.7145 336 ASP B OD1 9803 O OD2 . ASP B 336 ? 2.3290 2.4290 1.2794 -0.6350 -0.4477 0.7669 336 ASP B OD2 9804 N N . SER B 337 ? 2.5898 2.4660 1.7332 -0.5023 -0.5032 0.7733 337 SER B N 9805 C CA . SER B 337 ? 2.4669 2.2861 1.6502 -0.5055 -0.4783 0.7811 337 SER B CA 9806 C C . SER B 337 ? 2.6311 2.3477 1.8480 -0.4922 -0.5442 0.8299 337 SER B C 9807 O O . SER B 337 ? 2.4694 2.1597 1.6847 -0.4761 -0.6057 0.8567 337 SER B O 9808 C CB . SER B 337 ? 2.3799 2.1762 1.6315 -0.4589 -0.4468 0.7372 337 SER B CB 9809 O OG . SER B 337 ? 2.4873 2.3781 1.7184 -0.4760 -0.3674 0.6871 337 SER B OG 9810 N N . SER B 338 ? 2.8073 2.4703 2.0575 -0.4990 -0.5298 0.8384 338 SER B N 9811 C CA . SER B 338 ? 2.8101 2.3693 2.1081 -0.4786 -0.5843 0.8709 338 SER B CA 9812 C C . SER B 338 ? 2.6256 2.1202 2.0168 -0.4050 -0.6128 0.8386 338 SER B C 9813 O O . SER B 338 ? 2.6533 2.0634 2.1001 -0.3768 -0.6579 0.8525 338 SER B O 9814 C CB . SER B 338 ? 2.7454 2.2775 2.0475 -0.5125 -0.5564 0.8825 338 SER B CB 9815 O OG . SER B 338 ? 2.7196 2.3137 1.9420 -0.5801 -0.5301 0.9074 338 SER B OG 9816 N N . ASN B 339 ? 2.3384 1.8768 1.7466 -0.3765 -0.5830 0.7922 339 ASN B N 9817 C CA . ASN B 339 ? 2.3340 1.8279 1.8275 -0.3080 -0.6035 0.7513 339 ASN B CA 9818 C C . ASN B 339 ? 2.5681 1.9774 2.1447 -0.2790 -0.6031 0.7329 339 ASN B C 9819 O O . ASN B 339 ? 2.7731 2.1785 2.3413 -0.3094 -0.5663 0.7367 339 ASN B O 9820 C CB . ASN B 339 ? 2.4971 1.9749 2.0111 -0.2737 -0.6705 0.7621 339 ASN B CB 9821 C CG . ASN B 339 ? 2.5095 1.9924 2.0894 -0.2116 -0.6816 0.7085 339 ASN B CG 9822 O OD1 . ASN B 339 ? 2.3939 1.8692 2.0160 -0.1877 -0.6439 0.6636 339 ASN B OD1 9823 N ND2 . ASN B 339 ? 2.3193 1.8177 1.9132 -0.1845 -0.7335 0.7100 339 ASN B ND2 9824 N N . VAL B 340 ? 2.6686 2.0176 2.3271 -0.2225 -0.6442 0.7095 340 VAL B N 9825 C CA . VAL B 340 ? 2.5583 1.8415 2.3035 -0.1884 -0.6356 0.6706 340 VAL B CA 9826 C C . VAL B 340 ? 2.4716 1.6890 2.2304 -0.2078 -0.6572 0.7020 340 VAL B C 9827 O O . VAL B 340 ? 2.4684 1.6459 2.2729 -0.2024 -0.6380 0.6776 340 VAL B O 9828 C CB . VAL B 340 ? 2.0004 1.2575 1.8348 -0.1203 -0.6628 0.6191 340 VAL B CB 9829 C CG1 . VAL B 340 ? 2.0243 1.2062 1.9316 -0.0941 -0.7042 0.6171 340 VAL B CG1 9830 C CG2 . VAL B 340 ? 1.7350 1.0006 1.6142 -0.0920 -0.6162 0.5562 340 VAL B CG2 9831 N N . LEU B 341 ? 2.2674 1.4770 1.9803 -0.2346 -0.6960 0.7575 341 LEU B N 9832 C CA . LEU B 341 ? 2.4791 1.6195 2.2025 -0.2522 -0.7238 0.7933 341 LEU B CA 9833 C C . LEU B 341 ? 2.6411 1.7905 2.3191 -0.3062 -0.6825 0.8102 341 LEU B C 9834 O O . LEU B 341 ? 2.6873 1.7915 2.4095 -0.3028 -0.6695 0.7914 341 LEU B O 9835 C CB . LEU B 341 ? 2.5727 1.7034 2.2557 -0.2665 -0.7783 0.8516 341 LEU B CB 9836 C CG . LEU B 341 ? 2.7018 1.8305 2.4364 -0.2116 -0.8232 0.8351 341 LEU B CG 9837 C CD1 . LEU B 341 ? 2.8285 1.9527 2.5209 -0.2268 -0.8795 0.8969 341 LEU B CD1 9838 C CD2 . LEU B 341 ? 2.7420 1.8036 2.5894 -0.1560 -0.8368 0.7886 341 LEU B CD2 9839 N N . GLN B 342 ? 2.6852 1.8993 2.2764 -0.3577 -0.6608 0.8422 342 GLN B N 9840 C CA . GLN B 342 ? 2.6159 1.8566 2.1657 -0.4104 -0.6167 0.8529 342 GLN B CA 9841 C C . GLN B 342 ? 2.4757 1.7443 2.0635 -0.3962 -0.5627 0.8003 342 GLN B C 9842 O O . GLN B 342 ? 2.5397 1.7896 2.1453 -0.4135 -0.5415 0.7943 342 GLN B O 9843 C CB . GLN B 342 ? 2.6044 1.9248 2.0594 -0.4659 -0.5976 0.8851 342 GLN B CB 9844 C CG . GLN B 342 ? 2.4624 1.7574 1.8609 -0.5144 -0.6295 0.9464 342 GLN B CG 9845 C CD . GLN B 342 ? 2.5536 1.7416 2.0017 -0.4932 -0.6813 0.9700 342 GLN B CD 9846 O OE1 . GLN B 342 ? 2.5999 1.7442 2.0794 -0.4551 -0.7319 0.9805 342 GLN B OE1 9847 N NE2 . GLN B 342 ? 2.6817 1.8301 2.1399 -0.5181 -0.6681 0.9772 342 GLN B NE2 9848 N N . LEU B 343 ? 1.9856 1.3588 1.9748 -0.3525 -0.4813 0.0877 343 LEU B N 9849 C CA . LEU B 343 ? 1.9405 1.2674 1.9002 -0.3550 -0.4433 0.0692 343 LEU B CA 9850 C C . LEU B 343 ? 1.8434 1.1685 1.8407 -0.3476 -0.4029 0.0801 343 LEU B C 9851 O O . LEU B 343 ? 1.8432 1.1363 1.7898 -0.3356 -0.3755 0.0798 343 LEU B O 9852 C CB . LEU B 343 ? 1.9760 1.2863 1.9612 -0.3815 -0.4494 0.0449 343 LEU B CB 9853 C CG . LEU B 343 ? 2.0283 1.2984 2.0201 -0.3962 -0.4139 0.0339 343 LEU B CG 9854 C CD1 . LEU B 343 ? 2.2516 1.4632 2.1577 -0.3856 -0.4021 0.0235 343 LEU B CD1 9855 C CD2 . LEU B 343 ? 1.9302 1.2017 1.9709 -0.4287 -0.4255 0.0164 343 LEU B CD2 9856 N N . ILE B 344 ? 1.7955 1.1584 1.8854 -0.3548 -0.4003 0.0861 344 ILE B N 9857 C CA . ILE B 344 ? 1.7238 1.0938 1.8552 -0.3499 -0.3613 0.0911 344 ILE B CA 9858 C C . ILE B 344 ? 1.7324 1.1104 1.8447 -0.3224 -0.3574 0.1134 344 ILE B C 9859 O O . ILE B 344 ? 1.6915 1.0507 1.7762 -0.3120 -0.3241 0.1158 344 ILE B O 9860 C CB . ILE B 344 ? 1.6808 1.0982 1.9269 -0.3649 -0.3584 0.0832 344 ILE B CB 9861 C CG1 . ILE B 344 ? 1.6588 1.0630 1.9181 -0.3972 -0.3368 0.0608 344 ILE B CG1 9862 C CG2 . ILE B 344 ? 1.6265 1.0712 1.9289 -0.3504 -0.3324 0.0907 344 ILE B CG2 9863 C CD1 . ILE B 344 ? 1.6187 1.0746 1.9877 -0.4155 -0.3177 0.0464 344 ILE B CD1 9864 N N . VAL B 345 ? 1.8460 1.2509 1.9712 -0.3132 -0.3938 0.1316 345 VAL B N 9865 C CA . VAL B 345 ? 1.7809 1.1926 1.8874 -0.2921 -0.3950 0.1571 345 VAL B CA 9866 C C . VAL B 345 ? 1.8060 1.1838 1.8050 -0.2817 -0.3786 0.1564 345 VAL B C 9867 O O . VAL B 345 ? 1.8135 1.1838 1.7967 -0.2670 -0.3519 0.1644 345 VAL B O 9868 C CB . VAL B 345 ? 1.8566 1.2982 1.9862 -0.2902 -0.4449 0.1821 345 VAL B CB 9869 C CG1 . VAL B 345 ? 2.0121 1.4495 2.0778 -0.2767 -0.4504 0.2096 345 VAL B CG1 9870 C CG2 . VAL B 345 ? 1.8109 1.2891 2.0656 -0.2889 -0.4587 0.1875 345 VAL B CG2 9871 N N . ASP B 346 ? 1.8792 1.2397 1.8106 -0.2892 -0.3949 0.1424 346 ASP B N 9872 C CA . ASP B 346 ? 1.9246 1.2583 1.7627 -0.2789 -0.3815 0.1327 346 ASP B CA 9873 C C . ASP B 346 ? 1.8499 1.1463 1.6761 -0.2727 -0.3420 0.1175 346 ASP B C 9874 O O . ASP B 346 ? 1.8553 1.1373 1.6329 -0.2568 -0.3226 0.1166 346 ASP B O 9875 C CB . ASP B 346 ? 2.1153 1.4405 1.8958 -0.2892 -0.4071 0.1112 346 ASP B CB 9876 C CG . ASP B 346 ? 2.3022 1.6653 2.0856 -0.2991 -0.4501 0.1271 346 ASP B CG 9877 O OD1 . ASP B 346 ? 2.2631 1.6538 2.0763 -0.2946 -0.4614 0.1594 346 ASP B OD1 9878 O OD2 . ASP B 346 ? 2.4331 1.7965 2.1899 -0.3125 -0.4755 0.1079 346 ASP B OD2 9879 N N . ALA B 347 ? 1.8044 1.0872 1.6748 -0.2878 -0.3315 0.1064 347 ALA B N 9880 C CA . ALA B 347 ? 1.7413 0.9871 1.5986 -0.2883 -0.2981 0.0970 347 ALA B CA 9881 C C . ALA B 347 ? 1.6742 0.9356 1.5598 -0.2755 -0.2691 0.1120 347 ALA B C 9882 O O . ALA B 347 ? 1.6495 0.8868 1.4921 -0.2618 -0.2479 0.1109 347 ALA B O 9883 C CB . ALA B 347 ? 1.8245 1.0574 1.7207 -0.3154 -0.2944 0.0852 347 ALA B CB 9884 N N . TYR B 348 ? 1.6668 0.9699 1.6308 -0.2792 -0.2705 0.1228 348 TYR B N 9885 C CA . TYR B 348 ? 1.5757 0.8989 1.5800 -0.2675 -0.2456 0.1329 348 TYR B CA 9886 C C . TYR B 348 ? 1.5839 0.9066 1.5431 -0.2442 -0.2469 0.1485 348 TYR B C 9887 O O . TYR B 348 ? 1.5371 0.8549 1.4893 -0.2323 -0.2202 0.1507 348 TYR B O 9888 C CB . TYR B 348 ? 1.5554 0.9260 1.6633 -0.2731 -0.2549 0.1369 348 TYR B CB 9889 C CG . TYR B 348 ? 1.5012 0.8956 1.6616 -0.2593 -0.2341 0.1435 348 TYR B CG 9890 C CD1 . TYR B 348 ? 1.4665 0.8579 1.6357 -0.2636 -0.1937 0.1298 348 TYR B CD1 9891 C CD2 . TYR B 348 ? 1.5056 0.9243 1.7065 -0.2441 -0.2571 0.1638 348 TYR B CD2 9892 C CE1 . TYR B 348 ? 1.4168 0.8324 1.6366 -0.2513 -0.1746 0.1307 348 TYR B CE1 9893 C CE2 . TYR B 348 ? 1.5806 1.0179 1.8364 -0.2313 -0.2403 0.1675 348 TYR B CE2 9894 C CZ . TYR B 348 ? 1.5422 0.9797 1.8089 -0.2340 -0.1979 0.1480 348 TYR B CZ 9895 O OH . TYR B 348 ? 1.4952 0.9535 1.8188 -0.2216 -0.1810 0.1466 348 TYR B OH 9896 N N . GLY B 349 ? 1.6535 0.9845 1.5806 -0.2408 -0.2777 0.1587 349 GLY B N 9897 C CA . GLY B 349 ? 1.6788 1.0137 1.5555 -0.2254 -0.2790 0.1732 349 GLY B CA 9898 C C . GLY B 349 ? 1.6895 0.9923 1.4892 -0.2156 -0.2580 0.1551 349 GLY B C 9899 O O . GLY B 349 ? 1.6820 0.9859 1.4573 -0.2011 -0.2405 0.1604 349 GLY B O 9900 N N . LYS B 350 ? 1.7348 1.0082 1.5022 -0.2235 -0.2622 0.1324 350 LYS B N 9901 C CA . LYS B 350 ? 1.7721 1.0093 1.4768 -0.2128 -0.2487 0.1113 350 LYS B CA 9902 C C . LYS B 350 ? 1.7030 0.9165 1.4207 -0.2072 -0.2184 0.1107 350 LYS B C 9903 O O . LYS B 350 ? 1.7096 0.9040 1.3877 -0.1912 -0.2046 0.1021 350 LYS B O 9904 C CB . LYS B 350 ? 1.7947 1.0018 1.4709 -0.2237 -0.2671 0.0871 350 LYS B CB 9905 C CG . LYS B 350 ? 1.8266 0.9963 1.4436 -0.2097 -0.2625 0.0607 350 LYS B CG 9906 C CD . LYS B 350 ? 1.9164 1.0581 1.5121 -0.2202 -0.2861 0.0341 350 LYS B CD 9907 C CE . LYS B 350 ? 2.0335 1.1399 1.5806 -0.2027 -0.2861 0.0023 350 LYS B CE 9908 N NZ . LYS B 350 ? 2.0988 1.1771 1.6303 -0.2117 -0.3114 -0.0285 350 LYS B NZ 9909 N N . ILE B 351 ? 1.7667 0.9862 1.5415 -0.2219 -0.2085 0.1176 351 ILE B N 9910 C CA . ILE B 351 ? 1.6167 0.8214 1.4030 -0.2230 -0.1792 0.1174 351 ILE B CA 9911 C C . ILE B 351 ? 1.5310 0.7623 1.3343 -0.2053 -0.1609 0.1290 351 ILE B C 9912 O O . ILE B 351 ? 1.6050 0.8199 1.3859 -0.1960 -0.1403 0.1259 351 ILE B O 9913 C CB . ILE B 351 ? 1.5032 0.7182 1.3477 -0.2490 -0.1705 0.1166 351 ILE B CB 9914 C CG1 . ILE B 351 ? 1.5887 0.7670 1.4100 -0.2701 -0.1840 0.1053 351 ILE B CG1 9915 C CG2 . ILE B 351 ? 1.5311 0.7475 1.3914 -0.2533 -0.1376 0.1172 351 ILE B CG2 9916 C CD1 . ILE B 351 ? 1.7696 0.9652 1.6489 -0.3011 -0.1760 0.1025 351 ILE B CD1 9917 N N . ARG B 352 ? 1.4912 0.7614 1.3342 -0.2014 -0.1722 0.1433 352 ARG B N 9918 C CA . ARG B 352 ? 1.4547 0.7489 1.3215 -0.1869 -0.1591 0.1562 352 ARG B CA 9919 C C . ARG B 352 ? 1.5038 0.7965 1.3109 -0.1710 -0.1637 0.1608 352 ARG B C 9920 O O . ARG B 352 ? 1.4619 0.7739 1.2814 -0.1609 -0.1560 0.1737 352 ARG B O 9921 C CB . ARG B 352 ? 1.5537 0.8860 1.4999 -0.1912 -0.1732 0.1718 352 ARG B CB 9922 C CG . ARG B 352 ? 1.6347 0.9842 1.6595 -0.2037 -0.1595 0.1611 352 ARG B CG 9923 C CD . ARG B 352 ? 1.7360 1.0868 1.7733 -0.1989 -0.1237 0.1516 352 ARG B CD 9924 N NE . ARG B 352 ? 1.9484 1.2721 1.9457 -0.2123 -0.1032 0.1359 352 ARG B NE 9925 C CZ . ARG B 352 ? 1.9578 1.2945 1.9965 -0.2338 -0.0862 0.1221 352 ARG B CZ 9926 N NH1 . ARG B 352 ? 1.8823 1.1889 1.8732 -0.2502 -0.0707 0.1143 352 ARG B NH1 9927 N NH2 . ARG B 352 ? 1.9120 1.2929 2.0422 -0.2403 -0.0859 0.1156 352 ARG B NH2 9928 N N . SER B 353 ? 1.6416 0.9141 1.3876 -0.1706 -0.1759 0.1472 353 SER B N 9929 C CA . SER B 353 ? 1.7636 1.0432 1.4531 -0.1586 -0.1781 0.1433 353 SER B CA 9930 C C . SER B 353 ? 1.8838 1.1403 1.5388 -0.1417 -0.1564 0.1249 353 SER B C 9931 O O . SER B 353 ? 1.9810 1.2457 1.5933 -0.1304 -0.1542 0.1135 353 SER B O 9932 C CB . SER B 353 ? 1.7182 0.9961 1.3636 -0.1662 -0.2028 0.1304 353 SER B CB 9933 O OG . SER B 353 ? 1.7331 0.9711 1.3593 -0.1675 -0.2049 0.1053 353 SER B OG 9934 N N . LYS B 354 ? 1.8860 1.1174 1.5603 -0.1419 -0.1412 0.1211 354 LYS B N 9935 C CA . LYS B 354 ? 1.7565 0.9601 1.3993 -0.1270 -0.1272 0.1058 354 LYS B CA 9936 C C . LYS B 354 ? 1.7484 0.9528 1.4233 -0.1271 -0.1043 0.1144 354 LYS B C 9937 O O . LYS B 354 ? 1.8394 1.0505 1.5565 -0.1433 -0.0986 0.1231 354 LYS B O 9938 C CB . LYS B 354 ? 1.6250 0.7803 1.2352 -0.1304 -0.1408 0.0871 354 LYS B CB 9939 C CG . LYS B 354 ? 1.6785 0.7986 1.2555 -0.1127 -0.1367 0.0706 354 LYS B CG 9940 C CD . LYS B 354 ? 1.9448 1.0103 1.4961 -0.1171 -0.1572 0.0546 354 LYS B CD 9941 C CE . LYS B 354 ? 2.0775 1.1033 1.6022 -0.0972 -0.1608 0.0392 354 LYS B CE 9942 N NZ . LYS B 354 ? 2.0818 1.0991 1.6143 -0.0999 -0.1439 0.0571 354 LYS B NZ 9943 N N . VAL B 355 ? 1.4416 0.6442 1.0988 -0.1098 -0.0908 0.1082 355 VAL B N 9944 C CA . VAL B 355 ? 1.3690 0.5721 1.0478 -0.1097 -0.0699 0.1120 355 VAL B CA 9945 C C . VAL B 355 ? 1.6489 0.8161 1.2860 -0.0969 -0.0685 0.0987 355 VAL B C 9946 O O . VAL B 355 ? 1.8957 1.0657 1.5097 -0.0765 -0.0706 0.0868 355 VAL B O 9947 C CB . VAL B 355 ? 1.3375 0.5830 1.0533 -0.1018 -0.0552 0.1217 355 VAL B CB 9948 C CG1 . VAL B 355 ? 1.3438 0.5899 1.0733 -0.0984 -0.0337 0.1179 355 VAL B CG1 9949 C CG2 . VAL B 355 ? 1.4631 0.7383 1.2339 -0.1150 -0.0603 0.1378 355 VAL B CG2 9950 N N . GLU B 356 ? 1.5095 0.6447 1.1383 -0.1110 -0.0665 0.1008 356 GLU B N 9951 C CA . GLU B 356 ? 1.4989 0.5945 1.0895 -0.1019 -0.0708 0.0942 356 GLU B CA 9952 C C . GLU B 356 ? 1.5251 0.6248 1.1251 -0.1178 -0.0516 0.1033 356 GLU B C 9953 O O . GLU B 356 ? 1.6893 0.8109 1.3213 -0.1411 -0.0376 0.1104 356 GLU B O 9954 C CB . GLU B 356 ? 1.6098 0.6484 1.1642 -0.1075 -0.0964 0.0892 356 GLU B CB 9955 C CG . GLU B 356 ? 1.9363 0.9270 1.4538 -0.0927 -0.1118 0.0822 356 GLU B CG 9956 C CD . GLU B 356 ? 2.0900 1.0189 1.5799 -0.0963 -0.1424 0.0764 356 GLU B CD 9957 O OE1 . GLU B 356 ? 2.1701 1.0961 1.6675 -0.1122 -0.1490 0.0766 356 GLU B OE1 9958 O OE2 . GLU B 356 ? 2.0241 0.9059 1.4890 -0.0829 -0.1630 0.0710 356 GLU B OE2 9959 N N . LEU B 357 ? 1.3890 0.4720 0.9634 -0.1059 -0.0514 0.1000 357 LEU B N 9960 C CA . LEU B 357 ? 1.3800 0.4749 0.9584 -0.1208 -0.0320 0.1056 357 LEU B CA 9961 C C . LEU B 357 ? 1.5441 0.5892 1.0762 -0.1438 -0.0427 0.1161 357 LEU B C 9962 O O . LEU B 357 ? 1.6111 0.6071 1.1022 -0.1315 -0.0678 0.1169 357 LEU B O 9963 C CB . LEU B 357 ? 1.4823 0.5997 1.0652 -0.0965 -0.0236 0.0968 357 LEU B CB 9964 C CG . LEU B 357 ? 1.4462 0.6164 1.0767 -0.0816 -0.0087 0.0914 357 LEU B CG 9965 C CD1 . LEU B 357 ? 1.4513 0.6417 1.0863 -0.0619 0.0003 0.0820 357 LEU B CD1 9966 C CD2 . LEU B 357 ? 1.3455 0.5530 1.0283 -0.1022 0.0104 0.0970 357 LEU B CD2 9967 N N . GLU B 358 ? 1.8011 0.8603 1.3427 -0.1788 -0.0248 0.1237 358 GLU B N 9968 C CA . GLU B 358 ? 1.6458 0.6664 1.1392 -0.2102 -0.0296 0.1377 358 GLU B CA 9969 C C . GLU B 358 ? 1.5153 0.5465 0.9866 -0.2101 -0.0193 0.1377 358 GLU B C 9970 O O . GLU B 358 ? 1.6758 0.7584 1.1845 -0.1959 0.0024 0.1239 358 GLU B O 9971 C CB . GLU B 358 ? 1.7969 0.8393 1.3095 -0.2530 -0.0098 0.1418 358 GLU B CB 9972 C CG . GLU B 358 ? 2.0335 1.0632 1.5656 -0.2591 -0.0226 0.1429 358 GLU B CG 9973 C CD . GLU B 358 ? 2.1824 1.2384 1.7386 -0.3034 -0.0023 0.1441 358 GLU B CD 9974 O OE1 . GLU B 358 ? 2.1508 1.2211 1.7462 -0.3073 -0.0055 0.1393 358 GLU B OE1 9975 O OE2 . GLU B 358 ? 2.1732 1.2397 1.7092 -0.3361 0.0170 0.1481 358 GLU B OE2 9976 N N . VAL B 359 ? 1.7482 0.7286 1.1585 -0.2275 -0.0379 0.1542 359 VAL B N 9977 C CA . VAL B 359 ? 1.6417 0.6305 1.0211 -0.2350 -0.0313 0.1571 359 VAL B CA 9978 C C . VAL B 359 ? 1.7538 0.7203 1.0796 -0.2874 -0.0291 0.1782 359 VAL B C 9979 O O . VAL B 359 ? 2.1348 1.0334 1.4117 -0.3024 -0.0604 0.2012 359 VAL B O 9980 C CB . VAL B 359 ? 1.6569 0.6040 1.0067 -0.1989 -0.0651 0.1583 359 VAL B CB 9981 C CG1 . VAL B 359 ? 1.6394 0.5950 0.9539 -0.2098 -0.0620 0.1629 359 VAL B CG1 9982 C CG2 . VAL B 359 ? 1.5429 0.5206 0.9427 -0.1525 -0.0628 0.1355 359 VAL B CG2 9983 N N . ARG B 360 ? 1.6507 0.6751 0.9866 -0.3175 0.0077 0.1690 360 ARG B N 9984 C CA . ARG B 360 ? 1.7152 0.7340 0.9996 -0.3753 0.0179 0.1856 360 ARG B CA 9985 C C . ARG B 360 ? 1.7620 0.7914 0.9949 -0.3912 0.0218 0.1894 360 ARG B C 9986 O O . ARG B 360 ? 1.9051 0.9877 1.1716 -0.3707 0.0422 0.1649 360 ARG B O 9987 C CB . ARG B 360 ? 1.6890 0.7753 1.0269 -0.4080 0.0607 0.1666 360 ARG B CB 9988 C CG . ARG B 360 ? 1.6848 0.7604 1.0662 -0.4032 0.0546 0.1663 360 ARG B CG 9989 C CD . ARG B 360 ? 1.8265 0.9755 1.2719 -0.4331 0.0950 0.1435 360 ARG B CD 9990 N NE . ARG B 360 ? 2.0372 1.1792 1.5269 -0.4288 0.0863 0.1430 360 ARG B NE 9991 C CZ . ARG B 360 ? 1.9705 1.1723 1.5309 -0.4459 0.1127 0.1220 360 ARG B CZ 9992 N NH1 . ARG B 360 ? 1.7407 1.0157 1.3407 -0.4674 0.1517 0.0962 360 ARG B NH1 9993 N NH2 . ARG B 360 ? 1.9225 1.1137 1.5185 -0.4408 0.0988 0.1235 360 ARG B NH2 9994 N N . ASP B 361 ? 1.8442 0.8205 0.9942 -0.4297 -0.0006 0.2217 361 ASP B N 9995 C CA . ASP B 361 ? 1.9048 0.8893 0.9901 -0.4579 0.0006 0.2313 361 ASP B CA 9996 C C . ASP B 361 ? 1.9003 0.8760 0.9826 -0.4106 -0.0228 0.2245 361 ASP B C 9997 O O . ASP B 361 ? 2.0559 1.0796 1.1280 -0.4185 -0.0039 0.2097 361 ASP B O 9998 C CB . ASP B 361 ? 1.9320 1.0101 1.0404 -0.4973 0.0572 0.2027 361 ASP B CB 9999 C CG . ASP B 361 ? 2.2767 1.3732 1.3887 -0.5502 0.0832 0.2058 361 ASP B CG 10000 O OD1 . ASP B 361 ? 2.3662 1.5002 1.5595 -0.5360 0.1052 0.1819 361 ASP B OD1 10001 O OD2 . ASP B 361 ? 2.3367 1.4114 1.3704 -0.6083 0.0802 0.2331 361 ASP B OD2 10002 N N . LEU B 362 ? 1.8821 0.8005 0.9759 -0.3627 -0.0635 0.2314 362 LEU B N 10003 C CA . LEU B 362 ? 1.8773 0.7873 0.9739 -0.3169 -0.0884 0.2230 362 LEU B CA 10004 C C . LEU B 362 ? 2.0971 0.9522 1.1083 -0.3369 -0.1293 0.2549 362 LEU B C 10005 O O . LEU B 362 ? 2.3429 1.1205 1.3035 -0.3550 -0.1689 0.2897 362 LEU B O 10006 C CB . LEU B 362 ? 1.8306 0.7056 0.9722 -0.2612 -0.1163 0.2140 362 LEU B CB 10007 C CG . LEU B 362 ? 1.8532 0.7230 1.0084 -0.2113 -0.1424 0.2003 362 LEU B CG 10008 C CD1 . LEU B 362 ? 1.9492 0.9024 1.1567 -0.1939 -0.1025 0.1677 362 LEU B CD1 10009 C CD2 . LEU B 362 ? 2.0573 0.8857 1.2456 -0.1657 -0.1735 0.1919 362 LEU B CD2 10010 N N . PRO B 363 ? 2.1068 1.0001 1.1027 -0.3349 -0.1231 0.2440 363 PRO B N 10011 C CA . PRO B 363 ? 2.1445 0.9921 1.0594 -0.3517 -0.1654 0.2736 363 PRO B CA 10012 C C . PRO B 363 ? 2.2057 0.9661 1.1130 -0.3102 -0.2318 0.2928 363 PRO B C 10013 O O . PRO B 363 ? 2.2450 1.0020 1.2189 -0.2582 -0.2379 0.2698 363 PRO B O 10014 C CB . PRO B 363 ? 2.2693 1.1884 1.2009 -0.3392 -0.1422 0.2432 363 PRO B CB 10015 C CG . PRO B 363 ? 2.2282 1.2330 1.2257 -0.3468 -0.0778 0.2062 363 PRO B CG 10016 C CD . PRO B 363 ? 2.1296 1.1149 1.1846 -0.3225 -0.0744 0.2029 363 PRO B CD 10017 N N . GLU B 364 ? 2.4530 1.1454 1.2808 -0.3349 -0.2819 0.3335 364 GLU B N 10018 C CA . GLU B 364 ? 2.5163 1.1159 1.3382 -0.3003 -0.3524 0.3543 364 GLU B CA 10019 C C . GLU B 364 ? 2.5779 1.1932 1.4610 -0.2316 -0.3729 0.3205 364 GLU B C 10020 O O . GLU B 364 ? 2.4362 1.0282 1.3792 -0.1836 -0.3904 0.3009 364 GLU B O 10021 C CB . GLU B 364 ? 2.4008 0.9677 1.1550 -0.3371 -0.3974 0.3918 364 GLU B CB 10022 C CG . GLU B 364 ? 2.8578 1.4354 1.5701 -0.4036 -0.3770 0.4159 364 GLU B CG 10023 C CD . GLU B 364 ? 3.1339 1.6747 1.8860 -0.3955 -0.3999 0.4211 364 GLU B CD 10024 O OE1 . GLU B 364 ? 3.1678 1.6953 1.8799 -0.4445 -0.4080 0.4487 364 GLU B OE1 10025 O OE2 . GLU B 364 ? 3.0892 1.6168 1.9108 -0.3422 -0.4090 0.3964 364 GLU B OE2 10026 N N . GLU B 365 ? 2.4661 1.1255 1.3348 -0.2294 -0.3693 0.3108 365 GLU B N 10027 C CA . GLU B 365 ? 2.3887 1.0649 1.3117 -0.1696 -0.3916 0.2802 365 GLU B CA 10028 C C . GLU B 365 ? 2.1953 0.9482 1.2107 -0.1303 -0.3400 0.2300 365 GLU B C 10029 O O . GLU B 365 ? 2.0892 0.8629 1.1599 -0.0806 -0.3515 0.2001 365 GLU B O 10030 C CB . GLU B 365 ? 2.4380 1.1404 1.3158 -0.1833 -0.4042 0.2852 365 GLU B CB 10031 C CG . GLU B 365 ? 2.7431 1.3640 1.5278 -0.2161 -0.4691 0.3381 365 GLU B CG 10032 C CD . GLU B 365 ? 3.0180 1.6696 1.7556 -0.2296 -0.4836 0.3413 365 GLU B CD 10033 O OE1 . GLU B 365 ? 3.0642 1.8052 1.8367 -0.2228 -0.4342 0.3019 365 GLU B OE1 10034 O OE2 . GLU B 365 ? 3.0638 1.6484 1.7303 -0.2479 -0.5473 0.3839 365 GLU B OE2 10035 N N . LEU B 366 ? 2.1202 0.9156 1.1535 -0.1544 -0.2850 0.2216 366 LEU B N 10036 C CA . LEU B 366 ? 2.0584 0.9222 1.1744 -0.1234 -0.2387 0.1810 366 LEU B CA 10037 C C . LEU B 366 ? 2.0294 0.8610 1.1897 -0.0915 -0.2504 0.1729 366 LEU B C 10038 O O . LEU B 366 ? 2.2095 0.9840 1.3417 -0.1104 -0.2684 0.1966 366 LEU B O 10039 C CB . LEU B 366 ? 1.9482 0.8771 1.0724 -0.1619 -0.1775 0.1726 366 LEU B CB 10040 C CG . LEU B 366 ? 1.8884 0.9002 1.0871 -0.1383 -0.1324 0.1329 366 LEU B CG 10041 C CD1 . LEU B 366 ? 1.9363 0.9741 1.1378 -0.1180 -0.1447 0.1170 366 LEU B CD1 10042 C CD2 . LEU B 366 ? 1.9238 0.9936 1.1358 -0.1770 -0.0787 0.1236 366 LEU B CD2 10043 N N . SER B 367 ? 1.8541 0.7249 1.0822 -0.0460 -0.2397 0.1381 367 SER B N 10044 C CA . SER B 367 ? 1.7748 0.6266 1.0452 -0.0146 -0.2487 0.1230 367 SER B CA 10045 C C . SER B 367 ? 1.7681 0.6935 1.1017 0.0006 -0.1999 0.0935 367 SER B C 10046 O O . SER B 367 ? 1.8926 0.8778 1.2541 0.0072 -0.1731 0.0762 367 SER B O 10047 C CB . SER B 367 ? 1.8269 0.6411 1.1145 0.0298 -0.2998 0.1091 367 SER B CB 10048 O OG . SER B 367 ? 2.0137 0.7581 1.2449 0.0164 -0.3514 0.1400 367 SER B OG 10049 N N . LEU B 368 ? 1.7159 0.6346 1.0709 0.0042 -0.1912 0.0892 368 LEU B N 10050 C CA . LEU B 368 ? 1.6131 0.5953 1.0208 0.0129 -0.1497 0.0686 368 LEU B CA 10051 C C . LEU B 368 ? 1.7366 0.7197 1.1795 0.0483 -0.1606 0.0443 368 LEU B C 10052 O O . LEU B 368 ? 1.9859 0.9168 1.4154 0.0549 -0.1905 0.0459 368 LEU B O 10053 C CB . LEU B 368 ? 1.5558 0.5484 0.9596 -0.0235 -0.1200 0.0845 368 LEU B CB 10054 C CG . LEU B 368 ? 1.5733 0.5881 0.9556 -0.0620 -0.0958 0.0982 368 LEU B CG 10055 C CD1 . LEU B 368 ? 1.5559 0.5919 0.9540 -0.0923 -0.0650 0.1046 368 LEU B CD1 10056 C CD2 . LEU B 368 ? 1.5654 0.6391 0.9776 -0.0511 -0.0733 0.0793 368 LEU B CD2 10057 N N . SER B 369 ? 1.6907 0.7352 1.1791 0.0682 -0.1356 0.0203 369 SER B N 10058 C CA . SER B 369 ? 1.7027 0.7658 1.2235 0.0950 -0.1364 -0.0059 369 SER B CA 10059 C C . SER B 369 ? 1.6762 0.7902 1.2229 0.0817 -0.0976 -0.0047 369 SER B C 10060 O O . SER B 369 ? 1.6524 0.8050 1.2152 0.0667 -0.0691 0.0036 369 SER B O 10061 C CB . SER B 369 ? 1.5670 0.6609 1.1186 0.1286 -0.1445 -0.0363 369 SER B CB 10062 O OG . SER B 369 ? 1.7387 0.7857 1.2710 0.1417 -0.1853 -0.0352 369 SER B OG 10063 N N . PHE B 370 ? 1.6441 0.7573 1.1965 0.0867 -0.0993 -0.0138 370 PHE B N 10064 C CA . PHE B 370 ? 1.5119 0.6661 1.0832 0.0712 -0.0700 -0.0069 370 PHE B CA 10065 C C . PHE B 370 ? 1.5665 0.7620 1.1583 0.0877 -0.0625 -0.0310 370 PHE B C 10066 O O . PHE B 370 ? 1.7691 0.9464 1.3510 0.0990 -0.0801 -0.0486 370 PHE B O 10067 C CB . PHE B 370 ? 1.5348 0.6536 1.0857 0.0474 -0.0754 0.0133 370 PHE B CB 10068 C CG . PHE B 370 ? 1.6505 0.7436 1.1827 0.0211 -0.0731 0.0377 370 PHE B CG 10069 C CD1 . PHE B 370 ? 1.5894 0.6249 1.0838 0.0172 -0.1007 0.0464 370 PHE B CD1 10070 C CD2 . PHE B 370 ? 1.3957 0.5234 0.9495 -0.0019 -0.0445 0.0511 370 PHE B CD2 10071 C CE1 . PHE B 370 ? 1.5946 0.6124 1.0642 -0.0138 -0.0959 0.0691 370 PHE B CE1 10072 C CE2 . PHE B 370 ? 1.5451 0.6594 1.0836 -0.0291 -0.0381 0.0668 370 PHE B CE2 10073 C CZ . PHE B 370 ? 1.7794 0.8410 1.2712 -0.0374 -0.0618 0.0765 370 PHE B CZ 10074 N N . ASN B 371 ? 1.4966 0.7488 1.1167 0.0861 -0.0360 -0.0327 371 ASN B N 10075 C CA . ASN B 371 ? 1.5083 0.8059 1.1405 0.0879 -0.0229 -0.0456 371 ASN B CA 10076 C C . ASN B 371 ? 1.5701 0.8796 1.2057 0.0619 -0.0088 -0.0174 371 ASN B C 10077 O O . ASN B 371 ? 1.5260 0.8375 1.1785 0.0469 0.0029 0.0049 371 ASN B O 10078 C CB . ASN B 371 ? 1.5597 0.9122 1.2206 0.0980 -0.0048 -0.0622 371 ASN B CB 10079 C CG . ASN B 371 ? 1.5610 0.9098 1.2281 0.1266 -0.0211 -0.0955 371 ASN B CG 10080 O OD1 . ASN B 371 ? 1.6052 0.9112 1.2562 0.1417 -0.0487 -0.1096 371 ASN B OD1 10081 N ND2 . ASN B 371 ? 1.8245 1.2174 1.5205 0.1343 -0.0068 -0.1088 371 ASN B ND2 10082 N N . ALA B 372 ? 1.5450 0.8644 1.1677 0.0566 -0.0118 -0.0212 372 ALA B N 10083 C CA . ALA B 372 ? 1.4942 0.8208 1.1201 0.0327 -0.0062 0.0064 372 ALA B CA 10084 C C . ALA B 372 ? 1.5762 0.9550 1.2074 0.0231 0.0069 0.0100 372 ALA B C 10085 O O . ALA B 372 ? 1.7145 1.1154 1.3261 0.0288 0.0055 -0.0133 372 ALA B O 10086 C CB . ALA B 372 ? 1.4805 0.7672 1.0811 0.0268 -0.0260 0.0072 372 ALA B CB 10087 N N . THR B 373 ? 1.5584 0.9573 1.2173 0.0066 0.0188 0.0386 373 THR B N 10088 C CA . THR B 373 ? 1.5414 0.9813 1.2019 -0.0101 0.0257 0.0541 373 THR B CA 10089 C C . THR B 373 ? 1.5223 0.9498 1.1807 -0.0292 0.0122 0.0815 373 THR B C 10090 O O . THR B 373 ? 1.4420 0.8561 1.1353 -0.0374 0.0105 0.1043 373 THR B O 10091 C CB . THR B 373 ? 1.5322 1.0009 1.2315 -0.0166 0.0425 0.0699 373 THR B CB 10092 O OG1 . THR B 373 ? 1.5318 1.0189 1.2342 0.0001 0.0545 0.0421 373 THR B OG1 10093 C CG2 . THR B 373 ? 1.5859 1.0890 1.2831 -0.0397 0.0446 0.0949 373 THR B CG2 10094 N N . CYS B 374 ? 1.6022 1.0383 1.2235 -0.0360 0.0019 0.0751 374 CYS B N 10095 C CA . CYS B 374 ? 1.6091 1.0351 1.2252 -0.0537 -0.0153 0.0983 374 CYS B CA 10096 C C . CYS B 374 ? 1.7258 1.1904 1.3320 -0.0762 -0.0174 0.1236 374 CYS B C 10097 O O . CYS B 374 ? 1.9353 1.3998 1.5734 -0.0907 -0.0254 0.1592 374 CYS B O 10098 C CB . CYS B 374 ? 1.9152 1.3172 1.4948 -0.0485 -0.0307 0.0741 374 CYS B CB 10099 S SG . CYS B 374 ? 1.8864 1.2311 1.4723 -0.0301 -0.0366 0.0553 374 CYS B SG 10100 N N . LEU B 375 ? 1.7768 1.2756 1.3402 -0.0807 -0.0116 0.1045 375 LEU B N 10101 C CA . LEU B 375 ? 1.7879 1.3256 1.3266 -0.1088 -0.0147 0.1300 375 LEU B CA 10102 C C . LEU B 375 ? 1.7812 1.3586 1.3262 -0.1174 0.0068 0.1361 375 LEU B C 10103 O O . LEU B 375 ? 1.8362 1.4462 1.3589 -0.1113 0.0250 0.1006 375 LEU B O 10104 C CB . LEU B 375 ? 1.8671 1.4260 1.3473 -0.1170 -0.0214 0.1040 375 LEU B CB 10105 C CG . LEU B 375 ? 1.9091 1.5138 1.3448 -0.1513 -0.0253 0.1258 375 LEU B CG 10106 C CD1 . LEU B 375 ? 2.0951 1.6812 1.5443 -0.1721 -0.0526 0.1798 375 LEU B CD1 10107 C CD2 . LEU B 375 ? 1.9751 1.6068 1.3542 -0.1554 -0.0262 0.0840 375 LEU B CD2 10108 N N . ASN B 376 ? 1.7454 1.3203 1.3265 -0.1322 0.0030 0.1793 376 ASN B N 10109 C CA . ASN B 376 ? 1.7044 1.3123 1.2965 -0.1477 0.0192 0.1958 376 ASN B CA 10110 C C . ASN B 376 ? 1.7415 1.3750 1.3366 -0.1304 0.0475 0.1541 376 ASN B C 10111 O O . ASN B 376 ? 1.8015 1.4826 1.3611 -0.1431 0.0633 0.1360 376 ASN B O 10112 C CB . ASN B 376 ? 1.7446 1.3900 1.2873 -0.1857 0.0127 0.2240 376 ASN B CB 10113 C CG . ASN B 376 ? 1.8329 1.5072 1.3083 -0.1909 0.0147 0.1901 376 ASN B CG 10114 O OD1 . ASN B 376 ? 1.8469 1.5179 1.2880 -0.2076 -0.0075 0.2069 376 ASN B OD1 10115 N ND2 . ASN B 376 ? 2.0676 1.7727 1.5286 -0.1761 0.0396 0.1388 376 ASN B ND2 10116 N N . ASN B 377 ? 1.8334 1.4390 1.4712 -0.1029 0.0531 0.1372 377 ASN B N 10117 C CA . ASN B 377 ? 1.8715 1.4969 1.5233 -0.0843 0.0746 0.1013 377 ASN B CA 10118 C C . ASN B 377 ? 1.9021 1.5503 1.5168 -0.0693 0.0814 0.0509 377 ASN B C 10119 O O . ASN B 377 ? 1.8823 1.5748 1.4970 -0.0681 0.1005 0.0238 377 ASN B O 10120 C CB . ASN B 377 ? 1.8076 1.4723 1.4779 -0.1053 0.0914 0.1192 377 ASN B CB 10121 C CG . ASN B 377 ? 1.8083 1.4521 1.5165 -0.1247 0.0794 0.1711 377 ASN B CG 10122 O OD1 . ASN B 377 ? 1.9043 1.5072 1.6485 -0.1126 0.0662 0.1824 377 ASN B OD1 10123 N ND2 . ASN B 377 ? 1.7141 1.3870 1.4171 -0.1566 0.0831 0.2019 377 ASN B ND2 10124 N N . GLU B 378 ? 2.0023 1.6218 1.5918 -0.0580 0.0650 0.0355 378 GLU B N 10125 C CA . GLU B 378 ? 1.9727 1.6078 1.5357 -0.0411 0.0665 -0.0163 378 GLU B CA 10126 C C . GLU B 378 ? 1.9723 1.5821 1.5629 -0.0054 0.0651 -0.0516 378 GLU B C 10127 O O . GLU B 378 ? 2.2093 1.8473 1.8000 0.0110 0.0718 -0.0978 378 GLU B O 10128 C CB . GLU B 378 ? 2.1783 1.7904 1.7056 -0.0448 0.0464 -0.0201 378 GLU B CB 10129 C CG . GLU B 378 ? 2.1895 1.7365 1.7316 -0.0353 0.0254 0.0005 378 GLU B CG 10130 C CD . GLU B 378 ? 2.3849 1.9120 1.8945 -0.0396 0.0056 -0.0080 378 GLU B CD 10131 O OE1 . GLU B 378 ? 2.5305 2.0967 2.0037 -0.0550 0.0071 -0.0213 378 GLU B OE1 10132 O OE2 . GLU B 378 ? 2.4388 1.9139 1.9580 -0.0303 -0.0108 -0.0028 378 GLU B OE2 10133 N N . VAL B 379 ? 1.8603 1.4197 1.4750 0.0052 0.0549 -0.0310 379 VAL B N 10134 C CA . VAL B 379 ? 1.7987 1.3290 1.4341 0.0341 0.0495 -0.0544 379 VAL B CA 10135 C C . VAL B 379 ? 1.7577 1.2643 1.3758 0.0575 0.0316 -0.0952 379 VAL B C 10136 O O . VAL B 379 ? 1.7237 1.2566 1.3511 0.0762 0.0345 -0.1367 379 VAL B O 10137 C CB . VAL B 379 ? 1.7280 1.2992 1.3936 0.0415 0.0681 -0.0698 379 VAL B CB 10138 C CG1 . VAL B 379 ? 1.6251 1.1617 1.3124 0.0669 0.0583 -0.0822 379 VAL B CG1 10139 C CG2 . VAL B 379 ? 1.9405 1.5381 1.6255 0.0156 0.0849 -0.0323 379 VAL B CG2 10140 N N . ILE B 380 ? 1.7844 1.2424 1.3830 0.0559 0.0117 -0.0853 380 ILE B N 10141 C CA . ILE B 380 ? 1.7033 1.1245 1.2906 0.0773 -0.0109 -0.1195 380 ILE B CA 10142 C C . ILE B 380 ? 1.7591 1.1286 1.3607 0.0977 -0.0271 -0.1197 380 ILE B C 10143 O O . ILE B 380 ? 1.9179 1.2483 1.5172 0.0874 -0.0320 -0.0863 380 ILE B O 10144 C CB . ILE B 380 ? 1.7258 1.1137 1.2864 0.0642 -0.0274 -0.1086 380 ILE B CB 10145 C CG1 . ILE B 380 ? 1.8123 1.2519 1.3506 0.0433 -0.0165 -0.1114 380 ILE B CG1 10146 C CG2 . ILE B 380 ? 1.8328 1.1721 1.3878 0.0858 -0.0544 -0.1415 380 ILE B CG2 10147 C CD1 . ILE B 380 ? 1.8623 1.2752 1.3752 0.0297 -0.0344 -0.1038 380 ILE B CD1 10148 N N . PRO B 381 ? 1.7962 1.1685 1.4133 0.1253 -0.0367 -0.1587 381 PRO B N 10149 C CA . PRO B 381 ? 1.7443 1.0697 1.3724 0.1450 -0.0573 -0.1590 381 PRO B CA 10150 C C . PRO B 381 ? 1.7452 0.9936 1.3530 0.1493 -0.0910 -0.1533 381 PRO B C 10151 O O . PRO B 381 ? 1.9823 1.2171 1.5803 0.1520 -0.1041 -0.1731 381 PRO B O 10152 C CB . PRO B 381 ? 1.8196 1.1804 1.4775 0.1738 -0.0602 -0.2079 381 PRO B CB 10153 C CG . PRO B 381 ? 1.9756 1.4134 1.6382 0.1627 -0.0307 -0.2287 381 PRO B CG 10154 C CD . PRO B 381 ? 1.9795 1.4083 1.6085 0.1377 -0.0276 -0.2067 381 PRO B CD 10155 N N . GLY B 382 ? 1.5324 0.7323 1.1325 0.1472 -0.1047 -0.1268 382 GLY B N 10156 C CA . GLY B 382 ? 1.5276 0.6505 1.1068 0.1486 -0.1395 -0.1179 382 GLY B CA 10157 C C . GLY B 382 ? 1.5604 0.6521 1.1146 0.1215 -0.1401 -0.0916 382 GLY B C 10158 O O . GLY B 382 ? 2.0148 1.0438 1.5524 0.1201 -0.1693 -0.0880 382 GLY B O 10159 N N . LEU B 383 ? 1.5387 0.6720 1.0938 0.0992 -0.1110 -0.0724 383 LEU B N 10160 C CA . LEU B 383 ? 1.6961 0.8092 1.2354 0.0746 -0.1123 -0.0517 383 LEU B CA 10161 C C . LEU B 383 ? 1.6159 0.7370 1.1589 0.0475 -0.0925 -0.0136 383 LEU B C 10162 O O . LEU B 383 ? 1.4680 0.6347 1.0313 0.0444 -0.0686 -0.0054 383 LEU B O 10163 C CB . LEU B 383 ? 1.6285 0.7840 1.1687 0.0724 -0.1035 -0.0695 383 LEU B CB 10164 C CG . LEU B 383 ? 1.8310 0.9657 1.3563 0.0508 -0.1118 -0.0560 383 LEU B CG 10165 C CD1 . LEU B 383 ? 1.9202 0.9836 1.4315 0.0546 -0.1437 -0.0637 383 LEU B CD1 10166 C CD2 . LEU B 383 ? 1.9591 1.1417 1.4791 0.0478 -0.1048 -0.0751 383 LEU B CD2 10167 N N . LYS B 384 ? 1.6508 0.7280 1.1788 0.0272 -0.1030 0.0067 384 LYS B N 10168 C CA . LYS B 384 ? 1.4517 0.5403 0.9901 -0.0001 -0.0842 0.0356 384 LYS B CA 10169 C C . LYS B 384 ? 1.6016 0.7104 1.1521 -0.0177 -0.0783 0.0447 384 LYS B C 10170 O O . LYS B 384 ? 1.5950 0.7173 1.1650 -0.0393 -0.0649 0.0642 384 LYS B O 10171 C CB . LYS B 384 ? 1.4444 0.4807 0.9598 -0.0179 -0.0959 0.0525 384 LYS B CB 10172 C CG . LYS B 384 ? 1.6608 0.6669 1.1568 -0.0030 -0.1112 0.0480 384 LYS B CG 10173 C CD . LYS B 384 ? 1.8105 0.7650 1.2743 -0.0290 -0.1236 0.0713 384 LYS B CD 10174 C CE . LYS B 384 ? 1.8620 0.7660 1.3081 -0.0440 -0.1455 0.0775 384 LYS B CE 10175 N NZ . LYS B 384 ? 1.8174 0.6857 1.2599 -0.0149 -0.1778 0.0542 384 LYS B NZ 10176 N N . SER B 385 ? 1.6726 0.7869 1.2143 -0.0088 -0.0896 0.0275 385 SER B N 10177 C CA . SER B 385 ? 1.5316 0.6560 1.0769 -0.0263 -0.0928 0.0354 385 SER B CA 10178 C C . SER B 385 ? 1.5310 0.7114 1.0852 -0.0245 -0.0826 0.0330 385 SER B C 10179 O O . SER B 385 ? 1.7915 1.0003 1.3420 -0.0082 -0.0752 0.0163 385 SER B O 10180 C CB . SER B 385 ? 1.8788 0.9574 1.4000 -0.0257 -0.1192 0.0190 385 SER B CB 10181 O OG . SER B 385 ? 1.9903 1.0104 1.4983 -0.0299 -0.1331 0.0253 385 SER B OG 10182 N N . CYS B 386 ? 1.5219 0.7192 1.0882 -0.0438 -0.0837 0.0507 386 CYS B N 10183 C CA . CYS B 386 ? 1.5718 0.8166 1.1389 -0.0487 -0.0807 0.0557 386 CYS B CA 10184 C C . CYS B 386 ? 1.6290 0.8711 1.1842 -0.0641 -0.0995 0.0574 386 CYS B C 10185 O O . CYS B 386 ? 1.5799 0.8053 1.1549 -0.0794 -0.1068 0.0733 386 CYS B O 10186 C CB . CYS B 386 ? 1.5110 0.7885 1.1169 -0.0572 -0.0652 0.0837 386 CYS B CB 10187 S SG . CYS B 386 ? 2.2676 1.5653 1.8861 -0.0405 -0.0427 0.0781 386 CYS B SG 10188 N N . MET B 387 ? 1.7992 1.0633 1.3233 -0.0615 -0.1065 0.0380 387 MET B N 10189 C CA . MET B 387 ? 1.8521 1.1144 1.3570 -0.0747 -0.1266 0.0313 387 MET B CA 10190 C C . MET B 387 ? 1.8965 1.2068 1.3959 -0.0927 -0.1300 0.0531 387 MET B C 10191 O O . MET B 387 ? 2.0509 1.3999 1.5436 -0.0929 -0.1169 0.0607 387 MET B O 10192 C CB . MET B 387 ? 1.9046 1.1558 1.3761 -0.0606 -0.1356 -0.0135 387 MET B CB 10193 C CG . MET B 387 ? 1.9614 1.2152 1.4094 -0.0734 -0.1561 -0.0296 387 MET B CG 10194 S SD . MET B 387 ? 2.6842 1.8798 2.1500 -0.0867 -0.1781 -0.0196 387 MET B SD 10195 C CE . MET B 387 ? 2.1704 1.3828 1.6053 -0.0993 -0.2011 -0.0468 387 MET B CE 10196 N N . GLY B 388 ? 1.8995 1.2060 1.4017 -0.1100 -0.1501 0.0650 388 GLY B N 10197 C CA . GLY B 388 ? 1.9254 1.2719 1.4162 -0.1291 -0.1626 0.0867 388 GLY B CA 10198 C C . GLY B 388 ? 1.8262 1.1925 1.3569 -0.1370 -0.1587 0.1291 388 GLY B C 10199 O O . GLY B 388 ? 1.8380 1.2399 1.3521 -0.1458 -0.1571 0.1465 388 GLY B O 10200 N N . LEU B 389 ? 1.7260 1.0704 1.3115 -0.1360 -0.1577 0.1445 389 LEU B N 10201 C CA . LEU B 389 ? 1.7695 1.1297 1.4078 -0.1401 -0.1549 0.1780 389 LEU B CA 10202 C C . LEU B 389 ? 1.8071 1.1751 1.4843 -0.1562 -0.1824 0.2036 389 LEU B C 10203 O O . LEU B 389 ? 1.6635 1.0172 1.3460 -0.1626 -0.1968 0.1937 389 LEU B O 10204 C CB . LEU B 389 ? 1.5903 0.9311 1.2724 -0.1280 -0.1325 0.1727 389 LEU B CB 10205 C CG . LEU B 389 ? 1.5471 0.8789 1.2007 -0.1104 -0.1089 0.1503 389 LEU B CG 10206 C CD1 . LEU B 389 ? 1.4535 0.7741 1.1512 -0.1034 -0.0895 0.1516 389 LEU B CD1 10207 C CD2 . LEU B 389 ? 1.7155 1.0800 1.3405 -0.1084 -0.1020 0.1538 389 LEU B CD2 10208 N N . LYS B 390 ? 1.8605 1.2503 1.5683 -0.1632 -0.1926 0.2369 390 LYS B N 10209 C CA . LYS B 390 ? 1.8258 1.2220 1.5888 -0.1747 -0.2225 0.2628 390 LYS B CA 10210 C C . LYS B 390 ? 1.8060 1.1956 1.6574 -0.1663 -0.2108 0.2629 390 LYS B C 10211 O O . LYS B 390 ? 1.8568 1.2351 1.7143 -0.1548 -0.1802 0.2427 390 LYS B O 10212 C CB . LYS B 390 ? 1.9389 1.3577 1.6925 -0.1885 -0.2471 0.3019 390 LYS B CB 10213 C CG . LYS B 390 ? 2.0561 1.4922 1.7180 -0.2031 -0.2572 0.3012 390 LYS B CG 10214 C CD . LYS B 390 ? 1.9957 1.4295 1.6356 -0.2128 -0.2828 0.2885 390 LYS B CD 10215 C CE . LYS B 390 ? 2.0947 1.5534 1.6439 -0.2303 -0.2935 0.2849 390 LYS B CE 10216 N NZ . LYS B 390 ? 2.1138 1.5976 1.6439 -0.2515 -0.3146 0.3312 390 LYS B NZ 10217 N N . ILE B 391 ? 1.7615 1.1610 1.6831 -0.1727 -0.2366 0.2832 391 ILE B N 10218 C CA . ILE B 391 ? 1.5045 0.9074 1.5211 -0.1656 -0.2261 0.2782 391 ILE B CA 10219 C C . ILE B 391 ? 1.4672 0.8795 1.5285 -0.1610 -0.2312 0.3046 391 ILE B C 10220 O O . ILE B 391 ? 1.7651 1.1834 1.8306 -0.1695 -0.2652 0.3387 391 ILE B O 10221 C CB . ILE B 391 ? 1.4620 0.8739 1.5502 -0.1730 -0.2507 0.2758 391 ILE B CB 10222 C CG1 . ILE B 391 ? 1.5475 0.9477 1.6032 -0.1800 -0.2403 0.2469 391 ILE B CG1 10223 C CG2 . ILE B 391 ? 1.3550 0.7813 1.5533 -0.1660 -0.2417 0.2682 391 ILE B CG2 10224 C CD1 . ILE B 391 ? 1.5359 0.9299 1.5198 -0.1902 -0.2660 0.2509 391 ILE B CD1 10225 N N . GLY B 392 ? 1.3239 0.7358 1.4175 -0.1496 -0.1998 0.2898 392 GLY B N 10226 C CA . GLY B 392 ? 1.4552 0.8725 1.5901 -0.1450 -0.2010 0.3104 392 GLY B CA 10227 C C . GLY B 392 ? 1.6408 1.0550 1.7063 -0.1411 -0.1744 0.3085 392 GLY B C 10228 O O . GLY B 392 ? 1.5791 0.9970 1.6731 -0.1380 -0.1684 0.3209 392 GLY B O 10229 N N . ASP B 393 ? 1.7083 1.1164 1.6887 -0.1409 -0.1599 0.2904 393 ASP B N 10230 C CA . ASP B 393 ? 1.6665 1.0761 1.5852 -0.1351 -0.1349 0.2811 393 ASP B CA 10231 C C . ASP B 393 ? 1.5797 0.9839 1.5251 -0.1204 -0.1018 0.2543 393 ASP B C 10232 O O . ASP B 393 ? 1.2702 0.6673 1.2537 -0.1174 -0.0935 0.2358 393 ASP B O 10233 C CB . ASP B 393 ? 1.7442 1.1499 1.5743 -0.1372 -0.1337 0.2642 393 ASP B CB 10234 C CG . ASP B 393 ? 2.0138 1.4319 1.8043 -0.1549 -0.1640 0.2878 393 ASP B CG 10235 O OD1 . ASP B 393 ? 2.1326 1.5540 1.9686 -0.1651 -0.1927 0.3173 393 ASP B OD1 10236 O OD2 . ASP B 393 ? 1.9700 1.3961 1.6856 -0.1589 -0.1607 0.2748 393 ASP B OD2 10237 N N . THR B 394 ? 1.7383 1.1493 1.6618 -0.1142 -0.0829 0.2516 394 THR B N 10238 C CA . THR B 394 ? 1.3254 0.7335 1.2672 -0.1010 -0.0540 0.2269 394 THR B CA 10239 C C . THR B 394 ? 1.2876 0.6939 1.1589 -0.0916 -0.0367 0.2069 394 THR B C 10240 O O . THR B 394 ? 1.3330 0.7539 1.1645 -0.0952 -0.0385 0.2151 394 THR B O 10241 C CB . THR B 394 ? 1.2858 0.7066 1.2957 -0.0996 -0.0485 0.2381 394 THR B CB 10242 O OG1 . THR B 394 ? 1.2472 0.6699 1.3305 -0.1068 -0.0717 0.2575 394 THR B OG1 10243 C CG2 . THR B 394 ? 1.1760 0.5969 1.2119 -0.0882 -0.0205 0.2087 394 THR B CG2 10244 N N . VAL B 395 ? 1.2698 0.6602 1.1273 -0.0812 -0.0212 0.1802 395 VAL B N 10245 C CA . VAL B 395 ? 1.2988 0.6840 1.1011 -0.0685 -0.0096 0.1584 395 VAL B CA 10246 C C . VAL B 395 ? 1.2594 0.6438 1.0817 -0.0575 0.0108 0.1423 395 VAL B C 10247 O O . VAL B 395 ? 1.2133 0.5968 1.0819 -0.0613 0.0181 0.1416 395 VAL B O 10248 C CB . VAL B 395 ? 1.3782 0.7360 1.1307 -0.0657 -0.0190 0.1414 395 VAL B CB 10249 C CG1 . VAL B 395 ? 1.4008 0.7653 1.1214 -0.0749 -0.0379 0.1496 395 VAL B CG1 10250 C CG2 . VAL B 395 ? 1.4946 0.8295 1.2704 -0.0723 -0.0193 0.1387 395 VAL B CG2 10251 N N . SER B 396 ? 1.4256 0.8149 1.2149 -0.0447 0.0196 0.1259 396 SER B N 10252 C CA . SER B 396 ? 1.3481 0.7392 1.1515 -0.0339 0.0356 0.1102 396 SER B CA 10253 C C . SER B 396 ? 1.4743 0.8413 1.2304 -0.0194 0.0328 0.0866 396 SER B C 10254 O O . SER B 396 ? 1.3379 0.6978 1.0544 -0.0124 0.0225 0.0766 396 SER B O 10255 C CB . SER B 396 ? 1.2700 0.6934 1.0944 -0.0315 0.0468 0.1130 396 SER B CB 10256 O OG . SER B 396 ? 1.3612 0.7884 1.1952 -0.0198 0.0602 0.0938 396 SER B OG 10257 N N . PHE B 397 ? 1.4626 0.8174 1.2246 -0.0157 0.0399 0.0768 397 PHE B N 10258 C CA . PHE B 397 ? 1.2707 0.5980 0.9914 -0.0023 0.0318 0.0589 397 PHE B CA 10259 C C . PHE B 397 ? 1.2938 0.6341 1.0275 0.0069 0.0426 0.0468 397 PHE B C 10260 O O . PHE B 397 ? 1.5878 0.9400 1.3526 -0.0032 0.0559 0.0502 397 PHE B O 10261 C CB . PHE B 397 ? 1.2640 0.5506 0.9605 -0.0136 0.0214 0.0635 397 PHE B CB 10262 C CG . PHE B 397 ? 1.3489 0.6195 1.0313 -0.0222 0.0078 0.0716 397 PHE B CG 10263 C CD1 . PHE B 397 ? 1.3782 0.6592 1.0915 -0.0409 0.0115 0.0872 397 PHE B CD1 10264 C CD2 . PHE B 397 ? 1.3747 0.6214 1.0185 -0.0109 -0.0104 0.0599 397 PHE B CD2 10265 C CE1 . PHE B 397 ? 1.3488 0.6170 1.0500 -0.0494 -0.0032 0.0938 397 PHE B CE1 10266 C CE2 . PHE B 397 ? 1.3453 0.5787 0.9761 -0.0198 -0.0235 0.0642 397 PHE B CE2 10267 C CZ . PHE B 397 ? 1.4480 0.6922 1.1051 -0.0398 -0.0201 0.0826 397 PHE B CZ 10268 N N . SER B 398 ? 1.3073 0.6490 1.0217 0.0264 0.0363 0.0287 398 SER B N 10269 C CA . SER B 398 ? 1.3872 0.7380 1.1094 0.0367 0.0407 0.0150 398 SER B CA 10270 C C . SER B 398 ? 1.4341 0.7403 1.1148 0.0433 0.0200 0.0091 398 SER B C 10271 O O . SER B 398 ? 1.3347 0.6113 0.9863 0.0543 -0.0007 0.0027 398 SER B O 10272 C CB . SER B 398 ? 1.4704 0.8572 1.2074 0.0532 0.0459 -0.0026 398 SER B CB 10273 O OG . SER B 398 ? 1.5924 0.9693 1.3024 0.0691 0.0303 -0.0192 398 SER B OG 10274 N N . ILE B 399 ? 1.4021 0.7029 1.0803 0.0347 0.0237 0.0111 399 ILE B N 10275 C CA . ILE B 399 ? 1.3442 0.5989 0.9763 0.0324 0.0019 0.0143 399 ILE B CA 10276 C C . ILE B 399 ? 1.3869 0.6469 1.0127 0.0431 -0.0053 0.0023 399 ILE B C 10277 O O . ILE B 399 ? 1.5232 0.8169 1.1730 0.0347 0.0144 -0.0022 399 ILE B O 10278 C CB . ILE B 399 ? 1.5386 0.7771 1.1566 0.0014 0.0100 0.0319 399 ILE B CB 10279 C CG1 . ILE B 399 ? 1.5544 0.7955 1.1898 -0.0098 0.0175 0.0425 399 ILE B CG1 10280 C CG2 . ILE B 399 ? 1.6262 0.8106 1.1869 -0.0074 -0.0156 0.0420 399 ILE B CG2 10281 C CD1 . ILE B 399 ? 1.6141 0.8561 1.2553 -0.0404 0.0315 0.0537 399 ILE B CD1 10282 N N . GLU B 400 ? 1.5824 0.8084 1.1798 0.0621 -0.0363 -0.0047 400 GLU B N 10283 C CA . GLU B 400 ? 1.6092 0.8336 1.1963 0.0727 -0.0521 -0.0138 400 GLU B CA 10284 C C . GLU B 400 ? 1.5445 0.7190 1.0757 0.0523 -0.0737 0.0070 400 GLU B C 10285 O O . GLU B 400 ? 1.6298 0.7510 1.1268 0.0487 -0.0984 0.0210 400 GLU B O 10286 C CB . GLU B 400 ? 1.6623 0.8835 1.2616 0.1080 -0.0775 -0.0368 400 GLU B CB 10287 C CG . GLU B 400 ? 1.7225 0.9445 1.3188 0.1223 -0.0990 -0.0480 400 GLU B CG 10288 C CD . GLU B 400 ? 1.9755 1.1869 1.5879 0.1586 -0.1317 -0.0729 400 GLU B CD 10289 O OE1 . GLU B 400 ? 2.1338 1.3709 1.7696 0.1769 -0.1415 -0.0927 400 GLU B OE1 10290 O OE2 . GLU B 400 ? 1.9743 1.1541 1.5813 0.1691 -0.1485 -0.0764 400 GLU B OE2 10291 N N . ALA B 401 ? 1.5414 0.7340 1.0619 0.0360 -0.0646 0.0087 401 ALA B N 10292 C CA . ALA B 401 ? 1.6182 0.7708 1.0773 0.0094 -0.0829 0.0299 401 ALA B CA 10293 C C . ALA B 401 ? 1.6895 0.8224 1.1224 0.0248 -0.1197 0.0272 401 ALA B C 10294 O O . ALA B 401 ? 1.7100 0.8843 1.1610 0.0298 -0.1104 0.0109 401 ALA B O 10295 C CB . ALA B 401 ? 1.6332 0.8230 1.0918 -0.0266 -0.0467 0.0322 401 ALA B CB 10296 N N . LYS B 402 ? 1.7278 0.7955 1.1216 0.0323 -0.1649 0.0429 402 LYS B N 10297 C CA . LYS B 402 ? 1.7962 0.8363 1.1696 0.0508 -0.2106 0.0425 402 LYS B CA 10298 C C . LYS B 402 ? 1.8866 0.8756 1.1808 0.0153 -0.2390 0.0778 402 LYS B C 10299 O O . LYS B 402 ? 1.9450 0.8849 1.1984 -0.0101 -0.2476 0.1050 402 LYS B O 10300 C CB . LYS B 402 ? 2.0850 1.0878 1.4842 0.0913 -0.2494 0.0297 402 LYS B CB 10301 C CG . LYS B 402 ? 2.3181 1.2900 1.7103 0.1164 -0.3038 0.0260 402 LYS B CG 10302 C CD . LYS B 402 ? 2.2381 1.2770 1.6754 0.1376 -0.2905 -0.0051 402 LYS B CD 10303 C CE . LYS B 402 ? 2.3385 1.3514 1.7848 0.1699 -0.3483 -0.0152 402 LYS B CE 10304 N NZ . LYS B 402 ? 2.4911 1.4411 1.8626 0.1456 -0.3943 0.0238 402 LYS B NZ 10305 N N . VAL B 403 ? 1.9629 0.9648 1.2331 0.0106 -0.2541 0.0779 403 VAL B N 10306 C CA . VAL B 403 ? 2.1440 1.0988 1.3301 -0.0256 -0.2864 0.1137 403 VAL B CA 10307 C C . VAL B 403 ? 2.1689 1.0776 1.3404 0.0019 -0.3528 0.1201 403 VAL B C 10308 O O . VAL B 403 ? 2.2332 1.1780 1.4554 0.0390 -0.3601 0.0895 403 VAL B O 10309 C CB . VAL B 403 ? 2.1292 1.1402 1.2848 -0.0665 -0.2485 0.1115 403 VAL B CB 10310 C CG1 . VAL B 403 ? 2.1786 1.2536 1.3824 -0.0408 -0.2367 0.0757 403 VAL B CG1 10311 C CG2 . VAL B 403 ? 2.1977 1.1638 1.2548 -0.1116 -0.2805 0.1507 403 VAL B CG2 10312 N N . ARG B 404 ? 2.1487 0.9765 1.2553 -0.0168 -0.4035 0.1602 404 ARG B N 10313 C CA . ARG B 404 ? 2.1992 0.9719 1.2905 0.0070 -0.4763 0.1723 404 ARG B CA 10314 C C . ARG B 404 ? 2.2870 1.0468 1.2900 -0.0362 -0.5001 0.2064 404 ARG B C 10315 O O . ARG B 404 ? 2.3473 1.0624 1.2702 -0.0864 -0.5078 0.2493 404 ARG B O 10316 C CB . ARG B 404 ? 2.1873 0.8676 1.2748 0.0206 -0.5283 0.1941 404 ARG B CB 10317 C CG . ARG B 404 ? 2.4412 1.0501 1.5129 0.0423 -0.6132 0.2127 404 ARG B CG 10318 C CD . ARG B 404 ? 2.6836 1.1922 1.7420 0.0432 -0.6634 0.2412 404 ARG B CD 10319 N NE . ARG B 404 ? 2.7861 1.2643 1.7700 -0.0177 -0.6398 0.2838 404 ARG B NE 10320 C CZ . ARG B 404 ? 2.8675 1.3176 1.8631 -0.0326 -0.6503 0.2942 404 ARG B CZ 10321 N NH1 . ARG B 404 ? 2.7475 1.1774 1.8134 0.0096 -0.6898 0.2705 404 ARG B NH1 10322 N NH2 . ARG B 404 ? 2.9748 1.4216 1.9150 -0.0902 -0.6204 0.3251 404 ARG B NH2 10323 N N . GLY B 405 ? 2.3254 1.1271 1.3411 -0.0195 -0.5117 0.1867 405 GLY B N 10324 C CA . GLY B 405 ? 2.4528 1.2579 1.3848 -0.0616 -0.5289 0.2124 405 GLY B CA 10325 C C . GLY B 405 ? 2.4953 1.3632 1.3914 -0.1147 -0.4579 0.2089 405 GLY B C 10326 O O . GLY B 405 ? 2.5054 1.4300 1.4631 -0.1062 -0.3963 0.1762 405 GLY B O 10327 N N . CYS B 406 ? 2.5437 1.4037 1.3419 -0.1708 -0.4673 0.2412 406 CYS B N 10328 C CA . CYS B 406 ? 2.4648 1.3854 1.2280 -0.2259 -0.4006 0.2348 406 CYS B CA 10329 C C . CYS B 406 ? 2.5896 1.4580 1.2408 -0.2928 -0.4169 0.2887 406 CYS B C 10330 O O . CYS B 406 ? 2.7865 1.5951 1.3593 -0.3111 -0.4800 0.3309 406 CYS B O 10331 C CB . CYS B 406 ? 2.5876 1.5919 1.3521 -0.2346 -0.3741 0.2003 406 CYS B CB 10332 S SG . CYS B 406 ? 3.5521 2.6393 2.2778 -0.3034 -0.2952 0.1825 406 CYS B SG 10333 N N . PRO B 407 ? 2.5527 1.4449 1.1975 -0.3316 -0.3611 0.2882 407 PRO B N 10334 C CA . PRO B 407 ? 2.7916 1.6486 1.3357 -0.4031 -0.3627 0.3345 407 PRO B CA 10335 C C . PRO B 407 ? 2.8832 1.7910 1.3369 -0.4654 -0.3474 0.3393 407 PRO B C 10336 O O . PRO B 407 ? 2.8966 1.7612 1.2431 -0.5255 -0.3731 0.3888 407 PRO B O 10337 C CB . PRO B 407 ? 2.5915 1.4826 1.1862 -0.4152 -0.2979 0.3149 407 PRO B CB 10338 C CG . PRO B 407 ? 2.3909 1.3016 1.1040 -0.3436 -0.2835 0.2737 407 PRO B CG 10339 C CD . PRO B 407 ? 2.3982 1.3458 1.1403 -0.3061 -0.2980 0.2453 407 PRO B CD 10340 N N . GLN B 408 ? 2.7951 1.7946 1.2921 -0.4534 -0.3053 0.2873 408 GLN B N 10341 C CA . GLN B 408 ? 2.8707 1.9416 1.2995 -0.5115 -0.2741 0.2738 408 GLN B CA 10342 C C . GLN B 408 ? 3.0083 2.1150 1.4005 -0.5784 -0.2159 0.2753 408 GLN B C 10343 O O . GLN B 408 ? 3.0265 2.1740 1.3314 -0.6455 -0.1973 0.2801 408 GLN B O 10344 C CB . GLN B 408 ? 2.9089 1.9331 1.2247 -0.5399 -0.3430 0.3192 408 GLN B CB 10345 C CG . GLN B 408 ? 2.9414 2.0484 1.1963 -0.5861 -0.3185 0.2947 408 GLN B CG 10346 C CD . GLN B 408 ? 2.9221 2.1264 1.2817 -0.5466 -0.2653 0.2193 408 GLN B CD 10347 O OE1 . GLN B 408 ? 2.9142 2.1113 1.3591 -0.4786 -0.2860 0.1976 408 GLN B OE1 10348 N NE2 . GLN B 408 ? 2.8606 2.1578 1.2179 -0.5907 -0.1963 0.1770 408 GLN B NE2 10349 N N . GLU B 409 ? 2.9654 2.0614 1.4267 -0.5609 -0.1868 0.2686 409 GLU B N 10350 C CA . GLU B 409 ? 2.8128 1.9605 1.2758 -0.6119 -0.1224 0.2539 409 GLU B CA 10351 C C . GLU B 409 ? 2.7938 2.0520 1.3471 -0.5977 -0.0544 0.1818 409 GLU B C 10352 O O . GLU B 409 ? 2.7101 1.9879 1.3424 -0.5386 -0.0572 0.1491 409 GLU B O 10353 C CB . GLU B 409 ? 2.5419 1.6338 1.0472 -0.5972 -0.1232 0.2744 409 GLU B CB 10354 C CG . GLU B 409 ? 2.4768 1.5725 1.1076 -0.5202 -0.1144 0.2407 409 GLU B CG 10355 C CD . GLU B 409 ? 2.6331 1.6615 1.2911 -0.5046 -0.1293 0.2664 409 GLU B CD 10356 O OE1 . GLU B 409 ? 2.8844 1.8486 1.4648 -0.5471 -0.1574 0.3148 409 GLU B OE1 10357 O OE2 . GLU B 409 ? 2.5165 1.5561 1.2715 -0.4525 -0.1138 0.2388 409 GLU B OE2 10358 N N . LYS B 410 ? 2.7311 2.0626 1.2780 -0.6523 0.0058 0.1551 410 LYS B N 10359 C CA . LYS B 410 ? 2.5948 2.0318 1.2281 -0.6430 0.0670 0.0836 410 LYS B CA 10360 C C . LYS B 410 ? 2.4605 1.9085 1.2295 -0.5855 0.0933 0.0529 410 LYS B C 10361 O O . LYS B 410 ? 2.4738 1.9295 1.3193 -0.5272 0.0862 0.0281 410 LYS B O 10362 C CB . LYS B 410 ? 2.6430 2.1609 1.2355 -0.7196 0.1236 0.0577 410 LYS B CB 10363 C CG . LYS B 410 ? 2.8303 2.3399 1.2738 -0.7890 0.1003 0.0934 410 LYS B CG 10364 C CD . LYS B 410 ? 2.8647 2.4707 1.2739 -0.8671 0.1645 0.0576 410 LYS B CD 10365 C CE . LYS B 410 ? 2.7479 2.4658 1.2406 -0.8541 0.2174 -0.0266 410 LYS B CE 10366 N NZ . LYS B 410 ? 2.7744 2.4965 1.2261 -0.8378 0.1838 -0.0326 410 LYS B NZ 10367 N N . GLU B 411 ? 2.3015 1.7498 1.0982 -0.6043 0.1213 0.0566 411 GLU B N 10368 C CA . GLU B 411 ? 2.2106 1.6662 1.1285 -0.5550 0.1420 0.0332 411 GLU B CA 10369 C C . GLU B 411 ? 2.1865 1.5894 1.0992 -0.5668 0.1359 0.0683 411 GLU B C 10370 O O . GLU B 411 ? 2.3029 1.7084 1.1518 -0.6276 0.1490 0.0862 411 GLU B O 10371 C CB . GLU B 411 ? 2.4138 1.9725 1.4257 -0.5602 0.2050 -0.0335 411 GLU B CB 10372 C CG . GLU B 411 ? 2.6110 2.2194 1.6723 -0.5288 0.2124 -0.0774 411 GLU B CG 10373 C CD . GLU B 411 ? 2.6570 2.3496 1.8405 -0.5179 0.2660 -0.1415 411 GLU B CD 10374 O OE1 . GLU B 411 ? 2.7095 2.4177 1.9494 -0.5254 0.2929 -0.1502 411 GLU B OE1 10375 O OE2 . GLU B 411 ? 2.6044 2.3466 1.8324 -0.5014 0.2783 -0.1840 411 GLU B OE2 10376 N N . LYS B 412 ? 2.1470 1.5061 1.1271 -0.5111 0.1171 0.0762 412 LYS B N 10377 C CA . LYS B 412 ? 2.1064 1.4232 1.1014 -0.5147 0.1140 0.1001 412 LYS B CA 10378 C C . LYS B 412 ? 2.0324 1.3664 1.1448 -0.4604 0.1290 0.0733 412 LYS B C 10379 O O . LYS B 412 ? 2.0159 1.3456 1.1735 -0.4081 0.1141 0.0617 412 LYS B O 10380 C CB . LYS B 412 ? 2.2158 1.4273 1.1340 -0.5102 0.0531 0.1580 412 LYS B CB 10381 C CG . LYS B 412 ? 2.4466 1.6269 1.2417 -0.5732 0.0323 0.1974 412 LYS B CG 10382 C CD . LYS B 412 ? 2.5787 1.6463 1.3116 -0.5657 -0.0335 0.2551 412 LYS B CD 10383 C CE . LYS B 412 ? 2.6414 1.6689 1.3976 -0.5731 -0.0320 0.2726 412 LYS B CE 10384 N NZ . LYS B 412 ? 2.5052 1.4200 1.2002 -0.5714 -0.0979 0.3273 412 LYS B NZ 10385 N N . SER B 413 ? 1.9832 1.3385 1.1438 -0.4756 0.1573 0.0644 413 SER B N 10386 C CA . SER B 413 ? 1.9011 1.2742 1.1692 -0.4308 0.1699 0.0425 413 SER B CA 10387 C C . SER B 413 ? 1.8712 1.1834 1.1388 -0.4228 0.1470 0.0738 413 SER B C 10388 O O . SER B 413 ? 2.0516 1.3480 1.2776 -0.4671 0.1506 0.0926 413 SER B O 10389 C CB . SER B 413 ? 1.8744 1.3380 1.2253 -0.4487 0.2231 -0.0057 413 SER B CB 10390 O OG . SER B 413 ? 2.0582 1.5809 1.4110 -0.4589 0.2454 -0.0403 413 SER B OG 10391 N N . PHE B 414 ? 1.8090 1.0898 1.1217 -0.3694 0.1245 0.0778 414 PHE B N 10392 C CA . PHE B 414 ? 1.7537 0.9828 1.0725 -0.3590 0.1037 0.1007 414 PHE B CA 10393 C C . PHE B 414 ? 1.6707 0.9369 1.0885 -0.3303 0.1227 0.0780 414 PHE B C 10394 O O . PHE B 414 ? 1.6401 0.9661 1.1247 -0.3166 0.1492 0.0469 414 PHE B O 10395 C CB . PHE B 414 ? 1.7579 0.9078 1.0305 -0.3257 0.0526 0.1290 414 PHE B CB 10396 C CG . PHE B 414 ? 1.7209 0.8805 1.0398 -0.2704 0.0430 0.1120 414 PHE B CG 10397 C CD1 . PHE B 414 ? 1.7890 0.9440 1.1647 -0.2332 0.0383 0.1058 414 PHE B CD1 10398 C CD2 . PHE B 414 ? 1.7670 0.9416 1.0689 -0.2588 0.0377 0.1026 414 PHE B CD2 10399 C CE1 . PHE B 414 ? 1.8051 0.9730 1.2194 -0.1884 0.0319 0.0910 414 PHE B CE1 10400 C CE2 . PHE B 414 ? 1.7242 0.9108 1.0710 -0.2112 0.0301 0.0861 414 PHE B CE2 10401 C CZ . PHE B 414 ? 1.6494 0.8332 1.0517 -0.1774 0.0286 0.0808 414 PHE B CZ 10402 N N . THR B 415 ? 1.6234 0.8515 1.0505 -0.3222 0.1060 0.0944 415 THR B N 10403 C CA . THR B 415 ? 1.5513 0.8118 1.0638 -0.3034 0.1201 0.0786 415 THR B CA 10404 C C . THR B 415 ? 1.5011 0.7162 1.0208 -0.2622 0.0885 0.0921 415 THR B C 10405 O O . THR B 415 ? 1.6926 0.8450 1.1575 -0.2612 0.0576 0.1147 415 THR B O 10406 C CB . THR B 415 ? 1.5544 0.8348 1.0859 -0.3440 0.1393 0.0767 415 THR B CB 10407 O OG1 . THR B 415 ? 1.6806 1.0090 1.2000 -0.3879 0.1716 0.0603 415 THR B OG1 10408 C CG2 . THR B 415 ? 1.5036 0.8245 1.1316 -0.3248 0.1517 0.0582 415 THR B CG2 10409 N N . ILE B 416 ? 1.4411 0.6889 1.0294 -0.2302 0.0956 0.0771 416 ILE B N 10410 C CA . ILE B 416 ? 1.3962 0.6158 0.9960 -0.1971 0.0719 0.0857 416 ILE B CA 10411 C C . ILE B 416 ? 1.4067 0.6565 1.0724 -0.1996 0.0822 0.0807 416 ILE B C 10412 O O . ILE B 416 ? 1.5077 0.8093 1.2404 -0.1978 0.1037 0.0644 416 ILE B O 10413 C CB . ILE B 416 ? 1.3682 0.5966 0.9821 -0.1583 0.0656 0.0777 416 ILE B CB 10414 C CG1 . ILE B 416 ? 1.4388 0.6383 0.9927 -0.1539 0.0506 0.0813 416 ILE B CG1 10415 C CG2 . ILE B 416 ? 1.3377 0.5466 0.9606 -0.1298 0.0454 0.0831 416 ILE B CG2 10416 C CD1 . ILE B 416 ? 1.6225 0.8361 1.1932 -0.1182 0.0457 0.0696 416 ILE B CD1 10417 N N . LYS B 417 ? 1.3658 0.5814 1.0158 -0.2032 0.0634 0.0938 417 LYS B N 10418 C CA . LYS B 417 ? 1.3436 0.5847 1.0492 -0.2130 0.0691 0.0911 417 LYS B CA 10419 C C . LYS B 417 ? 1.4852 0.6999 1.1886 -0.1925 0.0430 0.1007 417 LYS B C 10420 O O . LYS B 417 ? 1.8130 0.9778 1.4615 -0.1843 0.0199 0.1094 417 LYS B O 10421 C CB . LYS B 417 ? 1.5143 0.7534 1.2076 -0.2559 0.0792 0.0930 417 LYS B CB 10422 C CG . LYS B 417 ? 1.6693 0.9736 1.4274 -0.2793 0.1127 0.0714 417 LYS B CG 10423 C CD . LYS B 417 ? 1.5544 0.8607 1.2926 -0.3271 0.1255 0.0718 417 LYS B CD 10424 C CE . LYS B 417 ? 1.7051 0.9704 1.4278 -0.3343 0.1015 0.0888 417 LYS B CE 10425 N NZ . LYS B 417 ? 1.7931 1.0835 1.5893 -0.3122 0.0930 0.0820 417 LYS B NZ 10426 N N . PRO B 418 ? 1.5546 0.8036 1.3196 -0.1849 0.0445 0.0977 418 PRO B N 10427 C CA . PRO B 418 ? 1.5579 0.7879 1.3184 -0.1762 0.0206 0.1063 418 PRO B CA 10428 C C . PRO B 418 ? 1.5646 0.7740 1.3138 -0.2055 0.0145 0.1098 418 PRO B C 10429 O O . PRO B 418 ? 1.5367 0.7725 1.3173 -0.2326 0.0338 0.1035 418 PRO B O 10430 C CB . PRO B 418 ? 1.3068 0.5821 1.1384 -0.1658 0.0229 0.1056 418 PRO B CB 10431 C CG . PRO B 418 ? 1.3182 0.6355 1.2078 -0.1789 0.0491 0.0926 418 PRO B CG 10432 C CD . PRO B 418 ? 1.4204 0.7251 1.2633 -0.1831 0.0642 0.0861 418 PRO B CD 10433 N N . VAL B 419 ? 1.4754 0.6417 1.1837 -0.2019 -0.0107 0.1162 419 VAL B N 10434 C CA . VAL B 419 ? 1.4626 0.6019 1.1562 -0.2314 -0.0190 0.1203 419 VAL B CA 10435 C C . VAL B 419 ? 1.4506 0.6331 1.2106 -0.2493 -0.0121 0.1159 419 VAL B C 10436 O O . VAL B 419 ? 1.5008 0.7067 1.2976 -0.2330 -0.0234 0.1154 419 VAL B O 10437 C CB . VAL B 419 ? 1.5520 0.6371 1.1984 -0.2204 -0.0507 0.1230 419 VAL B CB 10438 C CG1 . VAL B 419 ? 1.7332 0.7897 1.3713 -0.2531 -0.0606 0.1275 419 VAL B CG1 10439 C CG2 . VAL B 419 ? 1.5271 0.5669 1.1170 -0.2023 -0.0619 0.1239 419 VAL B CG2 10440 N N . GLY B 420 ? 1.5758 0.7714 1.3514 -0.2848 0.0054 0.1124 420 GLY B N 10441 C CA . GLY B 420 ? 1.6847 0.9237 1.5300 -0.3044 0.0117 0.1034 420 GLY B CA 10442 C C . GLY B 420 ? 1.4193 0.7231 1.3487 -0.2933 0.0287 0.0898 420 GLY B C 10443 O O . GLY B 420 ? 1.4361 0.7728 1.4328 -0.2924 0.0200 0.0845 420 GLY B O 10444 N N . PHE B 421 ? 1.4950 0.8159 1.4251 -0.2846 0.0495 0.0833 421 PHE B N 10445 C CA . PHE B 421 ? 1.3573 0.7363 1.3728 -0.2739 0.0653 0.0670 421 PHE B CA 10446 C C . PHE B 421 ? 1.3236 0.7354 1.3496 -0.2931 0.1009 0.0467 421 PHE B C 10447 O O . PHE B 421 ? 1.4182 0.8017 1.3710 -0.3012 0.1092 0.0525 421 PHE B O 10448 C CB . PHE B 421 ? 1.4003 0.7737 1.4191 -0.2357 0.0502 0.0776 421 PHE B CB 10449 C CG . PHE B 421 ? 1.6960 1.0710 1.7468 -0.2207 0.0208 0.0901 421 PHE B CG 10450 C CD1 . PHE B 421 ? 1.5094 0.9127 1.6277 -0.2344 0.0130 0.0838 421 PHE B CD1 10451 C CD2 . PHE B 421 ? 1.7673 1.1197 1.7806 -0.1953 0.0006 0.1071 421 PHE B CD2 10452 C CE1 . PHE B 421 ? 1.3525 0.7570 1.4959 -0.2223 -0.0186 0.0979 421 PHE B CE1 10453 C CE2 . PHE B 421 ? 1.8521 1.2086 1.8852 -0.1866 -0.0271 0.1207 421 PHE B CE2 10454 C CZ . PHE B 421 ? 1.6948 1.0751 1.7911 -0.1998 -0.0388 0.1179 421 PHE B CZ 10455 N N . LYS B 422 ? 1.3080 0.7812 1.4276 -0.3006 0.1200 0.0207 422 LYS B N 10456 C CA . LYS B 422 ? 1.3196 0.8370 1.4590 -0.3222 0.1572 -0.0075 422 LYS B CA 10457 C C . LYS B 422 ? 1.3828 0.9019 1.5131 -0.2974 0.1647 -0.0114 422 LYS B C 10458 O O . LYS B 422 ? 1.4816 1.0114 1.5749 -0.3141 0.1889 -0.0237 422 LYS B O 10459 C CB . LYS B 422 ? 1.3432 0.9320 1.6002 -0.3350 0.1746 -0.0428 422 LYS B CB 10460 C CG . LYS B 422 ? 1.4935 1.1398 1.7753 -0.3641 0.2177 -0.0811 422 LYS B CG 10461 C CD . LYS B 422 ? 1.5889 1.2186 1.7762 -0.4099 0.2361 -0.0735 422 LYS B CD 10462 C CE . LYS B 422 ? 1.6061 1.3001 1.8086 -0.4449 0.2812 -0.1125 422 LYS B CE 10463 N NZ . LYS B 422 ? 1.8421 1.5184 1.9438 -0.4963 0.2972 -0.0989 422 LYS B NZ 10464 N N . ASP B 423 ? 1.3278 0.8376 1.4899 -0.2607 0.1431 0.0000 423 ASP B N 10465 C CA . ASP B 423 ? 1.4179 0.9290 1.5788 -0.2365 0.1477 -0.0025 423 ASP B CA 10466 C C . ASP B 423 ? 1.2743 0.7402 1.3268 -0.2355 0.1465 0.0136 423 ASP B C 10467 O O . ASP B 423 ? 1.2689 0.6852 1.2541 -0.2301 0.1241 0.0385 423 ASP B O 10468 C CB . ASP B 423 ? 1.5857 1.0889 1.7901 -0.2033 0.1211 0.0144 423 ASP B CB 10469 C CG . ASP B 423 ? 1.5098 1.0553 1.8317 -0.2006 0.1158 -0.0003 423 ASP B CG 10470 O OD1 . ASP B 423 ? 1.3222 0.9039 1.7203 -0.1932 0.1289 -0.0240 423 ASP B OD1 10471 O OD2 . ASP B 423 ? 1.4990 1.0410 1.8413 -0.2053 0.0961 0.0101 423 ASP B OD2 10472 N N . SER B 424 ? 1.5969 0.7504 1.3779 -0.0421 0.1396 0.2554 424 SER B N 10473 C CA . SER B 424 ? 1.6204 0.8178 1.4520 -0.0812 0.1493 0.2421 424 SER B CA 10474 C C . SER B 424 ? 1.8083 0.9052 1.5767 -0.1229 0.1224 0.2452 424 SER B C 10475 O O . SER B 424 ? 1.8529 0.8299 1.5339 -0.1050 0.0982 0.2513 424 SER B O 10476 C CB . SER B 424 ? 1.6211 0.8562 1.4902 -0.0339 0.1689 0.2230 424 SER B CB 10477 O OG . SER B 424 ? 1.8084 0.9419 1.6009 0.0143 0.1530 0.2185 424 SER B OG 10478 N N . LEU B 425 ? 1.7139 0.8629 1.5309 -0.1785 0.1269 0.2381 425 LEU B N 10479 C CA . LEU B 425 ? 1.4186 0.4951 1.1916 -0.2177 0.1045 0.2335 425 LEU B CA 10480 C C . LEU B 425 ? 1.3794 0.4744 1.1802 -0.2002 0.1114 0.2151 425 LEU B C 10481 O O . LEU B 425 ? 1.5128 0.7091 1.3983 -0.2163 0.1295 0.2060 425 LEU B O 10482 C CB . LEU B 425 ? 1.4368 0.5875 1.2571 -0.2851 0.0978 0.2316 425 LEU B CB 10483 C CG . LEU B 425 ? 1.4857 0.6252 1.3005 -0.3179 0.0783 0.2153 425 LEU B CG 10484 C CD1 . LEU B 425 ? 1.5326 0.5579 1.2549 -0.3126 0.0531 0.2198 425 LEU B CD1 10485 C CD2 . LEU B 425 ? 1.7420 0.9858 1.6277 -0.3703 0.0822 0.2052 425 LEU B CD2 10486 N N . ILE B 426 ? 1.5835 0.5849 1.3152 -0.1661 0.0959 0.2090 426 ILE B N 10487 C CA . ILE B 426 ? 1.5461 0.5623 1.2931 -0.1458 0.1002 0.1931 426 ILE B CA 10488 C C . ILE B 426 ? 1.6360 0.6199 1.3615 -0.1909 0.0778 0.1827 426 ILE B C 10489 O O . ILE B 426 ? 1.7199 0.6346 1.3867 -0.2009 0.0534 0.1793 426 ILE B O 10490 C CB . ILE B 426 ? 1.5471 0.5024 1.2401 -0.0781 0.0987 0.1864 426 ILE B CB 10491 C CG1 . ILE B 426 ? 1.5953 0.6074 1.3232 -0.0294 0.1215 0.1908 426 ILE B CG1 10492 C CG2 . ILE B 426 ? 1.4845 0.4541 1.1845 -0.0623 0.1013 0.1716 426 ILE B CG2 10493 C CD1 . ILE B 426 ? 1.8324 0.7953 1.5128 0.0376 0.1219 0.1803 426 ILE B CD1 10494 N N . VAL B 427 ? 1.4402 0.4903 1.2242 -0.2146 0.0868 0.1749 427 VAL B N 10495 C CA . VAL B 427 ? 1.4581 0.5023 1.2360 -0.2550 0.0658 0.1612 427 VAL B CA 10496 C C . VAL B 427 ? 1.4411 0.4665 1.2022 -0.2296 0.0640 0.1509 427 VAL B C 10497 O O . VAL B 427 ? 1.3630 0.4735 1.1915 -0.2123 0.0805 0.1509 427 VAL B O 10498 C CB . VAL B 427 ? 1.3386 0.4932 1.2068 -0.3059 0.0699 0.1564 427 VAL B CB 10499 C CG1 . VAL B 427 ? 1.3633 0.5170 1.2271 -0.3415 0.0501 0.1385 427 VAL B CG1 10500 C CG2 . VAL B 427 ? 1.4363 0.6256 1.3232 -0.3290 0.0710 0.1642 427 VAL B CG2 10501 N N . GLN B 428 ? 1.5431 0.4716 1.2215 -0.2242 0.0426 0.1406 428 GLN B N 10502 C CA . GLN B 428 ? 1.5639 0.4881 1.2243 -0.2015 0.0359 0.1272 428 GLN B CA 10503 C C . GLN B 428 ? 1.5680 0.5304 1.2583 -0.2520 0.0226 0.1162 428 GLN B C 10504 O O . GLN B 428 ? 1.8690 0.7883 1.5314 -0.3016 0.0054 0.1083 428 GLN B O 10505 C CB . GLN B 428 ? 1.6791 0.4886 1.2413 -0.1748 0.0189 0.1155 428 GLN B CB 10506 C CG . GLN B 428 ? 1.7874 0.5480 1.3152 -0.1271 0.0269 0.1232 428 GLN B CG 10507 C CD . GLN B 428 ? 2.0392 0.6866 1.4776 -0.1063 0.0069 0.1082 428 GLN B CD 10508 O OE1 . GLN B 428 ? 2.0018 0.6159 1.4170 -0.0737 0.0059 0.1110 428 GLN B OE1 10509 N NE2 . GLN B 428 ? 1.9786 0.5817 1.3756 -0.1242 -0.0100 0.0893 428 GLN B NE2 10510 N N . VAL B 429 ? 1.4930 0.5363 1.2402 -0.2398 0.0300 0.1157 429 VAL B N 10511 C CA . VAL B 429 ? 1.5664 0.6600 1.3545 -0.2834 0.0170 0.1052 429 VAL B CA 10512 C C . VAL B 429 ? 1.8244 0.8993 1.5721 -0.2687 -0.0002 0.0925 429 VAL B C 10513 O O . VAL B 429 ? 1.9451 1.0348 1.6872 -0.2211 0.0084 0.0986 429 VAL B O 10514 C CB . VAL B 429 ? 1.5970 0.8078 1.4952 -0.2887 0.0351 0.1144 429 VAL B CB 10515 C CG1 . VAL B 429 ? 1.5369 0.7989 1.4827 -0.3405 0.0194 0.1004 429 VAL B CG1 10516 C CG2 . VAL B 429 ? 1.8643 1.1046 1.8043 -0.2933 0.0563 0.1259 429 VAL B CG2 10517 N N . THR B 430 ? 1.9384 0.9841 1.6570 -0.3120 -0.0238 0.0737 430 THR B N 10518 C CA . THR B 430 ? 1.7889 0.8304 1.4757 -0.3065 -0.0426 0.0582 430 THR B CA 10519 C C . THR B 430 ? 1.7023 0.8081 1.4427 -0.3561 -0.0577 0.0455 430 THR B C 10520 O O . THR B 430 ? 1.7270 0.8429 1.4957 -0.4055 -0.0593 0.0396 430 THR B O 10521 C CB . THR B 430 ? 1.9275 0.8592 1.5118 -0.3062 -0.0599 0.0389 430 THR B CB 10522 O OG1 . THR B 430 ? 2.1762 1.0568 1.7391 -0.3616 -0.0713 0.0275 430 THR B OG1 10523 C CG2 . THR B 430 ? 1.9726 0.8419 1.5068 -0.2540 -0.0470 0.0473 430 THR B CG2 10524 N N . PHE B 431 ? 1.7821 0.9348 1.5363 -0.3431 -0.0693 0.0408 431 PHE B N 10525 C CA . PHE B 431 ? 1.8325 1.0528 1.6412 -0.3839 -0.0862 0.0266 431 PHE B CA 10526 C C . PHE B 431 ? 1.9025 1.0936 1.6511 -0.3960 -0.1138 0.0014 431 PHE B C 10527 O O . PHE B 431 ? 2.0599 1.2426 1.7681 -0.3567 -0.1192 0.0037 431 PHE B O 10528 C CB . PHE B 431 ? 1.7096 1.0314 1.6094 -0.3605 -0.0776 0.0447 431 PHE B CB 10529 C CG . PHE B 431 ? 1.6260 0.9862 1.5929 -0.3483 -0.0489 0.0659 431 PHE B CG 10530 C CD1 . PHE B 431 ? 1.6708 1.0276 1.6334 -0.2953 -0.0270 0.0888 431 PHE B CD1 10531 C CD2 . PHE B 431 ? 1.4806 0.8857 1.5155 -0.3917 -0.0427 0.0598 431 PHE B CD2 10532 C CE1 . PHE B 431 ? 1.5605 0.9573 1.5870 -0.2850 0.0003 0.1048 431 PHE B CE1 10533 C CE2 . PHE B 431 ? 1.3176 0.7643 1.4157 -0.3814 -0.0158 0.0760 431 PHE B CE2 10534 C CZ . PHE B 431 ? 1.3681 0.8104 1.4629 -0.3276 0.0056 0.0982 431 PHE B CZ 10535 N N . ASP B 432 ? 1.8165 0.9962 1.5590 -0.4525 -0.1302 -0.0244 432 ASP B N 10536 C CA . ASP B 432 ? 1.9076 1.0696 1.6012 -0.4707 -0.1564 -0.0536 432 ASP B CA 10537 C C . ASP B 432 ? 1.9727 1.2380 1.7369 -0.4842 -0.1729 -0.0623 432 ASP B C 10538 O O . ASP B 432 ? 1.9620 1.2800 1.7898 -0.5287 -0.1761 -0.0736 432 ASP B O 10539 C CB . ASP B 432 ? 2.1228 1.2098 1.7652 -0.5265 -0.1653 -0.0803 432 ASP B CB 10540 C CG . ASP B 432 ? 2.3150 1.2837 1.8663 -0.5070 -0.1595 -0.0791 432 ASP B CG 10541 O OD1 . ASP B 432 ? 2.2823 1.2319 1.8264 -0.4584 -0.1419 -0.0540 432 ASP B OD1 10542 O OD2 . ASP B 432 ? 2.3935 1.2885 1.8825 -0.5402 -0.1726 -0.1052 432 ASP B OD2 10543 N N . CYS B 433 ? 2.0489 1.3446 1.8011 -0.4452 -0.1841 -0.0573 433 CYS B N 10544 C CA . CYS B 433 ? 1.9833 1.3747 1.7977 -0.4484 -0.2033 -0.0616 433 CYS B CA 10545 C C . CYS B 433 ? 2.2031 1.5869 1.9542 -0.4439 -0.2301 -0.0842 433 CYS B C 10546 O O . CYS B 433 ? 2.3402 1.7527 2.0993 -0.4838 -0.2527 -0.1157 433 CYS B O 10547 C CB . CYS B 433 ? 1.8731 1.3291 1.7528 -0.4009 -0.1901 -0.0244 433 CYS B CB 10548 S SG . CYS B 433 ? 2.1184 1.6032 2.0874 -0.4069 -0.1585 -0.0026 433 CYS B SG 10549 N N . ASP B 434 ? 2.2847 1.6361 1.9745 -0.3960 -0.2266 -0.0702 434 ASP B N 10550 C CA . ASP B 434 ? 2.4777 1.8208 2.0991 -0.3880 -0.2495 -0.0919 434 ASP B CA 10551 C C . ASP B 434 ? 2.5331 1.8025 2.0895 -0.4319 -0.2595 -0.1341 434 ASP B C 10552 O O . ASP B 434 ? 2.4843 1.6684 2.0019 -0.4401 -0.2434 -0.1367 434 ASP B O 10553 C CB . ASP B 434 ? 2.5837 1.9007 2.1478 -0.3306 -0.2386 -0.0703 434 ASP B CB 10554 C CG . ASP B 434 ? 2.5314 1.9070 2.1553 -0.2889 -0.2228 -0.0257 434 ASP B CG 10555 O OD1 . ASP B 434 ? 2.5267 1.9793 2.2318 -0.2972 -0.2311 -0.0140 434 ASP B OD1 10556 O OD2 . ASP B 434 ? 2.5226 1.8673 2.1147 -0.2482 -0.2016 -0.0042 434 ASP B OD2 10557 N N . CYS B 435 ? 2.4862 1.7885 2.0319 -0.4598 -0.2864 -0.1673 435 CYS B N 10558 C CA . CYS B 435 ? 2.4918 1.7299 1.9803 -0.5066 -0.2966 -0.2114 435 CYS B CA 10559 C C . CYS B 435 ? 2.5425 1.6975 1.9336 -0.4809 -0.2946 -0.2247 435 CYS B C 10560 O O . CYS B 435 ? 2.5424 1.7109 1.9081 -0.4294 -0.2916 -0.2060 435 CYS B O 10561 C CB . CYS B 435 ? 2.4386 1.7482 1.9502 -0.5435 -0.3259 -0.2467 435 CYS B CB 10562 S SG . CYS B 435 ? 3.0618 2.4713 2.6924 -0.5793 -0.3304 -0.2427 435 CYS B SG 10563 N N . ALA B 436 ? 2.5499 1.6187 1.8878 -0.5187 -0.2955 -0.2581 436 ALA B N 10564 C CA . ALA B 436 ? 2.6249 1.6072 1.8740 -0.4989 -0.2940 -0.2780 436 ALA B CA 10565 C C . ALA B 436 ? 2.8176 1.8447 2.0285 -0.4887 -0.3164 -0.3076 436 ALA B C 10566 O O . ALA B 436 ? 2.9035 1.8794 2.0449 -0.4651 -0.3161 -0.3257 436 ALA B O 10567 C CB . ALA B 436 ? 2.6115 1.4867 1.8195 -0.5456 -0.2904 -0.3057 436 ALA B CB 10568 N N . CYS B 437 ? 2.8970 2.0236 2.1549 -0.5058 -0.3367 -0.3144 437 CYS B N 10569 C CA . CYS B 437 ? 3.0478 2.2316 2.2742 -0.4968 -0.3610 -0.3408 437 CYS B CA 10570 C C . CYS B 437 ? 3.1402 2.3943 2.3749 -0.4367 -0.3619 -0.3019 437 CYS B C 10571 O O . CYS B 437 ? 3.2619 2.5761 2.4724 -0.4223 -0.3824 -0.3141 437 CYS B O 10572 C CB . CYS B 437 ? 2.9675 2.2263 2.2380 -0.5453 -0.3857 -0.3711 437 CYS B CB 10573 S SG . CYS B 437 ? 3.0211 2.3987 2.4032 -0.5387 -0.3926 -0.3330 437 CYS B SG 10574 N N . GLN B 438 ? 3.0260 2.2735 2.2938 -0.4034 -0.3392 -0.2549 438 GLN B N 10575 C CA . GLN B 438 ? 2.9532 2.2581 2.2296 -0.3482 -0.3352 -0.2137 438 GLN B CA 10576 C C . GLN B 438 ? 2.9561 2.2371 2.1458 -0.3155 -0.3361 -0.2276 438 GLN B C 10577 O O . GLN B 438 ? 2.9841 2.3332 2.1605 -0.2865 -0.3483 -0.2143 438 GLN B O 10578 C CB . GLN B 438 ? 3.0227 2.3092 2.3427 -0.3218 -0.3057 -0.1679 438 GLN B CB 10579 C CG . GLN B 438 ? 3.0292 2.3923 2.3896 -0.2775 -0.3022 -0.1208 438 GLN B CG 10580 C CD . GLN B 438 ? 2.9609 2.4098 2.4123 -0.2942 -0.3173 -0.1060 438 GLN B CD 10581 O OE1 . GLN B 438 ? 2.9105 2.3575 2.4135 -0.3343 -0.3175 -0.1194 438 GLN B OE1 10582 N NE2 . GLN B 438 ? 2.9079 2.4332 2.3796 -0.2635 -0.3304 -0.0785 438 GLN B NE2 10583 N N . ALA B 439 ? 3.0282 2.2129 2.1594 -0.3206 -0.3235 -0.2546 439 ALA B N 10584 C CA . ALA B 439 ? 3.0777 2.2355 2.1269 -0.2963 -0.3249 -0.2804 439 ALA B CA 10585 C C . ALA B 439 ? 3.1365 2.3338 2.1555 -0.3253 -0.3544 -0.3263 439 ALA B C 10586 O O . ALA B 439 ? 3.1245 2.3171 2.1658 -0.3741 -0.3678 -0.3546 439 ALA B O 10587 C CB . ALA B 439 ? 3.1363 2.1774 2.1393 -0.2953 -0.3059 -0.3011 439 ALA B CB 10588 N N . GLN B 440 ? 3.2015 2.4418 2.1692 -0.2966 -0.3635 -0.3350 440 GLN B N 10589 C CA . GLN B 440 ? 3.2982 2.5981 2.2384 -0.3171 -0.3929 -0.3746 440 GLN B CA 10590 C C . GLN B 440 ? 3.2853 2.6732 2.2940 -0.3410 -0.4162 -0.3623 440 GLN B C 10591 O O . GLN B 440 ? 3.2828 2.6749 2.3055 -0.3880 -0.4327 -0.4018 440 GLN B O 10592 C CB . GLN B 440 ? 3.3884 2.6120 2.2816 -0.3563 -0.3968 -0.4393 440 GLN B CB 10593 C CG . GLN B 440 ? 3.4971 2.6904 2.3092 -0.3330 -0.3928 -0.4737 440 GLN B CG 10594 C CD . GLN B 440 ? 3.5411 2.8344 2.3205 -0.3260 -0.4176 -0.4936 440 GLN B CD 10595 O OE1 . GLN B 440 ? 3.5555 2.8854 2.3359 -0.3636 -0.4410 -0.5334 440 GLN B OE1 10596 N NE2 . GLN B 440 ? 3.5365 2.8779 2.2854 -0.2791 -0.4125 -0.4662 440 GLN B NE2 10597 N N . ALA B 441 ? 3.2323 2.6900 2.2852 -0.3083 -0.4168 -0.3086 441 ALA B N 10598 C CA . ALA B 441 ? 3.2223 2.7747 2.3418 -0.3193 -0.4416 -0.2932 441 ALA B CA 10599 C C . ALA B 441 ? 3.3314 2.9717 2.4137 -0.2986 -0.4694 -0.2963 441 ALA B C 10600 O O . ALA B 441 ? 3.3255 3.0543 2.4548 -0.2945 -0.4937 -0.2770 441 ALA B O 10601 C CB . ALA B 441 ? 3.0896 2.6645 2.2843 -0.2959 -0.4273 -0.2333 441 ALA B CB 10602 N N . GLU B 442 ? 3.4484 3.0630 2.4466 -0.2834 -0.4650 -0.3199 442 GLU B N 10603 C CA . GLU B 442 ? 3.4981 3.1877 2.4414 -0.2590 -0.4854 -0.3223 442 GLU B CA 10604 C C . GLU B 442 ? 3.5177 3.2439 2.4659 -0.2081 -0.4745 -0.2546 442 GLU B C 10605 O O . GLU B 442 ? 3.4411 3.1705 2.4575 -0.1973 -0.4645 -0.2074 442 GLU B O 10606 C CB . GLU B 442 ? 3.4093 3.1912 2.3756 -0.2831 -0.5252 -0.3459 442 GLU B CB 10607 C CG . GLU B 442 ? 3.4171 3.2603 2.3108 -0.2768 -0.5487 -0.3784 442 GLU B CG 10608 C CD . GLU B 442 ? 3.3780 3.2723 2.2823 -0.3194 -0.5807 -0.4349 442 GLU B CD 10609 O OE1 . GLU B 442 ? 3.2856 3.1608 2.2507 -0.3568 -0.5825 -0.4516 442 GLU B OE1 10610 O OE2 . GLU B 442 ? 3.4176 3.3753 2.2691 -0.3171 -0.6033 -0.4646 442 GLU B OE2 10611 N N . PRO B 443 ? 3.5756 3.3310 2.4515 -0.1786 -0.4752 -0.2509 443 PRO B N 10612 C CA . PRO B 443 ? 3.5405 3.3264 2.4128 -0.1332 -0.4618 -0.1868 443 PRO B CA 10613 C C . PRO B 443 ? 3.5051 3.3816 2.4286 -0.1184 -0.4871 -0.1355 443 PRO B C 10614 O O . PRO B 443 ? 3.4443 3.3252 2.4047 -0.0907 -0.4716 -0.0763 443 PRO B O 10615 C CB . PRO B 443 ? 3.5748 3.3765 2.3501 -0.1145 -0.4597 -0.2077 443 PRO B CB 10616 C CG . PRO B 443 ? 3.5816 3.3931 2.3202 -0.1486 -0.4835 -0.2781 443 PRO B CG 10617 C CD . PRO B 443 ? 3.5823 3.3245 2.3740 -0.1871 -0.4790 -0.3087 443 PRO B CD 10618 N N . ASN B 444 ? 3.5094 3.4564 2.4373 -0.1358 -0.5254 -0.1586 444 ASN B N 10619 C CA . ASN B 444 ? 3.4136 3.4518 2.3793 -0.1155 -0.5545 -0.1108 444 ASN B CA 10620 C C . ASN B 444 ? 3.3438 3.4327 2.3826 -0.1428 -0.5881 -0.1300 444 ASN B C 10621 O O . ASN B 444 ? 3.2639 3.3156 2.3319 -0.1823 -0.5859 -0.1781 444 ASN B O 10622 C CB . ASN B 444 ? 3.4477 3.5552 2.3310 -0.0929 -0.5745 -0.1044 444 ASN B CB 10623 C CG . ASN B 444 ? 3.4337 3.5208 2.2642 -0.0567 -0.5449 -0.0603 444 ASN B CG 10624 O OD1 . ASN B 444 ? 3.3349 3.3845 2.2081 -0.0386 -0.5181 -0.0125 444 ASN B OD1 10625 N ND2 . ASN B 444 ? 3.5476 3.6642 2.2860 -0.0477 -0.5484 -0.0791 444 ASN B ND2 10626 N N . SER B 445 ? 3.3501 3.5253 2.4174 -0.1208 -0.6193 -0.0908 445 SER B N 10627 C CA . SER B 445 ? 3.2875 3.5243 2.4375 -0.1367 -0.6529 -0.0981 445 SER B CA 10628 C C . SER B 445 ? 3.3114 3.5995 2.4388 -0.1702 -0.6866 -0.1662 445 SER B C 10629 O O . SER B 445 ? 3.3056 3.6484 2.5009 -0.1878 -0.7147 -0.1832 445 SER B O 10630 C CB . SER B 445 ? 3.2524 3.5622 2.4378 -0.0960 -0.6770 -0.0305 445 SER B CB 10631 O OG . SER B 445 ? 3.3165 3.6777 2.4164 -0.0703 -0.6953 -0.0141 445 SER B OG 10632 N N . HIS B 446 ? 3.3046 3.5784 2.3401 -0.1796 -0.6830 -0.2086 446 HIS B N 10633 C CA . HIS B 446 ? 3.3328 3.6654 2.3367 -0.2078 -0.7154 -0.2729 446 HIS B CA 10634 C C . HIS B 446 ? 3.2620 3.5563 2.3063 -0.2626 -0.7118 -0.3392 446 HIS B C 10635 O O . HIS B 446 ? 3.1616 3.3978 2.2700 -0.2779 -0.6902 -0.3296 446 HIS B O 10636 C CB . HIS B 446 ? 3.4372 3.7668 2.3313 -0.2014 -0.7100 -0.3005 446 HIS B CB 10637 C CG . HIS B 446 ? 3.4419 3.8747 2.2884 -0.1701 -0.7432 -0.2749 446 HIS B CG 10638 N ND1 . HIS B 446 ? 3.4367 3.9556 2.2558 -0.1860 -0.7810 -0.3230 446 HIS B ND1 10639 C CD2 . HIS B 446 ? 3.4358 3.9007 2.2552 -0.1250 -0.7444 -0.2052 446 HIS B CD2 10640 C CE1 . HIS B 446 ? 3.4502 4.0515 2.2257 -0.1505 -0.8057 -0.2826 446 HIS B CE1 10641 N NE2 . HIS B 446 ? 3.4665 4.0345 2.2401 -0.1140 -0.7839 -0.2095 446 HIS B NE2 10642 N N . ARG B 447 ? 3.2971 3.6322 2.3045 -0.2926 -0.7344 -0.4053 447 ARG B N 10643 C CA . ARG B 447 ? 3.2365 3.5381 2.2627 -0.3505 -0.7319 -0.4785 447 ARG B CA 10644 C C . ARG B 447 ? 3.1531 3.5258 2.2699 -0.3752 -0.7606 -0.4931 447 ARG B C 10645 O O . ARG B 447 ? 3.1163 3.4790 2.2525 -0.4267 -0.7627 -0.5552 447 ARG B O 10646 C CB . ARG B 447 ? 3.1594 3.3302 2.1880 -0.3710 -0.6874 -0.4836 447 ARG B CB 10647 C CG . ARG B 447 ? 3.1754 3.2820 2.1664 -0.4226 -0.6764 -0.5608 447 ARG B CG 10648 C CD . ARG B 447 ? 3.1000 3.1910 2.1627 -0.4754 -0.6772 -0.5931 447 ARG B CD 10649 N NE . ARG B 447 ? 3.1076 3.1198 2.1332 -0.5266 -0.6621 -0.6605 447 ARG B NE 10650 C CZ . ARG B 447 ? 3.0013 2.9969 2.0701 -0.5832 -0.6623 -0.7030 447 ARG B CZ 10651 N NH1 . ARG B 447 ? 2.8443 2.9039 1.9977 -0.5954 -0.6772 -0.6890 447 ARG B NH1 10652 N NH2 . ARG B 447 ? 3.0961 3.0113 2.1248 -0.6287 -0.6474 -0.7608 447 ARG B NH2 10653 N N . CYS B 448 ? 3.0967 3.5424 2.2697 -0.3396 -0.7831 -0.4383 448 CYS B N 10654 C CA . CYS B 448 ? 3.0226 3.5472 2.2861 -0.3580 -0.8138 -0.4543 448 CYS B CA 10655 C C . CYS B 448 ? 3.0420 3.6913 2.2903 -0.3443 -0.8632 -0.4716 448 CYS B C 10656 O O . CYS B 448 ? 3.0425 3.7363 2.2832 -0.3831 -0.8821 -0.5411 448 CYS B O 10657 C CB . CYS B 448 ? 2.9123 3.4386 2.2654 -0.3298 -0.8088 -0.3888 448 CYS B CB 10658 S SG . CYS B 448 ? 2.9877 3.4454 2.4298 -0.3779 -0.7782 -0.4095 448 CYS B SG 10659 N N . ASN B 449 ? 3.0355 3.7412 2.2787 -0.2898 -0.8840 -0.4075 449 ASN B N 10660 C CA . ASN B 449 ? 3.1320 3.9559 2.3499 -0.2685 -0.9324 -0.4125 449 ASN B CA 10661 C C . ASN B 449 ? 3.2203 4.0470 2.3458 -0.2233 -0.9308 -0.3629 449 ASN B C 10662 O O . ASN B 449 ? 3.2975 4.1513 2.3375 -0.2295 -0.9384 -0.3994 449 ASN B O 10663 C CB . ASN B 449 ? 3.0955 4.0069 2.4114 -0.2459 -0.9705 -0.3815 449 ASN B CB 10664 C CG . ASN B 449 ? 3.2342 4.2727 2.5277 -0.2232 -1.0250 -0.3881 449 ASN B CG 10665 O OD1 . ASN B 449 ? 3.2613 4.3372 2.4837 -0.2422 -1.0370 -0.4415 449 ASN B OD1 10666 N ND2 . ASN B 449 ? 3.2627 4.3691 2.6184 -0.1815 -1.0589 -0.3345 449 ASN B ND2 10667 N N . ASN B 450 ? 3.1892 3.9902 2.3337 -0.1799 -0.9196 -0.2812 450 ASN B N 10668 C CA . ASN B 450 ? 3.2878 4.0785 2.3473 -0.1397 -0.9096 -0.2276 450 ASN B CA 10669 C C . ASN B 450 ? 3.3028 3.9861 2.3660 -0.1258 -0.8600 -0.1787 450 ASN B C 10670 O O . ASN B 450 ? 3.3834 3.9985 2.3764 -0.1330 -0.8257 -0.1938 450 ASN B O 10671 C CB . ASN B 450 ? 3.2685 4.1552 2.3332 -0.0925 -0.9527 -0.1661 450 ASN B CB 10672 C CG . ASN B 450 ? 3.2552 4.1278 2.2371 -0.0522 -0.9391 -0.1005 450 ASN B CG 10673 O OD1 . ASN B 450 ? 3.2917 4.1925 2.1759 -0.0519 -0.9427 -0.1207 450 ASN B OD1 10674 N ND2 . ASN B 450 ? 3.2118 4.0434 2.2332 -0.0202 -0.9221 -0.0240 450 ASN B ND2 10675 N N . GLY B 451 ? 3.2647 3.9359 2.4138 -0.1057 -0.8566 -0.1236 451 GLY B N 10676 C CA . GLY B 451 ? 3.2728 3.8560 2.4315 -0.0878 -0.8124 -0.0712 451 GLY B CA 10677 C C . GLY B 451 ? 3.2776 3.8609 2.5457 -0.0696 -0.8133 -0.0192 451 GLY B C 10678 O O . GLY B 451 ? 3.2347 3.8670 2.5858 -0.0832 -0.8404 -0.0403 451 GLY B O 10679 N N . ASN B 452 ? 3.3424 3.8714 2.6129 -0.0409 -0.7816 0.0439 452 ASN B N 10680 C CA . ASN B 452 ? 3.3040 3.8241 2.6751 -0.0201 -0.7755 0.0988 452 ASN B CA 10681 C C . ASN B 452 ? 3.2901 3.7589 2.7476 -0.0546 -0.7502 0.0650 452 ASN B C 10682 O O . ASN B 452 ? 3.2592 3.7143 2.8046 -0.0428 -0.7384 0.1018 452 ASN B O 10683 C CB . ASN B 452 ? 3.2623 3.8763 2.6893 0.0055 -0.8269 0.1278 452 ASN B CB 10684 C CG . ASN B 452 ? 3.2995 3.9704 2.6391 0.0391 -0.8560 0.1646 452 ASN B CG 10685 O OD1 . ASN B 452 ? 3.3357 3.9904 2.5699 0.0357 -0.8421 0.1521 452 ASN B OD1 10686 N ND2 . ASN B 452 ? 3.2898 4.0295 2.6733 0.0718 -0.8974 0.2097 452 ASN B ND2 10687 N N . GLY B 453 ? 3.3092 3.7502 2.7408 -0.0985 -0.7414 -0.0052 453 GLY B N 10688 C CA . GLY B 453 ? 3.2418 3.6305 2.7395 -0.1369 -0.7163 -0.0401 453 GLY B CA 10689 C C . GLY B 453 ? 3.2508 3.5355 2.7008 -0.1462 -0.6664 -0.0422 453 GLY B C 10690 O O . GLY B 453 ? 3.2635 3.5138 2.6706 -0.1135 -0.6435 0.0045 453 GLY B O 10691 N N . THR B 454 ? 3.2391 3.4741 2.6994 -0.1915 -0.6497 -0.0961 454 THR B N 10692 C CA . THR B 454 ? 3.2124 3.3465 2.6222 -0.2038 -0.6072 -0.1081 454 THR B CA 10693 C C . THR B 454 ? 3.1880 3.2904 2.5702 -0.2559 -0.6085 -0.1822 454 THR B C 10694 O O . THR B 454 ? 3.1668 3.3309 2.5533 -0.2784 -0.6415 -0.2230 454 THR B O 10695 C CB . THR B 454 ? 3.1289 3.2103 2.6086 -0.1999 -0.5720 -0.0736 454 THR B CB 10696 O OG1 . THR B 454 ? 3.1389 3.1244 2.5662 -0.2104 -0.5342 -0.0879 454 THR B OG1 10697 C CG2 . THR B 454 ? 3.0437 3.1512 2.6244 -0.2351 -0.5809 -0.0971 454 THR B CG2 10698 N N . PHE B 455 ? 3.1718 3.1782 2.5214 -0.2743 -0.5736 -0.2002 455 PHE B N 10699 C CA . PHE B 455 ? 3.1729 3.1362 2.5112 -0.3284 -0.5712 -0.2650 455 PHE B CA 10700 C C . PHE B 455 ? 3.2080 3.0805 2.5759 -0.3500 -0.5346 -0.2626 455 PHE B C 10701 O O . PHE B 455 ? 3.2967 3.0954 2.6216 -0.3294 -0.5048 -0.2429 455 PHE B O 10702 C CB . PHE B 455 ? 3.1624 3.0971 2.3976 -0.3348 -0.5739 -0.3082 455 PHE B CB 10703 C CG . PHE B 455 ? 3.1163 3.0069 2.3354 -0.3917 -0.5739 -0.3772 455 PHE B CG 10704 C CD1 . PHE B 455 ? 3.0797 3.0401 2.3169 -0.4260 -0.6059 -0.4242 455 PHE B CD1 10705 C CD2 . PHE B 455 ? 3.0920 2.8708 2.2772 -0.4110 -0.5422 -0.3951 455 PHE B CD2 10706 C CE1 . PHE B 455 ? 3.0681 2.9864 2.2902 -0.4821 -0.6039 -0.4883 455 PHE B CE1 10707 C CE2 . PHE B 455 ? 3.1092 2.8400 2.2777 -0.4650 -0.5418 -0.4555 455 PHE B CE2 10708 C CZ . PHE B 455 ? 3.0883 2.8882 2.2748 -0.5024 -0.5714 -0.5024 455 PHE B CZ 10709 N N . GLU B 456 ? 3.1276 3.0083 2.5674 -0.3911 -0.5366 -0.2831 456 GLU B N 10710 C CA . GLU B 456 ? 2.9858 2.7758 2.4354 -0.4211 -0.5043 -0.2915 456 GLU B CA 10711 C C . GLU B 456 ? 2.8286 2.6007 2.2872 -0.4867 -0.5103 -0.3509 456 GLU B C 10712 O O . GLU B 456 ? 2.7667 2.5914 2.3024 -0.5174 -0.5207 -0.3625 456 GLU B O 10713 C CB . GLU B 456 ? 2.8379 2.6393 2.3746 -0.4061 -0.4866 -0.2437 456 GLU B CB 10714 C CG . GLU B 456 ? 2.8197 2.5306 2.3622 -0.4265 -0.4510 -0.2406 456 GLU B CG 10715 C CD . GLU B 456 ? 2.8318 2.4709 2.3169 -0.3850 -0.4227 -0.2079 456 GLU B CD 10716 O OE1 . GLU B 456 ? 2.8517 2.5161 2.2981 -0.3413 -0.4286 -0.1846 456 GLU B OE1 10717 O OE2 . GLU B 456 ? 2.8156 2.3760 2.2939 -0.3964 -0.3950 -0.2057 456 GLU B OE2 10718 N N . CYS B 457 ? 2.7393 2.4363 2.1185 -0.5082 -0.5028 -0.3896 457 CYS B N 10719 C CA . CYS B 457 ? 2.7175 2.3432 2.0828 -0.5681 -0.4924 -0.4358 457 CYS B CA 10720 C C . CYS B 457 ? 2.6936 2.3761 2.1053 -0.6269 -0.5131 -0.4838 457 CYS B C 10721 O O . CYS B 457 ? 2.6940 2.3286 2.0658 -0.6749 -0.5128 -0.5345 457 CYS B O 10722 C CB . CYS B 457 ? 2.6690 2.2173 2.0612 -0.5736 -0.4593 -0.4051 457 CYS B CB 10723 S SG . CYS B 457 ? 3.2245 2.6939 2.5649 -0.5125 -0.4297 -0.3566 457 CYS B SG 10724 N N . GLY B 458 ? 2.6333 2.4163 2.1299 -0.6249 -0.5307 -0.4711 458 GLY B N 10725 C CA . GLY B 458 ? 2.5984 2.4539 2.1390 -0.6754 -0.5544 -0.5214 458 GLY B CA 10726 C C . GLY B 458 ? 2.4506 2.4328 2.0261 -0.6529 -0.5932 -0.5277 458 GLY B C 10727 O O . GLY B 458 ? 2.3028 2.3473 1.8953 -0.6915 -0.6167 -0.5795 458 GLY B O 10728 N N . VAL B 459 ? 2.5385 2.5592 2.1244 -0.5900 -0.6001 -0.4740 459 VAL B N 10729 C CA . VAL B 459 ? 2.6185 2.7609 2.2650 -0.5630 -0.6355 -0.4625 459 VAL B CA 10730 C C . VAL B 459 ? 2.7377 2.9126 2.3275 -0.5054 -0.6538 -0.4323 459 VAL B C 10731 O O . VAL B 459 ? 2.8366 3.0864 2.4074 -0.5037 -0.6876 -0.4601 459 VAL B O 10732 C CB . VAL B 459 ? 2.5248 2.7031 2.2753 -0.5449 -0.6290 -0.4182 459 VAL B CB 10733 C CG1 . VAL B 459 ? 2.4995 2.8031 2.3220 -0.5240 -0.6693 -0.4160 459 VAL B CG1 10734 C CG2 . VAL B 459 ? 2.3944 2.5373 2.1973 -0.6008 -0.6056 -0.4422 459 VAL B CG2 10735 N N . CYS B 460 ? 2.7285 2.8502 2.2940 -0.4603 -0.6303 -0.3751 460 CYS B N 10736 C CA . CYS B 460 ? 2.8399 2.9874 2.3624 -0.4002 -0.6396 -0.3280 460 CYS B CA 10737 C C . CYS B 460 ? 2.8557 3.0809 2.4623 -0.3621 -0.6569 -0.2765 460 CYS B C 10738 O O . CYS B 460 ? 2.8662 3.1084 2.4504 -0.3114 -0.6610 -0.2251 460 CYS B O 10739 C CB . CYS B 460 ? 2.9884 3.1809 2.4344 -0.3975 -0.6685 -0.3624 460 CYS B CB 10740 S SG . CYS B 460 ? 3.1789 3.5178 2.6729 -0.3749 -0.7228 -0.3573 460 CYS B SG 10741 N N . ARG B 461 ? 2.8295 3.0990 2.5341 -0.3878 -0.6656 -0.2908 461 ARG B N 10742 C CA . ARG B 461 ? 2.7290 3.0709 2.5282 -0.3551 -0.6825 -0.2487 461 ARG B CA 10743 C C . ARG B 461 ? 2.8107 3.2324 2.5863 -0.3117 -0.7227 -0.2268 461 ARG B C 10744 O O . ARG B 461 ? 2.9230 3.3880 2.6512 -0.3258 -0.7504 -0.2688 461 ARG B O 10745 C CB . ARG B 461 ? 2.6374 2.9234 2.4662 -0.3244 -0.6471 -0.1883 461 ARG B CB 10746 C CG . ARG B 461 ? 2.6432 2.8286 2.4499 -0.3558 -0.6031 -0.2006 461 ARG B CG 10747 C CD . ARG B 461 ? 2.5655 2.7103 2.4132 -0.3262 -0.5697 -0.1447 461 ARG B CD 10748 N NE . ARG B 461 ? 2.5124 2.6884 2.4736 -0.3473 -0.5639 -0.1475 461 ARG B NE 10749 C CZ . ARG B 461 ? 2.5046 2.6547 2.5208 -0.3326 -0.5342 -0.1102 461 ARG B CZ 10750 N NH1 . ARG B 461 ? 2.5072 2.5986 2.4753 -0.2966 -0.5073 -0.0662 461 ARG B NH1 10751 N NH2 . ARG B 461 ? 2.4864 2.6744 2.6075 -0.3553 -0.5306 -0.1201 461 ARG B NH2 10752 N N . CYS B 462 ? 2.7593 3.1982 2.5656 -0.2601 -0.7247 -0.1605 462 CYS B N 10753 C CA . CYS B 462 ? 2.8268 3.3284 2.6014 -0.2125 -0.7588 -0.1235 462 CYS B CA 10754 C C . CYS B 462 ? 2.8071 3.3049 2.6296 -0.1626 -0.7503 -0.0462 462 CYS B C 10755 O O . CYS B 462 ? 2.6780 3.1337 2.5652 -0.1665 -0.7195 -0.0278 462 CYS B O 10756 C CB . CYS B 462 ? 2.8100 3.4194 2.6272 -0.2197 -0.8102 -0.1588 462 CYS B CB 10757 S SG . CYS B 462 ? 2.8530 3.5064 2.5574 -0.2283 -0.8417 -0.2046 462 CYS B SG 10758 N N . GLY B 463 ? 2.8771 2.3316 2.8407 -0.4050 -0.5709 0.4063 463 GLY B N 10759 C CA . GLY B 463 ? 2.9537 2.3266 2.8777 -0.4096 -0.5605 0.4408 463 GLY B CA 10760 C C . GLY B 463 ? 2.8920 2.2152 2.7903 -0.3827 -0.5797 0.4493 463 GLY B C 10761 O O . GLY B 463 ? 2.8388 2.1890 2.7639 -0.3671 -0.6014 0.4267 463 GLY B O 10762 N N . PRO B 464 ? 2.8885 2.1352 2.7340 -0.3772 -0.5688 0.4821 464 PRO B N 10763 C CA . PRO B 464 ? 2.9754 2.1589 2.7873 -0.3538 -0.5808 0.4974 464 PRO B CA 10764 C C . PRO B 464 ? 3.0046 2.1956 2.7607 -0.3025 -0.6072 0.4944 464 PRO B C 10765 O O . PRO B 464 ? 3.1268 2.2752 2.8089 -0.2771 -0.6011 0.5186 464 PRO B O 10766 C CB . PRO B 464 ? 2.9950 2.0963 2.7672 -0.3687 -0.5497 0.5333 464 PRO B CB 10767 C CG . PRO B 464 ? 2.9094 2.0358 2.7147 -0.4080 -0.5228 0.5319 464 PRO B CG 10768 C CD . PRO B 464 ? 2.8304 2.0417 2.6499 -0.3992 -0.5369 0.5074 464 PRO B CD 10769 N N . GLY B 465 ? 2.9074 2.1500 2.6972 -0.2851 -0.6349 0.4639 465 GLY B N 10770 C CA . GLY B 465 ? 2.9886 2.2519 2.7363 -0.2359 -0.6626 0.4523 465 GLY B CA 10771 C C . GLY B 465 ? 3.0283 2.3818 2.8003 -0.2245 -0.6745 0.4170 465 GLY B C 10772 O O . GLY B 465 ? 3.0274 2.4024 2.7580 -0.1819 -0.6953 0.4062 465 GLY B O 10773 N N . TRP B 466 ? 3.0580 2.4645 2.8963 -0.2606 -0.6608 0.3973 466 TRP B N 10774 C CA . TRP B 466 ? 3.0558 2.5511 2.9336 -0.2531 -0.6702 0.3572 466 TRP B CA 10775 C C . TRP B 466 ? 2.9316 2.4670 2.8883 -0.2698 -0.6725 0.3251 466 TRP B C 10776 O O . TRP B 466 ? 2.9146 2.4858 2.8912 -0.2443 -0.6927 0.2950 466 TRP B O 10777 C CB . TRP B 466 ? 3.0732 2.6014 2.9542 -0.2756 -0.6487 0.3591 466 TRP B CB 10778 C CG . TRP B 466 ? 3.1194 2.6854 2.9570 -0.2392 -0.6622 0.3477 466 TRP B CG 10779 C CD1 . TRP B 466 ? 3.0724 2.6816 2.9047 -0.1965 -0.6917 0.3164 466 TRP B CD1 10780 C CD2 . TRP B 466 ? 3.1439 2.7081 2.9363 -0.2391 -0.6479 0.3649 466 TRP B CD2 10781 N NE1 . TRP B 466 ? 3.0568 2.6943 2.8434 -0.1677 -0.6990 0.3111 466 TRP B NE1 10782 C CE2 . TRP B 466 ? 3.1163 2.7248 2.8749 -0.1928 -0.6717 0.3423 466 TRP B CE2 10783 C CE3 . TRP B 466 ? 3.1437 2.6746 2.9225 -0.2727 -0.6171 0.3948 466 TRP B CE3 10784 C CZ2 . TRP B 466 ? 3.1547 2.7725 2.8613 -0.1770 -0.6664 0.3507 466 TRP B CZ2 10785 C CZ3 . TRP B 466 ? 3.1769 2.7149 2.9057 -0.2598 -0.6091 0.4048 466 TRP B CZ3 10786 C CH2 . TRP B 466 ? 3.1901 2.7701 2.8808 -0.2114 -0.6339 0.3838 466 TRP B CH2 10787 N N . LEU B 467 ? 2.8497 2.3778 2.8494 -0.3101 -0.6504 0.3301 467 LEU B N 10788 C CA . LEU B 467 ? 2.7891 2.3326 2.8511 -0.3247 -0.6480 0.3082 467 LEU B CA 10789 C C . LEU B 467 ? 2.7414 2.3515 2.8474 -0.3078 -0.6573 0.2645 467 LEU B C 10790 O O . LEU B 467 ? 2.8326 2.4368 2.9464 -0.2859 -0.6746 0.2511 467 LEU B O 10791 C CB . LEU B 467 ? 2.8227 2.3006 2.8732 -0.3198 -0.6580 0.3263 467 LEU B CB 10792 C CG . LEU B 467 ? 2.9001 2.3376 2.9002 -0.2832 -0.6823 0.3384 467 LEU B CG 10793 C CD1 . LEU B 467 ? 2.8933 2.3342 2.9244 -0.2677 -0.6992 0.3173 467 LEU B CD1 10794 C CD2 . LEU B 467 ? 2.9637 2.3210 2.9170 -0.2905 -0.6749 0.3794 467 LEU B CD2 10795 N N . GLY B 468 ? 2.5525 2.2253 2.6907 -0.3189 -0.6437 0.2406 468 GLY B N 10796 C CA . GLY B 468 ? 2.4546 2.1930 2.6426 -0.3062 -0.6464 0.1948 468 GLY B CA 10797 C C . GLY B 468 ? 2.3951 2.1840 2.6361 -0.3345 -0.6178 0.1727 468 GLY B C 10798 O O . GLY B 468 ? 2.4176 2.1914 2.6540 -0.3630 -0.5988 0.1940 468 GLY B O 10799 N N . SER B 469 ? 2.3352 2.1820 2.6289 -0.3270 -0.6128 0.1286 469 SER B N 10800 C CA . SER B 469 ? 2.2312 2.1294 2.5767 -0.3505 -0.5829 0.1028 469 SER B CA 10801 C C . SER B 469 ? 2.2139 2.1320 2.5337 -0.3634 -0.5775 0.1178 469 SER B C 10802 O O . SER B 469 ? 2.0999 2.0011 2.4184 -0.3926 -0.5566 0.1387 469 SER B O 10803 C CB . SER B 469 ? 2.1081 2.0715 2.5097 -0.3349 -0.5806 0.0491 469 SER B CB 10804 O OG . SER B 469 ? 2.0619 2.0048 2.4831 -0.3196 -0.5873 0.0354 469 SER B OG 10805 N N . GLN B 470 ? 2.3609 2.3156 2.6593 -0.3388 -0.5972 0.1051 470 GLN B N 10806 C CA . GLN B 470 ? 2.4761 2.4229 2.7205 -0.3392 -0.6017 0.1328 470 GLN B CA 10807 C C . GLN B 470 ? 2.6059 2.4968 2.7816 -0.3093 -0.6298 0.1621 470 GLN B C 10808 O O . GLN B 470 ? 2.6687 2.5374 2.8470 -0.2912 -0.6455 0.1568 470 GLN B O 10809 C CB . GLN B 470 ? 2.4855 2.5082 2.7450 -0.3285 -0.6033 0.0996 470 GLN B CB 10810 C CG . GLN B 470 ? 2.4161 2.4653 2.6972 -0.3634 -0.5738 0.1022 470 GLN B CG 10811 C CD . GLN B 470 ? 2.2892 2.4055 2.6498 -0.3772 -0.5518 0.0542 470 GLN B CD 10812 O OE1 . GLN B 470 ? 2.2652 2.4296 2.6639 -0.3555 -0.5616 0.0103 470 GLN B OE1 10813 N NE2 . GLN B 470 ? 2.1422 2.2611 2.5295 -0.4129 -0.5198 0.0605 470 GLN B NE2 10814 N N . CYS B 471 ? 2.6769 2.5410 2.7892 -0.3029 -0.6336 0.1934 471 CYS B N 10815 C CA . CYS B 471 ? 2.7979 2.5974 2.8374 -0.2746 -0.6537 0.2258 471 CYS B CA 10816 C C . CYS B 471 ? 2.7426 2.5704 2.7660 -0.2250 -0.6866 0.1976 471 CYS B C 10817 O O . CYS B 471 ? 2.6897 2.5801 2.7168 -0.2031 -0.6973 0.1666 471 CYS B O 10818 C CB . CYS B 471 ? 2.9131 2.6761 2.8865 -0.2771 -0.6441 0.2638 471 CYS B CB 10819 S SG . CYS B 471 ? 3.5694 3.2880 3.5575 -0.3330 -0.6078 0.2989 471 CYS B SG 10820 N N . GLU B 472 ? 2.7994 2.5821 2.8051 -0.2059 -0.7037 0.2066 472 GLU B N 10821 C CA . GLU B 472 ? 2.8538 2.6638 2.8527 -0.1592 -0.7361 0.1759 472 GLU B CA 10822 C C . GLU B 472 ? 2.9796 2.7238 2.9504 -0.1430 -0.7515 0.1965 472 GLU B C 10823 O O . GLU B 472 ? 2.9998 2.6879 2.9761 -0.1720 -0.7360 0.2256 472 GLU B O 10824 C CB . GLU B 472 ? 2.7301 2.6248 2.8175 -0.1630 -0.7355 0.1170 472 GLU B CB 10825 C CG . GLU B 472 ? 2.7588 2.7209 2.8487 -0.1170 -0.7646 0.0704 472 GLU B CG 10826 C CD . GLU B 472 ? 2.8162 2.8299 2.8925 -0.1105 -0.7630 0.0578 472 GLU B CD 10827 O OE1 . GLU B 472 ? 2.7567 2.8520 2.9024 -0.1167 -0.7570 0.0078 472 GLU B OE1 10828 O OE2 . GLU B 472 ? 2.9269 2.8978 2.9235 -0.0987 -0.7655 0.0970 472 GLU B OE2 10829 N N . CYS B 473 ? 3.0554 2.8100 2.9975 -0.0946 -0.7832 0.1783 473 CYS B N 10830 C CA . CYS B 473 ? 3.1205 2.8192 3.0337 -0.0719 -0.8020 0.1928 473 CYS B CA 10831 C C . CYS B 473 ? 3.1992 2.7987 3.0435 -0.0813 -0.7906 0.2528 473 CYS B C 10832 O O . CYS B 473 ? 3.2214 2.7920 3.0066 -0.0785 -0.7805 0.2820 473 CYS B O 10833 C CB . CYS B 473 ? 3.0424 2.7566 3.0343 -0.0932 -0.7971 0.1681 473 CYS B CB 10834 S SG . CYS B 473 ? 3.2251 2.8811 3.1919 -0.0648 -0.8220 0.1786 473 CYS B SG 10835 N N . SER B 474 ? 3.2388 2.7858 3.0930 -0.0925 -0.7900 0.2692 474 SER B N 10836 C CA . SER B 474 ? 3.2404 2.6988 3.0543 -0.1141 -0.7719 0.3198 474 SER B CA 10837 C C . SER B 474 ? 3.2550 2.6490 2.9699 -0.0822 -0.7752 0.3571 474 SER B C 10838 O O . SER B 474 ? 3.2836 2.6669 2.9639 -0.0907 -0.7568 0.3769 474 SER B O 10839 C CB . SER B 474 ? 3.1634 2.6260 3.0153 -0.1657 -0.7393 0.3310 474 SER B CB 10840 O OG . SER B 474 ? 3.1276 2.5152 2.9689 -0.1917 -0.7227 0.3672 474 SER B OG 10841 N N . GLU B 475 ? 3.2276 2.5795 2.8964 -0.0436 -0.7972 0.3650 475 GLU B N 10842 C CA . GLU B 475 ? 3.2581 2.5436 2.8231 -0.0006 -0.8032 0.3975 475 GLU B CA 10843 C C . GLU B 475 ? 3.2821 2.6208 2.8086 0.0570 -0.8341 0.3676 475 GLU B C 10844 O O . GLU B 475 ? 3.3371 2.6283 2.7717 0.1048 -0.8447 0.3878 475 GLU B O 10845 C CB . GLU B 475 ? 3.2523 2.4771 2.7680 -0.0227 -0.7680 0.4412 475 GLU B CB 10846 C CG . GLU B 475 ? 3.4165 2.5518 2.8212 0.0169 -0.7627 0.4820 475 GLU B CG 10847 C CD . GLU B 475 ? 3.4523 2.5606 2.8038 0.0112 -0.7332 0.5091 475 GLU B CD 10848 O OE1 . GLU B 475 ? 3.3473 2.5067 2.7529 -0.0277 -0.7177 0.4972 475 GLU B OE1 10849 O OE2 . GLU B 475 ? 3.5196 2.5529 2.7725 0.0471 -0.7236 0.5427 475 GLU B OE2 10850 N N . GLU B 476 ? 3.2424 2.6790 2.8393 0.0552 -0.8484 0.3168 476 GLU B N 10851 C CA . GLU B 476 ? 3.2727 2.7693 2.8522 0.1118 -0.8842 0.2761 476 GLU B CA 10852 C C . GLU B 476 ? 3.2204 2.7009 2.7983 0.1430 -0.9121 0.2640 476 GLU B C 10853 O O . GLU B 476 ? 3.1630 2.5885 2.7555 0.1184 -0.9024 0.2874 476 GLU B O 10854 C CB . GLU B 476 ? 3.1831 2.7906 2.8507 0.0979 -0.8882 0.2196 476 GLU B CB 10855 C CG . GLU B 476 ? 3.2028 2.8402 2.8695 0.0769 -0.8669 0.2233 476 GLU B CG 10856 C CD . GLU B 476 ? 3.2052 2.9531 2.9600 0.0674 -0.8713 0.1633 476 GLU B CD 10857 O OE1 . GLU B 476 ? 3.1715 2.9666 2.9980 0.0669 -0.8833 0.1214 476 GLU B OE1 10858 O OE2 . GLU B 476 ? 3.2557 3.0418 3.0094 0.0601 -0.8606 0.1569 476 GLU B OE2 10859 N N . ASP B 477 ? 3.2162 2.7471 2.7787 0.1984 -0.9481 0.2248 477 ASP B N 10860 C CA . ASP B 477 ? 3.1830 2.7180 2.7628 0.2258 -0.9763 0.2016 477 ASP B CA 10861 C C . ASP B 477 ? 3.1171 2.7466 2.8155 0.2020 -0.9802 0.1422 477 ASP B C 10862 O O . ASP B 477 ? 3.0678 2.7848 2.8025 0.2204 -0.9942 0.0917 477 ASP B O 10863 C CB . ASP B 477 ? 3.2110 2.7462 2.7087 0.3029 -1.0142 0.1888 477 ASP B CB 10864 C CG . ASP B 477 ? 3.3169 2.7375 2.6968 0.3304 -1.0090 0.2499 477 ASP B CG 10865 O OD1 . ASP B 477 ? 3.3923 2.7370 2.7718 0.2918 -0.9837 0.2928 477 ASP B OD1 10866 O OD2 . ASP B 477 ? 3.3315 2.7363 2.6186 0.3927 -1.0290 0.2533 477 ASP B OD2 10867 N N . TYR B 478 ? 3.0610 2.6710 2.8196 0.1623 -0.9657 0.1468 478 TYR B N 10868 C CA . TYR B 478 ? 2.9384 2.6236 2.8079 0.1319 -0.9569 0.0978 478 TYR B CA 10869 C C . TYR B 478 ? 2.9546 2.6843 2.8649 0.1656 -0.9860 0.0481 478 TYR B C 10870 O O . TYR B 478 ? 2.9893 2.6699 2.8823 0.1775 -0.9979 0.0626 478 TYR B O 10871 C CB . TYR B 478 ? 2.8806 2.5246 2.7954 0.0731 -0.9231 0.1250 478 TYR B CB 10872 C CG . TYR B 478 ? 3.0271 2.5919 2.9176 0.0720 -0.9269 0.1580 478 TYR B CG 10873 C CD1 . TYR B 478 ? 3.0201 2.5963 2.9724 0.0651 -0.9300 0.1331 478 TYR B CD1 10874 C CD2 . TYR B 478 ? 3.1296 2.6063 2.9372 0.0774 -0.9243 0.2134 478 TYR B CD2 10875 C CE1 . TYR B 478 ? 3.0543 2.5599 2.9852 0.0648 -0.9345 0.1621 478 TYR B CE1 10876 C CE2 . TYR B 478 ? 3.1447 2.5505 2.9344 0.0756 -0.9268 0.2411 478 TYR B CE2 10877 C CZ . TYR B 478 ? 3.0828 2.5052 2.9339 0.0698 -0.9338 0.2152 478 TYR B CZ 10878 O OH . TYR B 478 ? 3.0467 2.4002 2.8806 0.0689 -0.9375 0.2417 478 TYR B OH 10879 N N . ARG B 479 ? 2.8993 2.7246 2.8667 0.1812 -0.9970 -0.0134 479 ARG B N 10880 C CA . ARG B 479 ? 2.8650 2.7488 2.8996 0.2026 -1.0167 -0.0728 479 ARG B CA 10881 C C . ARG B 479 ? 2.8272 2.7056 2.9469 0.1525 -0.9857 -0.0789 479 ARG B C 10882 O O . ARG B 479 ? 2.7035 2.5499 2.8338 0.1053 -0.9520 -0.0460 479 ARG B O 10883 C CB . ARG B 479 ? 2.7532 2.7450 2.8383 0.2265 -1.0309 -0.1417 479 ARG B CB 10884 C CG . ARG B 479 ? 2.7568 2.7604 2.7559 0.2821 -1.0630 -0.1410 479 ARG B CG 10885 C CD . ARG B 479 ? 2.6923 2.8110 2.7543 0.3037 -1.0772 -0.2166 479 ARG B CD 10886 N NE . ARG B 479 ? 2.7326 2.8661 2.7091 0.3639 -1.1110 -0.2205 479 ARG B NE 10887 C CZ . ARG B 479 ? 2.6921 2.9230 2.7033 0.3953 -1.1314 -0.2847 479 ARG B CZ 10888 N NH1 . ARG B 479 ? 2.5859 2.9081 2.7218 0.3684 -1.1183 -0.3512 479 ARG B NH1 10889 N NH2 . ARG B 479 ? 2.7620 2.9974 2.6826 0.4555 -1.1632 -0.2838 479 ARG B NH2 10890 N N . PRO B 480 ? 2.8561 2.7637 3.0350 0.1644 -0.9960 -0.1216 480 PRO B N 10891 C CA . PRO B 480 ? 2.7841 2.6882 3.0436 0.1185 -0.9610 -0.1304 480 PRO B CA 10892 C C . PRO B 480 ? 2.8276 2.7994 3.1644 0.0850 -0.9281 -0.1667 480 PRO B C 10893 O O . PRO B 480 ? 2.8174 2.8577 3.2396 0.0856 -0.9206 -0.2285 480 PRO B O 10894 C CB . PRO B 480 ? 2.7216 2.6495 3.0273 0.1443 -0.9795 -0.1751 480 PRO B CB 10895 C CG . PRO B 480 ? 2.7433 2.7243 3.0219 0.2008 -1.0221 -0.2119 480 PRO B CG 10896 C CD . PRO B 480 ? 2.8361 2.7694 3.0067 0.2184 -1.0364 -0.1582 480 PRO B CD 10897 N N . SER B 481 ? 2.8401 2.7913 3.1477 0.0561 -0.9072 -0.1292 481 SER B N 10898 C CA . SER B 481 ? 2.7541 2.7620 3.1233 0.0235 -0.8749 -0.1557 481 SER B CA 10899 C C . SER B 481 ? 2.6317 2.6493 3.0890 -0.0100 -0.8381 -0.1822 481 SER B C 10900 O O . SER B 481 ? 2.5209 2.6094 3.0583 -0.0181 -0.8192 -0.2380 481 SER B O 10901 C CB . SER B 481 ? 2.6489 2.6157 2.9659 -0.0052 -0.8568 -0.1015 481 SER B CB 10902 O OG . SER B 481 ? 2.5721 2.5892 2.9484 -0.0385 -0.8237 -0.1245 481 SER B OG 10903 N N . GLN B 482 ? 2.5507 2.4943 2.9911 -0.0268 -0.8269 -0.1434 482 GLN B N 10904 C CA . GLN B 482 ? 2.4882 2.4236 2.9962 -0.0524 -0.7921 -0.1613 482 GLN B CA 10905 C C . GLN B 482 ? 2.4578 2.3047 2.9260 -0.0606 -0.7914 -0.1122 482 GLN B C 10906 O O . GLN B 482 ? 2.3782 2.1690 2.7730 -0.0574 -0.8094 -0.0610 482 GLN B O 10907 C CB . GLN B 482 ? 2.4563 2.4164 3.0115 -0.0915 -0.7471 -0.1702 482 GLN B CB 10908 C CG . GLN B 482 ? 2.4614 2.4929 3.1137 -0.0962 -0.7200 -0.2389 482 GLN B CG 10909 C CD . GLN B 482 ? 2.4232 2.4741 3.1165 -0.1334 -0.6730 -0.2456 482 GLN B CD 10910 O OE1 . GLN B 482 ? 2.4387 2.4398 3.0942 -0.1581 -0.6561 -0.1982 482 GLN B OE1 10911 N NE2 . GLN B 482 ? 2.2645 2.3891 3.0381 -0.1369 -0.6508 -0.3073 482 GLN B NE2 10912 N N . GLN B 483 ? 2.4874 2.3215 3.0066 -0.0705 -0.7681 -0.1307 483 GLN B N 10913 C CA . GLN B 483 ? 2.3505 2.1058 2.8426 -0.0778 -0.7641 -0.0921 483 GLN B CA 10914 C C . GLN B 483 ? 2.2724 1.9937 2.7654 -0.1140 -0.7269 -0.0642 483 GLN B C 10915 O O . GLN B 483 ? 2.2588 1.9194 2.7378 -0.1222 -0.7175 -0.0377 483 GLN B O 10916 C CB . GLN B 483 ? 2.3792 2.1352 2.9216 -0.0656 -0.7574 -0.1271 483 GLN B CB 10917 C CG . GLN B 483 ? 2.4237 2.2163 3.0469 -0.0858 -0.7096 -0.1709 483 GLN B CG 10918 C CD . GLN B 483 ? 2.3974 2.2008 3.0777 -0.0714 -0.7009 -0.2148 483 GLN B CD 10919 O OE1 . GLN B 483 ? 2.4336 2.2135 3.0917 -0.0471 -0.7320 -0.2096 483 GLN B OE1 10920 N NE2 . GLN B 483 ? 2.3524 2.1897 3.1079 -0.0865 -0.6556 -0.2593 483 GLN B NE2 10921 N N . ASP B 484 ? 2.3463 2.1087 2.8552 -0.1331 -0.7074 -0.0724 484 ASP B N 10922 C CA . ASP B 484 ? 2.3701 2.1212 2.9024 -0.1650 -0.6643 -0.0659 484 ASP B CA 10923 C C . ASP B 484 ? 2.2103 1.8853 2.6943 -0.1786 -0.6623 -0.0138 484 ASP B C 10924 O O . ASP B 484 ? 2.2395 1.8880 2.6697 -0.1820 -0.6827 0.0249 484 ASP B O 10925 C CB . ASP B 484 ? 2.4653 2.2693 3.0072 -0.1811 -0.6525 -0.0747 484 ASP B CB 10926 C CG . ASP B 484 ? 2.4060 2.2156 2.9875 -0.2103 -0.6035 -0.0839 484 ASP B CG 10927 O OD1 . ASP B 484 ? 2.3514 2.2176 2.9646 -0.2217 -0.5868 -0.1088 484 ASP B OD1 10928 O OD2 . ASP B 484 ? 2.3817 2.1386 2.9603 -0.2195 -0.5817 -0.0670 484 ASP B OD2 10929 N N . GLU B 485 ? 2.1670 1.8074 2.6728 -0.1851 -0.6350 -0.0167 485 GLU B N 10930 C CA . GLU B 485 ? 2.3384 1.9121 2.8097 -0.1959 -0.6283 0.0224 485 GLU B CA 10931 C C . GLU B 485 ? 2.4257 1.9524 2.8381 -0.1884 -0.6666 0.0642 485 GLU B C 10932 O O . GLU B 485 ? 2.4167 1.9068 2.7982 -0.2034 -0.6658 0.0975 485 GLU B O 10933 C CB . GLU B 485 ? 2.3465 1.9269 2.8199 -0.2223 -0.5985 0.0322 485 GLU B CB 10934 C CG . GLU B 485 ? 2.2911 1.8518 2.7924 -0.2288 -0.5550 0.0187 485 GLU B CG 10935 C CD . GLU B 485 ? 2.2183 1.8288 2.7807 -0.2296 -0.5203 -0.0292 485 GLU B CD 10936 O OE1 . GLU B 485 ? 2.2515 1.8436 2.8411 -0.2185 -0.4980 -0.0509 485 GLU B OE1 10937 O OE2 . GLU B 485 ? 2.0697 1.7365 2.6544 -0.2415 -0.5132 -0.0465 485 GLU B OE2 10938 N N . CYS B 486 ? 2.3553 1.8826 2.7539 -0.1646 -0.6985 0.0605 486 CYS B N 10939 C CA . CYS B 486 ? 2.2934 1.7679 2.6369 -0.1551 -0.7305 0.0987 486 CYS B CA 10940 C C . CYS B 486 ? 2.3055 1.7285 2.6495 -0.1444 -0.7338 0.1039 486 CYS B C 10941 O O . CYS B 486 ? 2.5652 1.9359 2.8701 -0.1394 -0.7547 0.1350 486 CYS B O 10942 C CB . CYS B 486 ? 2.3614 1.8573 2.6776 -0.1309 -0.7641 0.0961 486 CYS B CB 10943 S SG . CYS B 486 ? 2.3756 1.8835 2.6440 -0.1392 -0.7730 0.1229 486 CYS B SG 10944 N N . SER B 487 ? 2.2225 1.6593 2.6120 -0.1405 -0.7105 0.0718 487 SER B N 10945 C CA . SER B 487 ? 2.1885 1.5762 2.5810 -0.1308 -0.7056 0.0741 487 SER B CA 10946 C C . SER B 487 ? 2.2349 1.6314 2.6703 -0.1385 -0.6611 0.0477 487 SER B C 10947 O O . SER B 487 ? 2.2467 1.6960 2.7228 -0.1447 -0.6385 0.0155 487 SER B O 10948 C CB . SER B 487 ? 2.2321 1.6175 2.6273 -0.1041 -0.7314 0.0601 487 SER B CB 10949 O OG . SER B 487 ? 2.2409 1.6852 2.6857 -0.0959 -0.7205 0.0143 487 SER B OG 10950 N N . PRO B 488 ? 2.3172 1.6604 2.7425 -0.1361 -0.6464 0.0597 488 PRO B N 10951 C CA . PRO B 488 ? 2.3095 1.6534 2.7686 -0.1384 -0.5992 0.0348 488 PRO B CA 10952 C C . PRO B 488 ? 2.3466 1.6941 2.8433 -0.1206 -0.5859 0.0009 488 PRO B C 10953 O O . PRO B 488 ? 2.3144 1.6214 2.8156 -0.1114 -0.5573 -0.0049 488 PRO B O 10954 C CB . PRO B 488 ? 2.1994 1.4816 2.6241 -0.1368 -0.5918 0.0616 488 PRO B CB 10955 C CG . PRO B 488 ? 2.1689 1.4135 2.5584 -0.1255 -0.6352 0.0880 488 PRO B CG 10956 C CD . PRO B 488 ? 2.2520 1.5336 2.6350 -0.1313 -0.6675 0.0943 488 PRO B CD 10957 N N . ARG B 489 ? 2.3385 1.7345 2.8610 -0.1142 -0.6054 -0.0230 489 ARG B N 10958 C CA . ARG B 489 ? 2.3786 1.7934 2.9480 -0.0988 -0.5951 -0.0635 489 ARG B CA 10959 C C . ARG B 489 ? 2.4367 1.9095 3.0205 -0.0891 -0.6315 -0.0838 489 ARG B C 10960 O O . ARG B 489 ? 2.4796 1.9678 3.0285 -0.0922 -0.6629 -0.0616 489 ARG B O 10961 C CB . ARG B 489 ? 2.3503 1.7035 2.9025 -0.0796 -0.6010 -0.0530 489 ARG B CB 10962 C CG . ARG B 489 ? 2.2691 1.5959 2.8534 -0.0762 -0.5480 -0.0767 489 ARG B CG 10963 C CD . ARG B 489 ? 2.2854 1.5691 2.8684 -0.0536 -0.5540 -0.0808 489 ARG B CD 10964 N NE . ARG B 489 ? 2.3273 1.5461 2.8504 -0.0438 -0.5802 -0.0376 489 ARG B NE 10965 C CZ . ARG B 489 ? 2.2906 1.4577 2.8011 -0.0241 -0.5816 -0.0333 489 ARG B CZ 10966 N NH1 . ARG B 489 ? 2.3629 1.5329 2.9156 -0.0129 -0.5563 -0.0681 489 ARG B NH1 10967 N NH2 . ARG B 489 ? 2.1365 1.2496 2.5954 -0.0156 -0.6072 0.0033 489 ARG B NH2 10968 N N . GLU B 490 ? 2.4084 1.9118 3.0423 -0.0752 -0.6260 -0.1276 490 GLU B N 10969 C CA . GLU B 490 ? 2.3624 1.9250 3.0130 -0.0594 -0.6619 -0.1549 490 GLU B CA 10970 C C . GLU B 490 ? 2.3292 1.8591 2.9272 -0.0364 -0.7135 -0.1267 490 GLU B C 10971 O O . GLU B 490 ? 2.3156 1.8524 2.8676 -0.0308 -0.7495 -0.1024 490 GLU B O 10972 C CB . GLU B 490 ? 2.3620 1.9735 3.0933 -0.0522 -0.6370 -0.2184 490 GLU B CB 10973 C CG . GLU B 490 ? 2.3907 2.0552 3.1817 -0.0728 -0.5921 -0.2564 490 GLU B CG 10974 C CD . GLU B 490 ? 2.4090 2.1335 3.1906 -0.0776 -0.6164 -0.2582 490 GLU B CD 10975 O OE1 . GLU B 490 ? 2.4145 2.1978 3.2163 -0.0587 -0.6485 -0.2912 490 GLU B OE1 10976 O OE2 . GLU B 490 ? 2.4101 2.1227 3.1618 -0.0977 -0.6042 -0.2274 490 GLU B OE2 10977 N N . GLY B 491 ? 2.3722 1.8630 2.9754 -0.0221 -0.7141 -0.1297 491 GLY B N 10978 C CA . GLY B 491 ? 2.4306 1.8904 2.9902 0.0013 -0.7601 -0.1081 491 GLY B CA 10979 C C . GLY B 491 ? 2.5446 1.9413 3.0311 -0.0039 -0.7815 -0.0480 491 GLY B C 10980 O O . GLY B 491 ? 2.5245 1.8947 2.9677 0.0135 -0.8200 -0.0252 491 GLY B O 10981 N N . GLN B 492 ? 2.6355 2.0079 3.1105 -0.0273 -0.7551 -0.0249 492 GLN B N 10982 C CA . GLN B 492 ? 2.5498 1.8680 2.9660 -0.0356 -0.7712 0.0261 492 GLN B CA 10983 C C . GLN B 492 ? 2.5512 1.8854 2.9266 -0.0335 -0.8048 0.0470 492 GLN B C 10984 O O . GLN B 492 ? 2.6035 1.9941 2.9940 -0.0361 -0.8035 0.0275 492 GLN B O 10985 C CB . GLN B 492 ? 2.4112 1.7136 2.8296 -0.0595 -0.7359 0.0383 492 GLN B CB 10986 C CG . GLN B 492 ? 2.4658 1.6996 2.8445 -0.0622 -0.7407 0.0758 492 GLN B CG 10987 C CD . GLN B 492 ? 2.5282 1.7195 2.9160 -0.0460 -0.7296 0.0675 492 GLN B CD 10988 O OE1 . GLN B 492 ? 2.5749 1.7853 3.0021 -0.0363 -0.7105 0.0337 492 GLN B OE1 10989 N NE2 . GLN B 492 ? 2.4583 1.5917 2.8119 -0.0425 -0.7404 0.0962 492 GLN B NE2 10990 N N . PRO B 493 ? 2.5053 1.7872 2.8278 -0.0274 -0.8327 0.0860 493 PRO B N 10991 C CA . PRO B 493 ? 2.4252 1.7053 2.6987 -0.0222 -0.8609 0.1113 493 PRO B CA 10992 C C . PRO B 493 ? 2.4137 1.7119 2.6763 -0.0465 -0.8463 0.1260 493 PRO B C 10993 O O . PRO B 493 ? 2.5170 1.8366 2.8131 -0.0671 -0.8157 0.1136 493 PRO B O 10994 C CB . PRO B 493 ? 2.3662 1.5738 2.5950 -0.0172 -0.8804 0.1497 493 PRO B CB 10995 C CG . PRO B 493 ? 2.3653 1.5518 2.6209 -0.0066 -0.8761 0.1341 493 PRO B CG 10996 C CD . PRO B 493 ? 2.4201 1.6391 2.7273 -0.0207 -0.8388 0.1047 493 PRO B CD 10997 N N . VAL B 494 ? 2.3777 1.6626 2.5904 -0.0427 -0.8661 0.1535 494 VAL B N 10998 C CA . VAL B 494 ? 2.3945 1.6953 2.5916 -0.0631 -0.8545 0.1686 494 VAL B CA 10999 C C . VAL B 494 ? 2.4207 1.6819 2.6183 -0.0929 -0.8338 0.1937 494 VAL B C 11000 O O . VAL B 494 ? 2.5228 1.7474 2.7310 -0.0935 -0.8308 0.1969 494 VAL B O 11001 C CB . VAL B 494 ? 2.5852 1.8689 2.7208 -0.0467 -0.8789 0.1941 494 VAL B CB 11002 C CG1 . VAL B 494 ? 2.6492 1.8551 2.7405 -0.0510 -0.8868 0.2367 494 VAL B CG1 11003 C CG2 . VAL B 494 ? 2.5954 1.9159 2.7202 -0.0586 -0.8685 0.1963 494 VAL B CG2 11004 N N . CYS B 495 ? 2.3578 1.6266 2.5443 -0.1155 -0.8204 0.2095 495 CYS B N 11005 C CA . CYS B 495 ? 2.3887 1.6344 2.5879 -0.1423 -0.7990 0.2221 495 CYS B CA 11006 C C . CYS B 495 ? 2.2155 1.3939 2.3885 -0.1434 -0.8113 0.2511 495 CYS B C 11007 O O . CYS B 495 ? 2.2106 1.3584 2.3465 -0.1469 -0.8212 0.2785 495 CYS B O 11008 C CB . CYS B 495 ? 2.4854 1.7531 2.6783 -0.1666 -0.7834 0.2329 495 CYS B CB 11009 S SG . CYS B 495 ? 3.1846 2.5330 3.4107 -0.1717 -0.7650 0.2001 495 CYS B SG 11010 N N . SER B 496 ? 2.1266 1.2814 2.3201 -0.1405 -0.8073 0.2436 496 SER B N 11011 C CA . SER B 496 ? 2.0851 1.1808 2.2638 -0.1415 -0.8176 0.2641 496 SER B CA 11012 C C . SER B 496 ? 2.1482 1.2042 2.2871 -0.1307 -0.8417 0.2886 496 SER B C 11013 O O . SER B 496 ? 2.3312 1.3428 2.4548 -0.1417 -0.8447 0.3107 496 SER B O 11014 C CB . SER B 496 ? 2.2475 1.3329 2.4322 -0.1675 -0.8019 0.2750 496 SER B CB 11015 O OG . SER B 496 ? 1.9692 1.0927 2.1828 -0.1766 -0.7775 0.2547 496 SER B OG 11016 N N . GLN B 497 ? 2.1387 1.2094 2.2619 -0.1076 -0.8575 0.2822 497 GLN B N 11017 C CA . GLN B 497 ? 2.2277 1.2635 2.3028 -0.0936 -0.8771 0.3064 497 GLN B CA 11018 C C . GLN B 497 ? 2.3175 1.3412 2.3652 -0.1137 -0.8657 0.3314 497 GLN B C 11019 O O . GLN B 497 ? 2.2743 1.3409 2.3224 -0.1199 -0.8557 0.3247 497 GLN B O 11020 C CB . GLN B 497 ? 2.2380 1.2135 2.3006 -0.0840 -0.8921 0.3209 497 GLN B CB 11021 C CG . GLN B 497 ? 2.2792 1.2501 2.3277 -0.0507 -0.9156 0.3123 497 GLN B CG 11022 C CD . GLN B 497 ? 2.1502 1.1725 2.2404 -0.0389 -0.9134 0.2751 497 GLN B CD 11023 O OE1 . GLN B 497 ? 2.1090 1.1479 2.2380 -0.0531 -0.8944 0.2592 497 GLN B OE1 11024 N NE2 . GLN B 497 ? 2.1896 1.2356 2.2717 -0.0112 -0.9311 0.2592 497 GLN B NE2 11025 N N . ARG B 498 ? 2.5053 1.4699 2.5308 -0.1232 -0.8659 0.3586 498 ARG B N 11026 C CA . ARG B 498 ? 2.5755 1.5206 2.5871 -0.1491 -0.8480 0.3805 498 ARG B CA 11027 C C . ARG B 498 ? 2.7643 1.7380 2.7467 -0.1481 -0.8401 0.3866 498 ARG B C 11028 O O . ARG B 498 ? 2.6185 1.6315 2.6231 -0.1687 -0.8233 0.3782 498 ARG B O 11029 C CB . ARG B 498 ? 2.2726 1.2328 2.3301 -0.1786 -0.8304 0.3698 498 ARG B CB 11030 C CG . ARG B 498 ? 2.2546 1.1812 2.3368 -0.1802 -0.8367 0.3652 498 ARG B CG 11031 C CD . ARG B 498 ? 2.2290 1.1769 2.3514 -0.2020 -0.8211 0.3504 498 ARG B CD 11032 N NE . ARG B 498 ? 2.2560 1.1849 2.4015 -0.1934 -0.8295 0.3374 498 ARG B NE 11033 C CZ . ARG B 498 ? 2.1695 1.1074 2.3442 -0.2037 -0.8204 0.3231 498 ARG B CZ 11034 N NH1 . ARG B 498 ? 2.2034 1.1700 2.3909 -0.2254 -0.8023 0.3201 498 ARG B NH1 11035 N NH2 . ARG B 498 ? 2.1007 1.0180 2.2887 -0.1895 -0.8299 0.3112 498 ARG B NH2 11036 N N . GLY B 499 ? 2.9093 1.8630 2.8395 -0.1214 -0.8526 0.4005 499 GLY B N 11037 C CA . GLY B 499 ? 3.0211 1.9949 2.9137 -0.1144 -0.8468 0.4079 499 GLY B CA 11038 C C . GLY B 499 ? 3.0710 2.1249 2.9892 -0.1052 -0.8514 0.3753 499 GLY B C 11039 O O . GLY B 499 ? 3.0532 2.1373 2.9574 -0.1086 -0.8420 0.3755 499 GLY B O 11040 N N . GLU B 500 ? 2.9539 2.0406 2.9126 -0.0944 -0.8634 0.3460 500 GLU B N 11041 C CA . GLU B 500 ? 2.7213 1.8828 2.7142 -0.0825 -0.8676 0.3077 500 GLU B CA 11042 C C . GLU B 500 ? 2.7306 1.9456 2.7525 -0.1069 -0.8455 0.2947 500 GLU B C 11043 O O . GLU B 500 ? 2.6843 1.8889 2.7264 -0.1389 -0.8247 0.3048 500 GLU B O 11044 C CB . GLU B 500 ? 2.7468 1.9253 2.7010 -0.0405 -0.8929 0.2981 500 GLU B CB 11045 C CG . GLU B 500 ? 2.7993 1.9575 2.6845 -0.0255 -0.8956 0.3235 500 GLU B CG 11046 C CD . GLU B 500 ? 2.8445 1.9187 2.6671 -0.0110 -0.9027 0.3618 500 GLU B CD 11047 O OE1 . GLU B 500 ? 2.8159 1.8591 2.6467 -0.0031 -0.9148 0.3623 500 GLU B OE1 11048 O OE2 . GLU B 500 ? 2.9040 1.9403 2.6687 -0.0076 -0.8935 0.3915 500 GLU B OE2 11049 N N . CYS B 501 ? 2.8830 2.1572 2.9083 -0.0900 -0.8514 0.2696 501 CYS B N 11050 C CA . CYS B 501 ? 2.8669 2.2000 2.9257 -0.1102 -0.8315 0.2508 501 CYS B CA 11051 C C . CYS B 501 ? 2.8616 2.2447 2.8991 -0.0855 -0.8436 0.2339 501 CYS B C 11052 O O . CYS B 501 ? 2.9079 2.2986 2.9232 -0.0485 -0.8692 0.2213 501 CYS B O 11053 C CB . CYS B 501 ? 2.8294 2.2030 2.9584 -0.1224 -0.8170 0.2155 501 CYS B CB 11054 S SG . CYS B 501 ? 3.0727 2.5346 3.2521 -0.1332 -0.7970 0.1752 501 CYS B SG 11055 N N . LEU B 502 ? 2.7404 2.1589 2.7841 -0.1036 -0.8266 0.2318 502 LEU B N 11056 C CA . LEU B 502 ? 2.6194 2.0962 2.6521 -0.0805 -0.8371 0.2085 502 LEU B CA 11057 C C . LEU B 502 ? 2.5759 2.1163 2.6583 -0.1069 -0.8135 0.1844 502 LEU B C 11058 O O . LEU B 502 ? 2.6078 2.1316 2.6971 -0.1417 -0.7892 0.2051 502 LEU B O 11059 C CB . LEU B 502 ? 2.6847 2.1205 2.6333 -0.0600 -0.8475 0.2436 502 LEU B CB 11060 C CG . LEU B 502 ? 2.7547 2.1218 2.6636 -0.0876 -0.8268 0.2927 502 LEU B CG 11061 C CD1 . LEU B 502 ? 2.7467 2.1450 2.6736 -0.1198 -0.8013 0.2943 502 LEU B CD1 11062 C CD2 . LEU B 502 ? 2.8143 2.1199 2.6349 -0.0563 -0.8388 0.3269 502 LEU B CD2 11063 N N . CYS B 503 ? 2.9189 2.1140 2.2641 -0.0962 -1.0560 0.3250 503 CYS B N 11064 C CA . CYS B 503 ? 2.5558 1.8550 1.8514 -0.0746 -0.9926 0.3000 503 CYS B CA 11065 C C . CYS B 503 ? 2.3549 1.8171 1.6830 -0.0512 -0.8842 0.2516 503 CYS B C 11066 O O . CYS B 503 ? 2.5113 2.0663 1.7467 -0.1031 -0.8334 0.2571 503 CYS B O 11067 C CB . CYS B 503 ? 2.5098 1.7947 1.6328 -0.1589 -1.0181 0.3533 503 CYS B CB 11068 S SG . CYS B 503 ? 2.9352 2.2629 1.9103 -0.2847 -0.9991 0.4103 503 CYS B SG 11069 N N . GLY B 504 ? 2.1705 1.6713 1.6333 0.0207 -0.8530 0.2009 504 GLY B N 11070 C CA . GLY B 504 ? 2.2028 1.8373 1.7063 0.0357 -0.7680 0.1611 504 GLY B CA 11071 C C . GLY B 504 ? 2.1765 1.8234 1.6644 -0.0123 -0.7425 0.1778 504 GLY B C 11072 O O . GLY B 504 ? 2.0909 1.6673 1.6381 -0.0068 -0.7752 0.1840 504 GLY B O 11073 N N . GLN B 505 ? 2.1966 1.9391 1.6176 -0.0564 -0.6855 0.1769 505 GLN B N 11074 C CA . GLN B 505 ? 2.3551 2.1266 1.7695 -0.0972 -0.6501 0.1869 505 GLN B CA 11075 C C . GLN B 505 ? 2.5126 2.1662 1.8948 -0.1417 -0.7136 0.2425 505 GLN B C 11076 O O . GLN B 505 ? 2.5852 2.1648 1.8741 -0.1931 -0.7725 0.2929 505 GLN B O 11077 C CB . GLN B 505 ? 2.4221 2.3049 1.7519 -0.1528 -0.5925 0.1805 505 GLN B CB 11078 C CG . GLN B 505 ? 2.3410 2.3483 1.7233 -0.1111 -0.5407 0.1154 505 GLN B CG 11079 C CD . GLN B 505 ? 2.3777 2.3965 1.7193 -0.0966 -0.5643 0.1050 505 GLN B CD 11080 O OE1 . GLN B 505 ? 2.4211 2.3509 1.6823 -0.1235 -0.6171 0.1503 505 GLN B OE1 11081 N NE2 . GLN B 505 ? 2.2871 2.4107 1.6898 -0.0551 -0.5342 0.0451 505 GLN B NE2 11082 N N . CYS B 506 ? 2.4792 2.1157 1.9430 -0.1250 -0.7088 0.2326 506 CYS B N 11083 C CA . CYS B 506 ? 2.4321 1.9545 1.9118 -0.1483 -0.7829 0.2701 506 CYS B CA 11084 C C . CYS B 506 ? 2.5380 2.0470 1.9141 -0.2353 -0.7934 0.3308 506 CYS B C 11085 O O . CYS B 506 ? 2.4292 2.0304 1.7742 -0.2609 -0.7220 0.3245 506 CYS B O 11086 C CB . CYS B 506 ? 2.2098 1.7340 1.8269 -0.0953 -0.7728 0.2244 506 CYS B CB 11087 S SG . CYS B 506 ? 2.4695 2.0221 2.2155 -0.0067 -0.7611 0.1519 506 CYS B SG 11088 N N . VAL B 507 ? 2.7091 2.1006 2.0364 -0.2852 -0.8902 0.3905 507 VAL B N 11089 C CA . VAL B 507 ? 2.7155 2.0724 1.9706 -0.3683 -0.9238 0.4550 507 VAL B CA 11090 C C . VAL B 507 ? 2.5997 1.8860 1.9831 -0.3332 -0.9739 0.4436 507 VAL B C 11091 O O . VAL B 507 ? 2.4545 1.6476 1.9347 -0.2916 -1.0539 0.4258 507 VAL B O 11092 C CB . VAL B 507 ? 2.8456 2.1106 1.9699 -0.4598 -1.0174 0.5367 507 VAL B CB 11093 C CG1 . VAL B 507 ? 2.8758 2.2430 1.8545 -0.5156 -0.9531 0.5453 507 VAL B CG1 11094 C CG2 . VAL B 507 ? 2.9142 2.0436 2.1015 -0.4244 -1.1255 0.5388 507 VAL B CG2 11095 N N . CYS B 508 ? 2.6057 1.9425 2.0019 -0.3469 -0.9269 0.4444 508 CYS B N 11096 C CA . CYS B 508 ? 2.5237 1.8181 2.0529 -0.3041 -0.9594 0.4172 508 CYS B CA 11097 C C . CYS B 508 ? 2.6563 1.8925 2.1563 -0.3694 -1.0191 0.4818 508 CYS B C 11098 O O . CYS B 508 ? 2.6635 1.7864 2.2251 -0.3764 -1.1350 0.5048 508 CYS B O 11099 C CB . CYS B 508 ? 2.3874 1.7907 1.9957 -0.2420 -0.8529 0.3454 508 CYS B CB 11100 S SG . CYS B 508 ? 2.3502 1.7982 2.0569 -0.1527 -0.8175 0.2616 508 CYS B SG 11101 N N . HIS B 509 ? 2.7718 2.0864 2.1891 -0.4173 -0.9462 0.5077 509 HIS B N 11102 C CA . HIS B 509 ? 2.9388 2.2188 2.3535 -0.4642 -0.9827 0.5567 509 HIS B CA 11103 C C . HIS B 509 ? 3.0359 2.2210 2.3507 -0.5653 -1.0946 0.6567 509 HIS B C 11104 O O . HIS B 509 ? 3.0727 2.2220 2.2933 -0.6146 -1.1399 0.6960 509 HIS B O 11105 C CB . HIS B 509 ? 2.9207 2.3191 2.2852 -0.4846 -0.8661 0.5481 509 HIS B CB 11106 C CG . HIS B 509 ? 3.0672 2.5461 2.2821 -0.5596 -0.8123 0.5774 509 HIS B CG 11107 N ND1 . HIS B 509 ? 3.1698 2.6335 2.2994 -0.5916 -0.8440 0.5973 509 HIS B ND1 11108 C CD2 . HIS B 509 ? 3.0078 2.5917 2.1501 -0.6106 -0.7287 0.5812 509 HIS B CD2 11109 C CE1 . HIS B 509 ? 3.1763 2.7420 2.1839 -0.6609 -0.7793 0.6090 509 HIS B CE1 11110 N NE2 . HIS B 509 ? 3.1407 2.7845 2.1592 -0.6734 -0.7080 0.5956 509 HIS B NE2 11111 N N . SER B 510 ? 2.9260 2.0692 2.2640 -0.5985 -1.1434 0.6995 510 SER B N 11112 C CA . SER B 510 ? 3.0547 2.1436 2.2793 -0.7153 -1.2243 0.8059 510 SER B CA 11113 C C . SER B 510 ? 3.0128 2.1791 2.2231 -0.7375 -1.1482 0.8165 510 SER B C 11114 O O . SER B 510 ? 3.0914 2.3347 2.1645 -0.8240 -1.0926 0.8601 510 SER B O 11115 C CB . SER B 510 ? 3.0301 1.9733 2.3556 -0.7300 -1.3693 0.8272 510 SER B CB 11116 O OG . SER B 510 ? 3.1360 2.0522 2.3880 -0.8479 -1.4129 0.9009 510 SER B OG 11117 N N . SER B 511 ? 2.9687 2.1226 2.3182 -0.6650 -1.1436 0.7731 511 SER B N 11118 C CA . SER B 511 ? 2.8905 1.9636 2.4115 -0.5762 -1.2205 0.7174 511 SER B CA 11119 C C . SER B 511 ? 3.0155 2.0103 2.6395 -0.5736 -1.3178 0.7408 511 SER B C 11120 O O . SER B 511 ? 3.1017 1.9979 2.7635 -0.6176 -1.4341 0.7753 511 SER B O 11121 C CB . SER B 511 ? 2.5438 1.7072 2.1581 -0.4726 -1.1047 0.6077 511 SER B CB 11122 O OG . SER B 511 ? 2.4392 1.6873 2.0509 -0.4639 -1.0027 0.5900 511 SER B OG 11123 N N . ASP B 512 ? 2.8154 1.8715 2.5109 -0.5220 -1.2398 0.6926 512 ASP B N 11124 C CA . ASP B 512 ? 2.8113 1.8111 2.6048 -0.5141 -1.3150 0.7082 512 ASP B CA 11125 C C . ASP B 512 ? 2.6588 1.7358 2.4139 -0.5239 -1.2108 0.7166 512 ASP B C 11126 O O . ASP B 512 ? 2.6105 1.6701 2.2893 -0.6003 -1.2384 0.8002 512 ASP B O 11127 C CB . ASP B 512 ? 2.8151 1.7897 2.8053 -0.4127 -1.3591 0.6084 512 ASP B CB 11128 C CG . ASP B 512 ? 2.6416 1.7041 2.6638 -0.3397 -1.2482 0.5097 512 ASP B CG 11129 O OD1 . ASP B 512 ? 2.5652 1.6075 2.7191 -0.2772 -1.2960 0.4334 512 ASP B OD1 11130 O OD2 . ASP B 512 ? 2.2985 1.4534 2.2217 -0.3480 -1.1190 0.5058 512 ASP B OD2 11131 N N . PHE B 513 ? 2.5218 1.6831 2.3337 -0.4491 -1.0949 0.6282 513 PHE B N 11132 C CA . PHE B 513 ? 2.3772 1.6029 2.1910 -0.4374 -0.9992 0.6132 513 PHE B CA 11133 C C . PHE B 513 ? 2.4329 1.7603 2.1260 -0.4722 -0.8710 0.6149 513 PHE B C 11134 O O . PHE B 513 ? 2.2901 1.6770 1.9890 -0.4596 -0.7829 0.5905 513 PHE B O 11135 C CB . PHE B 513 ? 2.2595 1.5112 2.2155 -0.3434 -0.9647 0.5146 513 PHE B CB 11136 C CG . PHE B 513 ? 2.3744 1.5503 2.4754 -0.2999 -1.0864 0.4826 513 PHE B CG 11137 C CD1 . PHE B 513 ? 2.3218 1.5298 2.5432 -0.2243 -1.0746 0.3793 513 PHE B CD1 11138 C CD2 . PHE B 513 ? 2.4362 1.5155 2.5624 -0.3390 -1.2187 0.5512 513 PHE B CD2 11139 C CE1 . PHE B 513 ? 2.2446 1.3990 2.6202 -0.1830 -1.1868 0.3308 513 PHE B CE1 11140 C CE2 . PHE B 513 ? 2.3253 1.3367 2.6102 -0.2956 -1.3439 0.5100 513 PHE B CE2 11141 C CZ . PHE B 513 ? 2.2321 1.2858 2.6479 -0.2146 -1.3251 0.3925 513 PHE B CZ 11142 N N . GLY B 514 ? 2.7576 2.1041 2.3506 -0.5162 -0.8674 0.6384 514 GLY B N 11143 C CA . GLY B 514 ? 2.7022 2.1572 2.2051 -0.5383 -0.7531 0.6167 514 GLY B CA 11144 C C . GLY B 514 ? 2.6354 2.1299 2.1596 -0.4827 -0.7128 0.5492 514 GLY B C 11145 O O . GLY B 514 ? 2.6256 2.0660 2.2313 -0.4284 -0.7681 0.5181 514 GLY B O 11146 N N . LYS B 515 ? 2.6661 2.2609 2.1285 -0.4962 -0.6194 0.5209 515 LYS B N 11147 C CA . LYS B 515 ? 2.7242 2.3588 2.1712 -0.4688 -0.5944 0.4788 515 LYS B CA 11148 C C . LYS B 515 ? 2.6157 2.2337 2.1763 -0.3786 -0.5969 0.4125 515 LYS B C 11149 O O . LYS B 515 ? 2.5088 2.1378 2.1567 -0.3323 -0.5674 0.3712 515 LYS B O 11150 C CB . LYS B 515 ? 2.6105 2.3687 2.0076 -0.4880 -0.4928 0.4420 515 LYS B CB 11151 C CG . LYS B 515 ? 2.4229 2.2378 1.9069 -0.4371 -0.4178 0.3788 515 LYS B CG 11152 C CD . LYS B 515 ? 2.4351 2.3665 1.9004 -0.4442 -0.3395 0.3266 515 LYS B CD 11153 C CE . LYS B 515 ? 2.3739 2.3444 1.9377 -0.3930 -0.2868 0.2643 515 LYS B CE 11154 N NZ . LYS B 515 ? 2.3852 2.4638 1.9581 -0.3944 -0.2298 0.2049 515 LYS B NZ 11155 N N . ILE B 516 ? 2.5074 2.1013 2.0611 -0.3613 -0.6341 0.4037 516 ILE B N 11156 C CA . ILE B 516 ? 2.3086 1.9068 1.9576 -0.2851 -0.6293 0.3377 516 ILE B CA 11157 C C . ILE B 516 ? 2.3070 1.9814 1.9166 -0.2731 -0.5718 0.3060 516 ILE B C 11158 O O . ILE B 516 ? 2.5267 2.1884 2.0628 -0.3002 -0.5991 0.3319 516 ILE B O 11159 C CB . ILE B 516 ? 2.3044 1.8040 2.0093 -0.2641 -0.7327 0.3428 516 ILE B CB 11160 C CG1 . ILE B 516 ? 2.3113 1.7381 2.0828 -0.2688 -0.8032 0.3629 516 ILE B CG1 11161 C CG2 . ILE B 516 ? 2.2340 1.7578 2.0346 -0.1918 -0.7184 0.2677 516 ILE B CG2 11162 C CD1 . ILE B 516 ? 2.4609 1.7879 2.3133 -0.2498 -0.9222 0.3590 516 ILE B CD1 11163 N N . THR B 517 ? 2.2200 1.9706 1.8804 -0.2359 -0.5008 0.2515 517 THR B N 11164 C CA . THR B 517 ? 2.2006 2.0302 1.8403 -0.2242 -0.4525 0.2181 517 THR B CA 11165 C C . THR B 517 ? 2.1203 1.9679 1.8446 -0.1618 -0.4469 0.1650 517 THR B C 11166 O O . THR B 517 ? 2.0590 1.8890 1.8611 -0.1321 -0.4536 0.1406 517 THR B O 11167 C CB . THR B 517 ? 2.2408 2.1573 1.8683 -0.2475 -0.3813 0.1993 517 THR B CB 11168 O OG1 . THR B 517 ? 2.3061 2.3005 1.9443 -0.2274 -0.3479 0.1549 517 THR B OG1 11169 C CG2 . THR B 517 ? 2.1666 2.0823 1.8715 -0.2266 -0.3570 0.1778 517 THR B CG2 11170 N N . GLY B 518 ? 2.1232 2.0131 1.8314 -0.1464 -0.4364 0.1456 518 GLY B N 11171 C CA . GLY B 518 ? 2.0176 1.9384 1.7994 -0.0959 -0.4292 0.0998 518 GLY B CA 11172 C C . GLY B 518 ? 1.9709 1.8918 1.7292 -0.0765 -0.4532 0.0963 518 GLY B C 11173 O O . GLY B 518 ? 2.0481 1.9402 1.7276 -0.1047 -0.4776 0.1295 518 GLY B O 11174 N N . LYS B 519 ? 1.8740 1.8278 1.6963 -0.0342 -0.4495 0.0592 519 LYS B N 11175 C CA . LYS B 519 ? 1.8465 1.7896 1.6625 -0.0064 -0.4794 0.0543 519 LYS B CA 11176 C C . LYS B 519 ? 1.8822 1.7338 1.7170 0.0079 -0.5368 0.0654 519 LYS B C 11177 O O . LYS B 519 ? 1.9310 1.7244 1.7153 0.0014 -0.5809 0.0919 519 LYS B O 11178 C CB . LYS B 519 ? 1.7246 1.7318 1.6107 0.0305 -0.4648 0.0150 519 LYS B CB 11179 C CG . LYS B 519 ? 1.7061 1.7147 1.5850 0.0605 -0.4915 0.0101 519 LYS B CG 11180 C CD . LYS B 519 ? 1.6178 1.6804 1.5763 0.0943 -0.4900 -0.0220 519 LYS B CD 11181 C CE . LYS B 519 ? 1.7276 1.8051 1.6801 0.1241 -0.5141 -0.0268 519 LYS B CE 11182 N NZ . LYS B 519 ? 1.8591 1.8565 1.7569 0.1308 -0.5503 -0.0037 519 LYS B NZ 11183 N N . TYR B 520 ? 1.9087 1.7507 1.8234 0.0244 -0.5404 0.0391 520 TYR B N 11184 C CA . TYR B 520 ? 1.9865 1.7505 1.9525 0.0393 -0.5998 0.0316 520 TYR B CA 11185 C C . TYR B 520 ? 2.0544 1.7625 2.0016 0.0049 -0.6247 0.0626 520 TYR B C 11186 O O . TYR B 520 ? 1.9699 1.6103 1.9757 0.0133 -0.6853 0.0538 520 TYR B O 11187 C CB . TYR B 520 ? 1.9376 1.7435 2.0162 0.0751 -0.5905 -0.0312 520 TYR B CB 11188 C CG . TYR B 520 ? 1.9517 1.8263 2.0516 0.1000 -0.5634 -0.0568 520 TYR B CG 11189 C CD1 . TYR B 520 ? 1.8644 1.8233 1.9571 0.0882 -0.5105 -0.0621 520 TYR B CD1 11190 C CD2 . TYR B 520 ? 1.9998 1.8487 2.1344 0.1332 -0.6008 -0.0738 520 TYR B CD2 11191 C CE1 . TYR B 520 ? 1.8614 1.8787 1.9794 0.1057 -0.5009 -0.0790 520 TYR B CE1 11192 C CE2 . TYR B 520 ? 1.8877 1.7988 2.0448 0.1548 -0.5822 -0.0923 520 TYR B CE2 11193 C CZ . TYR B 520 ? 1.8270 1.8230 1.9752 0.1394 -0.5349 -0.0926 520 TYR B CZ 11194 O OH . TYR B 520 ? 1.7093 1.7629 1.8853 0.1558 -0.5310 -0.1049 520 TYR B OH 11195 N N . CYS B 521 ? 2.2249 1.9646 2.1024 -0.0332 -0.5828 0.0942 521 CYS B N 11196 C CA . CYS B 521 ? 2.1800 1.8801 2.0385 -0.0692 -0.5973 0.1270 521 CYS B CA 11197 C C . CYS B 521 ? 2.0204 1.7230 1.9839 -0.0439 -0.5991 0.0842 521 CYS B C 11198 O O . CYS B 521 ? 2.1034 1.7433 2.0997 -0.0519 -0.6519 0.0955 521 CYS B O 11199 C CB . CYS B 521 ? 2.2658 1.8665 2.0709 -0.1033 -0.6786 0.1818 521 CYS B CB 11200 S SG . CYS B 521 ? 2.2079 1.8169 1.8663 -0.1541 -0.6744 0.2347 521 CYS B SG 11201 N N . GLU B 522 ? 1.9267 1.7065 1.9439 -0.0182 -0.5469 0.0339 522 GLU B N 11202 C CA . GLU B 522 ? 1.8836 1.6899 1.9951 -0.0007 -0.5392 -0.0178 522 GLU B CA 11203 C C . GLU B 522 ? 1.8772 1.7003 1.9750 -0.0264 -0.5025 -0.0045 522 GLU B C 11204 O O . GLU B 522 ? 1.8441 1.6765 2.0106 -0.0189 -0.5047 -0.0400 522 GLU B O 11205 C CB . GLU B 522 ? 1.9247 1.8123 2.0874 0.0218 -0.5025 -0.0720 522 GLU B CB 11206 C CG . GLU B 522 ? 1.9835 1.9402 2.1028 0.0031 -0.4427 -0.0615 522 GLU B CG 11207 C CD . GLU B 522 ? 1.9026 1.8602 1.9554 0.0023 -0.4407 -0.0289 522 GLU B CD 11208 O OE1 . GLU B 522 ? 1.9513 1.8543 1.9725 0.0101 -0.4799 -0.0068 522 GLU B OE1 11209 O OE2 . GLU B 522 ? 1.7490 1.7626 1.7867 -0.0085 -0.4064 -0.0285 522 GLU B OE2 11210 N N . CYS B 523 ? 1.9212 1.7537 1.9373 -0.0566 -0.4692 0.0395 523 CYS B N 11211 C CA . CYS B 523 ? 1.9662 1.8096 1.9701 -0.0817 -0.4348 0.0536 523 CYS B CA 11212 C C . CYS B 523 ? 2.1352 1.9059 2.1282 -0.1000 -0.4797 0.0927 523 CYS B C 11213 O O . CYS B 523 ? 2.1489 1.8705 2.0838 -0.1221 -0.5196 0.1392 523 CYS B O 11214 C CB . CYS B 523 ? 2.0081 1.8962 1.9493 -0.1073 -0.3866 0.0736 523 CYS B CB 11215 S SG . CYS B 523 ? 2.1441 2.1132 2.1140 -0.0910 -0.3511 0.0324 523 CYS B SG 11216 N N . ASP B 524 ? 2.2178 1.9824 2.2651 -0.0960 -0.4787 0.0758 524 ASP B N 11217 C CA . ASP B 524 ? 2.1970 1.8921 2.2534 -0.1096 -0.5314 0.1103 524 ASP B CA 11218 C C . ASP B 524 ? 2.1156 1.7998 2.0861 -0.1558 -0.5078 0.1726 524 ASP B C 11219 O O . ASP B 524 ? 2.1817 1.8183 2.0921 -0.1898 -0.5507 0.2289 524 ASP B O 11220 C CB . ASP B 524 ? 2.1341 1.8364 2.2870 -0.0860 -0.5378 0.0621 524 ASP B CB 11221 C CG . ASP B 524 ? 2.2042 1.9342 2.4552 -0.0465 -0.5620 -0.0133 524 ASP B CG 11222 O OD1 . ASP B 524 ? 2.1541 1.9611 2.4233 -0.0376 -0.5078 -0.0620 524 ASP B OD1 11223 O OD2 . ASP B 524 ? 2.2070 1.8840 2.5228 -0.0291 -0.6407 -0.0257 524 ASP B OD2 11224 N N . ASP B 525 ? 2.0681 1.7981 2.0366 -0.1627 -0.4439 0.1604 525 ASP B N 11225 C CA . ASP B 525 ? 2.1338 1.8663 2.0458 -0.2030 -0.4122 0.2021 525 ASP B CA 11226 C C . ASP B 525 ? 2.0722 1.7423 2.0047 -0.2143 -0.4536 0.2364 525 ASP B C 11227 O O . ASP B 525 ? 2.0727 1.7420 1.9759 -0.2443 -0.4281 0.2666 525 ASP B O 11228 C CB . ASP B 525 ? 2.3906 2.1404 2.2102 -0.2427 -0.4057 0.2403 525 ASP B CB 11229 C CG . ASP B 525 ? 2.3100 2.0956 2.0838 -0.2860 -0.3570 0.2609 525 ASP B CG 11230 O OD1 . ASP B 525 ? 2.2838 2.1332 2.0704 -0.2823 -0.3010 0.2230 525 ASP B OD1 11231 O OD2 . ASP B 525 ? 2.2301 1.9811 1.9632 -0.3264 -0.3808 0.3128 525 ASP B OD2 11232 N N . PHE B 526 ? 2.0585 1.6786 2.0544 -0.1888 -0.5226 0.2263 526 PHE B N 11233 C CA . PHE B 526 ? 2.0278 1.5930 2.0745 -0.1874 -0.5715 0.2435 526 PHE B CA 11234 C C . PHE B 526 ? 1.9789 1.5611 2.1386 -0.1381 -0.5785 0.1687 526 PHE B C 11235 O O . PHE B 526 ? 1.9404 1.5353 2.1302 -0.1324 -0.5480 0.1518 526 PHE B O 11236 C CB . PHE B 526 ? 2.0627 1.5473 2.0968 -0.2126 -0.6716 0.3025 526 PHE B CB 11237 C CG . PHE B 526 ? 2.1215 1.5839 2.1627 -0.2021 -0.7265 0.2920 526 PHE B CG 11238 C CD1 . PHE B 526 ? 2.0979 1.5297 2.2568 -0.1572 -0.7975 0.2390 526 PHE B CD1 11239 C CD2 . PHE B 526 ? 2.1958 1.6690 2.1333 -0.2389 -0.7120 0.3302 526 PHE B CD2 11240 C CE1 . PHE B 526 ? 2.1665 1.5694 2.3421 -0.1470 -0.8538 0.2268 526 PHE B CE1 11241 C CE2 . PHE B 526 ? 2.3522 1.7942 2.2940 -0.2300 -0.7672 0.3242 526 PHE B CE2 11242 C CZ . PHE B 526 ? 2.3638 1.7647 2.4260 -0.1834 -0.8398 0.2747 526 PHE B CZ 11243 N N . SER B 527 ? 2.0097 1.5977 2.2337 -0.1061 -0.6181 0.1190 527 SER B N 11244 C CA . SER B 527 ? 2.0421 1.6676 2.3819 -0.0653 -0.6250 0.0332 527 SER B CA 11245 C C . SER B 527 ? 1.9406 1.6461 2.2689 -0.0671 -0.5337 -0.0077 527 SER B C 11246 O O . SER B 527 ? 2.0027 1.7555 2.2780 -0.0775 -0.4795 -0.0108 527 SER B O 11247 C CB . SER B 527 ? 2.2031 1.8401 2.6119 -0.0353 -0.6693 -0.0226 527 SER B CB 11248 O OG . SER B 527 ? 2.3634 1.9123 2.7951 -0.0378 -0.7722 0.0145 527 SER B OG 11249 N N . CYS B 528 ? 1.9168 1.6330 2.2978 -0.0603 -0.5268 -0.0373 528 CYS B N 11250 C CA . CYS B 528 ? 1.8231 1.6006 2.1876 -0.0745 -0.4530 -0.0665 528 CYS B CA 11251 C C . CYS B 528 ? 1.8948 1.6966 2.3464 -0.0589 -0.4641 -0.1272 528 CYS B C 11252 O O . CYS B 528 ? 2.2251 1.9866 2.7522 -0.0341 -0.5305 -0.1377 528 CYS B O 11253 C CB . CYS B 528 ? 1.8229 1.5702 2.0990 -0.1081 -0.4100 0.0018 528 CYS B CB 11254 S SG . CYS B 528 ? 1.8124 1.5999 2.0051 -0.1329 -0.3548 0.0222 528 CYS B SG 11255 N N . VAL B 529 ? 1.7113 1.5809 2.1548 -0.0779 -0.4060 -0.1681 529 VAL B N 11256 C CA . VAL B 529 ? 1.6961 1.6026 2.2077 -0.0728 -0.4057 -0.2293 529 VAL B CA 11257 C C . VAL B 529 ? 1.7766 1.6040 2.2814 -0.0722 -0.4238 -0.1773 529 VAL B C 11258 O O . VAL B 529 ? 1.6879 1.4524 2.1164 -0.0913 -0.4100 -0.0970 529 VAL B O 11259 C CB . VAL B 529 ? 1.5411 1.5359 2.0202 -0.1125 -0.3400 -0.2714 529 VAL B CB 11260 C CG1 . VAL B 529 ? 1.5134 1.6052 2.0225 -0.1139 -0.3277 -0.3397 529 VAL B CG1 11261 C CG2 . VAL B 529 ? 1.5271 1.4846 1.9022 -0.1527 -0.2983 -0.1972 529 VAL B CG2 11262 N N . ARG B 530 ? 1.7598 1.5988 2.3534 -0.0500 -0.4555 -0.2303 530 ARG B N 11263 C CA . ARG B 530 ? 1.6534 1.4183 2.2561 -0.0442 -0.4809 -0.1866 530 ARG B CA 11264 C C . ARG B 530 ? 1.6303 1.4466 2.2699 -0.0501 -0.4540 -0.2494 530 ARG B C 11265 O O . ARG B 530 ? 1.6617 1.5730 2.3756 -0.0407 -0.4527 -0.3487 530 ARG B O 11266 C CB . ARG B 530 ? 1.7455 1.4476 2.4348 -0.0059 -0.5782 -0.1752 530 ARG B CB 11267 C CG . ARG B 530 ? 1.8134 1.4531 2.4527 -0.0128 -0.6153 -0.1008 530 ARG B CG 11268 C CD . ARG B 530 ? 1.9534 1.5316 2.6902 0.0159 -0.7310 -0.0956 530 ARG B CD 11269 N NE . ARG B 530 ? 1.9563 1.4654 2.6261 -0.0066 -0.7730 -0.0098 530 ARG B NE 11270 C CZ . ARG B 530 ? 1.9326 1.3623 2.5386 -0.0365 -0.8026 0.0903 530 ARG B CZ 11271 N NH1 . ARG B 530 ? 1.8685 1.2693 2.4779 -0.0397 -0.7970 0.1184 530 ARG B NH1 11272 N NH2 . ARG B 530 ? 1.9831 1.3665 2.5189 -0.0686 -0.8381 0.1621 530 ARG B NH2 11273 N N . TYR B 531 ? 1.6494 1.4090 2.2394 -0.0693 -0.4324 -0.1967 531 TYR B N 11274 C CA . TYR B 531 ? 1.7056 1.5010 2.3206 -0.0796 -0.4116 -0.2477 531 TYR B CA 11275 C C . TYR B 531 ? 1.9705 1.7451 2.7020 -0.0314 -0.4808 -0.2839 531 TYR B C 11276 O O . TYR B 531 ? 2.1279 1.9888 2.9606 -0.0085 -0.5025 -0.3872 531 TYR B O 11277 C CB . TYR B 531 ? 1.5493 1.2822 2.0718 -0.1201 -0.3681 -0.1787 531 TYR B CB 11278 C CG . TYR B 531 ? 1.4490 1.1892 1.9909 -0.1313 -0.3590 -0.2136 531 TYR B CG 11279 C CD1 . TYR B 531 ? 1.5109 1.3600 2.0653 -0.1584 -0.3299 -0.3022 531 TYR B CD1 11280 C CD2 . TYR B 531 ? 1.4283 1.0714 1.9719 -0.1203 -0.3787 -0.1586 531 TYR B CD2 11281 C CE1 . TYR B 531 ? 1.5934 1.4545 2.1564 -0.1758 -0.3214 -0.3360 531 TYR B CE1 11282 C CE2 . TYR B 531 ? 1.5710 1.2146 2.1306 -0.1296 -0.3731 -0.1896 531 TYR B CE2 11283 C CZ . TYR B 531 ? 1.5417 1.2942 2.1079 -0.1582 -0.3447 -0.2786 531 TYR B CZ 11284 O OH . TYR B 531 ? 1.4501 1.2082 2.0235 -0.1745 -0.3390 -0.3111 531 TYR B OH 11285 N N . LYS B 532 ? 1.8324 1.4997 2.5592 -0.0177 -0.5192 -0.2043 532 LYS B N 11286 C CA . LYS B 532 ? 1.5510 1.1811 2.3955 0.0299 -0.6070 -0.2213 532 LYS B CA 11287 C C . LYS B 532 ? 1.6217 1.1480 2.4561 0.0384 -0.6731 -0.1225 532 LYS B C 11288 O O . LYS B 532 ? 1.5528 1.0021 2.3089 0.0149 -0.6564 -0.0293 532 LYS B O 11289 C CB . LYS B 532 ? 1.4102 1.0157 2.2729 0.0332 -0.6017 -0.2271 532 LYS B CB 11290 C CG . LYS B 532 ? 1.4101 1.1291 2.3178 0.0284 -0.5662 -0.3436 532 LYS B CG 11291 C CD . LYS B 532 ? 1.5539 1.2349 2.4609 0.0257 -0.5597 -0.3369 532 LYS B CD 11292 C CE . LYS B 532 ? 1.6997 1.4965 2.7048 0.0395 -0.5641 -0.4696 532 LYS B CE 11293 N NZ . LYS B 532 ? 1.6068 1.4298 2.7844 0.1061 -0.6598 -0.5416 532 LYS B NZ 11294 N N . GLY B 533 ? 1.8065 1.3336 2.7219 0.0651 -0.7518 -0.1447 533 GLY B N 11295 C CA . GLY B 533 ? 1.9808 1.4090 2.8976 0.0645 -0.8378 -0.0529 533 GLY B CA 11296 C C . GLY B 533 ? 1.7728 1.1616 2.5457 0.0169 -0.7937 0.0472 533 GLY B C 11297 O O . GLY B 533 ? 1.9345 1.2555 2.6879 0.0007 -0.8599 0.1250 533 GLY B O 11298 N N . GLU B 534 ? 1.6591 1.0953 2.3345 -0.0107 -0.6881 0.0428 534 GLU B N 11299 C CA . GLU B 534 ? 1.7818 1.1916 2.3318 -0.0548 -0.6382 0.1260 534 GLU B CA 11300 C C . GLU B 534 ? 1.8345 1.3156 2.3242 -0.0708 -0.5653 0.0910 534 GLU B C 11301 O O . GLU B 534 ? 1.7989 1.3446 2.3047 -0.0664 -0.5186 0.0220 534 GLU B O 11302 C CB . GLU B 534 ? 1.7439 1.1120 2.2419 -0.0776 -0.5929 0.1779 534 GLU B CB 11303 C CG . GLU B 534 ? 1.7975 1.1253 2.2031 -0.1207 -0.5763 0.2697 534 GLU B CG 11304 C CD . GLU B 534 ? 1.9355 1.2134 2.3237 -0.1366 -0.5539 0.3160 534 GLU B CD 11305 O OE1 . GLU B 534 ? 1.9160 1.1828 2.3544 -0.1135 -0.5485 0.2805 534 GLU B OE1 11306 O OE2 . GLU B 534 ? 2.0365 1.2913 2.3622 -0.1751 -0.5414 0.3842 534 GLU B OE2 11307 N N . MET B 535 ? 1.9248 1.3972 2.3423 -0.0951 -0.5592 0.1408 535 MET B N 11308 C CA . MET B 535 ? 1.9102 1.4447 2.2762 -0.1072 -0.5023 0.1139 535 MET B CA 11309 C C . MET B 535 ? 1.8202 1.3759 2.1208 -0.1368 -0.4205 0.1227 535 MET B C 11310 O O . MET B 535 ? 1.7007 1.2201 1.9512 -0.1627 -0.4013 0.1795 535 MET B O 11311 C CB . MET B 535 ? 1.9839 1.5013 2.2967 -0.1237 -0.5285 0.1624 535 MET B CB 11312 C CG . MET B 535 ? 1.8348 1.4122 2.1012 -0.1308 -0.4793 0.1365 535 MET B CG 11313 S SD . MET B 535 ? 1.8662 1.4207 2.0485 -0.1609 -0.5013 0.2037 535 MET B SD 11314 C CE . MET B 535 ? 2.0983 1.5815 2.3474 -0.1457 -0.6217 0.2233 535 MET B CE 11315 N N . CYS B 536 ? 1.6401 1.2574 1.9479 -0.1382 -0.3790 0.0635 536 CYS B N 11316 C CA . CYS B 536 ? 1.5634 1.1951 1.8248 -0.1708 -0.3201 0.0660 536 CYS B CA 11317 C C . CYS B 536 ? 1.5042 1.0780 1.7698 -0.1806 -0.3148 0.0937 536 CYS B C 11318 O O . CYS B 536 ? 1.6013 1.1552 1.8307 -0.2093 -0.2814 0.1192 536 CYS B O 11319 C CB . CYS B 536 ? 1.5970 1.2375 1.7963 -0.1935 -0.2925 0.1003 536 CYS B CB 11320 S SG . CYS B 536 ? 1.7258 1.4350 1.9136 -0.1855 -0.2902 0.0665 536 CYS B SG 11321 N N . SER B 537 ? 1.4878 1.0332 1.8101 -0.1542 -0.3550 0.0845 537 SER B N 11322 C CA . SER B 537 ? 1.4370 0.9218 1.7743 -0.1557 -0.3596 0.1095 537 SER B CA 11323 C C . SER B 537 ? 1.4360 0.8575 1.7377 -0.1708 -0.3625 0.1866 537 SER B C 11324 O O . SER B 537 ? 1.3987 0.7630 1.7142 -0.1717 -0.3697 0.2163 537 SER B O 11325 C CB . SER B 537 ? 1.3795 0.8756 1.6972 -0.1845 -0.3151 0.0832 537 SER B CB 11326 O OG . SER B 537 ? 1.3614 0.9318 1.7029 -0.1845 -0.3091 0.0113 537 SER B OG 11327 N N . GLY B 538 ? 1.5470 0.9861 1.8026 -0.1862 -0.3554 0.2156 538 GLY B N 11328 C CA . GLY B 538 ? 1.5399 0.9485 1.7529 -0.2142 -0.3467 0.2778 538 GLY B CA 11329 C C . GLY B 538 ? 1.5379 0.9621 1.7232 -0.2436 -0.2864 0.2696 538 GLY B C 11330 O O . GLY B 538 ? 1.5898 1.0118 1.7484 -0.2713 -0.2657 0.3013 538 GLY B O 11331 N N . HIS B 539 ? 1.4964 0.9412 1.6948 -0.2429 -0.2642 0.2225 539 HIS B N 11332 C CA . HIS B 539 ? 1.4680 0.9156 1.6597 -0.2721 -0.2273 0.2096 539 HIS B CA 11333 C C . HIS B 539 ? 1.5120 1.0244 1.6815 -0.2854 -0.2077 0.1846 539 HIS B C 11334 O O . HIS B 539 ? 1.4965 1.0152 1.6759 -0.3091 -0.1920 0.1658 539 HIS B O 11335 C CB . HIS B 539 ? 1.3958 0.8153 1.6104 -0.2783 -0.2280 0.1836 539 HIS B CB 11336 C CG . HIS B 539 ? 1.4431 0.7964 1.6851 -0.2639 -0.2469 0.2042 539 HIS B CG 11337 N ND1 . HIS B 539 ? 1.4075 0.7218 1.6521 -0.2628 -0.2397 0.2398 539 HIS B ND1 11338 C CD2 . HIS B 539 ? 1.5191 0.8597 1.7878 -0.2444 -0.2687 0.1839 539 HIS B CD2 11339 C CE1 . HIS B 539 ? 1.4003 0.6964 1.6601 -0.2329 -0.2509 0.2400 539 HIS B CE1 11340 N NE2 . HIS B 539 ? 1.5328 0.8215 1.8183 -0.2275 -0.2778 0.2126 539 HIS B NE2 11341 N N . GLY B 540 ? 1.5643 1.1190 1.7124 -0.2700 -0.2180 0.1832 540 GLY B N 11342 C CA . GLY B 540 ? 1.6090 1.2239 1.7382 -0.2780 -0.2030 0.1607 540 GLY B CA 11343 C C . GLY B 540 ? 1.7021 1.3488 1.7973 -0.2687 -0.2128 0.1761 540 GLY B C 11344 O O . GLY B 540 ? 1.7173 1.3401 1.8080 -0.2533 -0.2445 0.1993 540 GLY B O 11345 N N . GLN B 541 ? 1.8085 1.5063 1.8851 -0.2805 -0.1941 0.1620 541 GLN B N 11346 C CA . GLN B 541 ? 1.9009 1.6325 1.9365 -0.2776 -0.2024 0.1740 541 GLN B CA 11347 C C . GLN B 541 ? 1.9144 1.6666 1.9561 -0.2507 -0.2226 0.1493 541 GLN B C 11348 O O . GLN B 541 ? 2.0083 1.7815 2.0774 -0.2458 -0.2157 0.1145 541 GLN B O 11349 C CB . GLN B 541 ? 1.9487 1.7376 1.9689 -0.3004 -0.1729 0.1593 541 GLN B CB 11350 C CG . GLN B 541 ? 2.0570 1.8472 2.0777 -0.3317 -0.1486 0.1718 541 GLN B CG 11351 C CD . GLN B 541 ? 2.1414 2.0112 2.1636 -0.3538 -0.1194 0.1368 541 GLN B CD 11352 O OE1 . GLN B 541 ? 2.1427 2.0599 2.1628 -0.3426 -0.1216 0.1088 541 GLN B OE1 11353 N NE2 . GLN B 541 ? 2.2158 2.1080 2.2504 -0.3849 -0.0928 0.1316 541 GLN B NE2 11354 N N . CYS B 542 ? 1.9041 1.6501 1.9213 -0.2399 -0.2524 0.1683 542 CYS B N 11355 C CA . CYS B 542 ? 1.8779 1.6428 1.9110 -0.2127 -0.2749 0.1401 542 CYS B CA 11356 C C . CYS B 542 ? 1.9656 1.7734 1.9609 -0.2159 -0.2673 0.1369 542 CYS B C 11357 O O . CYS B 542 ? 2.0374 1.8372 1.9846 -0.2304 -0.2812 0.1701 542 CYS B O 11358 C CB . CYS B 542 ? 1.8973 1.6160 1.9519 -0.1936 -0.3302 0.1540 542 CYS B CB 11359 S SG . CYS B 542 ? 1.9121 1.6551 2.0126 -0.1572 -0.3635 0.1043 542 CYS B SG 11360 N N . SER B 543 ? 1.9752 1.8296 1.9897 -0.2079 -0.2497 0.0992 543 SER B N 11361 C CA . SER B 543 ? 1.9249 1.8227 1.9154 -0.2048 -0.2462 0.0902 543 SER B CA 11362 C C . SER B 543 ? 1.8609 1.7778 1.8757 -0.1774 -0.2654 0.0616 543 SER B C 11363 O O . SER B 543 ? 1.7616 1.7071 1.8121 -0.1763 -0.2571 0.0309 543 SER B O 11364 C CB . SER B 543 ? 1.9015 1.8438 1.9052 -0.2221 -0.2180 0.0699 543 SER B CB 11365 O OG . SER B 543 ? 1.9589 1.9490 1.9517 -0.2143 -0.2199 0.0543 543 SER B OG 11366 N N . CYS B 544 ? 1.9093 1.8106 1.9028 -0.1623 -0.2944 0.0730 544 CYS B N 11367 C CA . CYS B 544 ? 1.9178 1.8349 1.9407 -0.1340 -0.3161 0.0432 544 CYS B CA 11368 C C . CYS B 544 ? 1.7999 1.7240 1.8874 -0.1205 -0.3227 0.0037 544 CYS B C 11369 O O . CYS B 544 ? 1.7097 1.6835 1.8296 -0.1132 -0.3147 -0.0358 544 CYS B O 11370 C CB . CYS B 544 ? 1.8918 1.8664 1.9122 -0.1317 -0.2976 0.0235 544 CYS B CB 11371 S SG . CYS B 544 ? 2.4460 2.4359 2.4843 -0.0983 -0.3265 0.0000 544 CYS B SG 11372 N N . GLY B 545 ? 1.8231 1.7058 1.9310 -0.1212 -0.3385 0.0115 545 GLY B N 11373 C CA . GLY B 545 ? 1.7678 1.6674 1.9452 -0.1085 -0.3462 -0.0369 545 GLY B CA 11374 C C . GLY B 545 ? 1.6887 1.6308 1.8705 -0.1332 -0.3036 -0.0572 545 GLY B C 11375 O O . GLY B 545 ? 1.6259 1.6114 1.8552 -0.1336 -0.2986 -0.1078 545 GLY B O 11376 N N . ASP B 546 ? 1.6920 1.6257 1.8281 -0.1591 -0.2768 -0.0223 546 ASP B N 11377 C CA . ASP B 546 ? 1.6124 1.5677 1.7509 -0.1908 -0.2501 -0.0321 546 ASP B CA 11378 C C . ASP B 546 ? 1.6298 1.5320 1.7504 -0.2068 -0.2402 0.0046 546 ASP B C 11379 O O . ASP B 546 ? 1.7039 1.5790 1.7963 -0.2055 -0.2404 0.0386 546 ASP B O 11380 C CB . ASP B 546 ? 1.6327 1.6346 1.7577 -0.2114 -0.2399 -0.0371 546 ASP B CB 11381 C CG . ASP B 546 ? 1.8690 1.9317 2.0147 -0.2042 -0.2463 -0.0751 546 ASP B CG 11382 O OD1 . ASP B 546 ? 1.9249 2.0112 2.0612 -0.1971 -0.2531 -0.0712 546 ASP B OD1 11383 O OD2 . ASP B 546 ? 1.9674 2.0615 2.1448 -0.2059 -0.2443 -0.1147 546 ASP B OD2 11384 N N . CYS B 547 ? 1.5633 1.4565 1.6995 -0.2266 -0.2308 -0.0049 547 CYS B N 11385 C CA . CYS B 547 ? 1.5608 1.3978 1.6902 -0.2395 -0.2239 0.0265 547 CYS B CA 11386 C C . CYS B 547 ? 1.5221 1.3570 1.6430 -0.2727 -0.2105 0.0366 547 CYS B C 11387 O O . CYS B 547 ? 1.4584 1.3128 1.5865 -0.3027 -0.2121 0.0202 547 CYS B O 11388 C CB . CYS B 547 ? 1.5099 1.3279 1.6663 -0.2416 -0.2272 0.0105 547 CYS B CB 11389 S SG . CYS B 547 ? 1.8561 1.6588 2.0555 -0.1976 -0.2617 -0.0043 547 CYS B SG 11390 N N . LEU B 548 ? 1.5850 1.4006 1.6960 -0.2732 -0.2034 0.0602 548 LEU B N 11391 C CA . LEU B 548 ? 1.5675 1.3788 1.6972 -0.3007 -0.1981 0.0577 548 LEU B CA 11392 C C . LEU B 548 ? 1.5674 1.3195 1.7097 -0.3122 -0.1909 0.0762 548 LEU B C 11393 O O . LEU B 548 ? 1.6455 1.3801 1.7751 -0.3039 -0.1806 0.0987 548 LEU B O 11394 C CB . LEU B 548 ? 1.6593 1.5103 1.7857 -0.2960 -0.1915 0.0526 548 LEU B CB 11395 C CG . LEU B 548 ? 1.6626 1.5664 1.7755 -0.2790 -0.2010 0.0382 548 LEU B CG 11396 C CD1 . LEU B 548 ? 1.7557 1.7043 1.8705 -0.2777 -0.1947 0.0256 548 LEU B CD1 11397 C CD2 . LEU B 548 ? 1.5430 1.4667 1.6784 -0.2935 -0.2204 0.0191 548 LEU B CD2 11398 N N . CYS B 549 ? 1.4859 1.2062 1.6494 -0.3377 -0.2001 0.0701 549 CYS B N 11399 C CA . CYS B 549 ? 1.4578 1.1125 1.6342 -0.3456 -0.1974 0.0874 549 CYS B CA 11400 C C . CYS B 549 ? 1.5271 1.1580 1.7355 -0.3580 -0.1900 0.0910 549 CYS B C 11401 O O . CYS B 549 ? 1.5578 1.2166 1.7988 -0.3729 -0.1973 0.0673 549 CYS B O 11402 C CB . CYS B 549 ? 1.3540 0.9811 1.5359 -0.3770 -0.2133 0.0792 549 CYS B CB 11403 S SG . CYS B 549 ? 2.0060 1.6810 2.1616 -0.3707 -0.2133 0.0574 549 CYS B SG 11404 N N . ASP B 550 ? 1.8707 1.0270 1.2753 -0.0403 0.0471 -0.1229 550 ASP B N 11405 C CA . ASP B 550 ? 1.8884 1.0117 1.2537 0.0214 0.0949 -0.1322 550 ASP B CA 11406 C C . ASP B 550 ? 1.7831 0.9315 1.1802 0.0386 0.1084 -0.1298 550 ASP B C 11407 O O . ASP B 550 ? 1.7432 0.9572 1.2123 0.0051 0.0874 -0.1228 550 ASP B O 11408 C CB . ASP B 550 ? 1.8867 1.1057 1.3312 0.0489 0.1373 -0.1328 550 ASP B CB 11409 C CG . ASP B 550 ? 1.9719 1.1635 1.3814 0.0367 0.1278 -0.1361 550 ASP B CG 11410 O OD1 . ASP B 550 ? 2.3123 1.3749 1.5979 0.0340 0.1056 -0.1409 550 ASP B OD1 11411 O OD2 . ASP B 550 ? 1.6788 0.9716 1.1790 0.0294 0.1405 -0.1339 550 ASP B OD2 11412 N N . SER B 551 ? 1.8062 0.9003 1.1463 0.0931 0.1446 -0.1327 551 SER B N 11413 C CA . SER B 551 ? 1.7844 0.8974 1.1493 0.1146 0.1608 -0.1290 551 SER B CA 11414 C C . SER B 551 ? 1.6792 0.9468 1.1963 0.1036 0.1737 -0.1218 551 SER B C 11415 O O . SER B 551 ? 1.8425 1.1975 1.4371 0.1032 0.1894 -0.1192 551 SER B O 11416 C CB . SER B 551 ? 1.8099 0.8607 1.1051 0.1832 0.2076 -0.1268 551 SER B CB 11417 O OG . SER B 551 ? 1.9715 0.8691 1.1123 0.2006 0.1991 -0.1341 551 SER B OG 11418 N N . ASP B 552 ? 1.6676 0.9590 1.2182 0.0934 0.1639 -0.1188 552 ASP B N 11419 C CA . ASP B 552 ? 1.5727 0.9909 1.2499 0.0835 0.1712 -0.1122 552 ASP B CA 11420 C C . ASP B 552 ? 1.5369 1.0272 1.2834 0.0342 0.1416 -0.1099 552 ASP B C 11421 O O . ASP B 552 ? 1.4828 1.0668 1.3213 0.0248 0.1438 -0.1047 552 ASP B O 11422 C CB . ASP B 552 ? 1.4959 0.9894 1.2402 0.1225 0.2143 -0.1051 552 ASP B CB 11423 C CG . ASP B 552 ? 1.5770 1.0230 1.2747 0.1757 0.2489 -0.0981 552 ASP B CG 11424 O OD1 . ASP B 552 ? 1.6469 1.0295 1.2730 0.2109 0.2720 -0.0965 552 ASP B OD1 11425 O OD2 . ASP B 552 ? 1.7735 1.2444 1.5037 0.1849 0.2545 -0.0921 552 ASP B OD2 11426 N N . TRP B 553 ? 1.5861 1.0290 1.2840 0.0050 0.1139 -0.1110 553 TRP B N 11427 C CA . TRP B 553 ? 1.5578 1.0650 1.3158 -0.0401 0.0860 -0.1023 553 TRP B CA 11428 C C . TRP B 553 ? 1.6077 1.0542 1.3163 -0.0818 0.0397 -0.0920 553 TRP B C 11429 O O . TRP B 553 ? 1.6825 1.0146 1.2865 -0.0846 0.0205 -0.0954 553 TRP B O 11430 C CB . TRP B 553 ? 1.6088 1.1386 1.3774 -0.0447 0.0909 -0.1044 553 TRP B CB 11431 C CG . TRP B 553 ? 1.4674 1.0709 1.2995 -0.0124 0.1298 -0.1087 553 TRP B CG 11432 C CD1 . TRP B 553 ? 1.4968 1.0726 1.2975 0.0261 0.1608 -0.1140 553 TRP B CD1 11433 C CD2 . TRP B 553 ? 1.3775 1.0905 1.3122 -0.0158 0.1395 -0.1040 553 TRP B CD2 11434 N NE1 . TRP B 553 ? 1.3661 1.0343 1.2525 0.0421 0.1862 -0.1101 553 TRP B NE1 11435 C CE2 . TRP B 553 ? 1.3084 1.0551 1.2722 0.0160 0.1715 -0.1060 553 TRP B CE2 11436 C CE3 . TRP B 553 ? 1.3791 1.1597 1.3781 -0.0406 0.1239 -0.0956 553 TRP B CE3 11437 C CZ2 . TRP B 553 ? 1.1965 1.0345 1.2472 0.0185 0.1819 -0.1015 553 TRP B CZ2 11438 C CZ3 . TRP B 553 ? 1.2463 1.1109 1.3221 -0.0323 0.1384 -0.0939 553 TRP B CZ3 11439 C CH2 . TRP B 553 ? 1.1675 1.0566 1.2666 -0.0056 0.1640 -0.0976 553 TRP B CH2 11440 N N . THR B 554 ? 1.5618 1.0818 1.3424 -0.1131 0.0209 -0.0760 554 THR B N 11441 C CA . THR B 554 ? 1.5852 1.0699 1.3409 -0.1576 -0.0252 -0.0562 554 THR B CA 11442 C C . THR B 554 ? 1.5115 1.0918 1.3508 -0.1907 -0.0398 -0.0326 554 THR B C 11443 O O . THR B 554 ? 1.5499 1.2128 1.4553 -0.1769 -0.0140 -0.0361 554 THR B O 11444 C CB . THR B 554 ? 1.5941 1.0627 1.3460 -0.1583 -0.0339 -0.0510 554 THR B CB 11445 O OG1 . THR B 554 ? 1.5275 1.0991 1.3728 -0.1407 -0.0062 -0.0508 554 THR B OG1 11446 C CG2 . THR B 554 ? 1.6707 1.0296 1.3249 -0.1269 -0.0239 -0.0697 554 THR B CG2 11447 N N . GLY B 555 ? 1.5054 1.0731 1.3402 -0.2334 -0.0818 -0.0047 555 GLY B N 11448 C CA . GLY B 555 ? 1.4183 1.0795 1.3337 -0.2623 -0.0945 0.0271 555 GLY B CA 11449 C C . GLY B 555 ? 1.4165 1.0523 1.3072 -0.2972 -0.1262 0.0445 555 GLY B C 11450 O O . GLY B 555 ? 1.4837 1.0357 1.2974 -0.2927 -0.1309 0.0248 555 GLY B O 11451 N N . TYR B 556 ? 1.3449 1.0534 1.3004 -0.3301 -0.1473 0.0848 556 TYR B N 11452 C CA . TYR B 556 ? 1.3298 1.0298 1.2771 -0.3676 -0.1803 0.1101 556 TYR B CA 11453 C C . TYR B 556 ? 1.3191 1.0434 1.2740 -0.3451 -0.1504 0.0867 556 TYR B C 11454 O O . TYR B 556 ? 1.3557 1.0170 1.2540 -0.3612 -0.1707 0.0827 556 TYR B O 11455 C CB . TYR B 556 ? 1.3109 1.1061 1.3443 -0.4005 -0.2010 0.1660 556 TYR B CB 11456 C CG . TYR B 556 ? 1.6666 1.4568 1.6987 -0.4466 -0.2431 0.2034 556 TYR B CG 11457 C CD1 . TYR B 556 ? 1.4797 1.3371 1.5576 -0.4412 -0.2250 0.2094 556 TYR B CD1 11458 C CD2 . TYR B 556 ? 1.8321 1.5479 1.8161 -0.4974 -0.3043 0.2354 556 TYR B CD2 11459 C CE1 . TYR B 556 ? 1.4074 1.2638 1.4880 -0.4840 -0.2643 0.2465 556 TYR B CE1 11460 C CE2 . TYR B 556 ? 1.8391 1.5496 1.8238 -0.5438 -0.3484 0.2744 556 TYR B CE2 11461 C CZ . TYR B 556 ? 1.7904 1.5745 1.8262 -0.5363 -0.3269 0.2800 556 TYR B CZ 11462 O OH . TYR B 556 ? 1.9919 1.7740 2.0319 -0.5828 -0.3712 0.3213 556 TYR B OH 11463 N N . TYR B 557 ? 1.4907 1.3009 1.5109 -0.3088 -0.1049 0.0723 557 TYR B N 11464 C CA . TYR B 557 ? 1.3752 1.2148 1.4090 -0.2861 -0.0754 0.0511 557 TYR B CA 11465 C C . TYR B 557 ? 1.3855 1.1713 1.3711 -0.2468 -0.0451 0.0076 557 TYR B C 11466 O O . TYR B 557 ? 1.5236 1.3285 1.5176 -0.2252 -0.0193 -0.0112 557 TYR B O 11467 C CB . TYR B 557 ? 1.2040 1.1599 1.3288 -0.2696 -0.0469 0.0637 557 TYR B CB 11468 C CG . TYR B 557 ? 1.3843 1.4076 1.5652 -0.2989 -0.0676 0.1138 557 TYR B CG 11469 C CD1 . TYR B 557 ? 1.3952 1.4453 1.5930 -0.3214 -0.0815 0.1376 557 TYR B CD1 11470 C CD2 . TYR B 557 ? 1.4369 1.5012 1.6571 -0.3022 -0.0716 0.1415 557 TYR B CD2 11471 C CE1 . TYR B 557 ? 1.3657 1.4861 1.6220 -0.3458 -0.0982 0.1917 557 TYR B CE1 11472 C CE2 . TYR B 557 ? 1.3613 1.4951 1.6384 -0.3250 -0.0869 0.1953 557 TYR B CE2 11473 C CZ . TYR B 557 ? 1.4000 1.5639 1.6970 -0.3464 -0.0998 0.2222 557 TYR B CZ 11474 O OH . TYR B 557 ? 1.4633 1.7046 1.8238 -0.3669 -0.1130 0.2836 557 TYR B OH 11475 N N . CYS B 558 ? 1.4106 1.1328 1.3490 -0.2369 -0.0479 -0.0041 558 CYS B N 11476 C CA . CYS B 558 ? 1.4303 1.1063 1.3274 -0.1957 -0.0169 -0.0371 558 CYS B CA 11477 C C . CYS B 558 ? 1.3661 1.1291 1.3365 -0.1618 0.0242 -0.0494 558 CYS B C 11478 O O . CYS B 558 ? 1.3775 1.1277 1.3342 -0.1300 0.0521 -0.0698 558 CYS B O 11479 C CB . CYS B 558 ? 1.4827 1.0753 1.2996 -0.1881 -0.0171 -0.0535 558 CYS B CB 11480 S SG . CYS B 558 ? 2.3224 1.7701 2.0161 -0.2200 -0.0679 -0.0459 558 CYS B SG 11481 N N . ASN B 559 ? 1.2831 1.1310 1.3276 -0.1680 0.0263 -0.0335 559 ASN B N 11482 C CA . ASN B 559 ? 1.2078 1.1253 1.3114 -0.1391 0.0575 -0.0432 559 ASN B CA 11483 C C . ASN B 559 ? 1.4295 1.3502 1.5453 -0.1219 0.0664 -0.0475 559 ASN B C 11484 O O . ASN B 559 ? 1.4722 1.4424 1.6321 -0.1008 0.0861 -0.0531 559 ASN B O 11485 C CB . ASN B 559 ? 1.1101 1.1095 1.2752 -0.1481 0.0584 -0.0248 559 ASN B CB 11486 C CG . ASN B 559 ? 1.3837 1.4132 1.5746 -0.1690 0.0396 0.0059 559 ASN B CG 11487 O OD1 . ASN B 559 ? 1.5413 1.5265 1.7023 -0.1882 0.0168 0.0160 559 ASN B OD1 11488 N ND2 . ASN B 559 ? 1.5363 1.6390 1.7798 -0.1635 0.0494 0.0237 559 ASN B ND2 11489 N N . CYS B 560 ? 1.4540 1.3162 1.5261 -0.1324 0.0488 -0.0439 560 CYS B N 11490 C CA . CYS B 560 ? 1.2878 1.1482 1.3674 -0.1179 0.0552 -0.0469 560 CYS B CA 11491 C C . CYS B 560 ? 1.3479 1.1506 1.3825 -0.0880 0.0737 -0.0677 560 CYS B C 11492 O O . CYS B 560 ? 1.4004 1.1323 1.3697 -0.0847 0.0715 -0.0759 560 CYS B O 11493 C CB . CYS B 560 ? 1.3063 1.1419 1.3694 -0.1461 0.0250 -0.0266 560 CYS B CB 11494 S SG . CYS B 560 ? 1.9600 1.8049 2.0414 -0.1312 0.0315 -0.0269 560 CYS B SG 11495 N N . THR B 561 ? 1.3225 1.1535 1.3891 -0.0642 0.0924 -0.0731 561 THR B N 11496 C CA . THR B 561 ? 1.3321 1.1283 1.3731 -0.0308 0.1156 -0.0854 561 THR B CA 11497 C C . THR B 561 ? 1.3734 1.1241 1.3826 -0.0224 0.1126 -0.0856 561 THR B C 11498 O O . THR B 561 ? 1.5277 1.2984 1.5594 -0.0384 0.0974 -0.0775 561 THR B O 11499 C CB . THR B 561 ? 1.2298 1.0952 1.3360 -0.0080 0.1395 -0.0873 561 THR B CB 11500 O OG1 . THR B 561 ? 1.5177 1.4396 1.6668 -0.0225 0.1352 -0.0840 561 THR B OG1 11501 C CG2 . THR B 561 ? 1.2044 1.0462 1.2906 0.0234 0.1652 -0.0919 561 THR B CG2 11502 N N . THR B 562 ? 1.4023 1.0904 1.3564 0.0058 0.1290 -0.0929 562 THR B N 11503 C CA . THR B 562 ? 1.4379 1.0772 1.3553 0.0208 0.1309 -0.0936 562 THR B CA 11504 C C . THR B 562 ? 1.3538 1.0500 1.3308 0.0505 0.1575 -0.0908 562 THR B C 11505 O O . THR B 562 ? 1.3676 1.0393 1.3295 0.0658 0.1627 -0.0895 562 THR B O 11506 C CB . THR B 562 ? 1.5265 1.0539 1.3370 0.0415 0.1358 -0.1000 562 THR B CB 11507 O OG1 . THR B 562 ? 1.5562 1.0361 1.3153 0.0193 0.1158 -0.1024 562 THR B OG1 11508 C CG2 . THR B 562 ? 2.0271 1.4811 1.7772 0.0398 0.1202 -0.1000 562 THR B CG2 11509 N N . ARG B 563 ? 1.2685 1.0380 1.3120 0.0569 0.1714 -0.0879 563 ARG B N 11510 C CA . ARG B 563 ? 1.2189 1.0423 1.3215 0.0811 0.1913 -0.0799 563 ARG B CA 11511 C C . ARG B 563 ? 1.1474 1.0116 1.2965 0.0689 0.1779 -0.0768 563 ARG B C 11512 O O . ARG B 563 ? 1.1228 1.0242 1.3024 0.0451 0.1609 -0.0774 563 ARG B O 11513 C CB . ARG B 563 ? 1.1314 1.0150 1.2876 0.0854 0.2021 -0.0749 563 ARG B CB 11514 C CG . ARG B 563 ? 1.3555 1.2092 1.4762 0.1068 0.2230 -0.0736 563 ARG B CG 11515 C CD . ARG B 563 ? 1.3335 1.2489 1.5092 0.1027 0.2275 -0.0686 563 ARG B CD 11516 N NE . ARG B 563 ? 1.1874 1.1712 1.4396 0.1084 0.2301 -0.0542 563 ARG B NE 11517 C CZ . ARG B 563 ? 0.9737 1.0118 1.2787 0.1039 0.2294 -0.0460 563 ARG B CZ 11518 N NH1 . ARG B 563 ? 0.9646 1.0020 1.2578 0.0962 0.2303 -0.0523 563 ARG B NH1 11519 N NH2 . ARG B 563 ? 0.8387 0.9275 1.2056 0.1054 0.2245 -0.0301 563 ARG B NH2 11520 N N . THR B 564 ? 1.2453 1.0998 1.3957 0.0886 0.1874 -0.0718 564 THR B N 11521 C CA . THR B 564 ? 1.2496 1.1418 1.4444 0.0821 0.1772 -0.0678 564 THR B CA 11522 C C . THR B 564 ? 1.1239 1.0751 1.3844 0.0966 0.1866 -0.0555 564 THR B C 11523 O O . THR B 564 ? 1.0465 1.0265 1.3425 0.0919 0.1761 -0.0513 564 THR B O 11524 C CB . THR B 564 ? 1.2703 1.1150 1.4276 0.0906 0.1767 -0.0683 564 THR B CB 11525 O OG1 . THR B 564 ? 1.3607 1.1772 1.4954 0.1254 0.2021 -0.0616 564 THR B OG1 11526 C CG2 . THR B 564 ? 1.2525 1.0360 1.3459 0.0689 0.1578 -0.0761 564 THR B CG2 11527 N N . ASP B 565 ? 1.1400 1.1066 1.4149 0.1133 0.2041 -0.0468 565 ASP B N 11528 C CA . ASP B 565 ? 1.1017 1.1221 1.4404 0.1266 0.2110 -0.0266 565 ASP B CA 11529 C C . ASP B 565 ? 0.9851 1.0530 1.3722 0.1037 0.1880 -0.0261 565 ASP B C 11530 O O . ASP B 565 ? 1.0630 1.1641 1.4961 0.1045 0.1790 -0.0112 565 ASP B O 11531 C CB . ASP B 565 ? 1.1700 1.1983 1.5138 0.1509 0.2364 -0.0115 565 ASP B CB 11532 C CG . ASP B 565 ? 1.1752 1.2114 1.5149 0.1367 0.2329 -0.0205 565 ASP B CG 11533 O OD1 . ASP B 565 ? 1.4119 1.3988 1.6915 0.1349 0.2367 -0.0359 565 ASP B OD1 11534 O OD2 . ASP B 565 ? 0.9438 1.0313 1.3373 0.1262 0.2235 -0.0110 565 ASP B OD2 11535 N N . THR B 566 ? 0.9726 1.0381 1.3436 0.0841 0.1770 -0.0404 566 THR B N 11536 C CA . THR B 566 ? 0.8799 0.9771 1.2796 0.0671 0.1569 -0.0411 566 THR B CA 11537 C C . THR B 566 ? 0.8255 0.9147 1.2162 0.0576 0.1406 -0.0471 566 THR B C 11538 O O . THR B 566 ? 0.8084 0.9120 1.2106 0.0495 0.1243 -0.0466 566 THR B O 11539 C CB . THR B 566 ? 0.8602 0.9603 1.2459 0.0543 0.1548 -0.0507 566 THR B CB 11540 O OG1 . THR B 566 ? 1.1352 1.2047 1.4782 0.0444 0.1541 -0.0624 566 THR B OG1 11541 C CG2 . THR B 566 ? 0.7903 0.8989 1.1847 0.0647 0.1713 -0.0442 566 THR B CG2 11542 N N . CYS B 567 ? 0.9061 0.9664 1.2696 0.0606 0.1451 -0.0515 567 CYS B N 11543 C CA . CYS B 567 ? 0.9944 1.0480 1.3502 0.0538 0.1324 -0.0540 567 CYS B CA 11544 C C . CYS B 567 ? 1.2145 1.2711 1.5912 0.0652 0.1303 -0.0456 567 CYS B C 11545 O O . CYS B 567 ? 1.4820 1.5320 1.8532 0.0625 0.1205 -0.0467 567 CYS B O 11546 C CB . CYS B 567 ? 0.9366 0.9569 1.2517 0.0453 0.1329 -0.0604 567 CYS B CB 11547 S SG . CYS B 567 ? 1.5335 1.5518 1.8267 0.0262 0.1287 -0.0641 567 CYS B SG 11548 N N . MET B 568 ? 1.1820 1.2515 1.5850 0.0789 0.1403 -0.0335 568 MET B N 11549 C CA . MET B 568 ? 1.2013 1.2778 1.6293 0.0907 0.1399 -0.0197 568 MET B CA 11550 C C . MET B 568 ? 1.1385 1.2395 1.6019 0.0820 0.1161 -0.0092 568 MET B C 11551 O O . MET B 568 ? 0.9939 1.1179 1.4839 0.0766 0.1073 0.0007 568 MET B O 11552 C CB . MET B 568 ? 1.3610 1.4458 1.8055 0.1128 0.1629 -0.0025 568 MET B CB 11553 C CG . MET B 568 ? 1.5498 1.5908 1.9410 0.1267 0.1855 -0.0125 568 MET B CG 11554 S SD . MET B 568 ? 1.6184 1.6101 1.9636 0.1304 0.1850 -0.0230 568 MET B SD 11555 C CE . MET B 568 ? 1.4646 1.4764 1.8471 0.1593 0.2007 0.0033 568 MET B CE 11556 N N . SER B 569 ? 1.3492 1.4387 1.8072 0.0802 0.1031 -0.0107 569 SER B N 11557 C CA . SER B 569 ? 1.1859 1.2815 1.6624 0.0727 0.0762 -0.0011 569 SER B CA 11558 C C . SER B 569 ? 1.1968 1.3189 1.7241 0.0772 0.0707 0.0267 569 SER B C 11559 O O . SER B 569 ? 1.2846 1.4203 1.8308 0.0925 0.0933 0.0388 569 SER B O 11560 C CB . SER B 569 ? 1.2078 1.2785 1.6572 0.0722 0.0658 -0.0102 569 SER B CB 11561 O OG . SER B 569 ? 1.1708 1.2342 1.6260 0.0668 0.0376 -0.0010 569 SER B OG 11562 N N . SER B 570 ? 1.3297 1.4558 1.8756 0.0647 0.0396 0.0403 570 SER B N 11563 C CA . SER B 570 ? 1.3097 1.4657 1.9118 0.0629 0.0259 0.0751 570 SER B CA 11564 C C . SER B 570 ? 1.1650 1.3247 1.7831 0.0751 0.0343 0.0864 570 SER B C 11565 O O . SER B 570 ? 0.9704 1.1661 1.6400 0.0840 0.0420 0.1186 570 SER B O 11566 C CB . SER B 570 ? 1.4256 1.5672 2.0292 0.0419 -0.0193 0.0863 570 SER B CB 11567 O OG . SER B 570 ? 1.3971 1.5323 1.9835 0.0322 -0.0274 0.0776 570 SER B OG 11568 N N . ASN B 571 ? 1.2147 1.3401 1.7904 0.0773 0.0341 0.0635 571 ASN B N 11569 C CA . ASN B 571 ? 1.2951 1.4185 1.8788 0.0888 0.0420 0.0705 571 ASN B CA 11570 C C . ASN B 571 ? 1.4343 1.5644 2.0162 0.1111 0.0817 0.0700 571 ASN B C 11571 O O . ASN B 571 ? 1.4759 1.6111 2.0725 0.1262 0.0937 0.0841 571 ASN B O 11572 C CB . ASN B 571 ? 1.3971 1.4806 1.9335 0.0851 0.0305 0.0471 571 ASN B CB 11573 C CG . ASN B 571 ? 1.5062 1.5678 1.9936 0.0853 0.0455 0.0181 571 ASN B CG 11574 O OD1 . ASN B 571 ? 1.5294 1.5947 2.0093 0.0921 0.0708 0.0108 571 ASN B OD1 11575 N ND2 . ASN B 571 ? 1.4806 1.5165 1.9317 0.0790 0.0291 0.0050 571 ASN B ND2 11576 N N . GLY B 572 ? 1.5025 1.6257 2.0593 0.1144 0.1011 0.0545 572 GLY B N 11577 C CA . GLY B 572 ? 1.5109 1.6234 2.0479 0.1364 0.1358 0.0526 572 GLY B CA 11578 C C . GLY B 572 ? 1.4562 1.5217 1.9302 0.1347 0.1436 0.0222 572 GLY B C 11579 O O . GLY B 572 ? 1.6255 1.6652 2.0640 0.1474 0.1657 0.0151 572 GLY B O 11580 N N . LEU B 573 ? 1.2255 1.2763 1.6825 0.1193 0.1237 0.0075 573 LEU B N 11581 C CA . LEU B 573 ? 1.3804 1.3949 1.7872 0.1133 0.1264 -0.0138 573 LEU B CA 11582 C C . LEU B 573 ? 1.4183 1.4314 1.8056 0.0986 0.1230 -0.0267 573 LEU B C 11583 O O . LEU B 573 ? 1.2737 1.3091 1.6801 0.0900 0.1110 -0.0248 573 LEU B O 11584 C CB . LEU B 573 ? 1.4219 1.4270 1.8223 0.1066 0.1101 -0.0181 573 LEU B CB 11585 C CG . LEU B 573 ? 1.5129 1.4856 1.8705 0.1007 0.1119 -0.0313 573 LEU B CG 11586 C CD1 . LEU B 573 ? 1.4805 1.4202 1.8100 0.1134 0.1293 -0.0321 573 LEU B CD1 11587 C CD2 . LEU B 573 ? 1.4285 1.3978 1.7854 0.0974 0.0979 -0.0312 573 LEU B CD2 11588 N N . LEU B 574 ? 1.3798 1.3626 1.7260 0.0950 0.1310 -0.0378 574 LEU B N 11589 C CA . LEU B 574 ? 1.2270 1.2099 1.5564 0.0800 0.1276 -0.0461 574 LEU B CA 11590 C C . LEU B 574 ? 1.2792 1.2784 1.6133 0.0665 0.1115 -0.0476 574 LEU B C 11591 O O . LEU B 574 ? 1.5242 1.5141 1.8480 0.0635 0.1049 -0.0469 574 LEU B O 11592 C CB . LEU B 574 ? 1.4018 1.3410 1.6821 0.0750 0.1325 -0.0533 574 LEU B CB 11593 C CG . LEU B 574 ? 1.2932 1.2299 1.5557 0.0583 0.1283 -0.0580 574 LEU B CG 11594 C CD1 . LEU B 574 ? 1.5463 1.4888 1.8136 0.0685 0.1420 -0.0586 574 LEU B CD1 11595 C CD2 . LEU B 574 ? 1.1715 1.0600 1.3839 0.0444 0.1201 -0.0604 574 LEU B CD2 11596 N N . CYS B 575 ? 1.1075 1.1288 1.4539 0.0615 0.1071 -0.0477 575 CYS B N 11597 C CA . CYS B 575 ? 1.0071 1.0393 1.3488 0.0560 0.0963 -0.0466 575 CYS B CA 11598 C C . CYS B 575 ? 0.9544 0.9821 1.2981 0.0634 0.0853 -0.0427 575 CYS B C 11599 O O . CYS B 575 ? 0.9489 0.9744 1.2761 0.0646 0.0814 -0.0397 575 CYS B O 11600 C CB . CYS B 575 ? 0.9557 0.9843 1.2759 0.0448 0.0979 -0.0450 575 CYS B CB 11601 S SG . CYS B 575 ? 1.3840 1.4147 1.6954 0.0324 0.1039 -0.0480 575 CYS B SG 11602 N N . SER B 576 ? 0.9754 1.0020 1.3392 0.0700 0.0812 -0.0391 576 SER B N 11603 C CA . SER B 576 ? 1.1294 1.1467 1.4946 0.0755 0.0670 -0.0343 576 SER B CA 11604 C C . SER B 576 ? 1.2930 1.2965 1.6394 0.0779 0.0703 -0.0359 576 SER B C 11605 O O . SER B 576 ? 1.4864 1.4786 1.8219 0.0835 0.0598 -0.0332 576 SER B O 11606 C CB . SER B 576 ? 0.9594 0.9692 1.3092 0.0763 0.0497 -0.0331 576 SER B CB 11607 O OG . SER B 576 ? 0.9542 0.9751 1.3188 0.0710 0.0443 -0.0309 576 SER B OG 11608 N N . GLY B 577 ? 1.2328 1.2317 1.5707 0.0732 0.0827 -0.0389 577 GLY B N 11609 C CA . GLY B 577 ? 1.1397 1.1256 1.4609 0.0711 0.0831 -0.0371 577 GLY B CA 11610 C C . GLY B 577 ? 1.0080 1.0036 1.3157 0.0678 0.0805 -0.0301 577 GLY B C 11611 O O . GLY B 577 ? 1.1250 1.1173 1.4238 0.0638 0.0804 -0.0224 577 GLY B O 11612 N N . ARG B 578 ? 0.9877 0.9959 1.2940 0.0709 0.0791 -0.0291 578 ARG B N 11613 C CA . ARG B 578 ? 1.0010 1.0193 1.2920 0.0766 0.0809 -0.0177 578 ARG B CA 11614 C C . ARG B 578 ? 1.0086 1.0482 1.3022 0.0647 0.0878 -0.0090 578 ARG B C 11615 O O . ARG B 578 ? 1.0081 1.0646 1.2946 0.0713 0.0927 0.0068 578 ARG B O 11616 C CB . ARG B 578 ? 0.9967 1.0047 1.2711 0.0918 0.0742 -0.0194 578 ARG B CB 11617 C CG . ARG B 578 ? 1.0089 0.9901 1.2730 0.1024 0.0612 -0.0223 578 ARG B CG 11618 C CD . ARG B 578 ? 1.0426 0.9965 1.2671 0.1197 0.0516 -0.0198 578 ARG B CD 11619 N NE . ARG B 578 ? 1.0600 0.9944 1.2842 0.1151 0.0318 -0.0264 578 ARG B NE 11620 C CZ . ARG B 578 ? 1.1008 1.0035 1.3143 0.1171 0.0099 -0.0263 578 ARG B CZ 11621 N NH1 . ARG B 578 ? 1.2992 1.1842 1.4977 0.1264 0.0079 -0.0236 578 ARG B NH1 11622 N NH2 . ARG B 578 ? 1.1195 1.0082 1.3382 0.1080 -0.0125 -0.0259 578 ARG B NH2 11623 N N . GLY B 579 ? 1.1231 1.1599 1.4240 0.0492 0.0886 -0.0163 579 GLY B N 11624 C CA . GLY B 579 ? 1.2067 1.2585 1.5078 0.0345 0.0904 -0.0076 579 GLY B CA 11625 C C . GLY B 579 ? 1.1565 1.1870 1.4501 0.0173 0.0878 -0.0149 579 GLY B C 11626 O O . GLY B 579 ? 1.2281 1.2311 1.5139 0.0203 0.0882 -0.0261 579 GLY B O 11627 N N . LYS B 580 ? 1.1442 1.1830 1.4349 0.0013 0.0852 -0.0066 580 LYS B N 11628 C CA . LYS B 580 ? 1.2839 1.2898 1.5531 -0.0151 0.0795 -0.0127 580 LYS B CA 11629 C C . LYS B 580 ? 1.2442 1.2551 1.5133 -0.0152 0.0857 -0.0224 580 LYS B C 11630 O O . LYS B 580 ? 1.1736 1.2187 1.4593 -0.0145 0.0887 -0.0155 580 LYS B O 11631 C CB . LYS B 580 ? 1.3445 1.3450 1.6042 -0.0407 0.0633 0.0092 580 LYS B CB 11632 C CG . LYS B 580 ? 1.4645 1.4624 1.7265 -0.0429 0.0559 0.0228 580 LYS B CG 11633 C CD . LYS B 580 ? 1.6161 1.5681 1.8546 -0.0328 0.0574 0.0032 580 LYS B CD 11634 C CE . LYS B 580 ? 1.5161 1.4666 1.7580 -0.0340 0.0505 0.0155 580 LYS B CE 11635 N NZ . LYS B 580 ? 1.3194 1.2274 1.5393 -0.0211 0.0541 -0.0025 580 LYS B NZ 11636 N N . CYS B 581 ? 1.2061 1.1804 1.4527 -0.0131 0.0893 -0.0367 581 CYS B N 11637 C CA . CYS B 581 ? 1.1506 1.1271 1.3957 -0.0108 0.0970 -0.0454 581 CYS B CA 11638 C C . CYS B 581 ? 1.1934 1.1482 1.4111 -0.0331 0.0860 -0.0398 581 CYS B C 11639 O O . CYS B 581 ? 1.2671 1.1689 1.4429 -0.0429 0.0762 -0.0406 581 CYS B O 11640 C CB . CYS B 581 ? 1.1371 1.0885 1.3726 0.0088 0.1106 -0.0582 581 CYS B CB 11641 S SG . CYS B 581 ? 1.4693 1.4244 1.7043 0.0153 0.1230 -0.0653 581 CYS B SG 11642 N N . GLU B 582 ? 1.1450 1.1351 1.3814 -0.0413 0.0855 -0.0330 582 GLU B N 11643 C CA . GLU B 582 ? 1.1772 1.1528 1.3935 -0.0649 0.0724 -0.0240 582 GLU B CA 11644 C C . GLU B 582 ? 1.1333 1.1274 1.3580 -0.0611 0.0821 -0.0318 582 GLU B C 11645 O O . GLU B 582 ? 1.0481 1.0892 1.3060 -0.0514 0.0912 -0.0298 582 GLU B O 11646 C CB . GLU B 582 ? 1.3328 1.3414 1.5694 -0.0854 0.0575 0.0049 582 GLU B CB 11647 C CG . GLU B 582 ? 1.6455 1.6313 1.8708 -0.0962 0.0426 0.0175 582 GLU B CG 11648 C CD . GLU B 582 ? 1.7926 1.8191 2.0456 -0.1170 0.0279 0.0550 582 GLU B CD 11649 O OE1 . GLU B 582 ? 1.6629 1.7411 1.9467 -0.1165 0.0343 0.0718 582 GLU B OE1 11650 O OE2 . GLU B 582 ? 1.8016 1.8099 2.0467 -0.1327 0.0105 0.0713 582 GLU B OE2 11651 N N . CYS B 583 ? 1.2490 1.1983 1.4356 -0.0672 0.0794 -0.0407 583 CYS B N 11652 C CA . CYS B 583 ? 1.1763 1.1359 1.3652 -0.0636 0.0887 -0.0487 583 CYS B CA 11653 C C . CYS B 583 ? 1.1081 1.0992 1.3285 -0.0375 0.1096 -0.0606 583 CYS B C 11654 O O . CYS B 583 ? 1.2354 1.2634 1.4811 -0.0355 0.1150 -0.0608 583 CYS B O 11655 C CB . CYS B 583 ? 1.1151 1.1163 1.3271 -0.0832 0.0791 -0.0317 583 CYS B CB 11656 S SG . CYS B 583 ? 1.3837 1.3471 1.5606 -0.1213 0.0483 -0.0113 583 CYS B SG 11657 N N . GLY B 584 ? 1.1114 1.0866 1.3301 -0.0188 0.1189 -0.0674 584 GLY B N 11658 C CA . GLY B 584 ? 1.0163 1.0189 1.2673 0.0025 0.1338 -0.0719 584 GLY B CA 11659 C C . GLY B 584 ? 0.9601 1.0083 1.2511 0.0044 0.1293 -0.0672 584 GLY B C 11660 O O . GLY B 584 ? 1.0481 1.1183 1.3658 0.0157 0.1338 -0.0677 584 GLY B O 11661 N N . SER B 585 ? 0.9529 1.0111 1.2440 -0.0058 0.1191 -0.0593 585 SER B N 11662 C CA . SER B 585 ? 0.8949 0.9830 1.2075 0.0014 0.1160 -0.0539 585 SER B CA 11663 C C . SER B 585 ? 0.9038 0.9885 1.2129 0.0012 0.1102 -0.0452 585 SER B C 11664 O O . SER B 585 ? 0.9838 1.0636 1.2822 -0.0127 0.1045 -0.0348 585 SER B O 11665 C CB . SER B 585 ? 0.8792 0.9935 1.1958 -0.0034 0.1154 -0.0474 585 SER B CB 11666 O OG . SER B 585 ? 1.0787 1.1976 1.4004 -0.0027 0.1201 -0.0556 585 SER B OG 11667 N N . CYS B 586 ? 0.8853 0.9716 1.2036 0.0150 0.1090 -0.0467 586 CYS B N 11668 C CA . CYS B 586 ? 0.9067 0.9892 1.2211 0.0180 0.1048 -0.0388 586 CYS B CA 11669 C C . CYS B 586 ? 0.9292 1.0341 1.2413 0.0186 0.1045 -0.0221 586 CYS B C 11670 O O . CYS B 586 ? 0.8715 0.9900 1.1817 0.0283 0.1073 -0.0196 586 CYS B O 11671 C CB . CYS B 586 ? 0.8857 0.9612 1.2075 0.0328 0.1016 -0.0436 586 CYS B CB 11672 S SG . CYS B 586 ? 1.6747 1.7317 2.0064 0.0372 0.1052 -0.0514 586 CYS B SG 11673 N N . VAL B 587 ? 0.9291 1.0366 1.2396 0.0097 0.1015 -0.0070 587 VAL B N 11674 C CA . VAL B 587 ? 0.9198 1.0554 1.2342 0.0152 0.1045 0.0179 587 VAL B CA 11675 C C . VAL B 587 ? 0.9807 1.1092 1.2909 0.0292 0.1045 0.0232 587 VAL B C 11676 O O . VAL B 587 ? 1.0799 1.1967 1.3920 0.0183 0.0981 0.0259 587 VAL B O 11677 C CB . VAL B 587 ? 0.9290 1.0824 1.2527 -0.0084 0.0983 0.0417 587 VAL B CB 11678 C CG1 . VAL B 587 ? 0.9022 1.0969 1.2390 0.0015 0.1055 0.0766 587 VAL B CG1 11679 C CG2 . VAL B 587 ? 0.9587 1.1109 1.2810 -0.0236 0.0959 0.0344 587 VAL B CG2 11680 N N . CYS B 588 ? 1.0310 1.1592 1.3284 0.0540 0.1103 0.0243 588 CYS B N 11681 C CA . CYS B 588 ? 1.1891 1.3006 1.4746 0.0703 0.1091 0.0249 588 CYS B CA 11682 C C . CYS B 588 ? 1.3623 1.4959 1.6522 0.0753 0.1153 0.0546 588 CYS B C 11683 O O . CYS B 588 ? 1.3843 1.5460 1.6743 0.0863 0.1262 0.0801 588 CYS B O 11684 C CB . CYS B 588 ? 0.9783 1.0667 1.2345 0.0954 0.1086 0.0166 588 CYS B CB 11685 S SG . CYS B 588 ? 1.8847 1.9515 2.1426 0.0879 0.0964 -0.0098 588 CYS B SG 11686 N N . ILE B 589 ? 1.1887 1.3118 1.4842 0.0685 0.1093 0.0548 589 ILE B N 11687 C CA . ILE B 589 ? 1.1496 1.2918 1.4499 0.0760 0.1143 0.0842 589 ILE B CA 11688 C C . ILE B 589 ? 1.3013 1.4147 1.5840 0.0935 0.1127 0.0734 589 ILE B C 11689 O O . ILE B 589 ? 1.4413 1.5333 1.7289 0.0806 0.1026 0.0568 589 ILE B O 11690 C CB . ILE B 589 ? 1.1558 1.3151 1.4815 0.0445 0.1040 0.1034 589 ILE B CB 11691 C CG1 . ILE B 589 ? 1.1107 1.2321 1.4310 0.0220 0.0897 0.0748 589 ILE B CG1 11692 C CG2 . ILE B 589 ? 1.1383 1.3356 1.4831 0.0306 0.1051 0.1304 589 ILE B CG2 11693 C CD1 . ILE B 589 ? 1.2137 1.3286 1.5333 0.0021 0.0841 0.0641 589 ILE B CD1 11694 N N . GLN B 590 ? 1.3196 1.4287 1.5765 0.1254 0.1233 0.0851 590 GLN B N 11695 C CA . GLN B 590 ? 1.3031 1.3749 1.5311 0.1460 0.1199 0.0740 590 GLN B CA 11696 C C . GLN B 590 ? 1.3851 1.4468 1.5705 0.1857 0.1347 0.0927 590 GLN B C 11697 O O . GLN B 590 ? 1.2972 1.3810 1.4779 0.1973 0.1482 0.1108 590 GLN B O 11698 C CB . GLN B 590 ? 1.1142 1.1480 1.3326 0.1395 0.1040 0.0399 590 GLN B CB 11699 C CG . GLN B 590 ? 1.1919 1.2143 1.4309 0.1220 0.0929 0.0252 590 GLN B CG 11700 C CD . GLN B 590 ? 1.5174 1.5064 1.7333 0.1387 0.0852 0.0201 590 GLN B CD 11701 O OE1 . GLN B 590 ? 1.3807 1.3367 1.5683 0.1513 0.0749 0.0102 590 GLN B OE1 11702 N NE2 . GLN B 590 ? 1.8089 1.8018 2.0337 0.1369 0.0869 0.0281 590 GLN B NE2 11703 N N . PRO B 591 ? 1.5765 1.6003 1.7250 0.2095 0.1330 0.0900 591 PRO B N 11704 C CA . PRO B 591 ? 1.6818 1.6784 1.7709 0.2538 0.1477 0.1064 591 PRO B CA 11705 C C . PRO B 591 ? 1.5516 1.5021 1.5917 0.2664 0.1396 0.0876 591 PRO B C 11706 O O . PRO B 591 ? 1.7325 1.6188 1.7221 0.2774 0.1219 0.0684 591 PRO B O 11707 C CB . PRO B 591 ? 1.8833 1.8385 1.9398 0.2712 0.1419 0.1026 591 PRO B CB 11708 C CG . PRO B 591 ? 1.7829 1.7345 1.8773 0.2352 0.1194 0.0759 591 PRO B CG 11709 C CD . PRO B 591 ? 1.6142 1.6209 1.7706 0.2009 0.1217 0.0796 591 PRO B CD 11710 N N . GLY B 592 ? 1.3822 1.3632 1.4366 0.2624 0.1494 0.0953 592 GLY B N 11711 C CA . GLY B 592 ? 1.5382 1.4780 1.5447 0.2754 0.1434 0.0816 592 GLY B CA 11712 C C . GLY B 592 ? 1.4128 1.3222 1.4266 0.2463 0.1136 0.0472 592 GLY B C 11713 O O . GLY B 592 ? 1.4335 1.2770 1.3911 0.2579 0.0942 0.0329 592 GLY B O 11714 N N . SER B 593 ? 1.1933 1.1475 1.2733 0.2090 0.1087 0.0373 593 SER B N 11715 C CA . SER B 593 ? 1.1076 1.0463 1.2047 0.1837 0.0860 0.0121 593 SER B CA 11716 C C . SER B 593 ? 1.0700 1.0359 1.1877 0.1703 0.0906 0.0090 593 SER B C 11717 O O . SER B 593 ? 1.1383 1.1481 1.2792 0.1676 0.1089 0.0240 593 SER B O 11718 C CB . SER B 593 ? 1.1838 1.1421 1.3316 0.1575 0.0783 0.0026 593 SER B CB 11719 O OG . SER B 593 ? 1.1960 1.2033 1.3873 0.1405 0.0927 0.0113 593 SER B OG 11720 N N . TYR B 594 ? 1.0783 1.0189 1.1892 0.1604 0.0717 -0.0072 594 TYR B N 11721 C CA . TYR B 594 ? 1.0588 1.0214 1.1871 0.1481 0.0746 -0.0114 594 TYR B CA 11722 C C . TYR B 594 ? 1.0663 1.0220 1.2207 0.1254 0.0535 -0.0269 594 TYR B C 11723 O O . TYR B 594 ? 1.0830 1.0230 1.2487 0.1178 0.0372 -0.0314 594 TYR B O 11724 C CB . TYR B 594 ? 1.0898 1.0249 1.1608 0.1745 0.0802 -0.0039 594 TYR B CB 11725 C CG . TYR B 594 ? 1.1572 1.0156 1.1570 0.1940 0.0581 -0.0095 594 TYR B CG 11726 C CD1 . TYR B 594 ? 1.2015 1.0228 1.1852 0.1813 0.0303 -0.0218 594 TYR B CD1 11727 C CD2 . TYR B 594 ? 1.1840 1.0020 1.1282 0.2245 0.0622 0.0002 594 TYR B CD2 11728 C CE1 . TYR B 594 ? 1.2610 1.0007 1.1715 0.1947 0.0022 -0.0247 594 TYR B CE1 11729 C CE2 . TYR B 594 ? 1.2456 0.9784 1.1108 0.2424 0.0378 -0.0052 594 TYR B CE2 11730 C CZ . TYR B 594 ? 1.2830 0.9736 1.1295 0.2256 0.0053 -0.0179 594 TYR B CZ 11731 O OH . TYR B 594 ? 1.3438 0.9385 1.1039 0.2391 -0.0267 -0.0212 594 TYR B OH 11732 N N . GLY B 595 ? 1.0504 1.0217 1.2175 0.1154 0.0547 -0.0309 595 GLY B N 11733 C CA . GLY B 595 ? 1.0468 1.0233 1.2473 0.0949 0.0392 -0.0391 595 GLY B CA 11734 C C . GLY B 595 ? 1.0022 1.0260 1.2544 0.0776 0.0558 -0.0419 595 GLY B C 11735 O O . GLY B 595 ? 1.1158 1.1615 1.3775 0.0766 0.0727 -0.0384 595 GLY B O 11736 N N . ASP B 596 ? 0.9693 1.0045 1.2510 0.0642 0.0493 -0.0453 596 ASP B N 11737 C CA . ASP B 596 ? 0.9120 0.9799 1.2304 0.0523 0.0653 -0.0482 596 ASP B CA 11738 C C . ASP B 596 ? 0.9778 1.0506 1.3140 0.0506 0.0734 -0.0480 596 ASP B C 11739 O O . ASP B 596 ? 1.3557 1.4376 1.6921 0.0461 0.0874 -0.0494 596 ASP B O 11740 C CB . ASP B 596 ? 1.1170 1.1954 1.4633 0.0437 0.0582 -0.0470 596 ASP B CB 11741 C CG . ASP B 596 ? 1.2274 1.2984 1.5545 0.0431 0.0492 -0.0479 596 ASP B CG 11742 O OD1 . ASP B 596 ? 1.3820 1.4491 1.6789 0.0501 0.0578 -0.0505 596 ASP B OD1 11743 O OD2 . ASP B 596 ? 1.1410 1.2113 1.4846 0.0359 0.0333 -0.0425 596 ASP B OD2 11744 N N . THR B 597 ? 1.0156 1.0783 1.3639 0.0530 0.0618 -0.0443 597 THR B N 11745 C CA . THR B 597 ? 0.9530 1.0161 1.3146 0.0545 0.0691 -0.0433 597 THR B CA 11746 C C . THR B 597 ? 1.0361 1.0816 1.3739 0.0616 0.0647 -0.0426 597 THR B C 11747 O O . THR B 597 ? 1.3096 1.3508 1.6549 0.0634 0.0671 -0.0414 597 THR B O 11748 C CB . THR B 597 ? 0.9641 1.0338 1.3601 0.0549 0.0619 -0.0340 597 THR B CB 11749 O OG1 . THR B 597 ? 1.3664 1.4213 1.7592 0.0537 0.0358 -0.0266 597 THR B OG1 11750 C CG2 . THR B 597 ? 1.0397 1.1317 1.4627 0.0522 0.0718 -0.0296 597 THR B CG2 11751 N N . CYS B 598 ? 0.9392 0.9726 1.2453 0.0688 0.0599 -0.0414 598 CYS B N 11752 C CA . CYS B 598 ? 0.9679 0.9825 1.2450 0.0814 0.0577 -0.0371 598 CYS B CA 11753 C C . CYS B 598 ? 1.0038 0.9914 1.2768 0.0853 0.0380 -0.0362 598 CYS B C 11754 O O . CYS B 598 ? 1.0134 0.9903 1.2787 0.0917 0.0380 -0.0339 598 CYS B O 11755 C CB . CYS B 598 ? 0.9459 0.9762 1.2310 0.0786 0.0728 -0.0332 598 CYS B CB 11756 S SG . CYS B 598 ? 1.3227 1.3819 1.6136 0.0678 0.0883 -0.0277 598 CYS B SG 11757 N N . GLU B 599 ? 1.0295 1.0063 1.3093 0.0792 0.0187 -0.0350 599 GLU B N 11758 C CA . GLU B 599 ? 1.0701 1.0209 1.3496 0.0775 -0.0074 -0.0287 599 GLU B CA 11759 C C . GLU B 599 ? 1.1304 1.0260 1.3455 0.0912 -0.0264 -0.0286 599 GLU B C 11760 O O . GLU B 599 ? 1.1814 1.0452 1.3817 0.0927 -0.0471 -0.0242 599 GLU B O 11761 C CB . GLU B 599 ? 1.0781 1.0410 1.3941 0.0624 -0.0254 -0.0195 599 GLU B CB 11762 C CG . GLU B 599 ? 1.1227 1.0646 1.4107 0.0590 -0.0416 -0.0199 599 GLU B CG 11763 C CD . GLU B 599 ? 1.1514 1.1217 1.4435 0.0602 -0.0159 -0.0286 599 GLU B CD 11764 O OE1 . GLU B 599 ? 1.1432 1.0964 1.4082 0.0601 -0.0250 -0.0302 599 GLU B OE1 11765 O OE2 . GLU B 599 ? 1.3006 1.3046 1.6183 0.0606 0.0110 -0.0330 599 GLU B OE2 11766 N N . LYS B 600 ? 1.1490 1.0288 1.3205 0.1036 -0.0186 -0.0319 600 LYS B N 11767 C CA . LYS B 600 ? 1.2099 1.0258 1.3038 0.1242 -0.0332 -0.0307 600 LYS B CA 11768 C C . LYS B 600 ? 1.2033 1.0149 1.2653 0.1491 -0.0097 -0.0273 600 LYS B C 11769 O O . LYS B 600 ? 1.1639 1.0112 1.2338 0.1576 0.0187 -0.0232 600 LYS B O 11770 C CB . LYS B 600 ? 1.2370 1.0301 1.2913 0.1302 -0.0371 -0.0322 600 LYS B CB 11771 C CG . LYS B 600 ? 1.2537 1.0411 1.3300 0.1065 -0.0663 -0.0313 600 LYS B CG 11772 C CD . LYS B 600 ? 1.4209 1.1770 1.4482 0.1140 -0.0716 -0.0336 600 LYS B CD 11773 C CE . LYS B 600 ? 1.5956 1.3448 1.6457 0.0878 -0.1050 -0.0288 600 LYS B CE 11774 N NZ . LYS B 600 ? 1.6581 1.3704 1.6554 0.0942 -0.1129 -0.0317 600 LYS B NZ 11775 N N . CYS B 601 ? 1.2317 1.0018 1.2604 0.1599 -0.0231 -0.0252 601 CYS B N 11776 C CA . CYS B 601 ? 1.2216 0.9810 1.2128 0.1878 -0.0025 -0.0180 601 CYS B CA 11777 C C . CYS B 601 ? 1.3298 1.0037 1.2371 0.2100 -0.0257 -0.0168 601 CYS B C 11778 O O . CYS B 601 ? 1.4061 1.0632 1.3142 0.2082 -0.0375 -0.0168 601 CYS B O 11779 C CB . CYS B 601 ? 1.1800 0.9899 1.2296 0.1772 0.0134 -0.0158 601 CYS B CB 11780 S SG . CYS B 601 ? 1.3343 1.1546 1.3593 0.2066 0.0433 0.0008 601 CYS B SG 11781 N N . PRO B 602 ? 1.3175 0.9296 1.1447 0.2322 -0.0334 -0.0158 602 PRO B N 11782 C CA . PRO B 602 ? 1.3715 0.8797 1.0958 0.2556 -0.0603 -0.0155 602 PRO B CA 11783 C C . PRO B 602 ? 1.3793 0.8689 1.0678 0.2858 -0.0428 -0.0075 602 PRO B C 11784 O O . PRO B 602 ? 1.4281 0.8561 1.0753 0.2869 -0.0709 -0.0101 602 PRO B O 11785 C CB . PRO B 602 ? 1.4102 0.8681 1.0542 0.2832 -0.0549 -0.0134 602 PRO B CB 11786 C CG . PRO B 602 ? 1.4481 0.9781 1.1659 0.2575 -0.0445 -0.0168 602 PRO B CG 11787 C CD . PRO B 602 ? 1.4351 1.0655 1.2570 0.2377 -0.0175 -0.0146 602 PRO B CD 11788 N N . THR B 603 ? 1.4481 0.9913 1.1542 0.3089 0.0012 0.0056 603 THR B N 11789 C CA . THR B 603 ? 1.3503 0.8913 1.0376 0.3357 0.0209 0.0181 603 THR B CA 11790 C C . THR B 603 ? 1.5060 1.1388 1.2982 0.3073 0.0361 0.0204 603 THR B C 11791 O O . THR B 603 ? 1.9720 1.6794 1.8219 0.3008 0.0636 0.0311 603 THR B O 11792 C CB . THR B 603 ? 1.4034 0.9378 1.0323 0.3867 0.0599 0.0412 603 THR B CB 11793 O OG1 . THR B 603 ? 1.3219 0.9542 1.0293 0.3768 0.0920 0.0554 603 THR B OG1 11794 C CG2 . THR B 603 ? 1.7004 1.1388 1.2169 0.4180 0.0482 0.0384 603 THR B CG2 11795 N N . CYS B 604 ? 1.5019 1.1223 1.3131 0.2899 0.0149 0.0116 604 CYS B N 11796 C CA . CYS B 604 ? 1.3800 1.0690 1.2744 0.2667 0.0259 0.0127 604 CYS B CA 11797 C C . CYS B 604 ? 1.3719 1.0227 1.2445 0.2729 0.0117 0.0114 604 CYS B C 11798 O O . CYS B 604 ? 1.4528 1.0262 1.2600 0.2821 -0.0167 0.0056 604 CYS B O 11799 C CB . CYS B 604 ? 1.3478 1.0822 1.3188 0.2254 0.0135 -0.0003 604 CYS B CB 11800 S SG . CYS B 604 ? 2.4023 2.2181 2.4373 0.2099 0.0425 0.0047 604 CYS B SG 11801 N N . PRO B 605 ? 1.2504 0.9495 1.1727 0.2666 0.0283 0.0179 605 PRO B N 11802 C CA . PRO B 605 ? 1.2485 0.9178 1.1620 0.2666 0.0128 0.0145 605 PRO B CA 11803 C C . PRO B 605 ? 1.2763 0.9233 1.2095 0.2379 -0.0239 -0.0003 605 PRO B C 11804 O O . PRO B 605 ? 1.4085 1.1030 1.4072 0.2097 -0.0253 -0.0060 605 PRO B O 11805 C CB . PRO B 605 ? 1.6319 1.3685 1.6123 0.2542 0.0347 0.0221 605 PRO B CB 11806 C CG . PRO B 605 ? 1.4546 1.2393 1.4495 0.2628 0.0642 0.0391 605 PRO B CG 11807 C CD . PRO B 605 ? 1.3045 1.0800 1.2856 0.2596 0.0585 0.0313 605 PRO B CD 11808 N N . ASP B 606 ? 1.3271 0.9013 1.2028 0.2458 -0.0538 -0.0025 606 ASP B N 11809 C CA . ASP B 606 ? 1.5540 1.1020 1.4424 0.2186 -0.0949 -0.0079 606 ASP B CA 11810 C C . ASP B 606 ? 1.7078 1.2778 1.6510 0.1984 -0.1079 -0.0067 606 ASP B C 11811 O O . ASP B 606 ? 1.8979 1.4588 1.8278 0.2119 -0.0996 -0.0049 606 ASP B O 11812 C CB . ASP B 606 ? 1.8265 1.2701 1.6129 0.2334 -0.1306 -0.0076 606 ASP B CB 11813 C CG . ASP B 606 ? 2.1396 1.5185 1.8649 0.2522 -0.1444 -0.0051 606 ASP B CG 11814 O OD1 . ASP B 606 ? 2.3386 1.6476 2.0233 0.2403 -0.1908 -0.0041 606 ASP B OD1 11815 O OD2 . ASP B 606 ? 2.1123 1.5097 1.8306 0.2773 -0.1111 -0.0015 606 ASP B OD2 11816 N N . ALA B 607 ? 1.6165 1.2189 1.6233 0.1684 -0.1258 -0.0047 607 ALA B N 11817 C CA . ALA B 607 ? 1.6156 1.2257 1.6655 0.1505 -0.1476 0.0028 607 ALA B CA 11818 C C . ALA B 607 ? 1.4438 1.0872 1.5232 0.1580 -0.1217 0.0009 607 ALA B C 11819 O O . ALA B 607 ? 1.2599 0.9633 1.3910 0.1544 -0.0904 -0.0022 607 ALA B O 11820 C CB . ALA B 607 ? 1.6547 1.1803 1.6402 0.1494 -0.1954 0.0093 607 ALA B CB 11821 N N . CYS B 608 ? 1.3331 0.9290 1.3725 0.1675 -0.1386 0.0034 608 CYS B N 11822 C CA . CYS B 608 ? 1.7061 1.3230 1.7682 0.1733 -0.1220 0.0033 608 CYS B CA 11823 C C . CYS B 608 ? 1.5673 1.2301 1.6454 0.1852 -0.0787 -0.0014 608 CYS B C 11824 O O . CYS B 608 ? 1.8638 1.5681 1.9907 0.1779 -0.0625 -0.0014 608 CYS B O 11825 C CB . CYS B 608 ? 1.9506 1.4948 1.9415 0.1899 -0.1434 0.0051 608 CYS B CB 11826 S SG . CYS B 608 ? 2.3711 1.8129 2.2599 0.1984 -0.1852 0.0062 608 CYS B SG 11827 N N . THR B 609 ? 1.2444 0.8972 1.2798 0.2032 -0.0620 -0.0020 609 THR B N 11828 C CA . THR B 609 ? 1.2807 0.9787 1.3330 0.2119 -0.0257 0.0016 609 THR B CA 11829 C C . THR B 609 ? 1.2411 1.0012 1.3652 0.1881 -0.0112 -0.0017 609 THR B C 11830 O O . THR B 609 ? 1.2155 1.0068 1.3652 0.1851 0.0073 0.0016 609 THR B O 11831 C CB . THR B 609 ? 1.2472 0.9349 1.2534 0.2332 -0.0104 0.0074 609 THR B CB 11832 O OG1 . THR B 609 ? 1.5146 1.2074 1.5307 0.2197 -0.0195 0.0011 609 THR B OG1 11833 C CG2 . THR B 609 ? 1.2496 0.8634 1.1669 0.2656 -0.0198 0.0121 609 THR B CG2 11834 N N . PHE B 610 ? 1.3037 1.0755 1.4541 0.1719 -0.0213 -0.0066 610 PHE B N 11835 C CA . PHE B 610 ? 1.3436 1.1627 1.5509 0.1538 -0.0079 -0.0095 610 PHE B CA 11836 C C . PHE B 610 ? 1.3241 1.1517 1.5688 0.1452 -0.0135 -0.0085 610 PHE B C 11837 O O . PHE B 610 ? 1.0902 0.9436 1.3642 0.1391 0.0032 -0.0101 610 PHE B O 11838 C CB . PHE B 610 ? 1.5588 1.3891 1.7798 0.1437 -0.0132 -0.0119 610 PHE B CB 11839 C CG . PHE B 610 ? 1.6018 1.4503 1.8124 0.1461 0.0053 -0.0131 610 PHE B CG 11840 C CD1 . PHE B 610 ? 1.6152 1.4385 1.7772 0.1620 0.0038 -0.0103 610 PHE B CD1 11841 C CD2 . PHE B 610 ? 1.5570 1.4426 1.8009 0.1342 0.0237 -0.0150 610 PHE B CD2 11842 C CE1 . PHE B 610 ? 1.6196 1.4656 1.7772 0.1654 0.0222 -0.0068 610 PHE B CE1 11843 C CE2 . PHE B 610 ? 1.6512 1.5551 1.8890 0.1335 0.0374 -0.0127 610 PHE B CE2 11844 C CZ . PHE B 610 ? 1.6739 1.5636 1.8738 0.1488 0.0376 -0.0073 610 PHE B CZ 11845 N N . LYS B 611 ? 1.4179 1.2187 1.6568 0.1454 -0.0386 -0.0038 611 LYS B N 11846 C CA . LYS B 611 ? 1.1672 0.9803 1.4461 0.1391 -0.0446 0.0028 611 LYS B CA 11847 C C . LYS B 611 ? 1.1397 0.9357 1.4022 0.1484 -0.0424 0.0022 611 LYS B C 11848 O O . LYS B 611 ? 1.1460 0.9499 1.4373 0.1461 -0.0452 0.0081 611 LYS B O 11849 C CB . LYS B 611 ? 1.1467 0.9480 1.4405 0.1290 -0.0773 0.0157 611 LYS B CB 11850 C CG . LYS B 611 ? 1.2990 1.1220 1.6172 0.1181 -0.0809 0.0203 611 LYS B CG 11851 C CD . LYS B 611 ? 1.3441 1.1616 1.6872 0.1037 -0.1173 0.0411 611 LYS B CD 11852 C CE . LYS B 611 ? 1.3020 1.1453 1.6734 0.0924 -0.1203 0.0488 611 LYS B CE 11853 N NZ . LYS B 611 ? 1.1232 1.0214 1.5436 0.0964 -0.0835 0.0491 611 LYS B NZ 11854 N N . LYS B 612 ? 1.2923 1.0672 1.5097 0.1612 -0.0355 -0.0018 612 LYS B N 11855 C CA . LYS B 612 ? 1.1265 0.8888 1.3280 0.1715 -0.0299 -0.0005 612 LYS B CA 11856 C C . LYS B 612 ? 1.0930 0.8886 1.3284 0.1648 -0.0078 -0.0019 612 LYS B C 11857 O O . LYS B 612 ? 1.0878 0.8802 1.3337 0.1657 -0.0078 -0.0006 612 LYS B O 11858 C CB . LYS B 612 ? 1.1703 0.9083 1.3173 0.1910 -0.0228 0.0020 612 LYS B CB 11859 C CG . LYS B 612 ? 1.3687 1.1035 1.5038 0.2027 -0.0114 0.0074 612 LYS B CG 11860 C CD . LYS B 612 ? 1.6033 1.3178 1.6849 0.2283 -0.0006 0.0170 612 LYS B CD 11861 C CE . LYS B 612 ? 1.6236 1.3689 1.7101 0.2288 0.0177 0.0228 612 LYS B CE 11862 N NZ . LYS B 612 ? 1.5720 1.2978 1.6039 0.2602 0.0312 0.0376 612 LYS B NZ 11863 N N . GLU B 613 ? 1.0832 0.9039 1.3297 0.1577 0.0085 -0.0041 613 GLU B N 11864 C CA . GLU B 613 ? 1.1030 0.9408 1.3681 0.1490 0.0243 -0.0053 613 GLU B CA 11865 C C . GLU B 613 ? 1.1584 0.9996 1.4522 0.1455 0.0247 -0.0076 613 GLU B C 11866 O O . GLU B 613 ? 1.3318 1.1685 1.6281 0.1447 0.0337 -0.0084 613 GLU B O 11867 C CB . GLU B 613 ? 1.3152 1.1718 1.5805 0.1401 0.0359 -0.0054 613 GLU B CB 11868 C CG . GLU B 613 ? 1.6038 1.4664 1.8468 0.1466 0.0405 0.0045 613 GLU B CG 11869 C CD . GLU B 613 ? 1.8876 1.7511 2.1231 0.1495 0.0457 0.0165 613 GLU B CD 11870 O OE1 . GLU B 613 ? 1.8736 1.7341 2.1202 0.1387 0.0461 0.0151 613 GLU B OE1 11871 O OE2 . GLU B 613 ? 2.0439 1.9085 2.2592 0.1647 0.0499 0.0295 613 GLU B OE2 11872 N N . CYS B 614 ? 1.2580 1.1055 1.5713 0.1450 0.0147 -0.0049 614 CYS B N 11873 C CA . CYS B 614 ? 1.1977 1.0576 1.5453 0.1462 0.0181 0.0017 614 CYS B CA 11874 C C . CYS B 614 ? 1.0639 0.9147 1.4208 0.1526 0.0103 0.0091 614 CYS B C 11875 O O . CYS B 614 ? 1.1525 1.0070 1.5235 0.1592 0.0235 0.0131 614 CYS B O 11876 C CB . CYS B 614 ? 1.0187 0.8961 1.3931 0.1419 0.0071 0.0105 614 CYS B CB 11877 S SG . CYS B 614 ? 2.2087 2.1048 2.5867 0.1368 0.0238 0.0046 614 CYS B SG 11878 N N . VAL B 615 ? 1.0439 0.8768 1.3865 0.1530 -0.0111 0.0116 615 VAL B N 11879 C CA . VAL B 615 ? 1.0426 0.8646 1.3925 0.1576 -0.0219 0.0193 615 VAL B CA 11880 C C . VAL B 615 ? 1.0690 0.8768 1.3951 0.1638 -0.0086 0.0110 615 VAL B C 11881 O O . VAL B 615 ? 1.4764 1.2780 1.8103 0.1688 -0.0103 0.0157 615 VAL B O 11882 C CB . VAL B 615 ? 1.0768 0.8716 1.4087 0.1552 -0.0545 0.0255 615 VAL B CB 11883 C CG1 . VAL B 615 ? 1.0722 0.8753 1.4234 0.1445 -0.0743 0.0362 615 VAL B CG1 11884 C CG2 . VAL B 615 ? 1.1987 0.9608 1.4740 0.1629 -0.0556 0.0142 615 VAL B CG2 11885 N N . GLU B 616 ? 1.0597 0.8650 1.3600 0.1624 0.0033 0.0024 616 GLU B N 11886 C CA . GLU B 616 ? 1.0731 0.8684 1.3541 0.1646 0.0127 0.0002 616 GLU B CA 11887 C C . GLU B 616 ? 1.0753 0.8712 1.3638 0.1612 0.0279 -0.0022 616 GLU B C 11888 O O . GLU B 616 ? 1.2122 0.9942 1.4940 0.1643 0.0302 -0.0015 616 GLU B O 11889 C CB . GLU B 616 ? 1.0888 0.8867 1.3449 0.1639 0.0178 0.0010 616 GLU B CB 11890 C CG . GLU B 616 ? 1.2190 1.0061 1.4534 0.1718 0.0188 0.0077 616 GLU B CG 11891 C CD . GLU B 616 ? 1.4043 1.1661 1.6197 0.1857 0.0040 0.0089 616 GLU B CD 11892 O OE1 . GLU B 616 ? 1.5629 1.3123 1.7647 0.1937 0.0044 0.0134 616 GLU B OE1 11893 O OE2 . GLU B 616 ? 1.2068 0.9564 1.4174 0.1874 -0.0107 0.0067 616 GLU B OE2 11894 N N . CYS B 617 ? 1.0754 0.8802 1.3702 0.1564 0.0374 -0.0051 617 CYS B N 11895 C CA . CYS B 617 ? 1.1267 0.9160 1.4113 0.1566 0.0510 -0.0079 617 CYS B CA 11896 C C . CYS B 617 ? 1.0849 0.8734 1.3883 0.1716 0.0583 -0.0019 617 CYS B C 11897 O O . CYS B 617 ? 1.1476 0.9113 1.4331 0.1797 0.0682 -0.0023 617 CYS B O 11898 C CB . CYS B 617 ? 1.1482 0.9397 1.4237 0.1483 0.0584 -0.0122 617 CYS B CB 11899 S SG . CYS B 617 ? 1.6019 1.4195 1.9087 0.1550 0.0633 -0.0092 617 CYS B SG 11900 N N . LYS B 618 ? 1.0547 0.8693 1.3932 0.1758 0.0525 0.0073 618 LYS B N 11901 C CA . LYS B 618 ? 1.0463 0.8736 1.4157 0.1906 0.0594 0.0230 618 LYS B CA 11902 C C . LYS B 618 ? 1.0672 0.8897 1.4460 0.1958 0.0495 0.0305 618 LYS B C 11903 O O . LYS B 618 ? 1.3889 1.1965 1.7593 0.2089 0.0627 0.0334 618 LYS B O 11904 C CB . LYS B 618 ? 1.0281 0.8903 1.4394 0.1884 0.0515 0.0378 618 LYS B CB 11905 C CG . LYS B 618 ? 1.0305 0.9030 1.4432 0.1920 0.0692 0.0379 618 LYS B CG 11906 C CD . LYS B 618 ? 1.2697 1.1395 1.6850 0.2159 0.0961 0.0505 618 LYS B CD 11907 C CE . LYS B 618 ? 1.4796 1.3585 1.8953 0.2239 0.1146 0.0543 618 LYS B CE 11908 N NZ . LYS B 618 ? 1.4568 1.3293 1.8687 0.2556 0.1447 0.0716 618 LYS B NZ 11909 N N . LYS B 619 ? 1.0329 0.8610 1.4221 0.1868 0.0253 0.0335 619 LYS B N 11910 C CA . LYS B 619 ? 1.0390 0.8610 1.4377 0.1902 0.0112 0.0425 619 LYS B CA 11911 C C . LYS B 619 ? 1.1767 0.9699 1.5387 0.1917 0.0142 0.0290 619 LYS B C 11912 O O . LYS B 619 ? 1.5191 1.3045 1.8844 0.2003 0.0178 0.0340 619 LYS B O 11913 C CB . LYS B 619 ? 1.0375 0.8602 1.4460 0.1798 -0.0206 0.0508 619 LYS B CB 11914 C CG . LYS B 619 ? 1.0952 0.9491 1.5552 0.1763 -0.0332 0.0769 619 LYS B CG 11915 C CD . LYS B 619 ? 1.2238 1.0958 1.7222 0.1867 -0.0291 0.1000 619 LYS B CD 11916 C CE . LYS B 619 ? 1.0963 1.0116 1.6577 0.1842 -0.0388 0.1362 619 LYS B CE 11917 N NZ . LYS B 619 ? 1.1609 1.1056 1.7417 0.1965 -0.0074 0.1425 619 LYS B NZ 11918 N N . PHE B 620 ? 1.0582 0.8389 1.3882 0.1841 0.0128 0.0159 620 PHE B N 11919 C CA . PHE B 620 ? 1.0721 0.8324 1.3733 0.1845 0.0144 0.0098 620 PHE B CA 11920 C C . PHE B 620 ? 1.0965 0.8452 1.3771 0.1803 0.0305 0.0035 620 PHE B C 11921 O O . PHE B 620 ? 1.1162 0.8497 1.3766 0.1776 0.0301 0.0027 620 PHE B O 11922 C CB . PHE B 620 ? 1.0801 0.8340 1.3580 0.1826 0.0033 0.0079 620 PHE B CB 11923 C CG . PHE B 620 ? 1.0815 0.8217 1.3561 0.1880 -0.0181 0.0131 620 PHE B CG 11924 C CD1 . PHE B 620 ? 1.0841 0.8237 1.3626 0.1848 -0.0350 0.0166 620 PHE B CD1 11925 C CD2 . PHE B 620 ? 1.0950 0.8164 1.3578 0.1948 -0.0247 0.0154 620 PHE B CD2 11926 C CE1 . PHE B 620 ? 1.1560 0.8695 1.4210 0.1867 -0.0618 0.0228 620 PHE B CE1 11927 C CE2 . PHE B 620 ? 1.1316 0.8301 1.3827 0.1987 -0.0486 0.0206 620 PHE B CE2 11928 C CZ . PHE B 620 ? 1.1851 0.8762 1.4346 0.1937 -0.0690 0.0246 620 PHE B CZ 11929 N N . ASP B 621 ? 1.1074 0.8588 1.3896 0.1791 0.0419 0.0012 621 ASP B N 11930 C CA . ASP B 621 ? 1.1462 0.8724 1.3971 0.1732 0.0515 -0.0042 621 ASP B CA 11931 C C . ASP B 621 ? 1.1736 0.8991 1.4069 0.1567 0.0436 -0.0038 621 ASP B C 11932 O O . ASP B 621 ? 1.3844 1.0872 1.5953 0.1493 0.0407 -0.0016 621 ASP B O 11933 C CB . ASP B 621 ? 1.4162 1.1103 1.6485 0.1838 0.0582 -0.0036 621 ASP B CB 11934 C CG . ASP B 621 ? 1.7054 1.3559 1.8923 0.1808 0.0655 -0.0089 621 ASP B CG 11935 O OD1 . ASP B 621 ? 1.5956 1.2172 1.7515 0.1672 0.0562 -0.0098 621 ASP B OD1 11936 O OD2 . ASP B 621 ? 1.9076 1.5485 2.0861 0.1922 0.0789 -0.0096 621 ASP B OD2 11937 N N . ARG B 622 ? 1.3173 1.0685 1.5616 0.1520 0.0397 -0.0020 622 ARG B N 11938 C CA . ARG B 622 ? 1.2291 0.9905 1.4646 0.1432 0.0354 0.0065 622 ARG B CA 11939 C C . ARG B 622 ? 1.3828 1.1618 1.6183 0.1318 0.0374 0.0099 622 ARG B C 11940 O O . ARG B 622 ? 1.4010 1.1788 1.6385 0.1284 0.0414 0.0023 622 ARG B O 11941 C CB . ARG B 622 ? 1.4246 1.1952 1.6631 0.1561 0.0302 0.0112 622 ARG B CB 11942 C CG . ARG B 622 ? 1.3470 1.1153 1.5743 0.1573 0.0292 0.0233 622 ARG B CG 11943 C CD . ARG B 622 ? 1.5061 1.2554 1.7317 0.1672 0.0247 0.0200 622 ARG B CD 11944 N NE . ARG B 622 ? 1.6865 1.4312 1.9111 0.1819 0.0171 0.0167 622 ARG B NE 11945 C CZ . ARG B 622 ? 1.4473 1.1845 1.6519 0.1952 0.0135 0.0237 622 ARG B CZ 11946 N NH1 . ARG B 622 ? 1.2286 0.9738 1.4223 0.1980 0.0214 0.0376 622 ARG B NH1 11947 N NH2 . ARG B 622 ? 1.3548 1.0730 1.5471 0.2062 0.0006 0.0201 622 ARG B NH2 11948 N N . GLY B 623 ? 1.5312 1.3288 1.7656 0.1286 0.0364 0.0245 623 GLY B N 11949 C CA . GLY B 623 ? 1.5054 1.3223 1.7415 0.1144 0.0373 0.0364 623 GLY B CA 11950 C C . GLY B 623 ? 1.5808 1.4102 1.8220 0.1109 0.0409 0.0295 623 GLY B C 11951 O O . GLY B 623 ? 1.7523 1.5868 1.9985 0.1236 0.0434 0.0194 623 GLY B O 11952 N N . ALA B 624 ? 1.4827 1.3123 1.7203 0.0907 0.0376 0.0368 624 ALA B N 11953 C CA . ALA B 624 ? 1.3403 1.1882 1.5832 0.0824 0.0398 0.0388 624 ALA B CA 11954 C C . ALA B 624 ? 1.3324 1.1659 1.5717 0.0844 0.0438 0.0178 624 ALA B C 11955 O O . ALA B 624 ? 1.5192 1.3580 1.7567 0.0730 0.0437 0.0184 624 ALA B O 11956 C CB . ALA B 624 ? 1.2447 1.1277 1.4985 0.0973 0.0473 0.0506 624 ALA B CB 11957 N N . LEU B 625 ? 1.4648 1.2834 1.7057 0.0991 0.0475 0.0033 625 LEU B N 11958 C CA . LEU B 625 ? 1.4477 1.2497 1.6840 0.1018 0.0536 -0.0093 625 LEU B CA 11959 C C . LEU B 625 ? 1.3973 1.1564 1.6075 0.1035 0.0547 -0.0134 625 LEU B C 11960 O O . LEU B 625 ? 1.2414 0.9754 1.4346 0.1101 0.0629 -0.0205 625 LEU B O 11961 C CB . LEU B 625 ? 1.4922 1.3122 1.7532 0.1176 0.0577 -0.0148 625 LEU B CB 11962 C CG . LEU B 625 ? 1.1392 0.9780 1.4105 0.1150 0.0610 -0.0178 625 LEU B CG 11963 C CD1 . LEU B 625 ? 1.1182 0.9761 1.3863 0.1053 0.0572 -0.0115 625 LEU B CD1 11964 C CD2 . LEU B 625 ? 1.0712 0.9264 1.3689 0.1263 0.0589 -0.0179 625 LEU B CD2 11965 N N . HIS B 626 ? 1.5019 1.2494 1.7043 0.1005 0.0478 -0.0073 626 HIS B N 11966 C CA . HIS B 626 ? 1.4176 1.1172 1.5873 0.1019 0.0463 -0.0101 626 HIS B CA 11967 C C . HIS B 626 ? 1.4542 1.1147 1.5840 0.0788 0.0331 -0.0049 626 HIS B C 11968 O O . HIS B 626 ? 1.7343 1.3365 1.8172 0.0806 0.0321 -0.0114 626 HIS B O 11969 C CB . HIS B 626 ? 1.4818 1.1844 1.6603 0.1074 0.0422 -0.0051 626 HIS B CB 11970 C CG . HIS B 626 ? 1.3603 1.0129 1.5050 0.1129 0.0420 -0.0086 626 HIS B CG 11971 N ND1 . HIS B 626 ? 1.5848 1.2126 1.7166 0.1344 0.0561 -0.0168 626 HIS B ND1 11972 C CD2 . HIS B 626 ? 1.3965 1.0178 1.5157 0.1015 0.0300 -0.0023 626 HIS B CD2 11973 C CE1 . HIS B 626 ? 1.8772 1.4556 1.9707 0.1387 0.0542 -0.0176 626 HIS B CE1 11974 N NE2 . HIS B 626 ? 1.7431 1.3146 1.8275 0.1168 0.0363 -0.0103 626 HIS B NE2 11975 N N . ASP B 627 ? 1.3826 1.0720 1.5275 0.0579 0.0217 0.0102 627 ASP B N 11976 C CA . ASP B 627 ? 1.4458 1.1056 1.5622 0.0287 0.0009 0.0247 627 ASP B CA 11977 C C . ASP B 627 ? 1.5047 1.1286 1.5866 0.0186 -0.0033 0.0174 627 ASP B C 11978 O O . ASP B 627 ? 1.6320 1.1939 1.6625 0.0000 -0.0224 0.0209 627 ASP B O 11979 C CB . ASP B 627 ? 1.4457 1.1606 1.6000 0.0123 -0.0074 0.0520 627 ASP B CB 11980 C CG . ASP B 627 ? 1.4557 1.2073 1.6404 0.0294 0.0015 0.0589 627 ASP B CG 11981 O OD1 . ASP B 627 ? 1.5124 1.2389 1.6857 0.0436 0.0054 0.0460 627 ASP B OD1 11982 O OD2 . ASP B 627 ? 1.3965 1.1990 1.6122 0.0312 0.0056 0.0788 627 ASP B OD2 11983 N N . GLU B 628 ? 1.4388 1.0949 1.5430 0.0304 0.0121 0.0080 628 GLU B N 11984 C CA . GLU B 628 ? 1.4702 1.0963 1.5437 0.0234 0.0106 0.0011 628 GLU B CA 11985 C C . GLU B 628 ? 1.4856 1.0647 1.5228 0.0503 0.0279 -0.0184 628 GLU B C 11986 O O . GLU B 628 ? 1.6998 1.2471 1.7042 0.0520 0.0313 -0.0254 628 GLU B O 11987 C CB . GLU B 628 ? 1.4733 1.1595 1.5891 0.0214 0.0180 0.0041 628 GLU B CB 11988 C CG . GLU B 628 ? 1.6827 1.4122 1.8268 -0.0026 0.0039 0.0296 628 GLU B CG 11989 C CD . GLU B 628 ? 1.7006 1.4838 1.8874 0.0100 0.0120 0.0407 628 GLU B CD 11990 O OE1 . GLU B 628 ? 1.7358 1.5078 1.9211 0.0257 0.0173 0.0325 628 GLU B OE1 11991 O OE2 . GLU B 628 ? 1.4940 1.3273 1.7112 0.0068 0.0141 0.0589 628 GLU B OE2 11992 N N . ASN B 629 ? 1.4507 1.0273 1.4943 0.0734 0.0404 -0.0236 629 ASN B N 11993 C CA . ASN B 629 ? 1.4506 0.9923 1.4678 0.1051 0.0614 -0.0339 629 ASN B CA 11994 C C . ASN B 629 ? 1.5033 1.0844 1.5527 0.1213 0.0807 -0.0374 629 ASN B C 11995 O O . ASN B 629 ? 1.5383 1.0883 1.5591 0.1453 0.0988 -0.0408 629 ASN B O 11996 C CB . ASN B 629 ? 1.6115 1.0560 1.5397 0.1053 0.0544 -0.0383 629 ASN B CB 11997 C CG . ASN B 629 ? 1.8574 1.2579 1.7490 0.1454 0.0791 -0.0435 629 ASN B CG 11998 O OD1 . ASN B 629 ? 1.9581 1.3944 1.8899 0.1653 0.0933 -0.0402 629 ASN B OD1 11999 N ND2 . ASN B 629 ? 1.8720 1.1923 1.6841 0.1596 0.0848 -0.0487 629 ASN B ND2 12000 N N . THR B 630 ? 1.6190 1.2660 1.7243 0.1104 0.0774 -0.0342 630 THR B N 12001 C CA . THR B 630 ? 1.4031 1.0901 1.5423 0.1209 0.0906 -0.0356 630 THR B CA 12002 C C . THR B 630 ? 1.4538 1.1855 1.6447 0.1397 0.0998 -0.0307 630 THR B C 12003 O O . THR B 630 ? 1.4830 1.2515 1.7089 0.1465 0.1065 -0.0276 630 THR B O 12004 C CB . THR B 630 ? 1.3035 1.0287 1.4658 0.0988 0.0799 -0.0338 630 THR B CB 12005 O OG1 . THR B 630 ? 1.4478 1.2132 1.6451 0.0927 0.0712 -0.0275 630 THR B OG1 12006 C CG2 . THR B 630 ? 1.3489 1.0359 1.4680 0.0748 0.0653 -0.0321 630 THR B CG2 12007 N N . CYS B 631 ? 1.4734 1.4889 1.6206 0.2173 0.1723 0.0825 631 CYS B N 12008 C CA . CYS B 631 ? 1.4858 1.4191 1.6439 0.2330 0.1459 0.0960 631 CYS B CA 12009 C C . CYS B 631 ? 1.4210 1.3538 1.6144 0.2171 0.1395 0.1191 631 CYS B C 12010 O O . CYS B 631 ? 1.4900 1.3881 1.6952 0.2239 0.1082 0.1432 631 CYS B O 12011 C CB . CYS B 631 ? 1.5072 1.3885 1.6450 0.2371 0.1619 0.0700 631 CYS B CB 12012 S SG . CYS B 631 ? 2.0751 1.8685 2.2228 0.2587 0.1281 0.0828 631 CYS B SG 12013 N N . ASN B 632 ? 1.4083 1.3815 1.6171 0.1928 0.1716 0.1078 632 ASN B N 12014 C CA . ASN B 632 ? 1.4436 1.4317 1.6899 0.1749 0.1705 0.1209 632 ASN B CA 12015 C C . ASN B 632 ? 1.5064 1.5362 1.7612 0.1557 0.1565 0.1504 632 ASN B C 12016 O O . ASN B 632 ? 1.5482 1.5829 1.8284 0.1377 0.1474 0.1655 632 ASN B O 12017 C CB . ASN B 632 ? 1.6037 1.6279 1.8639 0.1561 0.2114 0.0957 632 ASN B CB 12018 C CG . ASN B 632 ? 1.8414 1.8703 2.1441 0.1496 0.2090 0.0972 632 ASN B CG 12019 O OD1 . ASN B 632 ? 1.9701 2.0541 2.3001 0.1228 0.2109 0.1082 632 ASN B OD1 12020 N ND2 . ASN B 632 ? 1.8941 1.8705 2.2010 0.1741 0.2045 0.0846 632 ASN B ND2 12021 N N . ARG B 633 ? 1.5346 1.5964 1.7640 0.1591 0.1545 0.1577 633 ARG B N 12022 C CA . ARG B 633 ? 1.6278 1.7208 1.8511 0.1458 0.1389 0.1903 633 ARG B CA 12023 C C . ARG B 633 ? 1.6344 1.6580 1.8370 0.1731 0.0968 0.2179 633 ARG B C 12024 O O . ARG B 633 ? 1.6564 1.6419 1.8615 0.1605 0.0769 0.2446 633 ARG B O 12025 C CB . ARG B 633 ? 1.7120 1.8889 1.9179 0.1375 0.1586 0.1838 633 ARG B CB 12026 C CG . ARG B 633 ? 1.6907 1.8995 1.8796 0.1290 0.1396 0.2214 633 ARG B CG 12027 C CD . ARG B 633 ? 1.6817 1.9091 1.8891 0.0860 0.1473 0.2391 633 ARG B CD 12028 N NE . ARG B 633 ? 1.5327 1.8369 1.7656 0.0523 0.1904 0.2090 633 ARG B NE 12029 C CZ . ARG B 633 ? 1.4588 1.8539 1.6842 0.0262 0.2126 0.2060 633 ARG B CZ 12030 N NH1 . ARG B 633 ? 1.5217 1.9464 1.7136 0.0337 0.1924 0.2347 633 ARG B NH1 12031 N NH2 . ARG B 633 ? 1.3325 1.7890 1.5821 -0.0054 0.2544 0.1736 633 ARG B NH2 12032 N N . TYR B 634 ? 1.6483 1.6558 1.8283 0.2081 0.0857 0.2078 634 TYR B N 12033 C CA . TYR B 634 ? 1.5720 1.5155 1.7302 0.2400 0.0474 0.2295 634 TYR B CA 12034 C C . TYR B 634 ? 1.5234 1.3772 1.6901 0.2442 0.0266 0.2340 634 TYR B C 12035 O O . TYR B 634 ? 1.7020 1.4920 1.8517 0.2561 -0.0027 0.2580 634 TYR B O 12036 C CB . TYR B 634 ? 1.5408 1.5015 1.6798 0.2776 0.0432 0.2073 634 TYR B CB 12037 C CG . TYR B 634 ? 1.6078 1.6559 1.7321 0.2831 0.0490 0.2105 634 TYR B CG 12038 C CD1 . TYR B 634 ? 1.6801 1.7736 1.8023 0.2564 0.0538 0.2382 634 TYR B CD1 12039 C CD2 . TYR B 634 ? 1.7413 1.8357 1.8527 0.3133 0.0493 0.1837 634 TYR B CD2 12040 C CE1 . TYR B 634 ? 1.7319 1.9136 1.8383 0.2620 0.0569 0.2419 634 TYR B CE1 12041 C CE2 . TYR B 634 ? 1.7007 1.8906 1.8007 0.3202 0.0527 0.1837 634 TYR B CE2 12042 C CZ . TYR B 634 ? 1.6987 1.9310 1.7954 0.2959 0.0554 0.2144 634 TYR B CZ 12043 O OH . TYR B 634 ? 1.7311 2.0661 1.8143 0.3034 0.0567 0.2151 634 TYR B OH 12044 N N . CYS B 635 ? 1.4769 1.3233 1.6658 0.2354 0.0413 0.2106 635 CYS B N 12045 C CA . CYS B 635 ? 1.5020 1.2821 1.7027 0.2348 0.0220 0.2138 635 CYS B CA 12046 C C . CYS B 635 ? 1.4835 1.2887 1.7145 0.1981 0.0316 0.2211 635 CYS B C 12047 O O . CYS B 635 ? 1.4794 1.3238 1.7348 0.1888 0.0548 0.2008 635 CYS B O 12048 C CB . CYS B 635 ? 1.3650 1.1170 1.5657 0.2555 0.0247 0.1842 635 CYS B CB 12049 S SG . CYS B 635 ? 1.4191 1.1377 1.5867 0.2945 0.0100 0.1689 635 CYS B SG 12050 N N . ARG B 636 ? 1.5988 1.3788 1.8250 0.1768 0.0146 0.2482 636 ARG B N 12051 C CA . ARG B 636 ? 1.6743 1.4821 1.9289 0.1366 0.0218 0.2516 636 ARG B CA 12052 C C . ARG B 636 ? 1.6009 1.3598 1.8684 0.1328 0.0020 0.2458 636 ARG B C 12053 O O . ARG B 636 ? 1.6582 1.4475 1.9536 0.1003 0.0061 0.2417 636 ARG B O 12054 C CB . ARG B 636 ? 1.8286 1.6493 2.0630 0.1020 0.0213 0.2836 636 ARG B CB 12055 C CG . ARG B 636 ? 1.8115 1.7046 2.0395 0.0968 0.0435 0.2868 636 ARG B CG 12056 C CD . ARG B 636 ? 1.8928 1.7974 2.0940 0.0601 0.0410 0.3218 636 ARG B CD 12057 N NE . ARG B 636 ? 2.0826 1.9007 2.2326 0.0779 0.0099 0.3558 636 ARG B NE 12058 C CZ . ARG B 636 ? 2.1251 1.9371 2.2400 0.1125 -0.0016 0.3716 636 ARG B CZ 12059 N NH1 . ARG B 636 ? 2.0908 1.9866 2.2166 0.1260 0.0174 0.3546 636 ARG B NH1 12060 N NH2 . ARG B 636 ? 2.1688 1.8923 2.2366 0.1343 -0.0315 0.4020 636 ARG B NH2 12061 N N . ASP B 637 ? 1.5883 1.2810 1.8367 0.1640 -0.0185 0.2417 637 ASP B N 12062 C CA . ASP B 637 ? 1.5766 1.2221 1.8316 0.1591 -0.0386 0.2353 637 ASP B CA 12063 C C . ASP B 637 ? 1.5219 1.2104 1.8164 0.1628 -0.0319 0.2078 637 ASP B C 12064 O O . ASP B 637 ? 1.5170 1.2393 1.8211 0.1836 -0.0150 0.1921 637 ASP B O 12065 C CB . ASP B 637 ? 1.7438 1.3117 1.9676 0.1925 -0.0603 0.2339 637 ASP B CB 12066 C CG . ASP B 637 ? 2.0013 1.5198 2.1846 0.1998 -0.0712 0.2606 637 ASP B CG 12067 O OD1 . ASP B 637 ? 2.1280 1.6661 2.2971 0.2280 -0.0658 0.2613 637 ASP B OD1 12068 O OD2 . ASP B 637 ? 2.0058 1.4653 2.1681 0.1776 -0.0851 0.2799 637 ASP B OD2 12069 N N . GLU B 638 ? 1.5540 1.2399 1.8673 0.1429 -0.0450 0.2011 638 GLU B N 12070 C CA . GLU B 638 ? 1.5302 1.2630 1.8817 0.1521 -0.0442 0.1757 638 GLU B CA 12071 C C . GLU B 638 ? 1.4605 1.1442 1.7974 0.1852 -0.0639 0.1629 638 GLU B C 12072 O O . GLU B 638 ? 1.6493 1.2901 1.9748 0.1753 -0.0841 0.1634 638 GLU B O 12073 C CB . GLU B 638 ? 1.6575 1.4394 2.0427 0.1105 -0.0470 0.1694 638 GLU B CB 12074 C CG . GLU B 638 ? 1.8413 1.7083 2.2774 0.1195 -0.0384 0.1434 638 GLU B CG 12075 C CD . GLU B 638 ? 1.9308 1.7923 2.3772 0.1521 -0.0591 0.1240 638 GLU B CD 12076 O OE1 . GLU B 638 ? 2.1673 1.9773 2.5921 0.1483 -0.0801 0.1263 638 GLU B OE1 12077 O OE2 . GLU B 638 ? 1.6291 1.5351 2.1020 0.1827 -0.0546 0.1065 638 GLU B OE2 12078 N N . ILE B 639 ? 1.3622 1.0488 1.6942 0.2206 -0.0561 0.1504 639 ILE B N 12079 C CA . ILE B 639 ? 1.3031 0.9436 1.6125 0.2501 -0.0724 0.1388 639 ILE B CA 12080 C C . ILE B 639 ? 1.3698 1.0430 1.7035 0.2645 -0.0817 0.1223 639 ILE B C 12081 O O . ILE B 639 ? 1.5964 1.3122 1.9502 0.2763 -0.0669 0.1153 639 ILE B O 12082 C CB . ILE B 639 ? 1.2308 0.8428 1.5043 0.2771 -0.0581 0.1353 639 ILE B CB 12083 C CG1 . ILE B 639 ? 1.2362 0.8333 1.4897 0.2696 -0.0512 0.1492 639 ILE B CG1 12084 C CG2 . ILE B 639 ? 1.1965 0.7606 1.4404 0.3010 -0.0740 0.1226 639 ILE B CG2 12085 C CD1 . ILE B 639 ? 1.3043 0.8914 1.5254 0.2909 -0.0356 0.1397 639 ILE B CD1 12086 N N . GLU B 640 ? 1.3234 0.9777 1.6542 0.2656 -0.1068 0.1148 640 GLU B N 12087 C CA . GLU B 640 ? 1.3368 1.0300 1.6892 0.2822 -0.1218 0.0995 640 GLU B CA 12088 C C . GLU B 640 ? 1.3052 0.9506 1.6224 0.3056 -0.1422 0.0923 640 GLU B C 12089 O O . GLU B 640 ? 1.3230 0.9239 1.6191 0.2923 -0.1537 0.0921 640 GLU B O 12090 C CB . GLU B 640 ? 1.4453 1.1987 1.8408 0.2483 -0.1331 0.0918 640 GLU B CB 12091 C CG . GLU B 640 ? 1.5328 1.3436 1.9553 0.2669 -0.1535 0.0724 640 GLU B CG 12092 C CD . GLU B 640 ? 1.7054 1.5851 2.1687 0.2253 -0.1634 0.0583 640 GLU B CD 12093 O OE1 . GLU B 640 ? 1.7283 1.6024 2.1944 0.1792 -0.1511 0.0662 640 GLU B OE1 12094 O OE2 . GLU B 640 ? 1.8186 1.7595 2.3072 0.2370 -0.1832 0.0388 640 GLU B OE2 12095 N N . SER B 641 ? 1.2740 0.9245 1.5806 0.3407 -0.1463 0.0860 641 SER B N 12096 C CA . SER B 641 ? 1.2976 0.9072 1.5647 0.3616 -0.1659 0.0802 641 SER B CA 12097 C C . SER B 641 ? 1.4638 1.1149 1.7551 0.3525 -0.1955 0.0684 641 SER B C 12098 O O . SER B 641 ? 1.7264 1.4483 2.0578 0.3591 -0.2047 0.0612 641 SER B O 12099 C CB . SER B 641 ? 1.3885 0.9776 1.6234 0.4014 -0.1599 0.0816 641 SER B CB 12100 O OG . SER B 641 ? 1.3078 0.8577 1.5140 0.4027 -0.1292 0.0874 641 SER B OG 12101 N N . VAL B 642 ? 1.4805 1.0940 1.7485 0.3371 -0.2097 0.0624 642 VAL B N 12102 C CA . VAL B 642 ? 1.4538 1.1055 1.7402 0.3201 -0.2352 0.0471 642 VAL B CA 12103 C C . VAL B 642 ? 1.4574 1.0891 1.7035 0.3463 -0.2559 0.0400 642 VAL B C 12104 O O . VAL B 642 ? 1.4051 0.9736 1.6022 0.3633 -0.2483 0.0455 642 VAL B O 12105 C CB . VAL B 642 ? 1.5189 1.1400 1.8078 0.2754 -0.2344 0.0424 642 VAL B CB 12106 C CG1 . VAL B 642 ? 1.6565 1.1939 1.8974 0.2806 -0.2332 0.0415 642 VAL B CG1 12107 C CG2 . VAL B 642 ? 1.6481 1.3228 1.9632 0.2455 -0.2542 0.0227 642 VAL B CG2 12108 N N . LYS B 643 ? 1.5622 1.2542 1.8262 0.3472 -0.2817 0.0264 643 LYS B N 12109 C CA . LYS B 643 ? 1.7924 1.4781 2.0163 0.3781 -0.3039 0.0237 643 LYS B CA 12110 C C . LYS B 643 ? 1.8522 1.5034 2.0438 0.3547 -0.3166 0.0092 643 LYS B C 12111 O O . LYS B 643 ? 1.9100 1.6045 2.1264 0.3242 -0.3309 -0.0095 643 LYS B O 12112 C CB . LYS B 643 ? 1.8031 1.5848 2.0616 0.4007 -0.3290 0.0159 643 LYS B CB 12113 C CG . LYS B 643 ? 1.8693 1.6566 2.0861 0.4300 -0.3591 0.0134 643 LYS B CG 12114 C CD . LYS B 643 ? 1.9238 1.8273 2.1848 0.4483 -0.3885 -0.0001 643 LYS B CD 12115 C CE . LYS B 643 ? 1.9728 1.9546 2.2894 0.3933 -0.3919 -0.0271 643 LYS B CE 12116 N NZ . LYS B 643 ? 1.9379 1.8807 2.2235 0.3527 -0.3972 -0.0408 643 LYS B NZ 12117 N N . GLU B 644 ? 1.8951 1.4707 2.0301 0.3657 -0.3083 0.0142 644 GLU B N 12118 C CA . GLU B 644 ? 2.0142 1.5564 2.1074 0.3531 -0.3201 -0.0015 644 GLU B CA 12119 C C . GLU B 644 ? 2.1029 1.6515 2.2209 0.3103 -0.3248 -0.0239 644 GLU B C 12120 O O . GLU B 644 ? 2.2024 1.7555 2.2998 0.2972 -0.3413 -0.0430 644 GLU B O 12121 C CB . GLU B 644 ? 2.1373 1.7116 2.1995 0.3777 -0.3479 -0.0018 644 GLU B CB 12122 C CG . GLU B 644 ? 2.1459 1.6810 2.1574 0.4196 -0.3432 0.0204 644 GLU B CG 12123 C CD . GLU B 644 ? 2.2479 1.7973 2.2122 0.4452 -0.3732 0.0239 644 GLU B CD 12124 O OE1 . GLU B 644 ? 2.1839 1.7814 2.1563 0.4278 -0.3972 0.0062 644 GLU B OE1 12125 O OE2 . GLU B 644 ? 2.3542 1.8634 2.2684 0.4818 -0.3724 0.0446 644 GLU B OE2 12126 N N . LEU B 645 ? 2.0959 1.6366 2.2505 0.2869 -0.3088 -0.0214 645 LEU B N 12127 C CA . LEU B 645 ? 2.1542 1.6830 2.3252 0.2436 -0.3097 -0.0402 645 LEU B CA 12128 C C . LEU B 645 ? 2.0104 1.5221 2.2112 0.2225 -0.2906 -0.0279 645 LEU B C 12129 O O . LEU B 645 ? 1.8738 1.4145 2.0967 0.2360 -0.2805 -0.0091 645 LEU B O 12130 C CB . LEU B 645 ? 2.2290 1.8357 2.4225 0.2210 -0.3320 -0.0609 645 LEU B CB 12131 C CG . LEU B 645 ? 2.2718 1.8598 2.4627 0.1737 -0.3354 -0.0898 645 LEU B CG 12132 C CD1 . LEU B 645 ? 2.2362 1.8780 2.4124 0.1712 -0.3601 -0.1129 645 LEU B CD1 12133 C CD2 . LEU B 645 ? 2.3039 1.9215 2.5340 0.1285 -0.3275 -0.0960 645 LEU B CD2 12134 N N . LYS B 646 ? 1.9311 1.3907 2.1274 0.1886 -0.2854 -0.0389 646 LYS B N 12135 C CA . LYS B 646 ? 1.8912 1.3303 2.1065 0.1586 -0.2709 -0.0276 646 LYS B CA 12136 C C . LYS B 646 ? 2.1055 1.5369 2.3236 0.1066 -0.2756 -0.0509 646 LYS B C 12137 O O . LYS B 646 ? 2.3318 1.6985 2.5219 0.0962 -0.2777 -0.0686 646 LYS B O 12138 C CB . LYS B 646 ? 1.7832 1.1361 1.9746 0.1743 -0.2549 -0.0108 646 LYS B CB 12139 C CG . LYS B 646 ? 1.6433 1.0077 1.8301 0.2167 -0.2453 0.0082 646 LYS B CG 12140 C CD . LYS B 646 ? 1.6869 0.9806 1.8492 0.2342 -0.2326 0.0169 646 LYS B CD 12141 C CE . LYS B 646 ? 1.9871 1.2254 2.1193 0.2409 -0.2399 -0.0074 646 LYS B CE 12142 N NZ . LYS B 646 ? 2.1878 1.3695 2.3005 0.2648 -0.2299 -0.0038 646 LYS B NZ 12143 N N . ASP B 647 ? 2.2089 1.7094 2.4599 0.0714 -0.2754 -0.0550 647 ASP B N 12144 C CA . ASP B 647 ? 2.4142 1.9185 2.6662 0.0120 -0.2764 -0.0814 647 ASP B CA 12145 C C . ASP B 647 ? 2.4179 1.7962 2.6336 -0.0166 -0.2606 -0.0763 647 ASP B C 12146 O O . ASP B 647 ? 2.3026 1.6235 2.5077 -0.0026 -0.2479 -0.0473 647 ASP B O 12147 C CB . ASP B 647 ? 2.5471 2.1550 2.8414 -0.0244 -0.2741 -0.0878 647 ASP B CB 12148 C CG . ASP B 647 ? 2.6164 2.3468 2.9492 0.0160 -0.2904 -0.0896 647 ASP B CG 12149 O OD1 . ASP B 647 ? 2.6751 2.3908 2.9993 0.0733 -0.2944 -0.0699 647 ASP B OD1 12150 O OD2 . ASP B 647 ? 2.6309 2.4717 2.9999 -0.0094 -0.2988 -0.1125 647 ASP B OD2 12151 N N . THR B 648 ? 2.5065 1.8386 2.6997 -0.0549 -0.2617 -0.1046 648 THR B N 12152 C CA . THR B 648 ? 2.5985 1.7988 2.7517 -0.0821 -0.2466 -0.1000 648 THR B CA 12153 C C . THR B 648 ? 2.6829 1.8893 2.8405 -0.1359 -0.2314 -0.0873 648 THR B C 12154 O O . THR B 648 ? 2.7024 1.9838 2.8787 -0.1900 -0.2299 -0.1110 648 THR B O 12155 C CB . THR B 648 ? 2.6290 1.7698 2.7534 -0.1135 -0.2481 -0.1378 648 THR B CB 12156 O OG1 . THR B 648 ? 2.7254 1.7417 2.8095 -0.1552 -0.2311 -0.1350 648 THR B OG1 12157 C CG2 . THR B 648 ? 2.5914 1.8471 2.7416 -0.1556 -0.2575 -0.1739 648 THR B CG2 12158 N N . GLY B 649 ? 2.7030 1.8372 2.8415 -0.1226 -0.2200 -0.0513 649 GLY B N 12159 C CA . GLY B 649 ? 2.7151 1.8584 2.8537 -0.1697 -0.2047 -0.0330 649 GLY B CA 12160 C C . GLY B 649 ? 2.8367 1.8329 2.9143 -0.2109 -0.1898 -0.0199 649 GLY B C 12161 O O . GLY B 649 ? 2.8906 1.7863 2.9294 -0.2231 -0.1895 -0.0378 649 GLY B O 12162 N N . LYS B 650 ? 2.8360 1.8162 2.9012 -0.2324 -0.1767 0.0120 650 LYS B N 12163 C CA . LYS B 650 ? 2.8654 1.6907 2.8616 -0.2554 -0.1648 0.0393 650 LYS B CA 12164 C C . LYS B 650 ? 2.7940 1.5357 2.7697 -0.1752 -0.1750 0.0665 650 LYS B C 12165 O O . LYS B 650 ? 2.5957 1.3948 2.6067 -0.1160 -0.1880 0.0560 650 LYS B O 12166 C CB . LYS B 650 ? 2.8417 1.6896 2.8287 -0.3057 -0.1484 0.0656 650 LYS B CB 12167 C CG . LYS B 650 ? 2.8682 1.8083 2.8751 -0.3914 -0.1356 0.0333 650 LYS B CG 12168 C CD . LYS B 650 ? 2.7813 1.8881 2.8531 -0.3931 -0.1329 0.0345 650 LYS B CD 12169 C CE . LYS B 650 ? 2.6925 1.9231 2.8343 -0.3232 -0.1524 0.0182 650 LYS B CE 12170 N NZ . LYS B 650 ? 2.6901 1.9733 2.8533 -0.3352 -0.1638 -0.0269 650 LYS B NZ 12171 N N . ASP B 651 ? 2.9052 1.5135 2.8205 -0.1733 -0.1696 0.1001 651 ASP B N 12172 C CA . ASP B 651 ? 2.8044 1.3363 2.6989 -0.0953 -0.1810 0.1212 651 ASP B CA 12173 C C . ASP B 651 ? 2.4368 1.0862 2.3832 -0.0371 -0.1875 0.1342 651 ASP B C 12174 O O . ASP B 651 ? 2.2946 1.0144 2.2590 -0.0503 -0.1799 0.1576 651 ASP B O 12175 C CB . ASP B 651 ? 3.0473 1.4306 2.8672 -0.1005 -0.1764 0.1620 651 ASP B CB 12176 C CG . ASP B 651 ? 3.1327 1.5578 2.9459 -0.1409 -0.1646 0.1978 651 ASP B CG 12177 O OD1 . ASP B 651 ? 3.2108 1.5660 2.9812 -0.1149 -0.1668 0.2403 651 ASP B OD1 12178 O OD2 . ASP B 651 ? 3.1340 1.6687 2.9852 -0.1976 -0.1538 0.1817 651 ASP B OD2 12179 N N . ALA B 652 ? 2.4799 1.1488 2.4470 0.0227 -0.1991 0.1154 652 ALA B N 12180 C CA . ALA B 652 ? 2.3285 1.0998 2.3374 0.0746 -0.2026 0.1210 652 ALA B CA 12181 C C . ALA B 652 ? 2.3157 1.0560 2.3192 0.1382 -0.2131 0.1043 652 ALA B C 12182 O O . ALA B 652 ? 2.5762 1.2403 2.5575 0.1400 -0.2187 0.0801 652 ALA B O 12183 C CB . ALA B 652 ? 2.0382 0.9428 2.1009 0.0556 -0.2014 0.1007 652 ALA B CB 12184 N N . VAL B 653 ? 1.9264 0.7297 1.9499 0.1864 -0.2134 0.1129 653 VAL B N 12185 C CA . VAL B 653 ? 2.0483 0.8376 2.0674 0.2437 -0.2207 0.0939 653 VAL B CA 12186 C C . VAL B 653 ? 2.0833 0.9801 2.1369 0.2646 -0.2186 0.0754 653 VAL B C 12187 O O . VAL B 653 ? 1.9043 0.8759 1.9784 0.2682 -0.2101 0.0924 653 VAL B O 12188 C CB . VAL B 653 ? 2.0079 0.7510 2.0019 0.2889 -0.2230 0.1198 653 VAL B CB 12189 C CG1 . VAL B 653 ? 1.8289 0.6235 1.8299 0.2759 -0.2139 0.1581 653 VAL B CG1 12190 C CG2 . VAL B 653 ? 1.8127 0.6211 1.8183 0.3401 -0.2160 0.0955 653 VAL B CG2 12191 N N . ASN B 654 ? 2.2166 1.1146 2.2709 0.2756 -0.2248 0.0399 654 ASN B N 12192 C CA . ASN B 654 ? 1.9904 0.9707 2.0619 0.2944 -0.2229 0.0220 654 ASN B CA 12193 C C . ASN B 654 ? 1.6672 0.6603 1.7309 0.3426 -0.2182 0.0184 654 ASN B C 12194 O O . ASN B 654 ? 1.6869 0.6361 1.7339 0.3659 -0.2175 0.0140 654 ASN B O 12195 C CB . ASN B 654 ? 2.1526 1.1325 2.2211 0.2823 -0.2314 -0.0148 654 ASN B CB 12196 C CG . ASN B 654 ? 2.2081 1.2031 2.2886 0.2334 -0.2361 -0.0171 654 ASN B CG 12197 O OD1 . ASN B 654 ? 2.4265 1.4131 2.5135 0.2041 -0.2322 0.0049 654 ASN B OD1 12198 N ND2 . ASN B 654 ? 2.0021 1.0270 2.0841 0.2218 -0.2443 -0.0460 654 ASN B ND2 12199 N N . CYS B 655 ? 1.5294 0.5987 1.6038 0.3526 -0.2085 0.0190 655 CYS B N 12200 C CA . CYS B 655 ? 1.6488 0.7476 1.7151 0.3894 -0.1999 0.0093 655 CYS B CA 12201 C C . CYS B 655 ? 1.5376 0.6895 1.5979 0.3909 -0.1925 -0.0147 655 CYS B C 12202 O O . CYS B 655 ? 1.4277 0.6068 1.4929 0.3694 -0.1919 -0.0100 655 CYS B O 12203 C CB . CYS B 655 ? 1.5396 0.6720 1.6134 0.3968 -0.1884 0.0406 655 CYS B CB 12204 S SG . CYS B 655 ? 2.6171 1.6937 2.6804 0.4009 -0.1917 0.0707 655 CYS B SG 12205 N N . THR B 656 ? 1.6417 0.8090 1.6876 0.4167 -0.1867 -0.0412 656 THR B N 12206 C CA . THR B 656 ? 1.4193 0.6251 1.4460 0.4129 -0.1776 -0.0674 656 THR B CA 12207 C C . THR B 656 ? 1.4427 0.6952 1.4586 0.4342 -0.1602 -0.0832 656 THR B C 12208 O O . THR B 656 ? 1.7030 0.9565 1.7284 0.4606 -0.1619 -0.0839 656 THR B O 12209 C CB . THR B 656 ? 1.5611 0.7377 1.5739 0.4081 -0.1895 -0.1023 656 THR B CB 12210 O OG1 . THR B 656 ? 1.5986 0.7326 1.6236 0.3875 -0.2053 -0.0918 656 THR B OG1 12211 C CG2 . THR B 656 ? 1.6143 0.8232 1.5986 0.3936 -0.1824 -0.1210 656 THR B CG2 12212 N N . TYR B 657 ? 1.3651 0.6554 1.3569 0.4222 -0.1436 -0.0964 657 TYR B N 12213 C CA . TYR B 657 ? 1.3450 0.6876 1.3206 0.4314 -0.1222 -0.1187 657 TYR B CA 12214 C C . TYR B 657 ? 1.3342 0.6943 1.2685 0.4068 -0.1031 -0.1324 657 TYR B C 12215 O O . TYR B 657 ? 1.3368 0.6707 1.2581 0.3895 -0.1072 -0.1146 657 TYR B O 12216 C CB . TYR B 657 ? 1.3142 0.6915 1.3087 0.4409 -0.1109 -0.0937 657 TYR B CB 12217 C CG . TYR B 657 ? 1.2795 0.6677 1.2718 0.4182 -0.0958 -0.0649 657 TYR B CG 12218 C CD1 . TYR B 657 ? 1.3637 0.7924 1.3305 0.4053 -0.0674 -0.0754 657 TYR B CD1 12219 C CD2 . TYR B 657 ? 1.4238 0.7829 1.4383 0.4082 -0.1081 -0.0312 657 TYR B CD2 12220 C CE1 . TYR B 657 ? 1.3655 0.7956 1.3288 0.3882 -0.0524 -0.0518 657 TYR B CE1 12221 C CE2 . TYR B 657 ? 1.2725 0.6472 1.2896 0.3926 -0.0946 -0.0097 657 TYR B CE2 12222 C CZ . TYR B 657 ? 1.3086 0.7139 1.2999 0.3853 -0.0671 -0.0194 657 TYR B CZ 12223 O OH . TYR B 657 ? 1.3797 0.7919 1.3720 0.3732 -0.0524 -0.0006 657 TYR B OH 12224 N N . LYS B 658 ? 1.4434 0.8483 1.3534 0.4055 -0.0821 -0.1649 658 LYS B N 12225 C CA . LYS B 658 ? 1.4168 0.8301 1.2745 0.3767 -0.0580 -0.1777 658 LYS B CA 12226 C C . LYS B 658 ? 1.4084 0.8558 1.2596 0.3676 -0.0301 -0.1652 658 LYS B C 12227 O O . LYS B 658 ? 1.4851 0.9856 1.3594 0.3811 -0.0215 -0.1743 658 LYS B O 12228 C CB . LYS B 658 ? 1.4364 0.8787 1.2613 0.3683 -0.0476 -0.2295 658 LYS B CB 12229 C CG . LYS B 658 ? 1.4938 0.8958 1.2851 0.3515 -0.0599 -0.2431 658 LYS B CG 12230 C CD . LYS B 658 ? 1.7250 1.1637 1.4723 0.3316 -0.0408 -0.2958 658 LYS B CD 12231 C CE . LYS B 658 ? 2.0006 1.4009 1.7032 0.3082 -0.0506 -0.3076 658 LYS B CE 12232 N NZ . LYS B 658 ? 2.0213 1.4589 1.6720 0.2795 -0.0277 -0.3595 658 LYS B NZ 12233 N N . ASN B 659 ? 1.3931 0.8103 1.2113 0.3466 -0.0165 -0.1453 659 ASN B N 12234 C CA . ASN B 659 ? 1.4748 0.9159 1.2791 0.3326 0.0149 -0.1383 659 ASN B CA 12235 C C . ASN B 659 ? 1.4505 0.9118 1.1930 0.3033 0.0486 -0.1765 659 ASN B C 12236 O O . ASN B 659 ? 1.4834 0.9499 1.1991 0.2956 0.0464 -0.2096 659 ASN B O 12237 C CB . ASN B 659 ? 1.7238 1.1178 1.5225 0.3278 0.0154 -0.1005 659 ASN B CB 12238 C CG . ASN B 659 ? 1.6804 1.0126 1.4312 0.3199 0.0050 -0.0960 659 ASN B CG 12239 O OD1 . ASN B 659 ? 1.7129 1.0351 1.4237 0.3088 0.0037 -0.1223 659 ASN B OD1 12240 N ND2 . ASN B 659 ? 1.3889 0.6849 1.1427 0.3268 -0.0032 -0.0640 659 ASN B ND2 12241 N N . GLU B 660 ? 1.4611 0.9344 1.1783 0.2823 0.0823 -0.1752 660 GLU B N 12242 C CA . GLU B 660 ? 1.5074 0.9979 1.1585 0.2445 0.1210 -0.2129 660 GLU B CA 12243 C C . GLU B 660 ? 1.5781 0.9903 1.1516 0.2202 0.1247 -0.2156 660 GLU B C 12244 O O . GLU B 660 ? 1.7198 1.1382 1.2292 0.1845 0.1518 -0.2518 660 GLU B O 12245 C CB . GLU B 660 ? 1.5011 1.0081 1.1384 0.2232 0.1581 -0.2083 660 GLU B CB 12246 C CG . GLU B 660 ? 1.7229 1.3064 1.4314 0.2452 0.1537 -0.1994 660 GLU B CG 12247 C CD . GLU B 660 ? 2.0177 1.6105 1.7163 0.2234 0.1883 -0.1903 660 GLU B CD 12248 O OE1 . GLU B 660 ? 2.2485 1.7839 1.8812 0.1912 0.2190 -0.1950 660 GLU B OE1 12249 O OE2 . GLU B 660 ? 1.9228 1.5751 1.6748 0.2377 0.1855 -0.1783 660 GLU B OE2 12250 N N . ASP B 661 ? 1.6478 0.9912 1.2247 0.2382 0.0972 -0.1779 661 ASP B N 12251 C CA . ASP B 661 ? 1.6725 0.9367 1.1739 0.2224 0.0944 -0.1710 661 ASP B CA 12252 C C . ASP B 661 ? 1.7525 1.0194 1.2554 0.2277 0.0651 -0.1872 661 ASP B C 12253 O O . ASP B 661 ? 1.9036 1.1115 1.3494 0.2182 0.0547 -0.1788 661 ASP B O 12254 C CB . ASP B 661 ? 1.7054 0.9034 1.2076 0.2428 0.0796 -0.1238 661 ASP B CB 12255 C CG . ASP B 661 ? 1.8150 1.0066 1.3163 0.2379 0.1102 -0.1108 661 ASP B CG 12256 O OD1 . ASP B 661 ? 1.8999 1.1079 1.3605 0.2053 0.1502 -0.1378 661 ASP B OD1 12257 O OD2 . ASP B 661 ? 1.7871 0.9637 1.3294 0.2638 0.0960 -0.0778 661 ASP B OD2 12258 N N . ASP B 662 ? 1.7310 1.0643 1.2978 0.2450 0.0511 -0.2098 662 ASP B N 12259 C CA . ASP B 662 ? 1.7629 1.1051 1.3405 0.2515 0.0257 -0.2326 662 ASP B CA 12260 C C . ASP B 662 ? 1.6391 0.9317 1.2361 0.2704 -0.0117 -0.1988 662 ASP B C 12261 O O . ASP B 662 ? 1.6802 0.9555 1.2529 0.2628 -0.0282 -0.2120 662 ASP B O 12262 C CB . ASP B 662 ? 1.9266 1.2656 1.4240 0.2125 0.0461 -0.2721 662 ASP B CB 12263 C CG . ASP B 662 ? 2.1423 1.5441 1.6181 0.1865 0.0858 -0.3140 662 ASP B CG 12264 O OD1 . ASP B 662 ? 2.0967 1.5169 1.5868 0.1873 0.1060 -0.3021 662 ASP B OD1 12265 O OD2 . ASP B 662 ? 2.2022 1.6433 1.6476 0.1626 0.0978 -0.3626 662 ASP B OD2 12266 N N . CYS B 663 ? 1.6304 0.9093 1.2716 0.2918 -0.0238 -0.1588 663 CYS B N 12267 C CA . CYS B 663 ? 1.5581 0.8078 1.2265 0.3084 -0.0583 -0.1304 663 CYS B CA 12268 C C . CYS B 663 ? 1.5118 0.7894 1.2608 0.3304 -0.0800 -0.1265 663 CYS B C 12269 O O . CYS B 663 ? 1.5941 0.9034 1.3816 0.3408 -0.0697 -0.1255 663 CYS B O 12270 C CB . CYS B 663 ? 1.5913 0.8060 1.2478 0.3153 -0.0576 -0.0909 663 CYS B CB 12271 S SG . CYS B 663 ? 1.9497 1.0977 1.4961 0.2953 -0.0398 -0.0857 663 CYS B SG 12272 N N . VAL B 664 ? 1.5724 0.8353 1.3406 0.3351 -0.1094 -0.1242 664 VAL B N 12273 C CA . VAL B 664 ? 1.5533 0.8246 1.3854 0.3499 -0.1289 -0.1215 664 VAL B CA 12274 C C . VAL B 664 ? 1.4870 0.7547 1.3598 0.3566 -0.1407 -0.0828 664 VAL B C 12275 O O . VAL B 664 ? 1.4268 0.6843 1.2940 0.3531 -0.1564 -0.0676 664 VAL B O 12276 C CB . VAL B 664 ? 1.4782 0.7357 1.3098 0.3447 -0.1509 -0.1456 664 VAL B CB 12277 C CG1 . VAL B 664 ? 1.4643 0.7107 1.3521 0.3544 -0.1704 -0.1372 664 VAL B CG1 12278 C CG2 . VAL B 664 ? 1.5216 0.7941 1.3268 0.3404 -0.1387 -0.1910 664 VAL B CG2 12279 N N . VAL B 665 ? 1.3843 0.6681 1.2973 0.3663 -0.1335 -0.0688 665 VAL B N 12280 C CA . VAL B 665 ? 1.3526 0.6422 1.3055 0.3676 -0.1405 -0.0358 665 VAL B CA 12281 C C . VAL B 665 ? 1.5161 0.7944 1.5111 0.3680 -0.1589 -0.0312 665 VAL B C 12282 O O . VAL B 665 ? 1.3481 0.6201 1.3530 0.3780 -0.1567 -0.0397 665 VAL B O 12283 C CB . VAL B 665 ? 1.2951 0.6099 1.2567 0.3709 -0.1161 -0.0198 665 VAL B CB 12284 C CG1 . VAL B 665 ? 1.2735 0.6014 1.2785 0.3690 -0.1223 0.0100 665 VAL B CG1 12285 C CG2 . VAL B 665 ? 1.3025 0.6145 1.2145 0.3656 -0.0935 -0.0251 665 VAL B CG2 12286 N N . ARG B 666 ? 1.7574 1.0323 1.7733 0.3571 -0.1768 -0.0188 666 ARG B N 12287 C CA . ARG B 666 ? 1.6404 0.8954 1.6873 0.3477 -0.1912 -0.0149 666 ARG B CA 12288 C C . ARG B 666 ? 1.4485 0.7250 1.5303 0.3373 -0.1893 0.0141 666 ARG B C 12289 O O . ARG B 666 ? 1.3237 0.6346 1.4149 0.3342 -0.1890 0.0249 666 ARG B O 12290 C CB . ARG B 666 ? 1.7825 1.0238 1.8249 0.3328 -0.2116 -0.0328 666 ARG B CB 12291 C CG . ARG B 666 ? 1.8354 1.0737 1.8375 0.3370 -0.2133 -0.0594 666 ARG B CG 12292 C CD . ARG B 666 ? 1.7667 0.9929 1.7654 0.3197 -0.2328 -0.0812 666 ARG B CD 12293 N NE . ARG B 666 ? 1.9044 1.0881 1.9117 0.3179 -0.2345 -0.1014 666 ARG B NE 12294 C CZ . ARG B 666 ? 1.8816 1.0468 1.8676 0.3272 -0.2310 -0.1333 666 ARG B CZ 12295 N NH1 . ARG B 666 ? 1.8289 1.0175 1.7805 0.3313 -0.2239 -0.1486 666 ARG B NH1 12296 N NH2 . ARG B 666 ? 1.8161 0.9362 1.8115 0.3317 -0.2336 -0.1515 666 ARG B NH2 12297 N N . PHE B 667 ? 1.5066 0.7621 1.6048 0.3331 -0.1880 0.0261 667 PHE B N 12298 C CA . PHE B 667 ? 1.3748 0.6513 1.5020 0.3158 -0.1846 0.0518 667 PHE B CA 12299 C C . PHE B 667 ? 1.3939 0.6221 1.5250 0.3002 -0.1911 0.0615 667 PHE B C 12300 O O . PHE B 667 ? 1.9612 1.1373 2.0731 0.3146 -0.1954 0.0528 667 PHE B O 12301 C CB . PHE B 667 ? 1.4201 0.7337 1.5519 0.3272 -0.1639 0.0680 667 PHE B CB 12302 C CG . PHE B 667 ? 1.3054 0.6024 1.4249 0.3435 -0.1553 0.0720 667 PHE B CG 12303 C CD1 . PHE B 667 ? 1.3205 0.6083 1.4503 0.3356 -0.1540 0.0956 667 PHE B CD1 12304 C CD2 . PHE B 667 ? 1.5338 0.8306 1.6290 0.3663 -0.1488 0.0511 667 PHE B CD2 12305 C CE1 . PHE B 667 ? 1.6350 0.9133 1.7517 0.3569 -0.1500 0.1010 667 PHE B CE1 12306 C CE2 . PHE B 667 ? 1.7057 1.0036 1.7938 0.3859 -0.1430 0.0510 667 PHE B CE2 12307 C CZ . PHE B 667 ? 1.5942 0.8831 1.6935 0.3846 -0.1453 0.0774 667 PHE B CZ 12308 N N . GLN B 668 ? 1.4026 0.6462 1.5552 0.2706 -0.1911 0.0782 668 GLN B N 12309 C CA . GLN B 668 ? 1.4956 0.6838 1.6413 0.2470 -0.1942 0.0915 668 GLN B CA 12310 C C . GLN B 668 ? 1.5047 0.7250 1.6658 0.2269 -0.1821 0.1196 668 GLN B C 12311 O O . GLN B 668 ? 1.4930 0.7862 1.6804 0.2248 -0.1731 0.1225 668 GLN B O 12312 C CB . GLN B 668 ? 1.6119 0.7772 1.7589 0.2120 -0.2062 0.0749 668 GLN B CB 12313 C CG . GLN B 668 ? 1.8410 1.0847 2.0214 0.1822 -0.2067 0.0722 668 GLN B CG 12314 C CD . GLN B 668 ? 1.8826 1.1172 2.0647 0.1422 -0.2173 0.0512 668 GLN B CD 12315 O OE1 . GLN B 668 ? 1.8887 1.0442 2.0433 0.1311 -0.2215 0.0411 668 GLN B OE1 12316 N NE2 . GLN B 668 ? 1.8633 1.1824 2.0778 0.1212 -0.2213 0.0415 668 GLN B NE2 12317 N N . TYR B 669 ? 1.5949 0.7565 1.7355 0.2124 -0.1817 0.1399 669 TYR B N 12318 C CA . TYR B 669 ? 1.7363 0.9235 1.8839 0.1848 -0.1702 0.1671 669 TYR B CA 12319 C C . TYR B 669 ? 1.8314 0.9457 1.9526 0.1412 -0.1735 0.1801 669 TYR B C 12320 O O . TYR B 669 ? 1.9499 0.9671 2.0331 0.1507 -0.1826 0.1822 669 TYR B O 12321 C CB . TYR B 669 ? 1.5863 0.7832 1.7229 0.2156 -0.1612 0.1881 669 TYR B CB 12322 C CG . TYR B 669 ? 1.8052 0.9172 1.9015 0.2446 -0.1712 0.1988 669 TYR B CG 12323 C CD1 . TYR B 669 ? 2.0679 1.1177 2.1314 0.2291 -0.1734 0.2301 669 TYR B CD1 12324 C CD2 . TYR B 669 ? 1.8470 0.9413 1.9348 0.2890 -0.1787 0.1770 669 TYR B CD2 12325 C CE1 . TYR B 669 ? 2.1671 1.1343 2.1908 0.2649 -0.1856 0.2413 669 TYR B CE1 12326 C CE2 . TYR B 669 ? 1.9926 1.0176 2.0484 0.3231 -0.1893 0.1825 669 TYR B CE2 12327 C CZ . TYR B 669 ? 2.0925 1.0517 2.1165 0.3149 -0.1941 0.2158 669 TYR B CZ 12328 O OH . TYR B 669 ? 2.1632 1.0530 2.1530 0.3564 -0.2057 0.2222 669 TYR B OH 12329 N N . TYR B 670 ? 1.8387 0.9978 1.9770 0.0921 -0.1647 0.1861 670 TYR B N 12330 C CA . TYR B 670 ? 2.0011 1.0930 2.1071 0.0382 -0.1629 0.1977 670 TYR B CA 12331 C C . TYR B 670 ? 2.1108 1.1345 2.1715 0.0415 -0.1589 0.2370 670 TYR B C 12332 O O . TYR B 670 ? 1.9566 1.0339 2.0287 0.0624 -0.1515 0.2549 670 TYR B O 12333 C CB . TYR B 670 ? 2.1418 1.3201 2.2820 -0.0193 -0.1528 0.1864 670 TYR B CB 12334 C CG . TYR B 670 ? 2.3036 1.5336 2.4766 -0.0299 -0.1614 0.1481 670 TYR B CG 12335 C CD1 . TYR B 670 ? 2.4090 1.5755 2.5632 -0.0123 -0.1749 0.1292 670 TYR B CD1 12336 C CD2 . TYR B 670 ? 2.3587 1.7074 2.5819 -0.0553 -0.1570 0.1289 670 TYR B CD2 12337 C CE1 . TYR B 670 ? 2.4406 1.6606 2.6213 -0.0231 -0.1841 0.0948 670 TYR B CE1 12338 C CE2 . TYR B 670 ? 2.4279 1.8327 2.6797 -0.0602 -0.1684 0.0946 670 TYR B CE2 12339 C CZ . TYR B 670 ? 2.4822 1.8223 2.7106 -0.0457 -0.1821 0.0790 670 TYR B CZ 12340 O OH . TYR B 670 ? 2.5205 1.9225 2.7741 -0.0520 -0.1947 0.0455 670 TYR B OH 12341 N N . GLU B 671 ? 2.3633 1.2657 2.3680 0.0203 -0.1636 0.2504 671 GLU B N 12342 C CA . GLU B 671 ? 2.5291 1.3446 2.4777 0.0343 -0.1657 0.2909 671 GLU B CA 12343 C C . GLU B 671 ? 2.5388 1.3894 2.4764 -0.0172 -0.1508 0.3199 671 GLU B C 12344 O O . GLU B 671 ? 2.4014 1.3150 2.3509 0.0036 -0.1458 0.3394 671 GLU B O 12345 C CB . GLU B 671 ? 2.7056 1.3626 2.5891 0.0289 -0.1751 0.2964 671 GLU B CB 12346 C CG . GLU B 671 ? 2.8139 1.3612 2.6272 0.0475 -0.1811 0.3421 671 GLU B CG 12347 C CD . GLU B 671 ? 2.9082 1.4527 2.7227 0.1347 -0.1967 0.3480 671 GLU B CD 12348 O OE1 . GLU B 671 ? 2.8196 1.4303 2.6826 0.1749 -0.2008 0.3138 671 GLU B OE1 12349 O OE2 . GLU B 671 ? 3.0235 1.5031 2.7875 0.1622 -0.2051 0.3861 671 GLU B OE2 12350 N N . ASP B 672 ? 2.5579 1.3720 2.4708 -0.0894 -0.1416 0.3193 672 ASP B N 12351 C CA . ASP B 672 ? 2.5571 1.4130 2.4592 -0.1507 -0.1246 0.3403 672 ASP B CA 12352 C C . ASP B 672 ? 2.5931 1.5198 2.5277 -0.2245 -0.1109 0.3074 672 ASP B C 12353 O O . ASP B 672 ? 2.7322 1.5847 2.6355 -0.2672 -0.1104 0.2925 672 ASP B O 12354 C CB . ASP B 672 ? 2.7532 1.4662 2.5612 -0.1728 -0.1256 0.3859 672 ASP B CB 12355 C CG . ASP B 672 ? 2.8496 1.5884 2.6323 -0.2569 -0.1054 0.4030 672 ASP B CG 12356 O OD1 . ASP B 672 ? 2.8576 1.5284 2.5981 -0.3281 -0.0957 0.3968 672 ASP B OD1 12357 O OD2 . ASP B 672 ? 2.8099 1.6400 2.6133 -0.2567 -0.0971 0.4195 672 ASP B OD2 12358 N N . SER B 673 ? 2.5128 1.5874 2.5108 -0.2389 -0.0990 0.2924 673 SER B N 12359 C CA . SER B 673 ? 2.6418 1.8070 2.6754 -0.3082 -0.0857 0.2598 673 SER B CA 12360 C C . SER B 673 ? 2.8066 2.0243 2.8300 -0.3665 -0.0651 0.2776 673 SER B C 12361 O O . SER B 673 ? 2.8747 2.0255 2.8386 -0.4388 -0.0537 0.2903 673 SER B O 12362 C CB . SER B 673 ? 2.4450 1.7488 2.5666 -0.2728 -0.0908 0.2191 673 SER B CB 12363 O OG . SER B 673 ? 2.4904 1.8969 2.6518 -0.3327 -0.0809 0.1839 673 SER B OG 12364 N N . SER B 674 ? 2.7674 2.1021 2.8448 -0.3385 -0.0583 0.2766 674 SER B N 12365 C CA . SER B 674 ? 2.7087 2.0878 2.7723 -0.3802 -0.0396 0.2987 674 SER B CA 12366 C C . SER B 674 ? 2.5781 1.8918 2.5992 -0.3293 -0.0462 0.3438 674 SER B C 12367 O O . SER B 674 ? 2.5122 1.8536 2.5132 -0.3534 -0.0335 0.3688 674 SER B O 12368 C CB . SER B 674 ? 2.5662 2.1222 2.7168 -0.3859 -0.0249 0.2643 674 SER B CB 12369 O OG . SER B 674 ? 2.5570 2.1621 2.6955 -0.4286 -0.0047 0.2821 674 SER B OG 12370 N N . GLY B 675 ? 2.5126 1.7486 2.5209 -0.2598 -0.0663 0.3508 675 GLY B N 12371 C CA . GLY B 675 ? 2.5050 1.7113 2.4913 -0.1978 -0.0747 0.3818 675 GLY B CA 12372 C C . GLY B 675 ? 2.4602 1.7826 2.5213 -0.1434 -0.0719 0.3555 675 GLY B C 12373 O O . GLY B 675 ? 2.4760 1.8164 2.5354 -0.0978 -0.0726 0.3706 675 GLY B O 12374 N N . LYS B 676 ? 2.3603 1.7606 2.4828 -0.1496 -0.0684 0.3150 676 LYS B N 12375 C CA . LYS B 676 ? 2.2049 1.7062 2.3925 -0.1032 -0.0641 0.2884 676 LYS B CA 12376 C C . LYS B 676 ? 2.2261 1.6794 2.4064 -0.0319 -0.0789 0.2875 676 LYS B C 12377 O O . LYS B 676 ? 2.2382 1.7413 2.4380 0.0073 -0.0717 0.2852 676 LYS B O 12378 C CB . LYS B 676 ? 2.1733 1.7563 2.4193 -0.1213 -0.0624 0.2476 676 LYS B CB 12379 C CG . LYS B 676 ? 2.2113 1.8941 2.4895 -0.1814 -0.0430 0.2347 676 LYS B CG 12380 C CD . LYS B 676 ? 2.2365 2.0109 2.5767 -0.1872 -0.0458 0.1906 676 LYS B CD 12381 C CE . LYS B 676 ? 2.2470 2.1498 2.6356 -0.2310 -0.0253 0.1690 676 LYS B CE 12382 N NZ . LYS B 676 ? 2.2889 2.1741 2.6372 -0.3134 -0.0118 0.1830 676 LYS B NZ 12383 N N . SER B 677 ? 2.2351 1.5946 2.3859 -0.0201 -0.0971 0.2854 677 SER B N 12384 C CA . SER B 677 ? 2.1999 1.5167 2.3443 0.0424 -0.1112 0.2774 677 SER B CA 12385 C C . SER B 677 ? 2.0782 1.4799 2.2752 0.0737 -0.1074 0.2463 677 SER B C 12386 O O . SER B 677 ? 2.1434 1.5820 2.3494 0.1105 -0.0998 0.2458 677 SER B O 12387 C CB . SER B 677 ? 2.1649 1.4470 2.2735 0.0802 -0.1132 0.3051 677 SER B CB 12388 O OG . SER B 677 ? 2.3870 1.5786 2.4375 0.0576 -0.1197 0.3388 677 SER B OG 12389 N N . ILE B 678 ? 1.8637 1.2945 2.0901 0.0575 -0.1125 0.2201 678 ILE B N 12390 C CA . ILE B 678 ? 1.7428 1.2479 2.0126 0.0864 -0.1113 0.1936 678 ILE B CA 12391 C C . ILE B 678 ? 1.6316 1.0903 1.8861 0.1324 -0.1254 0.1804 678 ILE B C 12392 O O . ILE B 678 ? 1.6530 1.0399 1.8812 0.1304 -0.1400 0.1772 678 ILE B O 12393 C CB . ILE B 678 ? 1.9055 1.4790 2.2156 0.0531 -0.1134 0.1700 678 ILE B CB 12394 C CG1 . ILE B 678 ? 1.9263 1.5707 2.2756 0.0916 -0.1150 0.1467 678 ILE B CG1 12395 C CG2 . ILE B 678 ? 1.9134 1.4307 2.2040 0.0247 -0.1290 0.1601 678 ILE B CG2 12396 C CD1 . ILE B 678 ? 1.9562 1.6879 2.3515 0.0693 -0.1192 0.1217 678 ILE B CD1 12397 N N . LEU B 679 ? 1.5853 1.0819 1.8519 0.1703 -0.1186 0.1710 679 LEU B N 12398 C CA . LEU B 679 ? 1.4686 0.9299 1.7166 0.2091 -0.1282 0.1565 679 LEU B CA 12399 C C . LEU B 679 ? 1.4216 0.9141 1.6888 0.2168 -0.1388 0.1337 679 LEU B C 12400 O O . LEU B 679 ? 1.4200 0.9779 1.7179 0.2174 -0.1323 0.1277 679 LEU B O 12401 C CB . LEU B 679 ? 1.3727 0.8483 1.6092 0.2411 -0.1123 0.1587 679 LEU B CB 12402 C CG . LEU B 679 ? 1.4683 0.8999 1.6724 0.2581 -0.1121 0.1699 679 LEU B CG 12403 C CD1 . LEU B 679 ? 1.5894 0.9575 1.7690 0.2781 -0.1302 0.1555 679 LEU B CD1 12404 C CD2 . LEU B 679 ? 1.7283 1.1431 1.9245 0.2335 -0.1118 0.1973 679 LEU B CD2 12405 N N . TYR B 680 ? 1.4212 0.8683 1.6693 0.2250 -0.1560 0.1201 680 TYR B N 12406 C CA . TYR B 680 ? 1.4245 0.8983 1.6812 0.2362 -0.1695 0.0998 680 TYR B CA 12407 C C . TYR B 680 ? 1.3453 0.7826 1.5681 0.2705 -0.1725 0.0896 680 TYR B C 12408 O O . TYR B 680 ? 1.4475 0.8299 1.6451 0.2728 -0.1802 0.0823 680 TYR B O 12409 C CB . TYR B 680 ? 1.7250 1.1922 1.9886 0.2047 -0.1870 0.0868 680 TYR B CB 12410 C CG . TYR B 680 ? 1.7395 1.2699 2.0403 0.1668 -0.1847 0.0862 680 TYR B CG 12411 C CD1 . TYR B 680 ? 1.7267 1.3328 2.0614 0.1736 -0.1734 0.0896 680 TYR B CD1 12412 C CD2 . TYR B 680 ? 1.7981 1.3139 2.0986 0.1211 -0.1913 0.0779 680 TYR B CD2 12413 C CE1 . TYR B 680 ? 1.7800 1.4568 2.1524 0.1376 -0.1701 0.0830 680 TYR B CE1 12414 C CE2 . TYR B 680 ? 1.9136 1.4967 2.2464 0.0792 -0.1865 0.0722 680 TYR B CE2 12415 C CZ . TYR B 680 ? 1.9156 1.5849 2.2869 0.0885 -0.1765 0.0739 680 TYR B CZ 12416 O OH . TYR B 680 ? 2.0668 1.8159 2.4740 0.0457 -0.1706 0.0626 680 TYR B OH 12417 N N . VAL B 681 ? 1.4115 0.8763 1.6303 0.2955 -0.1651 0.0870 681 VAL B N 12418 C CA . VAL B 681 ? 1.2784 0.7100 1.4568 0.3208 -0.1641 0.0765 681 VAL B CA 12419 C C . VAL B 681 ? 1.2705 0.7114 1.4386 0.3314 -0.1825 0.0645 681 VAL B C 12420 O O . VAL B 681 ? 1.5596 1.0435 1.7473 0.3396 -0.1866 0.0675 681 VAL B O 12421 C CB . VAL B 681 ? 1.2127 0.6516 1.3756 0.3377 -0.1387 0.0821 681 VAL B CB 12422 C CG1 . VAL B 681 ? 1.2274 0.6327 1.3410 0.3554 -0.1351 0.0684 681 VAL B CG1 12423 C CG2 . VAL B 681 ? 1.3048 0.7434 1.4737 0.3293 -0.1226 0.0928 681 VAL B CG2 12424 N N . VAL B 682 ? 1.2936 0.6980 1.4304 0.3335 -0.1946 0.0496 682 VAL B N 12425 C CA . VAL B 682 ? 1.3485 0.7613 1.4673 0.3419 -0.2142 0.0390 682 VAL B CA 12426 C C . VAL B 682 ? 1.5042 0.9079 1.5844 0.3686 -0.2053 0.0441 682 VAL B C 12427 O O . VAL B 682 ? 1.5728 0.9404 1.6149 0.3739 -0.1871 0.0412 682 VAL B O 12428 C CB . VAL B 682 ? 1.4422 0.8188 1.5346 0.3320 -0.2271 0.0185 682 VAL B CB 12429 C CG1 . VAL B 682 ? 1.4246 0.8176 1.4946 0.3381 -0.2486 0.0086 682 VAL B CG1 12430 C CG2 . VAL B 682 ? 1.4293 0.7957 1.5503 0.3047 -0.2336 0.0126 682 VAL B CG2 12431 N N . GLU B 683 ? 1.5635 0.9995 1.6506 0.3853 -0.2177 0.0503 683 GLU B N 12432 C CA . GLU B 683 ? 1.3503 0.7605 1.3891 0.4133 -0.2126 0.0575 683 GLU B CA 12433 C C . GLU B 683 ? 1.5995 0.9679 1.5767 0.4136 -0.2241 0.0475 683 GLU B C 12434 O O . GLU B 683 ? 2.0570 1.4341 2.0405 0.3970 -0.2421 0.0334 683 GLU B O 12435 C CB . GLU B 683 ? 1.4294 0.8846 1.4919 0.4394 -0.2279 0.0661 683 GLU B CB 12436 C CG . GLU B 683 ? 2.0547 1.5515 2.1704 0.4416 -0.2109 0.0730 683 GLU B CG 12437 C CD . GLU B 683 ? 2.4676 1.9317 2.5527 0.4700 -0.1894 0.0831 683 GLU B CD 12438 O OE1 . GLU B 683 ? 2.8655 2.2605 2.8828 0.4755 -0.1769 0.0856 683 GLU B OE1 12439 O OE2 . GLU B 683 ? 2.1323 1.6389 2.2588 0.4841 -0.1831 0.0856 683 GLU B OE2 12440 N N . GLU B 684 ? 1.4292 0.7492 1.3423 0.4283 -0.2113 0.0532 684 GLU B N 12441 C CA . GLU B 684 ? 1.7694 1.0458 1.6119 0.4233 -0.2174 0.0439 684 GLU B CA 12442 C C . GLU B 684 ? 1.5412 0.8089 1.3821 0.3956 -0.2094 0.0204 684 GLU B C 12443 O O . GLU B 684 ? 1.4912 0.7717 1.3384 0.3836 -0.2300 0.0056 684 GLU B O 12444 C CB . GLU B 684 ? 1.7182 1.0173 1.5514 0.4355 -0.2542 0.0459 684 GLU B CB 12445 C CG . GLU B 684 ? 1.9722 1.2777 1.7957 0.4737 -0.2675 0.0673 684 GLU B CG 12446 C CD . GLU B 684 ? 2.2038 1.4308 1.9301 0.4906 -0.2600 0.0807 684 GLU B CD 12447 O OE1 . GLU B 684 ? 2.2244 1.3967 1.8968 0.4670 -0.2343 0.0723 684 GLU B OE1 12448 O OE2 . GLU B 684 ? 2.3210 1.5408 2.0212 0.5275 -0.2798 0.0986 684 GLU B OE2 12449 N N . PRO B 685 ? 1.4403 0.6911 1.2741 0.3867 -0.1793 0.0141 685 PRO B N 12450 C CA . PRO B 685 ? 1.4697 0.7149 1.2974 0.3688 -0.1715 -0.0117 685 PRO B CA 12451 C C . PRO B 685 ? 1.5211 0.7394 1.2822 0.3583 -0.1766 -0.0304 685 PRO B C 12452 O O . PRO B 685 ? 1.7640 0.9523 1.4652 0.3627 -0.1759 -0.0196 685 PRO B O 12453 C CB . PRO B 685 ? 1.5787 0.8218 1.4014 0.3664 -0.1377 -0.0138 685 PRO B CB 12454 C CG . PRO B 685 ? 1.3823 0.6395 1.2371 0.3785 -0.1309 0.0117 685 PRO B CG 12455 C CD . PRO B 685 ? 1.4193 0.6656 1.2564 0.3937 -0.1513 0.0270 685 PRO B CD 12456 N N . GLU B 686 ? 1.5409 0.7655 1.3083 0.3448 -0.1813 -0.0585 686 GLU B N 12457 C CA . GLU B 686 ? 1.6810 0.8890 1.3883 0.3295 -0.1850 -0.0818 686 GLU B CA 12458 C C . GLU B 686 ? 1.7281 0.9149 1.3723 0.3173 -0.1535 -0.0950 686 GLU B C 12459 O O . GLU B 686 ? 1.7285 0.9319 1.3910 0.3148 -0.1312 -0.1112 686 GLU B O 12460 C CB . GLU B 686 ? 1.7574 0.9805 1.4945 0.3190 -0.1965 -0.1140 686 GLU B CB 12461 C CG . GLU B 686 ? 1.9371 1.1767 1.7302 0.3209 -0.2231 -0.1065 686 GLU B CG 12462 C CD . GLU B 686 ? 2.2284 1.4675 2.0383 0.3075 -0.2322 -0.1413 686 GLU B CD 12463 O OE1 . GLU B 686 ? 2.3855 1.6210 2.1521 0.2943 -0.2313 -0.1696 686 GLU B OE1 12464 O OE2 . GLU B 686 ? 2.2244 1.4623 2.0867 0.3081 -0.2388 -0.1418 686 GLU B OE2 12465 N N . CYS B 687 ? 1.7661 0.9171 1.3312 0.3083 -0.1519 -0.0885 687 CYS B N 12466 C CA . CYS B 687 ? 1.8272 0.9491 1.3167 0.2871 -0.1191 -0.1013 687 CYS B CA 12467 C C . CYS B 687 ? 1.9586 1.0600 1.3698 0.2611 -0.1233 -0.1217 687 CYS B C 12468 O O . CYS B 687 ? 2.0133 1.1141 1.4189 0.2653 -0.1539 -0.1144 687 CYS B O 12469 C CB . CYS B 687 ? 1.8219 0.8976 1.2717 0.2972 -0.1039 -0.0680 687 CYS B CB 12470 S SG . CYS B 687 ? 1.9861 1.0913 1.5136 0.3157 -0.0858 -0.0536 687 CYS B SG 12471 N N . PRO B 688 ? 2.0139 1.1062 1.3629 0.2300 -0.0917 -0.1500 688 PRO B N 12472 C CA . PRO B 688 ? 2.1328 1.2078 1.3997 0.1975 -0.0918 -0.1724 688 PRO B CA 12473 C C . PRO B 688 ? 2.3680 1.3734 1.5458 0.1976 -0.1060 -0.1347 688 PRO B C 12474 O O . PRO B 688 ? 2.4943 1.4652 1.6767 0.2273 -0.1151 -0.0933 688 PRO B O 12475 C CB . PRO B 688 ? 2.1281 1.2120 1.3478 0.1617 -0.0485 -0.2093 688 PRO B CB 12476 C CG . PRO B 688 ? 2.0634 1.1437 1.3116 0.1757 -0.0255 -0.1917 688 PRO B CG 12477 C CD . PRO B 688 ? 1.9682 1.0787 1.3221 0.2186 -0.0535 -0.1685 688 PRO B CD 12478 N N . LYS B 689 ? 2.4790 1.4650 1.5737 0.1661 -0.1084 -0.1499 689 LYS B N 12479 C CA . LYS B 689 ? 2.6486 1.5672 1.6496 0.1687 -0.1276 -0.1127 689 LYS B CA 12480 C C . LYS B 689 ? 2.7818 1.6257 1.6487 0.1266 -0.0941 -0.1149 689 LYS B C 12481 O O . LYS B 689 ? 2.8414 1.7082 1.6856 0.0836 -0.0603 -0.1585 689 LYS B O 12482 C CB . LYS B 689 ? 2.6767 1.6303 1.6811 0.1659 -0.1650 -0.1211 689 LYS B CB 12483 C CG . LYS B 689 ? 2.5293 1.5563 1.6590 0.1936 -0.1925 -0.1296 689 LYS B CG 12484 C CD . LYS B 689 ? 2.5612 1.5840 1.7483 0.2403 -0.2106 -0.0864 689 LYS B CD 12485 C CE . LYS B 689 ? 2.6860 1.6706 1.8091 0.2629 -0.2410 -0.0445 689 LYS B CE 12486 N NZ . LYS B 689 ? 2.5912 1.5845 1.7761 0.3109 -0.2584 -0.0090 689 LYS B NZ 12487 N N . GLY B 690 ? 2.7795 1.5335 1.5545 0.1392 -0.1034 -0.0691 690 GLY B N 12488 C CA . GLY B 690 ? 2.8720 1.5310 1.5019 0.0976 -0.0718 -0.0641 690 GLY B CA 12489 C C . GLY B 690 ? 2.9885 1.5871 1.5051 0.0901 -0.0993 -0.0379 690 GLY B C 12490 O O . GLY B 690 ? 2.9772 1.6216 1.4779 0.0590 -0.1103 -0.0661 690 GLY B O 12506 N N . ALA C 76 ? 3.2980 2.5410 2.4276 -0.1220 0.0151 0.3822 1492 ALA C N 12507 C CA . ALA C 76 ? 2.5304 1.7865 1.7880 -0.1624 -0.0350 0.3587 1492 ALA C CA 12508 C C . ALA C 76 ? 2.1825 1.4719 1.5814 -0.1938 0.0089 0.3873 1492 ALA C C 12509 O O . ALA C 76 ? 2.0611 1.3584 1.4623 -0.1852 0.0724 0.4426 1492 ALA C O 12510 C CB . ALA C 76 ? 2.2397 1.4942 1.5118 -0.1705 -0.0857 0.3841 1492 ALA C CB 12511 N N . ARG C 77 ? 1.9237 1.2425 1.4407 -0.2332 -0.0262 0.3559 1493 ARG C N 12512 C CA . ARG C 77 ? 1.6821 1.0375 1.3368 -0.2729 0.0097 0.3813 1493 ARG C CA 12513 C C . ARG C 77 ? 1.6512 1.0505 1.4252 -0.3153 -0.0390 0.3627 1493 ARG C C 12514 O O . ARG C 77 ? 1.6710 1.0834 1.4308 -0.3130 -0.1016 0.3201 1493 ARG C O 12515 C CB . ARG C 77 ? 1.6152 0.9824 1.2990 -0.2805 0.0393 0.3544 1493 ARG C CB 12516 C CG . ARG C 77 ? 1.7423 1.0941 1.3627 -0.2654 -0.0121 0.2830 1493 ARG C CG 12517 C CD . ARG C 77 ? 1.8916 1.2137 1.4540 -0.2329 0.0320 0.2651 1493 ARG C CD 12518 N NE . ARG C 77 ? 1.7163 1.0712 1.4035 -0.2619 0.0842 0.2915 1493 ARG C NE 12519 C CZ . ARG C 77 ? 1.6802 1.0569 1.4632 -0.2914 0.0636 0.2570 1493 ARG C CZ 12520 N NH1 . ARG C 77 ? 1.7161 1.0846 1.4815 -0.2942 -0.0127 0.1953 1493 ARG C NH1 12521 N NH2 . ARG C 77 ? 1.7858 1.1948 1.6888 -0.3219 0.1140 0.2918 1493 ARG C NH2 12522 N N . GLY C 78 ? 1.5505 0.9785 1.4401 -0.3536 -0.0100 0.3966 1494 GLY C N 12523 C CA . GLY C 78 ? 1.4086 0.8967 1.4043 -0.3756 -0.0439 0.3681 1494 GLY C CA 12524 C C . GLY C 78 ? 1.5036 0.9410 1.4676 -0.3598 -0.0678 0.4037 1494 GLY C C 12525 O O . GLY C 78 ? 1.3823 0.7733 1.2867 -0.3334 -0.0359 0.4575 1494 GLY C O 12526 N N . ASP C 79 ? 1.6465 1.1070 1.6561 -0.3682 -0.1247 0.3701 1495 ASP C N 12527 C CA . ASP C 79 ? 1.3218 0.7386 1.3080 -0.3391 -0.1554 0.3886 1495 ASP C CA 12528 C C . ASP C 79 ? 1.5942 1.0016 1.4900 -0.3036 -0.2016 0.3564 1495 ASP C C 12529 O O . ASP C 79 ? 1.9414 1.3988 1.8652 -0.3059 -0.2490 0.3035 1495 ASP C O 12530 C CB . ASP C 79 ? 1.2494 0.6961 1.3482 -0.3592 -0.1859 0.3671 1495 ASP C CB 12531 C CG . ASP C 79 ? 1.3218 0.7238 1.4128 -0.3248 -0.2320 0.3723 1495 ASP C CG 12532 O OD1 . ASP C 79 ? 1.6018 0.9404 1.6266 -0.3003 -0.2273 0.4273 1495 ASP C OD1 12533 O OD2 . ASP C 79 ? 1.2787 0.7178 1.4365 -0.3223 -0.2751 0.3222 1495 ASP C OD2 12534 N N . TRP C 80 ? 1.5152 0.8671 1.3040 -0.2733 -0.1882 0.3962 1496 TRP C N 12535 C CA . TRP C 80 ? 1.8044 1.1376 1.4866 -0.2440 -0.2252 0.3784 1496 TRP C CA 12536 C C . TRP C 80 ? 2.1545 1.4405 1.7256 -0.2199 -0.1923 0.4349 1496 TRP C C 12537 O O . TRP C 80 ? 2.1729 1.4541 1.7436 -0.2238 -0.1356 0.4779 1496 TRP C O 12538 C CB . TRP C 80 ? 1.9307 1.2956 1.5802 -0.2508 -0.2420 0.3214 1496 TRP C CB 12539 C CG . TRP C 80 ? 2.0795 1.4296 1.6354 -0.2288 -0.2959 0.3000 1496 TRP C CG 12540 C CD1 . TRP C 80 ? 2.1331 1.4370 1.5515 -0.2068 -0.2935 0.3057 1496 TRP C CD1 12541 C CD2 . TRP C 80 ? 2.1816 1.5672 1.7726 -0.2276 -0.3611 0.2721 1496 TRP C CD2 12542 N NE1 . TRP C 80 ? 2.2955 1.5957 1.6605 -0.1977 -0.3562 0.2880 1496 TRP C NE1 12543 C CE2 . TRP C 80 ? 2.3373 1.6899 1.8101 -0.2090 -0.3977 0.2706 1496 TRP C CE2 12544 C CE3 . TRP C 80 ? 2.1309 1.5796 1.8401 -0.2386 -0.3914 0.2479 1496 TRP C CE3 12545 C CZ2 . TRP C 80 ? 2.3444 1.7234 1.8197 -0.2036 -0.4636 0.2555 1496 TRP C CZ2 12546 C CZ3 . TRP C 80 ? 2.1162 1.6001 1.8277 -0.2265 -0.4534 0.2263 1496 TRP C CZ3 12547 C CH2 . TRP C 80 ? 2.1716 1.6198 1.7700 -0.2103 -0.4891 0.2350 1496 TRP C CH2 12548 N N . ASN C 81 ? 2.3720 1.6348 1.8499 -0.1972 -0.2276 0.4391 1497 ASN C N 12549 C CA . ASN C 81 ? 2.3618 1.5997 1.7201 -0.1765 -0.2014 0.4884 1497 ASN C CA 12550 C C . ASN C 81 ? 2.3694 1.5890 1.6280 -0.1614 -0.2518 0.4799 1497 ASN C C 12551 O O . ASN C 81 ? 2.3102 1.5335 1.5745 -0.1641 -0.3007 0.4298 1497 ASN C O 12552 C CB . ASN C 81 ? 2.3038 1.5372 1.7062 -0.1792 -0.1818 0.5725 1497 ASN C CB 12553 C CG . ASN C 81 ? 2.3936 1.6159 1.9082 -0.1883 -0.2364 0.5841 1497 ASN C CG 12554 O OD1 . ASN C 81 ? 2.5190 1.7428 2.0596 -0.1852 -0.2875 0.5339 1497 ASN C OD1 12555 N ND2 . ASN C 81 ? 2.2306 1.4432 1.8154 -0.1975 -0.2294 0.6518 1497 ASN C ND2 # 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 PHE 1 1 1 PHE PHE A . n A 1 2 ASN 2 2 2 ASN ASN A . n A 1 3 LEU 3 3 3 LEU LEU A . n A 1 4 ASP 4 4 4 ASP ASP A . n A 1 5 VAL 5 5 5 VAL VAL A . n A 1 6 ASP 6 6 6 ASP ASP A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 PRO 8 8 8 PRO PRO A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 GLU 10 10 10 GLU GLU A . n A 1 11 TYR 11 11 11 TYR TYR A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 GLY 13 13 13 GLY GLY A . n A 1 14 PRO 14 14 14 PRO PRO A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 TYR 18 18 18 TYR TYR A . n A 1 19 PHE 19 19 19 PHE PHE A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 PHE 21 21 21 PHE PHE A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 VAL 23 23 23 VAL VAL A . n A 1 24 ASP 24 24 24 ASP ASP A . n A 1 25 PHE 25 25 25 PHE PHE A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 VAL 27 27 27 VAL VAL A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 ALA 30 30 30 ALA ALA A . n A 1 31 SER 31 31 31 SER SER A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 ARG 33 33 33 ARG ARG A . n A 1 34 MET 34 34 34 MET MET A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 VAL 38 38 38 VAL VAL A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 LYS 42 42 42 LYS LYS A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 ASN 44 44 44 ASN ASN A . n A 1 45 THR 45 45 45 THR THR A . n A 1 46 THR 46 46 46 THR THR A . n A 1 47 GLN 47 47 47 GLN GLN A . n A 1 48 PRO 48 48 48 PRO PRO A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 VAL 51 51 51 VAL VAL A . n A 1 52 GLU 52 52 52 GLU GLU A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 GLY 54 54 54 GLY GLY A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 LYS 58 58 58 LYS LYS A . n A 1 59 CYS 59 59 59 CYS CYS A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 TRP 61 61 61 TRP TRP A . n A 1 62 SER 62 62 62 SER SER A . n A 1 63 SER 63 63 63 SER SER A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 ARG 65 65 65 ARG ARG A . n A 1 66 ARG 66 66 66 ARG ARG A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 GLN 68 68 68 GLN GLN A . n A 1 69 PRO 69 69 69 PRO PRO A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 THR 75 75 75 THR THR A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 ASN 77 77 77 ASN ASN A . n A 1 78 ARG 78 78 78 ARG ARG A . n A 1 79 ASP 79 79 79 ASP ASP A . n A 1 80 TYR 80 80 80 TYR TYR A . n A 1 81 ALA 81 81 81 ALA ALA A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ASP 83 83 83 ASP ASP A . n A 1 84 ASP 84 84 84 ASP ASP A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 GLU 87 87 87 GLU GLU A . n A 1 88 PHE 88 88 88 PHE PHE A . n A 1 89 LYS 89 89 89 LYS LYS A . n A 1 90 SER 90 90 90 SER SER A . n A 1 91 HIS 91 91 91 HIS HIS A . n A 1 92 GLN 92 92 92 GLN GLN A . n A 1 93 TRP 93 93 93 TRP TRP A . n A 1 94 PHE 94 94 94 PHE PHE A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 SER 97 97 97 SER SER A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 ARG 99 99 99 ARG ARG A . n A 1 100 SER 100 100 100 SER SER A . n A 1 101 LYS 101 101 101 LYS LYS A . n A 1 102 GLN 102 102 102 GLN GLN A . n A 1 103 ASP 103 103 103 ASP ASP A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 ILE 105 105 105 ILE ILE A . n A 1 106 LEU 106 106 106 LEU LEU A . n A 1 107 ALA 107 107 107 ALA ALA A . n A 1 108 CYS 108 108 108 CYS CYS A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 PRO 110 110 110 PRO PRO A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 TYR 112 112 112 TYR TYR A . n A 1 113 HIS 113 113 113 HIS HIS A . n A 1 114 TRP 114 114 114 TRP TRP A . n A 1 115 ARG 115 115 115 ARG ARG A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 GLU 117 117 117 GLU GLU A . n A 1 118 MET 118 118 118 MET MET A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 GLN 120 120 120 GLN GLN A . n A 1 121 GLU 121 121 121 GLU GLU A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 PRO 124 124 124 PRO PRO A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 GLY 126 126 126 GLY GLY A . n A 1 127 THR 127 127 127 THR THR A . n A 1 128 CYS 128 128 128 CYS CYS A . n A 1 129 PHE 129 129 129 PHE PHE A . n A 1 130 LEU 130 130 130 LEU LEU A . n A 1 131 GLN 131 131 131 GLN GLN A . n A 1 132 ASP 132 132 132 ASP ASP A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 THR 134 134 134 THR THR A . n A 1 135 LYS 135 135 135 LYS LYS A . n A 1 136 THR 136 136 136 THR THR A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 TYR 139 139 139 TYR TYR A . n A 1 140 ALA 140 140 140 ALA ALA A . n A 1 141 PRO 141 141 141 PRO PRO A . n A 1 142 CYS 142 142 142 CYS CYS A . n A 1 143 ARG 143 143 143 ARG ARG A . n A 1 144 SER 144 144 144 SER SER A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 ILE 147 147 147 ILE ILE A . n A 1 148 ASP 148 148 148 ASP ASP A . n A 1 149 ALA 149 149 149 ALA ALA A . n A 1 150 ASP 150 150 150 ASP ASP A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 GLN 152 152 152 GLN GLN A . n A 1 153 GLY 153 153 153 GLY GLY A . n A 1 154 PHE 154 154 154 PHE PHE A . n A 1 155 CYS 155 155 155 CYS CYS A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 GLY 158 158 158 GLY GLY A . n A 1 159 PHE 159 159 159 PHE PHE A . n A 1 160 SER 160 160 160 SER SER A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 PHE 163 163 163 PHE PHE A . n A 1 164 THR 164 164 164 THR THR A . n A 1 165 LYS 165 165 165 LYS LYS A . n A 1 166 ALA 166 166 166 ALA ALA A . n A 1 167 ASP 167 167 167 ASP ASP A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 VAL 169 169 169 VAL VAL A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 LEU 171 171 171 LEU LEU A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 GLY 173 173 173 GLY GLY A . n A 1 174 PRO 174 174 174 PRO PRO A . n A 1 175 GLY 175 175 175 GLY GLY A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 PHE 177 177 177 PHE PHE A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 TRP 179 179 179 TRP TRP A . n A 1 180 GLN 180 180 180 GLN GLN A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 ILE 184 184 184 ILE ILE A . n A 1 185 SER 185 185 185 SER SER A . n A 1 186 ASP 186 186 186 ASP ASP A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 VAL 188 188 188 VAL VAL A . n A 1 189 ALA 189 189 189 ALA ALA A . n A 1 190 GLU 190 190 190 GLU GLU A . n A 1 191 ILE 191 191 191 ILE ILE A . n A 1 192 VAL 192 192 192 VAL VAL A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LYS 194 194 194 LYS LYS A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 ASP 196 196 196 ASP ASP A . n A 1 197 PRO 197 197 197 PRO PRO A . n A 1 198 ASN 198 198 198 ASN ASN A . n A 1 199 VAL 199 199 199 VAL VAL A . n A 1 200 TYR 200 200 200 TYR TYR A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 LYS 203 203 203 LYS LYS A . n A 1 204 TYR 204 204 204 TYR TYR A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 ALA 209 209 209 ALA ALA A . n A 1 210 THR 210 210 210 THR THR A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 ALA 213 213 213 ALA ALA A . n A 1 214 GLN 214 214 214 GLN GLN A . n A 1 215 ALA 215 215 215 ALA ALA A . n A 1 216 ILE 216 216 216 ILE ILE A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 ASP 218 218 218 ASP ASP A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 SER 220 220 220 SER SER A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 LEU 222 222 222 LEU LEU A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 TYR 224 224 224 TYR TYR A . n A 1 225 SER 225 225 225 SER SER A . n A 1 226 VAL 226 226 226 VAL VAL A . n A 1 227 ALA 227 227 227 ALA ALA A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 ASP 230 230 230 ASP ASP A . n A 1 231 PHE 231 231 231 PHE PHE A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 GLY 233 233 233 GLY GLY A . n A 1 234 ASP 234 234 234 ASP ASP A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 ILE 236 236 236 ILE ILE A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ASP 238 238 238 ASP ASP A . n A 1 239 PHE 239 239 239 PHE PHE A . n A 1 240 VAL 240 240 240 VAL VAL A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 GLY 242 242 242 GLY GLY A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 PRO 244 244 244 PRO PRO A . n A 1 245 ARG 245 245 245 ARG ARG A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 ALA 247 247 247 ALA ALA A . n A 1 248 ARG 248 248 248 ARG ARG A . n A 1 249 THR 249 249 249 THR THR A . n A 1 250 LEU 250 250 250 LEU LEU A . n A 1 251 GLY 251 251 251 GLY GLY A . n A 1 252 MET 252 252 252 MET MET 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 ILE 255 255 255 ILE ILE A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 MET 261 261 261 MET MET A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 SER 263 263 263 SER SER A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 TYR 265 265 265 TYR TYR A . n A 1 266 ASN 266 266 266 ASN ASN A . n A 1 267 PHE 267 267 267 PHE PHE A . n A 1 268 THR 268 268 268 THR THR A . n A 1 269 GLY 269 269 269 GLY GLY A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 GLN 271 271 271 GLN GLN A . n A 1 272 MET 272 272 272 MET MET A . n A 1 273 ALA 273 273 273 ALA ALA A . n A 1 274 ALA 274 274 274 ALA ALA A . n A 1 275 TYR 275 275 275 TYR TYR A . n A 1 276 PHE 276 276 276 PHE PHE A . n A 1 277 GLY 277 277 277 GLY GLY A . n A 1 278 PHE 278 278 278 PHE PHE A . n A 1 279 SER 279 279 279 SER SER A . n A 1 280 VAL 280 280 280 VAL VAL A . n A 1 281 ALA 281 281 281 ALA ALA A . n A 1 282 ALA 282 282 282 ALA ALA A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 ASP 284 284 284 ASP ASP A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 GLY 287 287 287 GLY GLY A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 ASP 289 289 289 ASP ASP A . n A 1 290 TYR 290 290 290 TYR TYR A . n A 1 291 ALA 291 291 291 ALA ALA A . n A 1 292 ASP 292 292 292 ASP ASP A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 ILE 295 295 295 ILE ILE A . n A 1 296 GLY 296 296 296 GLY GLY A . n A 1 297 ALA 297 297 297 ALA ALA A . n A 1 298 PRO 298 298 298 PRO PRO A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 PHE 300 300 300 PHE PHE 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 ARG 303 303 303 ARG ARG A . n A 1 304 GLY 304 304 304 GLY GLY A . n A 1 305 SER 305 305 305 SER SER A . n A 1 306 ASP 306 306 306 ASP ASP A . n A 1 307 GLY 307 307 307 GLY GLY A . n A 1 308 LYS 308 308 308 LYS LYS A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 GLN 310 310 310 GLN GLN A . n A 1 311 GLU 311 311 311 GLU GLU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 GLY 313 313 313 GLY GLY A . n A 1 314 GLN 314 314 314 GLN GLN A . n A 1 315 VAL 315 315 315 VAL VAL A . n A 1 316 SER 316 316 316 SER SER A . n A 1 317 VAL 317 317 317 VAL VAL A . n A 1 318 SER 318 318 318 SER SER A . n A 1 319 LEU 319 319 319 LEU LEU A . n A 1 320 GLN 320 320 320 GLN GLN A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ALA 322 322 322 ALA ALA A . n A 1 323 SER 323 323 323 SER SER A . n A 1 324 GLY 324 324 324 GLY GLY A . n A 1 325 ASP 325 325 325 ASP ASP A . n A 1 326 PHE 326 326 326 PHE PHE A . n A 1 327 GLN 327 327 327 GLN GLN A . n A 1 328 THR 328 328 328 THR THR A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 LYS 330 330 330 LYS LYS A . n A 1 331 LEU 331 331 331 LEU LEU A . n A 1 332 ASN 332 332 332 ASN ASN A . n A 1 333 GLY 333 333 333 GLY GLY A . n A 1 334 PHE 334 334 334 PHE PHE A . n A 1 335 GLU 335 335 335 GLU GLU A . n A 1 336 VAL 336 336 336 VAL VAL A . n A 1 337 PHE 337 337 337 PHE PHE A . n A 1 338 ALA 338 338 338 ALA ALA A . n A 1 339 ARG 339 339 339 ARG ARG A . n A 1 340 PHE 340 340 340 PHE PHE A . n A 1 341 GLY 341 341 341 GLY GLY A . n A 1 342 SER 342 342 342 SER SER A . n A 1 343 ALA 343 343 343 ALA ALA A . n A 1 344 ILE 344 344 344 ILE ILE A . n A 1 345 ALA 345 345 345 ALA ALA A . n A 1 346 PRO 346 346 346 PRO PRO A . n A 1 347 LEU 347 347 347 LEU LEU A . n A 1 348 GLY 348 348 348 GLY GLY A . n A 1 349 ASP 349 349 349 ASP ASP A . n A 1 350 LEU 350 350 350 LEU LEU A . n A 1 351 ASP 351 351 351 ASP ASP A . n A 1 352 GLN 352 352 352 GLN GLN A . n A 1 353 ASP 353 353 353 ASP ASP A . n A 1 354 GLY 354 354 354 GLY GLY A . n A 1 355 PHE 355 355 355 PHE PHE A . n A 1 356 ASN 356 356 356 ASN ASN A . n A 1 357 ASP 357 357 357 ASP ASP A . n A 1 358 ILE 358 358 358 ILE ILE A . n A 1 359 ALA 359 359 359 ALA ALA A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 ALA 361 361 361 ALA ALA A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 PRO 363 363 363 PRO PRO A . n A 1 364 TYR 364 364 364 TYR TYR A . n A 1 365 GLY 365 365 365 GLY GLY A . n A 1 366 GLY 366 366 366 GLY GLY A . n A 1 367 GLU 367 367 367 GLU GLU A . n A 1 368 ASP 368 368 368 ASP ASP A . n A 1 369 LYS 369 369 369 LYS LYS A . n A 1 370 LYS 370 370 370 LYS LYS A . n A 1 371 GLY 371 371 371 GLY GLY A . n A 1 372 ILE 372 372 372 ILE ILE A . n A 1 373 VAL 373 373 373 VAL VAL A . n A 1 374 TYR 374 374 374 TYR TYR A . n A 1 375 ILE 375 375 375 ILE ILE A . n A 1 376 PHE 376 376 376 PHE PHE A . n A 1 377 ASN 377 377 377 ASN ASN A . n A 1 378 GLY 378 378 378 GLY GLY A . n A 1 379 ARG 379 379 379 ARG ARG A . n A 1 380 SER 380 380 380 SER SER A . n A 1 381 THR 381 381 381 THR THR A . n A 1 382 GLY 382 382 382 GLY GLY A . n A 1 383 LEU 383 383 383 LEU LEU A . n A 1 384 ASN 384 384 384 ASN ASN A . n A 1 385 ALA 385 385 385 ALA ALA A . n A 1 386 VAL 386 386 386 VAL VAL A . n A 1 387 PRO 387 387 387 PRO PRO A . n A 1 388 SER 388 388 388 SER SER A . n A 1 389 GLN 389 389 389 GLN GLN A . n A 1 390 ILE 390 390 390 ILE ILE A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 GLU 392 392 392 GLU GLU A . n A 1 393 GLY 393 393 393 GLY GLY A . n A 1 394 GLN 394 394 394 GLN GLN A . n A 1 395 TRP 395 395 395 TRP TRP A . n A 1 396 ALA 396 396 396 ALA ALA A . n A 1 397 ALA 397 397 397 ALA ALA A . n A 1 398 ARG 398 398 398 ARG ARG A . n A 1 399 SER 399 399 399 SER SER A . n A 1 400 MET 400 400 400 MET MET A . n A 1 401 PRO 401 401 401 PRO PRO A . n A 1 402 PRO 402 402 402 PRO PRO A . n A 1 403 SER 403 403 403 SER SER A . n A 1 404 PHE 404 404 404 PHE PHE A . n A 1 405 GLY 405 405 405 GLY GLY A . n A 1 406 TYR 406 406 406 TYR TYR A . n A 1 407 SER 407 407 407 SER SER A . n A 1 408 MET 408 408 408 MET MET A . n A 1 409 LYS 409 409 409 LYS LYS A . n A 1 410 GLY 410 410 410 GLY GLY A . n A 1 411 ALA 411 411 411 ALA ALA A . n A 1 412 THR 412 412 412 THR THR A . n A 1 413 ASP 413 413 413 ASP ASP A . n A 1 414 ILE 414 414 414 ILE ILE A . n A 1 415 ASP 415 415 415 ASP ASP A . n A 1 416 LYS 416 416 416 LYS LYS A . n A 1 417 ASN 417 417 417 ASN ASN A . n A 1 418 GLY 418 418 418 GLY GLY A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 PRO 420 420 420 PRO PRO A . n A 1 421 ASP 421 421 421 ASP ASP A . n A 1 422 LEU 422 422 422 LEU LEU A . n A 1 423 ILE 423 423 423 ILE ILE A . n A 1 424 VAL 424 424 424 VAL VAL A . n A 1 425 GLY 425 425 425 GLY GLY A . n A 1 426 ALA 426 426 426 ALA ALA A . n A 1 427 PHE 427 427 427 PHE PHE A . n A 1 428 GLY 428 428 428 GLY GLY A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 ASP 430 430 430 ASP ASP A . n A 1 431 ARG 431 431 431 ARG ARG A . n A 1 432 ALA 432 432 432 ALA ALA A . n A 1 433 ILE 433 433 433 ILE ILE A . n A 1 434 LEU 434 434 434 LEU LEU A . n A 1 435 TYR 435 435 435 TYR TYR A . n A 1 436 ARG 436 436 436 ARG ARG A . n A 1 437 ALA 437 437 437 ALA ALA A . n A 1 438 ARG 438 438 438 ARG ARG A . n A 1 439 PRO 439 439 439 PRO PRO A . n A 1 440 VAL 440 440 440 VAL VAL A . n A 1 441 ILE 441 441 441 ILE ILE A . n A 1 442 THR 442 442 442 THR THR A . n A 1 443 VAL 443 443 443 VAL VAL A . n A 1 444 ASN 444 444 444 ASN ASN A . n A 1 445 ALA 445 445 445 ALA ALA A . n A 1 446 GLY 446 446 446 GLY GLY A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 GLU 448 448 448 GLU GLU A . n A 1 449 VAL 449 449 449 VAL VAL A . n A 1 450 TYR 450 450 450 TYR TYR A . n A 1 451 PRO 451 451 451 PRO PRO A . n A 1 452 SER 452 452 452 SER SER A . n A 1 453 ILE 453 453 453 ILE ILE A . n A 1 454 LEU 454 454 454 LEU LEU A . n A 1 455 ASN 455 455 455 ASN ASN A . n A 1 456 GLN 456 456 456 GLN GLN A . n A 1 457 ASP 457 457 457 ASP ASP A . n A 1 458 ASN 458 458 458 ASN ASN A . n A 1 459 LYS 459 459 459 LYS LYS A . n A 1 460 THR 460 460 460 THR THR A . n A 1 461 CYS 461 461 461 CYS CYS A . n A 1 462 SER 462 462 462 SER SER A . n A 1 463 LEU 463 463 463 LEU LEU A . n A 1 464 PRO 464 464 464 PRO PRO A . n A 1 465 GLY 465 465 465 GLY GLY A . n A 1 466 THR 466 466 466 THR THR A . n A 1 467 ALA 467 467 467 ALA ALA A . n A 1 468 LEU 468 468 468 LEU LEU A . n A 1 469 LYS 469 469 469 LYS LYS A . n A 1 470 VAL 470 470 470 VAL VAL A . n A 1 471 SER 471 471 471 SER SER A . n A 1 472 CYS 472 472 472 CYS CYS A . n A 1 473 PHE 473 473 473 PHE PHE A . n A 1 474 ASN 474 474 474 ASN ASN A . n A 1 475 VAL 475 475 475 VAL VAL A . n A 1 476 ARG 476 476 476 ARG ARG A . n A 1 477 PHE 477 477 477 PHE PHE A . n A 1 478 CYS 478 478 478 CYS CYS A . n A 1 479 LEU 479 479 479 LEU LEU A . n A 1 480 LYS 480 480 480 LYS LYS A . n A 1 481 ALA 481 481 481 ALA ALA A . n A 1 482 ASP 482 482 482 ASP ASP A . n A 1 483 GLY 483 483 483 GLY GLY A . n A 1 484 LYS 484 484 484 LYS LYS A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 VAL 486 486 486 VAL VAL A . n A 1 487 LEU 487 487 487 LEU LEU A . n A 1 488 PRO 488 488 488 PRO PRO A . n A 1 489 ARG 489 489 489 ARG ARG A . n A 1 490 LYS 490 490 490 LYS LYS A . n A 1 491 LEU 491 491 491 LEU LEU A . n A 1 492 ASN 492 492 492 ASN ASN A . n A 1 493 PHE 493 493 493 PHE PHE A . n A 1 494 GLN 494 494 494 GLN GLN A . n A 1 495 VAL 495 495 495 VAL VAL A . n A 1 496 GLU 496 496 496 GLU GLU A . n A 1 497 LEU 497 497 497 LEU LEU A . n A 1 498 LEU 498 498 498 LEU LEU A . n A 1 499 LEU 499 499 499 LEU LEU A . n A 1 500 ASP 500 500 500 ASP ASP A . n A 1 501 LYS 501 501 501 LYS LYS A . n A 1 502 LEU 502 502 502 LEU LEU A . n A 1 503 LYS 503 503 503 LYS LYS A . n A 1 504 GLN 504 504 504 GLN GLN A . n A 1 505 LYS 505 505 505 LYS LYS A . n A 1 506 GLY 506 506 506 GLY GLY A . n A 1 507 ALA 507 507 507 ALA ALA A . n A 1 508 ILE 508 508 508 ILE ILE A . n A 1 509 ARG 509 509 509 ARG ARG A . n A 1 510 ARG 510 510 510 ARG ARG A . n A 1 511 ALA 511 511 511 ALA ALA A . n A 1 512 LEU 512 512 512 LEU LEU A . n A 1 513 PHE 513 513 513 PHE PHE A . n A 1 514 LEU 514 514 514 LEU LEU A . n A 1 515 TYR 515 515 515 TYR TYR A . n A 1 516 SER 516 516 516 SER SER A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 SER 518 518 518 SER SER A . n A 1 519 PRO 519 519 519 PRO PRO A . n A 1 520 SER 520 520 520 SER SER A . n A 1 521 HIS 521 521 521 HIS HIS A . n A 1 522 SER 522 522 522 SER SER A . n A 1 523 LYS 523 523 523 LYS LYS A . n A 1 524 ASN 524 524 524 ASN ASN A . n A 1 525 MET 525 525 525 MET MET A . n A 1 526 THR 526 526 526 THR THR A . n A 1 527 ILE 527 527 527 ILE ILE A . n A 1 528 SER 528 528 528 SER SER A . n A 1 529 ARG 529 529 529 ARG ARG A . n A 1 530 GLY 530 530 530 GLY GLY A . n A 1 531 GLY 531 531 531 GLY GLY A . n A 1 532 LEU 532 532 532 LEU LEU A . n A 1 533 MET 533 533 533 MET MET A . n A 1 534 GLN 534 534 534 GLN GLN A . n A 1 535 CYS 535 535 535 CYS CYS A . n A 1 536 GLU 536 536 536 GLU GLU A . n A 1 537 GLU 537 537 537 GLU GLU A . n A 1 538 LEU 538 538 538 LEU LEU A . n A 1 539 ILE 539 539 539 ILE ILE A . n A 1 540 ALA 540 540 540 ALA ALA A . n A 1 541 TYR 541 541 541 TYR TYR A . n A 1 542 LEU 542 542 542 LEU LEU A . n A 1 543 ARG 543 543 543 ARG ARG A . n A 1 544 ASP 544 544 544 ASP ASP A . n A 1 545 GLU 545 545 545 GLU GLU A . n A 1 546 SER 546 546 546 SER SER A . n A 1 547 GLU 547 547 547 GLU GLU A . n A 1 548 PHE 548 548 548 PHE PHE A . n A 1 549 ARG 549 549 549 ARG ARG A . n A 1 550 ASP 550 550 550 ASP ASP A . n A 1 551 LYS 551 551 551 LYS LYS A . n A 1 552 LEU 552 552 552 LEU LEU A . n A 1 553 THR 553 553 553 THR THR A . n A 1 554 PRO 554 554 554 PRO PRO A . n A 1 555 ILE 555 555 555 ILE ILE A . n A 1 556 THR 556 556 556 THR THR A . n A 1 557 ILE 557 557 557 ILE ILE A . n A 1 558 PHE 558 558 558 PHE PHE A . n A 1 559 MET 559 559 559 MET MET A . n A 1 560 GLU 560 560 560 GLU GLU A . n A 1 561 TYR 561 561 561 TYR TYR A . n A 1 562 ARG 562 562 562 ARG ARG A . n A 1 563 LEU 563 563 563 LEU LEU A . n A 1 564 ASP 564 564 564 ASP ASP A . n A 1 565 TYR 565 565 565 TYR TYR A . n A 1 566 ARG 566 566 566 ARG ARG A . n A 1 567 THR 567 567 567 THR THR A . n A 1 568 ALA 568 568 568 ALA ALA A . n A 1 569 ALA 569 569 569 ALA ALA A . n A 1 570 ASP 570 570 570 ASP ASP A . n A 1 571 THR 571 571 571 THR THR A . n A 1 572 THR 572 572 572 THR THR A . n A 1 573 GLY 573 573 573 GLY GLY A . n A 1 574 LEU 574 574 574 LEU LEU A . n A 1 575 GLN 575 575 575 GLN GLN A . n A 1 576 PRO 576 576 576 PRO PRO A . n A 1 577 ILE 577 577 577 ILE ILE A . n A 1 578 LEU 578 578 578 LEU LEU A . n A 1 579 ASN 579 579 579 ASN ASN A . n A 1 580 GLN 580 580 580 GLN GLN A . n A 1 581 PHE 581 581 581 PHE PHE A . n A 1 582 THR 582 582 582 THR THR A . n A 1 583 PRO 583 583 583 PRO PRO A . n A 1 584 ALA 584 584 584 ALA ALA A . n A 1 585 ASN 585 585 585 ASN ASN A . n A 1 586 ILE 586 586 586 ILE ILE A . n A 1 587 SER 587 587 587 SER SER A . n A 1 588 ARG 588 588 588 ARG ARG A . n A 1 589 GLN 589 589 589 GLN GLN A . n A 1 590 ALA 590 590 590 ALA ALA A . n A 1 591 HIS 591 591 591 HIS HIS A . n A 1 592 ILE 592 592 592 ILE ILE A . n A 1 593 LEU 593 593 593 LEU LEU A . n A 1 594 LEU 594 594 594 LEU LEU A . n A 1 595 ASP 595 595 595 ASP ASP A . n A 1 596 CYS 596 596 596 CYS CYS A . n A 1 597 GLY 597 597 597 GLY GLY A . n A 1 598 GLU 598 598 598 GLU GLU A . n A 1 599 ASP 599 599 599 ASP ASP A . n A 1 600 ASN 600 600 600 ASN ASN A . n A 1 601 VAL 601 601 601 VAL VAL A . n A 1 602 CYS 602 602 602 CYS CYS A . n A 1 603 LYS 603 603 603 LYS LYS A . n A 1 604 PRO 604 604 604 PRO PRO A . n A 1 605 LYS 605 605 605 LYS LYS A . n A 1 606 LEU 606 606 606 LEU LEU A . n A 1 607 GLU 607 607 607 GLU GLU A . n A 1 608 VAL 608 608 608 VAL VAL A . n A 1 609 SER 609 609 609 SER SER A . n A 1 610 VAL 610 610 610 VAL VAL A . n A 1 611 ASP 611 611 611 ASP ASP A . n A 1 612 SER 612 612 612 SER SER A . n A 1 613 ASP 613 613 613 ASP ASP A . n A 1 614 GLN 614 614 614 GLN GLN A . n A 1 615 LYS 615 615 615 LYS LYS A . n A 1 616 LYS 616 616 616 LYS LYS A . n A 1 617 ILE 617 617 617 ILE ILE A . n A 1 618 TYR 618 618 618 TYR TYR A . n A 1 619 ILE 619 619 619 ILE ILE A . n A 1 620 GLY 620 620 620 GLY GLY A . n A 1 621 ASP 621 621 621 ASP ASP A . n A 1 622 ASP 622 622 622 ASP ASP A . n A 1 623 ASN 623 623 623 ASN ASN A . n A 1 624 PRO 624 624 624 PRO PRO A . n A 1 625 LEU 625 625 625 LEU LEU A . n A 1 626 THR 626 626 626 THR THR A . n A 1 627 LEU 627 627 627 LEU LEU A . n A 1 628 ILE 628 628 628 ILE ILE A . n A 1 629 VAL 629 629 629 VAL VAL A . n A 1 630 LYS 630 630 630 LYS LYS A . n A 1 631 ALA 631 631 631 ALA ALA A . n A 1 632 GLN 632 632 632 GLN GLN A . n A 1 633 ASN 633 633 633 ASN ASN A . n A 1 634 GLN 634 634 634 GLN GLN A . n A 1 635 GLY 635 635 635 GLY GLY A . n A 1 636 GLU 636 636 636 GLU GLU A . n A 1 637 GLY 637 637 637 GLY GLY A . n A 1 638 ALA 638 638 638 ALA ALA A . n A 1 639 TYR 639 639 639 TYR TYR A . n A 1 640 GLU 640 640 640 GLU GLU A . n A 1 641 ALA 641 641 641 ALA ALA A . n A 1 642 GLU 642 642 642 GLU GLU A . n A 1 643 LEU 643 643 643 LEU LEU A . n A 1 644 ILE 644 644 644 ILE ILE A . n A 1 645 VAL 645 645 645 VAL VAL A . n A 1 646 SER 646 646 646 SER SER A . n A 1 647 ILE 647 647 647 ILE ILE A . n A 1 648 PRO 648 648 648 PRO PRO A . n A 1 649 LEU 649 649 649 LEU LEU A . n A 1 650 GLN 650 650 650 GLN GLN A . n A 1 651 ALA 651 651 651 ALA ALA A . n A 1 652 ASP 652 652 652 ASP ASP A . n A 1 653 PHE 653 653 653 PHE PHE A . n A 1 654 ILE 654 654 654 ILE ILE A . n A 1 655 GLY 655 655 655 GLY GLY A . n A 1 656 VAL 656 656 656 VAL VAL A . n A 1 657 VAL 657 657 657 VAL VAL A . n A 1 658 ARG 658 658 658 ARG ARG A . n A 1 659 ASN 659 659 659 ASN ASN A . n A 1 660 ASN 660 660 660 ASN ASN A . n A 1 661 GLU 661 661 661 GLU GLU A . n A 1 662 ALA 662 662 662 ALA ALA A . n A 1 663 LEU 663 663 663 LEU LEU A . n A 1 664 ALA 664 664 664 ALA ALA A . n A 1 665 ARG 665 665 665 ARG ARG A . n A 1 666 LEU 666 666 666 LEU LEU A . n A 1 667 SER 667 667 667 SER SER A . n A 1 668 CYS 668 668 668 CYS CYS A . n A 1 669 ALA 669 669 669 ALA ALA A . n A 1 670 PHE 670 670 670 PHE PHE A . n A 1 671 LYS 671 671 671 LYS LYS A . n A 1 672 THR 672 672 672 THR THR A . n A 1 673 GLU 673 673 673 GLU GLU A . n A 1 674 ASN 674 674 674 ASN ASN A . n A 1 675 GLN 675 675 675 GLN GLN A . n A 1 676 THR 676 676 676 THR THR A . n A 1 677 ARG 677 677 677 ARG ARG A . n A 1 678 GLN 678 678 678 GLN GLN A . n A 1 679 VAL 679 679 679 VAL VAL A . n A 1 680 VAL 680 680 680 VAL VAL A . n A 1 681 CYS 681 681 681 CYS CYS A . n A 1 682 ASP 682 682 682 ASP ASP A . n A 1 683 LEU 683 683 683 LEU LEU A . n A 1 684 GLY 684 684 684 GLY GLY A . n A 1 685 ASN 685 685 685 ASN ASN A . n A 1 686 PRO 686 686 686 PRO PRO A . n A 1 687 MET 687 687 687 MET MET A . n A 1 688 LYS 688 688 688 LYS LYS A . n A 1 689 ALA 689 689 689 ALA ALA A . n A 1 690 GLY 690 690 690 GLY GLY A . n A 1 691 THR 691 691 691 THR THR A . n A 1 692 GLN 692 692 692 GLN GLN A . n A 1 693 LEU 693 693 693 LEU LEU A . n A 1 694 LEU 694 694 694 LEU LEU A . n A 1 695 ALA 695 695 695 ALA ALA A . n A 1 696 GLY 696 696 696 GLY GLY A . n A 1 697 LEU 697 697 697 LEU LEU A . n A 1 698 ARG 698 698 698 ARG ARG A . n A 1 699 PHE 699 699 699 PHE PHE A . n A 1 700 SER 700 700 700 SER SER A . n A 1 701 VAL 701 701 701 VAL VAL A . n A 1 702 HIS 702 702 702 HIS HIS A . n A 1 703 GLN 703 703 703 GLN GLN A . n A 1 704 GLN 704 704 704 GLN GLN A . n A 1 705 SER 705 705 705 SER SER A . n A 1 706 GLU 706 706 706 GLU GLU A . n A 1 707 MET 707 707 707 MET MET A . n A 1 708 ASP 708 708 708 ASP ASP A . n A 1 709 THR 709 709 709 THR THR A . n A 1 710 SER 710 710 710 SER SER A . n A 1 711 VAL 711 711 711 VAL VAL A . n A 1 712 LYS 712 712 712 LYS LYS A . n A 1 713 PHE 713 713 713 PHE PHE A . n A 1 714 ASP 714 714 714 ASP ASP A . n A 1 715 LEU 715 715 715 LEU LEU A . n A 1 716 GLN 716 716 716 GLN GLN A . n A 1 717 ILE 717 717 717 ILE ILE A . n A 1 718 GLN 718 718 718 GLN GLN A . n A 1 719 SER 719 719 719 SER SER A . n A 1 720 SER 720 720 720 SER SER A . n A 1 721 ASN 721 721 721 ASN ASN A . n A 1 722 LEU 722 722 722 LEU LEU A . n A 1 723 PHE 723 723 723 PHE PHE A . n A 1 724 ASP 724 724 724 ASP ASP A . n A 1 725 LYS 725 725 725 LYS LYS A . n A 1 726 VAL 726 726 726 VAL VAL A . n A 1 727 SER 727 727 727 SER SER A . n A 1 728 PRO 728 728 728 PRO PRO A . n A 1 729 VAL 729 729 729 VAL VAL A . n A 1 730 VAL 730 730 730 VAL VAL A . n A 1 731 SER 731 731 731 SER SER A . n A 1 732 HIS 732 732 732 HIS HIS A . n A 1 733 LYS 733 733 733 LYS LYS A . n A 1 734 VAL 734 734 734 VAL VAL A . n A 1 735 ASP 735 735 735 ASP ASP A . n A 1 736 LEU 736 736 736 LEU LEU A . n A 1 737 ALA 737 737 737 ALA ALA A . n A 1 738 VAL 738 738 738 VAL VAL A . n A 1 739 LEU 739 739 739 LEU LEU A . n A 1 740 ALA 740 740 740 ALA ALA A . n A 1 741 ALA 741 741 741 ALA ALA A . n A 1 742 VAL 742 742 742 VAL VAL A . n A 1 743 GLU 743 743 743 GLU GLU A . n A 1 744 ILE 744 744 744 ILE ILE A . n A 1 745 ARG 745 745 745 ARG ARG A . n A 1 746 GLY 746 746 746 GLY GLY A . n A 1 747 VAL 747 747 747 VAL VAL A . n A 1 748 SER 748 748 748 SER SER A . n A 1 749 SER 749 749 749 SER SER A . n A 1 750 PRO 750 750 750 PRO PRO A . n A 1 751 ASP 751 751 751 ASP ASP A . n A 1 752 HIS 752 752 752 HIS HIS A . n A 1 753 VAL 753 753 753 VAL VAL A . n A 1 754 PHE 754 754 754 PHE PHE A . n A 1 755 LEU 755 755 755 LEU LEU A . n A 1 756 PRO 756 756 756 PRO PRO A . n A 1 757 ILE 757 757 757 ILE ILE A . n A 1 758 PRO 758 758 758 PRO PRO A . n A 1 759 ASN 759 759 759 ASN ASN A . n A 1 760 TRP 760 760 760 TRP TRP A . n A 1 761 GLU 761 761 761 GLU GLU A . n A 1 762 HIS 762 762 762 HIS HIS A . n A 1 763 LYS 763 763 763 LYS LYS A . n A 1 764 GLU 764 764 764 GLU GLU A . n A 1 765 ASN 765 765 765 ASN ASN A . n A 1 766 PRO 766 766 766 PRO PRO A . n A 1 767 GLU 767 767 767 GLU GLU A . n A 1 768 THR 768 768 768 THR THR A . n A 1 769 GLU 769 769 769 GLU GLU A . n A 1 770 GLU 770 770 770 GLU GLU A . n A 1 771 ASP 771 771 771 ASP ASP A . n A 1 772 VAL 772 772 772 VAL VAL A . n A 1 773 GLY 773 773 773 GLY GLY A . n A 1 774 PRO 774 774 774 PRO PRO A . n A 1 775 VAL 775 775 775 VAL VAL A . n A 1 776 VAL 776 776 776 VAL VAL A . n A 1 777 GLN 777 777 777 GLN GLN A . n A 1 778 HIS 778 778 778 HIS HIS A . n A 1 779 ILE 779 779 779 ILE ILE A . n A 1 780 TYR 780 780 780 TYR TYR A . n A 1 781 GLU 781 781 781 GLU GLU A . n A 1 782 LEU 782 782 782 LEU LEU A . n A 1 783 ARG 783 783 783 ARG ARG A . n A 1 784 ASN 784 784 784 ASN ASN A . n A 1 785 ASN 785 785 785 ASN ASN A . n A 1 786 GLY 786 786 786 GLY GLY A . n A 1 787 PRO 787 787 787 PRO PRO A . n A 1 788 SER 788 788 788 SER SER A . n A 1 789 SER 789 789 789 SER SER A . n A 1 790 PHE 790 790 790 PHE PHE A . n A 1 791 SER 791 791 791 SER SER A . n A 1 792 LYS 792 792 792 LYS LYS A . n A 1 793 ALA 793 793 793 ALA ALA A . n A 1 794 MET 794 794 794 MET MET A . n A 1 795 LEU 795 795 795 LEU LEU A . n A 1 796 HIS 796 796 796 HIS HIS A . n A 1 797 LEU 797 797 797 LEU LEU A . n A 1 798 GLN 798 798 798 GLN GLN A . n A 1 799 TRP 799 799 799 TRP TRP A . n A 1 800 PRO 800 800 800 PRO PRO A . n A 1 801 TYR 801 801 801 TYR TYR A . n A 1 802 LYS 802 802 802 LYS LYS A . n A 1 803 TYR 803 803 803 TYR TYR A . n A 1 804 ASN 804 804 804 ASN ASN A . n A 1 805 ASN 805 805 805 ASN ASN A . n A 1 806 ASN 806 806 806 ASN ASN A . n A 1 807 THR 807 807 807 THR THR A . n A 1 808 LEU 808 808 808 LEU LEU A . n A 1 809 LEU 809 809 809 LEU LEU A . n A 1 810 TYR 810 810 810 TYR TYR A . n A 1 811 ILE 811 811 811 ILE ILE A . n A 1 812 LEU 812 812 812 LEU LEU A . n A 1 813 HIS 813 813 813 HIS HIS A . n A 1 814 TYR 814 814 814 TYR TYR A . n A 1 815 ASP 815 815 815 ASP ASP A . n A 1 816 ILE 816 816 816 ILE ILE A . n A 1 817 ASP 817 817 817 ASP ASP A . n A 1 818 GLY 818 818 818 GLY GLY A . n A 1 819 PRO 819 819 819 PRO PRO A . n A 1 820 MET 820 820 820 MET MET A . n A 1 821 ASN 821 821 821 ASN ASN A . n A 1 822 CYS 822 822 822 CYS CYS A . n A 1 823 THR 823 823 823 THR THR A . n A 1 824 SER 824 824 824 SER SER A . n A 1 825 ASP 825 825 825 ASP ASP A . n A 1 826 MET 826 826 826 MET MET A . n A 1 827 GLU 827 827 827 GLU GLU A . n A 1 828 ILE 828 828 828 ILE ILE A . n A 1 829 ASN 829 829 829 ASN ASN A . n A 1 830 PRO 830 830 830 PRO PRO A . n A 1 831 LEU 831 831 831 LEU LEU A . n A 1 832 ARG 832 832 832 ARG ARG A . n A 1 833 ILE 833 833 833 ILE ILE A . n A 1 834 LYS 834 834 834 LYS LYS A . n A 1 835 ILE 835 835 835 ILE ILE A . n A 1 836 SER 836 836 ? ? ? A . n A 1 837 SER 837 837 ? ? ? A . n A 1 838 LEU 838 838 ? ? ? A . n A 1 839 GLN 839 839 ? ? ? A . n A 1 840 THR 840 840 ? ? ? A . n A 1 841 THR 841 841 ? ? ? A . n A 1 842 GLU 842 842 ? ? ? A . n A 1 843 LYS 843 843 ? ? ? A . n A 1 844 ASN 844 844 ? ? ? A . n A 1 845 ASP 845 845 ? ? ? A . n A 1 846 THR 846 846 ? ? ? A . n A 1 847 VAL 847 847 ? ? ? A . n A 1 848 ALA 848 848 ? ? ? A . n A 1 849 GLY 849 849 ? ? ? A . n A 1 850 GLN 850 850 ? ? ? A . n A 1 851 GLY 851 851 ? ? ? A . n A 1 852 GLU 852 852 ? ? ? A . n A 1 853 ARG 853 853 ? ? ? A . n A 1 854 ASP 854 854 ? ? ? A . n A 1 855 HIS 855 855 ? ? ? A . n A 1 856 LEU 856 856 ? ? ? A . n A 1 857 ILE 857 857 ? ? ? A . n A 1 858 THR 858 858 ? ? ? A . n A 1 859 LYS 859 859 ? ? ? A . n A 1 860 ARG 860 860 ? ? ? A . n A 1 861 ASP 861 861 ? ? ? A . n A 1 862 LEU 862 862 ? ? ? A . n A 1 863 ALA 863 863 ? ? ? A . n A 1 864 LEU 864 864 ? ? ? A . n A 1 865 SER 865 865 ? ? ? A . n A 1 866 GLU 866 866 ? ? ? A . n A 1 867 GLY 867 867 ? ? ? A . n A 1 868 ASP 868 868 868 ASP ASP A . n A 1 869 ILE 869 869 869 ILE ILE A . n A 1 870 HIS 870 870 870 HIS HIS A . n A 1 871 THR 871 871 871 THR THR A . n A 1 872 LEU 872 872 872 LEU LEU A . n A 1 873 GLY 873 873 873 GLY GLY A . n A 1 874 CYS 874 874 874 CYS CYS A . n A 1 875 GLY 875 875 875 GLY GLY A . n A 1 876 VAL 876 876 876 VAL VAL A . n A 1 877 ALA 877 877 877 ALA ALA A . n A 1 878 GLN 878 878 878 GLN GLN A . n A 1 879 CYS 879 879 879 CYS CYS A . n A 1 880 LEU 880 880 880 LEU LEU A . n A 1 881 LYS 881 881 881 LYS LYS A . n A 1 882 ILE 882 882 882 ILE ILE A . n A 1 883 VAL 883 883 883 VAL VAL A . n A 1 884 CYS 884 884 884 CYS CYS A . n A 1 885 GLN 885 885 885 GLN GLN A . n A 1 886 VAL 886 886 886 VAL VAL A . n A 1 887 GLY 887 887 887 GLY GLY A . n A 1 888 ARG 888 888 888 ARG ARG A . n A 1 889 LEU 889 889 889 LEU LEU A . n A 1 890 ASP 890 890 890 ASP ASP A . n A 1 891 ARG 891 891 891 ARG ARG A . n A 1 892 GLY 892 892 892 GLY GLY A . n A 1 893 LYS 893 893 893 LYS LYS A . n A 1 894 SER 894 894 894 SER SER A . n A 1 895 ALA 895 895 895 ALA ALA A . n A 1 896 ILE 896 896 896 ILE ILE A . n A 1 897 LEU 897 897 897 LEU LEU A . n A 1 898 TYR 898 898 898 TYR TYR A . n A 1 899 VAL 899 899 899 VAL VAL A . n A 1 900 LYS 900 900 900 LYS LYS A . n A 1 901 SER 901 901 901 SER SER A . n A 1 902 LEU 902 902 902 LEU LEU A . n A 1 903 LEU 903 903 903 LEU LEU A . n A 1 904 TRP 904 904 904 TRP TRP A . n A 1 905 THR 905 905 905 THR THR A . n A 1 906 GLU 906 906 906 GLU GLU A . n A 1 907 THR 907 907 907 THR THR A . n A 1 908 PHE 908 908 908 PHE PHE A . n A 1 909 MET 909 909 909 MET MET A . n A 1 910 ASN 910 910 910 ASN ASN A . n A 1 911 LYS 911 911 911 LYS LYS A . n A 1 912 GLU 912 912 912 GLU GLU A . n A 1 913 ASN 913 913 913 ASN ASN A . n A 1 914 GLN 914 914 914 GLN GLN A . n A 1 915 ASN 915 915 915 ASN ASN A . n A 1 916 HIS 916 916 916 HIS HIS A . n A 1 917 SER 917 917 917 SER SER A . n A 1 918 TYR 918 918 918 TYR TYR A . n A 1 919 SER 919 919 919 SER SER A . n A 1 920 LEU 920 920 920 LEU LEU A . n A 1 921 LYS 921 921 921 LYS LYS A . n A 1 922 SER 922 922 922 SER SER A . n A 1 923 SER 923 923 923 SER SER A . n A 1 924 ALA 924 924 924 ALA ALA A . n A 1 925 SER 925 925 925 SER SER A . n A 1 926 PHE 926 926 926 PHE PHE A . n A 1 927 ASN 927 927 927 ASN ASN A . n A 1 928 VAL 928 928 928 VAL VAL A . n A 1 929 ILE 929 929 929 ILE ILE A . n A 1 930 GLU 930 930 930 GLU GLU A . n A 1 931 PHE 931 931 931 PHE PHE A . n A 1 932 PRO 932 932 932 PRO PRO A . n A 1 933 TYR 933 933 933 TYR TYR A . n A 1 934 LYS 934 934 934 LYS LYS A . n A 1 935 ASN 935 935 935 ASN ASN A . n A 1 936 LEU 936 936 936 LEU LEU A . n A 1 937 PRO 937 937 937 PRO PRO A . n A 1 938 ILE 938 938 938 ILE ILE A . n A 1 939 GLU 939 939 939 GLU GLU A . n A 1 940 ASP 940 940 940 ASP ASP A . n A 1 941 ILE 941 941 941 ILE ILE A . n A 1 942 THR 942 942 942 THR THR A . n A 1 943 ASN 943 943 943 ASN ASN A . n A 1 944 SER 944 944 944 SER SER A . n A 1 945 THR 945 945 945 THR THR A . n A 1 946 LEU 946 946 946 LEU LEU A . n A 1 947 VAL 947 947 947 VAL VAL A . n A 1 948 THR 948 948 948 THR THR A . n A 1 949 THR 949 949 949 THR THR A . n A 1 950 ASN 950 950 950 ASN ASN A . n A 1 951 VAL 951 951 951 VAL VAL A . n A 1 952 THR 952 952 952 THR THR A . n A 1 953 TRP 953 953 953 TRP TRP A . n A 1 954 GLY 954 954 954 GLY GLY A . n A 1 955 ILE 955 955 955 ILE ILE A . n A 1 956 GLN 956 956 956 GLN GLN A . n A 1 957 PRO 957 957 ? ? ? A . n A 1 958 ALA 958 958 ? ? ? A . n A 1 959 PRO 959 959 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 PRO 2 2 2 PRO PRO B . n B 2 3 ASN 3 3 3 ASN ASN B . n B 2 4 ILE 4 4 4 ILE ILE B . n B 2 5 CYS 5 5 5 CYS CYS B . n B 2 6 THR 6 6 6 THR THR B . n B 2 7 THR 7 7 7 THR THR B . n B 2 8 ARG 8 8 8 ARG ARG B . n B 2 9 GLY 9 9 9 GLY GLY B . n B 2 10 VAL 10 10 10 VAL VAL B . n B 2 11 SER 11 11 11 SER SER B . n B 2 12 SER 12 12 12 SER SER B . n B 2 13 CYS 13 13 13 CYS CYS B . n B 2 14 GLN 14 14 14 GLN GLN B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 CYS 16 16 16 CYS CYS B . n B 2 17 LEU 17 17 17 LEU LEU B . n B 2 18 ALA 18 18 18 ALA ALA B . n B 2 19 VAL 19 19 19 VAL VAL B . n B 2 20 SER 20 20 20 SER SER B . n B 2 21 PRO 21 21 21 PRO PRO B . n B 2 22 MET 22 22 22 MET MET B . n B 2 23 CYS 23 23 23 CYS CYS B . n B 2 24 ALA 24 24 24 ALA ALA B . n B 2 25 TRP 25 25 25 TRP TRP B . n B 2 26 CYS 26 26 26 CYS CYS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASP 28 28 28 ASP ASP B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 ALA 30 30 30 ALA ALA B . n B 2 31 LEU 31 31 31 LEU LEU B . n B 2 32 PRO 32 32 32 PRO PRO B . n B 2 33 LEU 33 33 33 LEU LEU B . n B 2 34 GLY 34 34 34 GLY GLY B . n B 2 35 SER 35 35 35 SER SER B . n B 2 36 PRO 36 36 36 PRO PRO B . n B 2 37 ARG 37 37 37 ARG ARG B . n B 2 38 CYS 38 38 38 CYS CYS B . n B 2 39 ASP 39 39 39 ASP ASP B . n B 2 40 LEU 40 40 40 LEU LEU B . n B 2 41 LYS 41 41 41 LYS LYS B . n B 2 42 GLU 42 42 42 GLU GLU B . n B 2 43 ASN 43 43 43 ASN ASN B . n B 2 44 LEU 44 44 44 LEU LEU B . n B 2 45 LEU 45 45 45 LEU LEU B . n B 2 46 LYS 46 46 46 LYS LYS B . n B 2 47 ASP 47 47 47 ASP ASP B . n B 2 48 ASN 48 48 48 ASN ASN B . n B 2 49 CYS 49 49 49 CYS CYS B . n B 2 50 ALA 50 50 50 ALA ALA B . n B 2 51 PRO 51 51 51 PRO PRO B . n B 2 52 GLU 52 52 52 GLU GLU B . n B 2 53 SER 53 53 53 SER SER B . n B 2 54 ILE 54 54 54 ILE ILE B . n B 2 55 GLU 55 55 55 GLU GLU B . n B 2 56 PHE 56 56 56 PHE PHE B . n B 2 57 PRO 57 57 57 PRO PRO B . n B 2 58 VAL 58 58 58 VAL VAL B . n B 2 59 SER 59 59 59 SER SER B . n B 2 60 GLU 60 60 60 GLU GLU B . n B 2 61 ALA 61 61 61 ALA ALA B . n B 2 62 ARG 62 62 62 ARG ARG B . n B 2 63 VAL 63 63 63 VAL VAL B . n B 2 64 LEU 64 64 64 LEU LEU B . n B 2 65 GLU 65 65 65 GLU GLU B . n B 2 66 ASP 66 66 66 ASP ASP B . n B 2 67 ARG 67 67 67 ARG ARG B . n B 2 68 PRO 68 68 68 PRO PRO B . n B 2 69 LEU 69 69 69 LEU LEU B . n B 2 70 SER 70 70 70 SER SER B . n B 2 71 ASP 71 71 71 ASP ASP B . n B 2 72 LYS 72 72 72 LYS LYS B . n B 2 73 GLY 73 73 73 GLY GLY B . n B 2 74 SER 74 74 74 SER SER B . n B 2 75 GLY 75 75 75 GLY GLY B . n B 2 76 ASP 76 76 76 ASP ASP B . n B 2 77 SER 77 77 77 SER SER B . n B 2 78 SER 78 78 78 SER SER B . n B 2 79 GLN 79 79 79 GLN GLN B . n B 2 80 VAL 80 80 80 VAL VAL B . n B 2 81 THR 81 81 81 THR THR B . n B 2 82 GLN 82 82 82 GLN GLN B . n B 2 83 VAL 83 83 83 VAL VAL B . n B 2 84 SER 84 84 84 SER SER B . n B 2 85 PRO 85 85 85 PRO PRO B . n B 2 86 GLN 86 86 86 GLN GLN B . n B 2 87 ARG 87 87 87 ARG ARG B . n B 2 88 ILE 88 88 88 ILE ILE B . n B 2 89 ALA 89 89 89 ALA ALA B . n B 2 90 LEU 90 90 90 LEU LEU B . n B 2 91 ARG 91 91 91 ARG ARG B . n B 2 92 LEU 92 92 92 LEU LEU B . n B 2 93 ARG 93 93 93 ARG ARG B . n B 2 94 PRO 94 94 94 PRO PRO B . n B 2 95 ASP 95 95 95 ASP ASP B . n B 2 96 ASP 96 96 96 ASP ASP B . n B 2 97 SER 97 97 97 SER SER B . n B 2 98 LYS 98 98 98 LYS LYS B . n B 2 99 ASN 99 99 99 ASN ASN B . n B 2 100 PHE 100 100 100 PHE PHE B . n B 2 101 SER 101 101 101 SER SER B . n B 2 102 ILE 102 102 102 ILE ILE B . n B 2 103 GLN 103 103 103 GLN GLN B . n B 2 104 VAL 104 104 104 VAL VAL B . n B 2 105 ARG 105 105 105 ARG ARG B . n B 2 106 GLN 106 106 106 GLN GLN B . n B 2 107 VAL 107 107 107 VAL VAL B . n B 2 108 GLU 108 108 108 GLU GLU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 TYR 110 110 110 TYR TYR B . n B 2 111 PRO 111 111 111 PRO PRO B . n B 2 112 VAL 112 112 112 VAL VAL B . n B 2 113 ASP 113 113 113 ASP ASP B . n B 2 114 ILE 114 114 114 ILE ILE B . n B 2 115 TYR 115 115 115 TYR TYR B . n B 2 116 TYR 116 116 116 TYR TYR B . n B 2 117 LEU 117 117 117 LEU LEU B . n B 2 118 MET 118 118 118 MET MET B . n B 2 119 ASP 119 119 119 ASP ASP B . n B 2 120 LEU 120 120 120 LEU LEU B . n B 2 121 SER 121 121 121 SER SER B . n B 2 122 TYR 122 122 122 TYR TYR B . n B 2 123 SER 123 123 123 SER SER B . n B 2 124 MET 124 124 124 MET MET B . n B 2 125 LYS 125 125 125 LYS LYS B . n B 2 126 ASP 126 126 126 ASP ASP B . n B 2 127 ASP 127 127 127 ASP ASP B . n B 2 128 LEU 128 128 128 LEU LEU B . n B 2 129 TRP 129 129 129 TRP TRP B . n B 2 130 SER 130 130 130 SER SER B . n B 2 131 ILE 131 131 131 ILE ILE B . n B 2 132 GLN 132 132 132 GLN GLN B . n B 2 133 ASN 133 133 133 ASN ASN B . n B 2 134 LEU 134 134 134 LEU LEU B . n B 2 135 GLY 135 135 135 GLY GLY B . n B 2 136 THR 136 136 136 THR THR B . n B 2 137 LYS 137 137 137 LYS LYS B . n B 2 138 LEU 138 138 138 LEU LEU B . n B 2 139 ALA 139 139 139 ALA ALA B . n B 2 140 THR 140 140 140 THR THR B . n B 2 141 GLN 141 141 141 GLN GLN B . n B 2 142 MET 142 142 142 MET MET B . n B 2 143 ARG 143 143 143 ARG ARG B . n B 2 144 LYS 144 144 144 LYS LYS B . n B 2 145 LEU 145 145 145 LEU LEU B . n B 2 146 THR 146 146 146 THR THR B . n B 2 147 SER 147 147 147 SER SER B . n B 2 148 ASN 148 148 148 ASN ASN B . n B 2 149 LEU 149 149 149 LEU LEU B . n B 2 150 ARG 150 150 150 ARG ARG B . n B 2 151 ILE 151 151 151 ILE ILE B . n B 2 152 GLY 152 152 152 GLY GLY B . n B 2 153 PHE 153 153 153 PHE PHE B . n B 2 154 GLY 154 154 154 GLY GLY B . n B 2 155 ALA 155 155 155 ALA ALA B . n B 2 156 PHE 156 156 156 PHE PHE B . n B 2 157 VAL 157 157 157 VAL VAL B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 LYS 159 159 159 LYS LYS B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 VAL 161 161 161 VAL VAL B . n B 2 162 SER 162 162 162 SER SER B . n B 2 163 PRO 163 163 163 PRO PRO B . n B 2 164 TYR 164 164 164 TYR TYR B . n B 2 165 MET 165 165 165 MET MET B . n B 2 166 TYR 166 166 166 TYR TYR B . n B 2 167 ILE 167 167 167 ILE ILE B . n B 2 168 SER 168 168 168 SER SER B . n B 2 169 PRO 169 169 169 PRO PRO B . n B 2 170 PRO 170 170 170 PRO PRO B . n B 2 171 GLU 171 171 171 GLU GLU B . n B 2 172 ALA 172 172 172 ALA ALA B . n B 2 173 LEU 173 173 173 LEU LEU B . n B 2 174 GLU 174 174 174 GLU GLU B . n B 2 175 ASN 175 175 175 ASN ASN B . n B 2 176 PRO 176 176 176 PRO PRO B . n B 2 177 CYS 177 177 177 CYS CYS B . n B 2 178 TYR 178 178 178 TYR TYR B . n B 2 179 ASP 179 179 179 ASP ASP B . n B 2 180 MET 180 180 180 MET MET B . n B 2 181 LYS 181 181 181 LYS LYS B . n B 2 182 THR 182 182 182 THR THR B . n B 2 183 THR 183 183 183 THR THR B . n B 2 184 CYS 184 184 184 CYS CYS B . n B 2 185 LEU 185 185 185 LEU LEU B . n B 2 186 PRO 186 186 186 PRO PRO B . n B 2 187 MET 187 187 187 MET MET B . n B 2 188 PHE 188 188 188 PHE PHE B . n B 2 189 GLY 189 189 189 GLY GLY B . n B 2 190 TYR 190 190 190 TYR TYR B . n B 2 191 LYS 191 191 191 LYS LYS B . n B 2 192 HIS 192 192 192 HIS HIS B . n B 2 193 VAL 193 193 193 VAL VAL B . n B 2 194 LEU 194 194 194 LEU LEU B . n B 2 195 THR 195 195 195 THR THR B . n B 2 196 LEU 196 196 196 LEU LEU B . n B 2 197 THR 197 197 197 THR THR B . n B 2 198 ASP 198 198 198 ASP ASP B . n B 2 199 GLN 199 199 199 GLN GLN B . n B 2 200 VAL 200 200 200 VAL VAL B . n B 2 201 THR 201 201 201 THR THR B . n B 2 202 ARG 202 202 202 ARG ARG B . n B 2 203 PHE 203 203 203 PHE PHE B . n B 2 204 ASN 204 204 204 ASN ASN B . n B 2 205 GLU 205 205 205 GLU GLU B . n B 2 206 GLU 206 206 206 GLU GLU B . n B 2 207 VAL 207 207 207 VAL VAL B . n B 2 208 LYS 208 208 208 LYS LYS B . n B 2 209 LYS 209 209 209 LYS LYS B . n B 2 210 GLN 210 210 210 GLN GLN B . n B 2 211 SER 211 211 211 SER SER B . n B 2 212 VAL 212 212 212 VAL VAL B . n B 2 213 SER 213 213 213 SER SER B . n B 2 214 ARG 214 214 214 ARG ARG B . n B 2 215 ASN 215 215 215 ASN ASN B . n B 2 216 ARG 216 216 216 ARG ARG B . n B 2 217 ASP 217 217 217 ASP ASP B . n B 2 218 ALA 218 218 218 ALA ALA B . n B 2 219 PRO 219 219 219 PRO PRO B . n B 2 220 GLU 220 220 220 GLU GLU B . n B 2 221 GLY 221 221 221 GLY GLY B . n B 2 222 GLY 222 222 222 GLY GLY B . n B 2 223 PHE 223 223 223 PHE PHE B . n B 2 224 ASP 224 224 224 ASP ASP B . n B 2 225 ALA 225 225 225 ALA ALA B . n B 2 226 ILE 226 226 226 ILE ILE B . n B 2 227 MET 227 227 227 MET MET B . n B 2 228 GLN 228 228 228 GLN GLN B . n B 2 229 ALA 229 229 229 ALA ALA B . n B 2 230 THR 230 230 230 THR THR B . n B 2 231 VAL 231 231 231 VAL VAL B . n B 2 232 CYS 232 232 232 CYS CYS B . n B 2 233 ASP 233 233 233 ASP ASP B . n B 2 234 GLU 234 234 234 GLU GLU B . n B 2 235 LYS 235 235 235 LYS LYS B . n B 2 236 ILE 236 236 236 ILE ILE B . n B 2 237 GLY 237 237 237 GLY GLY B . n B 2 238 TRP 238 238 238 TRP TRP B . n B 2 239 ARG 239 239 239 ARG ARG B . n B 2 240 ASN 240 240 240 ASN ASN B . n B 2 241 ASP 241 241 241 ASP ASP B . n B 2 242 ALA 242 242 242 ALA ALA B . n B 2 243 SER 243 243 243 SER SER B . n B 2 244 HIS 244 244 244 HIS HIS B . n B 2 245 LEU 245 245 245 LEU LEU B . n B 2 246 LEU 246 246 246 LEU LEU B . n B 2 247 VAL 247 247 247 VAL VAL B . n B 2 248 PHE 248 248 248 PHE PHE B . n B 2 249 THR 249 249 249 THR THR B . n B 2 250 THR 250 250 250 THR THR B . n B 2 251 ASP 251 251 251 ASP ASP B . n B 2 252 ALA 252 252 252 ALA ALA B . n B 2 253 LYS 253 253 253 LYS LYS B . n B 2 254 THR 254 254 254 THR THR B . n B 2 255 HIS 255 255 255 HIS HIS B . n B 2 256 ILE 256 256 256 ILE ILE B . n B 2 257 ALA 257 257 257 ALA ALA B . n B 2 258 LEU 258 258 258 LEU LEU B . n B 2 259 ASP 259 259 259 ASP ASP B . n B 2 260 GLY 260 260 260 GLY GLY B . n B 2 261 ARG 261 261 261 ARG ARG B . n B 2 262 LEU 262 262 262 LEU LEU B . n B 2 263 ALA 263 263 263 ALA ALA B . n B 2 264 GLY 264 264 264 GLY GLY B . n B 2 265 ILE 265 265 265 ILE ILE B . n B 2 266 VAL 266 266 266 VAL VAL B . n B 2 267 GLN 267 267 267 GLN GLN B . n B 2 268 PRO 268 268 268 PRO PRO B . n B 2 269 ASN 269 269 269 ASN ASN B . n B 2 270 ASP 270 270 270 ASP ASP B . n B 2 271 GLY 271 271 271 GLY GLY B . n B 2 272 GLN 272 272 272 GLN GLN B . n B 2 273 CYS 273 273 273 CYS CYS B . n B 2 274 HIS 274 274 274 HIS HIS B . n B 2 275 VAL 275 275 275 VAL VAL B . n B 2 276 GLY 276 276 276 GLY GLY B . n B 2 277 SER 277 277 277 SER SER B . n B 2 278 ASP 278 278 278 ASP ASP B . n B 2 279 ASN 279 279 279 ASN ASN B . n B 2 280 HIS 280 280 280 HIS HIS B . n B 2 281 TYR 281 281 281 TYR TYR B . n B 2 282 SER 282 282 282 SER SER B . n B 2 283 ALA 283 283 283 ALA ALA B . n B 2 284 SER 284 284 284 SER SER B . n B 2 285 THR 285 285 285 THR THR B . n B 2 286 THR 286 286 286 THR THR B . n B 2 287 MET 287 287 287 MET MET B . n B 2 288 ASP 288 288 288 ASP ASP B . n B 2 289 TYR 289 289 289 TYR TYR B . n B 2 290 PRO 290 290 290 PRO PRO B . n B 2 291 SER 291 291 291 SER SER B . n B 2 292 LEU 292 292 292 LEU LEU B . n B 2 293 GLY 293 293 293 GLY GLY B . n B 2 294 LEU 294 294 294 LEU LEU B . n B 2 295 MET 295 295 295 MET MET B . n B 2 296 THR 296 296 296 THR THR B . n B 2 297 GLU 297 297 297 GLU GLU B . n B 2 298 LYS 298 298 298 LYS LYS B . n B 2 299 LEU 299 299 299 LEU LEU B . n B 2 300 SER 300 300 300 SER SER B . n B 2 301 GLN 301 301 301 GLN GLN B . n B 2 302 LYS 302 302 302 LYS LYS B . n B 2 303 ASN 303 303 303 ASN ASN B . n B 2 304 ILE 304 304 304 ILE ILE B . n B 2 305 ASN 305 305 305 ASN ASN B . n B 2 306 LEU 306 306 306 LEU LEU B . n B 2 307 ILE 307 307 307 ILE ILE B . n B 2 308 PHE 308 308 308 PHE PHE B . n B 2 309 ALA 309 309 309 ALA ALA B . n B 2 310 VAL 310 310 310 VAL VAL B . n B 2 311 THR 311 311 311 THR THR B . n B 2 312 GLU 312 312 312 GLU GLU B . n B 2 313 ASN 313 313 313 ASN ASN B . n B 2 314 VAL 314 314 314 VAL VAL B . n B 2 315 VAL 315 315 315 VAL VAL B . n B 2 316 ASN 316 316 316 ASN ASN B . n B 2 317 LEU 317 317 317 LEU LEU B . n B 2 318 TYR 318 318 318 TYR TYR B . n B 2 319 GLN 319 319 319 GLN GLN B . n B 2 320 ASN 320 320 320 ASN ASN B . n B 2 321 TYR 321 321 321 TYR TYR B . n B 2 322 SER 322 322 322 SER SER B . n B 2 323 GLU 323 323 323 GLU GLU B . n B 2 324 LEU 324 324 324 LEU LEU B . n B 2 325 ILE 325 325 325 ILE ILE B . n B 2 326 PRO 326 326 326 PRO PRO B . n B 2 327 GLY 327 327 327 GLY GLY B . n B 2 328 THR 328 328 328 THR THR B . n B 2 329 THR 329 329 329 THR THR B . n B 2 330 VAL 330 330 330 VAL VAL B . n B 2 331 GLY 331 331 331 GLY GLY B . n B 2 332 VAL 332 332 332 VAL VAL B . n B 2 333 LEU 333 333 333 LEU LEU B . n B 2 334 SER 334 334 334 SER SER B . n B 2 335 MET 335 335 335 MET MET B . n B 2 336 ASP 336 336 336 ASP ASP B . n B 2 337 SER 337 337 337 SER SER B . n B 2 338 SER 338 338 338 SER SER B . n B 2 339 ASN 339 339 339 ASN ASN B . n B 2 340 VAL 340 340 340 VAL VAL B . n B 2 341 LEU 341 341 341 LEU LEU B . n B 2 342 GLN 342 342 342 GLN GLN B . n B 2 343 LEU 343 343 343 LEU LEU B . n B 2 344 ILE 344 344 344 ILE ILE B . n B 2 345 VAL 345 345 345 VAL VAL B . n B 2 346 ASP 346 346 346 ASP ASP B . n B 2 347 ALA 347 347 347 ALA ALA B . n B 2 348 TYR 348 348 348 TYR TYR B . n B 2 349 GLY 349 349 349 GLY GLY B . n B 2 350 LYS 350 350 350 LYS LYS B . n B 2 351 ILE 351 351 351 ILE ILE B . n B 2 352 ARG 352 352 352 ARG ARG B . n B 2 353 SER 353 353 353 SER SER B . n B 2 354 LYS 354 354 354 LYS LYS B . n B 2 355 VAL 355 355 355 VAL VAL B . n B 2 356 GLU 356 356 356 GLU GLU B . n B 2 357 LEU 357 357 357 LEU LEU B . n B 2 358 GLU 358 358 358 GLU GLU B . n B 2 359 VAL 359 359 359 VAL VAL B . n B 2 360 ARG 360 360 360 ARG ARG B . n B 2 361 ASP 361 361 361 ASP ASP B . n B 2 362 LEU 362 362 362 LEU LEU B . n B 2 363 PRO 363 363 363 PRO PRO B . n B 2 364 GLU 364 364 364 GLU GLU B . n B 2 365 GLU 365 365 365 GLU GLU B . n B 2 366 LEU 366 366 366 LEU LEU B . n B 2 367 SER 367 367 367 SER SER B . n B 2 368 LEU 368 368 368 LEU LEU B . n B 2 369 SER 369 369 369 SER SER B . n B 2 370 PHE 370 370 370 PHE PHE B . n B 2 371 ASN 371 371 371 ASN ASN B . n B 2 372 ALA 372 372 372 ALA ALA B . n B 2 373 THR 373 373 373 THR THR B . n B 2 374 CYS 374 374 374 CYS CYS B . n B 2 375 LEU 375 375 375 LEU LEU B . n B 2 376 ASN 376 376 376 ASN ASN B . n B 2 377 ASN 377 377 377 ASN ASN B . n B 2 378 GLU 378 378 378 GLU GLU B . n B 2 379 VAL 379 379 379 VAL VAL B . n B 2 380 ILE 380 380 380 ILE ILE B . n B 2 381 PRO 381 381 381 PRO PRO B . n B 2 382 GLY 382 382 382 GLY GLY B . n B 2 383 LEU 383 383 383 LEU LEU B . n B 2 384 LYS 384 384 384 LYS LYS B . n B 2 385 SER 385 385 385 SER SER B . n B 2 386 CYS 386 386 386 CYS CYS B . n B 2 387 MET 387 387 387 MET MET B . n B 2 388 GLY 388 388 388 GLY GLY B . n B 2 389 LEU 389 389 389 LEU LEU B . n B 2 390 LYS 390 390 390 LYS LYS B . n B 2 391 ILE 391 391 391 ILE ILE B . n B 2 392 GLY 392 392 392 GLY GLY B . n B 2 393 ASP 393 393 393 ASP ASP B . n B 2 394 THR 394 394 394 THR THR B . n B 2 395 VAL 395 395 395 VAL VAL B . n B 2 396 SER 396 396 396 SER SER B . n B 2 397 PHE 397 397 397 PHE PHE B . n B 2 398 SER 398 398 398 SER SER B . n B 2 399 ILE 399 399 399 ILE ILE B . n B 2 400 GLU 400 400 400 GLU GLU B . n B 2 401 ALA 401 401 401 ALA ALA B . n B 2 402 LYS 402 402 402 LYS LYS B . n B 2 403 VAL 403 403 403 VAL VAL B . n B 2 404 ARG 404 404 404 ARG ARG B . n B 2 405 GLY 405 405 405 GLY GLY B . n B 2 406 CYS 406 406 406 CYS CYS B . n B 2 407 PRO 407 407 407 PRO PRO B . n B 2 408 GLN 408 408 408 GLN GLN B . n B 2 409 GLU 409 409 409 GLU GLU B . n B 2 410 LYS 410 410 410 LYS LYS B . n B 2 411 GLU 411 411 411 GLU GLU B . n B 2 412 LYS 412 412 412 LYS LYS B . n B 2 413 SER 413 413 413 SER SER B . n B 2 414 PHE 414 414 414 PHE PHE B . n B 2 415 THR 415 415 415 THR THR B . n B 2 416 ILE 416 416 416 ILE ILE B . n B 2 417 LYS 417 417 417 LYS LYS B . n B 2 418 PRO 418 418 418 PRO PRO B . n B 2 419 VAL 419 419 419 VAL VAL B . n B 2 420 GLY 420 420 420 GLY GLY B . n B 2 421 PHE 421 421 421 PHE PHE B . n B 2 422 LYS 422 422 422 LYS LYS B . n B 2 423 ASP 423 423 423 ASP ASP B . n B 2 424 SER 424 424 424 SER SER B . n B 2 425 LEU 425 425 425 LEU LEU B . n B 2 426 ILE 426 426 426 ILE ILE B . n B 2 427 VAL 427 427 427 VAL VAL B . n B 2 428 GLN 428 428 428 GLN GLN B . n B 2 429 VAL 429 429 429 VAL VAL B . n B 2 430 THR 430 430 430 THR THR B . n B 2 431 PHE 431 431 431 PHE PHE B . n B 2 432 ASP 432 432 432 ASP ASP B . n B 2 433 CYS 433 433 433 CYS CYS B . n B 2 434 ASP 434 434 434 ASP ASP B . n B 2 435 CYS 435 435 435 CYS CYS B . n B 2 436 ALA 436 436 436 ALA ALA B . n B 2 437 CYS 437 437 437 CYS CYS B . n B 2 438 GLN 438 438 438 GLN GLN B . n B 2 439 ALA 439 439 439 ALA ALA B . n B 2 440 GLN 440 440 440 GLN GLN B . n B 2 441 ALA 441 441 441 ALA ALA B . n B 2 442 GLU 442 442 442 GLU GLU B . n B 2 443 PRO 443 443 443 PRO PRO B . n B 2 444 ASN 444 444 444 ASN ASN B . n B 2 445 SER 445 445 445 SER SER B . n B 2 446 HIS 446 446 446 HIS HIS B . n B 2 447 ARG 447 447 447 ARG ARG B . n B 2 448 CYS 448 448 448 CYS CYS B . n B 2 449 ASN 449 449 449 ASN ASN B . n B 2 450 ASN 450 450 450 ASN ASN B . n B 2 451 GLY 451 451 451 GLY GLY B . n B 2 452 ASN 452 452 452 ASN ASN B . n B 2 453 GLY 453 453 453 GLY GLY B . n B 2 454 THR 454 454 454 THR THR B . n B 2 455 PHE 455 455 455 PHE PHE B . n B 2 456 GLU 456 456 456 GLU GLU B . n B 2 457 CYS 457 457 457 CYS CYS B . n B 2 458 GLY 458 458 458 GLY GLY B . n B 2 459 VAL 459 459 459 VAL VAL B . n B 2 460 CYS 460 460 460 CYS CYS B . n B 2 461 ARG 461 461 461 ARG ARG B . n B 2 462 CYS 462 462 462 CYS CYS B . n B 2 463 GLY 463 463 463 GLY GLY B . n B 2 464 PRO 464 464 464 PRO PRO B . n B 2 465 GLY 465 465 465 GLY GLY B . n B 2 466 TRP 466 466 466 TRP TRP B . n B 2 467 LEU 467 467 467 LEU LEU B . n B 2 468 GLY 468 468 468 GLY GLY B . n B 2 469 SER 469 469 469 SER SER B . n B 2 470 GLN 470 470 470 GLN GLN B . n B 2 471 CYS 471 471 471 CYS CYS B . n B 2 472 GLU 472 472 472 GLU GLU B . n B 2 473 CYS 473 473 473 CYS CYS B . n B 2 474 SER 474 474 474 SER SER B . n B 2 475 GLU 475 475 475 GLU GLU B . n B 2 476 GLU 476 476 476 GLU GLU B . n B 2 477 ASP 477 477 477 ASP ASP B . n B 2 478 TYR 478 478 478 TYR TYR B . n B 2 479 ARG 479 479 479 ARG ARG B . n B 2 480 PRO 480 480 480 PRO PRO B . n B 2 481 SER 481 481 481 SER SER B . n B 2 482 GLN 482 482 482 GLN GLN B . n B 2 483 GLN 483 483 483 GLN GLN B . n B 2 484 ASP 484 484 484 ASP ASP B . n B 2 485 GLU 485 485 485 GLU GLU B . n B 2 486 CYS 486 486 486 CYS CYS B . n B 2 487 SER 487 487 487 SER SER B . n B 2 488 PRO 488 488 488 PRO PRO B . n B 2 489 ARG 489 489 489 ARG ARG B . n B 2 490 GLU 490 490 490 GLU GLU B . n B 2 491 GLY 491 491 491 GLY GLY B . n B 2 492 GLN 492 492 492 GLN GLN B . n B 2 493 PRO 493 493 493 PRO PRO B . n B 2 494 VAL 494 494 494 VAL VAL B . n B 2 495 CYS 495 495 495 CYS CYS B . n B 2 496 SER 496 496 496 SER SER B . n B 2 497 GLN 497 497 497 GLN GLN B . n B 2 498 ARG 498 498 498 ARG ARG B . n B 2 499 GLY 499 499 499 GLY GLY B . n B 2 500 GLU 500 500 500 GLU GLU B . n B 2 501 CYS 501 501 501 CYS CYS B . n B 2 502 LEU 502 502 502 LEU LEU B . n B 2 503 CYS 503 503 503 CYS CYS B . n B 2 504 GLY 504 504 504 GLY GLY B . n B 2 505 GLN 505 505 505 GLN GLN B . n B 2 506 CYS 506 506 506 CYS CYS B . n B 2 507 VAL 507 507 507 VAL VAL B . n B 2 508 CYS 508 508 508 CYS CYS B . n B 2 509 HIS 509 509 509 HIS HIS B . n B 2 510 SER 510 510 510 SER SER B . n B 2 511 SER 511 511 511 SER SER B . n B 2 512 ASP 512 512 512 ASP ASP B . n B 2 513 PHE 513 513 513 PHE PHE B . n B 2 514 GLY 514 514 514 GLY GLY B . n B 2 515 LYS 515 515 515 LYS LYS B . n B 2 516 ILE 516 516 516 ILE ILE B . n B 2 517 THR 517 517 517 THR THR B . n B 2 518 GLY 518 518 518 GLY GLY B . n B 2 519 LYS 519 519 519 LYS LYS B . n B 2 520 TYR 520 520 520 TYR TYR B . n B 2 521 CYS 521 521 521 CYS CYS B . n B 2 522 GLU 522 522 522 GLU GLU B . n B 2 523 CYS 523 523 523 CYS CYS B . n B 2 524 ASP 524 524 524 ASP ASP B . n B 2 525 ASP 525 525 525 ASP ASP B . n B 2 526 PHE 526 526 526 PHE PHE B . n B 2 527 SER 527 527 527 SER SER B . n B 2 528 CYS 528 528 528 CYS CYS B . n B 2 529 VAL 529 529 529 VAL VAL B . n B 2 530 ARG 530 530 530 ARG ARG B . n B 2 531 TYR 531 531 531 TYR TYR B . n B 2 532 LYS 532 532 532 LYS LYS B . n B 2 533 GLY 533 533 533 GLY GLY B . n B 2 534 GLU 534 534 534 GLU GLU B . n B 2 535 MET 535 535 535 MET MET B . n B 2 536 CYS 536 536 536 CYS CYS B . n B 2 537 SER 537 537 537 SER SER B . n B 2 538 GLY 538 538 538 GLY GLY B . n B 2 539 HIS 539 539 539 HIS HIS B . n B 2 540 GLY 540 540 540 GLY GLY B . n B 2 541 GLN 541 541 541 GLN GLN B . n B 2 542 CYS 542 542 542 CYS CYS B . n B 2 543 SER 543 543 543 SER SER B . n B 2 544 CYS 544 544 544 CYS CYS B . n B 2 545 GLY 545 545 545 GLY GLY B . n B 2 546 ASP 546 546 546 ASP ASP B . n B 2 547 CYS 547 547 547 CYS CYS B . n B 2 548 LEU 548 548 548 LEU LEU B . n B 2 549 CYS 549 549 549 CYS CYS B . n B 2 550 ASP 550 550 550 ASP ASP B . n B 2 551 SER 551 551 551 SER SER B . n B 2 552 ASP 552 552 552 ASP ASP B . n B 2 553 TRP 553 553 553 TRP TRP B . n B 2 554 THR 554 554 554 THR THR B . n B 2 555 GLY 555 555 555 GLY GLY B . n B 2 556 TYR 556 556 556 TYR TYR B . n B 2 557 TYR 557 557 557 TYR TYR B . n B 2 558 CYS 558 558 558 CYS CYS B . n B 2 559 ASN 559 559 559 ASN ASN B . n B 2 560 CYS 560 560 560 CYS CYS B . n B 2 561 THR 561 561 561 THR THR B . n B 2 562 THR 562 562 562 THR THR B . n B 2 563 ARG 563 563 563 ARG ARG B . n B 2 564 THR 564 564 564 THR THR B . n B 2 565 ASP 565 565 565 ASP ASP B . n B 2 566 THR 566 566 566 THR THR B . n B 2 567 CYS 567 567 567 CYS CYS B . n B 2 568 MET 568 568 568 MET MET B . n B 2 569 SER 569 569 569 SER SER B . n B 2 570 SER 570 570 570 SER SER B . n B 2 571 ASN 571 571 571 ASN ASN B . n B 2 572 GLY 572 572 572 GLY GLY B . n B 2 573 LEU 573 573 573 LEU LEU B . n B 2 574 LEU 574 574 574 LEU LEU B . n B 2 575 CYS 575 575 575 CYS CYS B . n B 2 576 SER 576 576 576 SER SER B . n B 2 577 GLY 577 577 577 GLY GLY B . n B 2 578 ARG 578 578 578 ARG ARG B . n B 2 579 GLY 579 579 579 GLY GLY B . n B 2 580 LYS 580 580 580 LYS LYS B . n B 2 581 CYS 581 581 581 CYS CYS B . n B 2 582 GLU 582 582 582 GLU GLU B . n B 2 583 CYS 583 583 583 CYS CYS B . n B 2 584 GLY 584 584 584 GLY GLY B . n B 2 585 SER 585 585 585 SER SER B . n B 2 586 CYS 586 586 586 CYS CYS B . n B 2 587 VAL 587 587 587 VAL VAL B . n B 2 588 CYS 588 588 588 CYS CYS B . n B 2 589 ILE 589 589 589 ILE ILE B . n B 2 590 GLN 590 590 590 GLN GLN B . n B 2 591 PRO 591 591 591 PRO PRO B . n B 2 592 GLY 592 592 592 GLY GLY B . n B 2 593 SER 593 593 593 SER SER B . n B 2 594 TYR 594 594 594 TYR TYR B . n B 2 595 GLY 595 595 595 GLY GLY B . n B 2 596 ASP 596 596 596 ASP ASP B . n B 2 597 THR 597 597 597 THR THR B . n B 2 598 CYS 598 598 598 CYS CYS B . n B 2 599 GLU 599 599 599 GLU GLU B . n B 2 600 LYS 600 600 600 LYS LYS B . n B 2 601 CYS 601 601 601 CYS CYS B . n B 2 602 PRO 602 602 602 PRO PRO B . n B 2 603 THR 603 603 603 THR THR B . n B 2 604 CYS 604 604 604 CYS CYS B . n B 2 605 PRO 605 605 605 PRO PRO B . n B 2 606 ASP 606 606 606 ASP ASP B . n B 2 607 ALA 607 607 607 ALA ALA B . n B 2 608 CYS 608 608 608 CYS CYS B . n B 2 609 THR 609 609 609 THR THR B . n B 2 610 PHE 610 610 610 PHE PHE B . n B 2 611 LYS 611 611 611 LYS LYS B . n B 2 612 LYS 612 612 612 LYS LYS B . n B 2 613 GLU 613 613 613 GLU GLU B . n B 2 614 CYS 614 614 614 CYS CYS B . n B 2 615 VAL 615 615 615 VAL VAL B . n B 2 616 GLU 616 616 616 GLU GLU B . n B 2 617 CYS 617 617 617 CYS CYS B . n B 2 618 LYS 618 618 618 LYS LYS B . n B 2 619 LYS 619 619 619 LYS LYS B . n B 2 620 PHE 620 620 620 PHE PHE B . n B 2 621 ASP 621 621 621 ASP ASP B . n B 2 622 ARG 622 622 622 ARG ARG B . n B 2 623 GLY 623 623 623 GLY GLY B . n B 2 624 ALA 624 624 624 ALA ALA B . n B 2 625 LEU 625 625 625 LEU LEU B . n B 2 626 HIS 626 626 626 HIS HIS B . n B 2 627 ASP 627 627 627 ASP ASP B . n B 2 628 GLU 628 628 628 GLU GLU B . n B 2 629 ASN 629 629 629 ASN ASN B . n B 2 630 THR 630 630 630 THR THR B . n B 2 631 CYS 631 631 631 CYS CYS B . n B 2 632 ASN 632 632 632 ASN ASN B . n B 2 633 ARG 633 633 633 ARG ARG B . n B 2 634 TYR 634 634 634 TYR TYR B . n B 2 635 CYS 635 635 635 CYS CYS B . n B 2 636 ARG 636 636 636 ARG ARG B . n B 2 637 ASP 637 637 637 ASP ASP B . n B 2 638 GLU 638 638 638 GLU GLU B . n B 2 639 ILE 639 639 639 ILE ILE B . n B 2 640 GLU 640 640 640 GLU GLU B . n B 2 641 SER 641 641 641 SER SER B . n B 2 642 VAL 642 642 642 VAL VAL B . n B 2 643 LYS 643 643 643 LYS LYS B . n B 2 644 GLU 644 644 644 GLU GLU B . n B 2 645 LEU 645 645 645 LEU LEU B . n B 2 646 LYS 646 646 646 LYS LYS B . n B 2 647 ASP 647 647 647 ASP ASP B . n B 2 648 THR 648 648 648 THR THR B . n B 2 649 GLY 649 649 649 GLY GLY B . n B 2 650 LYS 650 650 650 LYS LYS B . n B 2 651 ASP 651 651 651 ASP ASP B . n B 2 652 ALA 652 652 652 ALA ALA B . n B 2 653 VAL 653 653 653 VAL VAL B . n B 2 654 ASN 654 654 654 ASN ASN B . n B 2 655 CYS 655 655 655 CYS CYS B . n B 2 656 THR 656 656 656 THR THR B . n B 2 657 TYR 657 657 657 TYR TYR B . n B 2 658 LYS 658 658 658 LYS LYS B . n B 2 659 ASN 659 659 659 ASN ASN B . n B 2 660 GLU 660 660 660 GLU GLU B . n B 2 661 ASP 661 661 661 ASP ASP B . n B 2 662 ASP 662 662 662 ASP ASP B . n B 2 663 CYS 663 663 663 CYS CYS B . n B 2 664 VAL 664 664 664 VAL VAL B . n B 2 665 VAL 665 665 665 VAL VAL B . n B 2 666 ARG 666 666 666 ARG ARG B . n B 2 667 PHE 667 667 667 PHE PHE B . n B 2 668 GLN 668 668 668 GLN GLN B . n B 2 669 TYR 669 669 669 TYR TYR B . n B 2 670 TYR 670 670 670 TYR TYR B . n B 2 671 GLU 671 671 671 GLU GLU B . n B 2 672 ASP 672 672 672 ASP ASP B . n B 2 673 SER 673 673 673 SER SER B . n B 2 674 SER 674 674 674 SER SER B . n B 2 675 GLY 675 675 675 GLY GLY B . n B 2 676 LYS 676 676 676 LYS LYS B . n B 2 677 SER 677 677 677 SER SER B . n B 2 678 ILE 678 678 678 ILE ILE B . n B 2 679 LEU 679 679 679 LEU LEU B . n B 2 680 TYR 680 680 680 TYR TYR B . n B 2 681 VAL 681 681 681 VAL VAL B . n B 2 682 VAL 682 682 682 VAL VAL B . n B 2 683 GLU 683 683 683 GLU GLU B . n B 2 684 GLU 684 684 684 GLU GLU B . n B 2 685 PRO 685 685 685 PRO PRO B . n B 2 686 GLU 686 686 686 GLU GLU B . n B 2 687 CYS 687 687 687 CYS CYS B . n B 2 688 PRO 688 688 688 PRO PRO B . n B 2 689 LYS 689 689 689 LYS LYS B . n B 2 690 GLY 690 690 690 GLY GLY B . n B 2 691 PRO 691 691 ? ? ? B . n B 2 692 ASP 692 692 ? ? ? B . n C 3 1 SER 1 1417 ? ? ? C . n C 3 2 ASP 2 1418 ? ? ? C . n C 3 3 VAL 3 1419 ? ? ? C . n C 3 4 PRO 4 1420 ? ? ? C . n C 3 5 ARG 5 1421 ? ? ? C . n C 3 6 ASP 6 1422 ? ? ? C . n C 3 7 LEU 7 1423 ? ? ? C . n C 3 8 GLU 8 1424 ? ? ? C . n C 3 9 VAL 9 1425 ? ? ? C . n C 3 10 VAL 10 1426 ? ? ? C . n C 3 11 ALA 11 1427 ? ? ? C . n C 3 12 ALA 12 1428 ? ? ? C . n C 3 13 THR 13 1429 ? ? ? C . n C 3 14 PRO 14 1430 ? ? ? C . n C 3 15 THR 15 1431 ? ? ? C . n C 3 16 SER 16 1432 ? ? ? C . n C 3 17 LEU 17 1433 ? ? ? C . n C 3 18 LEU 18 1434 ? ? ? C . n C 3 19 ILE 19 1435 ? ? ? C . n C 3 20 SER 20 1436 ? ? ? C . n C 3 21 TRP 21 1437 ? ? ? C . n C 3 22 ASP 22 1438 ? ? ? C . n C 3 23 ALA 23 1439 ? ? ? C . n C 3 24 PRO 24 1440 ? ? ? C . n C 3 25 ALA 25 1441 ? ? ? C . n C 3 26 VAL 26 1442 ? ? ? C . n C 3 27 THR 27 1443 ? ? ? C . n C 3 28 VAL 28 1444 ? ? ? C . n C 3 29 ARG 29 1445 ? ? ? C . n C 3 30 TYR 30 1446 ? ? ? C . n C 3 31 TYR 31 1447 ? ? ? C . n C 3 32 ARG 32 1448 ? ? ? C . n C 3 33 ILE 33 1449 ? ? ? C . n C 3 34 THR 34 1450 ? ? ? C . n C 3 35 TYR 35 1451 ? ? ? C . n C 3 36 GLY 36 1452 ? ? ? C . n C 3 37 GLU 37 1453 ? ? ? C . n C 3 38 THR 38 1454 ? ? ? C . n C 3 39 GLY 39 1455 ? ? ? C . n C 3 40 GLY 40 1456 ? ? ? C . n C 3 41 ASN 41 1457 ? ? ? C . n C 3 42 SER 42 1458 ? ? ? C . n C 3 43 PRO 43 1459 ? ? ? C . n C 3 44 VAL 44 1460 ? ? ? C . n C 3 45 GLN 45 1461 ? ? ? C . n C 3 46 GLU 46 1462 ? ? ? C . n C 3 47 PHE 47 1463 ? ? ? C . n C 3 48 THR 48 1464 ? ? ? C . n C 3 49 VAL 49 1465 ? ? ? C . n C 3 50 PRO 50 1466 ? ? ? C . n C 3 51 GLY 51 1467 ? ? ? C . n C 3 52 SER 52 1468 ? ? ? C . n C 3 53 LYS 53 1469 ? ? ? C . n C 3 54 SER 54 1470 ? ? ? C . n C 3 55 THR 55 1471 ? ? ? C . n C 3 56 ALA 56 1472 ? ? ? C . n C 3 57 THR 57 1473 ? ? ? C . n C 3 58 ILE 58 1474 ? ? ? C . n C 3 59 SER 59 1475 ? ? ? C . n C 3 60 GLY 60 1476 ? ? ? C . n C 3 61 LEU 61 1477 ? ? ? C . n C 3 62 LYS 62 1478 ? ? ? C . n C 3 63 PRO 63 1479 ? ? ? C . n C 3 64 GLY 64 1480 ? ? ? C . n C 3 65 VAL 65 1481 ? ? ? C . n C 3 66 ASP 66 1482 ? ? ? C . n C 3 67 TYR 67 1483 ? ? ? C . n C 3 68 THR 68 1484 ? ? ? C . n C 3 69 ILE 69 1485 ? ? ? C . n C 3 70 THR 70 1486 ? ? ? C . n C 3 71 VAL 71 1487 ? ? ? C . n C 3 72 TYR 72 1488 ? ? ? C . n C 3 73 ALA 73 1489 ? ? ? C . n C 3 74 VAL 74 1490 1490 VAL VAL C . n C 3 75 ILE 75 1491 1491 ILE ILE C . n C 3 76 ALA 76 1492 1492 ALA ALA C . n C 3 77 ARG 77 1493 1493 ARG ARG C . n C 3 78 GLY 78 1494 1494 GLY GLY C . n C 3 79 ASP 79 1495 1495 ASP ASP C . n C 3 80 TRP 80 1496 1496 TRP TRP C . n C 3 81 ASN 81 1497 1497 ASN ASN C . n C 3 82 ASP 82 1498 ? ? ? C . n C 3 83 GLY 83 1499 ? ? ? C . n C 3 84 SER 84 1500 ? ? ? C . n C 3 85 LYS 85 1501 ? ? ? C . n C 3 86 PRO 86 1502 ? ? ? C . n C 3 87 ILE 87 1503 ? ? ? C . n C 3 88 SER 88 1504 ? ? ? C . n C 3 89 ILE 89 1505 ? ? ? C . n C 3 90 ASN 90 1506 ? ? ? C . n C 3 91 TYR 91 1507 ? ? ? C . n C 3 92 ARG 92 1508 ? ? ? C . n C 3 93 THR 93 1509 ? ? ? C . n C 3 94 GLY 94 1510 ? ? ? C . n C 3 95 LYS 95 1511 ? ? ? C . n C 3 96 LYS 96 1512 ? ? ? C . n C 3 97 GLY 97 1513 ? ? ? C . n C 3 98 LYS 98 1514 ? ? ? C . 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 D 4 NAG 1 1001 1001 NAG NAG A . E 4 NAG 2 1002 1002 NAG NAG A . F 5 BMA 3 1003 1003 BMA BMA A . G 6 MAN 4 1004 1004 MAN MAN A . H 4 NAG 1 1005 1005 NAG NAG A . I 4 NAG 2 1006 1006 NAG NAG A . J 4 NAG 1 1007 1007 NAG NAG A . K 4 NAG 2 1008 1008 NAG NAG A . L 5 BMA 3 1009 1009 BMA BMA A . M 6 MAN 4 1010 1010 MAN MAN A . N 5 BMA 5 1011 1011 BMA BMA A . O 6 MAN 6 1012 1012 MAN MAN A . P 4 NAG 1 1013 1013 NAG NAG A . Q 4 NAG 2 1014 1014 NAG NAG A . R 5 BMA 3 1015 1015 BMA BMA A . S 6 MAN 4 1016 1016 MAN MAN A . T 4 NAG 1 1017 1017 NAG NAG A . U 4 NAG 1 1018 1018 NAG NAG A . V 4 NAG 2 1019 1019 NAG NAG A . W 4 NAG 1 1020 1020 NAG NAG A . X 4 NAG 1 1021 1021 NAG NAG A . Y 4 NAG 1 1022 1022 NAG NAG A . Z 4 NAG 2 1023 1023 NAG NAG A . AA 4 NAG 1 1024 1024 NAG NAG A . BA 4 NAG 2 1025 1025 NAG NAG A . CA 5 BMA 3 1026 1026 BMA BMA A . DA 7 MN 1 1027 1027 MN MN A . EA 7 MN 1 1028 1028 MN MN A . FA 7 MN 1 1029 1029 MN MN A . GA 7 MN 1 1030 1030 MN MN A . HA 7 MN 1 1031 1031 MN MN A . IA 4 NAG 1 701 701 NAG NAG B . JA 4 NAG 1 702 702 NAG NAG B . KA 4 NAG 1 703 703 NAG NAG B . LA 4 NAG 2 704 704 NAG NAG B . MA 4 NAG 1 705 705 NAG NAG B . NA 4 NAG 2 706 706 NAG NAG B . OA 5 BMA 3 707 707 BMA BMA B . PA 7 MN 1 708 708 MN MN B . QA 7 MN 1 709 709 MN MN B . RA 7 MN 1 710 710 MN MN B . SA 8 HOH 1 1101 1101 HOH HOH A . SA 8 HOH 2 1102 1102 HOH HOH A . SA 8 HOH 3 1103 1103 HOH HOH A . TA 8 HOH 1 801 801 HOH HOH B . TA 8 HOH 2 802 802 HOH HOH 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 821 A ASN 821 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 524 A ASN 524 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 458 A ASN 458 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 559 B ASN 559 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 44 A ASN 44 ? ASN 'GLYCOSYLATION SITE' 6 B ASN 99 B ASN 99 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 585 A ASN 585 ? ASN 'GLYCOSYLATION SITE' 8 B ASN 320 B ASN 320 ? ASN 'GLYCOSYLATION SITE' 9 A ASN 266 A ASN 266 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 950 A ASN 950 ? ASN 'GLYCOSYLATION SITE' 11 A ASN 943 A ASN 943 ? ASN 'GLYCOSYLATION SITE' 12 B ASN 371 B ASN 371 ? ASN 'GLYCOSYLATION SITE' 13 A ASN 674 A ASN 674 ? ASN 'GLYCOSYLATION SITE' 14 A ASN 260 A ASN 260 ? 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 trimeric _pdbx_struct_assembly.oligomeric_count 3 # _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,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA # 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)' 15920 ? 1 MORE 52 ? 1 'SSA (A^2)' 75180 ? # _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 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 115.3 ? 2 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 147.5 ? 3 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 96.6 ? 4 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 132.7 ? 5 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 72.3 ? 6 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 61.0 ? 7 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 68.7 ? 8 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 93.3 ? 9 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 117.6 ? 10 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 O ? B SER 123 ? B SER 123 ? 1_555 64.2 ? 11 OD1 ? B ASP 251 ? B ASP 251 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 62.0 ? 12 OD1 ? B ASP 127 ? B ASP 127 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 64.9 ? 13 OD2 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 134.5 ? 14 OD1 ? B ASP 126 ? B ASP 126 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 135.3 ? 15 O ? B SER 123 ? B SER 123 ? 1_555 MN ? QA MN . ? B MN 709 ? 1_555 OD2 ? B ASP 251 ? B ASP 251 ? 1_555 105.3 ? 16 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 75.6 ? 17 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 96.7 ? 18 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 144.4 ? 19 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 90.4 ? 20 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 64.8 ? 21 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 150.8 ? 22 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 100.5 ? 23 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 86.3 ? 24 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 60.6 ? 25 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 145.6 ? 26 O ? A TYR 290 ? A TYR 290 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 148.5 ? 27 OD2 ? A ASP 284 ? A ASP 284 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 74.4 ? 28 OD2 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 113.4 ? 29 OD1 ? A ASP 288 ? A ASP 288 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 68.2 ? 30 OD1 ? A ASP 292 ? A ASP 292 ? 1_555 MN ? EA MN . ? A MN 1028 ? 1_555 OD1 ? A ASN 286 ? A ASN 286 ? 1_555 87.0 ? 31 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 69.3 ? 32 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 90.2 ? 33 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 82.7 ? 34 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 121.1 ? 35 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 140.2 ? 36 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 60.4 ? 37 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 82.1 ? 38 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 70.6 ? 39 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 153.2 ? 40 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 144.2 ? 41 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 132.0 ? 42 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 63.6 ? 43 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 75.7 ? 44 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 91.5 ? 45 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 90.5 ? 46 O ? A TYR 419 ? A TYR 419 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 155.5 ? 47 OD1 ? A ASP 413 ? A ASP 413 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 107.9 ? 48 OD2 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 113.9 ? 49 OD1 ? A ASP 421 ? A ASP 421 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 77.4 ? 50 OD1 ? A ASN 417 ? A ASN 417 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 74.3 ? 51 OD1 ? A ASP 415 ? A ASP 415 ? 1_555 MN ? GA MN . ? A MN 1030 ? 1_555 OD2 ? A ASP 415 ? A ASP 415 ? 1_555 55.9 ? 52 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 145.5 ? 53 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 65.2 ? 54 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 149.0 ? 55 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 89.6 ? 56 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 60.7 ? 57 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 137.6 ? 58 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 68.4 ? 59 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 112.4 ? 60 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 68.4 ? 61 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 70.8 ? 62 OD2 ? A ASP 230 ? A ASP 230 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 77.9 ? 63 OD1 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 97.3 ? 64 OD1 ? A ASP 234 ? A ASP 234 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 94.7 ? 65 OD2 ? A ASP 238 ? A ASP 238 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 113.5 ? 66 OD1 ? A ASN 232 ? A ASN 232 ? 1_555 MN ? DA MN . ? A MN 1027 ? 1_555 O ? A ILE 236 ? A ILE 236 ? 1_555 146.1 ? 67 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 146.7 ? 68 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 72.8 ? 69 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B ASP 217 ? B ASP 217 ? 1_555 84.4 ? 70 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 95.4 ? 71 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 107.9 ? 72 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 167.7 ? 73 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 82.2 ? 74 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 70.3 ? 75 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 81.1 ? 76 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 101.2 ? 77 OD1 ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 102.8 ? 78 OE2 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 103.9 ? 79 O ? B ASP 217 ? B ASP 217 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 97.2 ? 80 OD2 ? B ASP 158 ? B ASP 158 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 81.7 ? 81 OD1 ? B ASN 215 ? B ASN 215 ? 1_555 MN ? RA MN . ? B MN 710 ? 1_555 O ? B PRO 219 ? B PRO 219 ? 1_555 174.0 ? 82 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 123 ? B SER 123 ? 1_555 145.0 ? 83 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 106.8 ? 84 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 OG ? B SER 121 ? B SER 121 ? 1_555 97.9 ? 85 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 802 ? 1_555 89.7 ? 86 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 802 ? 1_555 64.6 ? 87 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 802 ? 1_555 92.1 ? 88 OE1 ? B GLU 220 ? B GLU 220 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 801 ? 1_555 76.2 ? 89 OG ? B SER 123 ? B SER 123 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 801 ? 1_555 74.7 ? 90 OG ? B SER 121 ? B SER 121 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 801 ? 1_555 167.7 ? 91 O ? TA HOH . ? B HOH 802 ? 1_555 MN ? PA MN . ? B MN 708 ? 1_555 O ? TA HOH . ? B HOH 801 ? 1_555 75.9 ? 92 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 151.4 ? 93 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 128.7 ? 94 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 61.2 ? 95 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 61.2 ? 96 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 129.5 ? 97 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 145.0 ? 98 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 100.3 ? 99 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 66.8 ? 100 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 127.6 ? 101 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A CYS 596 ? A CYS 596 ? 1_555 70.4 ? 102 OE2 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 80.9 ? 103 OD1 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 71.2 ? 104 OD2 ? A ASP 599 ? A ASP 599 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 93.9 ? 105 OE1 ? A GLU 636 ? A GLU 636 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 120.9 ? 106 O ? A CYS 596 ? A CYS 596 ? 1_555 MN ? HA MN . ? A MN 1031 ? 1_555 O ? A VAL 601 ? A VAL 601 ? 1_555 74.5 ? 107 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 61.0 ? 108 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 100.2 ? 109 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 136.4 ? 110 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 79.0 ? 111 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 94.4 ? 112 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 121.9 ? 113 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 133.8 ? 114 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 160.0 ? 115 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 60.8 ? 116 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 78.3 ? 117 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 137.3 ? 118 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 77.3 ? 119 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 117.1 ? 120 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 96.7 ? 121 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 85.1 ? 122 OD2 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 99.7 ? 123 OD1 ? A ASP 353 ? A ASP 353 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 64.7 ? 124 OD1 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 82.5 ? 125 OD2 ? A ASP 351 ? A ASP 351 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 155.5 ? 126 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 116.9 ? 127 OD1 ? A ASP 349 ? A ASP 349 ? 1_555 MN ? FA MN . ? A MN 1029 ? 1_555 O ? A PHE 355 ? A PHE 355 ? 1_555 67.5 ? # 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 2014-03-26 2 'Structure model' 1 1 2014-04-09 3 'Structure model' 1 2 2014-04-30 4 'Structure model' 1 3 2017-11-15 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # 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' 'Database references' 2 3 'Structure model' 'Database references' 3 4 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # 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 3.4461 54.0378 21.0785 0.8556 0.4284 0.6111 -0.2561 -0.0618 0.0553 5.1006 2.1819 2.0999 0.7562 0.8758 -0.6107 -0.4137 0.3676 0.3743 -0.4862 0.3263 0.2311 -0.2305 0.0354 0.0694 'X-RAY DIFFRACTION' 2 ? refined -41.4919 47.0121 -0.5515 1.2144 0.8907 1.0916 -0.2904 -0.3816 0.2270 4.0147 0.3841 0.3307 0.1507 0.8565 -0.0572 -0.4184 1.2202 0.7077 -0.4571 0.3235 0.3711 -0.2641 0.0738 0.0928 'X-RAY DIFFRACTION' 3 ? refined -50.1378 43.0450 22.8554 1.0342 0.9815 0.9535 -0.1020 -0.1911 0.2071 3.8081 2.9092 2.1086 -1.4457 1.8088 0.4630 -0.4217 0.1941 -0.0316 -0.1480 0.3559 0.6634 -0.1369 1.0327 0.1278 'X-RAY DIFFRACTION' 4 ? refined -25.4010 36.2757 73.2419 0.9144 0.5255 0.7861 0.2798 0.0084 -0.0050 5.0923 3.7039 6.1554 -0.5549 1.3561 -0.6591 -0.2209 -0.5872 -0.2364 0.6500 0.0797 -0.1693 0.1068 0.1869 0.1319 'X-RAY DIFFRACTION' 5 ? refined -41.0860 4.4011 7.4339 1.6242 1.2968 1.4471 -0.1405 -0.4571 0.1298 9.7703 6.7475 5.0062 7.5125 6.5614 5.8039 -0.0883 0.3319 -0.6041 -1.2881 -0.0319 0.5210 0.1529 -1.3848 0.1176 'X-RAY DIFFRACTION' 6 ? refined 4.4249 13.0033 34.4407 1.1617 0.5429 1.0336 -0.0817 -0.0436 0.1608 3.3677 5.5251 0.9965 2.9972 -0.2154 -0.4963 0.4520 -0.5558 -1.5020 0.6903 -0.4534 -1.3764 0.6007 0.0194 -0.0229 'X-RAY DIFFRACTION' 7 ? refined 17.7740 27.5064 31.4178 0.6986 0.5756 1.2418 -0.0749 -0.0180 0.1148 2.2078 8.7177 5.1829 1.0351 -0.7365 -2.1201 0.1368 -0.2111 -1.2283 -0.0750 0.0047 -1.1922 0.5740 0.6383 -0.1416 'X-RAY DIFFRACTION' 8 ? refined 4.5267 25.4391 40.9380 1.0984 0.7285 1.0282 -0.2034 -0.1231 0.3713 7.0102 4.5466 4.5983 3.2035 -0.5580 1.7224 1.0063 -1.4254 -1.3363 0.9355 0.0514 -0.1604 1.5170 -1.0085 -1.0437 'X-RAY DIFFRACTION' 9 ? refined -12.7125 12.3477 31.6404 1.3095 0.4542 0.9112 -0.0876 -0.0121 0.0922 6.4282 4.1863 3.0913 2.4244 2.0979 2.0976 -0.5339 0.1383 0.1251 -0.3079 0.0762 -0.3560 -1.1057 0.0974 0.4643 'X-RAY DIFFRACTION' 10 ? refined -30.0764 7.9994 -2.2448 2.0399 1.5723 1.4870 -0.3400 -0.3721 -0.1613 4.6833 1.4943 3.2985 0.9235 -0.0134 2.0820 0.3582 1.8108 -0.1143 -1.1775 -0.7827 0.7315 1.5333 -1.1896 0.4356 'X-RAY DIFFRACTION' 11 ? refined -52.3490 20.3744 -2.4562 1.9505 1.5018 2.1137 -0.1292 -0.7949 0.1574 1.7700 3.3176 1.9638 -2.4305 -1.8526 2.5539 -0.1153 1.2887 0.0806 -0.7514 -0.7162 0.4595 -1.2477 -0.8099 0.8490 'X-RAY DIFFRACTION' 12 ? refined -38.7892 27.4267 12.6184 1.5104 1.2192 1.5142 -0.1578 -0.4571 0.1576 9.8785 6.2424 2.0157 5.9002 8.4614 3.9868 -1.1871 0.9943 1.9490 -1.4792 -0.1668 0.9876 -1.3670 0.0431 1.3881 'X-RAY DIFFRACTION' 13 ? refined -21.0985 20.8275 49.0150 0.7680 0.7624 1.0796 0.0584 0.0884 -0.0376 0.3918 4.6654 4.7499 -1.3394 1.3127 -4.5916 -0.1289 -0.0118 -0.1924 -0.0571 0.1867 -0.2727 0.4116 -0.1288 -0.0563 'X-RAY DIFFRACTION' 14 ? refined -7.9635 15.3585 68.8222 1.2685 0.6311 1.4314 0.3112 -0.1556 0.0874 4.3554 2.1196 8.9222 1.7477 -1.0502 3.1036 -0.2945 0.0567 0.8464 0.3458 0.0444 -0.5591 -0.8531 0.5260 0.2575 'X-RAY DIFFRACTION' 15 ? refined 20.3706 42.2829 44.1906 1.5850 0.9243 1.2104 -0.2546 -0.1467 0.3680 9.9686 2.0000 3.9348 1.9989 5.9633 -5.1421 -0.3923 -1.7517 -0.9299 2.7280 1.0869 0.4328 0.2911 0.1667 -0.6747 # 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 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 1 through 421 ) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 422 through 633 ) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 634 through 737 ) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resid 738 through 956 ) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 1 through 59 ) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 60 through 169 ) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 170 through 291 ) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 292 through 342 ) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 343 through 423 ) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 424 through 462 ) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 463 through 502 ) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 503 through 549 ) ; 'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 550 through 630 ) ; 'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? ;chain 'B' and (resid 631 through 690 ) ; 'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? ;chain 'C' and (resid 1492 through 1497 ) ; # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 PHASER phasing . ? 3 PHENIX refinement '(phenix.refine: 1.8.2_1309)' ? 4 HKL-2000 'data reduction' . ? 5 HKL-2000 'data scaling' . ? 6 # 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 64 ? ? 65.09 -7.90 2 1 ASP A 73 ? ? -123.50 -65.95 3 1 ALA A 74 ? ? 67.29 -3.20 4 1 LYS A 82 ? ? -48.86 -72.07 5 1 ASP A 84 ? ? -153.29 80.08 6 1 GLN A 102 ? ? 55.00 -118.16 7 1 TRP A 114 ? ? -120.53 -74.93 8 1 ARG A 115 ? ? 90.17 -7.67 9 1 THR A 116 ? ? 54.40 -149.13 10 1 MET A 118 ? ? -108.60 -74.67 11 1 PRO A 124 ? ? -68.78 74.31 12 1 THR A 134 ? ? -139.50 -67.71 13 1 ASP A 148 ? ? 56.86 -144.56 14 1 ASP A 234 ? ? -67.54 -178.80 15 1 THR A 249 ? ? 74.77 -3.24 16 1 LEU A 264 ? ? -122.17 -67.28 17 1 ALA A 273 ? ? 67.11 -3.25 18 1 ASP A 289 ? ? 70.74 -4.08 19 1 VAL A 312 ? ? -127.05 -57.92 20 1 PHE A 334 ? ? -122.79 -65.95 21 1 ARG A 339 ? ? 56.25 70.25 22 1 ARG A 398 ? ? -113.51 -74.99 23 1 TYR A 406 ? ? 73.87 -18.30 24 1 THR A 466 ? ? 59.67 70.60 25 1 LEU A 487 ? ? -176.63 145.52 26 1 LEU A 532 ? ? 57.81 74.17 27 1 LEU A 552 ? ? -91.91 -62.26 28 1 LEU A 563 ? ? 62.00 72.83 29 1 ALA A 568 ? ? -127.59 -61.06 30 1 ASP A 570 ? ? 63.37 -3.73 31 1 THR A 572 ? ? 45.67 -111.66 32 1 THR A 582 ? ? -177.62 134.87 33 1 ASP A 613 ? ? 55.82 -116.07 34 1 LEU A 649 ? ? 55.04 -115.77 35 1 HIS A 702 ? ? -102.22 -77.33 36 1 GLN A 703 ? ? 176.97 161.61 37 1 SER A 705 ? ? 48.51 -129.78 38 1 THR A 709 ? ? 52.99 -118.76 39 1 VAL A 772 ? ? -102.68 -65.06 40 1 ASN A 785 ? ? -103.21 -60.07 41 1 ASN A 805 ? ? 66.36 -3.94 42 1 LEU A 808 ? ? -102.44 -73.73 43 1 ARG A 832 ? ? 52.65 -147.92 44 1 ILE A 833 ? ? 171.71 167.80 45 1 LYS A 834 ? ? -122.86 -76.28 46 1 ARG A 888 ? ? 44.01 70.89 47 1 MET A 909 ? ? 64.75 -132.85 48 1 ASN A 910 ? ? 51.95 -140.34 49 1 GLU A 912 ? ? -63.91 2.68 50 1 ASN A 913 ? ? 91.31 -3.44 51 1 GLN A 914 ? ? 56.17 -114.53 52 1 HIS A 916 ? ? 175.57 164.54 53 1 VAL B 19 ? ? -136.71 -67.04 54 1 SER B 27 ? ? -80.50 -153.95 55 1 ASP B 28 ? ? 113.55 -96.78 56 1 GLU B 29 ? ? 86.88 -20.84 57 1 LEU B 31 ? ? 125.55 67.01 58 1 SER B 35 ? ? 52.34 76.46 59 1 CYS B 38 ? ? -101.63 -77.19 60 1 ASP B 39 ? ? 49.00 -143.43 61 1 LYS B 41 ? ? 44.05 -119.11 62 1 ASN B 48 ? ? -46.53 -70.78 63 1 ASN B 133 ? ? 58.43 -105.79 64 1 LEU B 134 ? ? 64.97 -108.70 65 1 GLN B 141 ? ? -99.07 -62.00 66 1 VAL B 157 ? ? -126.23 -69.02 67 1 PRO B 163 ? ? -92.92 43.72 68 1 GLU B 174 ? ? 74.79 -17.86 69 1 TYR B 178 ? ? -121.72 -61.31 70 1 MET B 180 ? ? 70.83 -5.15 71 1 VAL B 193 ? ? -93.38 -69.77 72 1 LYS B 253 ? ? -61.54 -179.42 73 1 LEU B 258 ? ? 72.29 -6.18 74 1 SER B 337 ? ? 173.58 177.33 75 1 ASN B 339 ? ? 55.58 -143.69 76 1 CYS B 374 ? ? -107.44 -62.87 77 1 ASN B 376 ? ? 38.05 68.21 78 1 VAL B 379 ? ? 57.94 72.86 79 1 LYS B 410 ? ? -74.29 -71.96 80 1 CYS B 433 ? ? -129.18 -63.34 81 1 GLU B 442 ? ? 76.27 148.36 82 1 ARG B 447 ? ? 85.00 -4.50 83 1 CYS B 448 ? ? -100.93 -74.85 84 1 ASN B 449 ? ? -128.71 -65.11 85 1 ASN B 450 ? ? -129.30 -65.90 86 1 ASN B 452 ? ? 72.18 -5.28 87 1 CYS B 457 ? ? 56.28 -34.31 88 1 VAL B 459 ? ? -133.07 -61.56 89 1 CYS B 460 ? ? 87.22 -7.93 90 1 ARG B 461 ? ? 50.77 -137.33 91 1 CYS B 462 ? ? 179.76 176.00 92 1 LEU B 467 ? ? 41.28 72.39 93 1 CYS B 473 ? ? 53.97 -140.43 94 1 SER B 474 ? ? 58.19 83.87 95 1 GLU B 475 ? ? 92.21 -3.23 96 1 PRO B 480 ? ? -66.11 73.72 97 1 PRO B 488 ? ? -83.42 47.49 98 1 ARG B 489 ? ? 174.96 175.89 99 1 PRO B 493 ? ? -62.10 -173.63 100 1 VAL B 494 ? ? -68.81 -179.02 101 1 GLN B 497 ? ? 51.57 -117.42 102 1 GLU B 500 ? ? 47.81 -141.65 103 1 CYS B 503 ? ? 42.46 73.39 104 1 CYS B 508 ? ? -122.56 -63.58 105 1 SER B 510 ? ? -132.17 -57.28 106 1 SER B 511 ? ? -129.10 -85.85 107 1 ASP B 512 ? ? -140.23 -70.17 108 1 ASP B 525 ? ? 75.04 -10.58 109 1 PHE B 526 ? ? -120.65 -60.91 110 1 TYR B 531 ? ? -82.76 -74.67 111 1 SER B 537 ? ? 66.03 -3.30 112 1 ASP B 552 ? ? 72.69 -2.06 113 1 GLN B 590 ? ? 179.51 169.79 114 1 PRO B 591 ? ? -68.84 79.14 115 1 ALA B 607 ? ? 52.10 -113.35 116 1 ALA B 624 ? ? 77.36 -20.49 117 1 ARG B 633 ? ? -94.98 -63.28 118 1 LEU B 645 ? ? 177.40 160.10 119 1 GLU B 671 ? ? -73.98 -71.35 120 1 SER B 673 ? ? -115.89 -76.93 121 1 GLU B 684 ? ? 56.53 70.07 122 1 TRP C 1496 ? ? 175.27 161.35 # 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 SER 836 ? A SER 836 2 1 Y 1 A SER 837 ? A SER 837 3 1 Y 1 A LEU 838 ? A LEU 838 4 1 Y 1 A GLN 839 ? A GLN 839 5 1 Y 1 A THR 840 ? A THR 840 6 1 Y 1 A THR 841 ? A THR 841 7 1 Y 1 A GLU 842 ? A GLU 842 8 1 Y 1 A LYS 843 ? A LYS 843 9 1 Y 1 A ASN 844 ? A ASN 844 10 1 Y 1 A ASP 845 ? A ASP 845 11 1 Y 1 A THR 846 ? A THR 846 12 1 Y 1 A VAL 847 ? A VAL 847 13 1 Y 1 A ALA 848 ? A ALA 848 14 1 Y 1 A GLY 849 ? A GLY 849 15 1 Y 1 A GLN 850 ? A GLN 850 16 1 Y 1 A GLY 851 ? A GLY 851 17 1 Y 1 A GLU 852 ? A GLU 852 18 1 Y 1 A ARG 853 ? A ARG 853 19 1 Y 1 A ASP 854 ? A ASP 854 20 1 Y 1 A HIS 855 ? A HIS 855 21 1 Y 1 A LEU 856 ? A LEU 856 22 1 Y 1 A ILE 857 ? A ILE 857 23 1 Y 1 A THR 858 ? A THR 858 24 1 Y 1 A LYS 859 ? A LYS 859 25 1 Y 1 A ARG 860 ? A ARG 860 26 1 Y 1 A ASP 861 ? A ASP 861 27 1 Y 1 A LEU 862 ? A LEU 862 28 1 Y 1 A ALA 863 ? A ALA 863 29 1 Y 1 A LEU 864 ? A LEU 864 30 1 Y 1 A SER 865 ? A SER 865 31 1 Y 1 A GLU 866 ? A GLU 866 32 1 Y 1 A GLY 867 ? A GLY 867 33 1 Y 1 A PRO 957 ? A PRO 957 34 1 Y 1 A ALA 958 ? A ALA 958 35 1 Y 1 A PRO 959 ? A PRO 959 36 1 Y 1 B PRO 691 ? B PRO 691 37 1 Y 1 B ASP 692 ? B ASP 692 38 1 Y 1 C SER 1417 ? C SER 1 39 1 Y 1 C ASP 1418 ? C ASP 2 40 1 Y 1 C VAL 1419 ? C VAL 3 41 1 Y 1 C PRO 1420 ? C PRO 4 42 1 Y 1 C ARG 1421 ? C ARG 5 43 1 Y 1 C ASP 1422 ? C ASP 6 44 1 Y 1 C LEU 1423 ? C LEU 7 45 1 Y 1 C GLU 1424 ? C GLU 8 46 1 Y 1 C VAL 1425 ? C VAL 9 47 1 Y 1 C VAL 1426 ? C VAL 10 48 1 Y 1 C ALA 1427 ? C ALA 11 49 1 Y 1 C ALA 1428 ? C ALA 12 50 1 Y 1 C THR 1429 ? C THR 13 51 1 Y 1 C PRO 1430 ? C PRO 14 52 1 Y 1 C THR 1431 ? C THR 15 53 1 Y 1 C SER 1432 ? C SER 16 54 1 Y 1 C LEU 1433 ? C LEU 17 55 1 Y 1 C LEU 1434 ? C LEU 18 56 1 Y 1 C ILE 1435 ? C ILE 19 57 1 Y 1 C SER 1436 ? C SER 20 58 1 Y 1 C TRP 1437 ? C TRP 21 59 1 Y 1 C ASP 1438 ? C ASP 22 60 1 Y 1 C ALA 1439 ? C ALA 23 61 1 Y 1 C PRO 1440 ? C PRO 24 62 1 Y 1 C ALA 1441 ? C ALA 25 63 1 Y 1 C VAL 1442 ? C VAL 26 64 1 Y 1 C THR 1443 ? C THR 27 65 1 Y 1 C VAL 1444 ? C VAL 28 66 1 Y 1 C ARG 1445 ? C ARG 29 67 1 Y 1 C TYR 1446 ? C TYR 30 68 1 Y 1 C TYR 1447 ? C TYR 31 69 1 Y 1 C ARG 1448 ? C ARG 32 70 1 Y 1 C ILE 1449 ? C ILE 33 71 1 Y 1 C THR 1450 ? C THR 34 72 1 Y 1 C TYR 1451 ? C TYR 35 73 1 Y 1 C GLY 1452 ? C GLY 36 74 1 Y 1 C GLU 1453 ? C GLU 37 75 1 Y 1 C THR 1454 ? C THR 38 76 1 Y 1 C GLY 1455 ? C GLY 39 77 1 Y 1 C GLY 1456 ? C GLY 40 78 1 Y 1 C ASN 1457 ? C ASN 41 79 1 Y 1 C SER 1458 ? C SER 42 80 1 Y 1 C PRO 1459 ? C PRO 43 81 1 Y 1 C VAL 1460 ? C VAL 44 82 1 Y 1 C GLN 1461 ? C GLN 45 83 1 Y 1 C GLU 1462 ? C GLU 46 84 1 Y 1 C PHE 1463 ? C PHE 47 85 1 Y 1 C THR 1464 ? C THR 48 86 1 Y 1 C VAL 1465 ? C VAL 49 87 1 Y 1 C PRO 1466 ? C PRO 50 88 1 Y 1 C GLY 1467 ? C GLY 51 89 1 Y 1 C SER 1468 ? C SER 52 90 1 Y 1 C LYS 1469 ? C LYS 53 91 1 Y 1 C SER 1470 ? C SER 54 92 1 Y 1 C THR 1471 ? C THR 55 93 1 Y 1 C ALA 1472 ? C ALA 56 94 1 Y 1 C THR 1473 ? C THR 57 95 1 Y 1 C ILE 1474 ? C ILE 58 96 1 Y 1 C SER 1475 ? C SER 59 97 1 Y 1 C GLY 1476 ? C GLY 60 98 1 Y 1 C LEU 1477 ? C LEU 61 99 1 Y 1 C LYS 1478 ? C LYS 62 100 1 Y 1 C PRO 1479 ? C PRO 63 101 1 Y 1 C GLY 1480 ? C GLY 64 102 1 Y 1 C VAL 1481 ? C VAL 65 103 1 Y 1 C ASP 1482 ? C ASP 66 104 1 Y 1 C TYR 1483 ? C TYR 67 105 1 Y 1 C THR 1484 ? C THR 68 106 1 Y 1 C ILE 1485 ? C ILE 69 107 1 Y 1 C THR 1486 ? C THR 70 108 1 Y 1 C VAL 1487 ? C VAL 71 109 1 Y 1 C TYR 1488 ? C TYR 72 110 1 Y 1 C ALA 1489 ? C ALA 73 111 1 Y 1 C ASP 1498 ? C ASP 82 112 1 Y 1 C GLY 1499 ? C GLY 83 113 1 Y 1 C SER 1500 ? C SER 84 114 1 Y 1 C LYS 1501 ? C LYS 85 115 1 Y 1 C PRO 1502 ? C PRO 86 116 1 Y 1 C ILE 1503 ? C ILE 87 117 1 Y 1 C SER 1504 ? C SER 88 118 1 Y 1 C ILE 1505 ? C ILE 89 119 1 Y 1 C ASN 1506 ? C ASN 90 120 1 Y 1 C TYR 1507 ? C TYR 91 121 1 Y 1 C ARG 1508 ? C ARG 92 122 1 Y 1 C THR 1509 ? C THR 93 123 1 Y 1 C GLY 1510 ? C GLY 94 124 1 Y 1 C LYS 1511 ? C LYS 95 125 1 Y 1 C LYS 1512 ? C LYS 96 126 1 Y 1 C GLY 1513 ? C GLY 97 127 1 Y 1 C LYS 1514 ? C LYS 98 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 BETA-D-MANNOSE BMA 6 ALPHA-D-MANNOSE MAN 7 'MANGANESE (II) ION' MN 8 water HOH #